data_9HHW
# 
_entry.id   9HHW 
# 
_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   9HHW         pdb_00009hhw 10.2210/pdb9hhw/pdb 
WWPDB D_1292143354 ?            ?                   
# 
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 2025-02-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               '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 
# 
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.journal_volume'          
2 2 'Structure model' '_citation.year'                    
3 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HHW 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-22 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 knapp@pharmchem.uni-frankfurt.de    Stefan   Knapp     ? 'principal investigator/group leader' 0000-0001-5995-6494 
3 matthias.gehringer@uni-tuebingen.de Matthias Gehringer ? 'principal investigator/group leader' 0000-0003-0163-3419 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, G.'                             1 0000-0003-2896-3928 
'Seidler, N.'                          2 0009-0007-4405-2397 
'Gehringer, M.'                        3 0000-0003-0163-3419 
'Knapp, S.'                            4 0000-0001-5995-6494 
'Structural Genomics Consortium (SGC)' 5 ?                   
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202419736 
_citation.page_last                 e202419736 
_citation.title                     
;Probing the Protein Kinases' Cysteinome by Covalent Fragments.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202419736 
_citation.pdbx_database_id_PubMed   39716901 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, G.'            1  ?                   
primary 'Seidler, N.J.'       2  0009-0007-4405-2397 
primary 'Rohm, S.'            3  0000-0003-3999-712X 
primary 'Pan, Y.'             4  ?                   
primary 'Liang, X.J.'         5  ?                   
primary 'Haarer, L.'          6  ?                   
primary 'Berger, B.T.'        7  0000-0002-3314-2617 
primary 'Sivashanmugam, S.A.' 8  ?                   
primary 'Wydra, V.R.'         9  0009-0004-3295-0526 
primary 'Forster, M.'         10 ?                   
primary 'Laufer, S.A.'        11 0000-0001-6952-1486 
primary 'Chaikuad, A.'        12 0000-0003-1120-2209 
primary 'Gehringer, M.'       13 0000-0003-0163-3419 
primary 'Knapp, S.'           14 0000-0001-5995-6494 
# 
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 'Tau-tubulin kinase 1'                                         35515.031 1  2.7.11.1 ? ? ? 
2 non-polymer syn '~{N}-[2-(1~{H}-pyrrolo[2,3-b]pyridin-5-yl)phenyl]propanamide' 265.310   1  ?        ? ? ? 
3 water       nat water                                                          18.015    18 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Brain-derived tau kinase' 
# 
_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       
;MNMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVC
RFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRK
CYMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI
KEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVC
RFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRK
CYMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI
KEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '~{N}-[2-(1~{H}-pyrrolo[2,3-b]pyridin-5-yl)phenyl]propanamide' A1IU7 
3 water                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   MET n 
1 4   SER n 
1 5   GLY n 
1 6   GLY n 
1 7   GLY n 
1 8   GLU n 
1 9   GLN n 
1 10  ALA n 
1 11  ASP n 
1 12  ILE n 
1 13  LEU n 
1 14  PRO n 
1 15  ALA n 
1 16  ASN n 
1 17  TYR n 
1 18  VAL n 
1 19  VAL n 
1 20  LYS n 
1 21  ASP n 
1 22  ARG n 
1 23  TRP n 
1 24  LYS n 
1 25  VAL n 
1 26  LEU n 
1 27  LYS n 
1 28  LYS n 
1 29  ILE n 
1 30  GLY n 
1 31  GLY n 
1 32  GLY n 
1 33  GLY n 
1 34  PHE n 
1 35  GLY n 
1 36  GLU n 
1 37  ILE n 
1 38  TYR n 
1 39  GLU n 
1 40  ALA n 
1 41  MET n 
1 42  ASP n 
1 43  LEU n 
1 44  LEU n 
1 45  THR n 
1 46  ARG n 
1 47  GLU n 
1 48  ASN n 
1 49  VAL n 
1 50  ALA n 
1 51  LEU n 
1 52  LYS n 
1 53  VAL n 
1 54  GLU n 
1 55  SER n 
1 56  ALA n 
1 57  GLN n 
1 58  GLN n 
1 59  PRO n 
1 60  LYS n 
1 61  GLN n 
1 62  VAL n 
1 63  LEU n 
1 64  LYS n 
1 65  MET n 
1 66  GLU n 
1 67  VAL n 
1 68  ALA n 
1 69  VAL n 
1 70  LEU n 
1 71  LYS n 
1 72  LYS n 
1 73  LEU n 
1 74  GLN n 
1 75  GLY n 
1 76  LYS n 
1 77  ASP n 
1 78  HIS n 
1 79  VAL n 
1 80  CYS n 
1 81  ARG n 
1 82  PHE n 
1 83  ILE n 
1 84  GLY n 
1 85  CYS n 
1 86  GLY n 
1 87  ARG n 
1 88  ASN n 
1 89  GLU n 
1 90  LYS n 
1 91  PHE n 
1 92  ASN n 
1 93  TYR n 
1 94  VAL n 
1 95  VAL n 
1 96  MET n 
1 97  GLN n 
1 98  LEU n 
1 99  GLN n 
1 100 GLY n 
1 101 ARG n 
1 102 ASN n 
1 103 LEU n 
1 104 ALA n 
1 105 ASP n 
1 106 LEU n 
1 107 ARG n 
1 108 ARG n 
1 109 SER n 
1 110 GLN n 
1 111 PRO n 
1 112 ARG n 
1 113 GLY n 
1 114 THR n 
1 115 PHE n 
1 116 THR n 
1 117 LEU n 
1 118 SER n 
1 119 THR n 
1 120 THR n 
1 121 LEU n 
1 122 ARG n 
1 123 LEU n 
1 124 GLY n 
1 125 LYS n 
1 126 GLN n 
1 127 ILE n 
1 128 LEU n 
1 129 GLU n 
1 130 SER n 
1 131 ILE n 
1 132 GLU n 
1 133 ALA n 
1 134 ILE n 
1 135 HIS n 
1 136 SER n 
1 137 VAL n 
1 138 GLY n 
1 139 PHE n 
1 140 LEU n 
1 141 HIS n 
1 142 ARG n 
1 143 ASP n 
1 144 ILE n 
1 145 LYS n 
1 146 PRO n 
1 147 SER n 
1 148 ASN n 
1 149 PHE n 
1 150 ALA n 
1 151 MET n 
1 152 GLY n 
1 153 ARG n 
1 154 LEU n 
1 155 PRO n 
1 156 SER n 
1 157 THR n 
1 158 TYR n 
1 159 ARG n 
1 160 LYS n 
1 161 CYS n 
1 162 TYR n 
1 163 MET n 
1 164 LEU n 
1 165 ASP n 
1 166 PHE n 
1 167 GLY n 
1 168 LEU n 
1 169 ALA n 
1 170 ARG n 
1 171 GLN n 
1 172 TYR n 
1 173 THR n 
1 174 ASN n 
1 175 THR n 
1 176 THR n 
1 177 GLY n 
1 178 ASP n 
1 179 VAL n 
1 180 ARG n 
1 181 PRO n 
1 182 PRO n 
1 183 ARG n 
1 184 ASN n 
1 185 VAL n 
1 186 ALA n 
1 187 GLY n 
1 188 PHE n 
1 189 ARG n 
1 190 GLY n 
1 191 THR n 
1 192 VAL n 
1 193 ARG n 
1 194 TYR n 
1 195 ALA n 
1 196 SER n 
1 197 VAL n 
1 198 ASN n 
1 199 ALA n 
1 200 HIS n 
1 201 LYS n 
1 202 ASN n 
1 203 ARG n 
1 204 GLU n 
1 205 MET n 
1 206 GLY n 
1 207 ARG n 
1 208 HIS n 
1 209 ASP n 
1 210 ASP n 
1 211 LEU n 
1 212 TRP n 
1 213 SER n 
1 214 LEU n 
1 215 PHE n 
1 216 TYR n 
1 217 MET n 
1 218 LEU n 
1 219 VAL n 
1 220 GLU n 
1 221 PHE n 
1 222 ALA n 
1 223 VAL n 
1 224 GLY n 
1 225 GLN n 
1 226 LEU n 
1 227 PRO n 
1 228 TRP n 
1 229 ARG n 
1 230 LYS n 
1 231 ILE n 
1 232 LYS n 
1 233 ASP n 
1 234 LYS n 
1 235 GLU n 
1 236 GLN n 
1 237 VAL n 
1 238 GLY n 
1 239 MET n 
1 240 ILE n 
1 241 LYS n 
1 242 GLU n 
1 243 LYS n 
1 244 TYR n 
1 245 GLU n 
1 246 HIS n 
1 247 ARG n 
1 248 MET n 
1 249 LEU n 
1 250 LEU n 
1 251 LYS n 
1 252 HIS n 
1 253 MET n 
1 254 PRO n 
1 255 SER n 
1 256 GLU n 
1 257 PHE n 
1 258 HIS n 
1 259 LEU n 
1 260 PHE n 
1 261 LEU n 
1 262 ASP n 
1 263 HIS n 
1 264 ILE n 
1 265 ALA n 
1 266 SER n 
1 267 LEU n 
1 268 ASP n 
1 269 TYR n 
1 270 PHE n 
1 271 THR n 
1 272 LYS n 
1 273 PRO n 
1 274 ASP n 
1 275 TYR n 
1 276 GLN n 
1 277 LEU n 
1 278 ILE n 
1 279 MET n 
1 280 SER n 
1 281 VAL n 
1 282 PHE n 
1 283 GLU n 
1 284 ASN n 
1 285 SER n 
1 286 MET n 
1 287 LYS n 
1 288 GLU n 
1 289 ARG n 
1 290 GLY n 
1 291 ILE n 
1 292 ALA n 
1 293 GLU n 
1 294 ASN n 
1 295 GLU n 
1 296 ALA n 
1 297 PHE n 
1 298 ASP n 
1 299 TRP n 
1 300 GLU n 
1 301 LYS n 
1 302 ALA n 
1 303 GLY n 
1 304 THR n 
1 305 ASP n 
1 306 ALA n 
1 307 LEU n 
1 308 LEU n 
1 309 SER 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                   309 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TTBK1, BDTK, KIAA1855' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_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 
A1IU7 non-polymer         . '~{N}-[2-(1~{H}-pyrrolo[2,3-b]pyridin-5-yl)phenyl]propanamide' ? 'C16 H15 N3 O'   265.310 
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 
GLN   'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                          ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                  ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                        ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                         ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                     ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   12  ?   ?   ?   A . n 
A 1 2   ASN 2   13  ?   ?   ?   A . n 
A 1 3   MET 3   14  ?   ?   ?   A . n 
A 1 4   SER 4   15  ?   ?   ?   A . n 
A 1 5   GLY 5   16  ?   ?   ?   A . n 
A 1 6   GLY 6   17  ?   ?   ?   A . n 
A 1 7   GLY 7   18  ?   ?   ?   A . n 
A 1 8   GLU 8   19  ?   ?   ?   A . n 
A 1 9   GLN 9   20  ?   ?   ?   A . n 
A 1 10  ALA 10  21  21  ALA ALA A . n 
A 1 11  ASP 11  22  22  ASP ASP A . n 
A 1 12  ILE 12  23  23  ILE ILE A . n 
A 1 13  LEU 13  24  24  LEU LEU A . n 
A 1 14  PRO 14  25  25  PRO PRO A . n 
A 1 15  ALA 15  26  26  ALA ALA A . n 
A 1 16  ASN 16  27  27  ASN ASN A . n 
A 1 17  TYR 17  28  28  TYR TYR A . n 
A 1 18  VAL 18  29  29  VAL VAL A . n 
A 1 19  VAL 19  30  30  VAL VAL A . n 
A 1 20  LYS 20  31  31  LYS LYS A . n 
A 1 21  ASP 21  32  32  ASP ASP A . n 
A 1 22  ARG 22  33  33  ARG ARG A . n 
A 1 23  TRP 23  34  34  TRP TRP A . n 
A 1 24  LYS 24  35  35  LYS LYS A . n 
A 1 25  VAL 25  36  36  VAL VAL A . n 
A 1 26  LEU 26  37  37  LEU LEU A . n 
A 1 27  LYS 27  38  38  LYS LYS A . n 
A 1 28  LYS 28  39  39  LYS LYS A . n 
A 1 29  ILE 29  40  40  ILE ILE A . n 
A 1 30  GLY 30  41  41  GLY GLY A . n 
A 1 31  GLY 31  42  42  GLY GLY A . n 
A 1 32  GLY 32  43  43  GLY GLY A . n 
A 1 33  GLY 33  44  44  GLY GLY A . n 
A 1 34  PHE 34  45  45  PHE PHE A . n 
A 1 35  GLY 35  46  46  GLY GLY A . n 
A 1 36  GLU 36  47  47  GLU GLU A . n 
A 1 37  ILE 37  48  48  ILE ILE A . n 
A 1 38  TYR 38  49  49  TYR TYR A . n 
A 1 39  GLU 39  50  50  GLU GLU A . n 
A 1 40  ALA 40  51  51  ALA ALA A . n 
A 1 41  MET 41  52  52  MET MET A . n 
A 1 42  ASP 42  53  53  ASP ASP A . n 
A 1 43  LEU 43  54  54  LEU LEU A . n 
A 1 44  LEU 44  55  55  LEU LEU A . n 
A 1 45  THR 45  56  56  THR THR A . n 
A 1 46  ARG 46  57  57  ARG ARG A . n 
A 1 47  GLU 47  58  58  GLU GLU A . n 
A 1 48  ASN 48  59  59  ASN ASN A . n 
A 1 49  VAL 49  60  60  VAL VAL A . n 
A 1 50  ALA 50  61  61  ALA ALA A . n 
A 1 51  LEU 51  62  62  LEU LEU A . n 
A 1 52  LYS 52  63  63  LYS LYS A . n 
A 1 53  VAL 53  64  64  VAL VAL A . n 
A 1 54  GLU 54  65  65  GLU GLU A . n 
A 1 55  SER 55  66  66  SER SER A . n 
A 1 56  ALA 56  67  67  ALA ALA A . n 
A 1 57  GLN 57  68  68  GLN GLN A . n 
A 1 58  GLN 58  69  69  GLN GLN A . n 
A 1 59  PRO 59  70  70  PRO PRO A . n 
A 1 60  LYS 60  71  71  LYS LYS A . n 
A 1 61  GLN 61  72  72  GLN GLN A . n 
A 1 62  VAL 62  73  73  VAL VAL A . n 
A 1 63  LEU 63  74  74  LEU LEU A . n 
A 1 64  LYS 64  75  75  LYS LYS A . n 
A 1 65  MET 65  76  76  MET MET A . n 
A 1 66  GLU 66  77  77  GLU GLU A . n 
A 1 67  VAL 67  78  78  VAL VAL A . n 
A 1 68  ALA 68  79  79  ALA ALA A . n 
A 1 69  VAL 69  80  80  VAL VAL A . n 
A 1 70  LEU 70  81  81  LEU LEU A . n 
A 1 71  LYS 71  82  82  LYS LYS A . n 
A 1 72  LYS 72  83  83  LYS LYS A . n 
A 1 73  LEU 73  84  84  LEU LEU A . n 
A 1 74  GLN 74  85  85  GLN GLN A . n 
A 1 75  GLY 75  86  86  GLY GLY A . n 
A 1 76  LYS 76  87  87  LYS LYS A . n 
A 1 77  ASP 77  88  88  ASP ASP A . n 
A 1 78  HIS 78  89  89  HIS HIS A . n 
A 1 79  VAL 79  90  90  VAL VAL A . n 
A 1 80  CYS 80  91  91  CYS CYS A . n 
A 1 81  ARG 81  92  92  ARG ARG A . n 
A 1 82  PHE 82  93  93  PHE PHE A . n 
A 1 83  ILE 83  94  94  ILE ILE A . n 
A 1 84  GLY 84  95  95  GLY GLY A . n 
A 1 85  CYS 85  96  96  CYS CYS A . n 
A 1 86  GLY 86  97  97  GLY GLY A . n 
A 1 87  ARG 87  98  98  ARG ARG A . n 
A 1 88  ASN 88  99  99  ASN ASN A . n 
A 1 89  GLU 89  100 100 GLU GLU A . n 
A 1 90  LYS 90  101 101 LYS LYS A . n 
A 1 91  PHE 91  102 102 PHE PHE A . n 
A 1 92  ASN 92  103 103 ASN ASN A . n 
A 1 93  TYR 93  104 104 TYR TYR A . n 
A 1 94  VAL 94  105 105 VAL VAL A . n 
A 1 95  VAL 95  106 106 VAL VAL A . n 
A 1 96  MET 96  107 107 MET MET A . n 
A 1 97  GLN 97  108 108 GLN GLN A . n 
A 1 98  LEU 98  109 109 LEU LEU A . n 
A 1 99  GLN 99  110 110 GLN GLN A . n 
A 1 100 GLY 100 111 111 GLY GLY A . n 
A 1 101 ARG 101 112 112 ARG ARG A . n 
A 1 102 ASN 102 113 113 ASN ASN A . n 
A 1 103 LEU 103 114 114 LEU LEU A . n 
A 1 104 ALA 104 115 115 ALA ALA A . n 
A 1 105 ASP 105 116 116 ASP ASP A . n 
A 1 106 LEU 106 117 117 LEU LEU A . n 
A 1 107 ARG 107 118 118 ARG ARG A . n 
A 1 108 ARG 108 119 119 ARG ARG A . n 
A 1 109 SER 109 120 120 SER SER A . n 
A 1 110 GLN 110 121 121 GLN GLN A . n 
A 1 111 PRO 111 122 122 PRO PRO A . n 
A 1 112 ARG 112 123 123 ARG ARG A . n 
A 1 113 GLY 113 124 124 GLY GLY A . n 
A 1 114 THR 114 125 125 THR THR A . n 
A 1 115 PHE 115 126 126 PHE PHE A . n 
A 1 116 THR 116 127 127 THR THR A . n 
A 1 117 LEU 117 128 128 LEU LEU A . n 
A 1 118 SER 118 129 129 SER SER A . n 
A 1 119 THR 119 130 130 THR THR A . n 
A 1 120 THR 120 131 131 THR THR A . n 
A 1 121 LEU 121 132 132 LEU LEU A . n 
A 1 122 ARG 122 133 133 ARG ARG A . n 
A 1 123 LEU 123 134 134 LEU LEU A . n 
A 1 124 GLY 124 135 135 GLY GLY A . n 
A 1 125 LYS 125 136 136 LYS LYS A . n 
A 1 126 GLN 126 137 137 GLN GLN A . n 
A 1 127 ILE 127 138 138 ILE ILE A . n 
A 1 128 LEU 128 139 139 LEU LEU A . n 
A 1 129 GLU 129 140 140 GLU GLU A . n 
A 1 130 SER 130 141 141 SER SER A . n 
A 1 131 ILE 131 142 142 ILE ILE A . n 
A 1 132 GLU 132 143 143 GLU GLU A . n 
A 1 133 ALA 133 144 144 ALA ALA A . n 
A 1 134 ILE 134 145 145 ILE ILE A . n 
A 1 135 HIS 135 146 146 HIS HIS A . n 
A 1 136 SER 136 147 147 SER SER A . n 
A 1 137 VAL 137 148 148 VAL VAL A . n 
A 1 138 GLY 138 149 149 GLY GLY A . n 
A 1 139 PHE 139 150 150 PHE PHE A . n 
A 1 140 LEU 140 151 151 LEU LEU A . n 
A 1 141 HIS 141 152 152 HIS HIS A . n 
A 1 142 ARG 142 153 153 ARG ARG A . n 
A 1 143 ASP 143 154 154 ASP ASP A . n 
A 1 144 ILE 144 155 155 ILE ILE A . n 
A 1 145 LYS 145 156 156 LYS LYS A . n 
A 1 146 PRO 146 157 157 PRO PRO A . n 
A 1 147 SER 147 158 158 SER SER A . n 
A 1 148 ASN 148 159 159 ASN ASN A . n 
A 1 149 PHE 149 160 160 PHE PHE A . n 
A 1 150 ALA 150 161 161 ALA ALA A . n 
A 1 151 MET 151 162 162 MET MET A . n 
A 1 152 GLY 152 163 163 GLY GLY A . n 
A 1 153 ARG 153 164 164 ARG ARG A . n 
A 1 154 LEU 154 165 165 LEU LEU A . n 
A 1 155 PRO 155 166 166 PRO PRO A . n 
A 1 156 SER 156 167 167 SER SER A . n 
A 1 157 THR 157 168 168 THR THR A . n 
A 1 158 TYR 158 169 169 TYR TYR A . n 
A 1 159 ARG 159 170 170 ARG ARG A . n 
A 1 160 LYS 160 171 171 LYS LYS A . n 
A 1 161 CYS 161 172 172 CYS CYS A . n 
A 1 162 TYR 162 173 173 TYR TYR A . n 
A 1 163 MET 163 174 174 MET MET A . n 
A 1 164 LEU 164 175 175 LEU LEU A . n 
A 1 165 ASP 165 176 176 ASP ASP A . n 
A 1 166 PHE 166 177 177 PHE PHE A . n 
A 1 167 GLY 167 178 178 GLY GLY A . n 
A 1 168 LEU 168 179 179 LEU LEU A . n 
A 1 169 ALA 169 180 180 ALA ALA A . n 
A 1 170 ARG 170 181 181 ARG ARG A . n 
A 1 171 GLN 171 182 182 GLN GLN A . n 
A 1 172 TYR 172 183 183 TYR TYR A . n 
A 1 173 THR 173 184 184 THR THR A . n 
A 1 174 ASN 174 185 185 ASN ASN A . n 
A 1 175 THR 175 186 186 THR THR A . n 
A 1 176 THR 176 187 187 THR THR A . n 
A 1 177 GLY 177 188 188 GLY GLY A . n 
A 1 178 ASP 178 189 189 ASP ASP A . n 
A 1 179 VAL 179 190 190 VAL VAL A . n 
A 1 180 ARG 180 191 191 ARG ARG A . n 
A 1 181 PRO 181 192 192 PRO PRO A . n 
A 1 182 PRO 182 193 193 PRO PRO A . n 
A 1 183 ARG 183 194 194 ARG ARG A . n 
A 1 184 ASN 184 195 195 ASN ASN A . n 
A 1 185 VAL 185 196 196 VAL VAL A . n 
A 1 186 ALA 186 197 197 ALA ALA A . n 
A 1 187 GLY 187 198 198 GLY GLY A . n 
A 1 188 PHE 188 199 199 PHE PHE A . n 
A 1 189 ARG 189 200 200 ARG ARG A . n 
A 1 190 GLY 190 201 201 GLY GLY A . n 
A 1 191 THR 191 202 202 THR THR A . n 
A 1 192 VAL 192 203 203 VAL VAL A . n 
A 1 193 ARG 193 204 204 ARG ARG A . n 
A 1 194 TYR 194 205 205 TYR TYR A . n 
A 1 195 ALA 195 206 206 ALA ALA A . n 
A 1 196 SER 196 207 207 SER SER A . n 
A 1 197 VAL 197 208 208 VAL VAL A . n 
A 1 198 ASN 198 209 209 ASN ASN A . n 
A 1 199 ALA 199 210 210 ALA ALA A . n 
A 1 200 HIS 200 211 211 HIS HIS A . n 
A 1 201 LYS 201 212 212 LYS LYS A . n 
A 1 202 ASN 202 213 213 ASN ASN A . n 
A 1 203 ARG 203 214 214 ARG ARG A . n 
A 1 204 GLU 204 215 215 GLU GLU A . n 
A 1 205 MET 205 216 216 MET MET A . n 
A 1 206 GLY 206 217 217 GLY GLY A . n 
A 1 207 ARG 207 218 218 ARG ARG A . n 
A 1 208 HIS 208 219 219 HIS HIS A . n 
A 1 209 ASP 209 220 220 ASP ASP A . n 
A 1 210 ASP 210 221 221 ASP ASP A . n 
A 1 211 LEU 211 222 222 LEU LEU A . n 
A 1 212 TRP 212 223 223 TRP TRP A . n 
A 1 213 SER 213 224 224 SER SER A . n 
A 1 214 LEU 214 225 225 LEU LEU A . n 
A 1 215 PHE 215 226 226 PHE PHE A . n 
A 1 216 TYR 216 227 227 TYR TYR A . n 
A 1 217 MET 217 228 228 MET MET A . n 
A 1 218 LEU 218 229 229 LEU LEU A . n 
A 1 219 VAL 219 230 230 VAL VAL A . n 
A 1 220 GLU 220 231 231 GLU GLU A . n 
A 1 221 PHE 221 232 232 PHE PHE A . n 
A 1 222 ALA 222 233 233 ALA ALA A . n 
A 1 223 VAL 223 234 234 VAL VAL A . n 
A 1 224 GLY 224 235 235 GLY GLY A . n 
A 1 225 GLN 225 236 236 GLN GLN A . n 
A 1 226 LEU 226 237 237 LEU LEU A . n 
A 1 227 PRO 227 238 238 PRO PRO A . n 
A 1 228 TRP 228 239 239 TRP TRP A . n 
A 1 229 ARG 229 240 240 ARG ARG A . n 
A 1 230 LYS 230 241 241 LYS LYS A . n 
A 1 231 ILE 231 242 242 ILE ILE A . n 
A 1 232 LYS 232 243 243 LYS LYS A . n 
A 1 233 ASP 233 244 244 ASP ASP A . n 
A 1 234 LYS 234 245 245 LYS LYS A . n 
A 1 235 GLU 235 246 246 GLU GLU A . n 
A 1 236 GLN 236 247 247 GLN GLN A . n 
A 1 237 VAL 237 248 248 VAL VAL A . n 
A 1 238 GLY 238 249 249 GLY GLY A . n 
A 1 239 MET 239 250 250 MET MET A . n 
A 1 240 ILE 240 251 251 ILE ILE A . n 
A 1 241 LYS 241 252 252 LYS LYS A . n 
A 1 242 GLU 242 253 253 GLU GLU A . n 
A 1 243 LYS 243 254 254 LYS LYS A . n 
A 1 244 TYR 244 255 255 TYR TYR A . n 
A 1 245 GLU 245 256 256 GLU GLU A . n 
A 1 246 HIS 246 257 257 HIS HIS A . n 
A 1 247 ARG 247 258 258 ARG ARG A . n 
A 1 248 MET 248 259 259 MET MET A . n 
A 1 249 LEU 249 260 260 LEU LEU A . n 
A 1 250 LEU 250 261 261 LEU LEU A . n 
A 1 251 LYS 251 262 262 LYS LYS A . n 
A 1 252 HIS 252 263 263 HIS HIS A . n 
A 1 253 MET 253 264 264 MET MET A . n 
A 1 254 PRO 254 265 265 PRO PRO A . n 
A 1 255 SER 255 266 266 SER SER A . n 
A 1 256 GLU 256 267 267 GLU GLU A . n 
A 1 257 PHE 257 268 268 PHE PHE A . n 
A 1 258 HIS 258 269 269 HIS HIS A . n 
A 1 259 LEU 259 270 270 LEU LEU A . n 
A 1 260 PHE 260 271 271 PHE PHE A . n 
A 1 261 LEU 261 272 272 LEU LEU A . n 
A 1 262 ASP 262 273 273 ASP ASP A . n 
A 1 263 HIS 263 274 274 HIS HIS A . n 
A 1 264 ILE 264 275 275 ILE ILE A . n 
A 1 265 ALA 265 276 276 ALA ALA A . n 
A 1 266 SER 266 277 277 SER SER A . n 
A 1 267 LEU 267 278 278 LEU LEU A . n 
A 1 268 ASP 268 279 279 ASP ASP A . n 
A 1 269 TYR 269 280 280 TYR TYR A . n 
A 1 270 PHE 270 281 281 PHE PHE A . n 
A 1 271 THR 271 282 282 THR THR A . n 
A 1 272 LYS 272 283 283 LYS LYS A . n 
A 1 273 PRO 273 284 284 PRO PRO A . n 
A 1 274 ASP 274 285 285 ASP ASP A . n 
A 1 275 TYR 275 286 286 TYR TYR A . n 
A 1 276 GLN 276 287 287 GLN GLN A . n 
A 1 277 LEU 277 288 288 LEU LEU A . n 
A 1 278 ILE 278 289 289 ILE ILE A . n 
A 1 279 MET 279 290 290 MET MET A . n 
A 1 280 SER 280 291 291 SER SER A . n 
A 1 281 VAL 281 292 292 VAL VAL A . n 
A 1 282 PHE 282 293 293 PHE PHE A . n 
A 1 283 GLU 283 294 294 GLU GLU A . n 
A 1 284 ASN 284 295 295 ASN ASN A . n 
A 1 285 SER 285 296 296 SER SER A . n 
A 1 286 MET 286 297 297 MET MET A . n 
A 1 287 LYS 287 298 298 LYS LYS A . n 
A 1 288 GLU 288 299 299 GLU GLU A . n 
A 1 289 ARG 289 300 300 ARG ARG A . n 
A 1 290 GLY 290 301 301 GLY GLY A . n 
A 1 291 ILE 291 302 302 ILE ILE A . n 
A 1 292 ALA 292 303 303 ALA ALA A . n 
A 1 293 GLU 293 304 304 GLU GLU A . n 
A 1 294 ASN 294 305 305 ASN ASN A . n 
A 1 295 GLU 295 306 306 GLU GLU A . n 
A 1 296 ALA 296 307 307 ALA ALA A . n 
A 1 297 PHE 297 308 308 PHE PHE A . n 
A 1 298 ASP 298 309 309 ASP ASP A . n 
A 1 299 TRP 299 310 310 TRP TRP A . n 
A 1 300 GLU 300 311 311 GLU GLU A . n 
A 1 301 LYS 301 312 312 LYS LYS A . n 
A 1 302 ALA 302 313 313 ALA ALA A . n 
A 1 303 GLY 303 314 ?   ?   ?   A . n 
A 1 304 THR 304 315 ?   ?   ?   A . n 
A 1 305 ASP 305 316 ?   ?   ?   A . n 
A 1 306 ALA 306 317 ?   ?   ?   A . n 
A 1 307 LEU 307 318 ?   ?   ?   A . n 
A 1 308 LEU 308 319 ?   ?   ?   A . n 
A 1 309 SER 309 320 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IU7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IU7 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1IU7 1  401 401 A1IU7 LIG A . 
C 3 HOH   1  501 14  HOH   HOH A . 
C 3 HOH   2  502 6   HOH   HOH A . 
C 3 HOH   3  503 13  HOH   HOH A . 
C 3 HOH   4  504 11  HOH   HOH A . 
C 3 HOH   5  505 17  HOH   HOH A . 
C 3 HOH   6  506 18  HOH   HOH A . 
C 3 HOH   7  507 5   HOH   HOH A . 
C 3 HOH   8  508 12  HOH   HOH A . 
C 3 HOH   9  509 15  HOH   HOH A . 
C 3 HOH   10 510 3   HOH   HOH A . 
C 3 HOH   11 511 10  HOH   HOH A . 
C 3 HOH   12 512 2   HOH   HOH A . 
C 3 HOH   13 513 4   HOH   HOH A . 
C 3 HOH   14 514 1   HOH   HOH A . 
C 3 HOH   15 515 9   HOH   HOH A . 
C 3 HOH   16 516 16  HOH   HOH A . 
C 3 HOH   17 517 7   HOH   HOH A . 
C 3 HOH   18 518 8   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 ARG 200 ? CG  ? A ARG 189 CG  
2 1 Y 1 A ARG 200 ? CD  ? A ARG 189 CD  
3 1 Y 1 A ARG 200 ? NE  ? A ARG 189 NE  
4 1 Y 1 A ARG 200 ? CZ  ? A ARG 189 CZ  
5 1 Y 1 A ARG 200 ? NH1 ? A ARG 189 NH1 
6 1 Y 1 A ARG 200 ? NH2 ? A ARG 189 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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.30 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HHW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.641 
_cell.length_a_esd                 ? 
_cell.length_b                     39.954 
_cell.length_b_esd                 ? 
_cell.length_c                     166.667 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9HHW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 1 2 1' 
_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                   9HHW 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.05 
_exptl_crystal.description                  ? 
_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              ? 
_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    '17% PEG 3350, 0.2 M sodium acetate pH 7.0 and 0.1 M tris pH 7.5-9.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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 EIGER X 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         2022-02-10 
_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   0.999995 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999995 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HHW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3 
_reflns.d_resolution_low                               48.26 
_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                                     6759 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.977 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    3 
_reflns_shell.d_res_low                                     3.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1077 
_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                               ? 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.772 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            -7.24 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.20 
_refine.aniso_B[2][2]                            1.68 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            5.54 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               36.710 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.899 
_refine.correlation_coeff_Fo_to_Fc_free          0.808 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9HHW 
_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                            3.00 
_refine.ls_d_res_low                             48.26 
_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                     6426 
_refine.ls_number_reflns_R_free                  332 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.23429 
_refine.ls_R_factor_R_free                       0.28592 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23162 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.537 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             25.236 
_refine.overall_SU_ML                            0.445 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        48.26 
_refine_hist.number_atoms_solvent             18 
_refine_hist.number_atoms_total               2417 
_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        2379 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.006  0.012  2470  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2385  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.818  1.857  3324  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.551  1.785  5477  ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.309  5.000  298   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.754 6.731  26    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.728 10.000 460   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.074  0.200  348   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2934  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  611   ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.720  3.491  1177  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.719  3.491  1177  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.643  6.262  1471  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.641  6.266  1472  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.645  3.858  1293  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.644  3.863  1294  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.659  6.950  1851  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.671 41.75  10329 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.670 41.75  10330 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.000 
_refine_ls_shell.d_res_low                        3.078 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_R_work             482 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.339 
_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   20 
_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                  0.230 
# 
_struct.entry_id                     9HHW 
_struct.title                        'Crystal structure of TTBK1 with a covalent compound GCL95' 
_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        9HHW 
_struct_keywords.text            'Kinase, Covalent, inhibitor, TTBK1, 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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TTBK1_HUMAN 
_struct_ref.pdbx_db_accession          Q5TCY1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCR
FIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKC
YMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIK
EKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLS
;
_struct_ref.pdbx_align_begin           13 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HHW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 309 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q5TCY1 
_struct_ref_seq.db_align_beg                  13 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  320 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       13 
_struct_ref_seq.pdbx_auth_seq_align_end       320 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9HHW 
_struct_ref_seq_dif.mon_id                       MET 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q5TCY1 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'initiating methionine' 
_struct_ref_seq_dif.pdbx_auth_seq_num            12 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 VAL A 62  ? LEU A 73  ? VAL A 73  LEU A 84  1 ? 12 
HELX_P HELX_P2  AA2 ASN A 102 ? GLN A 110 ? ASN A 113 GLN A 121 1 ? 9  
HELX_P HELX_P3  AA3 THR A 116 ? VAL A 137 ? THR A 127 VAL A 148 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 145 ? SER A 147 ? LYS A 156 SER A 158 5 ? 3  
HELX_P HELX_P5  AA5 THR A 191 ? ALA A 195 ? THR A 202 ALA A 206 5 ? 5  
HELX_P HELX_P6  AA6 SER A 196 ? LYS A 201 ? SER A 207 LYS A 212 1 ? 6  
HELX_P HELX_P7  AA7 GLY A 206 ? GLY A 224 ? GLY A 217 GLY A 235 1 ? 19 
HELX_P HELX_P8  AA8 ASP A 233 ? TYR A 244 ? ASP A 244 TYR A 255 1 ? 12 
HELX_P HELX_P9  AA9 GLU A 245 ? HIS A 252 ? GLU A 256 HIS A 263 5 ? 8  
HELX_P HELX_P10 AB1 GLU A 256 ? ALA A 265 ? GLU A 267 ALA A 276 1 ? 10 
HELX_P HELX_P11 AB2 ASP A 274 ? GLU A 288 ? ASP A 285 GLU A 299 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            80 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1IU7 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C1 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             91 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1IU7 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.772 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1IU7 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      80 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1IU7 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       91 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C1 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1IU7 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? 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 VAL A 18  ? VAL A 19  ? VAL A 29  VAL A 30  
AA1 2 TRP A 23  ? GLY A 30  ? TRP A 34  GLY A 41  
AA1 3 GLU A 36  ? ASP A 42  ? GLU A 47  ASP A 53  
AA1 4 ASN A 48  ? SER A 55  ? ASN A 59  SER A 66  
AA1 5 PHE A 91  ? GLN A 97  ? PHE A 102 GLN A 108 
AA1 6 PHE A 82  ? ASN A 88  ? PHE A 93  ASN A 99  
AA2 1 PHE A 139 ? LEU A 140 ? PHE A 150 LEU A 151 
AA2 2 ARG A 170 ? GLN A 171 ? ARG A 181 GLN A 182 
AA3 1 PHE A 149 ? MET A 151 ? PHE A 160 MET A 162 
AA3 2 CYS A 161 ? MET A 163 ? CYS A 172 MET A 174 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 19  ? N VAL A 30  O TRP A 23  ? O TRP A 34  
AA1 2 3 N LEU A 26  ? N LEU A 37  O GLU A 39  ? O GLU A 50  
AA1 3 4 N TYR A 38  ? N TYR A 49  O LEU A 51  ? O LEU A 62  
AA1 4 5 N GLU A 54  ? N GLU A 65  O ASN A 92  ? O ASN A 103 
AA1 5 6 O VAL A 95  ? O VAL A 106 N GLY A 84  ? N GLY A 95  
AA2 1 2 N LEU A 140 ? N LEU A 151 O ARG A 170 ? O ARG A 181 
AA3 1 2 N ALA A 150 ? N ALA A 161 O TYR A 162 ? O TYR A 173 
# 
_pdbx_entry_details.entry_id                   9HHW 
_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   Y 
# 
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 ARG A 33  ? ? -157.82 -25.00 
2  1 ILE A 40  ? ? -133.63 -31.92 
3  1 ARG A 57  ? ? 82.64   -4.14  
4  1 GLN A 69  ? ? -36.09  128.77 
5  1 HIS A 89  ? ? 80.19   14.78  
6  1 GLU A 100 ? ? -75.69  26.44  
7  1 PHE A 102 ? ? -172.74 142.59 
8  1 THR A 127 ? ? -57.75  175.24 
9  1 ARG A 153 ? ? 68.09   -25.52 
10 1 SER A 158 ? ? -52.70  -9.44  
11 1 THR A 168 ? ? -143.70 -9.44  
12 1 ASP A 176 ? ? 63.39   128.70 
13 1 THR A 187 ? ? -70.54  -88.37 
14 1 ALA A 197 ? ? -162.93 113.04 
15 1 PRO A 265 ? ? -37.65  143.84 
16 1 GLU A 299 ? ? -63.69  31.03  
17 1 ARG A 300 ? ? -161.30 4.88   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     181 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.157 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 12  ? A MET 1   
2  1 Y 1 A ASN 13  ? A ASN 2   
3  1 Y 1 A MET 14  ? A MET 3   
4  1 Y 1 A SER 15  ? A SER 4   
5  1 Y 1 A GLY 16  ? A GLY 5   
6  1 Y 1 A GLY 17  ? A GLY 6   
7  1 Y 1 A GLY 18  ? A GLY 7   
8  1 Y 1 A GLU 19  ? A GLU 8   
9  1 Y 1 A GLN 20  ? A GLN 9   
10 1 Y 1 A GLY 314 ? A GLY 303 
11 1 Y 1 A THR 315 ? A THR 304 
12 1 Y 1 A ASP 316 ? A ASP 305 
13 1 Y 1 A ALA 317 ? A ALA 306 
14 1 Y 1 A LEU 318 ? A LEU 307 
15 1 Y 1 A LEU 319 ? A LEU 308 
16 1 Y 1 A SER 320 ? A SER 309 
# 
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 
A1IU7 N1   N N N 1   
A1IU7 N3   N Y N 2   
A1IU7 C4   C Y N 3   
A1IU7 C5   C Y N 4   
A1IU7 C6   C Y N 5   
A1IU7 C7   C Y N 6   
A1IU7 C8   C Y N 7   
A1IU7 C10  C Y N 8   
A1IU7 C13  C Y N 9   
A1IU7 C15  C Y N 10  
A1IU7 C1   C N N 11  
A1IU7 C2   C N N 12  
A1IU7 C3   C N N 13  
A1IU7 O1   O N N 14  
A1IU7 C9   C Y N 15  
A1IU7 C11  C Y N 16  
A1IU7 N2   N Y N 17  
A1IU7 C12  C Y N 18  
A1IU7 C14  C Y N 19  
A1IU7 C16  C Y N 20  
A1IU7 H1   H N N 21  
A1IU7 H2   H N N 22  
A1IU7 H3   H N N 23  
A1IU7 H4   H N N 24  
A1IU7 H5   H N N 25  
A1IU7 H6   H N N 26  
A1IU7 H7   H N N 27  
A1IU7 H8   H N N 28  
A1IU7 H9   H N N 29  
A1IU7 H10  H N N 30  
A1IU7 H11  H N N 31  
A1IU7 H12  H N N 32  
A1IU7 H13  H N N 33  
A1IU7 H14  H N N 34  
A1IU7 H15  H N N 35  
ALA   N    N N N 36  
ALA   CA   C N S 37  
ALA   C    C N N 38  
ALA   O    O N N 39  
ALA   CB   C N N 40  
ALA   OXT  O N N 41  
ALA   H    H N N 42  
ALA   H2   H N N 43  
ALA   HA   H N N 44  
ALA   HB1  H N N 45  
ALA   HB2  H N N 46  
ALA   HB3  H N N 47  
ALA   HXT  H N N 48  
ARG   N    N N N 49  
ARG   CA   C N S 50  
ARG   C    C N N 51  
ARG   O    O N N 52  
ARG   CB   C N N 53  
ARG   CG   C N N 54  
ARG   CD   C N N 55  
ARG   NE   N N N 56  
ARG   CZ   C N N 57  
ARG   NH1  N N N 58  
ARG   NH2  N N N 59  
ARG   OXT  O N N 60  
ARG   H    H N N 61  
ARG   H2   H N N 62  
ARG   HA   H N N 63  
ARG   HB2  H N N 64  
ARG   HB3  H N N 65  
ARG   HG2  H N N 66  
ARG   HG3  H N N 67  
ARG   HD2  H N N 68  
ARG   HD3  H N N 69  
ARG   HE   H N N 70  
ARG   HH11 H N N 71  
ARG   HH12 H N N 72  
ARG   HH21 H N N 73  
ARG   HH22 H N N 74  
ARG   HXT  H N N 75  
ASN   N    N N N 76  
