data_9CB8
# 
_entry.id   9CB8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9CB8         pdb_00009cb8 10.2210/pdb9cb8/pdb 
WWPDB D_1000284519 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CB8 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              cristy@fcfrp.usp.br 
_pdbx_contact_author.name_first         Maria 
_pdbx_contact_author.name_last          Nonato 
_pdbx_contact_author.name_mi            Cristina 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4916-1505 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Froes, T.Q.'      1 0000-0001-7951-7560 
'Vaidergorn, M.M.' 2 0000-0003-2343-2888 
'dos Santos, T.'   3 0000-0001-7908-8604 
'Leite, P.I.P.L.'  4 0000-0003-1848-4923 
'Godoi, B.F.'      5 0000-0002-5910-0511 
'Emery, F.S.'      6 0000-0002-8652-7123 
'Nonato, M.C.'     7 0000-0002-4916-1505 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystal structure of dihydroorotate dehydrogenase from Leishmania brasiliensis in complex with 5-benzylidenepyrimidine-2,4,6(1H,3H,5H)-trione
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Froes, T.Q.'      1 0000-0001-7951-7560 
primary 'Vaidergorn, M.M.' 2 0000-0003-2343-2888 
primary 'dos Santos, T.'   3 0000-0001-7908-8604 
primary 'Leite, P.I.P.L.'  4 0000-0003-1848-4923 
primary 'Godoi, B.F.'      5 0000-0002-5910-0511 
primary 'Emery, F.S.'      6 0000-0002-8652-7123 
primary 'Nonato, M.C.'     7 0000-0002-4916-1505 
# 
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 'Dihydroorotate dehydrogenase'      37401.789 2   1.3.3.1  ? ? 'TAG: MGSSHHHHHHSSGLVPRGSHMASMTGGGQMGRG' 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'             456.344   2   ?        ? ? ?                                        
3 non-polymer syn GLYCEROL                            92.094    4   ?        ? ? ?                                        
4 non-polymer man 5-benzyl-1,3-diazinane-2,4,6-trione 218.209   2   1.3.98.1 ? ? 'TAG: MGSSHHHHHHSSGLVPRGSHMASMTGGGQMGRG' 
5 water       nat water                               18.015    262 ?        ? ? ?                                        
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMASMTGGGQMGRGSMSLQVGILGNTFANPFMNAAGVMCSTEEELAAMTESTSGSLITKSC
TPALREGNPAPRYYTLPLGSINSMGLPNKGFDFYLAYSARHHDYSRKPLFISISGFSAEENAEMCKRLAPVAAEKGVILE
LNLSCPNVPGKPQVAYDFDAMRRYLAAISEAYPHPFGVKMPPYFDFAHFDAAAEILNQFPKVQFITCINSIGNGLVIDVE
TESVVIKPKQGFGGLGGRYVFPTALANVNAFYRRCPGKLIFGCGGVYTGEDAFLHVLAGASMVQVGTALHEEGAAIFERL
TAELLDVMAKKGYKALDEFRGKVKAMD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMASMTGGGQMGRGSMSLQVGILGNTFANPFMNAAGVMCSTEEELAAMTESTSGSLITKSC
TPALREGNPAPRYYTLPLGSINSMGLPNKGFDFYLAYSARHHDYSRKPLFISISGFSAEENAEMCKRLAPVAAEKGVILE
LNLSCPNVPGKPQVAYDFDAMRRYLAAISEAYPHPFGVKMPPYFDFAHFDAAAEILNQFPKVQFITCINSIGNGLVIDVE
TESVVIKPKQGFGGLGGRYVFPTALANVNAFYRRCPGKLIFGCGGVYTGEDAFLHVLAGASMVQVGTALHEEGAAIFERL
TAELLDVMAKKGYKALDEFRGKVKAMD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE'             FMN   
3 GLYCEROL                            GOL   
4 5-benzyl-1,3-diazinane-2,4,6-trione A1AVS 
5 water                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  SER n 
1 24  MET n 
1 25  THR n 
1 26  GLY n 
1 27  GLY n 
1 28  GLY n 
1 29  GLN n 
1 30  MET n 
1 31  GLY n 
1 32  ARG n 
1 33  GLY n 
1 34  SER n 
1 35  MET n 
1 36  SER n 
1 37  LEU n 
1 38  GLN n 
1 39  VAL n 
1 40  GLY n 
1 41  ILE n 
1 42  LEU n 
1 43  GLY n 
1 44  ASN n 
1 45  THR n 
1 46  PHE n 
1 47  ALA n 
1 48  ASN n 
1 49  PRO n 
1 50  PHE n 
1 51  MET n 
1 52  ASN n 
1 53  ALA n 
1 54  ALA n 
1 55  GLY n 
1 56  VAL n 
1 57  MET n 
1 58  CYS n 
1 59  SER n 
1 60  THR n 
1 61  GLU n 
1 62  GLU n 
1 63  GLU n 
1 64  LEU n 
1 65  ALA n 
1 66  ALA n 
1 67  MET n 
1 68  THR n 
1 69  GLU n 
1 70  SER n 
1 71  THR n 
1 72  SER n 
1 73  GLY n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  THR n 
1 78  LYS n 
1 79  SER n 
1 80  CYS n 
1 81  THR n 
1 82  PRO n 
1 83  ALA n 
1 84  LEU n 
1 85  ARG n 
1 86  GLU n 
1 87  GLY n 
1 88  ASN n 
1 89  PRO n 
1 90  ALA n 
1 91  PRO n 
1 92  ARG n 
1 93  TYR n 
1 94  TYR n 
1 95  THR n 
1 96  LEU n 
1 97  PRO n 
1 98  LEU n 
1 99  GLY n 
1 100 SER n 
1 101 ILE n 
1 102 ASN n 
1 103 SER n 
1 104 MET n 
1 105 GLY n 
1 106 LEU n 
1 107 PRO n 
1 108 ASN n 
1 109 LYS n 
1 110 GLY n 
1 111 PHE n 
1 112 ASP n 
1 113 PHE n 
1 114 TYR n 
1 115 LEU n 
1 116 ALA n 
1 117 TYR n 
1 118 SER n 
1 119 ALA n 
1 120 ARG n 
1 121 HIS n 
1 122 HIS n 
1 123 ASP n 
1 124 TYR n 
1 125 SER n 
1 126 ARG n 
1 127 LYS n 
1 128 PRO n 
1 129 LEU n 
1 130 PHE n 
1 131 ILE n 
1 132 SER n 
1 133 ILE n 
1 134 SER n 
1 135 GLY n 
1 136 PHE n 
1 137 SER n 
1 138 ALA n 
1 139 GLU n 
1 140 GLU n 
1 141 ASN n 
1 142 ALA n 
1 143 GLU n 
1 144 MET n 
1 145 CYS n 
1 146 LYS n 
1 147 ARG n 
1 148 LEU n 
1 149 ALA n 
1 150 PRO n 
1 151 VAL n 
1 152 ALA n 
1 153 ALA n 
1 154 GLU n 
1 155 LYS n 
1 156 GLY n 
1 157 VAL n 
1 158 ILE n 
1 159 LEU n 
1 160 GLU n 
1 161 LEU n 
1 162 ASN n 
1 163 LEU n 
1 164 SER n 
1 165 CYS n 
1 166 PRO n 
1 167 ASN n 
1 168 VAL n 
1 169 PRO n 
1 170 GLY n 
1 171 LYS n 
1 172 PRO n 
1 173 GLN n 
1 174 VAL n 
1 175 ALA n 
1 176 TYR n 
1 177 ASP n 
1 178 PHE n 
1 179 ASP n 
1 180 ALA n 
1 181 MET n 
1 182 ARG n 
1 183 ARG n 
1 184 TYR n 
1 185 LEU n 
1 186 ALA n 
1 187 ALA n 
1 188 ILE n 
1 189 SER n 
1 190 GLU n 
1 191 ALA n 
1 192 TYR n 
1 193 PRO n 
1 194 HIS n 
1 195 PRO n 
1 196 PHE n 
1 197 GLY n 
1 198 VAL n 
1 199 LYS n 
1 200 MET n 
1 201 PRO n 
1 202 PRO n 
1 203 TYR n 
1 204 PHE n 
1 205 ASP n 
1 206 PHE n 
1 207 ALA n 
1 208 HIS n 
1 209 PHE n 
1 210 ASP n 
1 211 ALA n 
1 212 ALA n 
1 213 ALA n 
1 214 GLU n 
1 215 ILE n 
1 216 LEU n 
1 217 ASN n 
1 218 GLN n 
1 219 PHE n 
1 220 PRO n 
1 221 LYS n 
1 222 VAL n 
1 223 GLN n 
1 224 PHE n 
1 225 ILE n 
1 226 THR n 
1 227 CYS n 
1 228 ILE n 
1 229 ASN n 
1 230 SER n 
1 231 ILE n 
1 232 GLY n 
1 233 ASN n 
1 234 GLY n 
1 235 LEU n 
1 236 VAL n 
1 237 ILE n 
1 238 ASP n 
1 239 VAL n 
1 240 GLU n 
1 241 THR n 
1 242 GLU n 
1 243 SER n 
1 244 VAL n 
1 245 VAL n 
1 246 ILE n 
1 247 LYS n 
1 248 PRO n 
1 249 LYS n 
1 250 GLN n 
1 251 GLY n 
1 252 PHE n 
1 253 GLY n 
1 254 GLY n 
1 255 LEU n 
1 256 GLY n 
1 257 GLY n 
1 258 ARG n 
1 259 TYR n 
1 260 VAL n 
1 261 PHE n 
1 262 PRO n 
1 263 THR n 
1 264 ALA n 
1 265 LEU n 
1 266 ALA n 
1 267 ASN n 
1 268 VAL n 
1 269 ASN n 
1 270 ALA n 
1 271 PHE n 
1 272 TYR n 
1 273 ARG n 
1 274 ARG n 
1 275 CYS n 
1 276 PRO n 
1 277 GLY n 
1 278 LYS n 
1 279 LEU n 
1 280 ILE n 
1 281 PHE n 
1 282 GLY n 
1 283 CYS n 
1 284 GLY n 
1 285 GLY n 
1 286 VAL n 
1 287 TYR n 
1 288 THR n 
1 289 GLY n 
1 290 GLU n 
1 291 ASP n 
1 292 ALA n 
1 293 PHE n 
1 294 LEU n 
1 295 HIS n 
1 296 VAL n 
1 297 LEU n 
1 298 ALA n 
1 299 GLY n 
1 300 ALA n 
1 301 SER n 
1 302 MET n 
1 303 VAL n 
1 304 GLN n 
1 305 VAL n 
1 306 GLY n 
1 307 THR n 
1 308 ALA n 
1 309 LEU n 
1 310 HIS n 
1 311 GLU n 
1 312 GLU n 
1 313 GLY n 
1 314 ALA n 
1 315 ALA n 
1 316 ILE n 
1 317 PHE n 
1 318 GLU n 
1 319 ARG n 
1 320 LEU n 
1 321 THR n 
1 322 ALA n 
1 323 GLU n 
1 324 LEU n 
1 325 LEU n 
1 326 ASP n 
1 327 VAL n 
1 328 MET n 
1 329 ALA n 
1 330 LYS n 
1 331 LYS n 
1 332 GLY n 
1 333 TYR n 
1 334 LYS n 
1 335 ALA n 
1 336 LEU n 
1 337 ASP n 
1 338 GLU n 
1 339 PHE n 
1 340 ARG n 
1 341 GLY n 
1 342 LYS n 
1 343 VAL n 
1 344 LYS n 
1 345 ALA n 
1 346 MET n 
1 347 ASP n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 347 ? ? 'DHODH, LBRM_16_0550' ? ? ? ? ? ? 'Leishmania braziliensis' 5660 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21' 511693 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample ?                     ? ?   ? ? ?                     ? ? ? ? ? ? 'Leishmania braziliensis' 5660 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21' 511693 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1AVS non-polymer         . 5-benzyl-1,3-diazinane-2,4,6-trione ?                               'C11 H10 N2 O3'   218.209 
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 
FMN   non-polymer         . 'FLAVIN MONONUCLEOTIDE'             'RIBOFLAVIN MONOPHOSPHATE'      'C17 H21 N4 O9 P' 456.344 
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  
GOL   non-polymer         . GLYCEROL                            'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
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 
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   -33 ?   ?   ?   A . n 
A 1 2   GLY 2   -32 ?   ?   ?   A . n 
A 1 3   SER 3   -31 ?   ?   ?   A . n 
A 1 4   SER 4   -30 ?   ?   ?   A . n 
A 1 5   HIS 5   -29 ?   ?   ?   A . n 
A 1 6   HIS 6   -28 ?   ?   ?   A . n 
A 1 7   HIS 7   -27 ?   ?   ?   A . n 
A 1 8   HIS 8   -26 ?   ?   ?   A . n 
A 1 9   HIS 9   -25 ?   ?   ?   A . n 
A 1 10  HIS 10  -24 ?   ?   ?   A . n 
A 1 11  SER 11  -23 ?   ?   ?   A . n 
A 1 12  SER 12  -22 ?   ?   ?   A . n 
A 1 13  GLY 13  -21 ?   ?   ?   A . n 
A 1 14  LEU 14  -20 ?   ?   ?   A . n 
A 1 15  VAL 15  -19 ?   ?   ?   A . n 
A 1 16  PRO 16  -18 ?   ?   ?   A . n 
A 1 17  ARG 17  -17 ?   ?   ?   A . n 
A 1 18  GLY 18  -16 ?   ?   ?   A . n 
A 1 19  SER 19  -15 ?   ?   ?   A . n 
A 1 20  HIS 20  -14 ?   ?   ?   A . n 
A 1 21  MET 21  -13 ?   ?   ?   A . n 
A 1 22  ALA 22  -12 ?   ?   ?   A . n 
A 1 23  SER 23  -11 ?   ?   ?   A . n 
A 1 24  MET 24  -10 ?   ?   ?   A . n 