ASN   CA   C N S 77  
ASN   C    C N N 78  
ASN   O    O N N 79  
ASN   CB   C N N 80  
ASN   CG   C N N 81  
ASN   OD1  O N N 82  
ASN   ND2  N N N 83  
ASN   OXT  O N N 84  
ASN   H    H N N 85  
ASN   H2   H N N 86  
ASN   HA   H N N 87  
ASN   HB2  H N N 88  
ASN   HB3  H N N 89  
ASN   HD21 H N N 90  
ASN   HD22 H N N 91  
ASN   HXT  H N N 92  
ASP   N    N N N 93  
ASP   CA   C N S 94  
ASP   C    C N N 95  
ASP   O    O N N 96  
ASP   CB   C N N 97  
ASP   CG   C N N 98  
ASP   OD1  O N N 99  
ASP   OD2  O N N 100 
ASP   OXT  O N N 101 
ASP   H    H N N 102 
ASP   H2   H N N 103 
ASP   HA   H N N 104 
ASP   HB2  H N N 105 
ASP   HB3  H N N 106 
ASP   HD2  H N N 107 
ASP   HXT  H N N 108 
CYS   N    N N N 109 
CYS   CA   C N R 110 
CYS   C    C N N 111 
CYS   O    O N N 112 
CYS   CB   C N N 113 
CYS   SG   S N N 114 
CYS   OXT  O N N 115 
CYS   H    H N N 116 
CYS   H2   H N N 117 
CYS   HA   H N N 118 
CYS   HB2  H N N 119 
CYS   HB3  H N N 120 
CYS   HG   H N N 121 
CYS   HXT  H N N 122 
GLN   N    N N N 123 
GLN   CA   C N S 124 
GLN   C    C N N 125 
GLN   O    O N N 126 
GLN   CB   C N N 127 
GLN   CG   C N N 128 
GLN   CD   C N N 129 
GLN   OE1  O N N 130 
GLN   NE2  N N N 131 
GLN   OXT  O N N 132 
GLN   H    H N N 133 
GLN   H2   H N N 134 
GLN   HA   H N N 135 
GLN   HB2  H N N 136 
GLN   HB3  H N N 137 
GLN   HG2  H N N 138 
GLN   HG3  H N N 139 
GLN   HE21 H N N 140 
GLN   HE22 H N N 141 
GLN   HXT  H N N 142 
GLU   N    N N N 143 
GLU   CA   C N S 144 
GLU   C    C N N 145 
GLU   O    O N N 146 
GLU   CB   C N N 147 
GLU   CG   C N N 148 
GLU   CD   C N N 149 
GLU   OE1  O N N 150 
GLU   OE2  O N N 151 
GLU   OXT  O N N 152 
GLU   H    H N N 153 
GLU   H2   H N N 154 
GLU   HA   H N N 155 
GLU   HB2  H N N 156 
GLU   HB3  H N N 157 
GLU   HG2  H N N 158 
GLU   HG3  H N N 159 
GLU   HE2  H N N 160 
GLU   HXT  H N N 161 
GLY   N    N N N 162 
GLY   CA   C N N 163 
GLY   C    C N N 164 
GLY   O    O N N 165 
GLY   OXT  O N N 166 
GLY   H    H N N 167 
GLY   H2   H N N 168 
GLY   HA2  H N N 169 
GLY   HA3  H N N 170 
GLY   HXT  H N N 171 
HIS   N    N N N 172 
HIS   CA   C N S 173 
HIS   C    C N N 174 
HIS   O    O N N 175 
HIS   CB   C N N 176 
HIS   CG   C Y N 177 
HIS   ND1  N Y N 178 
HIS   CD2  C Y N 179 
HIS   CE1  C Y N 180 
HIS   NE2  N Y N 181 
HIS   OXT  O N N 182 
HIS   H    H N N 183 
HIS   H2   H N N 184 
HIS   HA   H N N 185 
HIS   HB2  H N N 186 
HIS   HB3  H N N 187 
HIS   HD1  H N N 188 
HIS   HD2  H N N 189 
HIS   HE1  H N N 190 
HIS   HE2  H N N 191 
HIS   HXT  H N N 192 
HOH   O    O N N 193 
HOH   H1   H N N 194 
HOH   H2   H N N 195 
ILE   N    N N N 196 
ILE   CA   C N S 197 
ILE   C    C N N 198 
ILE   O    O N N 199 
ILE   CB   C N S 200 
ILE   CG1  C N N 201 
ILE   CG2  C N N 202 
ILE   CD1  C N N 203 
ILE   OXT  O N N 204 
ILE   H    H N N 205 
ILE   H2   H N N 206 
ILE   HA   H N N 207 
ILE   HB   H N N 208 
ILE   HG12 H N N 209 
ILE   HG13 H N N 210 
ILE   HG21 H N N 211 
ILE   HG22 H N N 212 
ILE   HG23 H N N 213 
ILE   HD11 H N N 214 
ILE   HD12 H N N 215 
ILE   HD13 H N N 216 
ILE   HXT  H N N 217 
LEU   N    N N N 218 
LEU   CA   C N S 219 
LEU   C    C N N 220 
LEU   O    O N N 221 
LEU   CB   C N N 222 
LEU   CG   C N N 223 
LEU   CD1  C N N 224 
LEU   CD2  C N N 225 
LEU   OXT  O N N 226 
LEU   H    H N N 227 
LEU   H2   H N N 228 
LEU   HA   H N N 229 
LEU   HB2  H N N 230 
LEU   HB3  H N N 231 
LEU   HG   H N N 232 
LEU   HD11 H N N 233 
LEU   HD12 H N N 234 
LEU   HD13 H N N 235 
LEU   HD21 H N N 236 
LEU   HD22 H N N 237 
LEU   HD23 H N N 238 
LEU   HXT  H N N 239 
LYS   N    N N N 240 
LYS   CA   C N S 241 
LYS   C    C N N 242 
LYS   O    O N N 243 
LYS   CB   C N N 244 
LYS   CG   C N N 245 
LYS   CD   C N N 246 
LYS   CE   C N N 247 
LYS   NZ   N N N 248 
LYS   OXT  O N N 249 
LYS   H    H N N 250 
LYS   H2   H N N 251 
LYS   HA   H N N 252 
LYS   HB2  H N N 253 
LYS   HB3  H N N 254 
LYS   HG2  H N N 255 
LYS   HG3  H N N 256 
LYS   HD2  H N N 257 
LYS   HD3  H N N 258 
LYS   HE2  H N N 259 
LYS   HE3  H N N 260 
LYS   HZ1  H N N 261 
LYS   HZ2  H N N 262 
LYS   HZ3  H N N 263 
LYS   HXT  H N N 264 
MET   N    N N N 265 
MET   CA   C N S 266 
MET   C    C N N 267 
MET   O    O N N 268 
MET   CB   C N N 269 
MET   CG   C N N 270 
MET   SD   S N N 271 
MET   CE   C N N 272 
MET   OXT  O N N 273 
MET   H    H N N 274 
MET   H2   H N N 275 
MET   HA   H N N 276 
MET   HB2  H N N 277 
MET   HB3  H N N 278 
MET   HG2  H N N 279 
MET   HG3  H N N 280 
MET   HE1  H N N 281 
MET   HE2  H N N 282 
MET   HE3  H N N 283 
MET   HXT  H N N 284 
PHE   N    N N N 285 
PHE   CA   C N S 286 
PHE   C    C N N 287 
PHE   O    O N N 288 
PHE   CB   C N N 289 
PHE   CG   C Y N 290 
PHE   CD1  C Y N 291 
PHE   CD2  C Y N 292 
PHE   CE1  C Y N 293 
PHE   CE2  C Y N 294 
PHE   CZ   C Y N 295 
PHE   OXT  O N N 296 
PHE   H    H N N 297 
PHE   H2   H N N 298 
PHE   HA   H N N 299 
PHE   HB2  H N N 300 
PHE   HB3  H N N 301 
PHE   HD1  H N N 302 
PHE   HD2  H N N 303 
PHE   HE1  H N N 304 
PHE   HE2  H N N 305 
PHE   HZ   H N N 306 
PHE   HXT  H N N 307 
PRO   N    N N N 308 
PRO   CA   C N S 309 
PRO   C    C N N 310 
PRO   O    O N N 311 
PRO   CB   C N N 312 
PRO   CG   C N N 313 
PRO   CD   C N N 314 
PRO   OXT  O N N 315 
PRO   H    H N N 316 
PRO   HA   H N N 317 
PRO   HB2  H N N 318 
PRO   HB3  H N N 319 
PRO   HG2  H N N 320 
PRO   HG3  H N N 321 
PRO   HD2  H N N 322 
PRO   HD3  H N N 323 
PRO   HXT  H N N 324 
SER   N    N N N 325 
SER   CA   C N S 326 
SER   C    C N N 327 
SER   O    O N N 328 
SER   CB   C N N 329 
SER   OG   O N N 330 
SER   OXT  O N N 331 
SER   H    H N N 332 
SER   H2   H N N 333 
SER   HA   H N N 334 
SER   HB2  H N N 335 
SER   HB3  H N N 336 
SER   HG   H N N 337 
SER   HXT  H N N 338 
THR   N    N N N 339 
THR   CA   C N S 340 
THR   C    C N N 341 
THR   O    O N N 342 
THR   CB   C N R 343 
THR   OG1  O N N 344 
THR   CG2  C N N 345 
THR   OXT  O N N 346 
THR   H    H N N 347 
THR   H2   H N N 348 
THR   HA   H N N 349 
THR   HB   H N N 350 
THR   HG1  H N N 351 
THR   HG21 H N N 352 
THR   HG22 H N N 353 
THR   HG23 H N N 354 
THR   HXT  H N N 355 
TRP   N    N N N 356 
TRP   CA   C N S 357 
TRP   C    C N N 358 
TRP   O    O N N 359 
TRP   CB   C N N 360 
TRP   CG   C Y N 361 
TRP   CD1  C Y N 362 
TRP   CD2  C Y N 363 
TRP   NE1  N Y N 364 
TRP   CE2  C Y N 365 
TRP   CE3  C Y N 366 
TRP   CZ2  C Y N 367 
TRP   CZ3  C Y N 368 
TRP   CH2  C Y N 369 
TRP   OXT  O N N 370 
TRP   H    H N N 371 
TRP   H2   H N N 372 
TRP   HA   H N N 373 
TRP   HB2  H N N 374 
TRP   HB3  H N N 375 
TRP   HD1  H N N 376 
TRP   HE1  H N N 377 
TRP   HE3  H N N 378 
TRP   HZ2  H N N 379 
TRP   HZ3  H N N 380 
TRP   HH2  H N N 381 
TRP   HXT  H N N 382 
TYR   N    N N N 383 
TYR   CA   C N S 384 
TYR   C    C N N 385 
TYR   O    O N N 386 
TYR   CB   C N N 387 
TYR   CG   C Y N 388 
TYR   CD1  C Y N 389 
TYR   CD2  C Y N 390 
TYR   CE1  C Y N 391 
TYR   CE2  C Y N 392 
TYR   CZ   C Y N 393 
TYR   OH   O N N 394 
TYR   OXT  O N N 395 
TYR   H    H N N 396 
TYR   H2   H N N 397 
TYR   HA   H N N 398 
TYR   HB2  H N N 399 
TYR   HB3  H N N 400 
TYR   HD1  H N N 401 
TYR   HD2  H N N 402 
TYR   HE1  H N N 403 
TYR   HE2  H N N 404 
TYR   HH   H N N 405 
TYR   HXT  H N N 406 
VAL   N    N N N 407 
VAL   CA   C N S 408 
VAL   C    C N N 409 
VAL   O    O N N 410 
VAL   CB   C N N 411 
VAL   CG1  C N N 412 
VAL   CG2  C N N 413 
VAL   OXT  O N N 414 
VAL   H    H N N 415 
VAL   H2   H N N 416 
VAL   HA   H N N 417 
VAL   HB   H N N 418 
VAL   HG11 H N N 419 
VAL   HG12 H N N 420 
VAL   HG13 H N N 421 
VAL   HG21 H N N 422 
VAL   HG22 H N N 423 
VAL   HG23 H N N 424 
VAL   HXT  H N N 425 
# 
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 
A1IU7 C13 N3   sing Y N 1   
A1IU7 C13 C14  doub Y N 2   
A1IU7 N3  C12  sing Y N 3   
A1IU7 C14 C15  sing Y N 4   
A1IU7 C12 N2   doub Y N 5   
A1IU7 C12 C15  sing Y N 6   
A1IU7 N2  C11  sing Y N 7   
A1IU7 C15 C16  doub Y N 8   
A1IU7 C11 C10  doub Y N 9   
A1IU7 C16 C10  sing Y N 10  
A1IU7 C10 C9   sing N N 11  
A1IU7 C9  C8   doub Y N 12  
A1IU7 C9  C4   sing Y N 13  
A1IU7 C8  C7   sing Y N 14  
A1IU7 C4  N1   sing N N 15  
A1IU7 C4  C5   doub Y N 16  
A1IU7 C7  C6   doub Y N 17  
A1IU7 N1  C3   sing N N 18  
A1IU7 C5  C6   sing Y N 19  
A1IU7 C3  C2   sing N N 20  
A1IU7 C3  O1   doub N N 21  
A1IU7 C2  C1   sing N N 22  
A1IU7 N1  H1   sing N N 23  
A1IU7 N3  H2   sing N N 24  
A1IU7 C5  H3   sing N N 25  
A1IU7 C6  H4   sing N N 26  
A1IU7 C7  H5   sing N N 27  
A1IU7 C8  H6   sing N N 28  
A1IU7 C13 H7   sing N N 29  
A1IU7 C1  H8   sing N N 30  
A1IU7 C1  H9   sing N N 31  
A1IU7 C1  H10  sing N N 32  
A1IU7 C2  H11  sing N N 33  
A1IU7 C2  H12  sing N N 34  
A1IU7 C11 H13  sing N N 35  
A1IU7 C14 H14  sing N N 36  
A1IU7 C16 H15  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TRP   N   CA   sing N N 343 
TRP   N   H    sing N N 344 
TRP   N   H2   sing N N 345 
TRP   CA  C    sing N N 346 
TRP   CA  CB   sing N N 347 
TRP   CA  HA   sing N N 348 
TRP   C   O    doub N N 349 
TRP   C   OXT  sing N N 350 
TRP   CB  CG   sing N N 351 
TRP   CB  HB2  sing N N 352 
TRP   CB  HB3  sing N N 353 
TRP   CG  CD1  doub Y N 354 
TRP   CG  CD2  sing Y N 355 
TRP   CD1 NE1  sing Y N 356 
TRP   CD1 HD1  sing N N 357 
TRP   CD2 CE2  doub Y N 358 
TRP   CD2 CE3  sing Y N 359 
TRP   NE1 CE2  sing Y N 360 
TRP   NE1 HE1  sing N N 361 
TRP   CE2 CZ2  sing Y N 362 
TRP   CE3 CZ3  doub Y N 363 
TRP   CE3 HE3  sing N N 364 
TRP   CZ2 CH2  doub Y N 365 
TRP   CZ2 HZ2  sing N N 366 
TRP   CZ3 CH2  sing Y N 367 
TRP   CZ3 HZ3  sing N N 368 
TRP   CH2 HH2  sing N N 369 
TRP   OXT HXT  sing N N 370 
TYR   N   CA   sing N N 371 
TYR   N   H    sing N N 372 
TYR   N   H2   sing N N 373 
TYR   CA  C    sing N N 374 
TYR   CA  CB   sing N N 375 
TYR   CA  HA   sing N N 376 
TYR   C   O    doub N N 377 
TYR   C   OXT  sing N N 378 
TYR   CB  CG   sing N N 379 
TYR   CB  HB2  sing N N 380 
TYR   CB  HB3  sing N N 381 
TYR   CG  CD1  doub Y N 382 
TYR   CG  CD2  sing Y N 383 
TYR   CD1 CE1  sing Y N 384 
TYR   CD1 HD1  sing N N 385 
TYR   CD2 CE2  doub Y N 386 
TYR   CD2 HD2  sing N N 387 
TYR   CE1 CZ   doub Y N 388 
TYR   CE1 HE1  sing N N 389 
TYR   CE2 CZ   sing Y N 390 
TYR   CE2 HE2  sing N N 391 
TYR   CZ  OH   sing N N 392 
TYR   OH  HH   sing N N 393 
TYR   OXT HXT  sing N N 394 
VAL   N   CA   sing N N 395 
VAL   N   H    sing N N 396 
VAL   N   H2   sing N N 397 
VAL   CA  C    sing N N 398 
VAL   CA  CB   sing N N 399 
VAL   CA  HA   sing N N 400 
VAL   C   O    doub N N 401 
VAL   C   OXT  sing N N 402 
VAL   CB  CG1  sing N N 403 
VAL   CB  CG2  sing N N 404 
VAL   CB  HB   sing N N 405 
VAL   CG1 HG11 sing N N 406 
VAL   CG1 HG12 sing N N 407 
VAL   CG1 HG13 sing N N 408 
VAL   CG2 HG21 sing N N 409 
VAL   CG2 HG22 sing N N 410 
VAL   CG2 HG23 sing N N 411 
VAL   OXT HXT  sing N N 412 
# 
_pdbx_audit_support.funding_organization   'The Structural Genomics Consortium (SGC)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7ZHQ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HHW 
_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]   0.020145 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001162 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.025029 
_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]   0.006010 
_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 
C 
N 
O 
S 
# 
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   . ALA   A 1 10  ? -13.636 39.160 -16.426 1.00 64.15  ? 21  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 10  ? -14.397 38.082 -17.110 1.00 64.18  ? 21  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 10  ? -13.993 36.713 -16.557 1.00 62.38  ? 21  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 10  ? -13.810 35.769 -17.333 1.00 58.03  ? 21  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 10  ? -14.180 38.179 -18.613 1.00 63.36  ? 21  ALA   A CB  1 
ATOM   6    N N   . ASP   A 1 11  ? -13.866 36.630 -15.216 1.00 60.00  ? 22  ASP   A N   1 
ATOM   7    C CA  . ASP   A 1 11  ? -13.490 35.412 -14.507 1.00 55.65  ? 22  ASP   A CA  1 
ATOM   8    C C   . ASP   A 1 11  ? -14.738 34.734 -13.961 1.00 48.51  ? 22  ASP   A C   1 
ATOM   9    O O   . ASP   A 1 11  ? -15.543 35.377 -13.289 1.00 46.22  ? 22  ASP   A O   1 
ATOM   10   C CB  . ASP   A 1 11  ? -12.538 35.658 -13.344 1.00 57.37  ? 22  ASP   A CB  1 
ATOM   11   C CG  . ASP   A 1 11  ? -11.059 35.695 -13.705 1.00 61.22  ? 22  ASP   A CG  1 
ATOM   12   O OD1 . ASP   A 1 11  ? -10.746 35.718 -14.919 1.00 62.79  ? 22  ASP   A OD1 1 
ATOM   13   O OD2 . ASP   A 1 11  ? -10.229 35.664 -12.773 1.00 60.24  ? 22  ASP   A OD2 1 
ATOM   14   N N   . ILE   A 1 12  ? -14.835 33.428 -14.240 1.00 42.76  ? 23  ILE   A N   1 
ATOM   15   C CA  . ILE   A 1 12  ? -16.036 32.636 -14.028 1.00 37.57  ? 23  ILE   A CA  1 
ATOM   16   C C   . ILE   A 1 12  ? -16.330 32.568 -12.534 1.00 37.39  ? 23  ILE   A C   1 
ATOM   17   O O   . ILE   A 1 12  ? -17.471 32.767 -12.126 1.00 37.24  ? 23  ILE   A O   1 
ATOM   18   C CB  . ILE   A 1 12  ? -15.876 31.243 -14.666 1.00 33.98  ? 23  ILE   A CB  1 
ATOM   19   C CG1 . ILE   A 1 12  ? -15.979 31.318 -16.187 1.00 31.99  ? 23  ILE   A CG1 1 
ATOM   20   C CG2 . ILE   A 1 12  ? -16.874 30.241 -14.088 1.00 32.44  ? 23  ILE   A CG2 1 
ATOM   21   C CD1 . ILE   A 1 12  ? -15.635 30.020 -16.899 1.00 32.55  ? 23  ILE   A CD1 1 
ATOM   22   N N   . LEU   A 1 13  ? -15.290 32.306 -11.732 1.00 38.33  ? 24  LEU   A N   1 
ATOM   23   C CA  . LEU   A 1 13  ? -15.384 32.404 -10.282 1.00 37.66  ? 24  LEU   A CA  1 
ATOM   24   C C   . LEU   A 1 13  ? -14.398 33.456 -9.782  1.00 38.67  ? 24  LEU   A C   1 
ATOM   25   O O   . LEU   A 1 13  ? -13.272 33.573 -10.277 1.00 36.37  ? 24  LEU   A O   1 
ATOM   26   C CB  . LEU   A 1 13  ? -15.119 31.062 -9.607  1.00 36.23  ? 24  LEU   A CB  1 
ATOM   27   C CG  . LEU   A 1 13  ? -15.758 29.851 -10.287 1.00 33.83  ? 24  LEU   A CG  1 
ATOM   28   C CD1 . LEU   A 1 13  ? -15.217 28.527 -9.783  1.00 34.34  ? 24  LEU   A CD1 1 
ATOM   29   C CD2 . LEU   A 1 13  ? -17.231 29.934 -10.076 1.00 32.93  ? 24  LEU   A CD2 1 
ATOM   30   N N   . PRO   A 1 14  ? -14.801 34.246 -8.764  1.00 39.51  ? 25  PRO   A N   1 
ATOM   31   C CA  . PRO   A 1 14  ? -13.875 35.108 -8.044  1.00 39.10  ? 25  PRO   A CA  1 
ATOM   32   C C   . PRO   A 1 14  ? -13.309 34.292 -6.891  1.00 37.89  ? 25  PRO   A C   1 
ATOM   33   O O   . PRO   A 1 14  ? -13.818 33.215 -6.578  1.00 35.85  ? 25  PRO   A O   1 
ATOM   34   C CB  . PRO   A 1 14  ? -14.755 36.280 -7.580  1.00 40.72  ? 25  PRO   A CB  1 
ATOM   35   C CG  . PRO   A 1 14  ? -16.196 35.761 -7.667  1.00 41.86  ? 25  PRO   A CG  1 
ATOM   36   C CD  . PRO   A 1 14  ? -16.165 34.342 -8.229  1.00 40.70  ? 25  PRO   A CD  1 
ATOM   37   N N   . ALA   A 1 15  ? -12.270 34.847 -6.264  1.00 39.11  ? 26  ALA   A N   1 
ATOM   38   C CA  . ALA   A 1 15  ? -11.586 34.205 -5.157  1.00 38.69  ? 26  ALA   A CA  1 
ATOM   39   C C   . ALA   A 1 15  ? -12.544 34.045 -3.986  1.00 39.81  ? 26  ALA   A C   1 
ATOM   40   O O   . ALA   A 1 15  ? -13.505 34.797 -3.858  1.00 40.81  ? 26  ALA   A O   1 
ATOM   41   C CB  . ALA   A 1 15  ? -10.375 35.012 -4.762  1.00 37.86  ? 26  ALA   A CB  1 
ATOM   42   N N   . ASN   A 1 16  ? -12.276 33.024 -3.169  1.00 42.34  ? 27  ASN   A N   1 
ATOM   43   C CA  . ASN   A 1 16  ? -13.016 32.742 -1.951  1.00 45.04  ? 27  ASN   A CA  1 
ATOM   44   C C   . ASN   A 1 16  ? -14.442 32.294 -2.274  1.00 49.38  ? 27  ASN   A C   1 
ATOM   45   O O   . ASN   A 1 16  ? -15.236 32.074 -1.361  1.00 55.82  ? 27  ASN   A O   1 
ATOM   46   C CB  . ASN   A 1 16  ? -12.885 33.899 -0.970  1.00 45.01  ? 27  ASN   A CB  1 
ATOM   47   C CG  . ASN   A 1 16  ? -11.432 34.276 -0.791  1.00 46.15  ? 27  ASN   A CG  1 
ATOM   48   O OD1 . ASN   A 1 16  ? -10.583 33.399 -0.594  1.00 48.12  ? 27  ASN   A OD1 1 
ATOM   49   N ND2 . ASN   A 1 16  ? -11.107 35.550 -0.929  1.00 44.34  ? 27  ASN   A ND2 1 
ATOM   50   N N   . TYR   A 1 17  ? -14.752 32.098 -3.563  1.00 50.89  ? 28  TYR   A N   1 
ATOM   51   C CA  . TYR   A 1 17  ? -15.975 31.411 -3.941  1.00 52.11  ? 28  TYR   A CA  1 
ATOM   52   C C   . TYR   A 1 17  ? -15.870 29.974 -3.427  1.00 50.49  ? 28  TYR   A C   1 
ATOM   53   O O   . TYR   A 1 17  ? -14.769 29.433 -3.390  1.00 53.90  ? 28  TYR   A O   1 
ATOM   54   C CB  . TYR   A 1 17  ? -16.176 31.513 -5.460  1.00 52.80  ? 28  TYR   A CB  1 
ATOM   55   C CG  . TYR   A 1 17  ? -17.574 31.067 -5.862  1.00 55.49  ? 28  TYR   A CG  1 
ATOM   56   C CD1 . TYR   A 1 17  ? -17.857 29.721 -6.079  1.00 54.49  ? 28  TYR   A CD1 1 
ATOM   57   C CD2 . TYR   A 1 17  ? -18.625 31.978 -5.948  1.00 54.15  ? 28  TYR   A CD2 1 
ATOM   58   C CE1 . TYR   A 1 17  ? -19.139 29.299 -6.399  1.00 56.53  ? 28  TYR   A CE1 1 
ATOM   59   C CE2 . TYR   A 1 17  ? -19.909 31.569 -6.271  1.00 54.08  ? 28  TYR   A CE2 1 
ATOM   60   C CZ  . TYR   A 1 17  ? -20.165 30.225 -6.496  1.00 57.55  ? 28  TYR   A CZ  1 
ATOM   61   O OH  . TYR   A 1 17  ? -21.424 29.807 -6.817  1.00 60.90  ? 28  TYR   A OH  1 
ATOM   62   N N   . VAL   A 1 18  ? -16.994 29.363 -3.023  1.00 47.01  ? 29  VAL   A N   1 
ATOM   63   C CA  . VAL   A 1 18  ? -16.990 27.985 -2.539  1.00 47.77  ? 29  VAL   A CA  1 
ATOM   64   C C   . VAL   A 1 18  ? -17.930 27.118 -3.373  1.00 50.52  ? 29  VAL   A C   1 
ATOM   65   O O   . VAL   A 1 18  ? -19.151 27.252 -3.287  1.00 60.09  ? 29  VAL   A O   1 
ATOM   66   C CB  . VAL   A 1 18  ? -17.387 27.888 -1.051  1.00 45.37  ? 29  VAL   A CB  1 
ATOM   67   C CG1 . VAL   A 1 18  ? -17.540 26.443 -0.582  1.00 41.31  ? 29  VAL   A CG1 1 
ATOM   68   C CG2 . VAL   A 1 18  ? -16.411 28.649 -0.164  1.00 45.97  ? 29  VAL   A CG2 1 
ATOM   69   N N   . VAL   A 1 19  ? -17.371 26.132 -4.077  1.00 48.43  ? 30  VAL   A N   1 
ATOM   70   C CA  . VAL   A 1 19  ? -18.201 25.194 -4.818  1.00 49.09  ? 30  VAL   A CA  1 
ATOM   71   C C   . VAL   A 1 19  ? -18.613 24.051 -3.878  1.00 49.65  ? 30  VAL   A C   1 
ATOM   72   O O   . VAL   A 1 19  ? -17.762 23.505 -3.183  1.00 47.19  ? 30  VAL   A O   1 
ATOM   73   C CB  . VAL   A 1 19  ? -17.457 24.697 -6.077  1.00 46.26  ? 30  VAL   A CB  1 
ATOM   74   C CG1 . VAL   A 1 19  ? -18.234 23.624 -6.840  1.00 45.09  ? 30  VAL   A CG1 1 
ATOM   75   C CG2 . VAL   A 1 19  ? -17.084 25.851 -6.999  1.00 43.71  ? 30  VAL   A CG2 1 
ATOM   76   N N   . LYS   A 1 20  ? -19.920 23.731 -3.832  1.00 50.87  ? 31  LYS   A N   1 
ATOM   77   C CA  . LYS   A 1 20  ? -20.473 22.576 -3.127  1.00 54.62  ? 31  LYS   A CA  1 
ATOM   78   C C   . LYS   A 1 20  ? -19.930 22.444 -1.692  1.00 55.28  ? 31  LYS   A C   1 
ATOM   79   O O   . LYS   A 1 20  ? -19.685 21.326 -1.228  1.00 50.93  ? 31  LYS   A O   1 
ATOM   80   C CB  . LYS   A 1 20  ? -20.230 21.338 -4.005  1.00 54.88  ? 31  LYS   A CB  1 
ATOM   81   C CG  . LYS   A 1 20  ? -21.279 20.234 -3.947  1.00 58.91  ? 31  LYS   A CG  1 
ATOM   82   C CD  . LYS   A 1 20  ? -20.638 18.856 -3.849  1.00 61.52  ? 31  LYS   A CD  1 
ATOM   83   C CE  . LYS   A 1 20  ? -21.633 17.753 -4.060  1.00 62.23  ? 31  LYS   A CE  1 
ATOM   84   N NZ  . LYS   A 1 20  ? -21.019 16.428 -3.935  1.00 60.45  ? 31  LYS   A NZ  1 
ATOM   85   N N   . ASP   A 1 21  ? -19.784 23.572 -0.972  1.00 54.65  ? 32  ASP   A N   1 
ATOM   86   C CA  . ASP   A 1 21  ? -19.322 23.570 0.409   1.00 53.07  ? 32  ASP   A CA  1 
ATOM   87   C C   . ASP   A 1 21  ? -18.144 22.620 0.631   1.00 49.80  ? 32  ASP   A C   1 
ATOM   88   O O   . ASP   A 1 21  ? -18.185 21.854 1.595   1.00 57.44  ? 32  ASP   A O   1 
ATOM   89   C CB  . ASP   A 1 21  ? -20.454 23.188 1.350   1.00 57.38  ? 32  ASP   A CB  1 
ATOM   90   C CG  . ASP   A 1 21  ? -21.335 24.343 1.802   1.00 65.82  ? 32  ASP   A CG  1 
ATOM   91   O OD1 . ASP   A 1 21  ? -20.810 25.262 2.467   1.00 71.42  ? 32  ASP   A OD1 1 
ATOM   92   O OD2 . ASP   A 1 21  ? -22.539 24.311 1.490   1.00 67.47  ? 32  ASP   A OD2 1 
ATOM   93   N N   . ARG   A 1 22  ? -17.107 22.689 -0.222  1.00 42.76  ? 33  ARG   A N   1 
ATOM   94   C CA  . ARG   A 1 22  ? -15.932 21.833 -0.086  1.00 35.88  ? 33  ARG   A CA  1 
ATOM   95   C C   . ARG   A 1 22  ? -14.694 22.418 -0.779  1.00 35.23  ? 33  ARG   A C   1 
ATOM   96   O O   . ARG   A 1 22  ? -13.561 22.099 -0.405  1.00 34.87  ? 33  ARG   A O   1 
ATOM   97   C CB  . ARG   A 1 22  ? -16.183 20.422 -0.635  1.00 29.34  ? 33  ARG   A CB  1 
ATOM   98   C CG  . ARG   A 1 22  ? -15.271 19.386 0.001   1.00 26.72  ? 33  ARG   A CG  1 
ATOM   99   C CD  . ARG   A 1 22  ? -15.534 18.037 -0.596  1.00 25.39  ? 33  ARG   A CD  1 
ATOM   100  N NE  . ARG   A 1 22  ? -14.300 17.263 -0.713  1.00 23.31  ? 33  ARG   A NE  1 
ATOM   101  C CZ  . ARG   A 1 22  ? -14.282 16.027 -1.164  1.00 23.00  ? 33  ARG   A CZ  1 
ATOM   102  N NH1 . ARG   A 1 22  ? -15.415 15.366 -1.313  1.00 21.28  ? 33  ARG   A NH1 1 
ATOM   103  N NH2 . ARG   A 1 22  ? -13.128 15.450 -1.455  1.00 25.62  ? 33  ARG   A NH2 1 
ATOM   104  N N   . TRP   A 1 23  ? -14.884 23.268 -1.791  1.00 32.69  ? 34  TRP   A N   1 
ATOM   105  C CA  . TRP   A 1 23  ? -13.745 23.714 -2.576  1.00 31.81  ? 34  TRP   A CA  1 
ATOM   106  C C   . TRP   A 1 23  ? -13.701 25.236 -2.676  1.00 34.90  ? 34  TRP   A C   1 
ATOM   107  O O   . TRP   A 1 23  ? -14.402 25.832 -3.497  1.00 34.84  ? 34  TRP   A O   1 
ATOM   108  C CB  . TRP   A 1 23  ? -13.768 23.053 -3.959  1.00 29.11  ? 34  TRP   A CB  1 
ATOM   109  C CG  . TRP   A 1 23  ? -13.714 21.553 -3.886  1.00 26.53  ? 34  TRP   A CG  1 
ATOM   110  C CD1 . TRP   A 1 23  ? -12.652 20.791 -3.508  1.00 26.55  ? 34  TRP   A CD1 1 
ATOM   111  C CD2 . TRP   A 1 23  ? -14.778 20.632 -4.192  1.00 25.71  ? 34  TRP   A CD2 1 
ATOM   112  N NE1 . TRP   A 1 23  ? -12.970 19.459 -3.566  1.00 26.14  ? 34  TRP   A NE1 1 
ATOM   113  C CE2 . TRP   A 1 23  ? -14.266 19.329 -3.982  1.00 24.86  ? 34  TRP   A CE2 1 
ATOM   114  C CE3 . TRP   A 1 23  ? -16.100 20.781 -4.630  1.00 26.03  ? 34  TRP   A CE3 1 
ATOM   115  C CZ2 . TRP   A 1 23  ? -15.026 18.182 -4.187  1.00 23.84  ? 34  TRP   A CZ2 1 
ATOM   116  C CZ3 . TRP   A 1 23  ? -16.858 19.645 -4.822  1.00 26.09  ? 34  TRP   A CZ3 1 
ATOM   117  C CH2 . TRP   A 1 23  ? -16.324 18.369 -4.606  1.00 25.52  ? 34  TRP   A CH2 1 
ATOM   118  N N   . LYS   A 1 24  ? -12.833 25.843 -1.848  1.00 37.59  ? 35  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 24  ? -12.701 27.291 -1.773  1.00 40.41  ? 35  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 24  ? -11.667 27.759 -2.795  1.00 38.37  ? 35  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 24  ? -10.490 27.410 -2.698  1.00 39.96  ? 35  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 24  ? -12.337 27.719 -0.345  1.00 42.79  ? 35  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 24  ? -12.151 29.210 -0.142  1.00 46.56  ? 35  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 24  ? -11.741 29.559 1.280   1.00 53.22  ? 35  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 24  ? -11.873 31.016 1.569   1.00 57.16  ? 35  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 24  ? -11.439 31.299 2.940   1.00 59.90  ? 35  LYS   A NZ  1 
ATOM   127  N N   . VAL   A 1 25  ? -12.109 28.558 -3.772  1.00 35.13  ? 36  VAL   A N   1 
ATOM   128  C CA  . VAL   A 1 25  ? -11.233 28.948 -4.861  1.00 36.02  ? 36  VAL   A CA  1 
ATOM   129  C C   . VAL   A 1 25  ? -10.153 29.854 -4.285  1.00 40.82  ? 36  VAL   A C   1 
ATOM   130  O O   . VAL   A 1 25  ? -10.473 30.758 -3.516  1.00 45.46  ? 36  VAL   A O   1 
ATOM   131  C CB  . VAL   A 1 25  ? -11.968 29.639 -6.021  1.00 34.66  ? 36  VAL   A CB  1 
ATOM   132  C CG1 . VAL   A 1 25  ? -10.996 30.263 -7.010  1.00 32.96  ? 36  VAL   A CG1 1 
ATOM   133  C CG2 . VAL   A 1 25  ? -12.921 28.689 -6.738  1.00 34.62  ? 36  VAL   A CG2 1 
ATOM   134  N N   . LEU   A 1 26  ? -8.891  29.594 -4.680  1.00 43.13  ? 37  LEU   A N   1 
ATOM   135  C CA  . LEU   A 1 26  ? -7.717  30.310 -4.198  1.00 39.37  ? 37  LEU   A CA  1 
ATOM   136  C C   . LEU   A 1 26  ? -7.200  31.255 -5.281  1.00 37.98  ? 37  LEU   A C   1 
ATOM   137  O O   . LEU   A 1 26  ? -7.030  32.447 -5.052  1.00 37.40  ? 37  LEU   A O   1 
ATOM   138  C CB  . LEU   A 1 26  ? -6.663  29.291 -3.773  1.00 39.14  ? 37  LEU   A CB  1 
ATOM   139  C CG  . LEU   A 1 26  ? -7.123  28.268 -2.726  1.00 39.38  ? 37  LEU   A CG  1 
ATOM   140  C CD1 . LEU   A 1 26  ? -6.110  27.145 -2.551  1.00 39.07  ? 37  LEU   A CD1 1 
ATOM   141  C CD2 . LEU   A 1 26  ? -7.401  28.949 -1.395  1.00 38.71  ? 37  LEU   A CD2 1 
ATOM   142  N N   . LYS   A 1 27  ? -6.966  30.739 -6.481  1.00 38.85  ? 38  LYS   A N   1 
ATOM   143  C CA  . LYS   A 1 27  ? -6.666  31.631 -7.585  1.00 41.03  ? 38  LYS   A CA  1 
ATOM   144  C C   . LYS   A 1 27  ? -6.933  30.938 -8.918  1.00 41.97  ? 38  LYS   A C   1 
ATOM   145  O O   . LYS   A 1 27  ? -7.049  29.710 -9.018  1.00 39.89  ? 38  LYS   A O   1 
ATOM   146  C CB  . LYS   A 1 27  ? -5.212  32.113 -7.508  1.00 43.31  ? 38  LYS   A CB  1 
ATOM   147  C CG  . LYS   A 1 27  ? -4.199  30.983 -7.593  1.00 46.94  ? 38  LYS   A CG  1 
ATOM   148  C CD  . LYS   A 1 27  ? -2.793  31.285 -7.087  1.00 48.17  ? 38  LYS   A CD  1 
ATOM   149  C CE  . LYS   A 1 27  ? -2.023  30.021 -6.839  1.00 49.01  ? 38  LYS   A CE  1 
ATOM   150  N NZ  . LYS   A 1 27  ? -0.861  30.259 -5.976  1.00 51.21  ? 38  LYS   A NZ  1 
ATOM   151  N N   . LYS   A 1 28  ? -7.038  31.778 -9.947  1.00 41.26  ? 39  LYS   A N   1 
ATOM   152  C CA  . LYS   A 1 28  ? -6.975  31.307 -11.311 1.00 42.36  ? 39  LYS   A CA  1 
ATOM   153  C C   . LYS   A 1 28  ? -5.525  30.897 -11.550 1.00 43.96  ? 39  LYS   A C   1 
ATOM   154  O O   . LYS   A 1 28  ? -4.609  31.467 -10.948 1.00 38.69  ? 39  LYS   A O   1 
ATOM   155  C CB  . LYS   A 1 28  ? -7.512  32.377 -12.272 1.00 42.56  ? 39  LYS   A CB  1 
ATOM   156  C CG  . LYS   A 1 28  ? -7.502  31.971 -13.742 1.00 46.70  ? 39  LYS   A CG  1 
ATOM   157  C CD  . LYS   A 1 28  ? -7.946  33.032 -14.747 1.00 49.54  ? 39  LYS   A CD  1 
ATOM   158  C CE  . LYS   A 1 28  ? -7.722  32.557 -16.168 1.00 50.12  ? 39  LYS   A CE  1 
ATOM   159  N NZ  . LYS   A 1 28  ? -7.965  33.569 -17.201 1.00 48.94  ? 39  LYS   A NZ  1 
ATOM   160  N N   . ILE   A 1 29  ? -5.348  29.862 -12.382 1.00 46.82  ? 40  ILE   A N   1 
ATOM   161  C CA  . ILE   A 1 29  ? -4.032  29.408 -12.807 1.00 45.85  ? 40  ILE   A CA  1 
ATOM   162  C C   . ILE   A 1 29  ? -4.018  29.179 -14.320 1.00 49.03  ? 40  ILE   A C   1 
ATOM   163  O O   . ILE   A 1 29  ? -2.992  29.383 -14.960 1.00 50.03  ? 40  ILE   A O   1 
ATOM   164  C CB  . ILE   A 1 29  ? -3.582  28.171 -11.999 1.00 43.04  ? 40  ILE   A CB  1 
ATOM   165  C CG1 . ILE   A 1 29  ? -4.574  27.005 -12.094 1.00 40.82  ? 40  ILE   A CG1 1 
ATOM   166  C CG2 . ILE   A 1 29  ? -3.324  28.565 -10.544 1.00 45.05  ? 40  ILE   A CG2 1 
ATOM   167  C CD1 . ILE   A 1 29  ? -4.128  25.738 -11.390 1.00 38.21  ? 40  ILE   A CD1 1 
ATOM   168  N N   . GLY   A 1 30  ? -5.150  28.771 -14.901 1.00 54.27  ? 41  GLY   A N   1 
ATOM   169  C CA  . GLY   A 1 30  ? -5.231  28.618 -16.342 1.00 59.73  ? 41  GLY   A CA  1 
ATOM   170  C C   . GLY   A 1 30  ? -6.442  29.366 -16.884 1.00 67.92  ? 41  GLY   A C   1 
ATOM   171  O O   . GLY   A 1 30  ? -7.432  29.542 -16.177 1.00 65.99  ? 41  GLY   A O   1 
ATOM   172  N N   . GLY   A 1 31  ? -6.330  29.815 -18.138 1.00 76.05  ? 42  GLY   A N   1 
ATOM   173  C CA  . GLY   A 1 31  ? -7.472  30.290 -18.898 1.00 77.66  ? 42  GLY   A CA  1 
ATOM   174  C C   . GLY   A 1 31  ? -7.515  29.614 -20.262 1.00 78.82  ? 42  GLY   A C   1 
ATOM   175  O O   . GLY   A 1 31  ? -6.861  28.591 -20.474 1.00 83.39  ? 42  GLY   A O   1 
ATOM   176  N N   . GLY   A 1 32  ? -8.299  30.205 -21.167 1.00 76.46  ? 43  GLY   A N   1 
ATOM   177  C CA  . GLY   A 1 32  ? -8.319  29.803 -22.563 1.00 74.35  ? 43  GLY   A CA  1 
ATOM   178  C C   . GLY   A 1 32  ? -9.680  30.096 -23.179 1.00 70.86  ? 43  GLY   A C   1 
ATOM   179  O O   . GLY   A 1 32  ? -10.550 30.665 -22.526 1.00 66.20  ? 43  GLY   A O   1 
ATOM   180  N N   . GLY   A 1 33  ? -9.857  29.684 -24.434 1.00 72.61  ? 44  GLY   A N   1 
ATOM   181  C CA  . GLY   A 1 33  ? -11.146 29.814 -25.087 1.00 75.97  ? 44  GLY   A CA  1 
ATOM   182  C C   . GLY   A 1 33  ? -12.242 29.061 -24.330 1.00 74.53  ? 44  GLY   A C   1 
ATOM   183  O O   . GLY   A 1 33  ? -13.342 29.582 -24.166 1.00 78.25  ? 44  GLY   A O   1 
ATOM   184  N N   . PHE   A 1 34  ? -11.927 27.856 -23.836 1.00 65.50  ? 45  PHE   A N   1 
ATOM   185  C CA  . PHE   A 1 34  ? -12.951 26.859 -23.564 1.00 60.24  ? 45  PHE   A CA  1 
ATOM   186  C C   . PHE   A 1 34  ? -12.987 26.475 -22.084 1.00 54.13  ? 45  PHE   A C   1 
ATOM   187  O O   . PHE   A 1 34  ? -13.446 25.392 -21.741 1.00 56.03  ? 45  PHE   A O   1 
ATOM   188  C CB  . PHE   A 1 34  ? -12.639 25.683 -24.498 1.00 64.12  ? 45  PHE   A CB  1 
ATOM   189  C CG  . PHE   A 1 34  ? -12.634 26.006 -25.990 1.00 70.92  ? 45  PHE   A CG  1 
ATOM   190  C CD1 . PHE   A 1 34  ? -11.648 26.819 -26.552 1.00 72.37  ? 45  PHE   A CD1 1 
ATOM   191  C CD2 . PHE   A 1 34  ? -13.592 25.458 -26.841 1.00 71.71  ? 45  PHE   A CD2 1 
ATOM   192  C CE1 . PHE   A 1 34  ? -11.646 27.105 -27.912 1.00 74.10  ? 45  PHE   A CE1 1 
ATOM   193  C CE2 . PHE   A 1 34  ? -13.578 25.738 -28.203 1.00 74.25  ? 45  PHE   A CE2 1 
ATOM   194  C CZ  . PHE   A 1 34  ? -12.608 26.561 -28.737 1.00 75.96  ? 45  PHE   A CZ  1 
ATOM   195  N N   . GLY   A 1 35  ? -12.531 27.357 -21.194 1.00 47.25  ? 46  GLY   A N   1 
ATOM   196  C CA  . GLY   A 1 35  ? -12.610 27.058 -19.777 1.00 44.03  ? 46  GLY   A CA  1 
ATOM   197  C C   . GLY   A 1 35  ? -11.507 27.764 -19.003 1.00 42.59  ? 46  GLY   A C   1 
ATOM   198  O O   . GLY   A 1 35  ? -10.496 28.169 -19.571 1.00 42.92  ? 46  GLY   A O   1 
ATOM   199  N N   . GLU   A 1 36  ? -11.737 27.908 -17.696 1.00 41.03  ? 47  GLU   A N   1 
ATOM   200  C CA  . GLU   A 1 36  ? -10.765 28.463 -16.774 1.00 40.04  ? 47  GLU   A CA  1 
ATOM   201  C C   . GLU   A 1 36  ? -10.395 27.374 -15.766 1.00 38.78  ? 47  GLU   A C   1 
ATOM   202  O O   . GLU   A 1 36  ? -11.214 26.510 -15.470 1.00 35.65  ? 47  GLU   A O   1 
ATOM   203  C CB  . GLU   A 1 36  ? -11.385 29.698 -16.119 1.00 41.63  ? 47  GLU   A CB  1 
ATOM   204  C CG  . GLU   A 1 36  ? -11.819 30.779 -17.109 1.00 43.41  ? 47  GLU   A CG  1 
ATOM   205  C CD  . GLU   A 1 36  ? -12.393 32.050 -16.491 1.00 45.49  ? 47  GLU   A CD  1 
ATOM   206  O OE1 . GLU   A 1 36  ? -12.505 32.100 -15.248 1.00 43.96  ? 47  GLU   A OE1 1 
ATOM   207  O OE2 . GLU   A 1 36  ? -12.732 33.005 -17.235 1.00 45.79  ? 47  GLU   A OE2 1 
ATOM   208  N N   . ILE   A 1 37  ? -9.152  27.413 -15.258 1.00 40.41  ? 48  ILE   A N   1 
ATOM   209  C CA  . ILE   A 1 37  ? -8.647  26.435 -14.301 1.00 37.09  ? 48  ILE   A CA  1 
ATOM   210  C C   . ILE   A 1 37  ? -8.169  27.170 -13.049 1.00 34.93  ? 48  ILE   A C   1 
ATOM   211  O O   . ILE   A 1 37  ? -7.682  28.299 -13.135 1.00 35.12  ? 48  ILE   A O   1 
ATOM   212  C CB  . ILE   A 1 37  ? -7.530  25.563 -14.905 1.00 36.50  ? 48  ILE   A CB  1 
ATOM   213  C CG1 . ILE   A 1 37  ? -7.925  24.923 -16.267 1.00 37.69  ? 48  ILE   A CG1 1 
ATOM   214  C CG2 . ILE   A 1 37  ? -7.107  24.508 -13.883 1.00 35.62  ? 48  ILE   A CG2 1 
ATOM   215  C CD1 . ILE   A 1 37  ? -7.563  25.722 -17.512 1.00 37.85  ? 48  ILE   A CD1 1 
ATOM   216  N N   . TYR   A 1 38  ? -8.314  26.511 -11.891 1.00 32.81  ? 49  TYR   A N   1 
ATOM   217  C CA  . TYR   A 1 38  ? -8.203  27.179 -10.606 1.00 32.72  ? 49  TYR   A CA  1 
ATOM   218  C C   . TYR   A 1 38  ? -7.588  26.272 -9.553  1.00 30.50  ? 49  TYR   A C   1 
ATOM   219  O O   . TYR   A 1 38  ? -7.864  25.078 -9.490  1.00 26.69  ? 49  TYR   A O   1 
ATOM   220  C CB  . TYR   A 1 38  ? -9.575  27.534 -10.032 1.00 36.31  ? 49  TYR   A CB  1 
ATOM   221  C CG  . TYR   A 1 38  ? -10.294 28.663 -10.748 1.00 38.52  ? 49  TYR   A CG  1 
ATOM   222  C CD1 . TYR   A 1 38  ? -10.976 28.439 -11.935 1.00 39.95  ? 49  TYR   A CD1 1 
ATOM   223  C CD2 . TYR   A 1 38  ? -10.298 29.948 -10.224 1.00 39.65  ? 49  TYR   A CD2 1 
ATOM   224  C CE1 . TYR   A 1 38  ? -11.619 29.473 -12.596 1.00 42.74  ? 49  TYR   A CE1 1 
ATOM   225  C CE2 . TYR   A 1 38  ? -10.951 30.987 -10.865 1.00 41.54  ? 49  TYR   A CE2 1 
ATOM   226  C CZ  . TYR   A 1 38  ? -11.615 30.751 -12.054 1.00 44.61  ? 49  TYR   A CZ  1 
ATOM   227  O OH  . TYR   A 1 38  ? -12.242 31.815 -12.649 1.00 49.20  ? 49  TYR   A OH  1 
ATOM   228  N N   . GLU   A 1 39  ? -6.817  26.897 -8.666  1.00 32.95  ? 50  GLU   A N   1 
ATOM   229  C CA  . GLU   A 1 39  ? -6.363  26.217 -7.467  1.00 34.14  ? 50  GLU   A CA  1 
ATOM   230  C C   . GLU   A 1 39  ? -7.425  26.400 -6.396  1.00 27.85  ? 50  GLU   A C   1 
ATOM   231  O O   . GLU   A 1 39  ? -7.868  27.515 -6.140  1.00 24.64  ? 50  GLU   A O   1 
ATOM   232  C CB  . GLU   A 1 39  ? -4.995  26.711 -6.981  1.00 38.43  ? 50  GLU   A CB  1 
ATOM   233  C CG  . GLU   A 1 39  ? -4.338  25.766 -5.972  1.00 40.27  ? 50  GLU   A CG  1 
ATOM   234  C CD  . GLU   A 1 39  ? -2.863  25.970 -5.662  1.00 43.02  ? 50  GLU   A CD  1 
ATOM   235  O OE1 . GLU   A 1 39  ? -2.156  26.846 -6.214  1.00 44.74  ? 50  GLU   A OE1 1 
ATOM   236  O OE2 . GLU   A 1 39  ? -2.415  25.179 -4.816  1.00 48.94  ? 50  GLU   A OE2 1 
ATOM   237  N N   . ALA   A 1 40  ? -7.809  25.293 -5.774  1.00 25.18  ? 51  ALA   A N   1 
ATOM   238  C CA  . ALA   A 1 40  ? -8.790  25.357 -4.717  1.00 26.79  ? 51  ALA   A CA  1 
ATOM   239  C C   . ALA   A 1 40  ? -8.299  24.613 -3.489  1.00 25.83  ? 51  ALA   A C   1 
ATOM   240  O O   . ALA   A 1 40  ? -7.783  23.507 -3.598  1.00 27.64  ? 51  ALA   A O   1 
ATOM   241  C CB  . ALA   A 1 40  ? -10.066 24.742 -5.219  1.00 30.18  ? 51  ALA   A CB  1 
ATOM   242  N N   . MET   A 1 41  ? -8.549  25.166 -2.309  1.00 24.63  ? 52  MET   A N   1 
ATOM   243  C CA  . MET   A 1 41  ? -8.390  24.355 -1.120  1.00 25.06  ? 52  MET   A CA  1 
ATOM   244  C C   . MET   A 1 41  ? -9.604  23.448 -0.942  1.00 27.98  ? 52  MET   A C   1 
ATOM   245  O O   . MET   A 1 41  ? -10.741 23.920 -0.939  1.00 30.43  ? 52  MET   A O   1 
ATOM   246  C CB  . MET   A 1 41  ? -8.276  25.199 0.140   1.00 23.75  ? 52  MET   A CB  1 
ATOM   247  C CG  . MET   A 1 41  ? -8.015  24.343 1.326   1.00 24.61  ? 52  MET   A CG  1 
ATOM   248  S SD  . MET   A 1 41  ? -8.134  25.311 2.836   1.00 28.09  ? 52  MET   A SD  1 
ATOM   249  C CE  . MET   A 1 41  ? -7.681  23.915 3.876   1.00 27.20  ? 52  MET   A CE  1 
ATOM   250  N N   . ASP   A 1 42  ? -9.352  22.147 -0.752  1.00 28.88  ? 53  ASP   A N   1 
ATOM   251  C CA  . ASP   A 1 42  ? -10.380 21.232 -0.278  1.00 29.86  ? 53  ASP   A CA  1 
ATOM   252  C C   . ASP   A 1 42  ? -10.610 21.531 1.203   1.00 30.16  ? 53  ASP   A C   1 
ATOM   253  O O   . ASP   A 1 42  ? -9.669  21.545 1.995   1.00 30.80  ? 53  ASP   A O   1 
ATOM   254  C CB  . ASP   A 1 42  ? -9.993  19.773 -0.508  1.00 30.93  ? 53  ASP   A CB  1 
ATOM   255  C CG  . ASP   A 1 42  ? -11.128 18.751 -0.514  1.00 30.76  ? 53  ASP   A CG  1 
ATOM   256  O OD1 . ASP   A 1 42  ? -12.092 18.925 0.259   1.00 31.96  ? 53  ASP   A OD1 1 
ATOM   257  O OD2 . ASP   A 1 42  ? -11.028 17.760 -1.273  1.00 29.19  ? 53  ASP   A OD2 1 
ATOM   258  N N   . LEU   A 1 43  ? -11.863 21.787 1.573   1.00 28.90  ? 54  LEU   A N   1 
ATOM   259  C CA  . LEU   A 1 43  ? -12.177 22.130 2.947   1.00 28.39  ? 54  LEU   A CA  1 
ATOM   260  C C   . LEU   A 1 43  ? -12.495 20.865 3.731   1.00 28.35  ? 54  LEU   A C   1 
ATOM   261  O O   . LEU   A 1 43  ? -12.444 20.875 4.959   1.00 30.26  ? 54  LEU   A O   1 
ATOM   262  C CB  . LEU   A 1 43  ? -13.329 23.131 2.983   1.00 28.15  ? 54  LEU   A CB  1 
ATOM   263  C CG  . LEU   A 1 43  ? -13.052 24.470 2.287   1.00 27.61  ? 54  LEU   A CG  1 
ATOM   264  C CD1 . LEU   A 1 43  ? -14.253 25.373 2.397   1.00 26.47  ? 54  LEU   A CD1 1 
ATOM   265  C CD2 . LEU   A 1 43  ? -11.828 25.175 2.846   1.00 27.07  ? 54  LEU   A CD2 1 
ATOM   266  N N   . LEU   A 1 44  ? -12.809 19.775 3.028   1.00 26.86  ? 55  LEU   A N   1 
ATOM   267  C CA  . LEU   A 1 44  ? -13.013 18.512 3.707   1.00 26.15  ? 55  LEU   A CA  1 
ATOM   268  C C   . LEU   A 1 44  ? -11.647 17.960 4.094   1.00 26.01  ? 55  LEU   A C   1 
ATOM   269  O O   . LEU   A 1 44  ? -11.405 17.782 5.290   1.00 24.91  ? 55  LEU   A O   1 
ATOM   270  C CB  . LEU   A 1 44  ? -13.815 17.518 2.869   1.00 26.18  ? 55  LEU   A CB  1 
ATOM   271  C CG  . LEU   A 1 44  ? -13.980 16.111 3.464   1.00 26.58  ? 55  LEU   A CG  1 
ATOM   272  C CD1 . LEU   A 1 44  ? -14.627 16.134 4.851   1.00 28.51  ? 55  LEU   A CD1 1 
ATOM   273  C CD2 . LEU   A 1 44  ? -14.769 15.202 2.553   1.00 25.10  ? 55  LEU   A CD2 1 
ATOM   274  N N   . THR   A 1 45  ? -10.781 17.732 3.082   1.00 27.06  ? 56  THR   A N   1 
ATOM   275  C CA  . THR   A 1 45  ? -9.553  16.944 3.247   1.00 29.82  ? 56  THR   A CA  1 
ATOM   276  C C   . THR   A 1 45  ? -8.310  17.845 3.324   1.00 30.17  ? 56  THR   A C   1 
ATOM   277  O O   . THR   A 1 45  ? -7.224  17.347 3.624   1.00 32.25  ? 56  THR   A O   1 
ATOM   278  C CB  . THR   A 1 45  ? -9.374  15.857 2.168   1.00 28.63  ? 56  THR   A CB  1 
ATOM   279  O OG1 . THR   A 1 45  ? -8.614  16.319 1.051   1.00 28.90  ? 56  THR   A OG1 1 
ATOM   280  C CG2 . THR   A 1 45  ? -10.691 15.300 1.663   1.00 27.99  ? 56  THR   A CG2 1 
ATOM   281  N N   . ARG   A 1 46  ? -8.453  19.153 3.045   1.00 27.32  ? 57  ARG   A N   1 
ATOM   282  C CA  . ARG   A 1 46  ? -7.484  20.152 3.480   1.00 25.23  ? 57  ARG   A CA  1 
ATOM   283  C C   . ARG   A 1 46  ? -6.316  20.196 2.507   1.00 24.43  ? 57  ARG   A C   1 
ATOM   284  O O   . ARG   A 1 46  ? -5.427  21.030 2.651   1.00 24.29  ? 57  ARG   A O   1 
ATOM   285  C CB  . ARG   A 1 46  ? -6.953  19.950 4.910   1.00 23.76  ? 57  ARG   A CB  1 
ATOM   286  C CG  . ARG   A 1 46  ? -7.993  19.670 5.994   1.00 22.74  ? 57  ARG   A CG  1 
ATOM   287  C CD  . ARG   A 1 46  ? -9.159  20.671 6.042   1.00 21.68  ? 57  ARG   A CD  1 
ATOM   288  N NE  . ARG   A 1 46  ? -8.694  22.020 6.390   1.00 22.09  ? 57  ARG   A NE  1 
ATOM   289  C CZ  . ARG   A 1 46  ? -9.428  23.126 6.487   1.00 22.16  ? 57  ARG   A CZ  1 
ATOM   290  N NH1 . ARG   A 1 46  ? -10.719 23.098 6.190   1.00 22.80  ? 57  ARG   A NH1 1 
ATOM   291  N NH2 . ARG   A 1 46  ? -8.849  24.260 6.857   1.00 20.86  ? 57  ARG   A NH2 1 
ATOM   292  N N   . GLU   A 1 47  ? -6.326  19.299 1.518   1.00 25.00  ? 58  GLU   A N   1 
ATOM   293  C CA  . GLU   A 1 47  ? -5.334  19.371 0.463   1.00 25.75  ? 58  GLU   A CA  1 
ATOM   294  C C   . GLU   A 1 47  ? -5.836  20.384 -0.558  1.00 23.06  ? 58  GLU   A C   1 
ATOM   295  O O   . GLU   A 1 47  ? -7.000  20.732 -0.579  1.00 23.69  ? 58  GLU   A O   1 
ATOM   296  C CB  . GLU   A 1 47  ? -5.013  17.984 -0.106  1.00 27.55  ? 58  GLU   A CB  1 
ATOM   297  C CG  . GLU   A 1 47  ? -5.920  17.519 -1.246  1.00 29.90  ? 58  GLU   A CG  1 
ATOM   298  C CD  . GLU   A 1 47  ? -5.239  16.532 -2.185  1.00 30.52  ? 58  GLU   A CD  1 
ATOM   299  O OE1 . GLU   A 1 47  ? -4.543  15.640 -1.674  1.00 29.16  ? 58  GLU   A OE1 1 
ATOM   300  O OE2 . GLU   A 1 47  ? -5.395  16.644 -3.423  1.00 34.49  ? 58  GLU   A OE2 1 
ATOM   301  N N   . ASN   A 1 48  ? -4.945  20.878 -1.392  1.00 23.48  ? 59  ASN   A N   1 
ATOM   302  C CA  . ASN   A 1 48  ? -5.363  21.695 -2.511  1.00 25.56  ? 59  ASN   A CA  1 
ATOM   303  C C   . ASN   A 1 48  ? -5.592  20.814 -3.724  1.00 27.18  ? 59  ASN   A C   1 
ATOM   304  O O   . ASN   A 1 48  ? -5.273  19.624 -3.729  1.00 28.17  ? 59  ASN   A O   1 
ATOM   305  C CB  . ASN   A 1 48  ? -4.358  22.796 -2.812  1.00 26.32  ? 59  ASN   A CB  1 
ATOM   306  C CG  . ASN   A 1 48  ? -4.372  23.793 -1.687  1.00 26.51  ? 59  ASN   A CG  1 
ATOM   307  O OD1 . ASN   A 1 48  ? -4.866  23.459 -0.601  1.00 27.77  ? 59  ASN   A OD1 1 
ATOM   308  N ND2 . ASN   A 1 48  ? -3.857  24.993 -1.924  1.00 25.66  ? 59  ASN   A ND2 1 
ATOM   309  N N   . VAL   A 1 49  ? -6.140  21.445 -4.758  1.00 27.72  ? 60  VAL   A N   1 
ATOM   310  C CA  . VAL   A 1 49  ? -6.710  20.703 -5.852  1.00 28.07  ? 60  VAL   A CA  1 
ATOM   311  C C   . VAL   A 1 49  ? -6.928  21.633 -7.028  1.00 27.52  ? 60  VAL   A C   1 
ATOM   312  O O   . VAL   A 1 49  ? -7.191  22.833 -6.875  1.00 24.73  ? 60  VAL   A O   1 
ATOM   313  C CB  . VAL   A 1 49  ? -8.049  20.079 -5.437  1.00 30.23  ? 60  VAL   A CB  1 
ATOM   314  C CG1 . VAL   A 1 49  ? -7.968  19.399 -4.073  1.00 31.38  ? 60  VAL   A CG1 1 
ATOM   315  C CG2 . VAL   A 1 49  ? -9.169  21.116 -5.448  1.00 31.01  ? 60  VAL   A CG2 1 
ATOM   316  N N   . ALA   A 1 50  ? -6.898  20.981 -8.188  1.00 29.06  ? 61  ALA   A N   1 
ATOM   317  C CA  . ALA   A 1 50  ? -7.186  21.594 -9.465  1.00 29.93  ? 61  ALA   A CA  1 
ATOM   318  C C   . ALA   A 1 50  ? -8.687  21.535 -9.738  1.00 30.01  ? 61  ALA   A C   1 
ATOM   319  O O   . ALA   A 1 50  ? -9.245  20.453 -9.892  1.00 29.66  ? 61  ALA   A O   1 
ATOM   320  C CB  . ALA   A 1 50  ? -6.404  20.863 -10.509 1.00 30.60  ? 61  ALA   A CB  1 
ATOM   321  N N   . LEU   A 1 51  ? -9.325  22.710 -9.767  1.00 30.42  ? 62  LEU   A N   1 
ATOM   322  C CA  . LEU   A 1 51  ? -10.724 22.840 -10.134 1.00 31.97  ? 62  LEU   A CA  1 
ATOM   323  C C   . LEU   A 1 51  ? -10.827 23.458 -11.529 1.00 34.69  ? 62  LEU   A C   1 
ATOM   324  O O   . LEU   A 1 51  ? -10.498 24.628 -11.705 1.00 41.92  ? 62  LEU   A O   1 
ATOM   325  C CB  . LEU   A 1 51  ? -11.390 23.728 -9.086  1.00 31.84  ? 62  LEU   A CB  1 
ATOM   326  C CG  . LEU   A 1 51  ? -12.856 24.071 -9.358  1.00 32.70  ? 62  LEU   A CG  1 
ATOM   327  C CD1 . LEU   A 1 51  ? -13.685 22.822 -9.147  1.00 33.34  ? 62  LEU   A CD1 1 
ATOM   328  C CD2 . LEU   A 1 51  ? -13.356 25.198 -8.489  1.00 33.02  ? 62  LEU   A CD2 1 
ATOM   329  N N   . LYS   A 1 52  ? -11.265 22.683 -12.524 1.00 33.03  ? 63  LYS   A N   1 
ATOM   330  C CA  . LYS   A 1 52  ? -11.478 23.225 -13.855 1.00 34.06  ? 63  LYS   A CA  1 
ATOM   331  C C   . LYS   A 1 52  ? -12.968 23.494 -14.031 1.00 35.14  ? 63  LYS   A C   1 
ATOM   332  O O   . LYS   A 1 52  ? -13.790 22.822 -13.416 1.00 33.46  ? 63  LYS   A O   1 
ATOM   333  C CB  . LYS   A 1 52  ? -10.928 22.301 -14.944 1.00 36.77  ? 63  LYS   A CB  1 
ATOM   334  C CG  . LYS   A 1 52  ? -11.168 22.842 -16.341 1.00 42.96  ? 63  LYS   A CG  1 
ATOM   335  C CD  . LYS   A 1 52  ? -10.482 22.099 -17.484 1.00 50.63  ? 63  LYS   A CD  1 
ATOM   336  C CE  . LYS   A 1 52  ? -10.469 22.869 -18.797 1.00 53.20  ? 63  LYS   A CE  1 
ATOM   337  N NZ  . LYS   A 1 52  ? -11.778 23.403 -19.199 1.00 51.33  ? 63  LYS   A NZ  1 
ATOM   338  N N   . VAL   A 1 53  ? -13.305 24.504 -14.848 1.00 38.51  ? 64  VAL   A N   1 
ATOM   339  C CA  . VAL   A 1 53  ? -14.675 24.991 -14.953 1.00 39.19  ? 64  VAL   A CA  1 
ATOM   340  C C   . VAL   A 1 53  ? -14.985 25.450 -16.384 1.00 42.54  ? 64  VAL   A C   1 
ATOM   341  O O   . VAL   A 1 53  ? -14.139 25.978 -17.112 1.00 43.10  ? 64  VAL   A O   1 
ATOM   342  C CB  . VAL   A 1 53  ? -14.981 26.104 -13.928 1.00 37.67  ? 64  VAL   A CB  1 
ATOM   343  C CG1 . VAL   A 1 53  ? -14.562 25.725 -12.509 1.00 38.17  ? 64  VAL   A CG1 1 
ATOM   344  C CG2 . VAL   A 1 53  ? -14.350 27.436 -14.310 1.00 38.40  ? 64  VAL   A CG2 1 
ATOM   345  N N   . GLU   A 1 54  ? -16.256 25.252 -16.747 1.00 47.11  ? 65  GLU   A N   1 
ATOM   346  C CA  . GLU   A 1 54  ? -16.797 25.524 -18.069 1.00 47.77  ? 65  GLU   A CA  1 
ATOM   347  C C   . GLU   A 1 54  ? -18.112 26.269 -17.870 1.00 50.19  ? 65  GLU   A C   1 
ATOM   348  O O   . GLU   A 1 54  ? -18.922 25.906 -17.015 1.00 49.55  ? 65  GLU   A O   1 
ATOM   349  C CB  . GLU   A 1 54  ? -16.960 24.157 -18.733 1.00 46.83  ? 65  GLU   A CB  1 
ATOM   350  C CG  . GLU   A 1 54  ? -17.686 24.144 -20.073 1.00 47.83  ? 65  GLU   A CG  1 
ATOM   351  C CD  . GLU   A 1 54  ? -17.994 22.722 -20.530 1.00 49.01  ? 65  GLU   A CD  1 
ATOM   352  O OE1 . GLU   A 1 54  ? -19.022 22.103 -20.139 1.00 43.94  ? 65  GLU   A OE1 1 
ATOM   353  O OE2 . GLU   A 1 54  ? -17.123 22.208 -21.263 1.00 47.12  ? 65  GLU   A OE2 1 
ATOM   354  N N   . SER   A 1 55  ? -18.311 27.345 -18.626 1.00 51.41  ? 66  SER   A N   1 
ATOM   355  C CA  . SER   A 1 55  ? -19.545 28.089 -18.476 1.00 49.09  ? 66  SER   A CA  1 
ATOM   356  C C   . SER   A 1 55  ? -20.717 27.187 -18.854 1.00 49.64  ? 66  SER   A C   1 
ATOM   357  O O   . SER   A 1 55  ? -20.608 26.355 -19.756 1.00 48.31  ? 66  SER   A O   1 
ATOM   358  C CB  . SER   A 1 55  ? -19.521 29.339 -19.282 1.00 46.01  ? 66  SER   A CB  1 
ATOM   359  O OG  . SER   A 1 55  ? -20.674 30.098 -18.974 1.00 44.88  ? 66  SER   A OG  1 
ATOM   360  N N   . ALA   A 1 56  ? -21.832 27.342 -18.137 1.00 50.63  ? 67  ALA   A N   1 
ATOM   361  C CA  . ALA   A 1 56  ? -23.031 26.572 -18.427 1.00 52.78  ? 67  ALA   A CA  1 
ATOM   362  C C   . ALA   A 1 56  ? -23.553 26.911 -19.821 1.00 54.30  ? 67  ALA   A C   1 
ATOM   363  O O   . ALA   A 1 56  ? -23.997 26.030 -20.546 1.00 51.69  ? 67  ALA   A O   1 
ATOM   364  C CB  . ALA   A 1 56  ? -24.082 26.832 -17.377 1.00 52.89  ? 67  ALA   A CB  1 
ATOM   365  N N   . GLN   A 1 57  ? -23.440 28.173 -20.221 1.00 58.19  ? 68  GLN   A N   1 
ATOM   366  C CA  . GLN   A 1 57  ? -24.012 28.611 -21.483 1.00 60.24  ? 68  GLN   A CA  1 
ATOM   367  C C   . GLN   A 1 57  ? -23.027 28.363 -22.629 1.00 60.63  ? 68  GLN   A C   1 
ATOM   368  O O   . GLN   A 1 57  ? -23.441 28.169 -23.770 1.00 67.00  ? 68  GLN   A O   1 
ATOM   369  C CB  . GLN   A 1 57  ? -24.397 30.086 -21.379 1.00 62.72  ? 68  GLN   A CB  1 
ATOM   370  C CG  . GLN   A 1 57  ? -24.475 30.633 -19.956 1.00 67.82  ? 68  GLN   A CG  1 
ATOM   371  C CD  . GLN   A 1 57  ? -25.833 30.522 -19.297 1.00 74.12  ? 68  GLN   A CD  1 
ATOM   372  O OE1 . GLN   A 1 57  ? -26.886 30.554 -19.952 1.00 69.40  ? 68  GLN   A OE1 1 
ATOM   373  N NE2 . GLN   A 1 57  ? -25.811 30.441 -17.970 1.00 75.17  ? 68  GLN   A NE2 1 
ATOM   374  N N   . GLN   A 1 58  ? -21.721 28.385 -22.333 1.00 58.77  ? 69  GLN   A N   1 
ATOM   375  C CA  . GLN   A 1 58  ? -20.693 28.210 -23.346 1.00 59.32  ? 69  GLN   A CA  1 
ATOM   376  C C   . GLN   A 1 58  ? -21.157 27.202 -24.394 1.00 57.57  ? 69  GLN   A C   1 
ATOM   377  O O   . GLN   A 1 58  ? -21.570 26.096 -24.042 1.00 56.87  ? 69  GLN   A O   1 
ATOM   378  C CB  . GLN   A 1 58  ? -19.393 27.756 -22.687 1.00 64.61  ? 69  GLN   A CB  1 
ATOM   379  C CG  . GLN   A 1 58  ? -18.426 27.032 -23.618 1.00 70.21  ? 69  GLN   A CG  1 
ATOM   380  C CD  . GLN   A 1 58  ? -17.245 26.447 -22.878 1.00 76.00  ? 69  GLN   A CD  1 
ATOM   381  O OE1 . GLN   A 1 58  ? -16.784 26.995 -21.869 1.00 87.89  ? 69  GLN   A OE1 1 
ATOM   382  N NE2 . GLN   A 1 58  ? -16.758 25.309 -23.350 1.00 75.78  ? 69  GLN   A NE2 1 
ATOM   383  N N   . PRO   A 1 59  ? -21.078 27.559 -25.696 1.00 54.12  ? 70  PRO   A N   1 
ATOM   384  C CA  . PRO   A 1 59  ? -21.491 26.676 -26.789 1.00 54.39  ? 70  PRO   A CA  1 
ATOM   385  C C   . PRO   A 1 59  ? -20.830 25.303 -26.848 1.00 59.35  ? 70  PRO   A C   1 
ATOM   386  O O   . PRO   A 1 59  ? -21.521 24.296 -26.989 1.00 59.70  ? 70  PRO   A O   1 
ATOM   387  C CB  . PRO   A 1 59  ? -21.108 27.523 -27.989 1.00 50.25  ? 70  PRO   A CB  1 
ATOM   388  C CG  . PRO   A 1 59  ? -21.347 28.919 -27.498 1.00 50.49  ? 70  PRO   A CG  1 
ATOM   389  C CD  . PRO   A 1 59  ? -20.642 28.877 -26.172 1.00 51.77  ? 70  PRO   A CD  1 
ATOM   390  N N   . LYS   A 1 60  ? -19.495 25.283 -26.738 1.00 62.03  ? 71  LYS   A N   1 
ATOM   391  C CA  . LYS   A 1 60  ? -18.705 24.075 -26.925 1.00 64.15  ? 71  LYS   A CA  1 
ATOM   392  C C   . LYS   A 1 60  ? -18.562 23.324 -25.601 1.00 60.18  ? 71  LYS   A C   1 
ATOM   393  O O   . LYS   A 1 60  ? -17.574 23.492 -24.895 1.00 60.37  ? 71  LYS   A O   1 
ATOM   394  C CB  . LYS   A 1 60  ? -17.360 24.526 -27.500 1.00 72.08  ? 71  LYS   A CB  1 
ATOM   395  C CG  . LYS   A 1 60  ? -17.465 25.466 -28.700 1.00 79.83  ? 71  LYS   A CG  1 
ATOM   396  C CD  . LYS   A 1 60  ? -18.052 24.824 -29.951 1.00 83.88  ? 71  LYS   A CD  1 
ATOM   397  C CE  . LYS   A 1 60  ? -18.034 25.754 -31.118 1.00 83.49  ? 71  LYS   A CE  1 
ATOM   398  N NZ  . LYS   A 1 60  ? -18.000 25.004 -32.376 1.00 84.05  ? 71  LYS   A NZ  1 
ATOM   399  N N   . GLN   A 1 61  ? -19.568 22.509 -25.259 1.00 58.36  ? 72  GLN   A N   1 
ATOM   400  C CA  . GLN   A 1 61  ? -19.625 21.832 -23.970 1.00 53.09  ? 72  GLN   A CA  1 
ATOM   401  C C   . GLN   A 1 61  ? -18.548 20.751 -23.948 1.00 50.80  ? 72  GLN   A C   1 
ATOM   402  O O   . GLN   A 1 61  ? -18.821 19.588 -24.230 1.00 56.84  ? 72  GLN   A O   1 
ATOM   403  C CB  . GLN   A 1 61  ? -21.014 21.236 -23.698 1.00 52.78  ? 72  GLN   A CB  1 
ATOM   404  C CG  . GLN   A 1 61  ? -22.065 22.238 -23.232 1.00 50.79  ? 72  GLN   A CG  1 
ATOM   405  C CD  . GLN   A 1 61  ? -21.647 22.976 -21.978 1.00 56.56  ? 72  GLN   A CD  1 
ATOM   406  O OE1 . GLN   A 1 61  ? -21.619 22.418 -20.873 1.00 51.34  ? 72  GLN   A OE1 1 
ATOM   407  N NE2 . GLN   A 1 61  ? -21.297 24.247 -22.140 1.00 63.26  ? 72  GLN   A NE2 1 
ATOM   408  N N   . VAL   A 1 62  ? -17.322 21.145 -23.596 1.00 48.12  ? 73  VAL   A N   1 
ATOM   409  C CA  . VAL   A 1 62  ? -16.162 20.276 -23.733 1.00 47.20  ? 73  VAL   A CA  1 
ATOM   410  C C   . VAL   A 1 62  ? -15.854 19.535 -22.431 1.00 47.96  ? 73  VAL   A C   1 
ATOM   411  O O   . VAL   A 1 62  ? -15.604 18.330 -22.454 1.00 51.93  ? 73  VAL   A O   1 
ATOM   412  C CB  . VAL   A 1 62  ? -14.976 21.128 -24.211 1.00 47.85  ? 73  VAL   A CB  1 
ATOM   413  C CG1 . VAL   A 1 62  ? -13.631 20.526 -23.833 1.00 45.48  ? 73  VAL   A CG1 1 
ATOM   414  C CG2 . VAL   A 1 62  ? -15.075 21.378 -25.711 1.00 53.11  ? 73  VAL   A CG2 1 
ATOM   415  N N   . LEU   A 1 63  ? -15.855 20.260 -21.307 1.00 43.03  ? 74  LEU   A N   1 
ATOM   416  C CA  . LEU   A 1 63  ? -15.557 19.692 -20.004 1.00 40.55  ? 74  LEU   A CA  1 
ATOM   417  C C   . LEU   A 1 63  ? -16.153 18.292 -19.833 1.00 44.55  ? 74  LEU   A C   1 
ATOM   418  O O   . LEU   A 1 63  ? -15.450 17.378 -19.414 1.00 44.48  ? 74  LEU   A O   1 
ATOM   419  C CB  . LEU   A 1 63  ? -16.051 20.652 -18.926 1.00 37.05  ? 74  LEU   A CB  1 
ATOM   420  C CG  . LEU   A 1 63  ? -15.829 20.221 -17.473 1.00 34.88  ? 74  LEU   A CG  1 
ATOM   421  C CD1 . LEU   A 1 63  ? -14.382 19.937 -17.172 1.00 35.74  ? 74  LEU   A CD1 1 
ATOM   422  C CD2 . LEU   A 1 63  ? -16.328 21.277 -16.534 1.00 34.38  ? 74  LEU   A CD2 1 
ATOM   423  N N   . LYS   A 1 64  ? -17.443 18.098 -20.130 1.00 52.26  ? 75  LYS   A N   1 
ATOM   424  C CA  . LYS   A 1 64  ? -18.065 16.815 -19.819 1.00 60.86  ? 75  LYS   A CA  1 
ATOM   425  C C   . LYS   A 1 64  ? -17.220 15.702 -20.434 1.00 54.66  ? 75  LYS   A C   1 
ATOM   426  O O   . LYS   A 1 64  ? -16.835 14.756 -19.752 1.00 51.91  ? 75  LYS   A O   1 
ATOM   427  C CB  . LYS   A 1 64  ? -19.544 16.689 -20.213 1.00 68.81  ? 75  LYS   A CB  1 
ATOM   428  C CG  . LYS   A 1 64  ? -19.891 16.835 -21.687 1.00 76.52  ? 75  LYS   A CG  1 
ATOM   429  C CD  . LYS   A 1 64  ? -21.364 17.169 -21.913 1.00 83.38  ? 75  LYS   A CD  1 
ATOM   430  C CE  . LYS   A 1 64  ? -21.676 17.538 -23.335 1.00 84.23  ? 75  LYS   A CE  1 
ATOM   431  N NZ  . LYS   A 1 64  ? -22.975 18.198 -23.487 1.00 82.63  ? 75  LYS   A NZ  1 
ATOM   432  N N   . MET   A 1 65  ? -16.872 15.866 -21.710 1.00 52.76  ? 76  MET   A N   1 
ATOM   433  C CA  . MET   A 1 65  ? -16.094 14.865 -22.417 1.00 50.45  ? 76  MET   A CA  1 
ATOM   434  C C   . MET   A 1 65  ? -14.720 14.697 -21.756 1.00 45.68  ? 76  MET   A C   1 
ATOM   435  O O   . MET   A 1 65  ? -14.245 13.569 -21.641 1.00 42.28  ? 76  MET   A O   1 
ATOM   436  C CB  . MET   A 1 65  ? -16.041 15.217 -23.908 1.00 49.46  ? 76  MET   A CB  1 
ATOM   437  C CG  . MET   A 1 65  ? -15.224 14.267 -24.751 1.00 46.63  ? 76  MET   A CG  1 
ATOM   438  S SD  . MET   A 1 65  ? -13.495 14.756 -24.687 1.00 45.94  ? 76  MET   A SD  1 
ATOM   439  C CE  . MET   A 1 65  ? -13.638 16.380 -25.442 1.00 46.99  ? 76  MET   A CE  1 
ATOM   440  N N   . GLU   A 1 66  ? -14.114 15.798 -21.278 1.00 41.88  ? 77  GLU   A N   1 
ATOM   441  C CA  . GLU   A 1 66  ? -12.935 15.734 -20.420 1.00 39.80  ? 77  GLU   A CA  1 
ATOM   442  C C   . GLU   A 1 66  ? -13.153 14.799 -19.223 1.00 36.26  ? 77  GLU   A C   1 
ATOM   443  O O   . GLU   A 1 66  ? -12.231 14.101 -18.807 1.00 34.15  ? 77  GLU   A O   1 
ATOM   444  C CB  . GLU   A 1 66  ? -12.470 17.076 -19.834 1.00 41.21  ? 77  GLU   A CB  1 
ATOM   445  C CG  . GLU   A 1 66  ? -11.209 17.654 -20.478 1.00 44.14  ? 77  GLU   A CG  1 
ATOM   446  C CD  . GLU   A 1 66  ? -10.048 18.122 -19.580 1.00 48.38  ? 77  GLU   A CD  1 
ATOM   447  O OE1 . GLU   A 1 66  ? -9.293  17.346 -18.919 1.00 38.99  ? 77  GLU   A OE1 1 
ATOM   448  O OE2 . GLU   A 1 66  ? -9.854  19.361 -19.589 1.00 59.39  ? 77  GLU   A OE2 1 
ATOM   449  N N   . VAL   A 1 67  ? -14.345 14.798 -18.627 1.00 33.54  ? 78  VAL   A N   1 
ATOM   450  C CA  . VAL   A 1 67  ? -14.521 14.075 -17.381 1.00 33.40  ? 78  VAL   A CA  1 
ATOM   451  C C   . VAL   A 1 67  ? -14.761 12.588 -17.652 1.00 34.95  ? 78  VAL   A C   1 
ATOM   452  O O   . VAL   A 1 67  ? -14.659 11.775 -16.732 1.00 37.11  ? 78  VAL   A O   1 
ATOM   453  C CB  . VAL   A 1 67  ? -15.639 14.662 -16.504 1.00 33.74  ? 78  VAL   A CB  1 
ATOM   454  C CG1 . VAL   A 1 67  ? -15.556 14.117 -15.079 1.00 34.61  ? 78  VAL   A CG1 1 
ATOM   455  C CG2 . VAL   A 1 67  ? -15.601 16.182 -16.476 1.00 34.13  ? 78  VAL   A CG2 1 
ATOM   456  N N   . ALA   A 1 68  ? -15.078 12.232 -18.906 1.00 34.86  ? 79  ALA   A N   1 
ATOM   457  C CA  . ALA   A 1 68  ? -15.302 10.844 -19.308 1.00 33.10  ? 79  ALA   A CA  1 
ATOM   458  C C   . ALA   A 1 68  ? -13.973 10.105 -19.529 1.00 32.04  ? 79  ALA   A C   1 
ATOM   459  O O   . ALA   A 1 68  ? -13.771 8.967  -19.085 1.00 28.45  ? 79  ALA   A O   1 
ATOM   460  C CB  . ALA   A 1 68  ? -16.146 10.846 -20.562 1.00 31.45  ? 79  ALA   A CB  1 
ATOM   461  N N   . VAL   A 1 69  ? -13.074 10.786 -20.246 1.00 30.94  ? 80  VAL   A N   1 
ATOM   462  C CA  . VAL   A 1 69  ? -11.706 10.340 -20.440 1.00 28.19  ? 80  VAL   A CA  1 
ATOM   463  C C   . VAL   A 1 69  ? -11.031 10.201 -19.079 1.00 27.31  ? 80  VAL   A C   1 
ATOM   464  O O   . VAL   A 1 69  ? -10.374 9.200  -18.818 1.00 25.99  ? 80  VAL   A O   1 
ATOM   465  C CB  . VAL   A 1 69  ? -10.927 11.315 -21.341 1.00 25.54  ? 80  VAL   A CB  1 
ATOM   466  C CG1 . VAL   A 1 69  ? -9.530  10.806 -21.620 1.00 25.11  ? 80  VAL   A CG1 1 
ATOM   467  C CG2 . VAL   A 1 69  ? -11.638 11.569 -22.657 1.00 25.46  ? 80  VAL   A CG2 1 
ATOM   468  N N   . LEU   A 1 70  ? -11.202 11.212 -18.221 1.00 27.61  ? 81  LEU   A N   1 
ATOM   469  C CA  . LEU   A 1 70  ? -10.559 11.214 -16.918 1.00 28.63  ? 81  LEU   A CA  1 
ATOM   470  C C   . LEU   A 1 70  ? -11.045 10.022 -16.099 1.00 29.62  ? 81  LEU   A C   1 
ATOM   471  O O   . LEU   A 1 70  ? -10.232 9.394  -15.427 1.00 27.71  ? 81  LEU   A O   1 
ATOM   472  C CB  . LEU   A 1 70  ? -10.785 12.533 -16.179 1.00 28.46  ? 81  LEU   A CB  1 
ATOM   473  C CG  . LEU   A 1 70  ? -9.926  12.767 -14.933 1.00 27.57  ? 81  LEU   A CG  1 
ATOM   474  C CD1 . LEU   A 1 70  ? -8.449  12.675 -15.248 1.00 27.30  ? 81  LEU   A CD1 1 
ATOM   475  C CD2 . LEU   A 1 70  ? -10.223 14.119 -14.302 1.00 27.80  ? 81  LEU   A CD2 1 
ATOM   476  N N   . LYS   A 1 71  ? -12.344 9.691  -16.216 1.00 33.54  ? 82  LYS   A N   1 
ATOM   477  C CA  . LYS   A 1 71  ? -12.961 8.595  -15.474 1.00 37.79  ? 82  LYS   A CA  1 
ATOM   478  C C   . LYS   A 1 71  ? -12.551 7.211  -15.993 1.00 38.89  ? 82  LYS   A C   1 
ATOM   479  O O   . LYS   A 1 71  ? -12.355 6.293  -15.199 1.00 40.70  ? 82  LYS   A O   1 
ATOM   480  C CB  . LYS   A 1 71  ? -14.489 8.689  -15.504 1.00 41.41  ? 82  LYS   A CB  1 
ATOM   481  C CG  . LYS   A 1 71  ? -15.125 9.583  -14.441 1.00 45.15  ? 82  LYS   A CG  1 
ATOM   482  C CD  . LYS   A 1 71  ? -16.645 9.441  -14.416 1.00 48.11  ? 82  LYS   A CD  1 
ATOM   483  C CE  . LYS   A 1 71  ? -17.288 10.173 -13.286 1.00 50.54  ? 82  LYS   A CE  1 
ATOM   484  N NZ  . LYS   A 1 71  ? -18.724 10.353 -13.521 1.00 51.94  ? 82  LYS   A NZ  1 
ATOM   485  N N   . LYS   A 1 72  ? -12.448 7.044  -17.318 1.00 38.04  ? 83  LYS   A N   1 
ATOM   486  C CA  . LYS   A 1 72  ? -11.980 5.797  -17.907 1.00 37.19  ? 83  LYS   A CA  1 
ATOM   487  C C   . LYS   A 1 72  ? -10.507 5.527  -17.583 1.00 37.62  ? 83  LYS   A C   1 
ATOM   488  O O   . LYS   A 1 72  ? -9.992  4.442  -17.850 1.00 36.34  ? 83  LYS   A O   1 
ATOM   489  C CB  . LYS   A 1 72  ? -12.062 5.891  -19.432 1.00 37.95  ? 83  LYS   A CB  1 
ATOM   490  C CG  . LYS   A 1 72  ? -13.431 6.077  -20.030 1.00 40.00  ? 83  LYS   A CG  1 
ATOM   491  C CD  . LYS   A 1 72  ? -13.348 6.400  -21.516 1.00 41.97  ? 83  LYS   A CD  1 
ATOM   492  C CE  . LYS   A 1 72  ? -14.693 6.599  -22.133 1.00 45.28  ? 83  LYS   A CE  1 
ATOM   493  N NZ  . LYS   A 1 72  ? -15.614 5.494  -21.855 1.00 46.84  ? 83  LYS   A NZ  1 
ATOM   494  N N   . LEU   A 1 73  ? -9.803  6.544  -17.082 1.00 37.14  ? 84  LEU   A N   1 
ATOM   495  C CA  . LEU   A 1 73  ? -8.359  6.472  -16.958 1.00 37.37  ? 84  LEU   A CA  1 
ATOM   496  C C   . LEU   A 1 73  ? -7.973  6.360  -15.488 1.00 40.30  ? 84  LEU   A C   1 
ATOM   497  O O   . LEU   A 1 73  ? -6.805  6.131  -15.181 1.00 38.92  ? 84  LEU   A O   1 
ATOM   498  C CB  . LEU   A 1 73  ? -7.729  7.700  -17.617 1.00 36.30  ? 84  LEU   A CB  1 
ATOM   499  C CG  . LEU   A 1 73  ? -7.655  7.715  -19.151 1.00 34.03  ? 84  LEU   A CG  1 
ATOM   500  C CD1 . LEU   A 1 73  ? -7.011  9.006  -19.647 1.00 31.14  ? 84  LEU   A CD1 1 
ATOM   501  C CD2 . LEU   A 1 73  ? -6.897  6.510  -19.700 1.00 35.63  ? 84  LEU   A CD2 1 
ATOM   502  N N   . GLN   A 1 74  ? -8.950  6.542  -14.588 1.00 43.51  ? 85  GLN   A N   1 
ATOM   503  C CA  . GLN   A 1 74  ? -8.766  6.172  -13.194 1.00 44.87  ? 85  GLN   A CA  1 
ATOM   504  C C   . GLN   A 1 74  ? -8.286  4.726  -13.161 1.00 46.33  ? 85  GLN   A C   1 
ATOM   505  O O   . GLN   A 1 74  ? -8.850  3.870  -13.839 1.00 44.49  ? 85  GLN   A O   1 
ATOM   506  C CB  . GLN   A 1 74  ? -10.057 6.305  -12.387 1.00 45.63  ? 85  GLN   A CB  1 
ATOM   507  C CG  . GLN   A 1 74  ? -10.549 7.740  -12.252 1.00 49.75  ? 85  GLN   A CG  1 
ATOM   508  C CD  . GLN   A 1 74  ? -9.440  8.713  -11.901 1.00 51.39  ? 85  GLN   A CD  1 
ATOM   509  O OE1 . GLN   A 1 74  ? -8.683  8.506  -10.946 1.00 51.79  ? 85  GLN   A OE1 1 
ATOM   510  N NE2 . GLN   A 1 74  ? -9.313  9.777  -12.684 1.00 51.83  ? 85  GLN   A NE2 1 
ATOM   511  N N   . GLY   A 1 75  ? -7.219  4.477  -12.396 1.00 46.59  ? 86  GLY   A N   1 
ATOM   512  C CA  . GLY   A 1 75  ? -6.566  3.179  -12.384 1.00 44.90  ? 86  GLY   A CA  1 
ATOM   513  C C   . GLY   A 1 75  ? -5.162  3.307  -12.956 1.00 44.39  ? 86  GLY   A C   1 
ATOM   514  O O   . GLY   A 1 75  ? -4.217  2.780  -12.383 1.00 43.38  ? 86  GLY   A O   1 
ATOM   515  N N   . LYS   A 1 76  ? -5.042  4.059  -14.054 1.00 45.89  ? 87  LYS   A N   1 
ATOM   516  C CA  . LYS   A 1 76  ? -3.789  4.182  -14.779 1.00 44.98  ? 87  LYS   A CA  1 
ATOM   517  C C   . LYS   A 1 76  ? -2.860  5.124  -14.026 1.00 48.95  ? 87  LYS   A C   1 
ATOM   518  O O   . LYS   A 1 76  ? -3.320  5.889  -13.182 1.00 46.23  ? 87  LYS   A O   1 
ATOM   519  C CB  . LYS   A 1 76  ? -4.036  4.722  -16.189 1.00 42.81  ? 87  LYS   A CB  1 
ATOM   520  C CG  . LYS   A 1 76  ? -5.106  3.956  -16.938 1.00 44.51  ? 87  LYS   A CG  1 
ATOM   521  C CD  . LYS   A 1 76  ? -4.699  3.460  -18.319 1.00 42.70  ? 87  LYS   A CD  1 
ATOM   522  C CE  . LYS   A 1 76  ? -5.841  2.761  -18.984 1.00 41.35  ? 87  LYS   A CE  1 
ATOM   523  N NZ  . LYS   A 1 76  ? -5.466  1.405  -19.365 1.00 41.97  ? 87  LYS   A NZ  1 
ATOM   524  N N   . ASP   A 1 77  ? -1.554  5.030  -14.326 1.00 54.60  ? 88  ASP   A N   1 
ATOM   525  C CA  . ASP   A 1 77  ? -0.573  5.979  -13.824 1.00 56.84  ? 88  ASP   A CA  1 
ATOM   526  C C   . ASP   A 1 77  ? -0.467  7.111  -14.842 1.00 54.62  ? 88  ASP   A C   1 
ATOM   527  O O   . ASP   A 1 77  ? -0.865  6.919  -15.986 1.00 55.95  ? 88  ASP   A O   1 
ATOM   528  C CB  . ASP   A 1 77  ? 0.755   5.294  -13.545 1.00 60.03  ? 88  ASP   A CB  1 
ATOM   529  C CG  . ASP   A 1 77  ? 1.752   6.117  -12.741 1.00 68.07  ? 88  ASP   A CG  1 
ATOM   530  O OD1 . ASP   A 1 77  ? 1.306   7.020  -11.996 1.00 69.66  ? 88  ASP   A OD1 1 
ATOM   531  O OD2 . ASP   A 1 77  ? 2.967   5.870  -12.891 1.00 72.80  ? 88  ASP   A OD2 1 
ATOM   532  N N   . HIS   A 1 78  ? 0.034   8.280  -14.411 1.00 51.88  ? 89  HIS   A N   1 
ATOM   533  C CA  . HIS   A 1 78  ? 0.211   9.447  -15.270 1.00 55.34  ? 89  HIS   A CA  1 
ATOM   534  C C   . HIS   A 1 78  ? -1.115  10.204 -15.460 1.00 54.85  ? 89  HIS   A C   1 
ATOM   535  O O   . HIS   A 1 78  ? -1.213  11.070 -16.331 1.00 53.54  ? 89  HIS   A O   1 
ATOM   536  C CB  . HIS   A 1 78  ? 0.873   9.081  -16.611 1.00 59.25  ? 89  HIS   A CB  1 
ATOM   537  C CG  . HIS   A 1 78  ? 2.044   8.145  -16.527 1.00 64.46  ? 89  HIS   A CG  1 
ATOM   538  N ND1 . HIS   A 1 78  ? 3.209   8.432  -15.842 1.00 63.79  ? 89  HIS   A ND1 1 
ATOM   539  C CD2 . HIS   A 1 78  ? 2.201   6.905  -17.026 1.00 60.84  ? 89  HIS   A CD2 1 
ATOM   540  C CE1 . HIS   A 1 78  ? 4.037   7.399  -15.941 1.00 60.36  ? 89  HIS   A CE1 1 
ATOM   541  N NE2 . HIS   A 1 78  ? 3.446   6.463  -16.658 1.00 59.42  ? 89  HIS   A NE2 1 
ATOM   542  N N   . VAL   A 1 79  ? -2.122  9.909  -14.618 1.00 52.65  ? 90  VAL   A N   1 
ATOM   543  C CA  . VAL   A 1 79  ? -3.442  10.536 -14.669 1.00 45.24  ? 90  VAL   A CA  1 
ATOM   544  C C   . VAL   A 1 79  ? -3.801  11.107 -13.290 1.00 42.04  ? 90  VAL   A C   1 
ATOM   545  O O   . VAL   A 1 79  ? -3.668  10.415 -12.282 1.00 41.49  ? 90  VAL   A O   1 
ATOM   546  C CB  . VAL   A 1 79  ? -4.475  9.475  -15.102 1.00 43.55  ? 90  VAL   A CB  1 
ATOM   547  C CG1 . VAL   A 1 79  ? -5.809  10.093 -15.503 1.00 43.65  ? 90  VAL   A CG1 1 
ATOM   548  C CG2 . VAL   A 1 79  ? -3.952  8.592  -16.226 1.00 45.44  ? 90  VAL   A CG2 1 
ATOM   549  N N   . CYS   A 1 80  ? -4.261  12.365 -13.234 1.00 39.23  ? 91  CYS   A N   1 
ATOM   550  C CA  . CYS   A 1 80  ? -4.687  12.960 -11.975 1.00 38.05  ? 91  CYS   A CA  1 
ATOM   551  C C   . CYS   A 1 80  ? -5.847  12.152 -11.395 1.00 37.71  ? 91  CYS   A C   1 
ATOM   552  O O   . CYS   A 1 80  ? -6.733  11.716 -12.128 1.00 35.84  ? 91  CYS   A O   1 
ATOM   553  C CB  . CYS   A 1 80  ? -5.186  14.392 -12.111 1.00 38.66  ? 91  CYS   A CB  1 
ATOM   554  S SG  . CYS   A 1 80  ? -4.118  15.535 -13.041 1.00 40.98  ? 91  CYS   A SG  1 
ATOM   555  N N   . ARG   A 1 81  ? -5.840  11.984 -10.070 1.00 37.47  ? 92  ARG   A N   1 
ATOM   556  C CA  . ARG   A 1 81  ? -6.944  11.350 -9.379  1.00 37.76  ? 92  ARG   A CA  1 
ATOM   557  C C   . ARG   A 1 81  ? -8.188  12.218 -9.555  1.00 39.46  ? 92  ARG   A C   1 
ATOM   558  O O   . ARG   A 1 81  ? -8.137  13.427 -9.324  1.00 36.39  ? 92  ARG   A O   1 
ATOM   559  C CB  . ARG   A 1 81  ? -6.586  11.165 -7.900  1.00 38.72  ? 92  ARG   A CB  1 
ATOM   560  C CG  . ARG   A 1 81  ? -7.686  10.536 -7.054  1.00 39.76  ? 92  ARG   A CG  1 
ATOM   561  C CD  . ARG   A 1 81  ? -7.301  10.351 -5.596  1.00 40.04  ? 92  ARG   A CD  1 
ATOM   562  N NE  . ARG   A 1 81  ? -6.599  11.525 -5.061  1.00 42.03  ? 92  ARG   A NE  1 
ATOM   563  C CZ  . ARG   A 1 81  ? -7.126  12.484 -4.298  1.00 42.07  ? 92  ARG   A CZ  1 
ATOM   564  N NH1 . ARG   A 1 81  ? -8.425  12.478 -4.009  1.00 38.51  ? 92  ARG   A NH1 1 
ATOM   565  N NH2 . ARG   A 1 81  ? -6.338  13.459 -3.849  1.00 42.81  ? 92  ARG   A NH2 1 
ATOM   566  N N   . PHE   A 1 82  ? -9.295  11.573 -9.961  1.00 43.05  ? 93  PHE   A N   1 
ATOM   567  C CA  . PHE   A 1 82  ? -10.593 12.220 -10.109 1.00 43.29  ? 93  PHE   A CA  1 
ATOM   568  C C   . PHE   A 1 82  ? -11.251 12.378 -8.739  1.00 39.28  ? 93  PHE   A C   1 
ATOM   569  O O   . PHE   A 1 82  ? -11.495 11.386 -8.059  1.00 38.66  ? 93  PHE   A O   1 
ATOM   570  C CB  . PHE   A 1 82  ? -11.544 11.438 -11.025 1.00 43.84  ? 93  PHE   A CB  1 
ATOM   571  C CG  . PHE   A 1 82  ? -12.987 11.930 -10.963 1.00 47.70  ? 93  PHE   A CG  1 
ATOM   572  C CD1 . PHE   A 1 82  ? -13.348 13.162 -11.518 1.00 48.12  ? 93  PHE   A CD1 1 
ATOM   573  C CD2 . PHE   A 1 82  ? -13.985 11.160 -10.353 1.00 48.32  ? 93  PHE   A CD2 1 
ATOM   574  C CE1 . PHE   A 1 82  ? -14.663 13.607 -11.463 1.00 48.93  ? 93  PHE   A CE1 1 
ATOM   575  C CE2 . PHE   A 1 82  ? -15.299 11.615 -10.293 1.00 46.54  ? 93  PHE   A CE2 1 
ATOM   576  C CZ  . PHE   A 1 82  ? -15.635 12.835 -10.848 1.00 47.53  ? 93  PHE   A CZ  1 
ATOM   577  N N   . ILE   A 1 83  ? -11.564 13.630 -8.368  1.00 37.18  ? 94  ILE   A N   1 
ATOM   578  C CA  . ILE   A 1 83  ? -12.126 13.956 -7.066  1.00 34.67  ? 94  ILE   A CA  1 
ATOM   579  C C   . ILE   A 1 83  ? -13.645 14.065 -7.188  1.00 35.92  ? 94  ILE   A C   1 
ATOM   580  O O   . ILE   A 1 83  ? -14.385 13.346 -6.526  1.00 38.88  ? 94  ILE   A O   1 
ATOM   581  C CB  . ILE   A 1 83  ? -11.494 15.249 -6.516  1.00 32.25  ? 94  ILE   A CB  1 
ATOM   582  C CG1 . ILE   A 1 83  ? -10.004 15.048 -6.212  1.00 29.40  ? 94  ILE   A CG1 1 
ATOM   583  C CG2 . ILE   A 1 83  ? -12.268 15.762 -5.297  1.00 34.74  ? 94  ILE   A CG2 1 
ATOM   584  C CD1 . ILE   A 1 83  ? -9.212  16.328 -6.039  1.00 28.37  ? 94  ILE   A CD1 1 
ATOM   585  N N   . GLY   A 1 84  ? -14.112 14.979 -8.035  1.00 36.11  ? 95  GLY   A N   1 
ATOM   586  C CA  . GLY   A 1 84  ? -15.540 15.141 -8.224  1.00 36.69  ? 95  GLY   A CA  1 
ATOM   587  C C   . GLY   A 1 84  ? -15.833 15.937 -9.487  1.00 38.56  ? 95  GLY   A C   1 
ATOM   588  O O   . GLY   A 1 84  ? -14.912 16.476 -10.103 1.00 39.01  ? 95  GLY   A O   1 
ATOM   589  N N   . CYS   A 1 85  ? -17.116 15.951 -9.875  1.00 38.72  ? 96  CYS   A N   1 
ATOM   590  C CA  . CYS   A 1 85  ? -17.616 16.821 -10.928 1.00 38.22  ? 96  CYS   A CA  1 
ATOM   591  C C   . CYS   A 1 85  ? -19.030 17.246 -10.558 1.00 38.75  ? 96  CYS   A C   1 
ATOM   592  O O   . CYS   A 1 85  ? -19.701 16.590 -9.770  1.00 39.61  ? 96  CYS   A O   1 
ATOM   593  C CB  . CYS   A 1 85  ? -17.589 16.156 -12.304 1.00 36.24  ? 96  CYS   A CB  1 
ATOM   594  S SG  . CYS   A 1 85  ? -18.912 14.952 -12.586 1.00 33.83  ? 96  CYS   A SG  1 
ATOM   595  N N   . GLY   A 1 86  ? -19.477 18.344 -11.149 1.00 39.26  ? 97  GLY   A N   1 
ATOM   596  C CA  . GLY   A 1 86  ? -20.842 18.778 -10.948 1.00 43.00  ? 97  GLY   A CA  1 
ATOM   597  C C   . GLY   A 1 86  ? -21.171 19.964 -11.840 1.00 47.32  ? 97  GLY   A C   1 
ATOM   598  O O   . GLY   A 1 86  ? -20.277 20.633 -12.356 1.00 49.01  ? 97  GLY   A O   1 
ATOM   599  N N   . ARG   A 1 87  ? -22.472 20.205 -12.009 1.00 52.79  ? 98  ARG   A N   1 
ATOM   600  C CA  . ARG   A 1 87  ? -22.954 21.251 -12.891 1.00 55.12  ? 98  ARG   A CA  1 
ATOM   601  C C   . ARG   A 1 87  ? -23.970 22.072 -12.107 1.00 50.55  ? 98  ARG   A C   1 
ATOM   602  O O   . ARG   A 1 87  ? -24.649 21.534 -11.246 1.00 52.05  ? 98  ARG   A O   1 
ATOM   603  C CB  . ARG   A 1 87  ? -23.451 20.619 -14.203 1.00 58.45  ? 98  ARG   A CB  1 
ATOM   604  C CG  . ARG   A 1 87  ? -24.255 19.328 -14.100 1.00 62.72  ? 98  ARG   A CG  1 
ATOM   605  C CD  . ARG   A 1 87  ? -24.637 18.775 -15.473 1.00 66.76  ? 98  ARG   A CD  1 