A 1 25  THR 25  -9  ?   ?   ?   A . n 
A 1 26  GLY 26  -8  ?   ?   ?   A . n 
A 1 27  GLY 27  -7  ?   ?   ?   A . n 
A 1 28  GLY 28  -6  ?   ?   ?   A . n 
A 1 29  GLN 29  -5  ?   ?   ?   A . n 
A 1 30  MET 30  -4  ?   ?   ?   A . n 
A 1 31  GLY 31  -3  ?   ?   ?   A . n 
A 1 32  ARG 32  -2  ?   ?   ?   A . n 
A 1 33  GLY 33  -1  ?   ?   ?   A . n 
A 1 34  SER 34  0   0   SER SER A . n 
A 1 35  MET 35  1   1   MET MET A . n 
A 1 36  SER 36  2   2   SER SER A . n 
A 1 37  LEU 37  3   3   LEU LEU A . n 
A 1 38  GLN 38  4   4   GLN GLN A . n 
A 1 39  VAL 39  5   5   VAL VAL A . n 
A 1 40  GLY 40  6   6   GLY GLY A . n 
A 1 41  ILE 41  7   7   ILE ILE A . n 
A 1 42  LEU 42  8   8   LEU LEU A . n 
A 1 43  GLY 43  9   9   GLY GLY A . n 
A 1 44  ASN 44  10  10  ASN ASN A . n 
A 1 45  THR 45  11  11  THR THR A . n 
A 1 46  PHE 46  12  12  PHE PHE A . n 
A 1 47  ALA 47  13  13  ALA ALA A . n 
A 1 48  ASN 48  14  14  ASN ASN A . n 
A 1 49  PRO 49  15  15  PRO PRO A . n 
A 1 50  PHE 50  16  16  PHE PHE A . n 
A 1 51  MET 51  17  17  MET MET A . n 
A 1 52  ASN 52  18  18  ASN ASN A . n 
A 1 53  ALA 53  19  19  ALA ALA A . n 
A 1 54  ALA 54  20  20  ALA ALA A . n 
A 1 55  GLY 55  21  21  GLY GLY A . n 
A 1 56  VAL 56  22  22  VAL VAL A . n 
A 1 57  MET 57  23  23  MET MET A . n 
A 1 58  CYS 58  24  24  CYS CYS A . n 
A 1 59  SER 59  25  25  SER SER A . n 
A 1 60  THR 60  26  26  THR THR A . n 
A 1 61  GLU 61  27  27  GLU GLU A . n 
A 1 62  GLU 62  28  28  GLU GLU A . n 
A 1 63  GLU 63  29  29  GLU GLU A . n 
A 1 64  LEU 64  30  30  LEU LEU A . n 
A 1 65  ALA 65  31  31  ALA ALA A . n 
A 1 66  ALA 66  32  32  ALA ALA A . n 
A 1 67  MET 67  33  33  MET MET A . n 
A 1 68  THR 68  34  34  THR THR A . n 
A 1 69  GLU 69  35  35  GLU GLU A . n 
A 1 70  SER 70  36  36  SER SER A . n 
A 1 71  THR 71  37  37  THR THR A . n 
A 1 72  SER 72  38  38  SER SER A . n 
A 1 73  GLY 73  39  39  GLY GLY A . n 
A 1 74  SER 74  40  40  SER SER A . n 
A 1 75  LEU 75  41  41  LEU LEU A . n 
A 1 76  ILE 76  42  42  ILE ILE A . n 
A 1 77  THR 77  43  43  THR THR A . n 
A 1 78  LYS 78  44  44  LYS LYS A . n 
A 1 79  SER 79  45  45  SER SER A . n 
A 1 80  CYS 80  46  46  CYS CYS A . n 
A 1 81  THR 81  47  47  THR THR A . n 
A 1 82  PRO 82  48  48  PRO PRO A . n 
A 1 83  ALA 83  49  ?   ?   ?   A . n 
A 1 84  LEU 84  50  ?   ?   ?   A . n 
A 1 85  ARG 85  51  ?   ?   ?   A . n 
A 1 86  GLU 86  52  ?   ?   ?   A . n 
A 1 87  GLY 87  53  ?   ?   ?   A . n 
A 1 88  ASN 88  54  ?   ?   ?   A . n 
A 1 89  PRO 89  55  ?   ?   ?   A . n 
A 1 90  ALA 90  56  ?   ?   ?   A . n 
A 1 91  PRO 91  57  57  PRO PRO A . n 
A 1 92  ARG 92  58  58  ARG ARG A . n 
A 1 93  TYR 93  59  59  TYR TYR A . n 
A 1 94  TYR 94  60  60  TYR TYR A . n 
A 1 95  THR 95  61  61  THR THR A . n 
A 1 96  LEU 96  62  62  LEU LEU A . n 
A 1 97  PRO 97  63  63  PRO PRO A . n 
A 1 98  LEU 98  64  64  LEU LEU A . n 
A 1 99  GLY 99  65  65  GLY GLY A . n 
A 1 100 SER 100 66  66  SER SER A . n 
A 1 101 ILE 101 67  67  ILE ILE A . n 
A 1 102 ASN 102 68  68  ASN ASN A . n 
A 1 103 SER 103 69  69  SER SER A . n 
A 1 104 MET 104 70  70  MET MET A . n 
A 1 105 GLY 105 71  71  GLY GLY A . n 
A 1 106 LEU 106 72  ?   ?   ?   A . n 
A 1 107 PRO 107 73  73  PRO PRO A . n 
A 1 108 ASN 108 74  74  ASN ASN A . n 
A 1 109 LYS 109 75  75  LYS LYS A . n 
A 1 110 GLY 110 76  76  GLY GLY A . n 
A 1 111 PHE 111 77  77  PHE PHE A . n 
A 1 112 ASP 112 78  78  ASP ASP A . n 
A 1 113 PHE 113 79  79  PHE PHE A . n 
A 1 114 TYR 114 80  80  TYR TYR A . n 
A 1 115 LEU 115 81  81  LEU LEU A . n 
A 1 116 ALA 116 82  82  ALA ALA A . n 
A 1 117 TYR 117 83  83  TYR TYR A . n 
A 1 118 SER 118 84  84  SER SER A . n 
A 1 119 ALA 119 85  85  ALA ALA A . n 
A 1 120 ARG 120 86  86  ARG ARG A . n 
A 1 121 HIS 121 87  87  HIS HIS A . n 
A 1 122 HIS 122 88  88  HIS HIS A . n 
A 1 123 ASP 123 89  89  ASP ASP A . n 
A 1 124 TYR 124 90  90  TYR TYR A . n 
A 1 125 SER 125 91  91  SER SER A . n 
A 1 126 ARG 126 92  92  ARG ARG A . n 
A 1 127 LYS 127 93  93  LYS LYS A . n 
A 1 128 PRO 128 94  94  PRO PRO A . n 
A 1 129 LEU 129 95  95  LEU LEU A . n 
A 1 130 PHE 130 96  96  PHE PHE A . n 
A 1 131 ILE 131 97  97  ILE ILE A . n 
A 1 132 SER 132 98  98  SER SER A . n 
A 1 133 ILE 133 99  99  ILE ILE A . n 
A 1 134 SER 134 100 100 SER SER A . n 
A 1 135 GLY 135 101 101 GLY GLY A . n 
A 1 136 PHE 136 102 102 PHE PHE A . n 
A 1 137 SER 137 103 103 SER SER A . n 
A 1 138 ALA 138 104 104 ALA ALA A . n 
A 1 139 GLU 139 105 105 GLU GLU A . n 
A 1 140 GLU 140 106 106 GLU GLU A . n 
A 1 141 ASN 141 107 107 ASN ASN A . n 
A 1 142 ALA 142 108 108 ALA ALA A . n 
A 1 143 GLU 143 109 109 GLU GLU A . n 
A 1 144 MET 144 110 110 MET MET A . n 
A 1 145 CYS 145 111 111 CYS CYS A . n 
A 1 146 LYS 146 112 112 LYS LYS A . n 
A 1 147 ARG 147 113 113 ARG ARG A . n 
A 1 148 LEU 148 114 114 LEU LEU A . n 
A 1 149 ALA 149 115 115 ALA ALA A . n 
A 1 150 PRO 150 116 116 PRO PRO A . n 
A 1 151 VAL 151 117 117 VAL VAL A . n 
A 1 152 ALA 152 118 118 ALA ALA A . n 
A 1 153 ALA 153 119 119 ALA ALA A . n 
A 1 154 GLU 154 120 120 GLU GLU A . n 
A 1 155 LYS 155 121 121 LYS LYS A . n 
A 1 156 GLY 156 122 122 GLY GLY A . n 
A 1 157 VAL 157 123 123 VAL VAL A . n 
A 1 158 ILE 158 124 124 ILE ILE A . n 
A 1 159 LEU 159 125 125 LEU LEU A . n 
A 1 160 GLU 160 126 126 GLU GLU A . n 
A 1 161 LEU 161 127 127 LEU LEU A . n 
A 1 162 ASN 162 128 128 ASN ASN A . n 
A 1 163 LEU 163 129 129 LEU LEU A . n 
A 1 164 SER 164 130 130 SER SER A . n 
A 1 165 CYS 165 131 131 CYS C55 A . n 
A 1 166 PRO 166 132 132 PRO PRO A . n 
A 1 167 ASN 167 133 133 ASN ASN A . n 
A 1 168 VAL 168 134 134 VAL VAL A . n 
A 1 169 PRO 169 135 135 PRO PRO A . n 
A 1 170 GLY 170 136 136 GLY GLY A . n 
A 1 171 LYS 171 137 137 LYS LYS A . n 
A 1 172 PRO 172 138 138 PRO PRO A . n 
A 1 173 GLN 173 139 139 GLN GLN A . n 
A 1 174 VAL 174 140 140 VAL VAL A . n 
A 1 175 ALA 175 141 141 ALA ALA A . n 
A 1 176 TYR 176 142 142 TYR TYR A . n 
A 1 177 ASP 177 143 143 ASP ASP A . n 
A 1 178 PHE 178 144 144 PHE PHE A . n 
A 1 179 ASP 179 145 145 ASP ASP A . n 
A 1 180 ALA 180 146 146 ALA ALA A . n 
A 1 181 MET 181 147 147 MET MET A . n 
A 1 182 ARG 182 148 148 ARG ARG A . n 
A 1 183 ARG 183 149 149 ARG ARG A . n 
A 1 184 TYR 184 150 150 TYR TYR A . n 
A 1 185 LEU 185 151 151 LEU LEU A . n 
A 1 186 ALA 186 152 152 ALA ALA A . n 
A 1 187 ALA 187 153 153 ALA ALA A . n 
A 1 188 ILE 188 154 154 ILE ILE A . n 
A 1 189 SER 189 155 155 SER SER A . n 
A 1 190 GLU 190 156 156 GLU GLU A . n 
A 1 191 ALA 191 157 157 ALA ALA A . n 
A 1 192 TYR 192 158 158 TYR TYR A . n 
A 1 193 PRO 193 159 159 PRO PRO A . n 
A 1 194 HIS 194 160 160 HIS HIS A . n 
A 1 195 PRO 195 161 161 PRO PRO A . n 
A 1 196 PHE 196 162 162 PHE PHE A . n 
A 1 197 GLY 197 163 163 GLY GLY A . n 
A 1 198 VAL 198 164 164 VAL VAL A . n 
A 1 199 LYS 199 165 165 LYS LYS A . n 
A 1 200 MET 200 166 166 MET MET A . n 
A 1 201 PRO 201 167 167 PRO PRO A . n 
A 1 202 PRO 202 168 168 PRO PRO A . n 
A 1 203 TYR 203 169 169 TYR TYR A . n 
A 1 204 PHE 204 170 170 PHE PHE A . n 
A 1 205 ASP 205 171 171 ASP ASP A . n 
A 1 206 PHE 206 172 172 PHE PHE A . n 
A 1 207 ALA 207 173 173 ALA ALA A . n 
A 1 208 HIS 208 174 174 HIS HIS A . n 
A 1 209 PHE 209 175 175 PHE PHE A . n 
A 1 210 ASP 210 176 176 ASP ASP A . n 
A 1 211 ALA 211 177 177 ALA ALA A . n 
A 1 212 ALA 212 178 178 ALA ALA A . n 
A 1 213 ALA 213 179 179 ALA ALA A . n 
A 1 214 GLU 214 180 180 GLU GLU A . n 
A 1 215 ILE 215 181 181 ILE ILE A . n 
A 1 216 LEU 216 182 182 LEU LEU A . n 
A 1 217 ASN 217 183 183 ASN ASN A . n 
A 1 218 GLN 218 184 184 GLN GLN A . n 
A 1 219 PHE 219 185 185 PHE PHE A . n 
A 1 220 PRO 220 186 186 PRO PRO A . n 
A 1 221 LYS 221 187 187 LYS LYS A . n 
A 1 222 VAL 222 188 188 VAL VAL A . n 
A 1 223 GLN 223 189 189 GLN GLN A . n 
A 1 224 PHE 224 190 190 PHE PHE A . n 
A 1 225 ILE 225 191 191 ILE ILE A . n 
A 1 226 THR 226 192 192 THR THR A . n 
A 1 227 CYS 227 193 193 CYS CYS A . n 
A 1 228 ILE 228 194 194 ILE ILE A . n 
A 1 229 ASN 229 195 195 ASN ASN A . n 
A 1 230 SER 230 196 196 SER SER A . n 
A 1 231 ILE 231 197 197 ILE ILE A . n 
A 1 232 GLY 232 198 198 GLY GLY A . n 
A 1 233 ASN 233 199 199 ASN ASN A . n 
A 1 234 GLY 234 200 200 GLY GLY A . n 
A 1 235 LEU 235 201 201 LEU LEU A . n 
A 1 236 VAL 236 202 202 VAL VAL A . n 
A 1 237 ILE 237 203 203 ILE ILE A . n 
A 1 238 ASP 238 204 204 ASP ASP A . n 
A 1 239 VAL 239 205 205 VAL VAL A . n 
A 1 240 GLU 240 206 206 GLU GLU A . n 
A 1 241 THR 241 207 207 THR THR A . n 
A 1 242 GLU 242 208 208 GLU GLU A . n 
A 1 243 SER 243 209 209 SER SER A . n 
A 1 244 VAL 244 210 210 VAL VAL A . n 
A 1 245 VAL 245 211 211 VAL VAL A . n 
A 1 246 ILE 246 212 212 ILE ILE A . n 
A 1 247 LYS 247 213 213 LYS LYS A . n 
A 1 248 PRO 248 214 214 PRO PRO A . n 
A 1 249 LYS 249 215 215 LYS LYS A . n 
A 1 250 GLN 250 216 216 GLN GLN A . n 
A 1 251 GLY 251 217 217 GLY GLY A . n 
A 1 252 PHE 252 218 218 PHE PHE A . n 
A 1 253 GLY 253 219 219 GLY GLY A . n 
A 1 254 GLY 254 220 220 GLY GLY A . n 
A 1 255 LEU 255 221 221 LEU LEU A . n 
A 1 256 GLY 256 222 222 GLY GLY A . n 
A 1 257 GLY 257 223 223 GLY GLY A . n 
A 1 258 ARG 258 224 224 ARG ARG A . n 
A 1 259 TYR 259 225 225 TYR TYR A . n 
A 1 260 VAL 260 226 226 VAL VAL A . n 
A 1 261 PHE 261 227 227 PHE PHE A . n 
A 1 262 PRO 262 228 228 PRO PRO A . n 
A 1 263 THR 263 229 229 THR THR A . n 