ATOM   606  N NE  . ARG   A 1 87  ? -25.699 17.761 -15.412 1.00 74.23  ? 98  ARG   A NE  1 
ATOM   607  C CZ  . ARG   A 1 87  ? -26.984 17.940 -15.062 1.00 76.16  ? 98  ARG   A CZ  1 
ATOM   608  N NH1 . ARG   A 1 87  ? -27.449 19.140 -14.752 1.00 75.93  ? 98  ARG   A NH1 1 
ATOM   609  N NH2 . ARG   A 1 87  ? -27.815 16.906 -15.035 1.00 74.43  ? 98  ARG   A NH2 1 
ATOM   610  N N   . ASN   A 1 88  ? -23.997 23.384 -12.352 1.00 49.42  ? 99  ASN   A N   1 
ATOM   611  C CA  . ASN   A 1 88  ? -25.115 24.214 -11.940 1.00 52.54  ? 99  ASN   A CA  1 
ATOM   612  C C   . ASN   A 1 88  ? -25.230 25.385 -12.911 1.00 57.72  ? 99  ASN   A C   1 
ATOM   613  O O   . ASN   A 1 88  ? -24.384 25.555 -13.789 1.00 52.74  ? 99  ASN   A O   1 
ATOM   614  C CB  . ASN   A 1 88  ? -25.010 24.634 -10.479 1.00 51.42  ? 99  ASN   A CB  1 
ATOM   615  C CG  . ASN   A 1 88  ? -23.976 25.706 -10.269 1.00 50.68  ? 99  ASN   A CG  1 
ATOM   616  O OD1 . ASN   A 1 88  ? -24.255 26.898 -10.451 1.00 45.83  ? 99  ASN   A OD1 1 
ATOM   617  N ND2 . ASN   A 1 88  ? -22.787 25.291 -9.864  1.00 54.48  ? 99  ASN   A ND2 1 
ATOM   618  N N   . GLU   A 1 89  ? -26.268 26.209 -12.710 1.00 65.76  ? 100 GLU   A N   1 
ATOM   619  C CA  . GLU   A 1 89  ? -26.809 27.061 -13.761 1.00 71.51  ? 100 GLU   A CA  1 
ATOM   620  C C   . GLU   A 1 89  ? -25.913 28.274 -14.030 1.00 71.37  ? 100 GLU   A C   1 
ATOM   621  O O   . GLU   A 1 89  ? -26.393 29.302 -14.505 1.00 75.52  ? 100 GLU   A O   1 
ATOM   622  C CB  . GLU   A 1 89  ? -28.246 27.496 -13.449 1.00 73.40  ? 100 GLU   A CB  1 
ATOM   623  C CG  . GLU   A 1 89  ? -28.381 28.463 -12.273 1.00 74.34  ? 100 GLU   A CG  1 
ATOM   624  C CD  . GLU   A 1 89  ? -28.703 27.798 -10.947 1.00 76.81  ? 100 GLU   A CD  1 
ATOM   625  O OE1 . GLU   A 1 89  ? -27.979 26.856 -10.560 1.00 78.60  ? 100 GLU   A OE1 1 
ATOM   626  O OE2 . GLU   A 1 89  ? -29.680 28.226 -10.299 1.00 77.30  ? 100 GLU   A OE2 1 
ATOM   627  N N   . LYS   A 1 90  ? -24.610 28.158 -13.751 1.00 68.90  ? 101 LYS   A N   1 
ATOM   628  C CA  . LYS   A 1 90  ? -23.655 29.199 -14.111 1.00 67.06  ? 101 LYS   A CA  1 
ATOM   629  C C   . LYS   A 1 90  ? -22.404 28.597 -14.765 1.00 56.23  ? 101 LYS   A C   1 
ATOM   630  O O   . LYS   A 1 90  ? -21.732 29.268 -15.549 1.00 47.60  ? 101 LYS   A O   1 
ATOM   631  C CB  . LYS   A 1 90  ? -23.351 30.019 -12.849 1.00 71.28  ? 101 LYS   A CB  1 
ATOM   632  C CG  . LYS   A 1 90  ? -24.536 30.763 -12.244 1.00 73.39  ? 101 LYS   A CG  1 
ATOM   633  C CD  . LYS   A 1 90  ? -24.165 31.608 -11.032 1.00 80.28  ? 101 LYS   A CD  1 
ATOM   634  C CE  . LYS   A 1 90  ? -25.213 32.622 -10.678 1.00 82.95  ? 101 LYS   A CE  1 
ATOM   635  N NZ  . LYS   A 1 90  ? -24.697 33.657 -9.773  1.00 82.96  ? 101 LYS   A NZ  1 
ATOM   636  N N   . PHE   A 1 91  ? -22.108 27.328 -14.442 1.00 51.03  ? 102 PHE   A N   1 
ATOM   637  C CA  . PHE   A 1 91  ? -20.846 26.691 -14.786 1.00 45.02  ? 102 PHE   A CA  1 
ATOM   638  C C   . PHE   A 1 91  ? -20.909 25.210 -14.433 1.00 42.14  ? 102 PHE   A C   1 
ATOM   639  O O   . PHE   A 1 91  ? -21.480 24.849 -13.407 1.00 42.81  ? 102 PHE   A O   1 
ATOM   640  C CB  . PHE   A 1 91  ? -19.670 27.264 -13.993 1.00 41.45  ? 102 PHE   A CB  1 
ATOM   641  C CG  . PHE   A 1 91  ? -19.786 27.150 -12.475 1.00 38.56  ? 102 PHE   A CG  1 
ATOM   642  C CD1 . PHE   A 1 91  ? -20.449 28.123 -11.730 1.00 36.93  ? 102 PHE   A CD1 1 
ATOM   643  C CD2 . PHE   A 1 91  ? -19.206 26.088 -11.784 1.00 38.34  ? 102 PHE   A CD2 1 
ATOM   644  C CE1 . PHE   A 1 91  ? -20.534 28.032 -10.345 1.00 36.66  ? 102 PHE   A CE1 1 
ATOM   645  C CE2 . PHE   A 1 91  ? -19.296 26.001 -10.398 1.00 37.65  ? 102 PHE   A CE2 1 
ATOM   646  C CZ  . PHE   A 1 91  ? -19.954 26.976 -9.680  1.00 36.23  ? 102 PHE   A CZ  1 
ATOM   647  N N   . ASN   A 1 92  ? -20.300 24.373 -15.277 1.00 40.50  ? 103 ASN   A N   1 
ATOM   648  C CA  . ASN   A 1 92  ? -20.020 22.987 -14.928 1.00 38.82  ? 103 ASN   A CA  1 
ATOM   649  C C   . ASN   A 1 92  ? -18.598 22.914 -14.380 1.00 35.52  ? 103 ASN   A C   1 
ATOM   650  O O   . ASN   A 1 92  ? -17.735 23.697 -14.781 1.00 35.84  ? 103 ASN   A O   1 
ATOM   651  C CB  . ASN   A 1 92  ? -20.180 22.042 -16.113 1.00 38.16  ? 103 ASN   A CB  1 
ATOM   652  C CG  . ASN   A 1 92  ? -21.408 22.359 -16.925 1.00 36.97  ? 103 ASN   A CG  1 
ATOM   653  O OD1 . ASN   A 1 92  ? -22.525 22.252 -16.409 1.00 34.85  ? 103 ASN   A OD1 1 
ATOM   654  N ND2 . ASN   A 1 92  ? -21.218 22.756 -18.177 1.00 36.88  ? 103 ASN   A ND2 1 
ATOM   655  N N   . TYR   A 1 93  ? -18.355 21.978 -13.461 1.00 29.71  ? 104 TYR   A N   1 
ATOM   656  C CA  . TYR   A 1 93  ? -17.072 21.941 -12.790 1.00 27.92  ? 104 TYR   A CA  1 
ATOM   657  C C   . TYR   A 1 93  ? -16.602 20.496 -12.735 1.00 25.60  ? 104 TYR   A C   1 
ATOM   658  O O   . TYR   A 1 93  ? -17.399 19.562 -12.784 1.00 23.32  ? 104 TYR   A O   1 
ATOM   659  C CB  . TYR   A 1 93  ? -17.128 22.641 -11.420 1.00 30.08  ? 104 TYR   A CB  1 
ATOM   660  C CG  . TYR   A 1 93  ? -17.824 21.864 -10.313 1.00 31.92  ? 104 TYR   A CG  1 
ATOM   661  C CD1 . TYR   A 1 93  ? -17.199 20.784 -9.695  1.00 33.17  ? 104 TYR   A CD1 1 
ATOM   662  C CD2 . TYR   A 1 93  ? -19.106 22.201 -9.900  1.00 33.30  ? 104 TYR   A CD2 1 
ATOM   663  C CE1 . TYR   A 1 93  ? -17.841 20.044 -8.718  1.00 35.05  ? 104 TYR   A CE1 1 
ATOM   664  C CE2 . TYR   A 1 93  ? -19.756 21.472 -8.917  1.00 35.45  ? 104 TYR   A CE2 1 
ATOM   665  C CZ  . TYR   A 1 93  ? -19.122 20.392 -8.326  1.00 36.59  ? 104 TYR   A CZ  1 
ATOM   666  O OH  . TYR   A 1 93  ? -19.757 19.668 -7.361  1.00 37.54  ? 104 TYR   A OH  1 
ATOM   667  N N   . VAL   A 1 94  ? -15.275 20.358 -12.681 1.00 26.10  ? 105 VAL   A N   1 
ATOM   668  C CA  . VAL   A 1 94  ? -14.602 19.101 -12.395 1.00 25.24  ? 105 VAL   A CA  1 
ATOM   669  C C   . VAL   A 1 94  ? -13.548 19.373 -11.325 1.00 22.79  ? 105 VAL   A C   1 
ATOM   670  O O   . VAL   A 1 94  ? -12.971 20.454 -11.264 1.00 21.88  ? 105 VAL   A O   1 
ATOM   671  C CB  . VAL   A 1 94  ? -13.991 18.449 -13.653 1.00 24.13  ? 105 VAL   A CB  1 
ATOM   672  C CG1 . VAL   A 1 94  ? -12.915 19.328 -14.260 1.00 23.69  ? 105 VAL   A CG1 1 
ATOM   673  C CG2 . VAL   A 1 94  ? -13.459 17.045 -13.374 1.00 24.50  ? 105 VAL   A CG2 1 
ATOM   674  N N   . VAL   A 1 95  ? -13.353 18.401 -10.442 1.00 22.75  ? 106 VAL   A N   1 
ATOM   675  C CA  . VAL   A 1 95  ? -12.363 18.526 -9.389  1.00 24.68  ? 106 VAL   A CA  1 
ATOM   676  C C   . VAL   A 1 95  ? -11.380 17.376 -9.615  1.00 26.98  ? 106 VAL   A C   1 
ATOM   677  O O   . VAL   A 1 95  ? -11.787 16.246 -9.915  1.00 29.27  ? 106 VAL   A O   1 
ATOM   678  C CB  . VAL   A 1 95  ? -12.959 18.571 -7.954  1.00 23.37  ? 106 VAL   A CB  1 
ATOM   679  C CG1 . VAL   A 1 95  ? -11.898 18.743 -6.872  1.00 22.57  ? 106 VAL   A CG1 1 
ATOM   680  C CG2 . VAL   A 1 95  ? -13.993 19.681 -7.785  1.00 22.75  ? 106 VAL   A CG2 1 
ATOM   681  N N   . MET   A 1 96  ? -10.082 17.700 -9.548  1.00 26.66  ? 107 MET   A N   1 
ATOM   682  C CA  . MET   A 1 96  ? -9.044  16.695 -9.640  1.00 26.45  ? 107 MET   A CA  1 
ATOM   683  C C   . MET   A 1 96  ? -7.784  17.170 -8.919  1.00 26.93  ? 107 MET   A C   1 
ATOM   684  O O   . MET   A 1 96  ? -7.616  18.345 -8.585  1.00 26.61  ? 107 MET   A O   1 
ATOM   685  C CB  . MET   A 1 96  ? -8.733  16.393 -11.108 1.00 28.75  ? 107 MET   A CB  1 
ATOM   686  C CG  . MET   A 1 96  ? -8.237  17.591 -11.901 1.00 30.02  ? 107 MET   A CG  1 
ATOM   687  S SD  . MET   A 1 96  ? -8.533  17.340 -13.661 1.00 34.62  ? 107 MET   A SD  1 
ATOM   688  C CE  . MET   A 1 96  ? -8.717  19.068 -14.103 1.00 36.18  ? 107 MET   A CE  1 
ATOM   689  N N   . GLN   A 1 97  ? -6.906  16.194 -8.694  1.00 27.54  ? 108 GLN   A N   1 
ATOM   690  C CA  . GLN   A 1 97  ? -5.599  16.373 -8.088  1.00 26.67  ? 108 GLN   A CA  1 
ATOM   691  C C   . GLN   A 1 97  ? -4.773  17.453 -8.780  1.00 23.15  ? 108 GLN   A C   1 
ATOM   692  O O   . GLN   A 1 97  ? -4.760  17.553 -9.991  1.00 23.15  ? 108 GLN   A O   1 
ATOM   693  C CB  . GLN   A 1 97  ? -4.959  15.000 -8.244  1.00 27.80  ? 108 GLN   A CB  1 
ATOM   694  C CG  . GLN   A 1 97  ? -3.547  14.909 -7.695  1.00 28.36  ? 108 GLN   A CG  1 
ATOM   695  C CD  . GLN   A 1 97  ? -2.943  13.549 -7.930  1.00 27.95  ? 108 GLN   A CD  1 
ATOM   696  O OE1 . GLN   A 1 97  ? -3.484  12.727 -8.679  1.00 28.57  ? 108 GLN   A OE1 1 
ATOM   697  N NE2 . GLN   A 1 97  ? -1.804  13.316 -7.295  1.00 28.04  ? 108 GLN   A NE2 1 
ATOM   698  N N   . LEU   A 1 98  ? -4.044  18.231 -7.989  1.00 22.24  ? 109 LEU   A N   1 
ATOM   699  C CA  . LEU   A 1 98  ? -3.174  19.271 -8.502  1.00 23.68  ? 109 LEU   A CA  1 
ATOM   700  C C   . LEU   A 1 98  ? -1.752  18.747 -8.721  1.00 23.20  ? 109 LEU   A C   1 
ATOM   701  O O   . LEU   A 1 98  ? -1.251  17.926 -7.959  1.00 24.74  ? 109 LEU   A O   1 
ATOM   702  C CB  . LEU   A 1 98  ? -3.232  20.349 -7.427  1.00 26.30  ? 109 LEU   A CB  1 
ATOM   703  C CG  . LEU   A 1 98  ? -2.608  21.703 -7.777  1.00 28.81  ? 109 LEU   A CG  1 
ATOM   704  C CD1 . LEU   A 1 98  ? -3.290  22.388 -8.956  1.00 28.51  ? 109 LEU   A CD1 1 
ATOM   705  C CD2 . LEU   A 1 98  ? -2.692  22.570 -6.536  1.00 30.17  ? 109 LEU   A CD2 1 
ATOM   706  N N   . GLN   A 1 99  ? -1.068  19.239 -9.756  1.00 22.10  ? 110 GLN   A N   1 
ATOM   707  C CA  . GLN   A 1 99  ? 0.251   18.719 -10.094 1.00 20.49  ? 110 GLN   A CA  1 
ATOM   708  C C   . GLN   A 1 99  ? 1.257   19.864 -10.144 1.00 19.47  ? 110 GLN   A C   1 
ATOM   709  O O   . GLN   A 1 99  ? 0.884   21.022 -10.019 1.00 18.17  ? 110 GLN   A O   1 
ATOM   710  C CB  . GLN   A 1 99  ? 0.224   17.944 -11.412 1.00 20.12  ? 110 GLN   A CB  1 
ATOM   711  C CG  . GLN   A 1 99  ? -0.722  16.755 -11.420 1.00 19.69  ? 110 GLN   A CG  1 
ATOM   712  C CD  . GLN   A 1 99  ? -0.242  15.590 -10.584 1.00 19.38  ? 110 GLN   A CD  1 
ATOM   713  O OE1 . GLN   A 1 99  ? 0.767   15.661 -9.882  1.00 19.29  ? 110 GLN   A OE1 1 
ATOM   714  N NE2 . GLN   A 1 99  ? -0.965  14.485 -10.652 1.00 19.98  ? 110 GLN   A NE2 1 
ATOM   715  N N   . GLY   A 1 100 ? 2.536   19.515 -10.316 1.00 20.60  ? 111 GLY   A N   1 
ATOM   716  C CA  . GLY   A 1 100 ? 3.642   20.459 -10.205 1.00 22.95  ? 111 GLY   A CA  1 
ATOM   717  C C   . GLY   A 1 100 ? 4.084   21.044 -11.547 1.00 23.29  ? 111 GLY   A C   1 
ATOM   718  O O   . GLY   A 1 100 ? 3.331   21.044 -12.522 1.00 24.05  ? 111 GLY   A O   1 
ATOM   719  N N   . ARG   A 1 101 ? 5.317   21.552 -11.582 1.00 22.60  ? 112 ARG   A N   1 
ATOM   720  C CA  . ARG   A 1 101 ? 5.764   22.331 -12.722 1.00 23.98  ? 112 ARG   A CA  1 
ATOM   721  C C   . ARG   A 1 101 ? 5.516   21.522 -13.994 1.00 23.30  ? 112 ARG   A C   1 
ATOM   722  O O   . ARG   A 1 101 ? 5.654   20.302 -13.983 1.00 22.36  ? 112 ARG   A O   1 
ATOM   723  C CB  . ARG   A 1 101 ? 7.220   22.760 -12.491 1.00 25.72  ? 112 ARG   A CB  1 
ATOM   724  C CG  . ARG   A 1 101 ? 7.374   23.797 -11.385 1.00 26.97  ? 112 ARG   A CG  1 
ATOM   725  C CD  . ARG   A 1 101 ? 8.739   23.809 -10.702 1.00 27.13  ? 112 ARG   A CD  1 
ATOM   726  N NE  . ARG   A 1 101 ? 9.069   22.526 -10.068 1.00 27.18  ? 112 ARG   A NE  1 
ATOM   727  C CZ  . ARG   A 1 101 ? 10.288  22.141 -9.694  1.00 27.95  ? 112 ARG   A CZ  1 
ATOM   728  N NH1 . ARG   A 1 101 ? 11.312  22.979 -9.749  1.00 28.69  ? 112 ARG   A NH1 1 
ATOM   729  N NH2 . ARG   A 1 101 ? 10.491  20.906 -9.268  1.00 27.65  ? 112 ARG   A NH2 1 
ATOM   730  N N   . ASN   A 1 102 ? 5.109   22.214 -15.071 1.00 23.55  ? 113 ASN   A N   1 
ATOM   731  C CA  . ASN   A 1 102 ? 4.929   21.584 -16.371 1.00 24.90  ? 113 ASN   A CA  1 
ATOM   732  C C   . ASN   A 1 102 ? 6.263   21.565 -17.113 1.00 24.60  ? 113 ASN   A C   1 
ATOM   733  O O   . ASN   A 1 102 ? 7.212   22.243 -16.711 1.00 23.58  ? 113 ASN   A O   1 
ATOM   734  C CB  . ASN   A 1 102 ? 3.830   22.235 -17.209 1.00 26.51  ? 113 ASN   A CB  1 
ATOM   735  C CG  . ASN   A 1 102 ? 4.192   23.601 -17.756 1.00 27.65  ? 113 ASN   A CG  1 
ATOM   736  O OD1 . ASN   A 1 102 ? 5.317   23.841 -18.197 1.00 28.99  ? 113 ASN   A OD1 1 
ATOM   737  N ND2 . ASN   A 1 102 ? 3.253   24.525 -17.761 1.00 28.14  ? 113 ASN   A ND2 1 
ATOM   738  N N   . LEU   A 1 103 ? 6.297   20.824 -18.229 1.00 24.26  ? 114 LEU   A N   1 
ATOM   739  C CA  . LEU   A 1 103 ? 7.554   20.513 -18.886 1.00 25.86  ? 114 LEU   A CA  1 
ATOM   740  C C   . LEU   A 1 103 ? 8.051   21.728 -19.668 1.00 27.56  ? 114 LEU   A C   1 
ATOM   741  O O   . LEU   A 1 103 ? 9.236   22.042 -19.625 1.00 27.72  ? 114 LEU   A O   1 
ATOM   742  C CB  . LEU   A 1 103 ? 7.452   19.268 -19.768 1.00 27.23  ? 114 LEU   A CB  1 
ATOM   743  C CG  . LEU   A 1 103 ? 7.222   17.917 -19.063 1.00 27.31  ? 114 LEU   A CG  1 
ATOM   744  C CD1 . LEU   A 1 103 ? 7.274   16.809 -20.114 1.00 27.11  ? 114 LEU   A CD1 1 
ATOM   745  C CD2 . LEU   A 1 103 ? 8.176   17.575 -17.916 1.00 25.89  ? 114 LEU   A CD2 1 
ATOM   746  N N   . ALA   A 1 104 ? 7.156   22.429 -20.368 1.00 29.85  ? 115 ALA   A N   1 
ATOM   747  C CA  . ALA   A 1 104 ? 7.514   23.692 -21.010 1.00 31.51  ? 115 ALA   A CA  1 
ATOM   748  C C   . ALA   A 1 104 ? 8.297   24.605 -20.067 1.00 30.43  ? 115 ALA   A C   1 
ATOM   749  O O   . ALA   A 1 104 ? 9.337   25.133 -20.449 1.00 27.79  ? 115 ALA   A O   1 
ATOM   750  C CB  . ALA   A 1 104 ? 6.264   24.397 -21.494 1.00 33.49  ? 115 ALA   A CB  1 
ATOM   751  N N   . ASP   A 1 105 ? 7.766   24.798 -18.850 1.00 33.17  ? 116 ASP   A N   1 
ATOM   752  C CA  . ASP   A 1 105 ? 8.330   25.725 -17.883 1.00 34.96  ? 116 ASP   A CA  1 
ATOM   753  C C   . ASP   A 1 105 ? 9.656   25.208 -17.359 1.00 33.22  ? 116 ASP   A C   1 
ATOM   754  O O   . ASP   A 1 105 ? 10.567  26.001 -17.173 1.00 35.74  ? 116 ASP   A O   1 
ATOM   755  C CB  . ASP   A 1 105 ? 7.401   26.032 -16.719 1.00 40.01  ? 116 ASP   A CB  1 
ATOM   756  C CG  . ASP   A 1 105 ? 6.458   27.212 -16.925 1.00 46.38  ? 116 ASP   A CG  1 
ATOM   757  O OD1 . ASP   A 1 105 ? 6.360   27.710 -18.079 1.00 46.33  ? 116 ASP   A OD1 1 
ATOM   758  O OD2 . ASP   A 1 105 ? 5.838   27.640 -15.925 1.00 49.80  ? 116 ASP   A OD2 1 
ATOM   759  N N   . LEU   A 1 106 ? 9.768   23.897 -17.123 1.00 32.12  ? 117 LEU   A N   1 
ATOM   760  C CA  . LEU   A 1 106 ? 11.033  23.318 -16.689 1.00 31.34  ? 117 LEU   A CA  1 
ATOM   761  C C   . LEU   A 1 106 ? 12.085  23.395 -17.797 1.00 31.76  ? 117 LEU   A C   1 
ATOM   762  O O   . LEU   A 1 106 ? 13.240  23.693 -17.503 1.00 32.00  ? 117 LEU   A O   1 
ATOM   763  C CB  . LEU   A 1 106 ? 10.802  21.893 -16.202 1.00 30.57  ? 117 LEU   A CB  1 
ATOM   764  C CG  . LEU   A 1 106 ? 10.049  21.811 -14.872 1.00 33.13  ? 117 LEU   A CG  1 
ATOM   765  C CD1 . LEU   A 1 106 ? 9.280   20.513 -14.725 1.00 33.87  ? 117 LEU   A CD1 1 
ATOM   766  C CD2 . LEU   A 1 106 ? 11.003  22.009 -13.693 1.00 33.93  ? 117 LEU   A CD2 1 
ATOM   767  N N   . ARG   A 1 107 ? 11.674  23.157 -19.054 1.00 31.38  ? 118 ARG   A N   1 
ATOM   768  C CA  . ARG   A 1 107 ? 12.564  23.210 -20.200 1.00 31.28  ? 118 ARG   A CA  1 
ATOM   769  C C   . ARG   A 1 107 ? 13.167  24.596 -20.369 1.00 35.86  ? 118 ARG   A C   1 
ATOM   770  O O   . ARG   A 1 107 ? 14.348  24.697 -20.682 1.00 41.04  ? 118 ARG   A O   1 
ATOM   771  C CB  . ARG   A 1 107 ? 11.898  22.938 -21.548 1.00 31.73  ? 118 ARG   A CB  1 
ATOM   772  C CG  . ARG   A 1 107 ? 12.957  22.471 -22.534 1.00 33.73  ? 118 ARG   A CG  1 
ATOM   773  C CD  . ARG   A 1 107 ? 12.372  22.022 -23.852 1.00 36.77  ? 118 ARG   A CD  1 
ATOM   774  N NE  . ARG   A 1 107 ? 11.668  23.124 -24.507 1.00 40.22  ? 118 ARG   A NE  1 
ATOM   775  C CZ  . ARG   A 1 107 ? 12.229  24.283 -24.822 1.00 43.74  ? 118 ARG   A CZ  1 
ATOM   776  N NH1 . ARG   A 1 107 ? 13.530  24.463 -24.688 1.00 43.57  ? 118 ARG   A NH1 1 
ATOM   777  N NH2 . ARG   A 1 107 ? 11.490  25.271 -25.283 1.00 47.65  ? 118 ARG   A NH2 1 
ATOM   778  N N   . ARG   A 1 108 ? 12.356  25.650 -20.201 1.00 41.21  ? 119 ARG   A N   1 
ATOM   779  C CA  . ARG   A 1 108 ? 12.840  27.025 -20.289 1.00 43.10  ? 119 ARG   A CA  1 
ATOM   780  C C   . ARG   A 1 108 ? 13.810  27.326 -19.147 1.00 38.90  ? 119 ARG   A C   1 
ATOM   781  O O   . ARG   A 1 108 ? 14.713  28.125 -19.341 1.00 37.10  ? 119 ARG   A O   1 
ATOM   782  C CB  . ARG   A 1 108 ? 11.735  28.095 -20.281 1.00 50.32  ? 119 ARG   A CB  1 
ATOM   783  C CG  . ARG   A 1 108 ? 11.120  28.442 -21.630 1.00 56.18  ? 119 ARG   A CG  1 
ATOM   784  C CD  . ARG   A 1 108 ? 9.973   29.461 -21.550 1.00 57.97  ? 119 ARG   A CD  1 
ATOM   785  N NE  . ARG   A 1 108 ? 8.790   28.947 -20.848 1.00 60.36  ? 119 ARG   A NE  1 
ATOM   786  C CZ  . ARG   A 1 108 ? 7.666   28.449 -21.398 1.00 63.17  ? 119 ARG   A CZ  1 
ATOM   787  N NH1 . ARG   A 1 108 ? 7.524   28.337 -22.712 1.00 63.46  ? 119 ARG   A NH1 1 
ATOM   788  N NH2 . ARG   A 1 108 ? 6.679   28.031 -20.617 1.00 58.37  ? 119 ARG   A NH2 1 
ATOM   789  N N   . SER   A 1 109 ? 13.609  26.705 -17.970 1.00 38.13  ? 120 SER   A N   1 
ATOM   790  C CA  . SER   A 1 109 ? 14.446  26.935 -16.798 1.00 38.88  ? 120 SER   A CA  1 
ATOM   791  C C   . SER   A 1 109 ? 15.870  26.439 -17.034 1.00 42.28  ? 120 SER   A C   1 
ATOM   792  O O   . SER   A 1 109 ? 16.792  26.877 -16.346 1.00 45.69  ? 120 SER   A O   1 
ATOM   793  C CB  . SER   A 1 109 ? 13.906  26.260 -15.567 1.00 38.55  ? 120 SER   A CB  1 
ATOM   794  O OG  . SER   A 1 109 ? 12.532  26.537 -15.369 1.00 38.41  ? 120 SER   A OG  1 
ATOM   795  N N   . GLN   A 1 110 ? 16.025  25.472 -17.947 1.00 40.64  ? 121 GLN   A N   1 
ATOM   796  C CA  . GLN   A 1 110 ? 17.326  24.903 -18.227 1.00 38.51  ? 121 GLN   A CA  1 
ATOM   797  C C   . GLN   A 1 110 ? 18.195  25.971 -18.859 1.00 39.26  ? 121 GLN   A C   1 
ATOM   798  O O   . GLN   A 1 110 ? 17.745  26.663 -19.765 1.00 39.70  ? 121 GLN   A O   1 
ATOM   799  C CB  . GLN   A 1 110 ? 17.231  23.686 -19.141 1.00 38.57  ? 121 GLN   A CB  1 
ATOM   800  C CG  . GLN   A 1 110 ? 16.654  22.479 -18.422 1.00 40.02  ? 121 GLN   A CG  1 
ATOM   801  C CD  . GLN   A 1 110 ? 17.359  22.211 -17.110 1.00 42.77  ? 121 GLN   A CD  1 
ATOM   802  O OE1 . GLN   A 1 110 ? 18.406  21.553 -17.074 1.00 43.84  ? 121 GLN   A OE1 1 
ATOM   803  N NE2 . GLN   A 1 110 ? 16.791  22.720 -16.022 1.00 43.34  ? 121 GLN   A NE2 1 
ATOM   804  N N   . PRO   A 1 111 ? 19.452  26.125 -18.384 1.00 41.12  ? 122 PRO   A N   1 
ATOM   805  C CA  . PRO   A 1 111 ? 20.408  27.056 -18.979 1.00 42.06  ? 122 PRO   A CA  1 
ATOM   806  C C   . PRO   A 1 111 ? 20.344  27.134 -20.498 1.00 42.51  ? 122 PRO   A C   1 
ATOM   807  O O   . PRO   A 1 111 ? 20.215  28.228 -21.042 1.00 47.74  ? 122 PRO   A O   1 
ATOM   808  C CB  . PRO   A 1 111 ? 21.728  26.467 -18.479 1.00 40.69  ? 122 PRO   A CB  1 
ATOM   809  C CG  . PRO   A 1 111 ? 21.395  26.046 -17.075 1.00 39.39  ? 122 PRO   A CG  1 
ATOM   810  C CD  . PRO   A 1 111 ? 20.025  25.411 -17.234 1.00 40.50  ? 122 PRO   A CD  1 
ATOM   811  N N   . ARG   A 1 112 ? 20.407  25.983 -21.174 1.00 39.07  ? 123 ARG   A N   1 
ATOM   812  C CA  . ARG   A 1 112 ? 20.502  26.009 -22.621 1.00 41.45  ? 123 ARG   A CA  1 
ATOM   813  C C   . ARG   A 1 112 ? 19.137  25.738 -23.243 1.00 34.63  ? 123 ARG   A C   1 
ATOM   814  O O   . ARG   A 1 112 ? 19.025  25.612 -24.460 1.00 32.38  ? 123 ARG   A O   1 
ATOM   815  C CB  . ARG   A 1 112 ? 21.609  25.056 -23.083 1.00 52.94  ? 123 ARG   A CB  1 
ATOM   816  C CG  . ARG   A 1 112 ? 22.980  25.359 -22.485 1.00 63.35  ? 123 ARG   A CG  1 
ATOM   817  C CD  . ARG   A 1 112 ? 24.171  24.805 -23.281 1.00 73.21  ? 123 ARG   A CD  1 
ATOM   818  N NE  . ARG   A 1 112 ? 24.337  23.350 -23.157 1.00 88.07  ? 123 ARG   A NE  1 
ATOM   819  C CZ  . ARG   A 1 112 ? 24.094  22.424 -24.097 1.00 97.26  ? 123 ARG   A CZ  1 
ATOM   820  N NH1 . ARG   A 1 112 ? 23.563  22.750 -25.267 1.00 95.30  ? 123 ARG   A NH1 1 
ATOM   821  N NH2 . ARG   A 1 112 ? 24.363  21.152 -23.848 1.00 98.16  ? 123 ARG   A NH2 1 
ATOM   822  N N   . GLY   A 1 113 ? 18.095  25.663 -22.412 1.00 30.21  ? 124 GLY   A N   1 
ATOM   823  C CA  . GLY   A 1 113 ? 16.782  25.284 -22.900 1.00 27.31  ? 124 GLY   A CA  1 
ATOM   824  C C   . GLY   A 1 113 ? 16.771  23.840 -23.395 1.00 25.70  ? 124 GLY   A C   1 
ATOM   825  O O   . GLY   A 1 113 ? 16.047  23.514 -24.323 1.00 25.54  ? 124 GLY   A O   1 
ATOM   826  N N   . THR   A 1 114 ? 17.569  22.978 -22.758 1.00 24.96  ? 125 THR   A N   1 
ATOM   827  C CA  . THR   A 1 114 ? 17.705  21.588 -23.168 1.00 23.56  ? 125 THR   A CA  1 
ATOM   828  C C   . THR   A 1 114 ? 17.826  20.729 -21.919 1.00 22.32  ? 125 THR   A C   1 
ATOM   829  O O   . THR   A 1 114 ? 18.482  21.125 -20.966 1.00 21.96  ? 125 THR   A O   1 
ATOM   830  C CB  . THR   A 1 114 ? 18.944  21.367 -24.026 1.00 24.93  ? 125 THR   A CB  1 
ATOM   831  O OG1 . THR   A 1 114 ? 20.007  21.291 -23.081 1.00 27.14  ? 125 THR   A OG1 1 
ATOM   832  C CG2 . THR   A 1 114 ? 19.223  22.484 -25.012 1.00 25.73  ? 125 THR   A CG2 1 
ATOM   833  N N   . PHE   A 1 115 ? 17.162  19.577 -21.943 1.00 21.57  ? 126 PHE   A N   1 
ATOM   834  C CA  . PHE   A 1 115 ? 17.325  18.554 -20.943 1.00 20.76  ? 126 PHE   A CA  1 
ATOM   835  C C   . PHE   A 1 115 ? 18.477  17.693 -21.423 1.00 21.26  ? 126 PHE   A C   1 
ATOM   836  O O   . PHE   A 1 115 ? 18.725  17.667 -22.638 1.00 20.32  ? 126 PHE   A O   1 
ATOM   837  C CB  . PHE   A 1 115 ? 16.018  17.760 -20.871 1.00 21.23  ? 126 PHE   A CB  1 
ATOM   838  C CG  . PHE   A 1 115 ? 14.788  18.460 -20.305 1.00 21.08  ? 126 PHE   A CG  1 
ATOM   839  C CD1 . PHE   A 1 115 ? 14.889  19.408 -19.293 1.00 22.02  ? 126 PHE   A CD1 1 
ATOM   840  C CD2 . PHE   A 1 115 ? 13.517  18.114 -20.741 1.00 21.43  ? 126 PHE   A CD2 1 
ATOM   841  C CE1 . PHE   A 1 115 ? 13.760  20.020 -18.769 1.00 21.86  ? 126 PHE   A CE1 1 
ATOM   842  C CE2 . PHE   A 1 115 ? 12.390  18.713 -20.199 1.00 21.82  ? 126 PHE   A CE2 1 
ATOM   843  C CZ  . PHE   A 1 115 ? 12.516  19.677 -19.227 1.00 21.89  ? 126 PHE   A CZ  1 
ATOM   844  N N   . THR   A 1 116 ? 19.139  17.015 -20.470 1.00 21.63  ? 127 THR   A N   1 
ATOM   845  C CA  . THR   A 1 116 ? 20.119  15.978 -20.781 1.00 22.05  ? 127 THR   A CA  1 
ATOM   846  C C   . THR   A 1 116 ? 19.429  14.911 -21.620 1.00 23.47  ? 127 THR   A C   1 
ATOM   847  O O   . THR   A 1 116 ? 18.205  14.944 -21.775 1.00 26.00  ? 127 THR   A O   1 
ATOM   848  C CB  . THR   A 1 116 ? 20.709  15.316 -19.530 1.00 21.49  ? 127 THR   A CB  1 
ATOM   849  O OG1 . THR   A 1 116 ? 19.701  14.534 -18.889 1.00 21.62  ? 127 THR   A OG1 1 
ATOM   850  C CG2 . THR   A 1 116 ? 21.327  16.299 -18.556 1.00 21.17  ? 127 THR   A CG2 1 
ATOM   851  N N   . LEU   A 1 117 ? 20.192  13.918 -22.090 1.00 22.73  ? 128 LEU   A N   1 
ATOM   852  C CA  . LEU   A 1 117 ? 19.554  12.772 -22.721 1.00 21.87  ? 128 LEU   A CA  1 
ATOM   853  C C   . LEU   A 1 117 ? 18.976  11.862 -21.649 1.00 19.68  ? 128 LEU   A C   1 
ATOM   854  O O   . LEU   A 1 117 ? 18.059  11.116 -21.962 1.00 17.87  ? 128 LEU   A O   1 
ATOM   855  C CB  . LEU   A 1 117 ? 20.441  11.965 -23.660 1.00 23.09  ? 128 LEU   A CB  1 
ATOM   856  C CG  . LEU   A 1 117 ? 19.689  11.107 -24.684 1.00 23.76  ? 128 LEU   A CG  1 
ATOM   857  C CD1 . LEU   A 1 117 ? 19.143  11.982 -25.798 1.00 23.64  ? 128 LEU   A CD1 1 
ATOM   858  C CD2 . LEU   A 1 117 ? 20.567  9.995  -25.245 1.00 23.86  ? 128 LEU   A CD2 1 
ATOM   859  N N   . SER   A 1 118 ? 19.508  11.942 -20.417 1.00 19.74  ? 129 SER   A N   1 
ATOM   860  C CA  . SER   A 1 118 ? 19.006  11.163 -19.289 1.00 21.18  ? 129 SER   A CA  1 
ATOM   861  C C   . SER   A 1 118 ? 17.541  11.475 -19.010 1.00 21.99  ? 129 SER   A C   1 
ATOM   862  O O   . SER   A 1 118 ? 16.690  10.578 -18.896 1.00 21.36  ? 129 SER   A O   1 
ATOM   863  C CB  . SER   A 1 118 ? 19.792  11.411 -18.037 1.00 21.26  ? 129 SER   A CB  1 
ATOM   864  O OG  . SER   A 1 118 ? 19.004  11.107 -16.893 1.00 21.65  ? 129 SER   A OG  1 
ATOM   865  N N   . THR   A 1 119 ? 17.291  12.778 -18.852 1.00 22.61  ? 130 THR   A N   1 
ATOM   866  C CA  . THR   A 1 119 ? 15.985  13.269 -18.448 1.00 21.32  ? 130 THR   A CA  1 
ATOM   867  C C   . THR   A 1 119 ? 15.013  13.143 -19.611 1.00 19.50  ? 130 THR   A C   1 
ATOM   868  O O   . THR   A 1 119 ? 13.893  12.702 -19.400 1.00 18.19  ? 130 THR   A O   1 
ATOM   869  C CB  . THR   A 1 119 ? 16.121  14.699 -17.946 1.00 21.30  ? 130 THR   A CB  1 
ATOM   870  O OG1 . THR   A 1 119 ? 16.414  14.481 -16.567 1.00 20.92  ? 130 THR   A OG1 1 
ATOM   871  C CG2 . THR   A 1 119 ? 14.844  15.486 -18.149 1.00 22.15  ? 130 THR   A CG2 1 
ATOM   872  N N   . THR   A 1 120 ? 15.480  13.478 -20.821 1.00 18.82  ? 131 THR   A N   1 
ATOM   873  C CA  . THR   A 1 120 ? 14.692  13.296 -22.031 1.00 19.83  ? 131 THR   A CA  1 
ATOM   874  C C   . THR   A 1 120 ? 14.230  11.848 -22.180 1.00 20.80  ? 131 THR   A C   1 
ATOM   875  O O   . THR   A 1 120 ? 13.048  11.596 -22.405 1.00 20.51  ? 131 THR   A O   1 
ATOM   876  C CB  . THR   A 1 120 ? 15.494  13.746 -23.249 1.00 20.40  ? 131 THR   A CB  1 
ATOM   877  O OG1 . THR   A 1 120 ? 15.677  15.138 -23.019 1.00 21.69  ? 131 THR   A OG1 1 
ATOM   878  C CG2 . THR   A 1 120 ? 14.786  13.511 -24.577 1.00 19.85  ? 131 THR   A CG2 1 
ATOM   879  N N   . LEU   A 1 121 ? 15.149  10.884 -22.096 1.00 23.03  ? 132 LEU   A N   1 
ATOM   880  C CA  . LEU   A 1 121 ? 14.774  9.517  -22.428 1.00 25.13  ? 132 LEU   A CA  1 
ATOM   881  C C   . LEU   A 1 121 ? 13.786  9.000  -21.394 1.00 28.59  ? 132 LEU   A C   1 
ATOM   882  O O   . LEU   A 1 121 ? 12.869  8.247  -21.728 1.00 28.46  ? 132 LEU   A O   1 
ATOM   883  C CB  . LEU   A 1 121 ? 15.990  8.608  -22.563 1.00 24.46  ? 132 LEU   A CB  1 
ATOM   884  C CG  . LEU   A 1 121 ? 16.835  8.857  -23.818 1.00 25.18  ? 132 LEU   A CG  1 
ATOM   885  C CD1 . LEU   A 1 121 ? 18.065  7.938  -23.887 1.00 25.04  ? 132 LEU   A CD1 1 
ATOM   886  C CD2 . LEU   A 1 121 ? 15.968  8.738  -25.084 1.00 24.64  ? 132 LEU   A CD2 1 
ATOM   887  N N   . ARG   A 1 122 ? 13.970  9.447  -20.147 1.00 32.73  ? 133 ARG   A N   1 
ATOM   888  C CA  . ARG   A 1 122 ? 13.112  9.021  -19.057 1.00 36.54  ? 133 ARG   A CA  1 
ATOM   889  C C   . ARG   A 1 122 ? 11.718  9.634  -19.207 1.00 36.44  ? 133 ARG   A C   1 
ATOM   890  O O   . ARG   A 1 122 ? 10.723  8.908  -19.130 1.00 36.18  ? 133 ARG   A O   1 
ATOM   891  C CB  . ARG   A 1 122 ? 13.848  9.260  -17.735 1.00 40.27  ? 133 ARG   A CB  1 
ATOM   892  C CG  . ARG   A 1 122 ? 14.875  8.160  -17.496 1.00 42.45  ? 133 ARG   A CG  1 
ATOM   893  C CD  . ARG   A 1 122 ? 15.573  8.269  -16.158 1.00 44.74  ? 133 ARG   A CD  1 
ATOM   894  N NE  . ARG   A 1 122 ? 16.452  9.442  -16.074 1.00 44.41  ? 133 ARG   A NE  1 
ATOM   895  C CZ  . ARG   A 1 122 ? 16.465  10.340 -15.101 1.00 41.59  ? 133 ARG   A CZ  1 
ATOM   896  N NH1 . ARG   A 1 122 ? 15.628  10.221 -14.075 1.00 41.84  ? 133 ARG   A NH1 1 
ATOM   897  N NH2 . ARG   A 1 122 ? 17.328  11.344 -15.178 1.00 38.83  ? 133 ARG   A NH2 1 
ATOM   898  N N   . LEU   A 1 123 ? 11.651  10.955 -19.441 1.00 36.02  ? 134 LEU   A N   1 
ATOM   899  C CA  . LEU   A 1 123 ? 10.395  11.616 -19.777 1.00 34.05  ? 134 LEU   A CA  1 
ATOM   900  C C   . LEU   A 1 123 ? 9.729   10.857 -20.926 1.00 33.82  ? 134 LEU   A C   1 
ATOM   901  O O   . LEU   A 1 123 ? 8.621   10.347 -20.772 1.00 35.27  ? 134 LEU   A O   1 
ATOM   902  C CB  . LEU   A 1 123 ? 10.629  13.088 -20.113 1.00 34.36  ? 134 LEU   A CB  1 
ATOM   903  C CG  . LEU   A 1 123 ? 11.032  13.994 -18.940 1.00 37.01  ? 134 LEU   A CG  1 
ATOM   904  C CD1 . LEU   A 1 123 ? 11.358  15.422 -19.377 1.00 36.59  ? 134 LEU   A CD1 1 
ATOM   905  C CD2 . LEU   A 1 123 ? 9.958   14.038 -17.853 1.00 38.63  ? 134 LEU   A CD2 1 
ATOM   906  N N   . GLY   A 1 124 ? 10.449  10.725 -22.045 1.00 33.35  ? 135 GLY   A N   1 
ATOM   907  C CA  . GLY   A 1 124 ? 10.045  9.866  -23.152 1.00 35.42  ? 135 GLY   A CA  1 
ATOM   908  C C   . GLY   A 1 124 ? 9.229   8.642  -22.723 1.00 35.70  ? 135 GLY   A C   1 
ATOM   909  O O   . GLY   A 1 124 ? 8.118   8.441  -23.219 1.00 37.91  ? 135 GLY   A O   1 
ATOM   910  N N   . LYS   A 1 125 ? 9.789   7.826  -21.817 1.00 34.02  ? 136 LYS   A N   1 
ATOM   911  C CA  . LYS   A 1 125 ? 9.163   6.575  -21.411 1.00 35.19  ? 136 LYS   A CA  1 
ATOM   912  C C   . LYS   A 1 125 ? 7.827   6.829  -20.714 1.00 31.91  ? 136 LYS   A C   1 
ATOM   913  O O   . LYS   A 1 125 ? 6.904   6.017  -20.824 1.00 31.19  ? 136 LYS   A O   1 
ATOM   914  C CB  . LYS   A 1 125 ? 9.986   5.737  -20.423 1.00 39.62  ? 136 LYS   A CB  1 
ATOM   915  C CG  . LYS   A 1 125 ? 11.234  5.005  -20.931 1.00 42.61  ? 136 LYS   A CG  1 
ATOM   916  C CD  . LYS   A 1 125 ? 11.856  4.059  -19.898 1.00 45.75  ? 136 LYS   A CD  1 
ATOM   917  C CE  . LYS   A 1 125 ? 10.915  2.998  -19.369 1.00 48.38  ? 136 LYS   A CE  1 
ATOM   918  N NZ  . LYS   A 1 125 ? 11.547  2.030  -18.462 1.00 48.34  ? 136 LYS   A NZ  1 
ATOM   919  N N   . GLN   A 1 126 ? 7.740   7.930  -19.960 1.00 29.52  ? 137 GLN   A N   1 
ATOM   920  C CA  . GLN   A 1 126 ? 6.565   8.179  -19.142 1.00 28.95  ? 137 GLN   A CA  1 
ATOM   921  C C   . GLN   A 1 126 ? 5.460   8.834  -19.964 1.00 29.16  ? 137 GLN   A C   1 
ATOM   922  O O   . GLN   A 1 126 ? 4.275   8.673  -19.662 1.00 30.83  ? 137 GLN   A O   1 
ATOM   923  C CB  . GLN   A 1 126 ? 6.883   9.064  -17.945 1.00 27.48  ? 137 GLN   A CB  1 
ATOM   924  C CG  . GLN   A 1 126 ? 7.486   8.327  -16.757 1.00 25.74  ? 137 GLN   A CG  1 
ATOM   925  C CD  . GLN   A 1 126 ? 7.398   9.182  -15.519 1.00 24.18  ? 137 GLN   A CD  1 
ATOM   926  O OE1 . GLN   A 1 126 ? 6.322   9.378  -14.942 1.00 24.84  ? 137 GLN   A OE1 1 
ATOM   927  N NE2 . GLN   A 1 126 ? 8.519   9.778  -15.160 1.00 23.39  ? 137 GLN   A NE2 1 
ATOM   928  N N   . ILE   A 1 127 ? 5.861   9.597  -20.981 1.00 27.62  ? 138 ILE   A N   1 
ATOM   929  C CA  . ILE   A 1 127 ? 4.891   10.281 -21.807 1.00 27.85  ? 138 ILE   A CA  1 
ATOM   930  C C   . ILE   A 1 127 ? 4.267   9.248  -22.729 1.00 26.60  ? 138 ILE   A C   1 
ATOM   931  O O   . ILE   A 1 127 ? 3.054   9.229  -22.871 1.00 28.38  ? 138 ILE   A O   1 
ATOM   932  C CB  . ILE   A 1 127 ? 5.517   11.481 -22.544 1.00 28.68  ? 138 ILE   A CB  1 
ATOM   933  C CG1 . ILE   A 1 127 ? 5.760   12.633 -21.562 1.00 26.27  ? 138 ILE   A CG1 1 
ATOM   934  C CG2 . ILE   A 1 127 ? 4.657   11.928 -23.729 1.00 29.37  ? 138 ILE   A CG2 1 
ATOM   935  C CD1 . ILE   A 1 127 ? 6.400   13.859 -22.176 1.00 25.50  ? 138 ILE   A CD1 1 
ATOM   936  N N   . LEU   A 1 128 ? 5.101   8.386  -23.309 1.00 26.14  ? 139 LEU   A N   1 
ATOM   937  C CA  . LEU   A 1 128 ? 4.636   7.298  -24.159 1.00 26.23  ? 139 LEU   A CA  1 
ATOM   938  C C   . LEU   A 1 128 ? 3.624   6.374  -23.487 1.00 24.88  ? 139 LEU   A C   1 
ATOM   939  O O   . LEU   A 1 128 ? 2.784   5.836  -24.192 1.00 23.26  ? 139 LEU   A O   1 
ATOM   940  C CB  . LEU   A 1 128 ? 5.804   6.438  -24.620 1.00 26.74  ? 139 LEU   A CB  1 
ATOM   941  C CG  . LEU   A 1 128 ? 5.399   5.161  -25.360 1.00 26.37  ? 139 LEU   A CG  1 
ATOM   942  C CD1 . LEU   A 1 128 ? 4.570   5.512  -26.592 1.00 26.06  ? 139 LEU   A CD1 1 
ATOM   943  C CD2 . LEU   A 1 128 ? 6.620   4.327  -25.749 1.00 27.46  ? 139 LEU   A CD2 1 
ATOM   944  N N   . GLU   A 1 129 ? 3.774   6.084  -22.185 1.00 26.07  ? 140 GLU   A N   1 
ATOM   945  C CA  . GLU   A 1 129 ? 2.788   5.292  -21.433 1.00 28.00  ? 140 GLU   A CA  1 
ATOM   946  C C   . GLU   A 1 129 ? 1.385   5.941  -21.377 1.00 26.36  ? 140 GLU   A C   1 
ATOM   947  O O   . GLU   A 1 129 ? 0.278   5.373  -21.600 1.00 23.41  ? 140 GLU   A O   1 
ATOM   948  C CB  . GLU   A 1 129 ? 3.375   5.143  -20.026 1.00 32.34  ? 140 GLU   A CB  1 
ATOM   949  C CG  . GLU   A 1 129 ? 4.420   4.038  -19.917 1.00 38.15  ? 140 GLU   A CG  1 
ATOM   950  C CD  . GLU   A 1 129 ? 5.079   3.973  -18.545 1.00 44.75  ? 140 GLU   A CD  1 
ATOM   951  O OE1 . GLU   A 1 129 ? 6.335   3.962  -18.490 1.00 47.40  ? 140 GLU   A OE1 1 
ATOM   952  O OE2 . GLU   A 1 129 ? 4.340   3.945  -17.525 1.00 47.05  ? 140 GLU   A OE2 1 
ATOM   953  N N   . SER   A 1 130 ? 1.410   7.223  -21.054 1.00 25.95  ? 141 SER   A N   1 
ATOM   954  C CA  . SER   A 1 130 ? 0.161   7.939  -20.929 1.00 24.71  ? 141 SER   A CA  1 
ATOM   955  C C   . SER   A 1 130 ? -0.506  8.068  -22.292 1.00 22.63  ? 141 SER   A C   1 
ATOM   956  O O   . SER   A 1 130 ? -1.721  8.206  -22.345 1.00 23.95  ? 141 SER   A O   1 
ATOM   957  C CB  . SER   A 1 130 ? 0.387   9.258  -20.311 1.00 26.07  ? 141 SER   A CB  1 
ATOM   958  O OG  . SER   A 1 130 ? 1.330   9.991  -21.077 1.00 28.12  ? 141 SER   A OG  1 
ATOM   959  N N   . ILE   A 1 131 ? 0.275   8.037  -23.379 1.00 20.95  ? 142 ILE   A N   1 
ATOM   960  C CA  . ILE   A 1 131 ? -0.300  8.059  -24.715 1.00 20.05  ? 142 ILE   A CA  1 
ATOM   961  C C   . ILE   A 1 131 ? -0.960  6.720  -25.015 1.00 19.87  ? 142 ILE   A C   1 
ATOM   962  O O   . ILE   A 1 131 ? -2.157  6.670  -25.307 1.00 18.40  ? 142 ILE   A O   1 
ATOM   963  C CB  . ILE   A 1 131 ? 0.730   8.446  -25.788 1.00 19.98  ? 142 ILE   A CB  1 
ATOM   964  C CG1 . ILE   A 1 131 ? 1.093   9.919  -25.651 1.00 20.45  ? 142 ILE   A CG1 1 
ATOM   965  C CG2 . ILE   A 1 131 ? 0.223   8.124  -27.199 1.00 19.59  ? 142 ILE   A CG2 1 
ATOM   966  C CD1 . ILE   A 1 131 ? 2.140   10.411 -26.634 1.00 20.68  ? 142 ILE   A CD1 1 
ATOM   967  N N   . GLU   A 1 132 ? -0.170  5.645  -24.956 1.00 21.10  ? 143 GLU   A N   1 
ATOM   968  C CA  . GLU   A 1 132 ? -0.721  4.302  -25.043 1.00 23.33  ? 143 GLU   A CA  1 
ATOM   969  C C   . GLU   A 1 132 ? -1.965  4.209  -24.155 1.00 23.36  ? 143 GLU   A C   1 
ATOM   970  O O   . GLU   A 1 132 ? -3.040  3.882  -24.658 1.00 23.33  ? 143 GLU   A O   1 