A 1 264 ALA 264 230 230 ALA ALA A . n 
A 1 265 LEU 265 231 231 LEU LEU A . n 
A 1 266 ALA 266 232 232 ALA ALA A . n 
A 1 267 ASN 267 233 233 ASN ASN A . n 
A 1 268 VAL 268 234 234 VAL VAL A . n 
A 1 269 ASN 269 235 235 ASN ASN A . n 
A 1 270 ALA 270 236 236 ALA ALA A . n 
A 1 271 PHE 271 237 237 PHE PHE A . n 
A 1 272 TYR 272 238 238 TYR TYR A . n 
A 1 273 ARG 273 239 239 ARG ARG A . n 
A 1 274 ARG 274 240 240 ARG ARG A . n 
A 1 275 CYS 275 241 241 CYS CYS A . n 
A 1 276 PRO 276 242 242 PRO PRO A . n 
A 1 277 GLY 277 243 243 GLY GLY A . n 
A 1 278 LYS 278 244 244 LYS LYS A . n 
A 1 279 LEU 279 245 245 LEU LEU A . n 
A 1 280 ILE 280 246 246 ILE ILE A . n 
A 1 281 PHE 281 247 247 PHE PHE A . n 
A 1 282 GLY 282 248 248 GLY GLY A . n 
A 1 283 CYS 283 249 249 CYS CYS A . n 
A 1 284 GLY 284 250 250 GLY GLY A . n 
A 1 285 GLY 285 251 251 GLY GLY A . n 
A 1 286 VAL 286 252 252 VAL VAL A . n 
A 1 287 TYR 287 253 253 TYR TYR A . n 
A 1 288 THR 288 254 254 THR THR A . n 
A 1 289 GLY 289 255 255 GLY GLY A . n 
A 1 290 GLU 290 256 256 GLU GLU A . n 
A 1 291 ASP 291 257 257 ASP ASP A . n 
A 1 292 ALA 292 258 258 ALA ALA A . n 
A 1 293 PHE 293 259 259 PHE PHE A . n 
A 1 294 LEU 294 260 260 LEU LEU A . n 
A 1 295 HIS 295 261 261 HIS HIS A . n 
A 1 296 VAL 296 262 262 VAL VAL A . n 
A 1 297 LEU 297 263 263 LEU LEU A . n 
A 1 298 ALA 298 264 264 ALA ALA A . n 
A 1 299 GLY 299 265 265 GLY GLY A . n 
A 1 300 ALA 300 266 266 ALA ALA A . n 
A 1 301 SER 301 267 267 SER SER A . n 
A 1 302 MET 302 268 268 MET MET A . n 
A 1 303 VAL 303 269 269 VAL VAL A . n 
A 1 304 GLN 304 270 270 GLN GLN A . n 
A 1 305 VAL 305 271 271 VAL VAL A . n 
A 1 306 GLY 306 272 272 GLY GLY A . n 
A 1 307 THR 307 273 273 THR THR A . n 
A 1 308 ALA 308 274 274 ALA ALA A . n 
A 1 309 LEU 309 275 275 LEU LEU A . n 
A 1 310 HIS 310 276 276 HIS HIS A . n 
A 1 311 GLU 311 277 277 GLU GLU A . n 
A 1 312 GLU 312 278 278 GLU GLU A . n 
A 1 313 GLY 313 279 279 GLY GLY A . n 
A 1 314 ALA 314 280 280 ALA ALA A . n 
A 1 315 ALA 315 281 281 ALA ALA A . n 
A 1 316 ILE 316 282 282 ILE ILE A . n 
A 1 317 PHE 317 283 283 PHE PHE A . n 
A 1 318 GLU 318 284 284 GLU GLU A . n 
A 1 319 ARG 319 285 285 ARG ARG A . n 
A 1 320 LEU 320 286 286 LEU LEU A . n 
A 1 321 THR 321 287 287 THR THR A . n 
A 1 322 ALA 322 288 288 ALA ALA A . n 
A 1 323 GLU 323 289 289 GLU GLU A . n 
A 1 324 LEU 324 290 290 LEU LEU A . n 
A 1 325 LEU 325 291 291 LEU LEU A . n 
A 1 326 ASP 326 292 292 ASP ASP A . n 
A 1 327 VAL 327 293 293 VAL VAL A . n 
A 1 328 MET 328 294 294 MET MET A . n 
A 1 329 ALA 329 295 295 ALA ALA A . n 
A 1 330 LYS 330 296 296 LYS LYS A . n 
A 1 331 LYS 331 297 297 LYS LYS A . n 
A 1 332 GLY 332 298 298 GLY GLY A . n 
A 1 333 TYR 333 299 299 TYR TYR A . n 
A 1 334 LYS 334 300 300 LYS LYS A . n 
A 1 335 ALA 335 301 301 ALA ALA A . n 
A 1 336 LEU 336 302 302 LEU LEU A . n 
A 1 337 ASP 337 303 303 ASP ASP A . n 
A 1 338 GLU 338 304 304 GLU GLU A . n 
A 1 339 PHE 339 305 305 PHE PHE A . n 
A 1 340 ARG 340 306 306 ARG ARG A . n 
A 1 341 GLY 341 307 307 GLY GLY A . n 
A 1 342 LYS 342 308 308 LYS LYS A . n 
A 1 343 VAL 343 309 309 VAL VAL A . n 
A 1 344 LYS 344 310 310 LYS LYS A . n 
A 1 345 ALA 345 311 311 ALA ALA A . n 
A 1 346 MET 346 312 312 MET MET A . n 
A 1 347 ASP 347 313 ?   ?   ?   A . n 
B 1 1   MET 1   -33 ?   ?   ?   B . n 
B 1 2   GLY 2   -32 ?   ?   ?   B . n 
B 1 3   SER 3   -31 ?   ?   ?   B . n 
B 1 4   SER 4   -30 ?   ?   ?   B . n 
B 1 5   HIS 5   -29 ?   ?   ?   B . n 
B 1 6   HIS 6   -28 ?   ?   ?   B . n 
B 1 7   HIS 7   -27 ?   ?   ?   B . n 
B 1 8   HIS 8   -26 ?   ?   ?   B . n 
B 1 9   HIS 9   -25 ?   ?   ?   B . n 
B 1 10  HIS 10  -24 ?   ?   ?   B . n 
B 1 11  SER 11  -23 ?   ?   ?   B . n 
B 1 12  SER 12  -22 ?   ?   ?   B . n 
B 1 13  GLY 13  -21 ?   ?   ?   B . n 
B 1 14  LEU 14  -20 ?   ?   ?   B . n 
B 1 15  VAL 15  -19 ?   ?   ?   B . n 
B 1 16  PRO 16  -18 ?   ?   ?   B . n 
B 1 17  ARG 17  -17 ?   ?   ?   B . n 
B 1 18  GLY 18  -16 ?   ?   ?   B . n 
B 1 19  SER 19  -15 ?   ?   ?   B . n 
B 1 20  HIS 20  -14 ?   ?   ?   B . n 
B 1 21  MET 21  -13 ?   ?   ?   B . n 
B 1 22  ALA 22  -12 ?   ?   ?   B . n 
B 1 23  SER 23  -11 ?   ?   ?   B . n 
B 1 24  MET 24  -10 ?   ?   ?   B . n 
B 1 25  THR 25  -9  ?   ?   ?   B . n 
B 1 26  GLY 26  -8  ?   ?   ?   B . n 
B 1 27  GLY 27  -7  ?   ?   ?   B . n 
B 1 28  GLY 28  -6  ?   ?   ?   B . n 
B 1 29  GLN 29  -5  ?   ?   ?   B . n 
B 1 30  MET 30  -4  ?   ?   ?   B . n 
B 1 31  GLY 31  -3  ?   ?   ?   B . n 
B 1 32  ARG 32  -2  ?   ?   ?   B . n 
B 1 33  GLY 33  -1  ?   ?   ?   B . n 
B 1 34  SER 34  0   0   SER SER B . n 
B 1 35  MET 35  1   1   MET MET B . n 
B 1 36  SER 36  2   2   SER SER B . n 
B 1 37  LEU 37  3   3   LEU LEU B . n 
B 1 38  GLN 38  4   4   GLN GLN B . n 
B 1 39  VAL 39  5   5   VAL VAL B . n 
B 1 40  GLY 40  6   6   GLY GLY B . n 
B 1 41  ILE 41  7   7   ILE ILE B . n 
B 1 42  LEU 42  8   8   LEU LEU B . n 
B 1 43  GLY 43  9   9   GLY GLY B . n 
B 1 44  ASN 44  10  10  ASN ASN B . n 
B 1 45  THR 45  11  11  THR THR B . n 
B 1 46  PHE 46  12  12  PHE PHE B . n 
B 1 47  ALA 47  13  13  ALA ALA B . n 
B 1 48  ASN 48  14  14  ASN ASN B . n 
B 1 49  PRO 49  15  15  PRO PRO B . n 
B 1 50  PHE 50  16  16  PHE PHE B . n 
B 1 51  MET 51  17  17  MET MET B . n 
B 1 52  ASN 52  18  18  ASN ASN B . n 
B 1 53  ALA 53  19  19  ALA ALA B . n 
B 1 54  ALA 54  20  20  ALA ALA B . n 
B 1 55  GLY 55  21  21  GLY GLY B . n 
B 1 56  VAL 56  22  22  VAL VAL B . n 
B 1 57  MET 57  23  23  MET MET B . n 
B 1 58  CYS 58  24  24  CYS CYS B . n 
B 1 59  SER 59  25  25  SER SER B . n 
B 1 60  THR 60  26  26  THR THR B . n 
B 1 61  GLU 61  27  27  GLU GLU B . n 
B 1 62  GLU 62  28  28  GLU GLU B . n 
B 1 63  GLU 63  29  29  GLU GLU B . n 
B 1 64  LEU 64  30  30  LEU LEU B . n 
B 1 65  ALA 65  31  31  ALA ALA B . n 
B 1 66  ALA 66  32  32  ALA ALA B . n 
B 1 67  MET 67  33  33  MET MET B . n 
B 1 68  THR 68  34  34  THR THR B . n 
B 1 69  GLU 69  35  35  GLU GLU B . n 
B 1 70  SER 70  36  36  SER SER B . n 
B 1 71  THR 71  37  37  THR THR B . n 
B 1 72  SER 72  38  38  SER SER B . n 
B 1 73  GLY 73  39  39  GLY GLY B . n 
B 1 74  SER 74  40  40  SER SER B . n 
B 1 75  LEU 75  41  41  LEU LEU B . n 
B 1 76  ILE 76  42  42  ILE ILE B . n 
B 1 77  THR 77  43  43  THR THR B . n 
B 1 78  LYS 78  44  44  LYS LYS B . n 
B 1 79  SER 79  45  45  SER SER B . n 
B 1 80  CYS 80  46  46  CYS CYS B . n 
B 1 81  THR 81  47  47  THR THR B . n 
B 1 82  PRO 82  48  48  PRO PRO B . n 
B 1 83  ALA 83  49  49  ALA ALA B . n 
B 1 84  LEU 84  50  50  LEU LEU B . n 
B 1 85  ARG 85  51  51  ARG ARG B . n 
B 1 86  GLU 86  52  52  GLU GLU B . n 
B 1 87  GLY 87  53  53  GLY GLY B . n 
B 1 88  ASN 88  54  54  ASN ASN B . n 
B 1 89  PRO 89  55  55  PRO PRO B . n 
B 1 90  ALA 90  56  56  ALA ALA B . n 
B 1 91  PRO 91  57  57  PRO PRO B . n 
B 1 92  ARG 92  58  58  ARG ARG B . n 
B 1 93  TYR 93  59  59  TYR TYR B . n 
B 1 94  TYR 94  60  60  TYR TYR B . n 
B 1 95  THR 95  61  61  THR THR B . n 
B 1 96  LEU 96  62  62  LEU LEU B . n 
B 1 97  PRO 97  63  63  PRO PRO B . n 
B 1 98  LEU 98  64  64  LEU LEU B . n 
B 1 99  GLY 99  65  65  GLY GLY B . n 
B 1 100 SER 100 66  66  SER SER B . n 
B 1 101 ILE 101 67  67  ILE ILE B . n 
B 1 102 ASN 102 68  68  ASN ASN B . n 
B 1 103 SER 103 69  69  SER SER B . n 
B 1 104 MET 104 70  70  MET MET B . n 
B 1 105 GLY 105 71  71  GLY GLY B . n 
B 1 106 LEU 106 72  72  LEU LEU B . n 
B 1 107 PRO 107 73  73  PRO PRO B . n 
B 1 108 ASN 108 74  74  ASN ASN B . n 
B 1 109 LYS 109 75  75  LYS LYS B . n 
B 1 110 GLY 110 76  76  GLY GLY B . n 
B 1 111 PHE 111 77  77  PHE PHE B . n 
B 1 112 ASP 112 78  78  ASP ASP B . n 
B 1 113 PHE 113 79  79  PHE PHE B . n 
B 1 114 TYR 114 80  80  TYR TYR B . n 
B 1 115 LEU 115 81  81  LEU LEU B . n 
B 1 116 ALA 116 82  82  ALA ALA B . n 
B 1 117 TYR 117 83  83  TYR TYR B . n 
B 1 118 SER 118 84  84  SER SER B . n 
B 1 119 ALA 119 85  85  ALA ALA B . n 
B 1 120 ARG 120 86  86  ARG ARG B . n 
B 1 121 HIS 121 87  87  HIS HIS B . n 
B 1 122 HIS 122 88  88  HIS HIS B . n 
B 1 123 ASP 123 89  89  ASP ASP B . n 
B 1 124 TYR 124 90  90  TYR TYR B . n 
B 1 125 SER 125 91  91  SER SER B . n 
B 1 126 ARG 126 92  92  ARG ARG B . n 
B 1 127 LYS 127 93  93  LYS LYS B . n 
B 1 128 PRO 128 94  94  PRO PRO B . n 
B 1 129 LEU 129 95  95  LEU LEU B . n 
B 1 130 PHE 130 96  96  PHE PHE B . n 
B 1 131 ILE 131 97  97  ILE ILE B . n 
B 1 132 SER 132 98  98  SER SER B . n 
B 1 133 ILE 133 99  99  ILE ILE B . n 
B 1 134 SER 134 100 100 SER SER B . n 
B 1 135 GLY 135 101 101 GLY GLY B . n 
B 1 136 PHE 136 102 102 PHE PHE B . n 
B 1 137 SER 137 103 103 SER SER B . n 
B 1 138 ALA 138 104 104 ALA ALA B . n 
B 1 139 GLU 139 105 105 GLU GLU B . n 
B 1 140 GLU 140 106 106 GLU GLU B . n 
B 1 141 ASN 141 107 107 ASN ASN B . n 
B 1 142 ALA 142 108 108 ALA ALA B . n 
B 1 143 GLU 143 109 109 GLU GLU B . n 
B 1 144 MET 144 110 110 MET MET B . n 
B 1 145 CYS 145 111 111 CYS CYS B . n 
B 1 146 LYS 146 112 112 LYS LYS B . n 
B 1 147 ARG 147 113 113 ARG ARG B . n 
B 1 148 LEU 148 114 114 LEU LEU B . n 
B 1 149 ALA 149 115 115 ALA ALA B . n 
B 1 150 PRO 150 116 116 PRO PRO B . n 
B 1 151 VAL 151 117 117 VAL VAL B . n 
B 1 152 ALA 152 118 118 ALA ALA B . n 
B 1 153 ALA 153 119 119 ALA ALA B . n 
B 1 154 GLU 154 120 120 GLU GLU B . n 
B 1 155 LYS 155 121 121 LYS LYS B . n 