ATOM   971  C CB  . GLU   A 1 132 ? 0.326   3.237  -24.706 1.00 24.82  ? 143 GLU   A CB  1 
ATOM   972  C CG  . GLU   A 1 132 ? -0.262  1.828  -24.632 1.00 26.62  ? 143 GLU   A CG  1 
ATOM   973  C CD  . GLU   A 1 132 ? 0.702   0.727  -25.014 1.00 27.82  ? 143 GLU   A CD  1 
ATOM   974  O OE1 . GLU   A 1 132 ? 1.714   0.461  -24.321 1.00 27.90  ? 143 GLU   A OE1 1 
ATOM   975  O OE2 . GLU   A 1 132 ? 0.408   0.149  -26.078 1.00 29.07  ? 143 GLU   A OE2 1 
ATOM   976  N N   . ALA   A 1 133 ? -1.814  4.530  -22.855 1.00 22.18  ? 144 ALA   A N   1 
ATOM   977  C CA  . ALA   A 1 133 ? -2.917  4.548  -21.900 1.00 22.40  ? 144 ALA   A CA  1 
ATOM   978  C C   . ALA   A 1 133 ? -4.204  5.109  -22.516 1.00 20.95  ? 144 ALA   A C   1 
ATOM   979  O O   . ALA   A 1 133 ? -5.252  4.464  -22.515 1.00 19.31  ? 144 ALA   A O   1 
ATOM   980  C CB  . ALA   A 1 133 ? -2.535  5.338  -20.662 1.00 23.89  ? 144 ALA   A CB  1 
ATOM   981  N N   . ILE   A 1 134 ? -4.140  6.340  -23.023 1.00 20.59  ? 145 ILE   A N   1 
ATOM   982  C CA  . ILE   A 1 134 ? -5.347  6.960  -23.538 1.00 19.85  ? 145 ILE   A CA  1 
ATOM   983  C C   . ILE   A 1 134 ? -5.751  6.248  -24.828 1.00 19.79  ? 145 ILE   A C   1 
ATOM   984  O O   . ILE   A 1 134 ? -6.940  6.054  -25.057 1.00 21.48  ? 145 ILE   A O   1 
ATOM   985  C CB  . ILE   A 1 134 ? -5.206  8.486  -23.702 1.00 18.62  ? 145 ILE   A CB  1 
ATOM   986  C CG1 . ILE   A 1 134 ? -6.550  9.131  -24.052 1.00 17.18  ? 145 ILE   A CG1 1 
ATOM   987  C CG2 . ILE   A 1 134 ? -4.107  8.843  -24.706 1.00 18.85  ? 145 ILE   A CG2 1 
ATOM   988  C CD1 . ILE   A 1 134 ? -6.508  10.646 -24.124 1.00 17.03  ? 145 ILE   A CD1 1 
ATOM   989  N N   . HIS   A 1 135 ? -4.795  5.826  -25.665 1.00 17.88  ? 146 HIS   A N   1 
ATOM   990  C CA  . HIS   A 1 135 ? -5.219  5.130  -26.868 1.00 17.31  ? 146 HIS   A CA  1 
ATOM   991  C C   . HIS   A 1 135 ? -6.038  3.914  -26.414 1.00 16.93  ? 146 HIS   A C   1 
ATOM   992  O O   . HIS   A 1 135 ? -7.140  3.688  -26.910 1.00 16.73  ? 146 HIS   A O   1 
ATOM   993  C CB  . HIS   A 1 135 ? -4.063  4.890  -27.859 1.00 16.90  ? 146 HIS   A CB  1 
ATOM   994  C CG  . HIS   A 1 135 ? -3.475  6.130  -28.472 1.00 16.18  ? 146 HIS   A CG  1 
ATOM   995  N ND1 . HIS   A 1 135 ? -2.166  6.209  -28.904 1.00 15.94  ? 146 HIS   A ND1 1 
ATOM   996  C CD2 . HIS   A 1 135 ? -3.993  7.348  -28.682 1.00 15.72  ? 146 HIS   A CD2 1 
ATOM   997  C CE1 . HIS   A 1 135 ? -1.922  7.422  -29.367 1.00 15.16  ? 146 HIS   A CE1 1 
ATOM   998  N NE2 . HIS   A 1 135 ? -3.023  8.129  -29.250 1.00 15.04  ? 146 HIS   A NE2 1 
ATOM   999  N N   . SER   A 1 136 ? -5.545  3.212  -25.387 1.00 16.47  ? 147 SER   A N   1 
ATOM   1000 C CA  . SER   A 1 136 ? -6.157  2.000  -24.866 1.00 15.91  ? 147 SER   A CA  1 
ATOM   1001 C C   . SER   A 1 136 ? -7.648  2.166  -24.572 1.00 17.07  ? 147 SER   A C   1 
ATOM   1002 O O   . SER   A 1 136 ? -8.383  1.189  -24.702 1.00 17.98  ? 147 SER   A O   1 
ATOM   1003 C CB  . SER   A 1 136 ? -5.487  1.573  -23.607 1.00 15.42  ? 147 SER   A CB  1 
ATOM   1004 O OG  . SER   A 1 136 ? -6.138  2.187  -22.506 1.00 14.67  ? 147 SER   A OG  1 
ATOM   1005 N N   . VAL   A 1 137 ? -8.071  3.352  -24.091 1.00 17.04  ? 148 VAL   A N   1 
ATOM   1006 C CA  . VAL   A 1 137 ? -9.473  3.647  -23.800 1.00 16.12  ? 148 VAL   A CA  1 
ATOM   1007 C C   . VAL   A 1 137 ? -10.081 4.502  -24.918 1.00 15.97  ? 148 VAL   A C   1 
ATOM   1008 O O   . VAL   A 1 137 ? -10.969 5.314  -24.667 1.00 16.12  ? 148 VAL   A O   1 
ATOM   1009 C CB  . VAL   A 1 137 ? -9.656  4.331  -22.428 1.00 16.09  ? 148 VAL   A CB  1 
ATOM   1010 C CG1 . VAL   A 1 137 ? -9.008  3.549  -21.293 1.00 16.03  ? 148 VAL   A CG1 1 
ATOM   1011 C CG2 . VAL   A 1 137 ? -9.139  5.764  -22.420 1.00 16.34  ? 148 VAL   A CG2 1 
ATOM   1012 N N   . GLY   A 1 138 ? -9.587  4.331  -26.151 1.00 16.28  ? 149 GLY   A N   1 
ATOM   1013 C CA  . GLY   A 1 138 ? -10.329 4.687  -27.350 1.00 16.65  ? 149 GLY   A CA  1 
ATOM   1014 C C   . GLY   A 1 138 ? -10.353 6.187  -27.631 1.00 17.23  ? 149 GLY   A C   1 
ATOM   1015 O O   . GLY   A 1 138 ? -11.277 6.658  -28.295 1.00 17.46  ? 149 GLY   A O   1 
ATOM   1016 N N   . PHE   A 1 139 ? -9.322  6.919  -27.167 1.00 17.84  ? 150 PHE   A N   1 
ATOM   1017 C CA  . PHE   A 1 139 ? -9.212  8.359  -27.395 1.00 18.04  ? 150 PHE   A CA  1 
ATOM   1018 C C   . PHE   A 1 139 ? -7.815  8.808  -27.870 1.00 18.82  ? 150 PHE   A C   1 
ATOM   1019 O O   . PHE   A 1 139 ? -6.779  8.352  -27.373 1.00 18.27  ? 150 PHE   A O   1 
ATOM   1020 C CB  . PHE   A 1 139 ? -9.604  9.052  -26.084 1.00 17.30  ? 150 PHE   A CB  1 
ATOM   1021 C CG  . PHE   A 1 139 ? -11.098 9.217  -25.849 1.00 16.71  ? 150 PHE   A CG  1 
ATOM   1022 C CD1 . PHE   A 1 139 ? -11.911 8.117  -25.599 1.00 16.51  ? 150 PHE   A CD1 1 
ATOM   1023 C CD2 . PHE   A 1 139 ? -11.680 10.474 -25.828 1.00 16.30  ? 150 PHE   A CD2 1 
ATOM   1024 C CE1 . PHE   A 1 139 ? -13.268 8.263  -25.373 1.00 16.04  ? 150 PHE   A CE1 1 
ATOM   1025 C CE2 . PHE   A 1 139 ? -13.040 10.604 -25.601 1.00 16.81  ? 150 PHE   A CE2 1 
ATOM   1026 C CZ  . PHE   A 1 139 ? -13.830 9.501  -25.375 1.00 15.91  ? 150 PHE   A CZ  1 
ATOM   1027 N N   . LEU   A 1 140 ? -7.804  9.764  -28.817 1.00 19.66  ? 151 LEU   A N   1 
ATOM   1028 C CA  . LEU   A 1 140 ? -6.615  10.531 -29.178 1.00 20.83  ? 151 LEU   A CA  1 
ATOM   1029 C C   . LEU   A 1 140 ? -6.506  11.753 -28.255 1.00 21.64  ? 151 LEU   A C   1 
ATOM   1030 O O   . LEU   A 1 140 ? -7.539  12.332 -27.920 1.00 22.43  ? 151 LEU   A O   1 
ATOM   1031 C CB  . LEU   A 1 140 ? -6.712  10.975 -30.644 1.00 20.57  ? 151 LEU   A CB  1 
ATOM   1032 C CG  . LEU   A 1 140 ? -7.091  9.915  -31.688 1.00 20.56  ? 151 LEU   A CG  1 
ATOM   1033 C CD1 . LEU   A 1 140 ? -7.115  10.533 -33.060 1.00 20.77  ? 151 LEU   A CD1 1 
ATOM   1034 C CD2 . LEU   A 1 140 ? -6.172  8.720  -31.743 1.00 20.83  ? 151 LEU   A CD2 1 
ATOM   1035 N N   . HIS   A 1 141 ? -5.281  12.180 -27.877 1.00 21.40  ? 152 HIS   A N   1 
ATOM   1036 C CA  . HIS   A 1 141 ? -5.091  13.456 -27.194 1.00 21.30  ? 152 HIS   A CA  1 
ATOM   1037 C C   . HIS   A 1 141 ? -5.116  14.629 -28.176 1.00 21.63  ? 152 HIS   A C   1 
ATOM   1038 O O   . HIS   A 1 141 ? -5.673  15.671 -27.852 1.00 21.88  ? 152 HIS   A O   1 
ATOM   1039 C CB  . HIS   A 1 141 ? -3.761  13.543 -26.446 1.00 21.60  ? 152 HIS   A CB  1 
ATOM   1040 C CG  . HIS   A 1 141 ? -3.713  14.709 -25.501 1.00 22.93  ? 152 HIS   A CG  1 
ATOM   1041 N ND1 . HIS   A 1 141 ? -3.516  16.017 -25.891 1.00 22.76  ? 152 HIS   A ND1 1 
ATOM   1042 C CD2 . HIS   A 1 141 ? -3.854  14.745 -24.157 1.00 23.10  ? 152 HIS   A CD2 1 
ATOM   1043 C CE1 . HIS   A 1 141 ? -3.530  16.798 -24.817 1.00 22.94  ? 152 HIS   A CE1 1 
ATOM   1044 N NE2 . HIS   A 1 141 ? -3.724  16.047 -23.754 1.00 23.25  ? 152 HIS   A NE2 1 
ATOM   1045 N N   . ARG   A 1 142 ? -4.433  14.466 -29.322 1.00 21.99  ? 153 ARG   A N   1 
ATOM   1046 C CA  . ARG   A 1 142 ? -4.383  15.410 -30.432 1.00 21.50  ? 153 ARG   A CA  1 
ATOM   1047 C C   . ARG   A 1 142 ? -3.639  16.702 -30.088 1.00 23.42  ? 153 ARG   A C   1 
ATOM   1048 O O   . ARG   A 1 142 ? -3.132  17.357 -31.009 1.00 24.90  ? 153 ARG   A O   1 
ATOM   1049 C CB  . ARG   A 1 142 ? -5.754  15.745 -31.010 1.00 21.33  ? 153 ARG   A CB  1 
ATOM   1050 C CG  . ARG   A 1 142 ? -6.411  14.547 -31.682 1.00 23.03  ? 153 ARG   A CG  1 
ATOM   1051 C CD  . ARG   A 1 142 ? -7.666  14.912 -32.500 1.00 22.64  ? 153 ARG   A CD  1 
ATOM   1052 N NE  . ARG   A 1 142 ? -8.691  15.602 -31.711 1.00 22.53  ? 153 ARG   A NE  1 
ATOM   1053 C CZ  . ARG   A 1 142 ? -9.735  16.242 -32.193 1.00 22.94  ? 153 ARG   A CZ  1 
ATOM   1054 N NH1 . ARG   A 1 142 ? -10.549 16.846 -31.357 1.00 24.37  ? 153 ARG   A NH1 1 
ATOM   1055 N NH2 . ARG   A 1 142 ? -9.979  16.294 -33.487 1.00 23.35  ? 153 ARG   A NH2 1 
ATOM   1056 N N   . ASP   A 1 143 ? -3.578  17.093 -28.800 1.00 23.23  ? 154 ASP   A N   1 
ATOM   1057 C CA  . ASP   A 1 143 ? -2.779  18.250 -28.415 1.00 24.42  ? 154 ASP   A CA  1 
ATOM   1058 C C   . ASP   A 1 143 ? -1.733  17.842 -27.385 1.00 23.02  ? 154 ASP   A C   1 
ATOM   1059 O O   . ASP   A 1 143 ? -1.864  18.130 -26.200 1.00 22.86  ? 154 ASP   A O   1 
ATOM   1060 C CB  . ASP   A 1 143 ? -3.614  19.449 -27.989 1.00 27.27  ? 154 ASP   A CB  1 
ATOM   1061 C CG  . ASP   A 1 143 ? -2.958  20.816 -28.189 1.00 30.86  ? 154 ASP   A CG  1 
ATOM   1062 O OD1 . ASP   A 1 143 ? -1.848  20.881 -28.778 1.00 32.72  ? 154 ASP   A OD1 1 
ATOM   1063 O OD2 . ASP   A 1 143 ? -3.557  21.829 -27.766 1.00 33.63  ? 154 ASP   A OD2 1 
ATOM   1064 N N   . ILE   A 1 144 ? -0.674  17.211 -27.901 1.00 22.29  ? 155 ILE   A N   1 
ATOM   1065 C CA  . ILE   A 1 144 ? 0.487   16.775 -27.149 1.00 20.90  ? 155 ILE   A CA  1 
ATOM   1066 C C   . ILE   A 1 144 ? 1.564   17.856 -27.224 1.00 20.19  ? 155 ILE   A C   1 
ATOM   1067 O O   . ILE   A 1 144 ? 2.108   18.136 -28.296 1.00 19.39  ? 155 ILE   A O   1 
ATOM   1068 C CB  . ILE   A 1 144 ? 0.990   15.427 -27.700 1.00 20.31  ? 155 ILE   A CB  1 
ATOM   1069 C CG1 . ILE   A 1 144 ? -0.102  14.365 -27.715 1.00 20.64  ? 155 ILE   A CG1 1 
ATOM   1070 C CG2 . ILE   A 1 144 ? 2.223   14.942 -26.940 1.00 20.18  ? 155 ILE   A CG2 1 
ATOM   1071 C CD1 . ILE   A 1 144 ? -0.436  13.809 -26.342 1.00 21.12  ? 155 ILE   A CD1 1 
ATOM   1072 N N   . LYS   A 1 145 ? 1.882   18.432 -26.062 1.00 20.56  ? 156 LYS   A N   1 
ATOM   1073 C CA  . LYS   A 1 145 ? 2.962   19.401 -25.972 1.00 21.39  ? 156 LYS   A CA  1 
ATOM   1074 C C   . LYS   A 1 145 ? 3.556   19.416 -24.564 1.00 19.92  ? 156 LYS   A C   1 
ATOM   1075 O O   . LYS   A 1 145 ? 2.953   18.907 -23.607 1.00 17.73  ? 156 LYS   A O   1 
ATOM   1076 C CB  . LYS   A 1 145 ? 2.456   20.789 -26.381 1.00 22.79  ? 156 LYS   A CB  1 
ATOM   1077 C CG  . LYS   A 1 145 ? 1.281   21.309 -25.582 1.00 24.55  ? 156 LYS   A CG  1 
ATOM   1078 C CD  . LYS   A 1 145 ? 0.674   22.536 -26.243 1.00 26.76  ? 156 LYS   A CD  1 
ATOM   1079 C CE  . LYS   A 1 145 ? -0.596  23.003 -25.605 1.00 27.68  ? 156 LYS   A CE  1 
ATOM   1080 N NZ  . LYS   A 1 145 ? -0.902  24.337 -26.127 1.00 27.79  ? 156 LYS   A NZ  1 
ATOM   1081 N N   . PRO   A 1 146 ? 4.767   20.011 -24.419 1.00 18.97  ? 157 PRO   A N   1 
ATOM   1082 C CA  . PRO   A 1 146 ? 5.415   20.114 -23.114 1.00 19.53  ? 157 PRO   A CA  1 
ATOM   1083 C C   . PRO   A 1 146 ? 4.389   20.587 -22.089 1.00 19.17  ? 157 PRO   A C   1 
ATOM   1084 O O   . PRO   A 1 146 ? 3.925   19.806 -21.263 1.00 17.65  ? 157 PRO   A O   1 
ATOM   1085 C CB  . PRO   A 1 146 ? 6.594   21.094 -23.377 1.00 19.46  ? 157 PRO   A CB  1 
ATOM   1086 C CG  . PRO   A 1 146 ? 6.926   20.869 -24.849 1.00 18.98  ? 157 PRO   A CG  1 
ATOM   1087 C CD  . PRO   A 1 146 ? 5.585   20.586 -25.505 1.00 18.52  ? 157 PRO   A CD  1 
ATOM   1088 N N   . SER   A 1 147 ? 3.945   21.831 -22.266 1.00 20.89  ? 158 SER   A N   1 
ATOM   1089 C CA  . SER   A 1 147 ? 3.063   22.528 -21.346 1.00 21.88  ? 158 SER   A CA  1 
ATOM   1090 C C   . SER   A 1 147 ? 1.804   21.722 -21.021 1.00 22.83  ? 158 SER   A C   1 
ATOM   1091 O O   . SER   A 1 147 ? 1.031   22.114 -20.141 1.00 22.54  ? 158 SER   A O   1 
ATOM   1092 C CB  . SER   A 1 147 ? 2.697   23.845 -21.942 1.00 21.63  ? 158 SER   A CB  1 
ATOM   1093 O OG  . SER   A 1 147 ? 2.124   23.599 -23.214 1.00 21.43  ? 158 SER   A OG  1 
ATOM   1094 N N   . ASN   A 1 148 ? 1.579   20.614 -21.745 1.00 23.60  ? 159 ASN   A N   1 
ATOM   1095 C CA  . ASN   A 1 148 ? 0.467   19.734 -21.422 1.00 23.84  ? 159 ASN   A CA  1 
ATOM   1096 C C   . ASN   A 1 148 ? 0.897   18.589 -20.517 1.00 22.89  ? 159 ASN   A C   1 
ATOM   1097 O O   . ASN   A 1 148 ? 0.059   17.752 -20.214 1.00 23.09  ? 159 ASN   A O   1 
ATOM   1098 C CB  . ASN   A 1 148 ? -0.261  19.204 -22.653 1.00 24.79  ? 159 ASN   A CB  1 
ATOM   1099 C CG  . ASN   A 1 148 ? -1.624  19.834 -22.804 1.00 26.50  ? 159 ASN   A CG  1 
ATOM   1100 O OD1 . ASN   A 1 148 ? -2.041  20.605 -21.937 1.00 28.90  ? 159 ASN   A OD1 1 
ATOM   1101 N ND2 . ASN   A 1 148 ? -2.329  19.543 -23.885 1.00 27.46  ? 159 ASN   A ND2 1 
ATOM   1102 N N   . PHE   A 1 149 ? 2.161   18.558 -20.073 1.00 21.71  ? 160 PHE   A N   1 
ATOM   1103 C CA  . PHE   A 1 149 ? 2.563   17.595 -19.060 1.00 21.03  ? 160 PHE   A CA  1 
ATOM   1104 C C   . PHE   A 1 149 ? 3.247   18.302 -17.904 1.00 19.13  ? 160 PHE   A C   1 
ATOM   1105 O O   . PHE   A 1 149 ? 3.872   19.343 -18.087 1.00 18.31  ? 160 PHE   A O   1 
ATOM   1106 C CB  . PHE   A 1 149 ? 3.522   16.521 -19.569 1.00 21.98  ? 160 PHE   A CB  1 
ATOM   1107 C CG  . PHE   A 1 149 ? 2.877   15.586 -20.578 1.00 22.14  ? 160 PHE   A CG  1 
ATOM   1108 C CD1 . PHE   A 1 149 ? 2.821   15.934 -21.923 1.00 22.35  ? 160 PHE   A CD1 1 
ATOM   1109 C CD2 . PHE   A 1 149 ? 2.340   14.366 -20.179 1.00 22.44  ? 160 PHE   A CD2 1 
ATOM   1110 C CE1 . PHE   A 1 149 ? 2.233   15.088 -22.851 1.00 22.60  ? 160 PHE   A CE1 1 
ATOM   1111 C CE2 . PHE   A 1 149 ? 1.755   13.525 -21.105 1.00 23.49  ? 160 PHE   A CE2 1 
ATOM   1112 C CZ  . PHE   A 1 149 ? 1.695   13.889 -22.440 1.00 23.33  ? 160 PHE   A CZ  1 
ATOM   1113 N N   . ALA   A 1 150 ? 3.141   17.675 -16.733 1.00 17.95  ? 161 ALA   A N   1 
ATOM   1114 C CA  . ALA   A 1 150 ? 3.689   18.235 -15.514 1.00 17.59  ? 161 ALA   A CA  1 
ATOM   1115 C C   . ALA   A 1 150 ? 4.205   17.133 -14.608 1.00 17.38  ? 161 ALA   A C   1 
ATOM   1116 O O   . ALA   A 1 150 ? 4.083   15.946 -14.875 1.00 17.39  ? 161 ALA   A O   1 
ATOM   1117 C CB  . ALA   A 1 150 ? 2.662   19.067 -14.792 1.00 17.35  ? 161 ALA   A CB  1 
ATOM   1118 N N   . MET   A 1 151 ? 4.812   17.577 -13.522 1.00 17.53  ? 162 MET   A N   1 
ATOM   1119 C CA  . MET   A 1 151 ? 5.418   16.673 -12.584 1.00 17.00  ? 162 MET   A CA  1 
ATOM   1120 C C   . MET   A 1 151 ? 4.555   16.723 -11.348 1.00 15.81  ? 162 MET   A C   1 
ATOM   1121 O O   . MET   A 1 151 ? 3.874   17.704 -11.119 1.00 14.78  ? 162 MET   A O   1 
ATOM   1122 C CB  . MET   A 1 151 ? 6.852   17.109 -12.269 1.00 18.27  ? 162 MET   A CB  1 
ATOM   1123 C CG  . MET   A 1 151 ? 7.777   17.132 -13.487 1.00 19.34  ? 162 MET   A CG  1 
ATOM   1124 S SD  . MET   A 1 151 ? 8.041   15.564 -14.354 1.00 21.00  ? 162 MET   A SD  1 
ATOM   1125 C CE  . MET   A 1 151 ? 8.685   14.401 -13.142 1.00 20.99  ? 162 MET   A CE  1 
ATOM   1126 N N   . GLY   A 1 152 ? 4.596   15.652 -10.571 1.00 16.80  ? 163 GLY   A N   1 
ATOM   1127 C CA  . GLY   A 1 152 ? 3.989   15.648 -9.252  1.00 17.19  ? 163 GLY   A CA  1 
ATOM   1128 C C   . GLY   A 1 152 ? 4.563   16.700 -8.303  1.00 16.38  ? 163 GLY   A C   1 
ATOM   1129 O O   . GLY   A 1 152 ? 5.518   17.407 -8.601  1.00 15.89  ? 163 GLY   A O   1 
ATOM   1130 N N   . ARG   A 1 153 ? 3.930   16.783 -7.137  1.00 17.25  ? 164 ARG   A N   1 
ATOM   1131 C CA  . ARG   A 1 153 ? 4.297   17.721 -6.093  1.00 18.53  ? 164 ARG   A CA  1 
ATOM   1132 C C   . ARG   A 1 153 ? 4.261   17.008 -4.737  1.00 17.02  ? 164 ARG   A C   1 
ATOM   1133 O O   . ARG   A 1 153 ? 4.084   17.614 -3.687  1.00 16.68  ? 164 ARG   A O   1 
ATOM   1134 C CB  . ARG   A 1 153 ? 3.383   18.951 -6.259  1.00 21.38  ? 164 ARG   A CB  1 
ATOM   1135 C CG  . ARG   A 1 153 ? 1.883   18.752 -6.064  1.00 23.41  ? 164 ARG   A CG  1 
ATOM   1136 C CD  . ARG   A 1 153 ? 1.002   19.950 -6.412  1.00 25.48  ? 164 ARG   A CD  1 
ATOM   1137 N NE  . ARG   A 1 153 ? 1.306   21.172 -5.660  1.00 29.42  ? 164 ARG   A NE  1 
ATOM   1138 C CZ  . ARG   A 1 153 ? 1.351   22.423 -6.146  1.00 34.08  ? 164 ARG   A CZ  1 
ATOM   1139 N NH1 . ARG   A 1 153 ? 1.441   23.450 -5.306  1.00 34.43  ? 164 ARG   A NH1 1 
ATOM   1140 N NH2 . ARG   A 1 153 ? 1.240   22.664 -7.451  1.00 34.51  ? 164 ARG   A NH2 1 
ATOM   1141 N N   . LEU   A 1 154 ? 4.467   15.698 -4.754  1.00 17.21  ? 165 LEU   A N   1 
ATOM   1142 C CA  . LEU   A 1 154 ? 4.307   14.897 -3.561  1.00 17.66  ? 165 LEU   A CA  1 
ATOM   1143 C C   . LEU   A 1 154 ? 5.470   13.930 -3.454  1.00 17.27  ? 165 LEU   A C   1 
ATOM   1144 O O   . LEU   A 1 154 ? 5.926   13.384 -4.455  1.00 15.46  ? 165 LEU   A O   1 
ATOM   1145 C CB  . LEU   A 1 154 ? 3.014   14.091 -3.617  1.00 18.51  ? 165 LEU   A CB  1 
ATOM   1146 C CG  . LEU   A 1 154 ? 1.710   14.880 -3.738  1.00 19.13  ? 165 LEU   A CG  1 
ATOM   1147 C CD1 . LEU   A 1 154 ? 0.535   13.929 -3.501  1.00 19.65  ? 165 LEU   A CD1 1 
ATOM   1148 C CD2 . LEU   A 1 154 ? 1.638   16.063 -2.798  1.00 19.35  ? 165 LEU   A CD2 1 
ATOM   1149 N N   . PRO   A 1 155 ? 5.918   13.647 -2.216  1.00 18.72  ? 166 PRO   A N   1 
ATOM   1150 C CA  . PRO   A 1 155 ? 6.780   12.507 -1.955  1.00 19.76  ? 166 PRO   A CA  1 
ATOM   1151 C C   . PRO   A 1 155 ? 6.484   11.370 -2.919  1.00 20.80  ? 166 PRO   A C   1 
ATOM   1152 O O   . PRO   A 1 155 ? 7.391   10.862 -3.571  1.00 22.81  ? 166 PRO   A O   1 
ATOM   1153 C CB  . PRO   A 1 155 ? 6.374   12.207 -0.511  1.00 19.92  ? 166 PRO   A CB  1 
ATOM   1154 C CG  . PRO   A 1 155 ? 6.295   13.580 0.102   1.00 19.73  ? 166 PRO   A CG  1 
ATOM   1155 C CD  . PRO   A 1 155 ? 5.641   14.422 -0.995  1.00 19.71  ? 166 PRO   A CD  1 
ATOM   1156 N N   . SER   A 1 156 ? 5.207   11.007 -3.041  1.00 21.25  ? 167 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 156 ? 4.834   9.818  -3.792  1.00 22.41  ? 167 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 156 ? 4.795   10.037 -5.316  1.00 24.21  ? 167 SER   A C   1 
ATOM   1159 O O   . SER   A 1 156 ? 4.508   9.094  -6.055  1.00 23.18  ? 167 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 156 ? 3.514   9.310  -3.281  1.00 21.84  ? 167 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 156 ? 2.553   10.351 -3.342  1.00 21.86  ? 167 SER   A OG  1 
ATOM   1162 N N   . THR   A 1 157 ? 5.065   11.262 -5.807  1.00 26.23  ? 168 THR   A N   1 
ATOM   1163 C CA  . THR   A 1 157 ? 4.761   11.600 -7.192  1.00 25.72  ? 168 THR   A CA  1 
ATOM   1164 C C   . THR   A 1 157 ? 5.807   12.516 -7.792  1.00 23.58  ? 168 THR   A C   1 
ATOM   1165 O O   . THR   A 1 157 ? 5.738   12.786 -8.976  1.00 21.30  ? 168 THR   A O   1 
ATOM   1166 C CB  . THR   A 1 157 ? 3.417   12.322 -7.307  1.00 26.63  ? 168 THR   A CB  1 
ATOM   1167 O OG1 . THR   A 1 157 ? 3.695   13.692 -7.030  1.00 26.28  ? 168 THR   A OG1 1 
ATOM   1168 C CG2 . THR   A 1 157 ? 2.342   11.778 -6.383  1.00 26.89  ? 168 THR   A CG2 1 
ATOM   1169 N N   . TYR   A 1 158 ? 6.718   13.038 -6.980  1.00 26.17  ? 169 TYR   A N   1 
ATOM   1170 C CA  . TYR   A 1 158 ? 7.514   14.181 -7.404  1.00 30.77  ? 169 TYR   A CA  1 
ATOM   1171 C C   . TYR   A 1 158 ? 8.387   13.824 -8.616  1.00 31.77  ? 169 TYR   A C   1 
ATOM   1172 O O   . TYR   A 1 158 ? 8.704   14.696 -9.425  1.00 27.71  ? 169 TYR   A O   1 
ATOM   1173 C CB  . TYR   A 1 158 ? 8.274   14.770 -6.207  1.00 31.20  ? 169 TYR   A CB  1 
ATOM   1174 C CG  . TYR   A 1 158 ? 9.561   14.087 -5.785  1.00 31.82  ? 169 TYR   A CG  1 
ATOM   1175 C CD1 . TYR   A 1 158 ? 9.559   12.953 -4.977  1.00 32.60  ? 169 TYR   A CD1 1 
ATOM   1176 C CD2 . TYR   A 1 158 ? 10.791  14.614 -6.161  1.00 34.74  ? 169 TYR   A CD2 1 
ATOM   1177 C CE1 . TYR   A 1 158 ? 10.747  12.343 -4.590  1.00 33.90  ? 169 TYR   A CE1 1 
ATOM   1178 C CE2 . TYR   A 1 158 ? 11.986  14.013 -5.782  1.00 34.86  ? 169 TYR   A CE2 1 
ATOM   1179 C CZ  . TYR   A 1 158 ? 11.963  12.876 -4.996  1.00 33.41  ? 169 TYR   A CZ  1 
ATOM   1180 O OH  . TYR   A 1 158 ? 13.160  12.336 -4.658  1.00 32.16  ? 169 TYR   A OH  1 
ATOM   1181 N N   . ARG   A 1 159 ? 8.725   12.541 -8.786  1.00 34.72  ? 170 ARG   A N   1 
ATOM   1182 C CA  . ARG   A 1 159 ? 9.442   12.101 -9.974  1.00 40.69  ? 170 ARG   A CA  1 
ATOM   1183 C C   . ARG   A 1 159 ? 8.490   11.490 -11.013 1.00 41.41  ? 170 ARG   A C   1 
ATOM   1184 O O   . ARG   A 1 159 ? 8.933   10.680 -11.836 1.00 37.13  ? 170 ARG   A O   1 
ATOM   1185 C CB  . ARG   A 1 159 ? 10.548  11.123 -9.547  1.00 46.92  ? 170 ARG   A CB  1 
ATOM   1186 C CG  . ARG   A 1 159 ? 11.790  11.769 -8.938  1.00 48.78  ? 170 ARG   A CG  1 
ATOM   1187 C CD  . ARG   A 1 159 ? 12.624  10.819 -8.073  1.00 52.29  ? 170 ARG   A CD  1 
ATOM   1188 N NE  . ARG   A 1 159 ? 13.462  9.848  -8.792  1.00 54.17  ? 170 ARG   A NE  1 
ATOM   1189 C CZ  . ARG   A 1 159 ? 14.596  10.109 -9.444  1.00 53.68  ? 170 ARG   A CZ  1 
ATOM   1190 N NH1 . ARG   A 1 159 ? 15.031  11.352 -9.607  1.00 51.46  ? 170 ARG   A NH1 1 
ATOM   1191 N NH2 . ARG   A 1 159 ? 15.286  9.104  -9.946  1.00 53.59  ? 170 ARG   A NH2 1 
ATOM   1192 N N   . LYS   A 1 160 ? 7.200   11.900 -10.986 1.00 40.76  ? 171 LYS   A N   1 
ATOM   1193 C CA  . LYS   A 1 160 ? 6.177   11.391 -11.893 1.00 37.33  ? 171 LYS   A CA  1 
ATOM   1194 C C   . LYS   A 1 160 ? 5.676   12.524 -12.785 1.00 30.59  ? 171 LYS   A C   1 
ATOM   1195 O O   . LYS   A 1 160 ? 5.314   13.598 -12.311 1.00 26.48  ? 171 LYS   A O   1 
ATOM   1196 C CB  . LYS   A 1 160 ? 5.004   10.698 -11.184 1.00 41.26  ? 171 LYS   A CB  1 
ATOM   1197 C CG  . LYS   A 1 160 ? 5.388   9.365  -10.567 1.00 46.49  ? 171 LYS   A CG  1 
ATOM   1198 C CD  . LYS   A 1 160 ? 4.242   8.509  -10.046 1.00 51.05  ? 171 LYS   A CD  1 
ATOM   1199 C CE  . LYS   A 1 160 ? 4.725   7.124  -9.684  1.00 55.25  ? 171 LYS   A CE  1 
ATOM   1200 N NZ  . LYS   A 1 160 ? 3.652   6.201  -9.285  1.00 56.68  ? 171 LYS   A NZ  1 
ATOM   1201 N N   . CYS   A 1 161 ? 5.685   12.231 -14.087 1.00 26.90  ? 172 CYS   A N   1 
ATOM   1202 C CA  . CYS   A 1 161 ? 5.228   13.116 -15.137 1.00 24.76  ? 172 CYS   A CA  1 
ATOM   1203 C C   . CYS   A 1 161 ? 3.806   12.696 -15.501 1.00 28.32  ? 172 CYS   A C   1 
ATOM   1204 O O   . CYS   A 1 161 ? 3.536   11.503 -15.678 1.00 30.81  ? 172 CYS   A O   1 
ATOM   1205 C CB  . CYS   A 1 161 ? 6.232   13.048 -16.280 1.00 22.88  ? 172 CYS   A CB  1 
ATOM   1206 S SG  . CYS   A 1 161 ? 5.574   13.391 -17.931 1.00 20.09  ? 172 CYS   A SG  1 
ATOM   1207 N N   . TYR   A 1 162 ? 2.908   13.691 -15.594 1.00 29.93  ? 173 TYR   A N   1 
ATOM   1208 C CA  . TYR   A 1 162 ? 1.482   13.485 -15.801 1.00 30.02  ? 173 TYR   A CA  1 
ATOM   1209 C C   . TYR   A 1 162 ? 0.998   14.084 -17.124 1.00 30.12  ? 173 TYR   A C   1 
ATOM   1210 O O   . TYR   A 1 162 ? 1.694   14.885 -17.750 1.00 27.39  ? 173 TYR   A O   1 
ATOM   1211 C CB  . TYR   A 1 162 ? 0.701   14.155 -14.667 1.00 30.34  ? 173 TYR   A CB  1 
ATOM   1212 C CG  . TYR   A 1 162 ? 0.850   13.411 -13.357 1.00 31.15  ? 173 TYR   A CG  1 
ATOM   1213 C CD1 . TYR   A 1 162 ? 0.119   12.256 -13.122 1.00 32.13  ? 173 TYR   A CD1 1 
ATOM   1214 C CD2 . TYR   A 1 162 ? 1.744   13.832 -12.383 1.00 31.97  ? 173 TYR   A CD2 1 
ATOM   1215 C CE1 . TYR   A 1 162 ? 0.256   11.545 -11.942 1.00 32.66  ? 173 TYR   A CE1 1 
ATOM   1216 C CE2 . TYR   A 1 162 ? 1.882   13.138 -11.191 1.00 32.67  ? 173 TYR   A CE2 1 
ATOM   1217 C CZ  . TYR   A 1 162 ? 1.135   11.992 -10.972 1.00 33.26  ? 173 TYR   A CZ  1 
ATOM   1218 O OH  . TYR   A 1 162 ? 1.254   11.273 -9.820  1.00 34.83  ? 173 TYR   A OH  1 
ATOM   1219 N N   . MET   A 1 163 ? -0.235  13.695 -17.490 1.00 30.11  ? 174 MET   A N   1 
ATOM   1220 C CA  A MET   A 1 163 ? -0.914  14.175 -18.680 0.50 30.06  ? 174 MET   A CA  1 
ATOM   1221 C CA  B MET   A 1 163 ? -0.907  14.181 -18.681 0.50 30.21  ? 174 MET   A CA  1 
ATOM   1222 C C   . MET   A 1 163 ? -2.062  15.082 -18.257 1.00 30.95  ? 174 MET   A C   1 
ATOM   1223 O O   . MET   A 1 163 ? -2.860  14.714 -17.403 1.00 35.17  ? 174 MET   A O   1 
ATOM   1224 C CB  A MET   A 1 163 ? -1.478  13.009 -19.504 0.50 29.82  ? 174 MET   A CB  1 
ATOM   1225 C CB  B MET   A 1 163 ? -1.430  13.011 -19.524 0.50 30.21  ? 174 MET   A CB  1 
ATOM   1226 C CG  A MET   A 1 163 ? -2.430  13.429 -20.618 0.50 29.47  ? 174 MET   A CG  1 
ATOM   1227 C CG  B MET   A 1 163 ? -2.066  13.415 -20.847 0.50 30.03  ? 174 MET   A CG  1 
ATOM   1228 S SD  A MET   A 1 163 ? -2.809  12.108 -21.789 0.50 27.73  ? 174 MET   A SD  1 
ATOM   1229 S SD  B MET   A 1 163 ? -2.207  12.043 -22.014 0.50 28.59  ? 174 MET   A SD  1 
ATOM   1230 C CE  A MET   A 1 163 ? -1.278  12.015 -22.727 0.50 27.63  ? 174 MET   A CE  1 
ATOM   1231 C CE  B MET   A 1 163 ? -2.994  10.759 -21.032 0.50 28.35  ? 174 MET   A CE  1 
ATOM   1232 N N   . LEU   A 1 164 ? -2.142  16.257 -18.887 1.00 32.96  ? 175 LEU   A N   1 
ATOM   1233 C CA  . LEU   A 1 164 ? -3.180  17.239 -18.627 1.00 32.62  ? 175 LEU   A CA  1 
ATOM   1234 C C   . LEU   A 1 164 ? -3.968  17.488 -19.911 1.00 36.53  ? 175 LEU   A C   1 
ATOM   1235 O O   . LEU   A 1 164 ? -3.494  17.196 -21.016 1.00 33.45  ? 175 LEU   A O   1 
ATOM   1236 C CB  . LEU   A 1 164 ? -2.463  18.499 -18.158 1.00 31.26  ? 175 LEU   A CB  1 
ATOM   1237 C CG  . LEU   A 1 164 ? -1.305  18.251 -17.190 1.00 30.71  ? 175 LEU   A CG  1 
ATOM   1238 C CD1 . LEU   A 1 164 ? -0.398  19.447 -16.969 1.00 29.84  ? 175 LEU   A CD1 1 
ATOM   1239 C CD2 . LEU   A 1 164 ? -1.918  17.770 -15.906 1.00 30.20  ? 175 LEU   A CD2 1 
ATOM   1240 N N   . ASP   A 1 165 ? -5.166  18.058 -19.723 1.00 42.72  ? 176 ASP   A N   1 
ATOM   1241 C CA  . ASP   A 1 165 ? -6.078  18.434 -20.793 1.00 43.95  ? 176 ASP   A CA  1 
ATOM   1242 C C   . ASP   A 1 165 ? -6.519  17.187 -21.545 1.00 42.13  ? 176 ASP   A C   1 
ATOM   1243 O O   . ASP   A 1 165 ? -5.688  16.377 -21.952 1.00 43.13  ? 176 ASP   A O   1 
ATOM   1244 C CB  . ASP   A 1 165 ? -5.476  19.417 -21.788 1.00 46.06  ? 176 ASP   A CB  1 
ATOM   1245 C CG  . ASP   A 1 165 ? -6.459  20.332 -22.514 1.00 46.65  ? 176 ASP   A CG  1 
ATOM   1246 O OD1 . ASP   A 1 165 ? -7.291  20.961 -21.828 1.00 41.25  ? 176 ASP   A OD1 1 
ATOM   1247 O OD2 . ASP   A 1 165 ? -6.344  20.461 -23.758 1.00 51.03  ? 176 ASP   A OD2 1 
ATOM   1248 N N   . PHE   A 1 166 ? -7.839  17.053 -21.693 1.00 39.42  ? 177 PHE   A N   1 
ATOM   1249 C CA  . PHE   A 1 166 ? -8.437  16.201 -22.702 1.00 36.92  ? 177 PHE   A CA  1 
ATOM   1250 C C   . PHE   A 1 166 ? -9.405  17.050 -23.512 1.00 32.23  ? 177 PHE   A C   1 
ATOM   1251 O O   . PHE   A 1 166 ? -10.276 16.527 -24.194 1.00 31.44  ? 177 PHE   A O   1 
ATOM   1252 C CB  . PHE   A 1 166 ? -9.117  15.000 -22.043 1.00 38.81  ? 177 PHE   A CB  1 
ATOM   1253 C CG  . PHE   A 1 166 ? -8.259  14.296 -21.000 1.00 41.00  ? 177 PHE   A CG  1 
ATOM   1254 C CD1 . PHE   A 1 166 ? -7.207  13.471 -21.383 1.00 41.38  ? 177 PHE   A CD1 1 
ATOM   1255 C CD2 . PHE   A 1 166 ? -8.516  14.445 -19.642 1.00 41.00  ? 177 PHE   A CD2 1 
ATOM   1256 C CE1 . PHE   A 1 166 ? -6.427  12.828 -20.433 1.00 39.34  ? 177 PHE   A CE1 1 
ATOM   1257 C CE2 . PHE   A 1 166 ? -7.744  13.784 -18.703 1.00 40.37  ? 177 PHE   A CE2 1 
ATOM   1258 C CZ  . PHE   A 1 166 ? -6.694  12.986 -19.099 1.00 38.75  ? 177 PHE   A CZ  1 
ATOM   1259 N N   . GLY   A 1 167 ? -9.238  18.367 -23.419 1.00 29.86  ? 178 GLY   A N   1 
ATOM   1260 C CA  . GLY   A 1 167 ? -10.081 19.277 -24.160 1.00 30.22  ? 178 GLY   A CA  1 
ATOM   1261 C C   . GLY   A 1 167 ? -10.208 18.827 -25.610 1.00 30.94  ? 178 GLY   A C   1 
ATOM   1262 O O   . GLY   A 1 167 ? -11.309 18.637 -26.112 1.00 35.47  ? 178 GLY   A O   1 
ATOM   1263 N N   . LEU   A 1 168 ? -9.083  18.628 -26.295 1.00 29.26  ? 179 LEU   A N   1 
ATOM   1264 C CA  . LEU   A 1 168 ? -9.170  18.459 -27.735 1.00 27.63  ? 179 LEU   A CA  1 
ATOM   1265 C C   . LEU   A 1 168 ? -9.334  16.985 -28.090 1.00 23.55  ? 179 LEU   A C   1 
ATOM   1266 O O   . LEU   A 1 168 ? -9.373  16.631 -29.261 1.00 20.07  ? 179 LEU   A O   1 
ATOM   1267 C CB  . LEU   A 1 168 ? -7.951  19.108 -28.386 1.00 28.78  ? 179 LEU   A CB  1 
ATOM   1268 C CG  . LEU   A 1 168 ? -7.920  20.640 -28.332 1.00 28.49  ? 179 LEU   A CG  1 
ATOM   1269 C CD1 . LEU   A 1 168 ? -6.670  21.145 -28.998 1.00 28.50  ? 179 LEU   A CD1 1 
ATOM   1270 C CD2 . LEU   A 1 168 ? -9.129  21.279 -28.980 1.00 28.56  ? 179 LEU   A CD2 1 
ATOM   1271 N N   . ALA   A 1 169 ? -9.513  16.148 -27.070 1.00 22.92  ? 180 ALA   A N   1 
ATOM   1272 C CA  . ALA   A 1 169 ? -9.586  14.710 -27.264 1.00 24.39  ? 180 ALA   A CA  1 
ATOM   1273 C C   . ALA   A 1 169 ? -10.776 14.311 -28.134 1.00 24.76  ? 180 ALA   A C   1 
ATOM   1274 O O   . ALA   A 1 169 ? -11.800 14.988 -28.141 1.00 26.34  ? 180 ALA   A O   1 
ATOM   1275 C CB  . ALA   A 1 169 ? -9.668  14.020 -25.924 1.00 24.60  ? 180 ALA   A CB  1 
ATOM   1276 N N   . ARG   A 1 170 ? -10.633 13.173 -28.830 1.00 24.03  ? 181 ARG   A N   1 
ATOM   1277 C CA  . ARG   A 1 170 ? -11.667 12.631 -29.697 1.00 24.00  ? 181 ARG   A CA  1 
ATOM   1278 C C   . ARG   A 1 170 ? -11.620 11.121 -29.583 1.00 23.64  ? 181 ARG   A C   1 
ATOM   1279 O O   . ARG   A 1 170 ? -10.547 10.547 -29.489 1.00 23.86  ? 181 ARG   A O   1 
ATOM   1280 C CB  . ARG   A 1 170 ? -11.512 13.040 -31.168 1.00 24.67  ? 181 ARG   A CB  1 
ATOM   1281 C CG  . ARG   A 1 170 ? -11.396 11.918 -32.187 1.00 26.49  ? 181 ARG   A CG  1 
ATOM   1282 C CD  . ARG   A 1 170 ? -11.474 12.411 -33.610 1.00 27.59  ? 181 ARG   A CD  1 
ATOM   1283 N NE  . ARG   A 1 170 ? -12.688 11.959 -34.286 1.00 29.03  ? 181 ARG   A NE  1 
ATOM   1284 C CZ  . ARG   A 1 170 ? -13.791 12.676 -34.410 1.00 31.07  ? 181 ARG   A CZ  1 
ATOM   1285 N NH1 . ARG   A 1 170 ? -14.183 13.498 -33.453 1.00 31.43  ? 181 ARG   A NH1 1 
ATOM   1286 N NH2 . ARG   A 1 170 ? -14.527 12.533 -35.495 1.00 32.93  ? 181 ARG   A NH2 1 
ATOM   1287 N N   . GLN   A 1 171 ? -12.784 10.490 -29.600 1.00 24.83  ? 182 GLN   A N   1 
ATOM   1288 C CA  . GLN   A 1 171 ? -12.824 9.047  -29.608 1.00 27.10  ? 182 GLN   A CA  1 
ATOM   1289 C C   . GLN   A 1 171 ? -12.611 8.535  -31.031 1.00 29.06  ? 182 GLN   A C   1 
ATOM   1290 O O   . GLN   A 1 171 ? -13.207 9.045  -31.978 1.00 26.76  ? 182 GLN   A O   1 
ATOM   1291 C CB  . GLN   A 1 171 ? -14.178 8.639  -29.051 1.00 28.50  ? 182 GLN   A CB  1 
ATOM   1292 C CG  . GLN   A 1 171 ? -14.279 7.144  -28.789 1.00 30.17  ? 182 GLN   A CG  1 
ATOM   1293 C CD  . GLN   A 1 171 ? -15.640 6.749  -28.277 1.00 30.78  ? 182 GLN   A CD  1 
ATOM   1294 O OE1 . GLN   A 1 171 ? -16.111 7.284  -27.270 1.00 30.25  ? 182 GLN   A OE1 1 
ATOM   1295 N NE2 . GLN   A 1 171 ? -16.283 5.827  -28.980 1.00 32.74  ? 182 GLN   A NE2 1 
ATOM   1296 N N   . TYR   A 1 172 ? -11.776 7.500  -31.178 1.00 33.46  ? 183 TYR   A N   1 
ATOM   1297 C CA  . TYR   A 1 172 ? -11.566 6.912  -32.495 1.00 41.02  ? 183 TYR   A CA  1 
ATOM   1298 C C   . TYR   A 1 172 ? -12.236 5.544  -32.626 1.00 40.96  ? 183 TYR   A C   1 
ATOM   1299 O O   . TYR   A 1 172 ? -12.383 5.052  -33.744 1.00 41.26  ? 183 TYR   A O   1 
ATOM   1300 C CB  . TYR   A 1 172 ? -10.089 6.793  -32.870 1.00 46.46  ? 183 TYR   A CB  1 
ATOM   1301 C CG  . TYR   A 1 172 ? -9.252  5.877  -31.992 1.00 51.46  ? 183 TYR   A CG  1 
ATOM   1302 C CD1 . TYR   A 1 172 ? -8.749  6.323  -30.774 1.00 54.50  ? 183 TYR   A CD1 1 
ATOM   1303 C CD2 . TYR   A 1 172 ? -8.928  4.587  -32.398 1.00 53.96  ? 183 TYR   A CD2 1 
ATOM   1304 C CE1 . TYR   A 1 172 ? -7.965  5.506  -29.972 1.00 56.08  ? 183 TYR   A CE1 1 
ATOM   1305 C CE2 . TYR   A 1 172 ? -8.141  3.762  -31.606 1.00 56.14  ? 183 TYR   A CE2 1 
ATOM   1306 C CZ  . TYR   A 1 172 ? -7.662  4.219  -30.386 1.00 57.10  ? 183 TYR   A CZ  1 
ATOM   1307 O OH  . TYR   A 1 172 ? -6.881  3.417  -29.597 1.00 58.51  ? 183 TYR   A OH  1 
ATOM   1308 N N   . THR   A 1 173 ? -12.636 4.934  -31.508 1.00 41.44  ? 184 THR   A N   1 
ATOM   1309 C CA  . THR   A 1 173 ? -13.351 3.672  -31.567 1.00 42.78  ? 184 THR   A CA  1 
ATOM   1310 C C   . THR   A 1 173 ? -14.850 3.944  -31.535 1.00 47.66  ? 184 THR   A C   1 
ATOM   1311 O O   . THR   A 1 173 ? -15.296 5.086  -31.702 1.00 46.76  ? 184 THR   A O   1 
ATOM   1312 C CB  . THR   A 1 173 ? -12.950 2.762  -30.410 1.00 42.05  ? 184 THR   A CB  1 
ATOM   1313 O OG1 . THR   A 1 173 ? -13.500 3.452  -29.293 1.00 41.12  ? 184 THR   A OG1 1 
ATOM   1314 C CG2 . THR   A 1 173 ? -11.451 2.543  -30.313 1.00 43.60  ? 184 THR   A CG2 1 
ATOM   1315 N N   . ASN   A 1 174 ? -15.595 2.847  -31.325 1.00 50.55  ? 185 ASN   A N   1 
ATOM   1316 C CA  . ASN   A 1 174 ? -17.030 2.850  -31.098 1.00 48.24  ? 185 ASN   A CA  1 
ATOM   1317 C C   . ASN   A 1 174 ? -17.320 2.044  -29.826 1.00 51.05  ? 185 ASN   A C   1 
ATOM   1318 O O   . ASN   A 1 174 ? -16.404 1.519  -29.194 1.00 46.38  ? 185 ASN   A O   1 
ATOM   1319 C CB  . ASN   A 1 174 ? -17.751 2.325  -32.333 1.00 44.08  ? 185 ASN   A CB  1 
ATOM   1320 C CG  . ASN   A 1 174 ? -17.773 0.816  -32.370 1.00 43.36  ? 185 ASN   A CG  1 
ATOM   1321 O OD1 . ASN   A 1 174 ? -16.795 0.177  -32.775 1.00 42.33  ? 185 ASN   A OD1 1 
ATOM   1322 N ND2 . ASN   A 1 174 ? -18.891 0.233  -31.969 1.00 44.97  ? 185 ASN   A ND2 1 
ATOM   1323 N N   . THR   A 1 175 ? -18.602 1.961  -29.452 1.00 59.58  ? 186 THR   A N   1 
ATOM   1324 C CA  . THR   A 1 175 ? -19.048 1.300  -28.230 1.00 65.52  ? 186 THR   A CA  1 
ATOM   1325 C C   . THR   A 1 175 ? -18.332 -0.034 -28.021 1.00 65.96  ? 186 THR   A C   1 
ATOM   1326 O O   . THR   A 1 175 ? -17.893 -0.324 -26.909 1.00 65.29  ? 186 THR   A O   1 
ATOM   1327 C CB  . THR   A 1 175 ? -20.558 1.088  -28.302 1.00 69.42  ? 186 THR   A CB  1 
ATOM   1328 O OG1 . THR   A 1 175 ? -20.743 0.528  -29.601 1.00 78.15  ? 186 THR   A OG1 1 
ATOM   1329 C CG2 . THR   A 1 175 ? -21.355 2.370  -28.121 1.00 66.86  ? 186 THR   A CG2 1 
ATOM   1330 N N   . THR   A 1 176 ? -18.267 -0.845 -29.083 1.00 67.77  ? 187 THR   A N   1 
ATOM   1331 C CA  . THR   A 1 176 ? -17.575 -2.122 -29.053 1.00 62.30  ? 187 THR   A CA  1 
ATOM   1332 C C   . THR   A 1 176 ? -16.077 -1.849 -28.981 1.00 55.23  ? 187 THR   A C   1 
ATOM   1333 O O   . THR   A 1 176 ? -15.532 -1.747 -27.885 1.00 53.20  ? 187 THR   A O   1 
ATOM   1334 C CB  . THR   A 1 176 ? -17.961 -2.952 -30.278 1.00 62.27  ? 187 THR   A CB  1 
ATOM   1335 O OG1 . THR   A 1 176 ? -17.475 -2.232 -31.408 1.00 68.39  ? 187 THR   A OG1 1 
ATOM   1336 C CG2 . THR   A 1 176 ? -19.464 -3.145 -30.376 1.00 59.17  ? 187 THR   A CG2 1 
ATOM   1337 N N   . GLY   A 1 177 ? -15.435 -1.705 -30.145 1.00 46.07  ? 188 GLY   A N   1 
ATOM   1338 C CA  . GLY   A 1 177 ? -14.001 -1.484 -30.177 1.00 43.23  ? 188 GLY   A CA  1 
ATOM   1339 C C   . GLY   A 1 177 ? -13.473 -1.463 -31.602 1.00 42.69  ? 188 GLY   A C   1 
ATOM   1340 O O   . GLY   A 1 177 ? -12.354 -1.890 -31.839 1.00 44.06  ? 188 GLY   A O   1 
ATOM   1341 N N   . ASP   A 1 178 ? -14.283 -0.961 -32.539 1.00 42.70  ? 189 ASP   A N   1 
ATOM   1342 C CA  . ASP   A 1 178 ? -13.870 -0.850 -33.930 1.00 39.10  ? 189 ASP   A CA  1 
ATOM   1343 C C   . ASP   A 1 178 ? -13.369 0.574  -34.162 1.00 33.95  ? 189 ASP   A C   1 
ATOM   1344 O O   . ASP   A 1 178 ? -13.620 1.455  -33.354 1.00 30.22  ? 189 ASP   A O   1 
ATOM   1345 C CB  . ASP   A 1 178 ? -15.000 -1.230 -34.878 1.00 40.24  ? 189 ASP   A CB  1 
ATOM   1346 C CG  . ASP   A 1 178 ? -15.803 -2.467 -34.506 1.00 42.77  ? 189 ASP   A CG  1 
ATOM   1347 O OD1 . ASP   A 1 178 ? -15.197 -3.560 -34.484 1.00 46.88  ? 189 ASP   A OD1 1 
ATOM   1348 O OD2 . ASP   A 1 178 ? -17.030 -2.331 -34.260 1.00 41.42  ? 189 ASP   A OD2 1 
ATOM   1349 N N   . VAL   A 1 179 ? -12.686 0.800  -35.278 1.00 31.81  ? 190 VAL   A N   1 
ATOM   1350 C CA  . VAL   A 1 179 ? -12.140 2.107  -35.566 1.00 32.34  ? 190 VAL   A CA  1 
ATOM   1351 C C   . VAL   A 1 179 ? -13.217 2.898  -36.289 1.00 29.65  ? 190 VAL   A C   1 
ATOM   1352 O O   . VAL   A 1 179 ? -13.651 2.479  -37.358 1.00 27.28  ? 190 VAL   A O   1 
ATOM   1353 C CB  . VAL   A 1 179 ? -10.851 2.003  -36.409 1.00 35.36  ? 190 VAL   A CB  1 
ATOM   1354 C CG1 . VAL   A 1 179 ? -10.256 3.371  -36.758 1.00 36.06  ? 190 VAL   A CG1 1 
ATOM   1355 C CG2 . VAL   A 1 179 ? -9.808  1.125  -35.728 1.00 34.52  ? 190 VAL   A CG2 1 
ATOM   1356 N N   . ARG   A 1 180 ? -13.616 4.027  -35.684 1.00 29.24  ? 191 ARG   A N   1 
ATOM   1357 C CA  . ARG   A 1 180 ? -14.541 4.962  -36.303 1.00 29.35  ? 191 ARG   A CA  1 
ATOM   1358 C C   . ARG   A 1 180 ? -13.961 5.331  -37.667 1.00 27.46  ? 191 ARG   A C   1 
ATOM   1359 O O   . ARG   A 1 180 ? -12.738 5.421  -37.804 1.00 26.22  ? 191 ARG   A O   1 
ATOM   1360 C CB  . ARG   A 1 180 ? -14.812 6.202  -35.432 1.00 31.21  ? 191 ARG   A CB  1 
ATOM   1361 C CG  . ARG   A 1 180 ? -13.949 7.420  -35.765 1.00 35.42  ? 191 ARG   A CG  1 
ATOM   1362 C CD  . ARG   A 1 180 ? -14.196 8.656  -34.909 1.00 36.86  ? 191 ARG   A CD  1 
ATOM   1363 N NE  . ARG   A 1 180 ? -15.622 9.017  -34.914 1.00 37.08  ? 191 ARG   A NE  1 
ATOM   1364 C CZ  . ARG   A 1 180 ? -16.269 9.712  -33.977 1.00 34.09  ? 191 ARG   A CZ  1 
ATOM   1365 N NH1 . ARG   A 1 180 ? -15.658 10.133 -32.877 1.00 35.19  ? 191 ARG   A NH1 1 
ATOM   1366 N NH2 . ARG   A 1 180 ? -17.548 9.965  -34.145 1.00 31.97  ? 191 ARG   A NH2 1 
ATOM   1367 N N   . PRO   A 1 181 ? -14.794 5.551  -38.711 1.00 25.55  ? 192 PRO   A N   1 
ATOM   1368 C CA  . PRO   A 1 181 ? -14.299 5.966  -40.014 1.00 26.28  ? 192 PRO   A CA  1 
ATOM   1369 C C   . PRO   A 1 181 ? -13.827 7.412  -39.943 1.00 27.14  ? 192 PRO   A C   1 
ATOM   1370 O O   . PRO   A 1 181 ? -14.317 8.251  -39.188 1.00 26.74  ? 192 PRO   A O   1 
ATOM   1371 C CB  . PRO   A 1 181 ? -15.440 5.785  -41.014 1.00 25.69  ? 192 PRO   A CB  1 
ATOM   1372 C CG  . PRO   A 1 181 ? -16.553 5.168  -40.202 1.00 26.00  ? 192 PRO   A CG  1 
ATOM   1373 C CD  . PRO   A 1 181 ? -16.254 5.431  -38.724 1.00 26.06  ? 192 PRO   A CD  1 
ATOM   1374 N N   . PRO   A 1 182 ? -12.824 7.733  -40.762 1.00 27.51  ? 193 PRO   A N   1 
ATOM   1375 C CA  . PRO   A 1 182 ? -12.172 9.028  -40.671 1.00 26.66  ? 193 PRO   A CA  1 
ATOM   1376 C C   . PRO   A 1 182 ? -13.077 9.966  -41.442 1.00 26.43  ? 193 PRO   A C   1 
ATOM   1377 O O   . PRO   A 1 182 ? -13.782 9.496  -42.333 1.00 26.90  ? 193 PRO   A O   1 
ATOM   1378 C CB  . PRO   A 1 182 ? -10.839 8.772  -41.359 1.00 27.50  ? 193 PRO   A CB  1 
ATOM   1379 C CG  . PRO   A 1 182 ? -11.148 7.691  -42.382 1.00 28.68  ? 193 PRO   A CG  1 
ATOM   1380 C CD  . PRO   A 1 182 ? -12.312 6.877  -41.843 1.00 28.06  ? 193 PRO   A CD  1 
ATOM   1381 N N   . ARG   A 1 183 ? -13.048 11.260 -41.081 1.00 24.86  ? 194 ARG   A N   1 
ATOM   1382 C CA  . ARG   A 1 183 ? -13.662 12.298 -41.886 1.00 21.97  ? 194 ARG   A CA  1 
ATOM   1383 C C   . ARG   A 1 183 ? -12.783 12.520 -43.098 1.00 21.62  ? 194 ARG   A C   1 
ATOM   1384 O O   . ARG   A 1 183 ? -11.571 12.360 -43.023 1.00 20.14  ? 194 ARG   A O   1 
ATOM   1385 C CB  . ARG   A 1 183 ? -13.828 13.614 -41.130 1.00 21.06  ? 194 ARG   A CB  1 
ATOM   1386 C CG  . ARG   A 1 183 ? -14.842 13.408 -40.023 1.00 21.53  ? 194 ARG   A CG  1 
ATOM   1387 C CD  . ARG   A 1 183 ? -14.846 14.473 -38.956 1.00 22.50  ? 194 ARG   A CD  1 
ATOM   1388 N NE  . ARG   A 1 183 ? -13.684 14.505 -38.063 1.00 22.29  ? 194 ARG   A NE  1 
ATOM   1389 C CZ  . ARG   A 1 183 ? -13.516 15.467 -37.171 1.00 22.05  ? 194 ARG   A CZ  1 
ATOM   1390 N NH1 . ARG   A 1 183 ? -14.516 16.266 -36.887 1.00 22.36  ? 194 ARG   A NH1 1 
ATOM   1391 N NH2 . ARG   A 1 183 ? -12.375 15.637 -36.538 1.00 23.32  ? 194 ARG   A NH2 1 
ATOM   1392 N N   . ASN   A 1 184 ? -13.432 12.893 -44.196 1.00 23.19  ? 195 ASN   A N   1 
ATOM   1393 C CA  . ASN   A 1 184 ? -12.737 13.274 -45.404 1.00 24.88  ? 195 ASN   A CA  1 
ATOM   1394 C C   . ASN   A 1 184 ? -11.994 14.599 -45.182 1.00 24.33  ? 195 ASN   A C   1 
ATOM   1395 O O   . ASN   A 1 184 ? -10.991 14.855 -45.844 1.00 26.06  ? 195 ASN   A O   1 
ATOM   1396 C CB  . ASN   A 1 184 ? -13.701 13.274 -46.583 1.00 27.54  ? 195 ASN   A CB  1 
ATOM   1397 C CG  . ASN   A 1 184 ? -12.940 13.179 -47.880 1.00 32.09  ? 195 ASN   A CG  1 
ATOM   1398 O OD1 . ASN   A 1 184 ? -12.682 14.201 -48.533 1.00 35.40  ? 195 ASN   A OD1 1 
ATOM   1399 N ND2 . ASN   A 1 184 ? -12.499 11.977 -48.221 1.00 33.65  ? 195 ASN   A ND2 1 
ATOM   1400 N N   . VAL   A 1 185 ? -12.454 15.444 -44.246 1.00 22.74  ? 196 VAL   A N   1 
ATOM   1401 C CA  . VAL   A 1 185 ? -11.636 16.542 -43.738 1.00 21.54  ? 196 VAL   A CA  1 
ATOM   1402 C C   . VAL   A 1 185 ? -11.872 16.691 -42.236 1.00 21.07  ? 196 VAL   A C   1 
ATOM   1403 O O   . VAL   A 1 185 ? -12.913 16.307 -41.699 1.00 21.15  ? 196 VAL   A O   1 
ATOM   1404 C CB  . VAL   A 1 185 ? -11.902 17.862 -44.488 1.00 21.69  ? 196 VAL   A CB  1 
ATOM   1405 C CG1 . VAL   A 1 185 ? -11.243 19.062 -43.825 1.00 21.33  ? 196 VAL   A CG1 1 
ATOM   1406 C CG2 . VAL   A 1 185 ? -11.451 17.765 -45.940 1.00 21.77  ? 196 VAL   A CG2 1 
ATOM   1407 N N   . ALA   A 1 186 ? -10.873 17.239 -41.549 1.00 21.69  ? 197 ALA   A N   1 
ATOM   1408 C CA  . ALA   A 1 186 ? -11.002 17.567 -40.136 1.00 23.71  ? 197 ALA   A CA  1 
ATOM   1409 C C   . ALA   A 1 186 ? -9.895  18.541 -39.741 1.00 25.44  ? 197 ALA   A C   1 
ATOM   1410 O O   . ALA   A 1 186 ? -8.708  18.171 -39.719 1.00 24.79  ? 197 ALA   A O   1 
ATOM   1411 C CB  . ALA   A 1 186 ? -10.985 16.322 -39.275 1.00 23.41  ? 197 ALA   A CB  1 
ATOM   1412 N N   . GLY   A 1 187 ? -10.341 19.769 -39.412 1.00 26.88  ? 198 GLY   A N   1 
ATOM   1413 C CA  . GLY   A 1 187 ? -9.506  20.962 -39.368 1.00 29.22  ? 198 GLY   A CA  1 
ATOM   1414 C C   . GLY   A 1 187 ? -8.664  21.048 -38.096 1.00 31.57  ? 198 GLY   A C   1 
ATOM   1415 O O   . GLY   A 1 187 ? -9.202  21.100 -36.989 1.00 32.15  ? 198 GLY   A O   1 
ATOM   1416 N N   . PHE   A 1 188 ? -7.336  21.083 -38.260 1.00 32.31  ? 199 PHE   A N   1 
ATOM   1417 C CA  . PHE   A 1 188 ? -6.465  21.030 -37.110 1.00 36.76  ? 199 PHE   A CA  1 
ATOM   1418 C C   . PHE   A 1 188 ? -6.886  22.135 -36.160 1.00 39.10  ? 199 PHE   A C   1 
ATOM   1419 O O   . PHE   A 1 188 ? -7.135  23.257 -36.608 1.00 43.48  ? 199 PHE   A O   1 
ATOM   1420 C CB  . PHE   A 1 188 ? -5.003  21.253 -37.481 1.00 44.30  ? 199 PHE   A CB  1 
ATOM   1421 C CG  . PHE   A 1 188 ? -4.037  21.102 -36.318 1.00 50.16  ? 199 PHE   A CG  1 
ATOM   1422 C CD1 . PHE   A 1 188 ? -4.159  20.037 -35.427 1.00 53.47  ? 199 PHE   A CD1 1 
ATOM   1423 C CD2 . PHE   A 1 188 ? -3.019  22.025 -36.130 1.00 52.98  ? 199 PHE   A CD2 1 
ATOM   1424 C CE1 . PHE   A 1 188 ? -3.274  19.892 -34.374 1.00 58.59  ? 199 PHE   A CE1 1 
ATOM   1425 C CE2 . PHE   A 1 188 ? -2.142  21.886 -35.069 1.00 61.18  ? 199 PHE   A CE2 1 
ATOM   1426 C CZ  . PHE   A 1 188 ? -2.266  20.820 -34.194 1.00 63.36  ? 199 PHE   A CZ  1 
ATOM   1427 N N   . ARG   A 1 189 ? -6.934  21.810 -34.863 1.00 39.70  ? 200 ARG   A N   1 
ATOM   1428 C CA  . ARG   A 1 189 ? -7.397  22.750 -33.860 1.00 39.70  ? 200 ARG   A CA  1 
ATOM   1429 C C   . ARG   A 1 189 ? -6.443  22.759 -32.672 1.00 42.84  ? 200 ARG   A C   1 
ATOM   1430 O O   . ARG   A 1 189 ? -6.914  22.750 -31.545 1.00 48.92  ? 200 ARG   A O   1 
ATOM   1431 C CB  . ARG   A 1 189 ? -8.817  22.342 -33.445 1.00 35.50  ? 200 ARG   A CB  1 
ATOM   1432 N N   . GLY   A 1 190 ? -5.122  22.796 -32.903 1.00 43.76  ? 201 GLY   A N   1 
ATOM   1433 C CA  . GLY   A 1 190 ? -4.172  22.599 -31.811 1.00 44.04  ? 201 GLY   A CA  1 
ATOM   1434 C C   . GLY   A 1 190 ? -2.952  23.518 -31.881 1.00 44.73  ? 201 GLY   A C   1 
ATOM   1435 O O   . GLY   A 1 190 ? -3.068  24.671 -32.298 1.00 49.78  ? 201 GLY   A O   1 
ATOM   1436 N N   . THR   A 1 191 ? -1.797  22.991 -31.435 1.00 41.81  ? 202 THR   A N   1 
ATOM   1437 C CA  . THR   A 1 191 ? -0.561  23.749 -31.294 1.00 38.35  ? 202 THR   A CA  1 
ATOM   1438 C C   . THR   A 1 191 ? 0.376   23.326 -32.412 1.00 35.26  ? 202 THR   A C   1 
ATOM   1439 O O   . THR   A 1 191 ? 0.672   22.145 -32.571 1.00 31.47  ? 202 THR   A O   1 
ATOM   1440 C CB  . THR   A 1 191 ? 0.090   23.499 -29.931 1.00 38.41  ? 202 THR   A CB  1 
ATOM   1441 O OG1 . THR   A 1 191 ? -0.690  24.183 -28.952 1.00 35.70  ? 202 THR   A OG1 1 
ATOM   1442 C CG2 . THR   A 1 191 ? 1.534   23.976 -29.888 1.00 37.94  ? 202 THR   A CG2 1 
ATOM   1443 N N   . VAL   A 1 192 ? 0.907   24.315 -33.118 1.00 36.74  ? 203 VAL   A N   1 
ATOM   1444 C CA  . VAL   A 1 192 ? 1.511   24.042 -34.409 1.00 39.51  ? 203 VAL   A CA  1 
ATOM   1445 C C   . VAL   A 1 192 ? 2.799   23.235 -34.213 1.00 35.81  ? 203 VAL   A C   1 
ATOM   1446 O O   . VAL   A 1 192 ? 2.966   22.190 -34.838 1.00 37.24  ? 203 VAL   A O   1 
ATOM   1447 C CB  . VAL   A 1 192 ? 1.744   25.338 -35.215 1.00 44.13  ? 203 VAL   A CB  1 
ATOM   1448 C CG1 . VAL   A 1 192 ? 2.127   25.016 -36.656 1.00 46.26  ? 203 VAL   A CG1 1 
ATOM   1449 C CG2 . VAL   A 1 192 ? 0.540   26.284 -35.186 1.00 42.30  ? 203 VAL   A CG2 1 
ATOM   1450 N N   . ARG   A 1 193 ? 3.666   23.682 -33.296 1.00 30.81  ? 204 ARG   A N   1 
ATOM   1451 C CA  . ARG   A 1 193 ? 5.044   23.219 -33.225 1.00 28.02  ? 204 ARG   A CA  1 
ATOM   1452 C C   . ARG   A 1 193 ? 5.154   21.689 -33.212 1.00 24.41  ? 204 ARG   A C   1 
ATOM   1453 O O   . ARG   A 1 193 ? 6.117   21.146 -33.746 1.00 22.67  ? 204 ARG   A O   1 
ATOM   1454 C CB  . ARG   A 1 193 ? 5.705   23.899 -32.021 1.00 28.52  ? 204 ARG   A CB  1 
ATOM   1455 C CG  . ARG   A 1 193 ? 7.127   23.421 -31.781 1.00 30.81  ? 204 ARG   A CG  1 
ATOM   1456 C CD  . ARG   A 1 193 ? 8.175   24.505 -31.591 1.00 34.51  ? 204 ARG   A CD  1 
ATOM   1457 N NE  . ARG   A 1 193 ? 7.677   25.730 -30.956 1.00 38.39  ? 204 ARG   A NE  1 
ATOM   1458 C CZ  . ARG   A 1 193 ? 7.759   26.038 -29.666 1.00 38.77  ? 204 ARG   A CZ  1 
ATOM   1459 N NH1 . ARG   A 1 193 ? 8.095   25.125 -28.768 1.00 36.22  ? 204 ARG   A NH1 1 
ATOM   1460 N NH2 . ARG   A 1 193 ? 7.436   27.261 -29.280 1.00 40.83  ? 204 ARG   A NH2 1 
ATOM   1461 N N   . TYR   A 1 194 ? 4.170   20.991 -32.626 1.00 21.88  ? 205 TYR   A N   1 
ATOM   1462 C CA  . TYR   A 1 194 ? 4.248   19.550 -32.421 1.00 20.07  ? 205 TYR   A CA  1 
ATOM   1463 C C   . TYR   A 1 194 ? 3.174   18.833 -33.239 1.00 19.23  ? 205 TYR   A C   1 
ATOM   1464 O O   . TYR   A 1 194 ? 2.840   17.685 -32.970 1.00 18.20  ? 205 TYR   A O   1 
ATOM   1465 C CB  . TYR   A 1 194 ? 4.131   19.254 -30.918 1.00 19.73  ? 205 TYR   A CB  1 
ATOM   1466 C CG  . TYR   A 1 194 ? 5.029   20.145 -30.068 1.00 18.72  ? 205 TYR   A CG  1 
ATOM   1467 C CD1 . TYR   A 1 194 ? 6.399   19.951 -30.017 1.00 18.78  ? 205 TYR   A CD1 1 
ATOM   1468 C CD2 . TYR   A 1 194 ? 4.502   21.196 -29.331 1.00 18.82  ? 205 TYR   A CD2 1 
ATOM   1469 C CE1 . TYR   A 1 194 ? 7.211   20.771 -29.251 1.00 19.54  ? 205 TYR   A CE1 1 
ATOM   1470 C CE2 . TYR   A 1 194 ? 5.300   22.029 -28.571 1.00 18.68  ? 205 TYR   A CE2 1 
ATOM   1471 C CZ  . TYR   A 1 194 ? 6.658   21.808 -28.520 1.00 19.47  ? 205 TYR   A CZ  1 
ATOM   1472 O OH  . TYR   A 1 194 ? 7.434   22.647 -27.777 1.00 20.71  ? 205 TYR   A OH  1 
ATOM   1473 N N   . ALA   A 1 195 ? 2.666   19.517 -34.266 1.00 19.45  ? 206 ALA   A N   1 
ATOM   1474 C CA  . ALA   A 1 195 ? 1.620   18.991 -35.130 1.00 18.29  ? 206 ALA   A CA  1 
ATOM   1475 C C   . ALA   A 1 195 ? 2.233   18.113 -36.216 1.00 16.49  ? 206 ALA   A C   1 
ATOM   1476 O O   . ALA   A 1 195 ? 3.192   18.526 -36.859 1.00 15.42  ? 206 ALA   A O   1 
ATOM   1477 C CB  . ALA   A 1 195 ? 0.867   20.157 -35.746 1.00 17.91  ? 206 ALA   A CB  1 
ATOM   1478 N N   . SER   A 1 196 ? 1.634   16.949 -36.467 1.00 15.62  ? 207 SER   A N   1 
ATOM   1479 C CA  . SER   A 1 196 ? 2.040   16.114 -37.587 1.00 16.23  ? 207 SER   A CA  1 
ATOM   1480 C C   . SER   A 1 196 ? 1.812   16.819 -38.918 1.00 16.08  ? 207 SER   A C   1 
ATOM   1481 O O   . SER   A 1 196 ? 1.171   17.845 -38.970 1.00 17.12  ? 207 SER   A O   1 
ATOM   1482 C CB  . SER   A 1 196 ? 1.296   14.815 -37.585 1.00 17.40  ? 207 SER   A CB  1 
ATOM   1483 O OG  . SER   A 1 196 ? -0.100  15.003 -37.777 1.00 18.62  ? 207 SER   A OG  1 
ATOM   1484 N N   . VAL   A 1 197 ? 2.278   16.229 -40.013 1.00 16.59  ? 208 VAL   A N   1 
ATOM   1485 C CA  . VAL   A 1 197 ? 1.926   16.730 -41.325 1.00 16.90  ? 208 VAL   A CA  1 
ATOM   1486 C C   . VAL   A 1 197 ? 0.509   16.276 -41.627 1.00 17.96  ? 208 VAL   A C   1 
ATOM   1487 O O   . VAL   A 1 197 ? -0.184  16.905 -42.406 1.00 19.77  ? 208 VAL   A O   1 
ATOM   1488 C CB  . VAL   A 1 197 ? 2.856   16.274 -42.454 1.00 17.79  ? 208 VAL   A CB  1 
ATOM   1489 C CG1 . VAL   A 1 197 ? 2.515   16.950 -43.776 1.00 17.66  ? 208 VAL   A CG1 1 
ATOM   1490 C CG2 . VAL   A 1 197 ? 4.318   16.510 -42.100 1.00 18.63  ? 208 VAL   A CG2 1 
ATOM   1491 N N   . ASN   A 1 198 ? 0.061   15.177 -41.033 1.00 18.99  ? 209 ASN   A N   1 
ATOM   1492 C CA  . ASN   A 1 198 ? -1.334  14.809 -41.207 1.00 20.27  ? 209 ASN   A CA  1 
ATOM   1493 C C   . ASN   A 1 198 ? -2.204  16.010 -40.825 1.00 21.08  ? 209 ASN   A C   1 
ATOM   1494 O O   . ASN   A 1 198 ? -3.096  16.415 -41.569 1.00 20.59  ? 209 ASN   A O   1 
ATOM   1495 C CB  . ASN   A 1 198 ? -1.671  13.527 -40.451 1.00 19.94  ? 209 ASN   A CB  1 
ATOM   1496 C CG  . ASN   A 1 198 ? -0.954  12.348 -41.052 1.00 19.61  ? 209 ASN   A CG  1 
ATOM   1497 O OD1 . ASN   A 1 198 ? -0.915  12.235 -42.284 1.00 20.08  ? 209 ASN   A OD1 1 
ATOM   1498 N ND2 . ASN   A 1 198 ? -0.347  11.512 -40.222 1.00 19.17  ? 209 ASN   A ND2 1 
ATOM   1499 N N   . ALA   A 1 199 ? -1.905  16.598 -39.666 1.00 21.71  ? 210 ALA   A N   1 
ATOM   1500 C CA  . ALA   A 1 199 ? -2.762  17.631 -39.121 1.00 22.56  ? 210 ALA   A CA  1 
ATOM   1501 C C   . ALA   A 1 199 ? -2.619  18.874 -39.986 1.00 22.81  ? 210 ALA   A C   1 
ATOM   1502 O O   . ALA   A 1 199 ? -3.598  19.544 -40.287 1.00 25.61  ? 210 ALA   A O   1 
ATOM   1503 C CB  . ALA   A 1 199 ? -2.439  17.885 -37.664 1.00 22.43  ? 210 ALA   A CB  1 
ATOM   1504 N N   . HIS   A 1 200 ? -1.409  19.154 -40.449 1.00 22.00  ? 211 HIS   A N   1 
ATOM   1505 C CA  . HIS   A 1 200 ? -1.228  20.321 -41.291 1.00 22.70  ? 211 HIS   A CA  1 
ATOM   1506 C C   . HIS   A 1 200 ? -2.085  20.187 -42.551 1.00 22.62  ? 211 HIS   A C   1 
ATOM   1507 O O   . HIS   A 1 200 ? -2.662  21.176 -43.001 1.00 24.07  ? 211 HIS   A O   1 
ATOM   1508 C CB  . HIS   A 1 200 ? 0.257   20.590 -41.562 1.00 23.34  ? 211 HIS   A CB  1 
ATOM   1509 C CG  . HIS   A 1 200 ? 0.957   21.278 -40.439 1.00 23.63  ? 211 HIS   A CG  1 
ATOM   1510 N ND1 . HIS   A 1 200 ? 0.972   22.652 -40.355 1.00 25.04  ? 211 HIS   A ND1 1 
ATOM   1511 C CD2 . HIS   A 1 200 ? 1.664   20.830 -39.384 1.00 24.23  ? 211 HIS   A CD2 1 
ATOM   1512 C CE1 . HIS   A 1 200 ? 1.666   23.006 -39.277 1.00 26.29  ? 211 HIS   A CE1 1 
ATOM   1513 N NE2 . HIS   A 1 200 ? 2.102   21.916 -38.676 1.00 25.16  ? 211 HIS   A NE2 1 
ATOM   1514 N N   . LYS   A 1 201 ? -2.202  18.960 -43.087 1.00 21.25  ? 212 LYS   A N   1 
ATOM   1515 C CA  . LYS   A 1 201 ? -2.965  18.718 -44.302 1.00 20.45  ? 212 LYS   A CA  1 
ATOM   1516 C C   . LYS   A 1 201 ? -4.462  18.633 -43.995 1.00 20.83  ? 212 LYS   A C   1 
ATOM   1517 O O   . LYS   A 1 201 ? -5.254  18.342 -44.893 1.00 22.69  ? 212 LYS   A O   1 
ATOM   1518 C CB  . LYS   A 1 201 ? -2.448  17.453 -44.991 1.00 20.11  ? 212 LYS   A CB  1 
ATOM   1519 C CG  . LYS   A 1 201 ? -1.053  17.580 -45.592 1.00 20.36  ? 212 LYS   A CG  1 
ATOM   1520 C CD  . LYS   A 1 201 ? -0.365  16.247 -45.867 1.00 20.39  ? 212 LYS   A CD  1 
ATOM   1521 C CE  . LYS   A 1 201 ? 0.995   16.398 -46.465 1.00 20.52  ? 212 LYS   A CE  1 
ATOM   1522 N NZ  . LYS   A 1 201 ? 0.909   16.514 -47.923 1.00 21.43  ? 212 LYS   A NZ  1 
ATOM   1523 N N   . ASN   A 1 202 ? -4.833  18.909 -42.731 1.00 20.13  ? 213 ASN   A N   1 
ATOM   1524 C CA  . ASN   A 1 202 ? -6.209  18.936 -42.245 1.00 19.42  ? 213 ASN   A CA  1 
ATOM   1525 C C   . ASN   A 1 202 ? -6.873  17.583 -42.490 1.00 19.55  ? 213 ASN   A C   1 
ATOM   1526 O O   . ASN   A 1 202 ? -8.038  17.528 -42.860 1.00 19.18  ? 213 ASN   A O   1 
ATOM   1527 C CB  . ASN   A 1 202 ? -7.022  20.091 -42.833 1.00 19.03  ? 213 ASN   A CB  1 
ATOM   1528 C CG  . ASN   A 1 202 ? -6.702  21.436 -42.224 1.00 17.93  ? 213 ASN   A CG  1 
ATOM   1529 O OD1 . ASN   A 1 202 ? -6.683  21.561 -40.998 1.00 17.64  ? 213 ASN   A OD1 1 
ATOM   1530 N ND2 . ASN   A 1 202 ? -6.480  22.450 -43.046 1.00 17.38  ? 213 ASN   A ND2 1 
ATOM   1531 N N   . ARG   A 1 203 ? -6.112  16.507 -42.267 1.00 21.65  ? 214 ARG   A N   1 
ATOM   1532 C CA  . ARG   A 1 203 ? -6.623  15.146 -42.297 1.00 22.94  ? 214 ARG   A CA  1 
ATOM   1533 C C   . ARG   A 1 203 ? -6.828  14.631 -40.874 1.00 21.65  ? 214 ARG   A C   1 
ATOM   1534 O O   . ARG   A 1 203 ? -6.086  14.967 -39.953 1.00 21.58  ? 214 ARG   A O   1 
ATOM   1535 C CB  . ARG   A 1 203 ? -5.669  14.241 -43.076 1.00 25.41  ? 214 ARG   A CB  1 
ATOM   1536 C CG  . ARG   A 1 203 ? -5.780  14.525 -44.562 1.00 30.06  ? 214 ARG   A CG  1 
ATOM   1537 C CD  . ARG   A 1 203 ? -4.606  13.961 -45.332 1.00 35.08  ? 214 ARG   A CD  1 
ATOM   1538 N NE  . ARG   A 1 203 ? -4.701  14.173 -46.783 1.00 39.77  ? 214 ARG   A NE  1 
ATOM   1539 C CZ  . ARG   A 1 203 ? -3.737  13.888 -47.672 1.00 42.11  ? 214 ARG   A CZ  1 
ATOM   1540 N NH1 . ARG   A 1 203 ? -2.577  13.366 -47.287 1.00 41.88  ? 214 ARG   A NH1 1 
ATOM   1541 N NH2 . ARG   A 1 203 ? -3.938  14.125 -48.962 1.00 42.37  ? 214 ARG   A NH2 1 
ATOM   1542 N N   . GLU   A 1 204 ? -7.846  13.784 -40.735 1.00 20.48  ? 215 GLU   A N   1 
ATOM   1543 C CA  . GLU   A 1 204 ? -8.232  13.191 -39.465 1.00 20.44  ? 215 GLU   A CA  1 
ATOM   1544 C C   . GLU   A 1 204 ? -7.013  12.529 -38.822 1.00 19.38  ? 215 GLU   A C   1 
ATOM   1545 O O   . GLU   A 1 204 ? -6.281  11.751 -39.451 1.00 16.59  ? 215 GLU   A O   1 
ATOM   1546 C CB  . GLU   A 1 204 ? -9.419  12.250 -39.707 1.00 21.34  ? 215 GLU   A CB  1 
ATOM   1547 C CG  . GLU   A 1 204 ? -10.085 11.694 -38.451 1.00 21.64  ? 215 GLU   A CG  1 
ATOM   1548 C CD  . GLU   A 1 204 ? -11.312 12.443 -37.963 1.00 22.43  ? 215 GLU   A CD  1 
ATOM   1549 O OE1 . GLU   A 1 204 ? -12.353 12.502 -38.661 1.00 21.01  ? 215 GLU   A OE1 1 
ATOM   1550 O OE2 . GLU   A 1 204 ? -11.203 12.957 -36.831 1.00 24.98  ? 215 GLU   A OE2 1 
ATOM   1551 N N   . MET   A 1 205 ? -6.826  12.880 -37.539 1.00 19.66  ? 216 MET   A N   1 
ATOM   1552 C CA  . MET   A 1 205 ? -5.635  12.526 -36.788 1.00 18.91  ? 216 MET   A CA  1 
ATOM   1553 C C   . MET   A 1 205 ? -5.760  11.094 -36.261 1.00 18.44  ? 216 MET   A C   1 
ATOM   1554 O O   . MET   A 1 205 ? -6.844  10.626 -35.936 1.00 16.50  ? 216 MET   A O   1 
ATOM   1555 C CB  . MET   A 1 205 ? -5.420  13.506 -35.627 1.00 18.55  ? 216 MET   A CB  1 
ATOM   1556 C CG  . MET   A 1 205 ? -5.187  14.949 -36.027 1.00 17.97  ? 216 MET   A CG  1 
ATOM   1557 S SD  . MET   A 1 205 ? -4.865  15.956 -34.563 1.00 17.70  ? 216 MET   A SD  1 
ATOM   1558 C CE  . MET   A 1 205 ? -3.133  15.688 -34.174 1.00 18.24  ? 216 MET   A CE  1 
ATOM   1559 N N   . GLY   A 1 206 ? -4.619  10.404 -36.188 1.00 19.78  ? 217 GLY   A N   1 
ATOM   1560 C CA  . GLY   A 1 206 ? -4.538  9.055  -35.651 1.00 20.39  ? 217 GLY   A CA  1 
ATOM   1561 C C   . GLY   A 1 206 ? -3.748  8.997  -34.339 1.00 20.87  ? 217 GLY   A C   1 
ATOM   1562 O O   . GLY   A 1 206 ? -3.335  10.018 -33.775 1.00 22.70  ? 217 GLY   A O   1 
ATOM   1563 N N   . ARG   A 1 207 ? -3.573  7.769  -33.845 1.00 19.72  ? 218 ARG   A N   1 
ATOM   1564 C CA  . ARG   A 1 207 ? -2.695  7.501  -32.726 1.00 18.43  ? 218 ARG   A CA  1 
ATOM   1565 C C   . ARG   A 1 207 ? -1.257  7.784  -33.141 1.00 17.20  ? 218 ARG   A C   1 
ATOM   1566 O O   . ARG   A 1 207 ? -0.422  8.135  -32.316 1.00 16.98  ? 218 ARG   A O   1 
ATOM   1567 C CB  . ARG   A 1 207 ? -2.872  6.039  -32.336 1.00 18.64  ? 218 ARG   A CB  1 
ATOM   1568 C CG  . ARG   A 1 207 ? -4.295  5.776  -31.886 1.00 19.46  ? 218 ARG   A CG  1 
ATOM   1569 C CD  . ARG   A 1 207 ? -4.518  4.286  -31.816 1.00 21.21  ? 218 ARG   A CD  1 
ATOM   1570 N NE  . ARG   A 1 207 ? -4.864  3.684  -33.113 1.00 21.38  ? 218 ARG   A NE  1 
ATOM   1571 C CZ  . ARG   A 1 207 ? -5.190  2.413  -33.276 1.00 20.16  ? 218 ARG   A CZ  1 
ATOM   1572 N NH1 . ARG   A 1 207 ? -5.281  1.622  -32.228 1.00 20.52  ? 218 ARG   A NH1 1 
ATOM   1573 N NH2 . ARG   A 1 207 ? -5.409  1.936  -34.483 1.00 19.98  ? 218 ARG   A NH2 1 
ATOM   1574 N N   . HIS   A 1 208 ? -0.961  7.634  -34.428 1.00 16.37  ? 219 HIS   A N   1 
ATOM   1575 C CA  . HIS   A 1 208 ? 0.376   7.953  -34.882 1.00 17.13  ? 219 HIS   A CA  1 
ATOM   1576 C C   . HIS   A 1 208 ? 0.616   9.456  -34.781 1.00 17.14  ? 219 HIS   A C   1 
ATOM   1577 O O   . HIS   A 1 208 ? 1.755   9.890  -34.605 1.00 17.19  ? 219 HIS   A O   1 
ATOM   1578 C CB  . HIS   A 1 208 ? 0.664   7.389  -36.275 1.00 17.79  ? 219 HIS   A CB  1 
ATOM   1579 C CG  . HIS   A 1 208 ? -0.222  7.905  -37.334 1.00 18.00  ? 219 HIS   A CG  1 
ATOM   1580 N ND1 . HIS   A 1 208 ? -1.560  8.164  -37.134 1.00 18.75  ? 219 HIS   A ND1 1 
ATOM   1581 C CD2 . HIS   A 1 208 ? 0.043   8.198  -38.598 1.00 18.57  ? 219 HIS   A CD2 1 
ATOM   1582 C CE1 . HIS   A 1 208 ? -2.087  8.603  -38.264 1.00 19.33  ? 219 HIS   A CE1 1 
ATOM   1583 N NE2 . HIS   A 1 208 ? -1.129  8.631  -39.169 1.00 20.04  ? 219 HIS   A NE2 1 
ATOM   1584 N N   . ASP   A 1 209 ? -0.449  10.257 -34.858 1.00 16.87  ? 220 ASP   A N   1 
ATOM   1585 C CA  . ASP   A 1 209 ? -0.239  11.692 -34.833 1.00 16.52  ? 220 ASP   A CA  1 
ATOM   1586 C C   . ASP   A 1 209 ? 0.026   12.141 -33.403 1.00 17.95  ? 220 ASP   A C   1 
ATOM   1587 O O   . ASP   A 1 209 ? 0.770   13.101 -33.233 1.00 18.46  ? 220 ASP   A O   1 
ATOM   1588 C CB  . ASP   A 1 209 ? -1.248  12.466 -35.661 1.00 15.49  ? 220 ASP   A CB  1 
ATOM   1589 C CG  . ASP   A 1 209 ? -1.225  12.120 -37.142 1.00 14.50  ? 220 ASP   A CG  1 
ATOM   1590 O OD1 . ASP   A 1 209 ? -0.139  12.087 -37.742 1.00 13.25  ? 220 ASP   A OD1 1 
ATOM   1591 O OD2 . ASP   A 1 209 ? -2.297  11.855 -37.686 1.00 15.01  ? 220 ASP   A OD2 1 
ATOM   1592 N N   . ASP   A 1 210 ? -0.477  11.418 -32.387 1.00 19.54  ? 221 ASP   A N   1 
ATOM   1593 C CA  . ASP   A 1 210 ? -0.074  11.720 -31.016 1.00 21.43  ? 221 ASP   A CA  1 
ATOM   1594 C C   . ASP   A 1 210 ? 1.378   11.309 -30.809 1.00 24.40  ? 221 ASP   A C   1 
ATOM   1595 O O   . ASP   A 1 210 ? 2.037   11.840 -29.919 1.00 27.15  ? 221 ASP   A O   1 
ATOM   1596 C CB  . ASP   A 1 210 ? -0.927  11.079 -29.936 1.00 21.76  ? 221 ASP   A CB  1 
ATOM   1597 C CG  . ASP   A 1 210 ? -2.406  11.447 -29.937 1.00 23.73  ? 221 ASP   A CG  1 
ATOM   1598 O OD1 . ASP   A 1 210 ? -2.708  12.649 -30.114 1.00 26.48  ? 221 ASP   A OD1 1 
ATOM   1599 O OD2 . ASP   A 1 210 ? -3.251  10.530 -29.743 1.00 23.33  ? 221 ASP   A OD2 1 
ATOM   1600 N N   . LEU   A 1 211 ? 1.870   10.389 -31.650 1.00 26.82  ? 222 LEU   A N   1 
ATOM   1601 C CA  . LEU   A 1 211 ? 3.254   9.930  -31.595 1.00 28.76  ? 222 LEU   A CA  1 
ATOM   1602 C C   . LEU   A 1 211 ? 4.187   10.794 -32.446 1.00 25.67  ? 222 LEU   A C   1 
ATOM   1603 O O   . LEU   A 1 211 ? 5.376   10.893 -32.155 1.00 25.69  ? 222 LEU   A O   1 
ATOM   1604 C CB  . LEU   A 1 211 ? 3.327   8.463  -32.019 1.00 32.29  ? 222 LEU   A CB  1 
ATOM   1605 C CG  . LEU   A 1 211 ? 2.644   7.468  -31.075 1.00 34.66  ? 222 LEU   A CG  1 
ATOM   1606 C CD1 . LEU   A 1 211 ? 2.391   6.154  -31.782 1.00 34.82  ? 222 LEU   A CD1 1 
ATOM   1607 C CD2 . LEU   A 1 211 ? 3.473   7.237  -29.815 1.00 35.86  ? 222 LEU   A CD2 1 
ATOM   1608 N N   . TRP   A 1 212 ? 3.690   11.414 -33.509 1.00 23.05  ? 223 TRP   A N   1 
ATOM   1609 C CA  . TRP   A 1 212 ? 4.522   12.422 -34.135 1.00 23.21  ? 223 TRP   A CA  1 
ATOM   1610 C C   . TRP   A 1 212 ? 4.855   13.504 -33.111 1.00 22.59  ? 223 TRP   A C   1 
ATOM   1611 O O   . TRP   A 1 212 ? 6.019   13.831 -32.921 1.00 22.59  ? 223 TRP   A O   1 
ATOM   1612 C CB  . TRP   A 1 212 ? 3.844   13.012 -35.372 1.00 23.01  ? 223 TRP   A CB  1 
ATOM   1613 C CG  . TRP   A 1 212 ? 4.072   12.212 -36.624 1.00 22.22  ? 223 TRP   A CG  1 
ATOM   1614 C CD1 . TRP   A 1 212 ? 3.191   11.406 -37.284 1.00 21.43  ? 223 TRP   A CD1 1 
ATOM   1615 C CD2 . TRP   A 1 212 ? 5.302   12.172 -37.370 1.00 22.18  ? 223 TRP   A CD2 1 
ATOM   1616 N NE1 . TRP   A 1 212 ? 3.782   10.877 -38.399 1.00 21.58  ? 223 TRP   A NE1 1 
ATOM   1617 C CE2 . TRP   A 1 212 ? 5.077   11.326 -38.477 1.00 22.05  ? 223 TRP   A CE2 1 
ATOM   1618 C CE3 . TRP   A 1 212 ? 6.556   12.773 -37.212 1.00 21.96  ? 223 TRP   A CE3 1 
ATOM   1619 C CZ2 . TRP   A 1 212 ? 6.072   11.066 -39.417 1.00 21.82  ? 223 TRP   A CZ2 1 
ATOM   1620 C CZ3 . TRP   A 1 212 ? 7.539   12.512 -38.146 1.00 22.13  ? 223 TRP   A CZ3 1 
ATOM   1621 C CH2 . TRP   A 1 212 ? 7.298   11.670 -39.233 1.00 21.64  ? 223 TRP   A CH2 1 
ATOM   1622 N N   . SER   A 1 213 ? 3.820   14.016 -32.433 1.00 22.25  ? 224 SER   A N   1 
ATOM   1623 C CA  . SER   A 1 213 ? 3.961   15.035 -31.399 1.00 21.87  ? 224 SER   A CA  1 
ATOM   1624 C C   . SER   A 1 213 ? 5.039   14.656 -30.383 1.00 21.55  ? 224 SER   A C   1 
ATOM   1625 O O   . SER   A 1 213 ? 5.883   15.464 -29.997 1.00 20.72  ? 224 SER   A O   1 
ATOM   1626 C CB  . SER   A 1 213 ? 2.646   15.254 -30.681 1.00 21.69  ? 224 SER   A CB  1 
ATOM   1627 O OG  . SER   A 1 213 ? 1.772   16.147 -31.355 1.00 21.84  ? 224 SER   A OG  1 
ATOM   1628 N N   . LEU   A 1 214 ? 4.957   13.421 -29.904 1.00 21.52  ? 225 LEU   A N   1 
ATOM   1629 C CA  . LEU   A 1 214 ? 5.921   12.932 -28.953 1.00 22.65  ? 225 LEU   A CA  1 
ATOM   1630 C C   . LEU   A 1 214 ? 7.325   13.029 -29.534 1.00 22.81  ? 225 LEU   A C   1 
ATOM   1631 O O   . LEU   A 1 214 ? 8.269   13.341 -28.811 1.00 23.70  ? 225 LEU   A O   1 
ATOM   1632 C CB  . LEU   A 1 214 ? 5.546   11.487 -28.647 1.00 25.32  ? 225 LEU   A CB  1 
ATOM   1633 C CG  . LEU   A 1 214 ? 6.485   10.770 -27.673 1.00 28.52  ? 225 LEU   A CG  1 
ATOM   1634 C CD1 . LEU   A 1 214 ? 6.469   11.523 -26.333 1.00 30.99  ? 225 LEU   A CD1 1 
ATOM   1635 C CD2 . LEU   A 1 214 ? 6.124   9.303  -27.490 1.00 28.45  ? 225 LEU   A CD2 1 
ATOM   1636 N N   . PHE   A 1 215 ? 7.459   12.717 -30.831 1.00 23.06  ? 226 PHE   A N   1 
ATOM   1637 C CA  . PHE   A 1 215 ? 8.759   12.647 -31.482 1.00 24.17  ? 226 PHE   A CA  1 
ATOM   1638 C C   . PHE   A 1 215 ? 9.432   14.014 -31.432 1.00 22.71  ? 226 PHE   A C   1 
ATOM   1639 O O   . PHE   A 1 215 ? 10.571  14.130 -30.994 1.00 24.68  ? 226 PHE   A O   1 
ATOM   1640 C CB  . PHE   A 1 215 ? 8.567   12.155 -32.919 1.00 26.45  ? 226 PHE   A CB  1 
ATOM   1641 C CG  . PHE   A 1 215 ? 9.825   12.114 -33.777 1.00 29.35  ? 226 PHE   A CG  1 
ATOM   1642 C CD1 . PHE   A 1 215 ? 10.681  11.016 -33.739 1.00 30.71  ? 226 PHE   A CD1 1 
ATOM   1643 C CD2 . PHE   A 1 215 ? 10.130  13.159 -34.646 1.00 31.99  ? 226 PHE   A CD2 1 
ATOM   1644 C CE1 . PHE   A 1 215 ? 11.822  10.971 -34.532 1.00 31.32  ? 226 PHE   A CE1 1 
ATOM   1645 C CE2 . PHE   A 1 215 ? 11.274  13.114 -35.438 1.00 33.57  ? 226 PHE   A CE2 1 
ATOM   1646 C CZ  . PHE   A 1 215 ? 12.120  12.020 -35.376 1.00 33.19  ? 226 PHE   A CZ  1 
ATOM   1647 N N   . TYR   A 1 216 ? 8.684   15.029 -31.871 1.00 20.09  ? 227 TYR   A N   1 
ATOM   1648 C CA  . TYR   A 1 216 ? 9.139   16.400 -31.952 1.00 18.46  ? 227 TYR   A CA  1 
ATOM   1649 C C   . TYR   A 1 216 ? 9.392   17.008 -30.578 1.00 18.89  ? 227 TYR   A C   1 
ATOM   1650 O O   . TYR   A 1 216 ? 10.280  17.841 -30.448 1.00 19.27  ? 227 TYR   A O   1 
ATOM   1651 C CB  . TYR   A 1 216 ? 8.052   17.186 -32.678 1.00 17.99  ? 227 TYR   A CB  1 
ATOM   1652 C CG  . TYR   A 1 216 ? 7.917   16.982 -34.182 1.00 17.84  ? 227 TYR   A CG  1 
ATOM   1653 C CD1 . TYR   A 1 216 ? 9.011   16.730 -35.008 1.00 18.47  ? 227 TYR   A CD1 1 
ATOM   1654 C CD2 . TYR   A 1 216 ? 6.674   17.103 -34.788 1.00 17.61  ? 227 TYR   A CD2 1 
ATOM   1655 C CE1 . TYR   A 1 216 ? 8.864   16.596 -36.383 1.00 18.91  ? 227 TYR   A CE1 1 
ATOM   1656 C CE2 . TYR   A 1 216 ? 6.513   16.969 -36.156 1.00 17.60  ? 227 TYR   A CE2 1 
ATOM   1657 C CZ  . TYR   A 1 216 ? 7.607   16.719 -36.956 1.00 18.54  ? 227 TYR   A CZ  1 
ATOM   1658 O OH  . TYR   A 1 216 ? 7.389   16.590 -38.295 1.00 18.99  ? 227 TYR   A OH  1 
ATOM   1659 N N   . MET   A 1 217 ? 8.585   16.653 -29.574 1.00 20.28  ? 228 MET   A N   1 
ATOM   1660 C CA  . MET   A 1 217 ? 8.837   17.088 -28.206 1.00 22.05  ? 228 MET   A CA  1 
ATOM   1661 C C   . MET   A 1 217 ? 10.240  16.708 -27.734 1.00 21.66  ? 228 MET   A C   1 
ATOM   1662 O O   . MET   A 1 217 ? 10.919  17.503 -27.085 1.00 22.50  ? 228 MET   A O   1 
ATOM   1663 C CB  . MET   A 1 217 ? 7.939   16.390 -27.186 1.00 24.69  ? 228 MET   A CB  1 
ATOM   1664 C CG  . MET   A 1 217 ? 6.528   16.894 -27.097 1.00 27.06  ? 228 MET   A CG  1 
ATOM   1665 S SD  . MET   A 1 217 ? 5.664   15.995 -25.787 1.00 31.15  ? 228 MET   A SD  1 
ATOM   1666 C CE  . MET   A 1 217 ? 6.443   16.874 -24.422 1.00 29.29  ? 228 MET   A CE  1 
ATOM   1667 N N   . LEU   A 1 218 ? 10.653  15.466 -28.002 1.00 20.91  ? 229 LEU   A N   1 
ATOM   1668 C CA  . LEU   A 1 218 ? 11.919  14.963 -27.494 1.00 20.99  ? 229 LEU   A CA  1 
ATOM   1669 C C   . LEU   A 1 218 ? 13.077  15.674 -28.191 1.00 20.68  ? 229 LEU   A C   1 
ATOM   1670 O O   . LEU   A 1 218 ? 13.946  16.235 -27.526 1.00 21.22  ? 229 LEU   A O   1 
ATOM   1671 C CB  . LEU   A 1 218 ? 11.965  13.448 -27.687 1.00 22.34  ? 229 LEU   A CB  1 
ATOM   1672 C CG  . LEU   A 1 218 ? 10.817  12.648 -27.055 1.00 23.00  ? 229 LEU   A CG  1 
ATOM   1673 C CD1 . LEU   A 1 218 ? 11.005  11.158 -27.327 1.00 22.37  ? 229 LEU   A CD1 1 
ATOM   1674 C CD2 . LEU   A 1 218 ? 10.666  12.924 -25.551 1.00 23.26  ? 229 LEU   A CD2 1 
ATOM   1675 N N   . VAL   A 1 219 ? 13.047  15.681 -29.532 1.00 19.95  ? 230 VAL   A N   1 
ATOM   1676 C CA  . VAL   A 1 219 ? 14.024  16.380 -30.358 1.00 19.62  ? 230 VAL   A CA  1 
ATOM   1677 C C   . VAL   A 1 219 ? 14.319  17.769 -29.794 1.00 20.34  ? 230 VAL   A C   1 
ATOM   1678 O O   . VAL   A 1 219 ? 15.467  18.174 -29.710 1.00 19.65  ? 230 VAL   A O   1 
ATOM   1679 C CB  . VAL   A 1 219 ? 13.506  16.450 -31.804 1.00 18.49  ? 230 VAL   A CB  1 
ATOM   1680 C CG1 . VAL   A 1 219 ? 14.352  17.353 -32.694 1.00 17.89  ? 230 VAL   A CG1 1 
ATOM   1681 C CG2 . VAL   A 1 219 ? 13.391  15.056 -32.406 1.00 18.48  ? 230 VAL   A CG2 1 
ATOM   1682 N N   . GLU   A 1 220 ? 13.277  18.489 -29.391 1.00 23.17  ? 231 GLU   A N   1 
ATOM   1683 C CA  . GLU   A 1 220 ? 13.453  19.809 -28.821 1.00 26.99  ? 231 GLU   A CA  1 
ATOM   1684 C C   . GLU   A 1 220 ? 14.029  19.729 -27.406 1.00 28.21  ? 231 GLU   A C   1 
ATOM   1685 O O   . GLU   A 1 220 ? 14.797  20.609 -27.046 1.00 33.92  ? 231 GLU   A O   1 
ATOM   1686 C CB  . GLU   A 1 220 ? 12.143  20.594 -28.858 1.00 30.13  ? 231 GLU   A CB  1 
ATOM   1687 C CG  . GLU   A 1 220 ? 12.299  22.055 -28.442 1.00 32.36  ? 231 GLU   A CG  1 
ATOM   1688 C CD  . GLU   A 1 220 ? 11.065  22.861 -28.796 1.00 34.77  ? 231 GLU   A CD  1 
ATOM   1689 O OE1 . GLU   A 1 220 ? 9.982   22.512 -28.276 1.00 30.15  ? 231 GLU   A OE1 1 
ATOM   1690 O OE2 . GLU   A 1 220 ? 11.189  23.812 -29.617 1.00 41.13  ? 231 GLU   A OE2 1 
ATOM   1691 N N   . PHE   A 1 221 ? 13.676  18.723 -26.595 1.00 25.59  ? 232 PHE   A N   1 
ATOM   1692 C CA  . PHE   A 1 221 ? 14.282  18.568 -25.278 1.00 25.91  ? 232 PHE   A CA  1 
ATOM   1693 C C   . PHE   A 1 221 ? 15.782  18.277 -25.329 1.00 27.09  ? 232 PHE   A C   1 
ATOM   1694 O O   . PHE   A 1 221 ? 16.539  18.581 -24.402 1.00 26.84  ? 232 PHE   A O   1 
ATOM   1695 C CB  . PHE   A 1 221 ? 13.773  17.357 -24.502 1.00 26.63  ? 232 PHE   A CB  1 
ATOM   1696 C CG  . PHE   A 1 221 ? 12.306  17.406 -24.119 1.00 27.39  ? 232 PHE   A CG  1 
ATOM   1697 C CD1 . PHE   A 1 221 ? 11.591  18.590 -24.191 1.00 27.16  ? 232 PHE   A CD1 1 
ATOM   1698 C CD2 . PHE   A 1 221 ? 11.661  16.264 -23.663 1.00 27.67  ? 232 PHE   A CD2 1 
ATOM   1699 C CE1 . PHE   A 1 221 ? 10.264  18.628 -23.819 1.00 28.30  ? 232 PHE   A CE1 1 
ATOM   1700 C CE2 . PHE   A 1 221 ? 10.332  16.309 -23.298 1.00 28.12  ? 232 PHE   A CE2 1 
ATOM   1701 C CZ  . PHE   A 1 221 ? 9.639   17.490 -23.372 1.00 28.67  ? 232 PHE   A CZ  1 