B 1 156 GLY 156 122 122 GLY GLY B . n 
B 1 157 VAL 157 123 123 VAL VAL B . n 
B 1 158 ILE 158 124 124 ILE ILE B . n 
B 1 159 LEU 159 125 125 LEU LEU B . n 
B 1 160 GLU 160 126 126 GLU GLU B . n 
B 1 161 LEU 161 127 127 LEU LEU B . n 
B 1 162 ASN 162 128 128 ASN ASN B . n 
B 1 163 LEU 163 129 129 LEU LEU B . n 
B 1 164 SER 164 130 130 SER SER B . n 
B 1 165 CYS 165 131 131 CYS C55 B . n 
B 1 166 PRO 166 132 132 PRO PRO B . n 
B 1 167 ASN 167 133 133 ASN ASN B . n 
B 1 168 VAL 168 134 134 VAL VAL B . n 
B 1 169 PRO 169 135 135 PRO PRO B . n 
B 1 170 GLY 170 136 136 GLY GLY B . n 
B 1 171 LYS 171 137 137 LYS LYS B . n 
B 1 172 PRO 172 138 138 PRO PRO B . n 
B 1 173 GLN 173 139 139 GLN GLN B . n 
B 1 174 VAL 174 140 140 VAL VAL B . n 
B 1 175 ALA 175 141 141 ALA ALA B . n 
B 1 176 TYR 176 142 142 TYR TYR B . n 
B 1 177 ASP 177 143 143 ASP ASP B . n 
B 1 178 PHE 178 144 144 PHE PHE B . n 
B 1 179 ASP 179 145 145 ASP ASP B . n 
B 1 180 ALA 180 146 146 ALA ALA B . n 
B 1 181 MET 181 147 147 MET MET B . n 
B 1 182 ARG 182 148 148 ARG ARG B . n 
B 1 183 ARG 183 149 149 ARG ARG B . n 
B 1 184 TYR 184 150 150 TYR TYR B . n 
B 1 185 LEU 185 151 151 LEU LEU B . n 
B 1 186 ALA 186 152 152 ALA ALA B . n 
B 1 187 ALA 187 153 153 ALA ALA B . n 
B 1 188 ILE 188 154 154 ILE ILE B . n 
B 1 189 SER 189 155 155 SER SER B . n 
B 1 190 GLU 190 156 156 GLU GLU B . n 
B 1 191 ALA 191 157 157 ALA ALA B . n 
B 1 192 TYR 192 158 158 TYR TYR B . n 
B 1 193 PRO 193 159 159 PRO PRO B . n 
B 1 194 HIS 194 160 160 HIS HIS B . n 
B 1 195 PRO 195 161 161 PRO PRO B . n 
B 1 196 PHE 196 162 162 PHE PHE B . n 
B 1 197 GLY 197 163 163 GLY GLY B . n 
B 1 198 VAL 198 164 164 VAL VAL B . n 
B 1 199 LYS 199 165 165 LYS LYS B . n 
B 1 200 MET 200 166 166 MET MET B . n 
B 1 201 PRO 201 167 167 PRO PRO B . n 
B 1 202 PRO 202 168 168 PRO PRO B . n 
B 1 203 TYR 203 169 169 TYR TYR B . n 
B 1 204 PHE 204 170 170 PHE PHE B . n 
B 1 205 ASP 205 171 171 ASP ASP B . n 
B 1 206 PHE 206 172 172 PHE PHE B . n 
B 1 207 ALA 207 173 173 ALA ALA B . n 
B 1 208 HIS 208 174 174 HIS HIS B . n 
B 1 209 PHE 209 175 175 PHE PHE B . n 
B 1 210 ASP 210 176 176 ASP ASP B . n 
B 1 211 ALA 211 177 177 ALA ALA B . n 
B 1 212 ALA 212 178 178 ALA ALA B . n 
B 1 213 ALA 213 179 179 ALA ALA B . n 
B 1 214 GLU 214 180 180 GLU GLU B . n 
B 1 215 ILE 215 181 181 ILE ILE B . n 
B 1 216 LEU 216 182 182 LEU LEU B . n 
B 1 217 ASN 217 183 183 ASN ASN B . n 
B 1 218 GLN 218 184 184 GLN GLN B . n 
B 1 219 PHE 219 185 185 PHE PHE B . n 
B 1 220 PRO 220 186 186 PRO PRO B . n 
B 1 221 LYS 221 187 187 LYS LYS B . n 
B 1 222 VAL 222 188 188 VAL VAL B . n 
B 1 223 GLN 223 189 189 GLN GLN B . n 
B 1 224 PHE 224 190 190 PHE PHE B . n 
B 1 225 ILE 225 191 191 ILE ILE B . n 
B 1 226 THR 226 192 192 THR THR B . n 
B 1 227 CYS 227 193 193 CYS CYS B . n 
B 1 228 ILE 228 194 194 ILE ILE B . n 
B 1 229 ASN 229 195 195 ASN ASN B . n 
B 1 230 SER 230 196 196 SER SER B . n 
B 1 231 ILE 231 197 197 ILE ILE B . n 
B 1 232 GLY 232 198 198 GLY GLY B . n 
B 1 233 ASN 233 199 199 ASN ASN B . n 
B 1 234 GLY 234 200 200 GLY GLY B . n 
B 1 235 LEU 235 201 201 LEU LEU B . n 
B 1 236 VAL 236 202 202 VAL VAL B . n 
B 1 237 ILE 237 203 203 ILE ILE B . n 
B 1 238 ASP 238 204 204 ASP ASP B . n 
B 1 239 VAL 239 205 205 VAL VAL B . n 
B 1 240 GLU 240 206 206 GLU GLU B . n 
B 1 241 THR 241 207 207 THR THR B . n 
B 1 242 GLU 242 208 208 GLU GLU B . n 
B 1 243 SER 243 209 209 SER SER B . n 
B 1 244 VAL 244 210 210 VAL VAL B . n 
B 1 245 VAL 245 211 211 VAL VAL B . n 
B 1 246 ILE 246 212 212 ILE ILE B . n 
B 1 247 LYS 247 213 213 LYS LYS B . n 
B 1 248 PRO 248 214 214 PRO PRO B . n 
B 1 249 LYS 249 215 215 LYS LYS B . n 
B 1 250 GLN 250 216 216 GLN GLN B . n 
B 1 251 GLY 251 217 217 GLY GLY B . n 
B 1 252 PHE 252 218 218 PHE PHE B . n 
B 1 253 GLY 253 219 219 GLY GLY B . n 
B 1 254 GLY 254 220 220 GLY GLY B . n 
B 1 255 LEU 255 221 221 LEU LEU B . n 
B 1 256 GLY 256 222 222 GLY GLY B . n 
B 1 257 GLY 257 223 223 GLY GLY B . n 
B 1 258 ARG 258 224 224 ARG ARG B . n 
B 1 259 TYR 259 225 225 TYR TYR B . n 
B 1 260 VAL 260 226 226 VAL VAL B . n 
B 1 261 PHE 261 227 227 PHE PHE B . n 
B 1 262 PRO 262 228 228 PRO PRO B . n 
B 1 263 THR 263 229 229 THR THR B . n 
B 1 264 ALA 264 230 230 ALA ALA B . n 
B 1 265 LEU 265 231 231 LEU LEU B . n 
B 1 266 ALA 266 232 232 ALA ALA B . n 
B 1 267 ASN 267 233 233 ASN ASN B . n 
B 1 268 VAL 268 234 234 VAL VAL B . n 
B 1 269 ASN 269 235 235 ASN ASN B . n 
B 1 270 ALA 270 236 236 ALA ALA B . n 
B 1 271 PHE 271 237 237 PHE PHE B . n 
B 1 272 TYR 272 238 238 TYR TYR B . n 
B 1 273 ARG 273 239 239 ARG ARG B . n 
B 1 274 ARG 274 240 240 ARG ARG B . n 
B 1 275 CYS 275 241 241 CYS CYS B . n 
B 1 276 PRO 276 242 242 PRO PRO B . n 
B 1 277 GLY 277 243 243 GLY GLY B . n 
B 1 278 LYS 278 244 244 LYS LYS B . n 
B 1 279 LEU 279 245 245 LEU LEU B . n 
B 1 280 ILE 280 246 246 ILE ILE B . n 
B 1 281 PHE 281 247 247 PHE PHE B . n 
B 1 282 GLY 282 248 248 GLY GLY B . n 
B 1 283 CYS 283 249 249 CYS CYS B . n 
B 1 284 GLY 284 250 250 GLY GLY B . n 
B 1 285 GLY 285 251 251 GLY GLY B . n 
B 1 286 VAL 286 252 252 VAL VAL B . n 
B 1 287 TYR 287 253 253 TYR TYR B . n 
B 1 288 THR 288 254 254 THR THR B . n 
B 1 289 GLY 289 255 255 GLY GLY B . n 
B 1 290 GLU 290 256 256 GLU GLU B . n 
B 1 291 ASP 291 257 257 ASP ASP B . n 
B 1 292 ALA 292 258 258 ALA ALA B . n 
B 1 293 PHE 293 259 259 PHE PHE B . n 
B 1 294 LEU 294 260 260 LEU LEU B . n 
B 1 295 HIS 295 261 261 HIS HIS B . n 
B 1 296 VAL 296 262 262 VAL VAL B . n 
B 1 297 LEU 297 263 263 LEU LEU B . n 
B 1 298 ALA 298 264 264 ALA ALA B . n 
B 1 299 GLY 299 265 265 GLY GLY B . n 
B 1 300 ALA 300 266 266 ALA ALA B . n 
B 1 301 SER 301 267 267 SER SER B . n 
B 1 302 MET 302 268 268 MET MET B . n 
B 1 303 VAL 303 269 269 VAL VAL B . n 
B 1 304 GLN 304 270 270 GLN GLN B . n 
B 1 305 VAL 305 271 271 VAL VAL B . n 
B 1 306 GLY 306 272 272 GLY GLY B . n 
B 1 307 THR 307 273 273 THR THR B . n 
B 1 308 ALA 308 274 274 ALA ALA B . n 
B 1 309 LEU 309 275 275 LEU LEU B . n 
B 1 310 HIS 310 276 276 HIS HIS B . n 
B 1 311 GLU 311 277 277 GLU GLU B . n 
B 1 312 GLU 312 278 278 GLU GLU B . n 
B 1 313 GLY 313 279 279 GLY GLY B . n 
B 1 314 ALA 314 280 280 ALA ALA B . n 
B 1 315 ALA 315 281 281 ALA ALA B . n 
B 1 316 ILE 316 282 282 ILE ILE B . n 
B 1 317 PHE 317 283 283 PHE PHE B . n 
B 1 318 GLU 318 284 284 GLU GLU B . n 
B 1 319 ARG 319 285 285 ARG ARG B . n 
B 1 320 LEU 320 286 286 LEU LEU B . n 
B 1 321 THR 321 287 287 THR THR B . n 
B 1 322 ALA 322 288 288 ALA ALA B . n 
B 1 323 GLU 323 289 289 GLU GLU B . n 
B 1 324 LEU 324 290 290 LEU LEU B . n 
B 1 325 LEU 325 291 291 LEU LEU B . n 
B 1 326 ASP 326 292 292 ASP ASP B . n 
B 1 327 VAL 327 293 293 VAL VAL B . n 
B 1 328 MET 328 294 294 MET MET B . n 
B 1 329 ALA 329 295 295 ALA ALA B . n 
B 1 330 LYS 330 296 296 LYS LYS B . n 
B 1 331 LYS 331 297 297 LYS LYS B . n 
B 1 332 GLY 332 298 298 GLY GLY B . n 
B 1 333 TYR 333 299 299 TYR TYR B . n 
B 1 334 LYS 334 300 300 LYS LYS B . n 
B 1 335 ALA 335 301 301 ALA ALA B . n 
B 1 336 LEU 336 302 302 LEU LEU B . n 
B 1 337 ASP 337 303 303 ASP ASP B . n 
B 1 338 GLU 338 304 304 GLU GLU B . n 
B 1 339 PHE 339 305 305 PHE PHE B . n 
B 1 340 ARG 340 306 306 ARG ARG B . n 
B 1 341 GLY 341 307 307 GLY GLY B . n 
B 1 342 LYS 342 308 308 LYS LYS B . n 
B 1 343 VAL 343 309 309 VAL VAL B . n 
B 1 344 LYS 344 310 310 LYS LYS B . n 
B 1 345 ALA 345 311 311 ALA ALA B . n 
B 1 346 MET 346 312 312 MET MET B . n 
B 1 347 ASP 347 313 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AVS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AVS 
_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 
C 2 FMN   1   401 401 FMN   FMN A . 
D 3 GOL   1   402 402 GOL   GOL A . 
E 3 GOL   1   403 407 GOL   GOL A . 
F 4 A1AVS 1   404 131 A1AVS C55 A . 
G 3 GOL   1   401 403 GOL   GOL B . 
H 2 FMN   1   402 401 FMN   FMN B . 
I 3 GOL   1   403 405 GOL   GOL B . 
J 4 A1AVS 1   404 131 A1AVS C55 B . 
K 5 HOH   1   501 236 HOH   HOH A . 
K 5 HOH   2   502 225 HOH   HOH A . 
K 5 HOH   3   503 93  HOH   HOH A . 
K 5 HOH   4   504 77  HOH   HOH A . 
K 5 HOH   5   505 239 HOH   HOH A . 
K 5 HOH   6   506 245 HOH   HOH A . 
K 5 HOH   7   507 189 HOH   HOH A . 
K 5 HOH   8   508 29  HOH   HOH A . 
K 5 HOH   9   509 97  HOH   HOH A . 
K 5 HOH   10  510 109 HOH   HOH A . 
K 5 HOH   11  511 140 HOH   HOH A . 
K 5 HOH   12  512 149 HOH   HOH A . 
K 5 HOH   13  513 32  HOH   HOH A . 
K 5 HOH   14  514 226 HOH   HOH A . 
K 5 HOH   15  515 138 HOH   HOH A . 
K 5 HOH   16  516 87  HOH   HOH A . 
K 5 HOH   17  517 42  HOH   HOH A . 
K 5 HOH   18  518 219 HOH   HOH A . 
K 5 HOH   19  519 13  HOH   HOH A . 
K 5 HOH   20  520 61  HOH   HOH A . 
K 5 HOH   21  521 143 HOH   HOH A . 
K 5 HOH   22  522 144 HOH   HOH A . 
K 5 HOH   23  523 215 HOH   HOH A . 
K 5 HOH   24  524 249 HOH   HOH A . 
K 5 HOH   25  525 96  HOH   HOH A . 
K 5 HOH   26  526 1   HOH   HOH A . 
K 5 HOH   27  527 56  HOH   HOH A . 
K 5 HOH   28  528 213 HOH   HOH A . 
K 5 HOH   29  529 21  HOH   HOH A . 
K 5 HOH   30  530 119 HOH   HOH A . 
K 5 HOH   31  531 251 HOH   HOH A . 
K 5 HOH   32  532 147 HOH   HOH A . 
K 5 HOH   33  533 47  HOH   HOH A . 
K 5 HOH   34  534 5   HOH   HOH A . 
K 5 HOH   35  535 30  HOH   HOH A . 
K 5 HOH   36  536 60  HOH   HOH A . 
K 5 HOH   37  537 52  HOH   HOH A . 
K 5 HOH   38  538 15  HOH   HOH A . 
K 5 HOH   39  539 17  HOH   HOH A . 
K 5 HOH   40  540 115 HOH   HOH A . 
K 5 HOH   41  541 8   HOH   HOH A . 
K 5 HOH   42  542 139 HOH   HOH A . 
K 5 HOH   43  543 24  HOH   HOH A . 
K 5 HOH   44  544 232 HOH   HOH A . 
K 5 HOH   45  545 59  HOH   HOH A . 
K 5 HOH   46  546 133 HOH   HOH A . 
K 5 HOH   47  547 161 HOH   HOH A . 
K 5 HOH   48  548 23  HOH   HOH A . 
K 5 HOH   49  549 80  HOH   HOH A . 
K 5 HOH   50  550 230 HOH   HOH A . 
K 5 HOH   51  551 216 HOH   HOH A . 
K 5 HOH   52  552 40  HOH   HOH A . 
K 5 HOH   53  553 185 HOH   HOH A . 
K 5 HOH   54  554 155 HOH   HOH A . 
K 5 HOH   55  555 73  HOH   HOH A . 
K 5 HOH   56  556 53  HOH   HOH A . 
K 5 HOH   57  557 148 HOH   HOH A . 
K 5 HOH   58  558 126 HOH   HOH A . 
K 5 HOH   59  559 114 HOH   HOH A . 
K 5 HOH   60  560 50  HOH   HOH A . 
K 5 HOH   61  561 260 HOH   HOH A . 
K 5 HOH   62  562 137 HOH   HOH A . 
K 5 HOH   63  563 82  HOH   HOH A . 
K 5 HOH   64  564 120 HOH   HOH A . 
K 5 HOH   65  565 71  HOH   HOH A . 
K 5 HOH   66  566 117 HOH   HOH A . 
K 5 HOH   67  567 112 HOH   HOH A . 
K 5 HOH   68  568 242 HOH   HOH A . 
K 5 HOH   69  569 153 HOH   HOH A . 
K 5 HOH   70  570 63  HOH   HOH A . 
K 5 HOH   71  571 157 HOH   HOH A . 
K 5 HOH   72  572 46  HOH   HOH A . 
K 5 HOH   73  573 218 HOH   HOH A . 
K 5 HOH   74  574 222 HOH   HOH A . 
K 5 HOH   75  575 243 HOH   HOH A . 
K 5 HOH   76  576 83  HOH   HOH A . 
K 5 HOH   77  577 252 HOH   HOH A . 
K 5 HOH   78  578 203 HOH   HOH A . 
K 5 HOH   79  579 228 HOH   HOH A . 
K 5 HOH   80  580 164 HOH   HOH A . 
K 5 HOH   81  581 194 HOH   HOH A . 
K 5 HOH   82  582 234 HOH   HOH A . 
K 5 HOH   83  583 240 HOH   HOH A . 
L 5 HOH   1   501 264 HOH   HOH B . 
L 5 HOH   2   502 272 HOH   HOH B . 
L 5 HOH   3   503 259 HOH   HOH B . 
L 5 HOH   4   504 269 HOH   HOH B . 
L 5 HOH   5   505 266 HOH   HOH B . 
L 5 HOH   6   506 207 HOH   HOH B . 
L 5 HOH   7   507 134 HOH   HOH B . 
L 5 HOH   8   508 105 HOH   HOH B . 
L 5 HOH   9   509 27  HOH   HOH B . 
L 5 HOH   10  510 113 HOH   HOH B . 
L 5 HOH   11  511 118 HOH   HOH B . 
L 5 HOH   12  512 165 HOH   HOH B . 
L 5 HOH   13  513 121 HOH   HOH B . 
L 5 HOH   14  514 76  HOH   HOH B . 
L 5 HOH   15  515 12  HOH   HOH B . 
L 5 HOH   16  516 184 HOH   HOH B . 
L 5 HOH   17  517 217 HOH   HOH B . 
L 5 HOH   18  518 81  HOH   HOH B . 
L 5 HOH   19  519 238 HOH   HOH B . 
L 5 HOH   20  520 268 HOH   HOH B . 
L 5 HOH   21  521 4   HOH   HOH B . 
L 5 HOH   22  522 31  HOH   HOH B . 
L 5 HOH   23  523 208 HOH   HOH B . 
L 5 HOH   24  524 127 HOH   HOH B . 
L 5 HOH   25  525 190 HOH   HOH B . 
L 5 HOH   26  526 244 HOH   HOH B . 
L 5 HOH   27  527 34  HOH   HOH B . 
L 5 HOH   28  528 159 HOH   HOH B . 
L 5 HOH   29  529 51  HOH   HOH B . 
L 5 HOH   30  530 271 HOH   HOH B . 
L 5 HOH   31  531 233 HOH   HOH B . 
L 5 HOH   32  532 129 HOH   HOH B . 
L 5 HOH   33  533 19  HOH   HOH B . 
L 5 HOH   34  534 36  HOH   HOH B . 
L 5 HOH   35  535 95  HOH   HOH B . 
L 5 HOH   36  536 14  HOH   HOH B . 
L 5 HOH   37  537 20  HOH   HOH B . 
L 5 HOH   38  538 25  HOH   HOH B . 
L 5 HOH   39  539 78  HOH   HOH B . 
L 5 HOH   40  540 132 HOH   HOH B . 
L 5 HOH   41  541 130 HOH   HOH B . 
L 5 HOH   42  542 237 HOH   HOH B . 
L 5 HOH   43  543 49  HOH   HOH B . 
L 5 HOH   44  544 62  HOH   HOH B . 
L 5 HOH   45  545 65  HOH   HOH B . 
L 5 HOH   46  546 74  HOH   HOH B . 
L 5 HOH   47  547 192 HOH   HOH B . 
L 5 HOH   48  548 10  HOH   HOH B . 
L 5 HOH   49  549 72  HOH   HOH B . 
L 5 HOH   50  550 68  HOH   HOH B . 
L 5 HOH   51  551 125 HOH   HOH B . 
L 5 HOH   52  552 92  HOH   HOH B . 
L 5 HOH   53  553 67  HOH   HOH B . 
L 5 HOH   54  554 26  HOH   HOH B . 
L 5 HOH   55  555 57  HOH   HOH B . 
L 5 HOH   56  556 94  HOH   HOH B . 
L 5 HOH   57  557 3   HOH   HOH B . 
L 5 HOH   58  558 154 HOH   HOH B . 
L 5 HOH   59  559 182 HOH   HOH B . 
L 5 HOH   60  560 99  HOH   HOH B . 
L 5 HOH   61  561 66  HOH   HOH B . 
L 5 HOH   62  562 18  HOH   HOH B . 
L 5 HOH   63  563 158 HOH   HOH B . 
L 5 HOH   64  564 160 HOH   HOH B . 
L 5 HOH   65  565 110 HOH   HOH B . 
L 5 HOH   66  566 265 HOH   HOH B . 
L 5 HOH   67  567 197 HOH   HOH B . 
L 5 HOH   68  568 6   HOH   HOH B . 
L 5 HOH   69  569 250 HOH   HOH B . 
L 5 HOH   70  570 173 HOH   HOH B . 
L 5 HOH   71  571 136 HOH   HOH B . 
L 5 HOH   72  572 176 HOH   HOH B . 
L 5 HOH   73  573 166 HOH   HOH B . 
L 5 HOH   74  574 84  HOH   HOH B . 
L 5 HOH   75  575 41  HOH   HOH B . 
L 5 HOH   76  576 156 HOH   HOH B . 
L 5 HOH   77  577 35  HOH   HOH B . 
L 5 HOH   78  578 54  HOH   HOH B . 
L 5 HOH   79  579 195 HOH   HOH B . 
L 5 HOH   80  580 128 HOH   HOH B . 
L 5 HOH   81  581 7   HOH   HOH B . 
L 5 HOH   82  582 206 HOH   HOH B . 
L 5 HOH   83  583 11  HOH   HOH B . 
L 5 HOH   84  584 205 HOH   HOH B . 
L 5 HOH   85  585 100 HOH   HOH B . 
L 5 HOH   86  586 235 HOH   HOH B . 
L 5 HOH   87  587 163 HOH   HOH B . 
L 5 HOH   88  588 227 HOH   HOH B . 
L 5 HOH   89  589 28  HOH   HOH B . 
L 5 HOH   90  590 199 HOH   HOH B . 
L 5 HOH   91  591 247 HOH   HOH B . 
L 5 HOH   92  592 79  HOH   HOH B . 
L 5 HOH   93  593 55  HOH   HOH B . 
L 5 HOH   94  594 142 HOH   HOH B . 
L 5 HOH   95  595 102 HOH   HOH B . 
L 5 HOH   96  596 64  HOH   HOH B . 
L 5 HOH   97  597 263 HOH   HOH B . 
L 5 HOH   98  598 22  HOH   HOH B . 
L 5 HOH   99  599 167 HOH   HOH B . 
L 5 HOH   100 600 39  HOH   HOH B . 
L 5 HOH   101 601 108 HOH   HOH B . 
L 5 HOH   102 602 33  HOH   HOH B . 
L 5 HOH   103 603 45  HOH   HOH B . 
L 5 HOH   104 604 70  HOH   HOH B . 
L 5 HOH   105 605 9   HOH   HOH B . 
L 5 HOH   106 606 103 HOH   HOH B . 
L 5 HOH   107 607 270 HOH   HOH B . 
L 5 HOH   108 608 223 HOH   HOH B . 
L 5 HOH   109 609 37  HOH   HOH B . 
L 5 HOH   110 610 170 HOH   HOH B . 
L 5 HOH   111 611 204 HOH   HOH B . 
L 5 HOH   112 612 44  HOH   HOH B . 
L 5 HOH   113 613 89  HOH   HOH B . 
L 5 HOH   114 614 135 HOH   HOH B . 
L 5 HOH   115 615 122 HOH   HOH B . 
L 5 HOH   116 616 98  HOH   HOH B . 
L 5 HOH   117 617 104 HOH   HOH B . 
L 5 HOH   118 618 123 HOH   HOH B . 
L 5 HOH   119 619 152 HOH   HOH B . 
L 5 HOH   120 620 193 HOH   HOH B . 
L 5 HOH   121 621 75  HOH   HOH B . 
L 5 HOH   122 622 48  HOH   HOH B . 
L 5 HOH   123 623 179 HOH   HOH B . 
L 5 HOH   124 624 58  HOH   HOH B . 
L 5 HOH   125 625 172 HOH   HOH B . 
L 5 HOH   126 626 145 HOH   HOH B . 
L 5 HOH   127 627 91  HOH   HOH B . 
L 5 HOH   128 628 186 HOH   HOH B . 
L 5 HOH   129 629 16  HOH   HOH B . 
L 5 HOH   130 630 106 HOH   HOH B . 
L 5 HOH   131 631 254 HOH   HOH B . 
L 5 HOH   132 632 88  HOH   HOH B . 
L 5 HOH   133 633 86  HOH   HOH B . 
L 5 HOH   134 634 85  HOH   HOH B . 
L 5 HOH   135 635 211 HOH   HOH B . 
L 5 HOH   136 636 177 HOH   HOH B . 
L 5 HOH   137 637 212 HOH   HOH B . 
L 5 HOH   138 638 221 HOH   HOH B . 
L 5 HOH   139 639 107 HOH   HOH B . 
L 5 HOH   140 640 246 HOH   HOH B . 
L 5 HOH   141 641 116 HOH   HOH B . 
L 5 HOH   142 642 255 HOH   HOH B . 
L 5 HOH   143 643 111 HOH   HOH B . 
L 5 HOH   144 644 150 HOH   HOH B . 
L 5 HOH   145 645 214 HOH   HOH B . 
L 5 HOH   146 646 183 HOH   HOH B . 
L 5 HOH   147 647 43  HOH   HOH B . 
L 5 HOH   148 648 124 HOH   HOH B . 
L 5 HOH   149 649 181 HOH   HOH B . 
L 5 HOH   150 650 169 HOH   HOH B . 
L 5 HOH   151 651 178 HOH   HOH B . 
L 5 HOH   152 652 231 HOH   HOH B . 
L 5 HOH   153 653 69  HOH   HOH B . 
L 5 HOH   154 654 38  HOH   HOH B . 
L 5 HOH   155 655 174 HOH   HOH B . 
L 5 HOH   156 656 210 HOH   HOH B . 
L 5 HOH   157 657 209 HOH   HOH B . 
L 5 HOH   158 658 90  HOH   HOH B . 
L 5 HOH   159 659 261 HOH   HOH B . 
L 5 HOH   160 660 101 HOH   HOH B . 
L 5 HOH   161 661 131 HOH   HOH B . 
L 5 HOH   162 662 188 HOH   HOH B . 
L 5 HOH   163 663 187 HOH   HOH B . 
L 5 HOH   164 664 220 HOH   HOH B . 
L 5 HOH   165 665 201 HOH   HOH B . 
L 5 HOH   166 666 151 HOH   HOH B . 
L 5 HOH   167 667 171 HOH   HOH B . 
L 5 HOH   168 668 200 HOH   HOH B . 
L 5 HOH   169 669 198 HOH   HOH B . 
L 5 HOH   170 670 162 HOH   HOH B . 
L 5 HOH   171 671 224 HOH   HOH B . 
L 5 HOH   172 672 146 HOH   HOH B . 
L 5 HOH   173 673 180 HOH   HOH B . 
L 5 HOH   174 674 168 HOH   HOH B . 
L 5 HOH   175 675 141 HOH   HOH B . 
L 5 HOH   176 676 196 HOH   HOH B . 
L 5 HOH   177 677 175 HOH   HOH B . 
L 5 HOH   178 678 253 HOH   HOH B . 
L 5 HOH   179 679 256 HOH   HOH B . 