ATOM   1702 N N   . ALA   A 1 222 ? 16.219  17.568 -26.359 1.00 29.21  ? 233 ALA   A N   1 
ATOM   1703 C CA  . ALA   A 1 222 ? 17.630  17.240 -26.419 1.00 29.98  ? 233 ALA   A CA  1 
ATOM   1704 C C   . ALA   A 1 222 ? 18.328  18.399 -27.095 1.00 26.74  ? 233 ALA   A C   1 
ATOM   1705 O O   . ALA   A 1 222 ? 19.066  19.106 -26.441 1.00 27.84  ? 233 ALA   A O   1 
ATOM   1706 C CB  . ALA   A 1 222 ? 17.856  15.941 -27.141 1.00 32.74  ? 233 ALA   A CB  1 
ATOM   1707 N N   . VAL   A 1 223 ? 17.964  18.643 -28.353 1.00 25.72  ? 234 VAL   A N   1 
ATOM   1708 C CA  . VAL   A 1 223 ? 18.646  19.603 -29.199 1.00 25.87  ? 234 VAL   A CA  1 
ATOM   1709 C C   . VAL   A 1 223 ? 18.420  21.033 -28.701 1.00 28.21  ? 234 VAL   A C   1 
ATOM   1710 O O   . VAL   A 1 223 ? 19.337  21.845 -28.774 1.00 28.52  ? 234 VAL   A O   1 
ATOM   1711 C CB  . VAL   A 1 223 ? 18.177  19.388 -30.646 1.00 25.65  ? 234 VAL   A CB  1 
ATOM   1712 C CG1 . VAL   A 1 223 ? 18.761  20.405 -31.615 1.00 26.71  ? 234 VAL   A CG1 1 
ATOM   1713 C CG2 . VAL   A 1 223 ? 18.495  17.972 -31.104 1.00 25.81  ? 234 VAL   A CG2 1 
ATOM   1714 N N   . GLY   A 1 224 ? 17.222  21.354 -28.190 1.00 30.05  ? 235 GLY   A N   1 
ATOM   1715 C CA  . GLY   A 1 224 ? 16.992  22.641 -27.537 1.00 30.76  ? 235 GLY   A CA  1 
ATOM   1716 C C   . GLY   A 1 224 ? 16.190  23.620 -28.392 1.00 32.25  ? 235 GLY   A C   1 
ATOM   1717 O O   . GLY   A 1 224 ? 15.888  24.721 -27.932 1.00 29.48  ? 235 GLY   A O   1 
ATOM   1718 N N   . GLN   A 1 225 ? 15.872  23.194 -29.626 1.00 36.29  ? 236 GLN   A N   1 
ATOM   1719 C CA  . GLN   A 1 225 ? 15.163  23.988 -30.618 1.00 38.45  ? 236 GLN   A CA  1 
ATOM   1720 C C   . GLN   A 1 225 ? 14.659  23.086 -31.741 1.00 37.75  ? 236 GLN   A C   1 
ATOM   1721 O O   . GLN   A 1 225 ? 15.206  22.007 -31.964 1.00 41.85  ? 236 GLN   A O   1 
ATOM   1722 C CB  . GLN   A 1 225 ? 16.116  24.954 -31.313 1.00 42.07  ? 236 GLN   A CB  1 
ATOM   1723 C CG  . GLN   A 1 225 ? 17.330  24.266 -31.934 1.00 47.12  ? 236 GLN   A CG  1 
ATOM   1724 C CD  . GLN   A 1 225 ? 17.700  24.828 -33.294 1.00 51.18  ? 236 GLN   A CD  1 
ATOM   1725 O OE1 . GLN   A 1 225 ? 17.445  24.215 -34.342 1.00 48.46  ? 236 GLN   A OE1 1 
ATOM   1726 N NE2 . GLN   A 1 225 ? 18.292  26.016 -33.286 1.00 50.35  ? 236 GLN   A NE2 1 
ATOM   1727 N N   . LEU   A 1 226 ? 13.653  23.560 -32.480 1.00 34.11  ? 237 LEU   A N   1 
ATOM   1728 C CA  . LEU   A 1 226 ? 13.214  22.901 -33.701 1.00 31.95  ? 237 LEU   A CA  1 
ATOM   1729 C C   . LEU   A 1 226 ? 13.471  23.833 -34.880 1.00 28.99  ? 237 LEU   A C   1 
ATOM   1730 O O   . LEU   A 1 226 ? 13.475  25.043 -34.676 1.00 28.34  ? 237 LEU   A O   1 
ATOM   1731 C CB  . LEU   A 1 226 ? 11.726  22.575 -33.566 1.00 33.95  ? 237 LEU   A CB  1 
ATOM   1732 C CG  . LEU   A 1 226 ? 11.339  21.312 -32.785 1.00 34.22  ? 237 LEU   A CG  1 
ATOM   1733 C CD1 . LEU   A 1 226 ? 9.826   21.211 -32.698 1.00 33.33  ? 237 LEU   A CD1 1 
ATOM   1734 C CD2 . LEU   A 1 226 ? 11.893  20.025 -33.390 1.00 34.76  ? 237 LEU   A CD2 1 
ATOM   1735 N N   . PRO   A 1 227 ? 13.643  23.329 -36.135 1.00 27.72  ? 238 PRO   A N   1 
ATOM   1736 C CA  . PRO   A 1 227 ? 13.855  24.187 -37.310 1.00 28.65  ? 238 PRO   A CA  1 
ATOM   1737 C C   . PRO   A 1 227 ? 12.932  25.404 -37.405 1.00 30.27  ? 238 PRO   A C   1 
ATOM   1738 O O   . PRO   A 1 227 ? 13.393  26.514 -37.668 1.00 28.40  ? 238 PRO   A O   1 
ATOM   1739 C CB  . PRO   A 1 227 ? 13.655  23.238 -38.508 1.00 27.06  ? 238 PRO   A CB  1 
ATOM   1740 C CG  . PRO   A 1 227 ? 14.049  21.885 -37.979 1.00 26.79  ? 238 PRO   A CG  1 
ATOM   1741 C CD  . PRO   A 1 227 ? 13.668  21.905 -36.498 1.00 26.96  ? 238 PRO   A CD  1 
ATOM   1742 N N   . TRP   A 1 228 ? 11.637  25.176 -37.148 1.00 34.12  ? 239 TRP   A N   1 
ATOM   1743 C CA  . TRP   A 1 228 ? 10.579  26.153 -37.367 1.00 34.35  ? 239 TRP   A CA  1 
ATOM   1744 C C   . TRP   A 1 228 ? 10.220  26.925 -36.099 1.00 36.46  ? 239 TRP   A C   1 
ATOM   1745 O O   . TRP   A 1 228 ? 9.385   27.804 -36.180 1.00 35.24  ? 239 TRP   A O   1 
ATOM   1746 C CB  . TRP   A 1 228 ? 9.329   25.450 -37.911 1.00 34.05  ? 239 TRP   A CB  1 
ATOM   1747 C CG  . TRP   A 1 228 ? 8.911   24.244 -37.105 1.00 37.75  ? 239 TRP   A CG  1 
ATOM   1748 C CD1 . TRP   A 1 228 ? 8.204   24.221 -35.933 1.00 38.15  ? 239 TRP   A CD1 1 
ATOM   1749 C CD2 . TRP   A 1 228 ? 9.192   22.862 -37.429 1.00 39.01  ? 239 TRP   A CD2 1 
ATOM   1750 N NE1 . TRP   A 1 228 ? 8.019   22.931 -35.513 1.00 37.46  ? 239 TRP   A NE1 1 
ATOM   1751 C CE2 . TRP   A 1 228 ? 8.621   22.077 -36.404 1.00 38.64  ? 239 TRP   A CE2 1 
ATOM   1752 C CE3 . TRP   A 1 228 ? 9.870   22.218 -38.473 1.00 38.22  ? 239 TRP   A CE3 1 
ATOM   1753 C CZ2 . TRP   A 1 228 ? 8.716   20.685 -36.407 1.00 38.58  ? 239 TRP   A CZ2 1 
ATOM   1754 C CZ3 . TRP   A 1 228 ? 9.964   20.843 -38.466 1.00 36.89  ? 239 TRP   A CZ3 1 
ATOM   1755 C CH2 . TRP   A 1 228 ? 9.395   20.089 -37.445 1.00 35.98  ? 239 TRP   A CH2 1 
ATOM   1756 N N   . ARG   A 1 229 ? 10.852  26.642 -34.952 1.00 41.52  ? 240 ARG   A N   1 
ATOM   1757 C CA  . ARG   A 1 229 ? 10.421  27.171 -33.661 1.00 47.89  ? 240 ARG   A CA  1 
ATOM   1758 C C   . ARG   A 1 229 ? 9.976   28.641 -33.719 1.00 48.96  ? 240 ARG   A C   1 
ATOM   1759 O O   . ARG   A 1 229 ? 9.148   29.065 -32.907 1.00 44.92  ? 240 ARG   A O   1 
ATOM   1760 C CB  . ARG   A 1 229 ? 11.557  27.021 -32.642 1.00 53.08  ? 240 ARG   A CB  1 
ATOM   1761 C CG  . ARG   A 1 229 ? 12.757  27.866 -33.040 1.00 59.00  ? 240 ARG   A CG  1 
ATOM   1762 C CD  . ARG   A 1 229 ? 14.034  27.587 -32.262 1.00 64.96  ? 240 ARG   A CD  1 
ATOM   1763 N NE  . ARG   A 1 229 ? 15.163  28.349 -32.812 1.00 70.81  ? 240 ARG   A NE  1 
ATOM   1764 C CZ  . ARG   A 1 229 ? 15.606  28.287 -34.077 1.00 82.17  ? 240 ARG   A CZ  1 
ATOM   1765 N NH1 . ARG   A 1 229 ? 15.116  27.396 -34.931 1.00 85.69  ? 240 ARG   A NH1 1 
ATOM   1766 N NH2 . ARG   A 1 229 ? 16.559  29.111 -34.490 1.00 84.01  ? 240 ARG   A NH2 1 
ATOM   1767 N N   . LYS   A 1 230 ? 10.534  29.426 -34.656 1.00 49.61  ? 241 LYS   A N   1 
ATOM   1768 C CA  . LYS   A 1 230 ? 10.318  30.868 -34.693 1.00 49.74  ? 241 LYS   A CA  1 
ATOM   1769 C C   . LYS   A 1 230 ? 9.002   31.222 -35.390 1.00 46.81  ? 241 LYS   A C   1 
ATOM   1770 O O   . LYS   A 1 230 ? 8.387   32.230 -35.052 1.00 51.94  ? 241 LYS   A O   1 
ATOM   1771 C CB  . LYS   A 1 230 ? 11.498  31.576 -35.374 1.00 51.36  ? 241 LYS   A CB  1 
ATOM   1772 C CG  . LYS   A 1 230 ? 12.858  31.425 -34.693 1.00 53.02  ? 241 LYS   A CG  1 
ATOM   1773 C CD  . LYS   A 1 230 ? 12.876  31.905 -33.244 1.00 58.62  ? 241 LYS   A CD  1 
ATOM   1774 C CE  . LYS   A 1 230 ? 14.233  31.877 -32.593 1.00 63.58  ? 241 LYS   A CE  1 
ATOM   1775 N NZ  . LYS   A 1 230 ? 15.177  32.846 -33.167 1.00 65.09  ? 241 LYS   A NZ  1 
ATOM   1776 N N   . ILE   A 1 231 ? 8.573   30.392 -36.349 1.00 42.28  ? 242 ILE   A N   1 
ATOM   1777 C CA  . ILE   A 1 231 ? 7.416   30.674 -37.193 1.00 38.23  ? 242 ILE   A CA  1 
ATOM   1778 C C   . ILE   A 1 231 ? 6.143   30.420 -36.379 1.00 37.03  ? 242 ILE   A C   1 
ATOM   1779 O O   . ILE   A 1 231 ? 6.143   29.584 -35.482 1.00 35.14  ? 242 ILE   A O   1 
ATOM   1780 C CB  . ILE   A 1 231 ? 7.462   29.822 -38.485 1.00 35.43  ? 242 ILE   A CB  1 
ATOM   1781 C CG1 . ILE   A 1 231 ? 8.868   29.751 -39.128 1.00 33.38  ? 242 ILE   A CG1 1 
ATOM   1782 C CG2 . ILE   A 1 231 ? 6.398   30.257 -39.493 1.00 34.28  ? 242 ILE   A CG2 1 
ATOM   1783 C CD1 . ILE   A 1 231 ? 9.607   31.073 -39.212 1.00 34.11  ? 242 ILE   A CD1 1 
ATOM   1784 N N   . LYS   A 1 232 ? 5.065   31.163 -36.674 1.00 40.80  ? 243 LYS   A N   1 
ATOM   1785 C CA  . LYS   A 1 232 ? 3.771   30.940 -36.035 1.00 40.16  ? 243 LYS   A CA  1 
ATOM   1786 C C   . LYS   A 1 232 ? 2.656   30.806 -37.070 1.00 36.53  ? 243 LYS   A C   1 
ATOM   1787 O O   . LYS   A 1 232 ? 1.520   30.557 -36.685 1.00 34.84  ? 243 LYS   A O   1 
ATOM   1788 C CB  . LYS   A 1 232 ? 3.376   32.060 -35.070 1.00 42.36  ? 243 LYS   A CB  1 
ATOM   1789 C CG  . LYS   A 1 232 ? 4.506   32.558 -34.183 1.00 46.38  ? 243 LYS   A CG  1 
ATOM   1790 C CD  . LYS   A 1 232 ? 4.020   33.150 -32.868 1.00 46.82  ? 243 LYS   A CD  1 
ATOM   1791 C CE  . LYS   A 1 232 ? 4.938   34.209 -32.349 1.00 46.86  ? 243 LYS   A CE  1 
ATOM   1792 N NZ  . LYS   A 1 232 ? 4.313   34.887 -31.211 1.00 48.51  ? 243 LYS   A NZ  1 
ATOM   1793 N N   . ASP   A 1 233 ? 2.985   30.980 -38.361 1.00 34.55  ? 244 ASP   A N   1 
ATOM   1794 C CA  . ASP   A 1 233 ? 2.077   30.675 -39.454 1.00 32.52  ? 244 ASP   A CA  1 
ATOM   1795 C C   . ASP   A 1 233 ? 1.912   29.161 -39.591 1.00 33.61  ? 244 ASP   A C   1 
ATOM   1796 O O   . ASP   A 1 233 ? 2.832   28.451 -40.001 1.00 35.12  ? 244 ASP   A O   1 
ATOM   1797 C CB  . ASP   A 1 233 ? 2.550   31.303 -40.754 1.00 33.34  ? 244 ASP   A CB  1 
ATOM   1798 C CG  . ASP   A 1 233 ? 1.588   31.127 -41.918 1.00 34.46  ? 244 ASP   A CG  1 
ATOM   1799 O OD1 . ASP   A 1 233 ? 0.388   31.387 -41.709 1.00 34.63  ? 244 ASP   A OD1 1 
ATOM   1800 O OD2 . ASP   A 1 233 ? 2.035   30.716 -43.014 1.00 35.07  ? 244 ASP   A OD2 1 
ATOM   1801 N N   . LYS   A 1 234 ? 0.706   28.683 -39.265 1.00 33.71  ? 245 LYS   A N   1 
ATOM   1802 C CA  . LYS   A 1 234 ? 0.349   27.277 -39.335 1.00 33.25  ? 245 LYS   A CA  1 
ATOM   1803 C C   . LYS   A 1 234 ? 0.680   26.721 -40.717 1.00 32.64  ? 245 LYS   A C   1 
ATOM   1804 O O   . LYS   A 1 234 ? 1.174   25.605 -40.824 1.00 33.18  ? 245 LYS   A O   1 
ATOM   1805 C CB  . LYS   A 1 234 ? -1.149  27.168 -39.027 1.00 37.30  ? 245 LYS   A CB  1 
ATOM   1806 C CG  . LYS   A 1 234 ? -1.698  25.770 -38.733 1.00 43.01  ? 245 LYS   A CG  1 
ATOM   1807 C CD  . LYS   A 1 234 ? -3.225  25.609 -38.753 1.00 43.76  ? 245 LYS   A CD  1 
ATOM   1808 C CE  . LYS   A 1 234 ? -3.993  26.269 -37.641 1.00 43.15  ? 245 LYS   A CE  1 
ATOM   1809 N NZ  . LYS   A 1 234 ? -5.436  26.024 -37.757 1.00 43.31  ? 245 LYS   A NZ  1 
ATOM   1810 N N   . GLU   A 1 235 ? 0.392   27.495 -41.774 1.00 32.50  ? 246 GLU   A N   1 
ATOM   1811 C CA  . GLU   A 1 235 ? 0.587   27.021 -43.134 1.00 32.70  ? 246 GLU   A CA  1 
ATOM   1812 C C   . GLU   A 1 235 ? 2.074   26.933 -43.458 1.00 32.94  ? 246 GLU   A C   1 
ATOM   1813 O O   . GLU   A 1 235 ? 2.507   25.942 -44.031 1.00 37.29  ? 246 GLU   A O   1 
ATOM   1814 C CB  . GLU   A 1 235 ? -0.096  27.844 -44.221 1.00 33.17  ? 246 GLU   A CB  1 
ATOM   1815 C CG  . GLU   A 1 235 ? 0.080   27.226 -45.607 1.00 33.06  ? 246 GLU   A CG  1 
ATOM   1816 C CD  . GLU   A 1 235 ? -0.888  27.744 -46.653 1.00 34.91  ? 246 GLU   A CD  1 
ATOM   1817 O OE1 . GLU   A 1 235 ? -1.792  28.537 -46.305 1.00 37.76  ? 246 GLU   A OE1 1 
ATOM   1818 O OE2 . GLU   A 1 235 ? -0.729  27.372 -47.834 1.00 36.28  ? 246 GLU   A OE2 1 
ATOM   1819 N N   . GLN   A 1 236 ? 2.854   27.961 -43.121 1.00 31.02  ? 247 GLN   A N   1 
ATOM   1820 C CA  . GLN   A 1 236 ? 4.286   27.916 -43.380 1.00 31.49  ? 247 GLN   A CA  1 
ATOM   1821 C C   . GLN   A 1 236 ? 4.879   26.641 -42.780 1.00 27.98  ? 247 GLN   A C   1 
ATOM   1822 O O   . GLN   A 1 236 ? 5.382   25.777 -43.504 1.00 25.52  ? 247 GLN   A O   1 
ATOM   1823 C CB  . GLN   A 1 236 ? 4.967   29.156 -42.796 1.00 35.63  ? 247 GLN   A CB  1 
ATOM   1824 C CG  . GLN   A 1 236 ? 4.936   30.383 -43.702 1.00 38.24  ? 247 GLN   A CG  1 
ATOM   1825 C CD  . GLN   A 1 236 ? 5.648   30.154 -45.023 1.00 41.96  ? 247 GLN   A CD  1 
ATOM   1826 O OE1 . GLN   A 1 236 ? 6.866   29.927 -45.093 1.00 40.25  ? 247 GLN   A OE1 1 
ATOM   1827 N NE2 . GLN   A 1 236 ? 4.885   30.204 -46.104 1.00 43.93  ? 247 GLN   A NE2 1 
ATOM   1828 N N   . VAL   A 1 237 ? 4.760   26.548 -41.449 1.00 25.61  ? 248 VAL   A N   1 
ATOM   1829 C CA  . VAL   A 1 237 ? 5.346   25.494 -40.641 1.00 23.90  ? 248 VAL   A CA  1 
ATOM   1830 C C   . VAL   A 1 237 ? 5.173   24.166 -41.375 1.00 23.73  ? 248 VAL   A C   1 
ATOM   1831 O O   . VAL   A 1 237 ? 6.144   23.477 -41.658 1.00 22.32  ? 248 VAL   A O   1 
ATOM   1832 C CB  . VAL   A 1 237 ? 4.718   25.475 -39.228 1.00 22.55  ? 248 VAL   A CB  1 
ATOM   1833 C CG1 . VAL   A 1 237 ? 5.256   24.343 -38.366 1.00 22.23  ? 248 VAL   A CG1 1 
ATOM   1834 C CG2 . VAL   A 1 237 ? 4.895   26.789 -38.481 1.00 21.65  ? 248 VAL   A CG2 1 
ATOM   1835 N N   . GLY   A 1 238 ? 3.925   23.830 -41.699 1.00 26.77  ? 249 GLY   A N   1 
ATOM   1836 C CA  . GLY   A 1 238 ? 3.614   22.624 -42.449 1.00 30.47  ? 249 GLY   A CA  1 
ATOM   1837 C C   . GLY   A 1 238 ? 4.520   22.460 -43.671 1.00 34.76  ? 249 GLY   A C   1 
ATOM   1838 O O   . GLY   A 1 238 ? 5.118   21.401 -43.862 1.00 41.31  ? 249 GLY   A O   1 
ATOM   1839 N N   . MET   A 1 239 ? 4.631   23.521 -44.483 1.00 32.37  ? 250 MET   A N   1 
ATOM   1840 C CA  . MET   A 1 239 ? 5.353   23.463 -45.742 1.00 31.72  ? 250 MET   A CA  1 
ATOM   1841 C C   . MET   A 1 239 ? 6.826   23.140 -45.492 1.00 31.43  ? 250 MET   A C   1 
ATOM   1842 O O   . MET   A 1 239 ? 7.473   22.474 -46.293 1.00 30.36  ? 250 MET   A O   1 
ATOM   1843 C CB  . MET   A 1 239 ? 5.221   24.800 -46.478 1.00 34.49  ? 250 MET   A CB  1 
ATOM   1844 C CG  . MET   A 1 239 ? 4.091   24.870 -47.502 1.00 35.38  ? 250 MET   A CG  1 
ATOM   1845 S SD  . MET   A 1 239 ? 3.350   26.516 -47.641 1.00 36.46  ? 250 MET   A SD  1 
ATOM   1846 C CE  . MET   A 1 239 ? 4.816   27.551 -47.481 1.00 35.93  ? 250 MET   A CE  1 
ATOM   1847 N N   . ILE   A 1 240 ? 7.349   23.640 -44.371 1.00 32.16  ? 251 ILE   A N   1 
ATOM   1848 C CA  . ILE   A 1 240 ? 8.716   23.378 -43.958 1.00 32.99  ? 251 ILE   A CA  1 
ATOM   1849 C C   . ILE   A 1 240 ? 8.846   21.925 -43.505 1.00 34.70  ? 251 ILE   A C   1 
ATOM   1850 O O   . ILE   A 1 240 ? 9.760   21.222 -43.938 1.00 37.64  ? 251 ILE   A O   1 
ATOM   1851 C CB  . ILE   A 1 240 ? 9.124   24.345 -42.835 1.00 33.32  ? 251 ILE   A CB  1 
ATOM   1852 C CG1 . ILE   A 1 240 ? 9.107   25.806 -43.293 1.00 32.44  ? 251 ILE   A CG1 1 
ATOM   1853 C CG2 . ILE   A 1 240 ? 10.486  23.951 -42.280 1.00 35.57  ? 251 ILE   A CG2 1 
ATOM   1854 C CD1 . ILE   A 1 240 ? 9.283   26.824 -42.181 1.00 30.93  ? 251 ILE   A CD1 1 
ATOM   1855 N N   . LYS   A 1 241 ? 7.942   21.508 -42.605 1.00 34.53  ? 252 LYS   A N   1 
ATOM   1856 C CA  . LYS   A 1 241 ? 7.887   20.143 -42.095 1.00 34.92  ? 252 LYS   A CA  1 
ATOM   1857 C C   . LYS   A 1 241 ? 7.596   19.145 -43.207 1.00 36.63  ? 252 LYS   A C   1 
ATOM   1858 O O   . LYS   A 1 241 ? 7.926   17.970 -43.082 1.00 35.86  ? 252 LYS   A O   1 
ATOM   1859 C CB  . LYS   A 1 241 ? 6.744   19.898 -41.104 1.00 33.15  ? 252 LYS   A CB  1 
ATOM   1860 C CG  . LYS   A 1 241 ? 6.941   20.444 -39.702 1.00 32.39  ? 252 LYS   A CG  1 
ATOM   1861 C CD  . LYS   A 1 241 ? 5.635   20.532 -38.920 1.00 30.28  ? 252 LYS   A CD  1 
ATOM   1862 C CE  . LYS   A 1 241 ? 5.867   20.794 -37.474 1.00 28.91  ? 252 LYS   A CE  1 
ATOM   1863 N NZ  . LYS   A 1 241 ? 4.623   20.720 -36.713 1.00 28.72  ? 252 LYS   A NZ  1 
ATOM   1864 N N   . GLU   A 1 242 ? 6.915   19.606 -44.258 1.00 42.08  ? 253 GLU   A N   1 
ATOM   1865 C CA  . GLU   A 1 242 ? 6.548   18.719 -45.346 1.00 52.39  ? 253 GLU   A CA  1 
ATOM   1866 C C   . GLU   A 1 242 ? 7.766   18.504 -46.232 1.00 55.93  ? 253 GLU   A C   1 
ATOM   1867 O O   . GLU   A 1 242 ? 7.857   17.505 -46.932 1.00 56.03  ? 253 GLU   A O   1 
ATOM   1868 C CB  . GLU   A 1 242 ? 5.416   19.222 -46.242 1.00 56.62  ? 253 GLU   A CB  1 
ATOM   1869 C CG  . GLU   A 1 242 ? 4.727   18.080 -46.990 1.00 60.91  ? 253 GLU   A CG  1 
ATOM   1870 C CD  . GLU   A 1 242 ? 3.866   18.479 -48.179 1.00 64.96  ? 253 GLU   A CD  1 
ATOM   1871 O OE1 . GLU   A 1 242 ? 3.960   19.641 -48.644 1.00 68.69  ? 253 GLU   A OE1 1 
ATOM   1872 O OE2 . GLU   A 1 242 ? 3.087   17.608 -48.632 1.00 58.20  ? 253 GLU   A OE2 1 
ATOM   1873 N N   . LYS   A 1 243 ? 8.694   19.456 -46.187 1.00 61.75  ? 254 LYS   A N   1 
ATOM   1874 C CA  . LYS   A 1 243 ? 9.861   19.409 -47.046 1.00 66.82  ? 254 LYS   A CA  1 
ATOM   1875 C C   . LYS   A 1 243 ? 11.104  18.958 -46.276 1.00 81.23  ? 254 LYS   A C   1 
ATOM   1876 O O   . LYS   A 1 243 ? 12.064  18.517 -46.907 1.00 92.67  ? 254 LYS   A O   1 
ATOM   1877 C CB  . LYS   A 1 243 ? 9.942   20.776 -47.727 1.00 61.40  ? 254 LYS   A CB  1 
ATOM   1878 C CG  . LYS   A 1 243 ? 8.900   20.919 -48.822 1.00 60.48  ? 254 LYS   A CG  1 
ATOM   1879 C CD  . LYS   A 1 243 ? 9.425   20.579 -50.211 1.00 56.90  ? 254 LYS   A CD  1 
ATOM   1880 C CE  . LYS   A 1 243 ? 8.390   20.724 -51.277 1.00 55.12  ? 254 LYS   A CE  1 
ATOM   1881 N NZ  . LYS   A 1 243 ? 7.728   19.445 -51.517 1.00 56.72  ? 254 LYS   A NZ  1 
ATOM   1882 N N   . TYR   A 1 244 ? 11.080  18.998 -44.932 1.00 83.88  ? 255 TYR   A N   1 
ATOM   1883 C CA  . TYR   A 1 244 ? 12.297  18.802 -44.148 1.00 79.08  ? 255 TYR   A CA  1 
ATOM   1884 C C   . TYR   A 1 244 ? 12.680  17.322 -44.045 1.00 67.81  ? 255 TYR   A C   1 
ATOM   1885 O O   . TYR   A 1 244 ? 11.830  16.431 -43.984 1.00 62.69  ? 255 TYR   A O   1 
ATOM   1886 C CB  . TYR   A 1 244 ? 12.157  19.418 -42.752 1.00 82.34  ? 255 TYR   A CB  1 
ATOM   1887 C CG  . TYR   A 1 244 ? 13.457  19.608 -41.977 1.00 84.98  ? 255 TYR   A CG  1 
ATOM   1888 C CD1 . TYR   A 1 244 ? 14.359  20.609 -42.330 1.00 85.32  ? 255 TYR   A CD1 1 
ATOM   1889 C CD2 . TYR   A 1 244 ? 13.753  18.834 -40.858 1.00 82.20  ? 255 TYR   A CD2 1 
ATOM   1890 C CE1 . TYR   A 1 244 ? 15.530  20.809 -41.616 1.00 86.69  ? 255 TYR   A CE1 1 
ATOM   1891 C CE2 . TYR   A 1 244 ? 14.918  19.028 -40.135 1.00 83.41  ? 255 TYR   A CE2 1 
ATOM   1892 C CZ  . TYR   A 1 244 ? 15.809  20.018 -40.513 1.00 87.77  ? 255 TYR   A CZ  1 
ATOM   1893 O OH  . TYR   A 1 244 ? 16.962  20.198 -39.799 1.00 89.78  ? 255 TYR   A OH  1 
ATOM   1894 N N   . GLU   A 1 245 ? 13.995  17.080 -44.014 1.00 62.08  ? 256 GLU   A N   1 
ATOM   1895 C CA  . GLU   A 1 245 ? 14.524  15.753 -43.762 1.00 66.00  ? 256 GLU   A CA  1 
ATOM   1896 C C   . GLU   A 1 245 ? 14.532  15.527 -42.250 1.00 65.30  ? 256 GLU   A C   1 
ATOM   1897 O O   . GLU   A 1 245 ? 15.241  16.196 -41.495 1.00 56.95  ? 256 GLU   A O   1 
ATOM   1898 C CB  . GLU   A 1 245 ? 15.892  15.562 -44.422 1.00 70.46  ? 256 GLU   A CB  1 
ATOM   1899 C CG  . GLU   A 1 245 ? 16.508  14.177 -44.212 1.00 72.53  ? 256 GLU   A CG  1 
ATOM   1900 C CD  . GLU   A 1 245 ? 15.634  12.966 -44.537 1.00 67.31  ? 256 GLU   A CD  1 
ATOM   1901 O OE1 . GLU   A 1 245 ? 15.071  12.876 -45.656 1.00 64.72  ? 256 GLU   A OE1 1 
ATOM   1902 O OE2 . GLU   A 1 245 ? 15.529  12.090 -43.651 1.00 57.36  ? 256 GLU   A OE2 1 
ATOM   1903 N N   . HIS   A 1 246 ? 13.708  14.567 -41.824 1.00 64.59  ? 257 HIS   A N   1 
ATOM   1904 C CA  . HIS   A 1 246 ? 13.501  14.302 -40.414 1.00 58.94  ? 257 HIS   A CA  1 
ATOM   1905 C C   . HIS   A 1 246 ? 14.726  13.596 -39.842 1.00 58.59  ? 257 HIS   A C   1 
ATOM   1906 O O   . HIS   A 1 246 ? 14.956  13.650 -38.642 1.00 67.59  ? 257 HIS   A O   1 
ATOM   1907 C CB  . HIS   A 1 246 ? 12.143  13.616 -40.196 1.00 54.53  ? 257 HIS   A CB  1 
ATOM   1908 C CG  . HIS   A 1 246 ? 10.992  14.570 -40.279 1.00 51.92  ? 257 HIS   A CG  1 
ATOM   1909 N ND1 . HIS   A 1 246 ? 10.480  15.060 -41.463 1.00 50.54  ? 257 HIS   A ND1 1 
ATOM   1910 C CD2 . HIS   A 1 246 ? 10.291  15.160 -39.298 1.00 48.04  ? 257 HIS   A CD2 1 
ATOM   1911 C CE1 . HIS   A 1 246 ? 9.491   15.903 -41.189 1.00 49.85  ? 257 HIS   A CE1 1 
ATOM   1912 N NE2 . HIS   A 1 246 ? 9.366   15.988 -39.879 1.00 45.86  ? 257 HIS   A NE2 1 
ATOM   1913 N N   . ARG   A 1 247 ? 15.553  12.978 -40.686 1.00 55.03  ? 258 ARG   A N   1 
ATOM   1914 C CA  . ARG   A 1 247 ? 16.771  12.377 -40.169 1.00 54.86  ? 258 ARG   A CA  1 
ATOM   1915 C C   . ARG   A 1 247 ? 17.760  13.452 -39.723 1.00 48.57  ? 258 ARG   A C   1 
ATOM   1916 O O   . ARG   A 1 247 ? 18.608  13.168 -38.885 1.00 46.89  ? 258 ARG   A O   1 
ATOM   1917 C CB  . ARG   A 1 247 ? 17.421  11.394 -41.147 1.00 57.21  ? 258 ARG   A CB  1 
ATOM   1918 C CG  . ARG   A 1 247 ? 16.642  10.095 -41.257 1.00 57.92  ? 258 ARG   A CG  1 
ATOM   1919 C CD  . ARG   A 1 247 ? 17.546  8.948  -41.664 1.00 58.01  ? 258 ARG   A CD  1 
ATOM   1920 N NE  . ARG   A 1 247 ? 16.758  7.846  -42.222 1.00 55.65  ? 258 ARG   A NE  1 
ATOM   1921 C CZ  . ARG   A 1 247 ? 15.814  7.169  -41.587 1.00 51.84  ? 258 ARG   A CZ  1 
ATOM   1922 N NH1 . ARG   A 1 247 ? 15.572  7.390  -40.303 1.00 49.62  ? 258 ARG   A NH1 1 
ATOM   1923 N NH2 . ARG   A 1 247 ? 15.126  6.256  -42.249 1.00 51.09  ? 258 ARG   A NH2 1 
ATOM   1924 N N   . MET   A 1 248 ? 17.653  14.678 -40.252 1.00 46.65  ? 259 MET   A N   1 
ATOM   1925 C CA  A MET   A 1 248 ? 18.523  15.803 -39.927 0.50 50.13  ? 259 MET   A CA  1 
ATOM   1926 C CA  B MET   A 1 248 ? 18.644  15.666 -39.875 0.50 50.16  ? 259 MET   A CA  1 
ATOM   1927 C C   . MET   A 1 248 ? 18.380  16.199 -38.461 1.00 50.78  ? 259 MET   A C   1 
ATOM   1928 O O   . MET   A 1 248 ? 19.224  16.889 -37.896 1.00 53.37  ? 259 MET   A O   1 
ATOM   1929 C CB  A MET   A 1 248 ? 18.161  17.076 -40.711 0.50 51.75  ? 259 MET   A CB  1 
ATOM   1930 C CB  B MET   A 1 248 ? 18.739  16.740 -40.961 0.50 52.15  ? 259 MET   A CB  1 
ATOM   1931 C CG  A MET   A 1 248 ? 18.903  17.306 -42.027 0.50 52.01  ? 259 MET   A CG  1 
ATOM   1932 C CG  B MET   A 1 248 ? 19.178  16.161 -42.309 0.50 51.49  ? 259 MET   A CG  1 
ATOM   1933 S SD  A MET   A 1 248 ? 18.832  19.022 -42.605 0.50 46.22  ? 259 MET   A SD  1 
ATOM   1934 S SD  B MET   A 1 248 ? 20.434  14.868 -42.168 0.50 47.82  ? 259 MET   A SD  1 
ATOM   1935 C CE  A MET   A 1 248 ? 19.905  19.873 -41.440 0.50 44.87  ? 259 MET   A CE  1 
ATOM   1936 C CE  B MET   A 1 248 ? 21.803  15.747 -41.402 0.50 47.14  ? 259 MET   A CE  1 
ATOM   1937 N N   . LEU   A 1 249 ? 17.259  15.827 -37.849 1.00 48.82  ? 260 LEU   A N   1 
ATOM   1938 C CA  . LEU   A 1 249 ? 17.023  16.182 -36.459 1.00 45.65  ? 260 LEU   A CA  1 
ATOM   1939 C C   . LEU   A 1 249 ? 17.775  15.215 -35.550 1.00 41.56  ? 260 LEU   A C   1 
ATOM   1940 O O   . LEU   A 1 249 ? 18.166  15.551 -34.430 1.00 38.97  ? 260 LEU   A O   1 
ATOM   1941 C CB  . LEU   A 1 249 ? 15.516  16.107 -36.227 1.00 45.86  ? 260 LEU   A CB  1 
ATOM   1942 C CG  . LEU   A 1 249 ? 14.653  17.058 -37.061 1.00 41.66  ? 260 LEU   A CG  1 
ATOM   1943 C CD1 . LEU   A 1 249 ? 13.216  16.629 -37.044 1.00 39.72  ? 260 LEU   A CD1 1 
ATOM   1944 C CD2 . LEU   A 1 249 ? 14.767  18.466 -36.536 1.00 43.22  ? 260 LEU   A CD2 1 
ATOM   1945 N N   . LEU   A 1 250 ? 17.952  14.000 -36.072 1.00 40.08  ? 261 LEU   A N   1 
ATOM   1946 C CA  . LEU   A 1 250 ? 18.474  12.877 -35.317 1.00 42.25  ? 261 LEU   A CA  1 
ATOM   1947 C C   . LEU   A 1 250 ? 19.985  12.763 -35.467 1.00 42.30  ? 261 LEU   A C   1 
ATOM   1948 O O   . LEU   A 1 250 ? 20.554  11.695 -35.210 1.00 39.34  ? 261 LEU   A O   1 
ATOM   1949 C CB  . LEU   A 1 250 ? 17.788  11.633 -35.860 1.00 42.48  ? 261 LEU   A CB  1 
ATOM   1950 C CG  . LEU   A 1 250 ? 16.263  11.683 -35.828 1.00 46.26  ? 261 LEU   A CG  1 
ATOM   1951 C CD1 . LEU   A 1 250 ? 15.761  10.346 -36.312 1.00 49.94  ? 261 LEU   A CD1 1 
ATOM   1952 C CD2 . LEU   A 1 250 ? 15.736  12.011 -34.442 1.00 47.57  ? 261 LEU   A CD2 1 
ATOM   1953 N N   . LYS   A 1 251 ? 20.596  13.871 -35.909 1.00 43.05  ? 262 LYS   A N   1 
ATOM   1954 C CA  . LYS   A 1 251 ? 22.010  13.926 -36.219 1.00 40.33  ? 262 LYS   A CA  1 
ATOM   1955 C C   . LYS   A 1 251 ? 22.768  13.981 -34.907 1.00 37.02  ? 262 LYS   A C   1 
ATOM   1956 O O   . LYS   A 1 251 ? 23.887  13.490 -34.832 1.00 37.21  ? 262 LYS   A O   1 
ATOM   1957 C CB  . LYS   A 1 251 ? 22.325  15.149 -37.082 1.00 41.78  ? 262 LYS   A CB  1 
ATOM   1958 C CG  . LYS   A 1 251 ? 23.778  15.272 -37.505 1.00 44.92  ? 262 LYS   A CG  1 
ATOM   1959 C CD  . LYS   A 1 251 ? 24.185  16.696 -37.877 1.00 46.90  ? 262 LYS   A CD  1 
ATOM   1960 C CE  . LYS   A 1 251 ? 25.672  16.890 -37.851 1.00 47.13  ? 262 LYS   A CE  1 
ATOM   1961 N NZ  . LYS   A 1 251 ? 26.018  18.311 -37.808 1.00 46.99  ? 262 LYS   A NZ  1 
ATOM   1962 N N   . HIS   A 1 252 ? 22.125  14.568 -33.889 1.00 38.20  ? 263 HIS   A N   1 
ATOM   1963 C CA  . HIS   A 1 252 ? 22.703  14.684 -32.561 1.00 38.07  ? 263 HIS   A CA  1 
ATOM   1964 C C   . HIS   A 1 252 ? 21.875  13.859 -31.576 1.00 34.39  ? 263 HIS   A C   1 
ATOM   1965 O O   . HIS   A 1 252 ? 22.038  14.028 -30.375 1.00 36.11  ? 263 HIS   A O   1 
ATOM   1966 C CB  . HIS   A 1 252 ? 22.876  16.170 -32.196 1.00 40.11  ? 263 HIS   A CB  1 
ATOM   1967 C CG  . HIS   A 1 252 ? 23.776  16.928 -33.137 1.00 43.06  ? 263 HIS   A CG  1 
ATOM   1968 N ND1 . HIS   A 1 252 ? 25.106  17.198 -32.880 1.00 43.81  ? 263 HIS   A ND1 1 
ATOM   1969 C CD2 . HIS   A 1 252 ? 23.531  17.462 -34.353 1.00 44.21  ? 263 HIS   A CD2 1 
ATOM   1970 C CE1 . HIS   A 1 252 ? 25.640  17.860 -33.906 1.00 42.61  ? 263 HIS   A CE1 1 
ATOM   1971 N NE2 . HIS   A 1 252 ? 24.698  18.036 -34.810 1.00 43.90  ? 263 HIS   A NE2 1 
ATOM   1972 N N   . MET   A 1 253 ? 21.031  12.948 -32.088 1.00 32.86  ? 264 MET   A N   1 
ATOM   1973 C CA  . MET   A 1 253 ? 20.160  12.107 -31.275 1.00 33.08  ? 264 MET   A CA  1 
ATOM   1974 C C   . MET   A 1 253 ? 20.498  10.629 -31.458 1.00 30.96  ? 264 MET   A C   1 
ATOM   1975 O O   . MET   A 1 253 ? 20.820  10.187 -32.557 1.00 28.95  ? 264 MET   A O   1 
ATOM   1976 C CB  . MET   A 1 253 ? 18.698  12.218 -31.714 1.00 38.12  ? 264 MET   A CB  1 
ATOM   1977 C CG  . MET   A 1 253 ? 18.101  13.605 -31.620 1.00 43.05  ? 264 MET   A CG  1 
ATOM   1978 S SD  . MET   A 1 253 ? 17.562  13.881 -29.924 1.00 50.94  ? 264 MET   A SD  1 
ATOM   1979 C CE  . MET   A 1 253 ? 15.992  13.002 -29.843 1.00 51.19  ? 264 MET   A CE  1 
ATOM   1980 N N   . PRO   A 1 254 ? 20.356  9.796  -30.406 1.00 32.40  ? 265 PRO   A N   1 
ATOM   1981 C CA  . PRO   A 1 254 ? 20.583  8.347  -30.513 1.00 32.78  ? 265 PRO   A CA  1 
ATOM   1982 C C   . PRO   A 1 254 ? 20.139  7.649  -31.790 1.00 31.30  ? 265 PRO   A C   1 
ATOM   1983 O O   . PRO   A 1 254 ? 19.053  7.903  -32.275 1.00 28.86  ? 265 PRO   A O   1 
ATOM   1984 C CB  . PRO   A 1 254 ? 19.739  7.829  -29.340 1.00 33.58  ? 265 PRO   A CB  1 
ATOM   1985 C CG  . PRO   A 1 254 ? 19.901  8.884  -28.282 1.00 33.20  ? 265 PRO   A CG  1 
ATOM   1986 C CD  . PRO   A 1 254 ? 19.990  10.211 -29.036 1.00 33.23  ? 265 PRO   A CD  1 
ATOM   1987 N N   . SER   A 1 255 ? 20.909  6.654  -32.234 1.00 36.04  ? 266 SER   A N   1 
ATOM   1988 C CA  . SER   A 1 255 ? 20.655  6.003  -33.515 1.00 39.04  ? 266 SER   A CA  1 
ATOM   1989 C C   . SER   A 1 255 ? 19.437  5.072  -33.469 1.00 37.98  ? 266 SER   A C   1 
ATOM   1990 O O   . SER   A 1 255 ? 19.040  4.519  -34.503 1.00 37.15  ? 266 SER   A O   1 
ATOM   1991 C CB  . SER   A 1 255 ? 21.895  5.283  -34.029 1.00 40.68  ? 266 SER   A CB  1 
ATOM   1992 O OG  . SER   A 1 255 ? 22.176  4.060  -33.356 1.00 41.39  ? 266 SER   A OG  1 
ATOM   1993 N N   . GLU   A 1 256 ? 18.832  4.930  -32.282 1.00 37.11  ? 267 GLU   A N   1 
ATOM   1994 C CA  . GLU   A 1 256 ? 17.615  4.147  -32.118 1.00 38.72  ? 267 GLU   A CA  1 
ATOM   1995 C C   . GLU   A 1 256 ? 16.371  4.922  -32.581 1.00 33.50  ? 267 GLU   A C   1 
ATOM   1996 O O   . GLU   A 1 256 ? 15.302  4.339  -32.773 1.00 30.38  ? 267 GLU   A O   1 
ATOM   1997 C CB  . GLU   A 1 256 ? 17.615  3.714  -30.650 1.00 44.34  ? 267 GLU   A CB  1 
ATOM   1998 C CG  . GLU   A 1 256 ? 18.558  2.543  -30.365 1.00 49.02  ? 267 GLU   A CG  1 
ATOM   1999 C CD  . GLU   A 1 256 ? 17.964  1.138  -30.521 1.00 52.77  ? 267 GLU   A CD  1 
ATOM   2000 O OE1 . GLU   A 1 256 ? 16.749  0.953  -30.814 1.00 52.44  ? 267 GLU   A OE1 1 
ATOM   2001 O OE2 . GLU   A 1 256 ? 18.746  0.187  -30.318 1.00 54.82  ? 267 GLU   A OE2 1 
ATOM   2002 N N   . PHE   A 1 257 ? 16.525  6.241  -32.765 1.00 31.76  ? 268 PHE   A N   1 
ATOM   2003 C CA  . PHE   A 1 257 ? 15.453  7.124  -33.194 1.00 31.22  ? 268 PHE   A CA  1 
ATOM   2004 C C   . PHE   A 1 257 ? 15.373  7.201  -34.723 1.00 38.01  ? 268 PHE   A C   1 
ATOM   2005 O O   . PHE   A 1 257 ? 14.581  7.974  -35.251 1.00 40.98  ? 268 PHE   A O   1 
ATOM   2006 C CB  . PHE   A 1 257 ? 15.665  8.519  -32.591 1.00 28.00  ? 268 PHE   A CB  1 
ATOM   2007 C CG  . PHE   A 1 257 ? 15.247  8.720  -31.137 1.00 26.43  ? 268 PHE   A CG  1 
ATOM   2008 C CD1 . PHE   A 1 257 ? 15.831  7.994  -30.104 1.00 25.72  ? 268 PHE   A CD1 1 
ATOM   2009 C CD2 . PHE   A 1 257 ? 14.321  9.697  -30.789 1.00 25.26  ? 268 PHE   A CD2 1 
ATOM   2010 C CE1 . PHE   A 1 257 ? 15.454  8.189  -28.782 1.00 24.00  ? 268 PHE   A CE1 1 
ATOM   2011 C CE2 . PHE   A 1 257 ? 13.970  9.902  -29.463 1.00 24.93  ? 268 PHE   A CE2 1 
ATOM   2012 C CZ  . PHE   A 1 257 ? 14.528  9.138  -28.465 1.00 24.13  ? 268 PHE   A CZ  1 
ATOM   2013 N N   . HIS   A 1 258 ? 16.164  6.409  -35.456 1.00 43.81  ? 269 HIS   A N   1 
ATOM   2014 C CA  . HIS   A 1 258 ? 15.916  6.235  -36.880 1.00 47.64  ? 269 HIS   A CA  1 
ATOM   2015 C C   . HIS   A 1 258 ? 14.824  5.177  -37.078 1.00 47.44  ? 269 HIS   A C   1 
ATOM   2016 O O   . HIS   A 1 258 ? 14.225  5.061  -38.148 1.00 47.65  ? 269 HIS   A O   1 
ATOM   2017 C CB  . HIS   A 1 258 ? 17.227  5.943  -37.622 1.00 51.31  ? 269 HIS   A CB  1 
ATOM   2018 C CG  . HIS   A 1 258 ? 18.247  7.036  -37.532 1.00 56.37  ? 269 HIS   A CG  1 
ATOM   2019 N ND1 . HIS   A 1 258 ? 18.192  8.199  -38.277 1.00 58.33  ? 269 HIS   A ND1 1 
ATOM   2020 C CD2 . HIS   A 1 258 ? 19.361  7.132  -36.784 1.00 56.67  ? 269 HIS   A CD2 1 
ATOM   2021 C CE1 . HIS   A 1 258 ? 19.237  8.965  -37.980 1.00 58.48  ? 269 HIS   A CE1 1 
ATOM   2022 N NE2 . HIS   A 1 258 ? 19.962  8.335  -37.075 1.00 58.32  ? 269 HIS   A NE2 1 
ATOM   2023 N N   . LEU   A 1 259 ? 14.538  4.409  -36.028 1.00 45.25  ? 270 LEU   A N   1 
ATOM   2024 C CA  . LEU   A 1 259 ? 13.500  3.399  -36.104 1.00 48.72  ? 270 LEU   A CA  1 
ATOM   2025 C C   . LEU   A 1 259 ? 12.154  4.050  -35.800 1.00 45.53  ? 270 LEU   A C   1 
ATOM   2026 O O   . LEU   A 1 259 ? 11.207  3.934  -36.579 1.00 44.09  ? 270 LEU   A O   1 
ATOM   2027 C CB  . LEU   A 1 259 ? 13.834  2.282  -35.119 1.00 53.47  ? 270 LEU   A CB  1 
ATOM   2028 C CG  . LEU   A 1 259 ? 15.295  1.822  -35.099 1.00 57.62  ? 270 LEU   A CG  1 
ATOM   2029 C CD1 . LEU   A 1 259 ? 15.444  0.635  -34.145 1.00 54.78  ? 270 LEU   A CD1 1 
ATOM   2030 C CD2 . LEU   A 1 259 ? 15.813  1.498  -36.512 1.00 58.20  ? 270 LEU   A CD2 1 
ATOM   2031 N N   . PHE   A 1 260 ? 12.099  4.742  -34.655 1.00 41.59  ? 271 PHE   A N   1 
ATOM   2032 C CA  . PHE   A 1 260 ? 10.909  5.461  -34.233 1.00 38.28  ? 271 PHE   A CA  1 
ATOM   2033 C C   . PHE   A 1 260 ? 10.402  6.270  -35.429 1.00 35.13  ? 271 PHE   A C   1 
ATOM   2034 O O   . PHE   A 1 260 ? 9.221   6.212  -35.754 1.00 35.80  ? 271 PHE   A O   1 
ATOM   2035 C CB  . PHE   A 1 260 ? 11.334  6.180  -32.943 1.00 37.08  ? 271 PHE   A CB  1 
ATOM   2036 C CG  . PHE   A 1 260 ? 10.317  7.008  -32.163 1.00 35.68  ? 271 PHE   A CG  1 
ATOM   2037 C CD1 . PHE   A 1 260 ? 8.987   7.115  -32.550 1.00 36.78  ? 271 PHE   A CD1 1 
ATOM   2038 C CD2 . PHE   A 1 260 ? 10.702  7.664  -31.000 1.00 34.85  ? 271 PHE   A CD2 1 
ATOM   2039 C CE1 . PHE   A 1 260 ? 8.089   7.888  -31.825 1.00 35.79  ? 271 PHE   A CE1 1 
ATOM   2040 C CE2 . PHE   A 1 260 ? 9.799   8.418  -30.269 1.00 34.83  ? 271 PHE   A CE2 1 
ATOM   2041 C CZ  . PHE   A 1 260 ? 8.494   8.527  -30.682 1.00 35.47  ? 271 PHE   A CZ  1 
ATOM   2042 N N   . LEU   A 1 261 ? 11.309  6.954  -36.135 1.00 33.16  ? 272 LEU   A N   1 
ATOM   2043 C CA  . LEU   A 1 261 ? 10.915  7.802  -37.250 1.00 32.19  ? 272 LEU   A CA  1 
ATOM   2044 C C   . LEU   A 1 261 ? 10.387  6.952  -38.402 1.00 31.15  ? 272 LEU   A C   1 
ATOM   2045 O O   . LEU   A 1 261 ? 9.400   7.340  -39.014 1.00 30.17  ? 272 LEU   A O   1 
ATOM   2046 C CB  . LEU   A 1 261 ? 12.048  8.719  -37.719 1.00 31.69  ? 272 LEU   A CB  1 
ATOM   2047 C CG  . LEU   A 1 261 ? 11.728  9.658  -38.889 1.00 30.83  ? 272 LEU   A CG  1 
ATOM   2048 C CD1 . LEU   A 1 261 ? 10.648  10.674 -38.562 1.00 31.21  ? 272 LEU   A CD1 1 
ATOM   2049 C CD2 . LEU   A 1 261 ? 12.986  10.365 -39.338 1.00 31.02  ? 272 LEU   A CD2 1 
ATOM   2050 N N   . ASP   A 1 262 ? 11.038  5.820  -38.714 1.00 31.31  ? 273 ASP   A N   1 
ATOM   2051 C CA  . ASP   A 1 262 ? 10.629  5.013  -39.861 1.00 33.44  ? 273 ASP   A CA  1 
ATOM   2052 C C   . ASP   A 1 262 ? 9.242   4.405  -39.606 1.00 32.09  ? 273 ASP   A C   1 
ATOM   2053 O O   . ASP   A 1 262 ? 8.432   4.228  -40.532 1.00 30.02  ? 273 ASP   A O   1 
ATOM   2054 C CB  . ASP   A 1 262 ? 11.686  3.981  -40.245 1.00 34.31  ? 273 ASP   A CB  1 
ATOM   2055 C CG  . ASP   A 1 262 ? 12.655  4.371  -41.358 1.00 35.80  ? 273 ASP   A CG  1 
ATOM   2056 O OD1 . ASP   A 1 262 ? 12.190  4.888  -42.405 1.00 32.86  ? 273 ASP   A OD1 1 
ATOM   2057 O OD2 . ASP   A 1 262 ? 13.875  4.117  -41.189 1.00 39.44  ? 273 ASP   A OD2 1 
ATOM   2058 N N   . HIS   A 1 263 ? 8.978   4.125  -38.323 1.00 30.04  ? 274 HIS   A N   1 
ATOM   2059 C CA  . HIS   A 1 263 ? 7.802   3.396  -37.896 1.00 29.03  ? 274 HIS   A CA  1 
ATOM   2060 C C   . HIS   A 1 263 ? 6.564   4.266  -38.044 1.00 27.70  ? 274 HIS   A C   1 
ATOM   2061 O O   . HIS   A 1 263 ? 5.536   3.812  -38.539 1.00 27.84  ? 274 HIS   A O   1 
ATOM   2062 C CB  . HIS   A 1 263 ? 7.965   2.949  -36.443 1.00 29.19  ? 274 HIS   A CB  1 
ATOM   2063 C CG  . HIS   A 1 263 ? 6.763   2.250  -35.932 1.00 29.74  ? 274 HIS   A CG  1 
ATOM   2064 N ND1 . HIS   A 1 263 ? 6.277   1.096  -36.508 1.00 30.51  ? 274 HIS   A ND1 1 
ATOM   2065 C CD2 . HIS   A 1 263 ? 5.917   2.566  -34.958 1.00 30.95  ? 274 HIS   A CD2 1 
ATOM   2066 C CE1 . HIS   A 1 263 ? 5.194   0.703  -35.855 1.00 30.99  ? 274 HIS   A CE1 1 