# 
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 GLU 27  ? CB  ? A GLU 61  CB  
2  1 Y 1 A GLU 27  ? CG  ? A GLU 61  CG  
3  1 Y 1 A GLU 27  ? CD  ? A GLU 61  CD  
4  1 Y 1 A GLU 27  ? OE1 ? A GLU 61  OE1 
5  1 Y 1 A GLU 27  ? OE2 ? A GLU 61  OE2 
6  1 Y 1 A ARG 58  ? CG  ? A ARG 92  CG  
7  1 Y 1 A ARG 58  ? CD  ? A ARG 92  CD  
8  1 Y 1 A ARG 58  ? NE  ? A ARG 92  NE  
9  1 Y 1 A ARG 58  ? CZ  ? A ARG 92  CZ  
10 1 Y 1 A ARG 58  ? NH1 ? A ARG 92  NH1 
11 1 Y 1 A ARG 58  ? NH2 ? A ARG 92  NH2 
12 1 Y 1 A PRO 73  ? CG  ? A PRO 107 CG  
13 1 Y 1 A PRO 73  ? CD  ? A PRO 107 CD  
14 1 Y 1 A LYS 75  ? CG  ? A LYS 109 CG  
15 1 Y 1 A LYS 75  ? CD  ? A LYS 109 CD  
16 1 Y 1 A LYS 75  ? CE  ? A LYS 109 CE  
17 1 Y 1 A LYS 75  ? NZ  ? A LYS 109 NZ  
18 1 Y 1 A ALA 85  ? CB  ? A ALA 119 CB  
19 1 Y 1 A ARG 86  ? CG  ? A ARG 120 CG  
20 1 Y 1 A ARG 86  ? CD  ? A ARG 120 CD  
21 1 Y 1 A ARG 86  ? NE  ? A ARG 120 NE  
22 1 Y 1 A ARG 86  ? CZ  ? A ARG 120 CZ  
23 1 Y 1 A ARG 86  ? NH1 ? A ARG 120 NH1 
24 1 Y 1 A ARG 86  ? NH2 ? A ARG 120 NH2 
25 1 Y 1 A ARG 92  ? CD  ? A ARG 126 CD  
26 1 Y 1 A ARG 92  ? NE  ? A ARG 126 NE  
27 1 Y 1 A ARG 92  ? CZ  ? A ARG 126 CZ  
28 1 Y 1 A ARG 92  ? NH1 ? A ARG 126 NH1 
29 1 Y 1 A ARG 92  ? NH2 ? A ARG 126 NH2 
30 1 Y 1 A GLU 105 ? CG  ? A GLU 139 CG  
31 1 Y 1 A GLU 105 ? CD  ? A GLU 139 CD  
32 1 Y 1 A GLU 105 ? OE1 ? A GLU 139 OE1 
33 1 Y 1 A GLU 105 ? OE2 ? A GLU 139 OE2 
34 1 Y 1 A GLU 109 ? CG  ? A GLU 143 CG  
35 1 Y 1 A GLU 109 ? CD  ? A GLU 143 CD  
36 1 Y 1 A GLU 109 ? OE1 ? A GLU 143 OE1 
37 1 Y 1 A GLU 109 ? OE2 ? A GLU 143 OE2 
38 1 Y 1 A GLU 120 ? CG  ? A GLU 154 CG  
39 1 Y 1 A GLU 120 ? CD  ? A GLU 154 CD  
40 1 Y 1 A GLU 120 ? OE1 ? A GLU 154 OE1 
41 1 Y 1 A GLU 120 ? OE2 ? A GLU 154 OE2 
42 1 Y 1 A PRO 135 ? CG  ? A PRO 169 CG  
43 1 Y 1 A PRO 135 ? CD  ? A PRO 169 CD  
44 1 Y 1 A GLU 156 ? CD  ? A GLU 190 CD  
45 1 Y 1 A GLU 156 ? OE1 ? A GLU 190 OE1 
46 1 Y 1 A GLU 156 ? OE2 ? A GLU 190 OE2 
47 1 Y 1 A GLU 206 ? CD  ? A GLU 240 CD  
48 1 Y 1 A GLU 206 ? OE1 ? A GLU 240 OE1 
49 1 Y 1 A GLU 206 ? OE2 ? A GLU 240 OE2 
50 1 Y 1 A LYS 213 ? CG  ? A LYS 247 CG  
51 1 Y 1 A LYS 213 ? CD  ? A LYS 247 CD  
52 1 Y 1 A LYS 213 ? CE  ? A LYS 247 CE  
53 1 Y 1 A LYS 213 ? NZ  ? A LYS 247 NZ  
54 1 Y 1 A LYS 296 ? CD  ? A LYS 330 CD  
55 1 Y 1 A LYS 296 ? CE  ? A LYS 330 CE  
56 1 Y 1 A LYS 296 ? NZ  ? A LYS 330 NZ  
57 1 Y 1 A LYS 308 ? CE  ? A LYS 342 CE  
58 1 Y 1 A LYS 308 ? NZ  ? A LYS 342 NZ  
59 1 Y 1 B LEU 72  ? CB  ? B LEU 106 CB  
60 1 Y 1 B LEU 72  ? CG  ? B LEU 106 CG  
61 1 Y 1 B LEU 72  ? CD1 ? B LEU 106 CD1 
62 1 Y 1 B LEU 72  ? CD2 ? B LEU 106 CD2 
63 1 Y 1 B GLU 105 ? OE1 ? B GLU 139 OE1 
64 1 Y 1 B GLU 105 ? OE2 ? B GLU 139 OE2 
65 1 Y 1 B LYS 112 ? CE  ? B LYS 146 CE  
66 1 Y 1 B LYS 112 ? NZ  ? B LYS 146 NZ  
67 1 Y 1 B LYS 137 ? CG  ? B LYS 171 CG  
68 1 Y 1 B LYS 137 ? CD  ? B LYS 171 CD  
69 1 Y 1 B LYS 137 ? CE  ? B LYS 171 CE  
70 1 Y 1 B LYS 137 ? NZ  ? B LYS 171 NZ  
71 1 Y 1 B GLU 156 ? CG  ? B GLU 190 CG  
72 1 Y 1 B GLU 156 ? CD  ? B GLU 190 CD  
73 1 Y 1 B GLU 156 ? OE1 ? B GLU 190 OE1 
74 1 Y 1 B GLU 156 ? OE2 ? B GLU 190 OE2 
75 1 Y 1 B GLU 180 ? CD  ? B GLU 214 CD  
76 1 Y 1 B GLU 180 ? OE1 ? B GLU 214 OE1 
77 1 Y 1 B GLU 180 ? OE2 ? B GLU 214 OE2 
78 1 Y 1 B LYS 215 ? CG  ? B LYS 249 CG  
79 1 Y 1 B LYS 215 ? CD  ? B LYS 249 CD  
80 1 Y 1 B LYS 215 ? CE  ? B LYS 249 CE  
81 1 Y 1 B LYS 215 ? NZ  ? B LYS 249 NZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CB8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.540 
_cell.length_a_esd                 ? 
_cell.length_b                     104.780 
_cell.length_b_esd                 ? 
_cell.length_c                     106.840 
_cell.length_c_esd                 ? 
_cell.volume                       688921.543 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CB8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CB8 
_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             2.3 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.58 
_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              5.6 
_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    'Ammonium sulfate, lithium sulfate, sodium citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294.15 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-24 
_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   0.98011 
_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                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98011 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          35.61 
_reflns.entry_id                                       9CB8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               39.89 
_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                                     133352 
_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                           99.04 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.67 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.08916 
_reflns.pdbx_Rpim_I_all                                0.03326 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.08265 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.77 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4337 
_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                                  0.202 
_reflns_shell.pdbx_CC_star                                  0.58 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               44.26 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CB8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.75 
_refine.ls_d_res_low                             39.89 
_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                     133320 
_refine.ls_number_reflns_R_free                  6683 
_refine.ls_number_reflns_R_work                  126637 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.04 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1705 
_refine.ls_R_factor_R_free                       0.1943 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1693 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.8612 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2648 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        39.89 
_refine_hist.number_atoms_solvent             262 
_refine_hist.number_atoms_total               4990 
_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        4642 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_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' ? 0.0096  ? 4882 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0362  ? 6621 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0866  ? 719  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0078  ? 848  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.2407 ? 699  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.75 1.77  . . 219 4112 97.19 . . . . 0.4047 . . . . . . . . . . . 0.4084 
'X-RAY DIFFRACTION' 1.77 1.79  . . 222 4208 98.07 . . . . 0.3660 . . . . . . . . . . . 0.3315 
'X-RAY DIFFRACTION' 1.79 1.81  . . 223 4270 98.36 . . . . 0.3512 . . . . . . . . . . . 0.3525 
'X-RAY DIFFRACTION' 1.81 1.84  . . 219 4126 98.21 . . . . 0.3030 . . . . . . . . . . . 0.2849 
'X-RAY DIFFRACTION' 1.84 1.86  . . 219 4189 98.37 . . . . 0.2938 . . . . . . . . . . . 0.3121 
'X-RAY DIFFRACTION' 1.86 1.89  . . 217 4191 98.61 . . . . 0.2771 . . . . . . . . . . . 0.3203 
'X-RAY DIFFRACTION' 1.89 1.91  . . 223 4182 98.59 . . . . 0.2618 . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 1.91 1.94  . . 220 4210 98.23 . . . . 0.2506 . . . . . . . . . . . 0.2999 
'X-RAY DIFFRACTION' 1.94 1.97  . . 217 4205 98.75 . . . . 0.2453 . . . . . . . . . . . 0.2536 
'X-RAY DIFFRACTION' 1.97 2.00  . . 223 4185 98.86 . . . . 0.2333 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 2.00 2.04  . . 226 4231 98.93 . . . . 0.2291 . . . . . . . . . . . 0.2355 
'X-RAY DIFFRACTION' 2.04 2.07  . . 225 4227 99.04 . . . . 0.2082 . . . . . . . . . . . 0.2678 
'X-RAY DIFFRACTION' 2.07 2.11  . . 223 4200 98.84 . . . . 0.1915 . . . . . . . . . . . 0.2330 
'X-RAY DIFFRACTION' 2.11 2.16  . . 222 4233 99.00 . . . . 0.1906 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 2.16 2.20  . . 221 4232 99.02 . . . . 0.1780 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 2.20 2.26  . . 226 4195 99.10 . . . . 0.1707 . . . . . . . . . . . 0.1973 
'X-RAY DIFFRACTION' 2.26 2.31  . . 225 4244 99.18 . . . . 0.1669 . . . . . . . . . . . 0.1865 
'X-RAY DIFFRACTION' 2.31 2.37  . . 221 4292 99.03 . . . . 0.1653 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 2.38 2.44  . . 218 4167 99.23 . . . . 0.1641 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 2.44 2.52  . . 224 4247 99.55 . . . . 0.1648 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 2.52 2.61  . . 228 4242 99.49 . . . . 0.1689 . . . . . . . . . . . 0.2099 
'X-RAY DIFFRACTION' 2.61 2.72  . . 219 4207 99.48 . . . . 0.1671 . . . . . . . . . . . 0.2047 
'X-RAY DIFFRACTION' 2.72 2.84  . . 228 4248 99.53 . . . . 0.1631 . . . . . . . . . . . 0.2262 
'X-RAY DIFFRACTION' 2.84 2.99  . . 221 4269 99.60 . . . . 0.1628 . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 2.99 3.18  . . 228 4258 99.73 . . . . 0.1813 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 3.18 3.42  . . 223 4254 99.84 . . . . 0.1606 . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 3.42 3.77  . . 226 4250 99.80 . . . . 0.1496 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 3.77 4.31  . . 229 4248 99.93 . . . . 0.1297 . . . . . . . . . . . 0.1431 
'X-RAY DIFFRACTION' 4.31 5.43  . . 223 4264 99.89 . . . . 0.1311 . . . . . . . . . . . 0.1337 
'X-RAY DIFFRACTION' 5.43 39.89 . . 225 4251 99.75 . . . . 0.1755 . . . . . . . . . . . 0.1799 
# 
_struct.entry_id                     9CB8 
_struct.title                        
;Crystal structure of dihydroorotate dehydrogenase from Leishmania brasiliensis in complex with 5-benzylidenepyrimidine-2,4,6(1H,3H,5H)-trione
;
_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        9CB8 
_struct_keywords.text            'LbDHODH, covalent, inhibitor, orotate, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    E9AI53_LEIBR 
_struct_ref.pdbx_db_accession          E9AI53 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLQVGILGNTFANPFMNAAGVMCSTEEELAAMTESTSGSLITKSCTPALREGNPAPRYYTLPLGSINSMGLPNKGFDFY
LAYSARHHDYSRKPLFISISGFSAEENAEMCKRLAPVAAEKGVILELNLSCPNVPGKPQVAYDFDAMRRYLAAISEAYPH
PFGVKMPPYFDFAHFDAAAEILNQFPKVQFITCINSIGNGLVIDVETESVVIKPKQGFGGLGGRYVFPTALANVNAFYRR
CPGKLIFGCGGVYTGEDAFLHVLAGASMVQVGTALHEEGAAIFERLTAELLDVMAKKGYKALDEFRGKVKAMD
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CB8 A 35 ? 347 ? E9AI53 1 ? 313 ? 1 313 
2 1 9CB8 B 35 ? 347 ? E9AI53 1 ? 313 ? 1 313 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CB8 MET A 1  ? UNP E9AI53 ? ? 'initiating methionine' -33 1  
1 9CB8 GLY A 2  ? UNP E9AI53 ? ? 'expression tag'        -32 2  
1 9CB8 SER A 3  ? UNP E9AI53 ? ? 'expression tag'        -31 3  
1 9CB8 SER A 4  ? UNP E9AI53 ? ? 'expression tag'        -30 4  
1 9CB8 HIS A 5  ? UNP E9AI53 ? ? 'expression tag'        -29 5  
1 9CB8 HIS A 6  ? UNP E9AI53 ? ? 'expression tag'        -28 6  
1 9CB8 HIS A 7  ? UNP E9AI53 ? ? 'expression tag'        -27 7  
1 9CB8 HIS A 8  ? UNP E9AI53 ? ? 'expression tag'        -26 8  
1 9CB8 HIS A 9  ? UNP E9AI53 ? ? 'expression tag'        -25 9  
1 9CB8 HIS A 10 ? UNP E9AI53 ? ? 'expression tag'        -24 10 
1 9CB8 SER A 11 ? UNP E9AI53 ? ? 'expression tag'        -23 11 
1 9CB8 SER A 12 ? UNP E9AI53 ? ? 'expression tag'        -22 12 
1 9CB8 GLY A 13 ? UNP E9AI53 ? ? 'expression tag'        -21 13 
1 9CB8 LEU A 14 ? UNP E9AI53 ? ? 'expression tag'        -20 14 
1 9CB8 VAL A 15 ? UNP E9AI53 ? ? 'expression tag'        -19 15 
1 9CB8 PRO A 16 ? UNP E9AI53 ? ? 'expression tag'        -18 16 
1 9CB8 ARG A 17 ? UNP E9AI53 ? ? 'expression tag'        -17 17 
1 9CB8 GLY A 18 ? UNP E9AI53 ? ? 'expression tag'        -16 18 
1 9CB8 SER A 19 ? UNP E9AI53 ? ? 'expression tag'        -15 19 
1 9CB8 HIS A 20 ? UNP E9AI53 ? ? 'expression tag'        -14 20 
1 9CB8 MET A 21 ? UNP E9AI53 ? ? 'expression tag'        -13 21 
1 9CB8 ALA A 22 ? UNP E9AI53 ? ? 'expression tag'        -12 22 
1 9CB8 SER A 23 ? UNP E9AI53 ? ? 'expression tag'        -11 23 
1 9CB8 MET A 24 ? UNP E9AI53 ? ? 'expression tag'        -10 24 
1 9CB8 THR A 25 ? UNP E9AI53 ? ? 'expression tag'        -9  25 
1 9CB8 GLY A 26 ? UNP E9AI53 ? ? 'expression tag'        -8  26 
1 9CB8 GLY A 27 ? UNP E9AI53 ? ? 'expression tag'        -7  27 
1 9CB8 GLY A 28 ? UNP E9AI53 ? ? 'expression tag'        -6  28 
1 9CB8 GLN A 29 ? UNP E9AI53 ? ? 'expression tag'        -5  29 
1 9CB8 MET A 30 ? UNP E9AI53 ? ? 'expression tag'        -4  30 
1 9CB8 GLY A 31 ? UNP E9AI53 ? ? 'expression tag'        -3  31 
1 9CB8 ARG A 32 ? UNP E9AI53 ? ? 'expression tag'        -2  32 
1 9CB8 GLY A 33 ? UNP E9AI53 ? ? 'expression tag'        -1  33 
1 9CB8 SER A 34 ? UNP E9AI53 ? ? 'expression tag'        0   34 
2 9CB8 MET B 1  ? UNP E9AI53 ? ? 'initiating methionine' -33 35 
2 9CB8 GLY B 2  ? UNP E9AI53 ? ? 'expression tag'        -32 36 
2 9CB8 SER B 3  ? UNP E9AI53 ? ? 'expression tag'        -31 37 
2 9CB8 SER B 4  ? UNP E9AI53 ? ? 'expression tag'        -30 38 
2 9CB8 HIS B 5  ? UNP E9AI53 ? ? 'expression tag'        -29 39 
2 9CB8 HIS B 6  ? UNP E9AI53 ? ? 'expression tag'        -28 40 
2 9CB8 HIS B 7  ? UNP E9AI53 ? ? 'expression tag'        -27 41 
2 9CB8 HIS B 8  ? UNP E9AI53 ? ? 'expression tag'        -26 42 
2 9CB8 HIS B 9  ? UNP E9AI53 ? ? 'expression tag'        -25 43 
2 9CB8 HIS B 10 ? UNP E9AI53 ? ? 'expression tag'        -24 44 
2 9CB8 SER B 11 ? UNP E9AI53 ? ? 'expression tag'        -23 45 
2 9CB8 SER B 12 ? UNP E9AI53 ? ? 'expression tag'        -22 46 
2 9CB8 GLY B 13 ? UNP E9AI53 ? ? 'expression tag'        -21 47 
2 9CB8 LEU B 14 ? UNP E9AI53 ? ? 'expression tag'        -20 48 
2 9CB8 VAL B 15 ? UNP E9AI53 ? ? 'expression tag'        -19 49 
2 9CB8 PRO B 16 ? UNP E9AI53 ? ? 'expression tag'        -18 50 
2 9CB8 ARG B 17 ? UNP E9AI53 ? ? 'expression tag'        -17 51 
2 9CB8 GLY B 18 ? UNP E9AI53 ? ? 'expression tag'        -16 52 
2 9CB8 SER B 19 ? UNP E9AI53 ? ? 'expression tag'        -15 53 
2 9CB8 HIS B 20 ? UNP E9AI53 ? ? 'expression tag'        -14 54 
2 9CB8 MET B 21 ? UNP E9AI53 ? ? 'expression tag'        -13 55 
2 9CB8 ALA B 22 ? UNP E9AI53 ? ? 'expression tag'        -12 56 
2 9CB8 SER B 23 ? UNP E9AI53 ? ? 'expression tag'        -11 57 
2 9CB8 MET B 24 ? UNP E9AI53 ? ? 'expression tag'        -10 58 
2 9CB8 THR B 25 ? UNP E9AI53 ? ? 'expression tag'        -9  59 
2 9CB8 GLY B 26 ? UNP E9AI53 ? ? 'expression tag'        -8  60 
2 9CB8 GLY B 27 ? UNP E9AI53 ? ? 'expression tag'        -7  61 
2 9CB8 GLY B 28 ? UNP E9AI53 ? ? 'expression tag'        -6  62 
2 9CB8 GLN B 29 ? UNP E9AI53 ? ? 'expression tag'        -5  63 
2 9CB8 MET B 30 ? UNP E9AI53 ? ? 'expression tag'        -4  64 
2 9CB8 GLY B 31 ? UNP E9AI53 ? ? 'expression tag'        -3  65 
2 9CB8 ARG B 32 ? UNP E9AI53 ? ? 'expression tag'        -2  66 
2 9CB8 GLY B 33 ? UNP E9AI53 ? ? 'expression tag'        -1  67 
2 9CB8 SER B 34 ? UNP E9AI53 ? ? 'expression tag'        0   68 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7310  ? 
1 MORE         -50   ? 
1 'SSA (A^2)'  20430 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_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 THR A 60  ? SER A 70  ? THR A 26  SER A 36  1 ? 11 
HELX_P HELX_P2  AA2 GLY A 110 ? HIS A 121 ? GLY A 76  HIS A 87  1 ? 12 
HELX_P HELX_P3  AA3 SER A 137 ? GLY A 156 ? SER A 103 GLY A 122 1 ? 20 
HELX_P HELX_P4  AA4 GLN A 173 ? TYR A 176 ? GLN A 139 TYR A 142 5 ? 4  
HELX_P HELX_P5  AA5 ASP A 177 ? TYR A 192 ? ASP A 143 TYR A 158 1 ? 16 
HELX_P HELX_P6  AA6 ASP A 205 ? ASN A 217 ? ASP A 171 ASN A 183 1 ? 13 
HELX_P HELX_P7  AA7 LYS A 247 ? GLN A 250 ? LYS A 213 GLN A 216 5 ? 4  
HELX_P HELX_P8  AA8 VAL A 260 ? CYS A 275 ? VAL A 226 CYS A 241 1 ? 16 
HELX_P HELX_P9  AA9 THR A 288 ? GLY A 299 ? THR A 254 GLY A 265 1 ? 12 
HELX_P HELX_P10 AB1 GLY A 306 ? GLY A 313 ? GLY A 272 GLY A 279 1 ? 8  
HELX_P HELX_P11 AB2 ALA A 315 ? GLY A 332 ? ALA A 281 GLY A 298 1 ? 18 
HELX_P HELX_P12 AB3 ALA A 335 ? PHE A 339 ? ALA A 301 PHE A 305 5 ? 5  
HELX_P HELX_P13 AB4 THR B 60  ? SER B 70  ? THR B 26  SER B 36  1 ? 11 
HELX_P HELX_P14 AB5 GLY B 110 ? HIS B 121 ? GLY B 76  HIS B 87  1 ? 12 
HELX_P HELX_P15 AB6 SER B 137 ? GLY B 156 ? SER B 103 GLY B 122 1 ? 20 
HELX_P HELX_P16 AB7 GLN B 173 ? TYR B 176 ? GLN B 139 TYR B 142 5 ? 4  
HELX_P HELX_P17 AB8 ASP B 177 ? TYR B 192 ? ASP B 143 TYR B 158 1 ? 16 
HELX_P HELX_P18 AB9 ASP B 205 ? ASN B 217 ? ASP B 171 ASN B 183 1 ? 13 
HELX_P HELX_P19 AC1 LYS B 247 ? GLN B 250 ? LYS B 213 GLN B 216 5 ? 4  
HELX_P HELX_P20 AC2 VAL B 260 ? CYS B 275 ? VAL B 226 CYS B 241 1 ? 16 
HELX_P HELX_P21 AC3 THR B 288 ? GLY B 299 ? THR B 254 GLY B 265 1 ? 12 
HELX_P HELX_P22 AC4 GLY B 306 ? GLY B 313 ? GLY B 272 GLY B 279 1 ? 8  
HELX_P HELX_P23 AC5 ALA B 315 ? GLY B 332 ? ALA B 281 GLY B 298 1 ? 18 
HELX_P HELX_P24 AC6 ALA B 335 ? PHE B 339 ? ALA B 301 PHE B 305 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_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 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_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 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 165 SG ? ? ? 1_555 F A1AVS . C06 ? ? A CYS 131 A A1AVS 404 1_555 ? ? ? ? ? ? ? 1.816 ? ? 
covale2 covale none ? B CYS 165 SG ? ? ? 1_555 J A1AVS . C06 ? ? B CYS 131 B A1AVS 404 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1AVS F . ? CYS A 165 ? A1AVS A 404 ? 1_555 CYS A 131 ? 1_555 C06 SG CYS 1 A1AVS None 'Covalent chemical modification' 
2 A1AVS J . ? CYS B 165 ? A1AVS B 404 ? 1_555 CYS B 131 ? 1_555 C06 SG CYS 1 A1AVS None 'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 CYS 227 A . ? CYS 193 A ILE 228 A ? ILE 194 A 1 13.89 
2 ALA 90  B . ? ALA 56  B PRO 91  B ? PRO 57  B 1 -7.40 
3 CYS 227 B . ? CYS 193 B ILE 228 B ? ILE 194 B 1 14.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 8 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 8 ? 
AA7 ? 4 ? 
AA8 ? 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 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 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 39  ? ILE A 41  ? VAL A 5   ILE A 7   
AA1 2 ASN A 44  ? PHE A 46  ? ASN A 10  PHE A 12  
AA2 1 PHE A 50  ? ASN A 52  ? PHE A 16  ASN A 18  
AA2 2 ALA A 300 ? VAL A 305 ? ALA A 266 VAL A 271 
AA2 3 LEU A 279 ? CYS A 283 ? LEU A 245 CYS A 249 
AA2 4 VAL A 222 ? CYS A 227 ? VAL A 188 CYS A 193 
AA2 5 PHE A 196 ? MET A 200 ? PHE A 162 MET A 166 
AA2 6 ILE A 158 ? ASN A 162 ? ILE A 124 ASN A 128 
AA2 7 LEU A 129 ? ILE A 133 ? LEU A 95  ILE A 99  
AA2 8 LEU A 75  ? ILE A 76  ? LEU A 41  ILE A 42  
AA3 1 TYR A 93  ? LEU A 96  ? TYR A 59  LEU A 62  
AA3 2 GLY A 99  ? ASN A 102 ? GLY A 65  ASN A 68  
AA3 3 PHE A 252 ? GLY A 257 ? PHE A 218 GLY A 223 
AA3 4 ILE A 231 ? LEU A 235 ? ILE A 197 LEU A 201 
AA4 1 ILE A 237 ? ASP A 238 ? ILE A 203 ASP A 204 
AA4 2 SER A 243 ? VAL A 244 ? SER A 209 VAL A 210 
AA5 1 VAL B 39  ? ILE B 41  ? VAL B 5   ILE B 7   
AA5 2 ASN B 44  ? PHE B 46  ? ASN B 10  PHE B 12  
AA6 1 PHE B 50  ? ASN B 52  ? PHE B 16  ASN B 18  
AA6 2 ALA B 300 ? VAL B 305 ? ALA B 266 VAL B 271 
AA6 3 LEU B 279 ? CYS B 283 ? LEU B 245 CYS B 249 
AA6 4 VAL B 222 ? CYS B 227 ? VAL B 188 CYS B 193 
AA6 5 PHE B 196 ? MET B 200 ? PHE B 162 MET B 166 
AA6 6 ILE B 158 ? ASN B 162 ? ILE B 124 ASN B 128 
AA6 7 LEU B 129 ? ILE B 133 ? LEU B 95  ILE B 99  
AA6 8 LEU B 75  ? ILE B 76  ? LEU B 41  ILE B 42  
AA7 1 TYR B 93  ? LEU B 96  ? TYR B 59  LEU B 62  
AA7 2 GLY B 99  ? ASN B 102 ? GLY B 65  ASN B 68  
AA7 3 PHE B 252 ? GLY B 257 ? PHE B 218 GLY B 223 
AA7 4 ILE B 231 ? LEU B 235 ? ILE B 197 LEU B 201 
AA8 1 ILE B 237 ? ASP B 238 ? ILE B 203 ASP B 204 
AA8 2 SER B 243 ? VAL B 244 ? SER B 209 VAL B 210 
# 
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 39  ? N VAL A 5   O PHE A 46  ? O PHE A 12  
AA2 1 2 N MET A 51  ? N MET A 17  O VAL A 305 ? O VAL A 271 
AA2 2 3 O SER A 301 ? O SER A 267 N ILE A 280 ? N ILE A 246 
AA2 3 4 O PHE A 281 ? O PHE A 247 N ILE A 225 ? N ILE A 191 
AA2 4 5 O THR A 226 ? O THR A 192 N VAL A 198 ? N VAL A 164 
AA2 5 6 O GLY A 197 ? O GLY A 163 N LEU A 161 ? N LEU A 127 
AA2 6 7 O ILE A 158 ? O ILE A 124 N ILE A 131 ? N ILE A 97  
AA2 7 8 O PHE A 130 ? O PHE A 96  N LEU A 75  ? N LEU A 41  
AA3 1 2 N LEU A 96  ? N LEU A 62  O GLY A 99  ? O GLY A 65  
AA3 2 3 N ASN A 102 ? N ASN A 68  O GLY A 254 ? O GLY A 220 
AA3 3 4 O LEU A 255 ? O LEU A 221 N ILE A 231 ? N ILE A 197 
AA4 1 2 N ASP A 238 ? N ASP A 204 O SER A 243 ? O SER A 209 
AA5 1 2 N VAL B 39  ? N VAL B 5   O PHE B 46  ? O PHE B 12  
AA6 1 2 N MET B 51  ? N MET B 17  O VAL B 305 ? O VAL B 271 
AA6 2 3 O SER B 301 ? O SER B 267 N ILE B 280 ? N ILE B 246 
AA6 3 4 O PHE B 281 ? O PHE B 247 N ILE B 225 ? N ILE B 191 
AA6 4 5 O THR B 226 ? O THR B 192 N VAL B 198 ? N VAL B 164 
AA6 5 6 O GLY B 197 ? O GLY B 163 N LEU B 161 ? N LEU B 127 
AA6 6 7 O GLU B 160 ? O GLU B 126 N ILE B 131 ? N ILE B 97  
AA6 7 8 O PHE B 130 ? O PHE B 96  N LEU B 75  ? N LEU B 41  
AA7 1 2 N LEU B 96  ? N LEU B 62  O GLY B 99  ? O GLY B 65  
AA7 2 3 N ASN B 102 ? N ASN B 68  O GLY B 254 ? O GLY B 220 
AA7 3 4 O LEU B 255 ? O LEU B 221 N ILE B 231 ? N ILE B 197 
AA8 1 2 N ASP B 238 ? N ASP B 204 O SER B 243 ? O SER B 209 
# 
_pdbx_entry_details.entry_id                   9CB8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1  A ASP 78  ? ? HH22 A ARG 113 ? ? 1.38 
2 1 HH11 B ARG 86  ? ? O    B HOH 501 ? ? 1.51 
3 1 OD1  B ASP 78  ? ? HH22 B ARG 113 ? ? 1.52 
4 1 NH1  B ARG 86  ? ? O    B HOH 501 ? ? 1.84 
5 1 O    B HOH 570 ? ? O    B HOH 659 ? ? 2.08 
6 1 OD1  A ASP 78  ? ? NH2  A ARG 113 ? ? 2.10 
7 1 O1   B GOL 401 ? ? O    B HOH 502 ? ? 2.10 
8 1 NZ   B LYS 121 ? ? O    B HOH 503 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 564 ? ? 1_555 O B HOH 551 ? ? 3_544 2.16 
2 1 ND1 B HIS 276 ? ? 1_555 O B HOH 501 ? ? 4_454 2.16 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CA A CYS 131 ? ? C A CYS 131 ? ? 1.337 1.525 -0.188 0.026 N 
2 1 CA B CYS 131 ? ? C B CYS 131 ? ? 1.359 1.525 -0.166 0.026 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS A 24  ? ? -160.13 14.06  
2 1 ARG A 86  ? ? -145.20 19.97  
3 1 SER A 130 ? ? -142.08 20.55  
4 1 CYS B 24  ? ? -155.63 23.11  
5 1 CYS B 24  ? ? -159.38 23.11  
6 1 SER B 100 ? ? -150.59 61.29  
7 1 SER B 130 ? ? -144.33 14.89  
8 1 GLN B 139 ? A -38.16  117.89 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 -33 ? A MET 1   
2  1 Y 1 A GLY -32 ? A GLY 2   
3  1 Y 1 A SER -31 ? A SER 3   
4  1 Y 1 A SER -30 ? A SER 4   
5  1 Y 1 A HIS -29 ? A HIS 5   
6  1 Y 1 A HIS -28 ? A HIS 6   
7  1 Y 1 A HIS -27 ? A HIS 7   
8  1 Y 1 A HIS -26 ? A HIS 8   
9  1 Y 1 A HIS -25 ? A HIS 9   
10 1 Y 1 A HIS -24 ? A HIS 10  
11 1 Y 1 A SER -23 ? A SER 11  
12 1 Y 1 A SER -22 ? A SER 12  
13 1 Y 1 A GLY -21 ? A GLY 13  
14 1 Y 1 A LEU -20 ? A LEU 14  
15 1 Y 1 A VAL -19 ? A VAL 15  
16 1 Y 1 A PRO -18 ? A PRO 16  
17 1 Y 1 A ARG -17 ? A ARG 17  
18 1 Y 1 A GLY -16 ? A GLY 18  
19 1 Y 1 A SER -15 ? A SER 19  
20 1 Y 1 A HIS -14 ? A HIS 20  
21 1 Y 1 A MET -13 ? A MET 21  
22 1 Y 1 A ALA -12 ? A ALA 22  
23 1 Y 1 A SER -11 ? A SER 23  
24 1 Y 1 A MET -10 ? A MET 24  
25 1 Y 1 A THR -9  ? A THR 25  
26 1 Y 1 A GLY -8  ? A GLY 26  
27 1 Y 1 A GLY -7  ? A GLY 27  
28 1 Y 1 A GLY -6  ? A GLY 28  
29 1 Y 1 A GLN -5  ? A GLN 29  
30 1 Y 1 A MET -4  ? A MET 30  