ATOM   2067 N NE2 . HIS   A 1 263 ? 4.957   1.582  -34.910 1.00 31.68  ? 274 HIS   A NE2 1 
ATOM   2068 N N   . ILE   A 1 264 ? 6.679   5.516  -37.601 1.00 26.19  ? 275 ILE   A N   1 
ATOM   2069 C CA  . ILE   A 1 264 ? 5.541   6.409  -37.590 1.00 24.89  ? 275 ILE   A CA  1 
ATOM   2070 C C   . ILE   A 1 264 ? 5.327   6.972  -38.990 1.00 25.44  ? 275 ILE   A C   1 
ATOM   2071 O O   . ILE   A 1 264 ? 4.190   7.218  -39.367 1.00 28.44  ? 275 ILE   A O   1 
ATOM   2072 C CB  . ILE   A 1 264 ? 5.688   7.490  -36.502 1.00 25.04  ? 275 ILE   A CB  1 
ATOM   2073 C CG1 . ILE   A 1 264 ? 6.892   8.382  -36.705 1.00 23.85  ? 275 ILE   A CG1 1 
ATOM   2074 C CG2 . ILE   A 1 264 ? 5.701   6.859  -35.103 1.00 25.52  ? 275 ILE   A CG2 1 
ATOM   2075 C CD1 . ILE   A 1 264 ? 7.106   9.339  -35.551 1.00 23.53  ? 275 ILE   A CD1 1 
ATOM   2076 N N   . ALA   A 1 265 ? 6.392   7.121  -39.789 1.00 26.74  ? 276 ALA   A N   1 
ATOM   2077 C CA  . ALA   A 1 265 ? 6.242   7.572  -41.172 1.00 26.83  ? 276 ALA   A CA  1 
ATOM   2078 C C   . ALA   A 1 265 ? 5.529   6.516  -41.999 1.00 27.23  ? 276 ALA   A C   1 
ATOM   2079 O O   . ALA   A 1 265 ? 5.084   6.826  -43.104 1.00 26.75  ? 276 ALA   A O   1 
ATOM   2080 C CB  . ALA   A 1 265 ? 7.573   7.900  -41.815 1.00 26.41  ? 276 ALA   A CB  1 
ATOM   2081 N N   . SER   A 1 266 ? 5.466   5.291  -41.448 1.00 27.81  ? 277 SER   A N   1 
ATOM   2082 C CA  . SER   A 1 266 ? 4.860   4.145  -42.100 1.00 30.65  ? 277 SER   A CA  1 
ATOM   2083 C C   . SER   A 1 266 ? 3.522   3.757  -41.456 1.00 31.89  ? 277 SER   A C   1 
ATOM   2084 O O   . SER   A 1 266 ? 3.126   2.593  -41.482 1.00 34.65  ? 277 SER   A O   1 
ATOM   2085 C CB  . SER   A 1 266 ? 5.839   3.003  -42.079 1.00 33.59  ? 277 SER   A CB  1 
ATOM   2086 O OG  . SER   A 1 266 ? 6.222   2.685  -40.745 1.00 37.81  ? 277 SER   A OG  1 
ATOM   2087 N N   . LEU   A 1 267 ? 2.794   4.721  -40.886 1.00 31.56  ? 278 LEU   A N   1 
ATOM   2088 C CA  . LEU   A 1 267 ? 1.505   4.425  -40.280 1.00 31.48  ? 278 LEU   A CA  1 
ATOM   2089 C C   . LEU   A 1 267 ? 0.459   5.315  -40.945 1.00 29.69  ? 278 LEU   A C   1 
ATOM   2090 O O   . LEU   A 1 267 ? 0.799   6.365  -41.485 1.00 26.91  ? 278 LEU   A O   1 
ATOM   2091 C CB  . LEU   A 1 267 ? 1.493   4.625  -38.756 1.00 35.13  ? 278 LEU   A CB  1 
ATOM   2092 C CG  . LEU   A 1 267 ? 2.126   3.558  -37.841 1.00 36.89  ? 278 LEU   A CG  1 
ATOM   2093 C CD1 . LEU   A 1 267 ? 2.102   4.038  -36.386 1.00 36.19  ? 278 LEU   A CD1 1 
ATOM   2094 C CD2 . LEU   A 1 267 ? 1.485   2.169  -37.887 1.00 37.96  ? 278 LEU   A CD2 1 
ATOM   2095 N N   . ASP   A 1 268 ? -0.809  4.873  -40.865 1.00 29.19  ? 279 ASP   A N   1 
ATOM   2096 C CA  . ASP   A 1 268 ? -1.977  5.651  -41.249 1.00 28.68  ? 279 ASP   A CA  1 
ATOM   2097 C C   . ASP   A 1 268 ? -2.928  5.698  -40.049 1.00 28.60  ? 279 ASP   A C   1 
ATOM   2098 O O   . ASP   A 1 268 ? -2.609  5.138  -39.002 1.00 26.02  ? 279 ASP   A O   1 
ATOM   2099 C CB  . ASP   A 1 268 ? -2.618  5.048  -42.491 1.00 28.93  ? 279 ASP   A CB  1 
ATOM   2100 C CG  . ASP   A 1 268 ? -3.010  3.582  -42.353 1.00 30.59  ? 279 ASP   A CG  1 
ATOM   2101 O OD1 . ASP   A 1 268 ? -3.095  3.095  -41.197 1.00 32.89  ? 279 ASP   A OD1 1 
ATOM   2102 O OD2 . ASP   A 1 268 ? -3.193  2.924  -43.395 1.00 30.34  ? 279 ASP   A OD2 1 
ATOM   2103 N N   . TYR   A 1 269 ? -4.091  6.354  -40.225 1.00 30.17  ? 280 TYR   A N   1 
ATOM   2104 C CA  . TYR   A 1 269 ? -5.176  6.405  -39.248 1.00 31.33  ? 280 TYR   A CA  1 
ATOM   2105 C C   . TYR   A 1 269 ? -5.415  5.052  -38.565 1.00 33.63  ? 280 TYR   A C   1 
ATOM   2106 O O   . TYR   A 1 269 ? -5.420  4.956  -37.328 1.00 34.45  ? 280 TYR   A O   1 
ATOM   2107 C CB  . TYR   A 1 269 ? -6.432  6.859  -39.997 1.00 29.86  ? 280 TYR   A CB  1 
ATOM   2108 C CG  . TYR   A 1 269 ? -7.693  7.086  -39.169 1.00 30.67  ? 280 TYR   A CG  1 
ATOM   2109 C CD1 . TYR   A 1 269 ? -7.768  8.112  -38.237 1.00 31.36  ? 280 TYR   A CD1 1 
ATOM   2110 C CD2 . TYR   A 1 269 ? -8.847  6.333  -39.376 1.00 31.53  ? 280 TYR   A CD2 1 
ATOM   2111 C CE1 . TYR   A 1 269 ? -8.926  8.343  -37.503 1.00 33.03  ? 280 TYR   A CE1 1 
ATOM   2112 C CE2 . TYR   A 1 269 ? -10.013 6.559  -38.655 1.00 32.46  ? 280 TYR   A CE2 1 
ATOM   2113 C CZ  . TYR   A 1 269 ? -10.061 7.571  -37.708 1.00 32.53  ? 280 TYR   A CZ  1 
ATOM   2114 O OH  . TYR   A 1 269 ? -11.204 7.821  -36.985 1.00 30.49  ? 280 TYR   A OH  1 
ATOM   2115 N N   . PHE   A 1 270 ? -5.589  4.013  -39.398 1.00 32.49  ? 281 PHE   A N   1 
ATOM   2116 C CA  . PHE   A 1 270 ? -6.117  2.719  -38.987 1.00 31.31  ? 281 PHE   A CA  1 
ATOM   2117 C C   . PHE   A 1 270 ? -5.065  1.936  -38.219 1.00 29.01  ? 281 PHE   A C   1 
ATOM   2118 O O   . PHE   A 1 270 ? -5.307  1.524  -37.090 1.00 27.58  ? 281 PHE   A O   1 
ATOM   2119 C CB  . PHE   A 1 270 ? -6.529  1.893  -40.208 1.00 31.33  ? 281 PHE   A CB  1 
ATOM   2120 C CG  . PHE   A 1 270 ? -7.511  2.637  -41.100 1.00 31.60  ? 281 PHE   A CG  1 
ATOM   2121 C CD1 . PHE   A 1 270 ? -8.881  2.541  -40.878 1.00 30.11  ? 281 PHE   A CD1 1 
ATOM   2122 C CD2 . PHE   A 1 270 ? -7.054  3.476  -42.117 1.00 32.82  ? 281 PHE   A CD2 1 
ATOM   2123 C CE1 . PHE   A 1 270 ? -9.770  3.239  -41.673 1.00 30.78  ? 281 PHE   A CE1 1 
ATOM   2124 C CE2 . PHE   A 1 270 ? -7.949  4.187  -42.901 1.00 32.37  ? 281 PHE   A CE2 1 
ATOM   2125 C CZ  . PHE   A 1 270 ? -9.304  4.057  -42.683 1.00 31.73  ? 281 PHE   A CZ  1 
ATOM   2126 N N   . THR   A 1 271 ? -3.908  1.759  -38.864 1.00 27.59  ? 282 THR   A N   1 
ATOM   2127 C CA  . THR   A 1 271 ? -2.875  0.857  -38.393 1.00 26.74  ? 282 THR   A CA  1 
ATOM   2128 C C   . THR   A 1 271 ? -2.459  1.235  -36.978 1.00 27.94  ? 282 THR   A C   1 
ATOM   2129 O O   . THR   A 1 271 ? -2.036  2.361  -36.729 1.00 27.37  ? 282 THR   A O   1 
ATOM   2130 C CB  . THR   A 1 271 ? -1.697  0.921  -39.353 1.00 25.29  ? 282 THR   A CB  1 
ATOM   2131 O OG1 . THR   A 1 271 ? -2.339  0.870  -40.621 1.00 24.90  ? 282 THR   A OG1 1 
ATOM   2132 C CG2 . THR   A 1 271 ? -0.719  -0.216 -39.134 1.00 24.66  ? 282 THR   A CG2 1 
ATOM   2133 N N   . LYS   A 1 272 ? -2.590  0.265  -36.069 1.00 30.52  ? 283 LYS   A N   1 
ATOM   2134 C CA  . LYS   A 1 272 ? -2.229  0.441  -34.675 1.00 33.18  ? 283 LYS   A CA  1 
ATOM   2135 C C   . LYS   A 1 272 ? -0.716  0.581  -34.539 1.00 33.37  ? 283 LYS   A C   1 
ATOM   2136 O O   . LYS   A 1 272 ? 0.050   -0.147 -35.169 1.00 33.36  ? 283 LYS   A O   1 
ATOM   2137 C CB  . LYS   A 1 272 ? -2.715  -0.737 -33.826 1.00 37.00  ? 283 LYS   A CB  1 
ATOM   2138 C CG  . LYS   A 1 272 ? -1.870  -1.017 -32.595 1.00 38.94  ? 283 LYS   A CG  1 
ATOM   2139 C CD  . LYS   A 1 272 ? -2.600  -1.886 -31.592 1.00 41.73  ? 283 LYS   A CD  1 
ATOM   2140 C CE  . LYS   A 1 272 ? -1.640  -2.364 -30.566 1.00 46.59  ? 283 LYS   A CE  1 
ATOM   2141 N NZ  . LYS   A 1 272 ? -2.350  -2.823 -29.370 1.00 51.82  ? 283 LYS   A NZ  1 
ATOM   2142 N N   . PRO   A 1 273 ? -0.225  1.515  -33.697 1.00 32.36  ? 284 PRO   A N   1 
ATOM   2143 C CA  . PRO   A 1 273 ? 1.211   1.654  -33.493 1.00 31.15  ? 284 PRO   A CA  1 
ATOM   2144 C C   . PRO   A 1 273 ? 1.766   0.541  -32.603 1.00 30.40  ? 284 PRO   A C   1 
ATOM   2145 O O   . PRO   A 1 273 ? 1.035   -0.036 -31.798 1.00 27.73  ? 284 PRO   A O   1 
ATOM   2146 C CB  . PRO   A 1 273 ? 1.356   3.063  -32.874 1.00 30.83  ? 284 PRO   A CB  1 
ATOM   2147 C CG  . PRO   A 1 273 ? -0.034  3.673  -32.905 1.00 31.45  ? 284 PRO   A CG  1 
ATOM   2148 C CD  . PRO   A 1 273 ? -1.006  2.513  -32.949 1.00 32.25  ? 284 PRO   A CD  1 
ATOM   2149 N N   . ASP   A 1 274 ? 3.064   0.252  -32.811 1.00 31.23  ? 285 ASP   A N   1 
ATOM   2150 C CA  . ASP   A 1 274 ? 3.855   -0.654 -31.994 1.00 31.83  ? 285 ASP   A CA  1 
ATOM   2151 C C   . ASP   A 1 274 ? 4.500   0.112  -30.847 1.00 31.39  ? 285 ASP   A C   1 
ATOM   2152 O O   . ASP   A 1 274 ? 5.581   0.683  -31.011 1.00 29.81  ? 285 ASP   A O   1 
ATOM   2153 C CB  . ASP   A 1 274 ? 4.969   -1.328 -32.784 1.00 33.10  ? 285 ASP   A CB  1 
ATOM   2154 C CG  . ASP   A 1 274 ? 5.753   -2.386 -32.010 1.00 35.12  ? 285 ASP   A CG  1 
ATOM   2155 O OD1 . ASP   A 1 274 ? 5.366   -2.708 -30.856 1.00 35.96  ? 285 ASP   A OD1 1 
ATOM   2156 O OD2 . ASP   A 1 274 ? 6.746   -2.891 -32.556 1.00 36.90  ? 285 ASP   A OD2 1 
ATOM   2157 N N   . TYR   A 1 275 ? 3.841   0.062  -29.683 1.00 31.68  ? 286 TYR   A N   1 
ATOM   2158 C CA  . TYR   A 1 275 ? 4.185   0.908  -28.550 1.00 31.61  ? 286 TYR   A CA  1 
ATOM   2159 C C   . TYR   A 1 275 ? 5.474   0.409  -27.907 1.00 31.97  ? 286 TYR   A C   1 
ATOM   2160 O O   . TYR   A 1 275 ? 6.286   1.199  -27.429 1.00 31.36  ? 286 TYR   A O   1 
ATOM   2161 C CB  . TYR   A 1 275 ? 2.958   0.914  -27.633 1.00 30.54  ? 286 TYR   A CB  1 
ATOM   2162 C CG  . TYR   A 1 275 ? 1.758   1.667  -28.204 1.00 27.60  ? 286 TYR   A CG  1 
ATOM   2163 C CD1 . TYR   A 1 275 ? 1.655   3.046  -28.038 1.00 28.00  ? 286 TYR   A CD1 1 
ATOM   2164 C CD2 . TYR   A 1 275 ? 0.743   1.024  -28.905 1.00 24.56  ? 286 TYR   A CD2 1 
ATOM   2165 C CE1 . TYR   A 1 275 ? 0.586   3.765  -28.544 1.00 25.86  ? 286 TYR   A CE1 1 
ATOM   2166 C CE2 . TYR   A 1 275 ? -0.332  1.734  -29.416 1.00 24.28  ? 286 TYR   A CE2 1 
ATOM   2167 C CZ  . TYR   A 1 275 ? -0.407  3.105  -29.230 1.00 23.97  ? 286 TYR   A CZ  1 
ATOM   2168 O OH  . TYR   A 1 275 ? -1.407  3.900  -29.669 1.00 23.32  ? 286 TYR   A OH  1 
ATOM   2169 N N   . GLN   A 1 276 ? 5.656   -0.910 -27.987 1.00 35.09  ? 287 GLN   A N   1 
ATOM   2170 C CA  . GLN   A 1 276 ? 6.775   -1.624 -27.390 1.00 37.79  ? 287 GLN   A CA  1 
ATOM   2171 C C   . GLN   A 1 276 ? 8.070   -1.220 -28.091 1.00 33.58  ? 287 GLN   A C   1 
ATOM   2172 O O   . GLN   A 1 276 ? 9.059   -0.885 -27.440 1.00 31.75  ? 287 GLN   A O   1 
ATOM   2173 C CB  . GLN   A 1 276 ? 6.458   -3.112 -27.534 1.00 43.58  ? 287 GLN   A CB  1 
ATOM   2174 C CG  . GLN   A 1 276 ? 4.955   -3.395 -27.523 1.00 50.38  ? 287 GLN   A CG  1 
ATOM   2175 C CD  . GLN   A 1 276 ? 4.582   -4.805 -27.122 1.00 55.06  ? 287 GLN   A CD  1 
ATOM   2176 O OE1 . GLN   A 1 276 ? 4.774   -5.757 -27.891 1.00 55.21  ? 287 GLN   A OE1 1 
ATOM   2177 N NE2 . GLN   A 1 276 ? 4.010   -4.941 -25.929 1.00 54.93  ? 287 GLN   A NE2 1 
ATOM   2178 N N   . LEU   A 1 277 ? 8.020   -1.226 -29.430 1.00 30.40  ? 288 LEU   A N   1 
ATOM   2179 C CA  . LEU   A 1 277 ? 9.125   -0.769 -30.247 1.00 28.20  ? 288 LEU   A CA  1 
ATOM   2180 C C   . LEU   A 1 277 ? 9.610   0.576  -29.717 1.00 27.71  ? 288 LEU   A C   1 
ATOM   2181 O O   . LEU   A 1 277 ? 10.782  0.720  -29.398 1.00 27.26  ? 288 LEU   A O   1 
ATOM   2182 C CB  . LEU   A 1 277 ? 8.724   -0.709 -31.720 1.00 27.93  ? 288 LEU   A CB  1 
ATOM   2183 C CG  . LEU   A 1 277 ? 9.789   -0.192 -32.697 1.00 28.38  ? 288 LEU   A CG  1 
ATOM   2184 C CD1 . LEU   A 1 277 ? 9.645   -0.834 -34.064 1.00 27.77  ? 288 LEU   A CD1 1 
ATOM   2185 C CD2 . LEU   A 1 277 ? 9.734   1.318  -32.863 1.00 29.53  ? 288 LEU   A CD2 1 
ATOM   2186 N N   . ILE   A 1 278 ? 8.705   1.543  -29.585 1.00 28.49  ? 289 ILE   A N   1 
ATOM   2187 C CA  . ILE   A 1 278 ? 9.111   2.895  -29.254 1.00 29.87  ? 289 ILE   A CA  1 
ATOM   2188 C C   . ILE   A 1 278 ? 9.573   2.943  -27.808 1.00 28.37  ? 289 ILE   A C   1 
ATOM   2189 O O   . ILE   A 1 278 ? 10.417  3.763  -27.471 1.00 28.43  ? 289 ILE   A O   1 
ATOM   2190 C CB  . ILE   A 1 278 ? 7.986   3.914  -29.491 1.00 35.61  ? 289 ILE   A CB  1 
ATOM   2191 C CG1 . ILE   A 1 278 ? 7.339   3.753  -30.874 1.00 38.52  ? 289 ILE   A CG1 1 
ATOM   2192 C CG2 . ILE   A 1 278 ? 8.517   5.338  -29.287 1.00 37.40  ? 289 ILE   A CG2 1 
ATOM   2193 C CD1 . ILE   A 1 278 ? 5.969   4.404  -30.992 1.00 38.55  ? 289 ILE   A CD1 1 
ATOM   2194 N N   . MET   A 1 279 ? 8.997   2.090  -26.957 1.00 28.34  ? 290 MET   A N   1 
ATOM   2195 C CA  . MET   A 1 279 ? 9.464   1.964  -25.587 1.00 30.54  ? 290 MET   A CA  1 
ATOM   2196 C C   . MET   A 1 279 ? 10.878  1.376  -25.513 1.00 32.28  ? 290 MET   A C   1 
ATOM   2197 O O   . MET   A 1 279 ? 11.573  1.605  -24.529 1.00 32.64  ? 290 MET   A O   1 
ATOM   2198 C CB  . MET   A 1 279 ? 8.524   1.089  -24.762 1.00 32.39  ? 290 MET   A CB  1 
ATOM   2199 C CG  . MET   A 1 279 ? 8.892   1.045  -23.301 1.00 34.08  ? 290 MET   A CG  1 
ATOM   2200 S SD  . MET   A 1 279 ? 8.858   2.692  -22.568 1.00 35.65  ? 290 MET   A SD  1 
ATOM   2201 C CE  . MET   A 1 279 ? 7.088   2.797  -22.260 1.00 34.71  ? 290 MET   A CE  1 
ATOM   2202 N N   . SER   A 1 280 ? 11.335  0.648  -26.550 1.00 33.44  ? 291 SER   A N   1 
ATOM   2203 C CA  A SER   A 1 280 ? 12.701  0.117  -26.615 0.50 33.10  ? 291 SER   A CA  1 
ATOM   2204 C CA  B SER   A 1 280 ? 12.701  0.120  -26.606 0.50 33.35  ? 291 SER   A CA  1 
ATOM   2205 C C   . SER   A 1 280 ? 13.724  1.180  -27.071 1.00 32.79  ? 291 SER   A C   1 
ATOM   2206 O O   . SER   A 1 280 ? 14.862  1.399  -26.526 1.00 32.16  ? 291 SER   A O   1 
ATOM   2207 C CB  A SER   A 1 280 ? 12.713  -1.086 -27.549 0.50 32.40  ? 291 SER   A CB  1 
ATOM   2208 C CB  B SER   A 1 280 ? 12.705  -1.105 -27.513 0.50 32.94  ? 291 SER   A CB  1 
ATOM   2209 O OG  A SER   A 1 280 ? 11.468  -1.767 -27.535 0.50 31.84  ? 291 SER   A OG  1 
ATOM   2210 O OG  B SER   A 1 280 ? 12.815  -0.733 -28.881 0.50 32.98  ? 291 SER   A OG  1 
ATOM   2211 N N   . VAL   A 1 281 ? 13.369  1.881  -28.136 1.00 32.81  ? 292 VAL   A N   1 
ATOM   2212 C CA  . VAL   A 1 281 ? 14.229  2.945  -28.623 1.00 32.22  ? 292 VAL   A CA  1 
ATOM   2213 C C   . VAL   A 1 281 ? 14.736  3.768  -27.438 1.00 32.41  ? 292 VAL   A C   1 
ATOM   2214 O O   . VAL   A 1 281 ? 15.877  4.230  -27.448 1.00 32.72  ? 292 VAL   A O   1 
ATOM   2215 C CB  . VAL   A 1 281 ? 13.403  3.785  -29.605 1.00 30.99  ? 292 VAL   A CB  1 
ATOM   2216 C CG1 . VAL   A 1 281 ? 14.006  5.155  -29.855 1.00 30.50  ? 292 VAL   A CG1 1 
ATOM   2217 C CG2 . VAL   A 1 281 ? 13.175  3.036  -30.911 1.00 31.01  ? 292 VAL   A CG2 1 
ATOM   2218 N N   . PHE   A 1 282 ? 13.871  3.918  -26.430 1.00 30.72  ? 293 PHE   A N   1 
ATOM   2219 C CA  . PHE   A 1 282 ? 14.181  4.636  -25.216 1.00 32.01  ? 293 PHE   A CA  1 
ATOM   2220 C C   . PHE   A 1 282 ? 15.053  3.787  -24.307 1.00 35.22  ? 293 PHE   A C   1 
ATOM   2221 O O   . PHE   A 1 282 ? 16.131  4.224  -23.916 1.00 36.12  ? 293 PHE   A O   1 
ATOM   2222 C CB  . PHE   A 1 282 ? 12.854  4.953  -24.537 1.00 33.81  ? 293 PHE   A CB  1 
ATOM   2223 C CG  . PHE   A 1 282 ? 11.890  5.837  -25.317 1.00 33.86  ? 293 PHE   A CG  1 
ATOM   2224 C CD1 . PHE   A 1 282 ? 12.326  6.668  -26.348 1.00 34.31  ? 293 PHE   A CD1 1 
ATOM   2225 C CD2 . PHE   A 1 282 ? 10.544  5.868  -24.972 1.00 32.77  ? 293 PHE   A CD2 1 
ATOM   2226 C CE1 . PHE   A 1 282 ? 11.435  7.486  -27.025 1.00 32.92  ? 293 PHE   A CE1 1 
ATOM   2227 C CE2 . PHE   A 1 282 ? 9.662   6.687  -25.655 1.00 32.73  ? 293 PHE   A CE2 1 
ATOM   2228 C CZ  . PHE   A 1 282 ? 10.108  7.492  -26.680 1.00 32.81  ? 293 PHE   A CZ  1 
ATOM   2229 N N   . GLU   A 1 283 ? 14.598  2.571  -23.988 1.00 38.64  ? 294 GLU   A N   1 
ATOM   2230 C CA  . GLU   A 1 283 ? 15.298  1.736  -23.017 1.00 44.45  ? 294 GLU   A CA  1 
ATOM   2231 C C   . GLU   A 1 283 ? 16.660  1.258  -23.540 1.00 46.32  ? 294 GLU   A C   1 
ATOM   2232 O O   . GLU   A 1 283 ? 17.572  1.034  -22.752 1.00 46.31  ? 294 GLU   A O   1 
ATOM   2233 C CB  . GLU   A 1 283 ? 14.441  0.541  -22.607 1.00 47.45  ? 294 GLU   A CB  1 
ATOM   2234 C CG  . GLU   A 1 283 ? 13.313  0.878  -21.635 1.00 49.20  ? 294 GLU   A CG  1 
ATOM   2235 C CD  . GLU   A 1 283 ? 12.224  -0.187 -21.593 1.00 50.34  ? 294 GLU   A CD  1 
ATOM   2236 O OE1 . GLU   A 1 283 ? 12.017  -0.877 -22.626 1.00 46.91  ? 294 GLU   A OE1 1 
ATOM   2237 O OE2 . GLU   A 1 283 ? 11.603  -0.345 -20.519 1.00 52.54  ? 294 GLU   A OE2 1 
ATOM   2238 N N   . ASN   A 1 284 ? 16.786  1.043  -24.856 1.00 47.87  ? 295 ASN   A N   1 
ATOM   2239 C CA  . ASN   A 1 284 ? 18.052  0.654  -25.454 1.00 48.30  ? 295 ASN   A CA  1 
ATOM   2240 C C   . ASN   A 1 284 ? 19.026  1.821  -25.386 1.00 53.60  ? 295 ASN   A C   1 
ATOM   2241 O O   . ASN   A 1 284 ? 20.134  1.687  -24.870 1.00 62.02  ? 295 ASN   A O   1 
ATOM   2242 C CB  . ASN   A 1 284 ? 17.915  0.255  -26.914 1.00 48.28  ? 295 ASN   A CB  1 
ATOM   2243 C CG  . ASN   A 1 284 ? 17.119  -1.015 -27.080 1.00 52.96  ? 295 ASN   A CG  1 
ATOM   2244 O OD1 . ASN   A 1 284 ? 16.985  -1.801 -26.133 1.00 50.12  ? 295 ASN   A OD1 1 
ATOM   2245 N ND2 . ASN   A 1 284 ? 16.607  -1.241 -28.281 1.00 55.97  ? 295 ASN   A ND2 1 
ATOM   2246 N N   . SER   A 1 285 ? 18.580  2.965  -25.914 1.00 51.07  ? 296 SER   A N   1 
ATOM   2247 C CA  . SER   A 1 285 ? 19.398  4.168  -25.918 1.00 45.99  ? 296 SER   A CA  1 
ATOM   2248 C C   . SER   A 1 285 ? 19.814  4.519  -24.488 1.00 43.72  ? 296 SER   A C   1 
ATOM   2249 O O   . SER   A 1 285 ? 20.966  4.896  -24.240 1.00 42.32  ? 296 SER   A O   1 
ATOM   2250 C CB  . SER   A 1 285 ? 18.682  5.303  -26.612 1.00 44.45  ? 296 SER   A CB  1 
ATOM   2251 O OG  . SER   A 1 285 ? 18.453  4.980  -27.976 1.00 40.99  ? 296 SER   A OG  1 
ATOM   2252 N N   . MET   A 1 286 ? 18.896  4.317  -23.536 1.00 41.06  ? 297 MET   A N   1 
ATOM   2253 C CA  . MET   A 1 286 ? 19.219  4.546  -22.140 1.00 44.75  ? 297 MET   A CA  1 
ATOM   2254 C C   . MET   A 1 286 ? 20.375  3.648  -21.711 1.00 49.70  ? 297 MET   A C   1 
ATOM   2255 O O   . MET   A 1 286 ? 21.227  4.098  -20.946 1.00 45.84  ? 297 MET   A O   1 
ATOM   2256 C CB  . MET   A 1 286 ? 18.034  4.218  -21.232 1.00 46.38  ? 297 MET   A CB  1 
ATOM   2257 C CG  . MET   A 1 286 ? 17.023  5.322  -21.027 1.00 46.76  ? 297 MET   A CG  1 
ATOM   2258 S SD  . MET   A 1 286 ? 15.702  4.662  -19.984 1.00 46.91  ? 297 MET   A SD  1 
ATOM   2259 C CE  . MET   A 1 286 ? 16.545  4.759  -18.394 1.00 47.33  ? 297 MET   A CE  1 
ATOM   2260 N N   . LYS   A 1 287 ? 20.369  2.386  -22.197 1.00 56.35  ? 298 LYS   A N   1 
ATOM   2261 C CA  . LYS   A 1 287 ? 21.335  1.355  -21.817 1.00 52.80  ? 298 LYS   A CA  1 
ATOM   2262 C C   . LYS   A 1 287 ? 22.700  1.614  -22.443 1.00 46.91  ? 298 LYS   A C   1 
ATOM   2263 O O   . LYS   A 1 287 ? 23.700  1.641  -21.736 1.00 42.03  ? 298 LYS   A O   1 
ATOM   2264 C CB  . LYS   A 1 287 ? 20.877  -0.046 -22.224 1.00 56.32  ? 298 LYS   A CB  1 
ATOM   2265 C CG  . LYS   A 1 287 ? 19.870  -0.657 -21.252 1.00 64.09  ? 298 LYS   A CG  1 
ATOM   2266 C CD  . LYS   A 1 287 ? 19.162  -1.915 -21.730 1.00 69.66  ? 298 LYS   A CD  1 
ATOM   2267 C CE  . LYS   A 1 287 ? 20.044  -3.130 -21.613 1.00 73.83  ? 298 LYS   A CE  1 
ATOM   2268 N NZ  . LYS   A 1 287 ? 19.262  -4.365 -21.672 1.00 77.00  ? 298 LYS   A NZ  1 
ATOM   2269 N N   . GLU   A 1 288 ? 22.736  1.830  -23.759 1.00 44.62  ? 299 GLU   A N   1 
ATOM   2270 C CA  . GLU   A 1 288 ? 23.970  2.185  -24.445 1.00 44.73  ? 299 GLU   A CA  1 
ATOM   2271 C C   . GLU   A 1 288 ? 24.515  3.531  -23.970 1.00 41.79  ? 299 GLU   A C   1 
ATOM   2272 O O   . GLU   A 1 288 ? 25.134  4.233  -24.766 1.00 41.50  ? 299 GLU   A O   1 
ATOM   2273 C CB  . GLU   A 1 288 ? 23.750  2.417  -25.937 1.00 47.10  ? 299 GLU   A CB  1 
ATOM   2274 C CG  . GLU   A 1 288 ? 22.834  1.389  -26.593 1.00 51.22  ? 299 GLU   A CG  1 
ATOM   2275 C CD  . GLU   A 1 288 ? 22.446  1.819  -27.995 1.00 54.21  ? 299 GLU   A CD  1 
ATOM   2276 O OE1 . GLU   A 1 288 ? 23.116  2.748  -28.538 1.00 51.71  ? 299 GLU   A OE1 1 
ATOM   2277 O OE2 . GLU   A 1 288 ? 21.454  1.245  -28.512 1.00 55.09  ? 299 GLU   A OE2 1 
ATOM   2278 N N   . ARG   A 1 289 ? 24.279  3.889  -22.700 1.00 38.57  ? 300 ARG   A N   1 
ATOM   2279 C CA  . ARG   A 1 289 ? 24.639  5.198  -22.179 1.00 40.20  ? 300 ARG   A CA  1 
ATOM   2280 C C   . ARG   A 1 289 ? 24.689  5.179  -20.652 1.00 38.04  ? 300 ARG   A C   1 
ATOM   2281 O O   . ARG   A 1 289 ? 24.895  6.217  -20.029 1.00 38.46  ? 300 ARG   A O   1 
ATOM   2282 C CB  . ARG   A 1 289 ? 23.647  6.236  -22.724 1.00 43.26  ? 300 ARG   A CB  1 
ATOM   2283 C CG  . ARG   A 1 289 ? 24.227  7.176  -23.773 1.00 44.20  ? 300 ARG   A CG  1 
ATOM   2284 C CD  . ARG   A 1 289 ? 23.168  7.563  -24.786 1.00 46.22  ? 300 ARG   A CD  1 
ATOM   2285 N NE  . ARG   A 1 289 ? 23.615  7.457  -26.179 1.00 44.84  ? 300 ARG   A NE  1 
ATOM   2286 C CZ  . ARG   A 1 289 ? 23.058  6.664  -27.092 1.00 47.72  ? 300 ARG   A CZ  1 
ATOM   2287 N NH1 . ARG   A 1 289 ? 22.232  5.691  -26.727 1.00 51.17  ? 300 ARG   A NH1 1 
ATOM   2288 N NH2 . ARG   A 1 289 ? 23.342  6.832  -28.374 1.00 46.50  ? 300 ARG   A NH2 1 
ATOM   2289 N N   . GLY   A 1 290 ? 24.508  4.001  -20.049 1.00 37.22  ? 301 GLY   A N   1 
ATOM   2290 C CA  . GLY   A 1 290 ? 24.654  3.846  -18.613 1.00 39.50  ? 301 GLY   A CA  1 
ATOM   2291 C C   . GLY   A 1 290 ? 23.661  4.714  -17.845 1.00 45.14  ? 301 GLY   A C   1 
ATOM   2292 O O   . GLY   A 1 290 ? 23.978  5.170  -16.745 1.00 46.94  ? 301 GLY   A O   1 
ATOM   2293 N N   . ILE   A 1 291 ? 22.466  4.920  -18.432 1.00 47.71  ? 302 ILE   A N   1 
ATOM   2294 C CA  . ILE   A 1 291 ? 21.442  5.765  -17.838 1.00 44.46  ? 302 ILE   A CA  1 
ATOM   2295 C C   . ILE   A 1 291 ? 20.461  4.874  -17.090 1.00 41.21  ? 302 ILE   A C   1 
ATOM   2296 O O   . ILE   A 1 291 ? 19.863  3.986  -17.697 1.00 37.31  ? 302 ILE   A O   1 
ATOM   2297 C CB  . ILE   A 1 291 ? 20.700  6.628  -18.876 1.00 46.77  ? 302 ILE   A CB  1 
ATOM   2298 C CG1 . ILE   A 1 291 ? 21.634  7.528  -19.671 1.00 46.79  ? 302 ILE   A CG1 1 
ATOM   2299 C CG2 . ILE   A 1 291 ? 19.598  7.455  -18.208 1.00 47.80  ? 302 ILE   A CG2 1 
ATOM   2300 C CD1 . ILE   A 1 291 ? 20.959  8.206  -20.855 1.00 46.00  ? 302 ILE   A CD1 1 
ATOM   2301 N N   . ALA   A 1 292 ? 20.294  5.180  -15.791 1.00 41.15  ? 303 ALA   A N   1 
ATOM   2302 C CA  . ALA   A 1 292 ? 19.425  4.458  -14.874 1.00 43.73  ? 303 ALA   A CA  1 
ATOM   2303 C C   . ALA   A 1 292 ? 18.170  5.270  -14.579 1.00 48.17  ? 303 ALA   A C   1 
ATOM   2304 O O   . ALA   A 1 292 ? 18.217  6.496  -14.592 1.00 52.50  ? 303 ALA   A O   1 
ATOM   2305 C CB  . ALA   A 1 292 ? 20.164  4.187  -13.588 1.00 42.69  ? 303 ALA   A CB  1 
ATOM   2306 N N   . GLU   A 1 293 ? 17.072  4.579  -14.253 1.00 51.67  ? 304 GLU   A N   1 
ATOM   2307 C CA  . GLU   A 1 293 ? 15.816  5.254  -13.963 1.00 59.26  ? 304 GLU   A CA  1 
ATOM   2308 C C   . GLU   A 1 293 ? 15.932  5.993  -12.630 1.00 62.49  ? 304 GLU   A C   1 
ATOM   2309 O O   . GLU   A 1 293 ? 15.382  7.085  -12.471 1.00 65.56  ? 304 GLU   A O   1 
ATOM   2310 C CB  . GLU   A 1 293 ? 14.620  4.303  -14.000 1.00 62.25  ? 304 GLU   A CB  1 
ATOM   2311 C CG  . GLU   A 1 293 ? 13.286  5.050  -13.997 1.00 66.58  ? 304 GLU   A CG  1 
ATOM   2312 C CD  . GLU   A 1 293 ? 12.189  4.440  -14.851 1.00 72.20  ? 304 GLU   A CD  1 
ATOM   2313 O OE1 . GLU   A 1 293 ? 11.083  4.222  -14.306 1.00 69.95  ? 304 GLU   A OE1 1 
ATOM   2314 O OE2 . GLU   A 1 293 ? 12.436  4.196  -16.059 1.00 76.65  ? 304 GLU   A OE2 1 
ATOM   2315 N N   . ASN   A 1 294 ? 16.687  5.404  -11.693 1.00 64.86  ? 305 ASN   A N   1 
ATOM   2316 C CA  . ASN   A 1 294 ? 16.955  6.001  -10.394 1.00 64.39  ? 305 ASN   A CA  1 
ATOM   2317 C C   . ASN   A 1 294 ? 17.906  7.197  -10.515 1.00 63.82  ? 305 ASN   A C   1 
ATOM   2318 O O   . ASN   A 1 294 ? 18.466  7.637  -9.508  1.00 63.85  ? 305 ASN   A O   1 
ATOM   2319 C CB  . ASN   A 1 294 ? 17.592  4.985  -9.453  1.00 61.97  ? 305 ASN   A CB  1 
ATOM   2320 C CG  . ASN   A 1 294 ? 18.919  4.531  -10.010 1.00 60.53  ? 305 ASN   A CG  1 
ATOM   2321 O OD1 . ASN   A 1 294 ? 18.970  3.618  -10.842 1.00 57.62  ? 305 ASN   A OD1 1 
ATOM   2322 N ND2 . ASN   A 1 294 ? 19.991  5.195  -9.610  1.00 60.72  ? 305 ASN   A ND2 1 
ATOM   2323 N N   . GLU   A 1 295 ? 18.118  7.704  -11.739 1.00 57.44  ? 306 GLU   A N   1 
ATOM   2324 C CA  . GLU   A 1 295 ? 18.893  8.921  -11.921 1.00 51.93  ? 306 GLU   A CA  1 
ATOM   2325 C C   . GLU   A 1 295 ? 18.030  10.133 -11.569 1.00 44.48  ? 306 GLU   A C   1 
ATOM   2326 O O   . GLU   A 1 295 ? 16.802  10.086 -11.614 1.00 41.11  ? 306 GLU   A O   1 
ATOM   2327 C CB  . GLU   A 1 295 ? 19.486  9.010  -13.327 1.00 51.95  ? 306 GLU   A CB  1 
ATOM   2328 C CG  . GLU   A 1 295 ? 20.639  8.035  -13.525 1.00 53.22  ? 306 GLU   A CG  1 
ATOM   2329 C CD  . GLU   A 1 295 ? 21.353  8.156  -14.856 1.00 56.42  ? 306 GLU   A CD  1 
ATOM   2330 O OE1 . GLU   A 1 295 ? 20.980  9.034  -15.670 1.00 52.79  ? 306 GLU   A OE1 1 
ATOM   2331 O OE2 . GLU   A 1 295 ? 22.298  7.352  -15.059 1.00 60.64  ? 306 GLU   A OE2 1 
ATOM   2332 N N   . ALA   A 1 296 ? 18.707  11.214 -11.183 1.00 37.92  ? 307 ALA   A N   1 
ATOM   2333 C CA  . ALA   A 1 296 ? 18.049  12.477 -10.935 1.00 34.97  ? 307 ALA   A CA  1 
ATOM   2334 C C   . ALA   A 1 296 ? 17.585  13.071 -12.264 1.00 33.05  ? 307 ALA   A C   1 
ATOM   2335 O O   . ALA   A 1 296 ? 18.060  12.684 -13.333 1.00 34.49  ? 307 ALA   A O   1 
ATOM   2336 C CB  . ALA   A 1 296 ? 18.999  13.397 -10.199 1.00 35.48  ? 307 ALA   A CB  1 
ATOM   2337 N N   . PHE   A 1 297 ? 16.649  14.018 -12.182 1.00 28.15  ? 308 PHE   A N   1 
ATOM   2338 C CA  . PHE   A 1 297 ? 16.287  14.836 -13.318 1.00 26.28  ? 308 PHE   A CA  1 
ATOM   2339 C C   . PHE   A 1 297 ? 17.035  16.172 -13.284 1.00 26.10  ? 308 PHE   A C   1 
ATOM   2340 O O   . PHE   A 1 297 ? 17.437  16.653 -12.231 1.00 27.44  ? 308 PHE   A O   1 
ATOM   2341 C CB  . PHE   A 1 297 ? 14.767  14.943 -13.222 1.00 27.61  ? 308 PHE   A CB  1 
ATOM   2342 C CG  . PHE   A 1 297 ? 13.998  13.731 -13.730 1.00 28.69  ? 308 PHE   A CG  1 
ATOM   2343 C CD1 . PHE   A 1 297 ? 13.976  13.428 -15.090 1.00 29.11  ? 308 PHE   A CD1 1 
ATOM   2344 C CD2 . PHE   A 1 297 ? 13.236  12.948 -12.869 1.00 28.28  ? 308 PHE   A CD2 1 
ATOM   2345 C CE1 . PHE   A 1 297 ? 13.249  12.349 -15.569 1.00 29.54  ? 308 PHE   A CE1 1 
ATOM   2346 C CE2 . PHE   A 1 297 ? 12.514  11.868 -13.353 1.00 29.31  ? 308 PHE   A CE2 1 
ATOM   2347 C CZ  . PHE   A 1 297 ? 12.519  11.573 -14.703 1.00 29.41  ? 308 PHE   A CZ  1 
ATOM   2348 N N   . ASP   A 1 298 ? 17.192  16.791 -14.458 1.00 25.31  ? 309 ASP   A N   1 
ATOM   2349 C CA  . ASP   A 1 298 ? 17.886  18.059 -14.608 1.00 23.78  ? 309 ASP   A CA  1 
ATOM   2350 C C   . ASP   A 1 298 ? 17.500  19.044 -13.512 1.00 24.46  ? 309 ASP   A C   1 
ATOM   2351 O O   . ASP   A 1 298 ? 18.366  19.630 -12.894 1.00 26.14  ? 309 ASP   A O   1 
ATOM   2352 C CB  . ASP   A 1 298 ? 17.616  18.670 -15.971 1.00 23.28  ? 309 ASP   A CB  1 
ATOM   2353 C CG  . ASP   A 1 298 ? 18.116  17.845 -17.143 1.00 23.19  ? 309 ASP   A CG  1 
ATOM   2354 O OD1 . ASP   A 1 298 ? 18.761  16.815 -16.882 1.00 23.43  ? 309 ASP   A OD1 1 
ATOM   2355 O OD2 . ASP   A 1 298 ? 17.866  18.235 -18.298 1.00 23.13  ? 309 ASP   A OD2 1 
ATOM   2356 N N   . TRP   A 1 299 ? 16.206  19.249 -13.276 1.00 26.98  ? 310 TRP   A N   1 
ATOM   2357 C CA  . TRP   A 1 299 ? 15.767  20.283 -12.349 1.00 29.90  ? 310 TRP   A CA  1 
ATOM   2358 C C   . TRP   A 1 299 ? 16.071  19.903 -10.901 1.00 34.30  ? 310 TRP   A C   1 
ATOM   2359 O O   . TRP   A 1 299 ? 16.032  20.769 -10.036 1.00 37.90  ? 310 TRP   A O   1 
ATOM   2360 C CB  . TRP   A 1 299 ? 14.269  20.588 -12.507 1.00 29.24  ? 310 TRP   A CB  1 
ATOM   2361 C CG  . TRP   A 1 299 ? 13.439  19.341 -12.600 1.00 28.15  ? 310 TRP   A CG  1 
ATOM   2362 C CD1 . TRP   A 1 299 ? 12.916  18.616 -11.574 1.00 28.22  ? 310 TRP   A CD1 1 
ATOM   2363 C CD2 . TRP   A 1 299 ? 13.092  18.647 -13.815 1.00 28.57  ? 310 TRP   A CD2 1 
ATOM   2364 N NE1 . TRP   A 1 299 ? 12.280  17.510 -12.066 1.00 28.47  ? 310 TRP   A NE1 1 
ATOM   2365 C CE2 . TRP   A 1 299 ? 12.360  17.505 -13.434 1.00 28.14  ? 310 TRP   A CE2 1 
ATOM   2366 C CE3 . TRP   A 1 299 ? 13.321  18.885 -15.179 1.00 29.18  ? 310 TRP   A CE3 1 
ATOM   2367 C CZ2 . TRP   A 1 299 ? 11.859  16.600 -14.368 1.00 28.04  ? 310 TRP   A CZ2 1 
ATOM   2368 C CZ3 . TRP   A 1 299 ? 12.809  17.997 -16.102 1.00 28.65  ? 310 TRP   A CZ3 1 
ATOM   2369 C CH2 . TRP   A 1 299 ? 12.100  16.863 -15.698 1.00 28.25  ? 310 TRP   A CH2 1 
ATOM   2370 N N   . GLU   A 1 300 ? 16.324  18.619 -10.621 1.00 38.46  ? 311 GLU   A N   1 
ATOM   2371 C CA  . GLU   A 1 300 ? 16.569  18.185 -9.254  1.00 43.35  ? 311 GLU   A CA  1 
ATOM   2372 C C   . GLU   A 1 300 ? 17.915  18.741 -8.811  1.00 53.79  ? 311 GLU   A C   1 
ATOM   2373 O O   . GLU   A 1 300 ? 18.807  18.916 -9.641  1.00 54.41  ? 311 GLU   A O   1 
ATOM   2374 C CB  . GLU   A 1 300 ? 16.586  16.665 -9.086  1.00 38.72  ? 311 GLU   A CB  1 
ATOM   2375 C CG  . GLU   A 1 300 ? 15.205  16.018 -9.134  1.00 34.11  ? 311 GLU   A CG  1 
ATOM   2376 C CD  . GLU   A 1 300 ? 15.264  14.507 -9.018  1.00 33.48  ? 311 GLU   A CD  1 
ATOM   2377 O OE1 . GLU   A 1 300 ? 16.378  13.985 -8.883  1.00 34.75  ? 311 GLU   A OE1 1 
ATOM   2378 O OE2 . GLU   A 1 300 ? 14.225  13.830 -9.074  1.00 33.35  ? 311 GLU   A OE2 1 
ATOM   2379 N N   . LYS   A 1 301 ? 18.046  19.024 -7.506  1.00 63.10  ? 312 LYS   A N   1 
ATOM   2380 C CA  . LYS   A 1 301 ? 19.265  19.639 -6.993  1.00 71.72  ? 312 LYS   A CA  1 
ATOM   2381 C C   . LYS   A 1 301 ? 20.232  18.583 -6.452  1.00 77.78  ? 312 LYS   A C   1 
ATOM   2382 O O   . LYS   A 1 301 ? 21.267  18.932 -5.882  1.00 71.67  ? 312 LYS   A O   1 
ATOM   2383 C CB  . LYS   A 1 301 ? 18.963  20.764 -5.999  1.00 71.72  ? 312 LYS   A CB  1 
ATOM   2384 C CG  . LYS   A 1 301 ? 18.950  22.121 -6.674  1.00 73.42  ? 312 LYS   A CG  1 
ATOM   2385 C CD  . LYS   A 1 301 ? 19.076  23.249 -5.674  1.00 78.37  ? 312 LYS   A CD  1 
ATOM   2386 C CE  . LYS   A 1 301 ? 17.792  23.469 -4.960  1.00 80.96  ? 312 LYS   A CE  1 
ATOM   2387 N NZ  . LYS   A 1 301 ? 18.074  24.133 -3.690  1.00 83.61  ? 312 LYS   A NZ  1 
ATOM   2388 N N   . ALA   A 1 302 ? 19.917  17.298 -6.683  1.00 81.17  ? 313 ALA   A N   1 
ATOM   2389 C CA  . ALA   A 1 302 ? 20.810  16.196 -6.354  1.00 77.79  ? 313 ALA   A CA  1 
ATOM   2390 C C   . ALA   A 1 302 ? 22.081  16.284 -7.204  1.00 76.98  ? 313 ALA   A C   1 
ATOM   2391 O O   . ALA   A 1 302 ? 22.004  15.979 -8.418  1.00 79.61  ? 313 ALA   A O   1 
ATOM   2392 C CB  . ALA   A 1 302 ? 20.097  14.875 -6.562  1.00 77.15  ? 313 ALA   A CB  1 
HETATM 2393 N N1  . A1IU7 B 2 .   ? -3.301  20.410 -14.297 1.00 81.41  ? 401 A1IU7 A N1  1 
HETATM 2394 N N3  . A1IU7 B 2 .   ? -5.100  22.381 -21.424 1.00 87.24  ? 401 A1IU7 A N3  1 
HETATM 2395 C C4  . A1IU7 B 2 .   ? -4.599  20.786 -14.752 1.00 92.61  ? 401 A1IU7 A C4  1 
HETATM 2396 C C5  . A1IU7 B 2 .   ? -5.337  20.800 -13.568 1.00 102.57 ? 401 A1IU7 A C5  1 
HETATM 2397 C C6  . A1IU7 B 2 .   ? -6.661  21.162 -13.554 1.00 110.21 ? 401 A1IU7 A C6  1 
HETATM 2398 C C7  . A1IU7 B 2 .   ? -7.282  21.510 -14.710 1.00 111.33 ? 401 A1IU7 A C7  1 
HETATM 2399 C C8  . A1IU7 B 2 .   ? -6.580  21.508 -15.893 1.00 107.20 ? 401 A1IU7 A C8  1 
HETATM 2400 C C10 . A1IU7 B 2 .   ? -5.063  21.399 -17.446 1.00 96.96  ? 401 A1IU7 A C10 1 
HETATM 2401 C C13 . A1IU7 B 2 .   ? -3.983  23.172 -21.535 1.00 84.47  ? 401 A1IU7 A C13 1 
HETATM 2402 C C15 . A1IU7 B 2 .   ? -4.137  22.541 -19.372 1.00 93.88  ? 401 A1IU7 A C15 1 
HETATM 2403 C C1  . A1IU7 B 2 .   ? -3.924  17.184 -12.422 1.00 50.05  ? 401 A1IU7 A C1  1 
HETATM 2404 C C2  . A1IU7 B 2 .   ? -4.023  18.312 -13.309 1.00 59.07  ? 401 A1IU7 A C2  1 
HETATM 2405 C C3  . A1IU7 B 2 .   ? -3.094  19.479 -13.317 1.00 69.29  ? 401 A1IU7 A C3  1 
HETATM 2406 O O1  . A1IU7 B 2 .   ? -2.191  19.579 -12.483 1.00 65.68  ? 401 A1IU7 A O1  1 
HETATM 2407 C C9  . A1IU7 B 2 .   ? -5.234  21.135 -15.974 1.00 98.62  ? 401 A1IU7 A C9  1 
HETATM 2408 C C11 . A1IU7 B 2 .   ? -6.121  20.964 -18.331 1.00 89.60  ? 401 A1IU7 A C11 1 
HETATM 2409 N N2  . A1IU7 B 2 .   ? -6.201  21.224 -19.624 1.00 84.42  ? 401 A1IU7 A N2  1 
HETATM 2410 C C12 . A1IU7 B 2 .   ? -5.218  21.996 -20.114 1.00 90.05  ? 401 A1IU7 A C12 1 
HETATM 2411 C C14 . A1IU7 B 2 .   ? -3.357  23.288 -20.319 1.00 85.97  ? 401 A1IU7 A C14 1 
HETATM 2412 C C16 . A1IU7 B 2 .   ? -4.096  22.256 -17.998 1.00 98.38  ? 401 A1IU7 A C16 1 
HETATM 2413 O O   . HOH   C 3 .   ? -4.629  17.638 -5.314  1.00 13.73  ? 501 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? -0.667  5.791  -18.081 1.00 22.97  ? 502 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? -5.970  22.814 -24.404 1.00 31.22  ? 503 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? -6.796  17.309 -38.393 1.00 14.48  ? 504 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? -3.926  13.025 -4.343  1.00 29.50  ? 505 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? 4.060   -0.430 -24.359 1.00 27.72  ? 506 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? -3.115  5.278  -35.988 1.00 15.21  ? 507 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? 4.140   23.366 -24.981 1.00 9.24   ? 508 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? -9.712  15.436 -2.192  1.00 15.04  ? 509 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? -7.044  15.819 -46.717 1.00 14.66  ? 510 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? -18.680 31.561 -2.149  1.00 20.27  ? 511 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 12.227  3.913  -45.151 1.00 11.33  ? 512 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? -14.665 3.449  -26.606 1.00 33.92  ? 513 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? 3.822   27.409 -20.087 1.00 10.01  ? 514 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? -12.874 33.858 2.215   1.00 19.26  ? 515 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? 18.473  18.482 -35.104 1.00 19.95  ? 516 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? -5.077  7.393  -11.185 1.00 25.65  ? 517 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? 6.026   28.804 -32.509 1.00 23.19  ? 518 HOH   A O   1 
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