31 1 Y 1 A GLY -3  ? A GLY 31  
32 1 Y 1 A ARG -2  ? A ARG 32  
33 1 Y 1 A GLY -1  ? A GLY 33  
34 1 Y 1 A ALA 49  ? A ALA 83  
35 1 Y 1 A LEU 50  ? A LEU 84  
36 1 Y 1 A ARG 51  ? A ARG 85  
37 1 Y 1 A GLU 52  ? A GLU 86  
38 1 Y 1 A GLY 53  ? A GLY 87  
39 1 Y 1 A ASN 54  ? A ASN 88  
40 1 Y 1 A PRO 55  ? A PRO 89  
41 1 Y 1 A ALA 56  ? A ALA 90  
42 1 Y 1 A LEU 72  ? A LEU 106 
43 1 Y 1 A ASP 313 ? A ASP 347 
44 1 Y 1 B MET -33 ? B MET 1   
45 1 Y 1 B GLY -32 ? B GLY 2   
46 1 Y 1 B SER -31 ? B SER 3   
47 1 Y 1 B SER -30 ? B SER 4   
48 1 Y 1 B HIS -29 ? B HIS 5   
49 1 Y 1 B HIS -28 ? B HIS 6   
50 1 Y 1 B HIS -27 ? B HIS 7   
51 1 Y 1 B HIS -26 ? B HIS 8   
52 1 Y 1 B HIS -25 ? B HIS 9   
53 1 Y 1 B HIS -24 ? B HIS 10  
54 1 Y 1 B SER -23 ? B SER 11  
55 1 Y 1 B SER -22 ? B SER 12  
56 1 Y 1 B GLY -21 ? B GLY 13  
57 1 Y 1 B LEU -20 ? B LEU 14  
58 1 Y 1 B VAL -19 ? B VAL 15  
59 1 Y 1 B PRO -18 ? B PRO 16  
60 1 Y 1 B ARG -17 ? B ARG 17  
61 1 Y 1 B GLY -16 ? B GLY 18  
62 1 Y 1 B SER -15 ? B SER 19  
63 1 Y 1 B HIS -14 ? B HIS 20  
64 1 Y 1 B MET -13 ? B MET 21  
65 1 Y 1 B ALA -12 ? B ALA 22  
66 1 Y 1 B SER -11 ? B SER 23  
67 1 Y 1 B MET -10 ? B MET 24  
68 1 Y 1 B THR -9  ? B THR 25  
69 1 Y 1 B GLY -8  ? B GLY 26  
70 1 Y 1 B GLY -7  ? B GLY 27  
71 1 Y 1 B GLY -6  ? B GLY 28  
72 1 Y 1 B GLN -5  ? B GLN 29  
73 1 Y 1 B MET -4  ? B MET 30  
74 1 Y 1 B GLY -3  ? B GLY 31  
75 1 Y 1 B ARG -2  ? B ARG 32  
76 1 Y 1 B GLY -1  ? B GLY 33  
77 1 Y 1 B ASP 313 ? B ASP 347 
# 
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 
A1AVS C02    C N N 1   
A1AVS C04    C N N 2   
A1AVS C05    C N N 3   
A1AVS C06    C N N 4   
A1AVS C14    C Y N 5   
A1AVS C15    C Y N 6   
A1AVS C16    C Y N 7   
A1AVS C17    C Y N 8   
A1AVS C18    C Y N 9   
A1AVS C19    C Y N 10  
A1AVS C22    C N N 11  
A1AVS N03    N N N 12  
A1AVS N21    N N N 13  
A1AVS O01    O N N 14  
A1AVS O20    O N N 15  
A1AVS O23    O N N 16  
A1AVS H051   H N N 17  
A1AVS H1     H N N 18  
A1AVS H061   H N N 19  
A1AVS H151   H N N 20  
A1AVS H161   H N N 21  
A1AVS H171   H N N 22  
A1AVS H181   H N N 23  
A1AVS H191   H N N 24  
A1AVS H031   H N N 25  
A1AVS H211   H N N 26  
ALA   N      N N N 27  
ALA   CA     C N S 28  
ALA   C      C N N 29  
ALA   O      O N N 30  
ALA   CB     C N N 31  
ALA   OXT    O N N 32  
ALA   H      H N N 33  
ALA   H2     H N N 34  
ALA   HA     H N N 35  
ALA   HB1    H N N 36  
ALA   HB2    H N N 37  
ALA   HB3    H N N 38  
ALA   HXT    H N N 39  
ARG   N      N N N 40  
ARG   CA     C N S 41  
ARG   C      C N N 42  
ARG   O      O N N 43  
ARG   CB     C N N 44  
ARG   CG     C N N 45  
ARG   CD     C N N 46  
ARG   NE     N N N 47  
ARG   CZ     C N N 48  
ARG   NH1    N N N 49  
ARG   NH2    N N N 50  
ARG   OXT    O N N 51  
ARG   H      H N N 52  
ARG   H2     H N N 53  
ARG   HA     H N N 54  
ARG   HB2    H N N 55  
ARG   HB3    H N N 56  
ARG   HG2    H N N 57  
ARG   HG3    H N N 58  
ARG   HD2    H N N 59  
ARG   HD3    H N N 60  
ARG   HE     H N N 61  
ARG   HH11   H N N 62  
ARG   HH12   H N N 63  
ARG   HH21   H N N 64  
ARG   HH22   H N N 65  
ARG   HXT    H N N 66  
ASN   N      N N N 67  
ASN   CA     C N S 68  
ASN   C      C N N 69  
ASN   O      O N N 70  
ASN   CB     C N N 71  
ASN   CG     C N N 72  
ASN   OD1    O N N 73  
ASN   ND2    N N N 74  
ASN   OXT    O N N 75  
ASN   H      H N N 76  
ASN   H2     H N N 77  
ASN   HA     H N N 78  
ASN   HB2    H N N 79  
ASN   HB3    H N N 80  
ASN   HD21   H N N 81  
ASN   HD22   H N N 82  
ASN   HXT    H N N 83  
ASP   N      N N N 84  
ASP   CA     C N S 85  
ASP   C      C N N 86  
ASP   O      O N N 87  
ASP   CB     C N N 88  
ASP   CG     C N N 89  
ASP   OD1    O N N 90  
ASP   OD2    O N N 91  
ASP   OXT    O N N 92  
ASP   H      H N N 93  
ASP   H2     H N N 94  
ASP   HA     H N N 95  
ASP   HB2    H N N 96  
ASP   HB3    H N N 97  
ASP   HD2    H N N 98  
ASP   HXT    H N N 99  
CYS   N      N N N 100 
CYS   CA     C N R 101 
CYS   C      C N N 102 
CYS   O      O N N 103 
CYS   CB     C N N 104 
CYS   SG     S N N 105 
CYS   OXT    O N N 106 
CYS   H      H N N 107 
CYS   H2     H N N 108 
CYS   HA     H N N 109 
CYS   HB2    H N N 110 
CYS   HB3    H N N 111 
CYS   HG     H N N 112 
CYS   HXT    H N N 113 
FMN   N1     N N N 114 
FMN   C2     C N N 115 
FMN   O2     O N N 116 
FMN   N3     N N N 117 
FMN   C4     C N N 118 
FMN   O4     O N N 119 
FMN   C4A    C N N 120 
FMN   N5     N N N 121 
FMN   C5A    C Y N 122 
FMN   C6     C Y N 123 
FMN   C7     C Y N 124 
FMN   C7M    C N N 125 
FMN   C8     C Y N 126 
FMN   C8M    C N N 127 
FMN   C9     C Y N 128 
FMN   C9A    C Y N 129 
FMN   N10    N N N 130 
FMN   C10    C N N 131 
FMN   "C1'"  C N N 132 
FMN   "C2'"  C N S 133 
FMN   "O2'"  O N N 134 
FMN   "C3'"  C N S 135 
FMN   "O3'"  O N N 136 
FMN   "C4'"  C N R 137 
FMN   "O4'"  O N N 138 
FMN   "C5'"  C N N 139 
FMN   "O5'"  O N N 140 
FMN   P      P N N 141 
FMN   O1P    O N N 142 
FMN   O2P    O N N 143 
FMN   O3P    O N N 144 
FMN   HN3    H N N 145 
FMN   H6     H N N 146 
FMN   HM71   H N N 147 
FMN   HM72   H N N 148 
FMN   HM73   H N N 149 
FMN   HM81   H N N 150 
FMN   HM82   H N N 151 
FMN   HM83   H N N 152 
FMN   H9     H N N 153 
FMN   "H1'1" H N N 154 
FMN   "H1'2" H N N 155 
FMN   "H2'"  H N N 156 
FMN   "HO2'" H N N 157 
FMN   "H3'"  H N N 158 
FMN   "HO3'" H N N 159 
FMN   "H4'"  H N N 160 
FMN   "HO4'" H N N 161 
FMN   "H5'1" H N N 162 
FMN   "H5'2" H N N 163 
FMN   HOP2   H N N 164 
FMN   HOP3   H N N 165 
GLN   N      N N N 166 
GLN   CA     C N S 167 
GLN   C      C N N 168 
GLN   O      O N N 169 
GLN   CB     C N N 170 
GLN   CG     C N N 171 
GLN   CD     C N N 172 
GLN   OE1    O N N 173 
GLN   NE2    N N N 174 
GLN   OXT    O N N 175 
GLN   H      H N N 176 
GLN   H2     H N N 177 
GLN   HA     H N N 178 
GLN   HB2    H N N 179 
GLN   HB3    H N N 180 
GLN   HG2    H N N 181 
GLN   HG3    H N N 182 
GLN   HE21   H N N 183 
GLN   HE22   H N N 184 
GLN   HXT    H N N 185 
GLU   N      N N N 186 
GLU   CA     C N S 187 
GLU   C      C N N 188 
GLU   O      O N N 189 
GLU   CB     C N N 190 
GLU   CG     C N N 191 
GLU   CD     C N N 192 
GLU   OE1    O N N 193 
GLU   OE2    O N N 194 
GLU   OXT    O N N 195 
GLU   H      H N N 196 
GLU   H2     H N N 197 
GLU   HA     H N N 198 
GLU   HB2    H N N 199 
GLU   HB3    H N N 200 
GLU   HG2    H N N 201 
GLU   HG3    H N N 202 
GLU   HE2    H N N 203 
GLU   HXT    H N N 204 
GLY   N      N N N 205 
GLY   CA     C N N 206 
GLY   C      C N N 207 
GLY   O      O N N 208 
GLY   OXT    O N N 209 
GLY   H      H N N 210 
GLY   H2     H N N 211 
GLY   HA2    H N N 212 
GLY   HA3    H N N 213 
GLY   HXT    H N N 214 
GOL   C1     C N N 215 
GOL   O1     O N N 216 
GOL   C2     C N N 217 
GOL   O2     O N N 218 
GOL   C3     C N N 219 
GOL   O3     O N N 220 
GOL   H11    H N N 221 
GOL   H12    H N N 222 
GOL   HO1    H N N 223 
GOL   H2     H N N 224 
GOL   HO2    H N N 225 
GOL   H31    H N N 226 
GOL   H32    H N N 227 
GOL   HO3    H N N 228 
HIS   N      N N N 229 
HIS   CA     C N S 230 
HIS   C      C N N 231 
HIS   O      O N N 232 
HIS   CB     C N N 233 
HIS   CG     C Y N 234 
HIS   ND1    N Y N 235 
HIS   CD2    C Y N 236 
HIS   CE1    C Y N 237 
HIS   NE2    N Y N 238 
HIS   OXT    O N N 239 
HIS   H      H N N 240 
HIS   H2     H N N 241 
HIS   HA     H N N 242 
HIS   HB2    H N N 243 
HIS   HB3    H N N 244 
HIS   HD1    H N N 245 
HIS   HD2    H N N 246 
HIS   HE1    H N N 247 
HIS   HE2    H N N 248 
HIS   HXT    H N N 249 
HOH   O      O N N 250 
HOH   H1     H N N 251 
HOH   H2     H N N 252 
ILE   N      N N N 253 
ILE   CA     C N S 254 
ILE   C      C N N 255 
ILE   O      O N N 256 
ILE   CB     C N S 257 
ILE   CG1    C N N 258 
ILE   CG2    C N N 259 
ILE   CD1    C N N 260 
ILE   OXT    O N N 261 
ILE   H      H N N 262 
ILE   H2     H N N 263 
ILE   HA     H N N 264 
ILE   HB     H N N 265 
ILE   HG12   H N N 266 
ILE   HG13   H N N 267 
ILE   HG21   H N N 268 
ILE   HG22   H N N 269 
ILE   HG23   H N N 270 
ILE   HD11   H N N 271 
ILE   HD12   H N N 272 
ILE   HD13   H N N 273 
ILE   HXT    H N N 274 
LEU   N      N N N 275 
LEU   CA     C N S 276 
LEU   C      C N N 277 
LEU   O      O N N 278 
LEU   CB     C N N 279 
LEU   CG     C N N 280 
LEU   CD1    C N N 281 
LEU   CD2    C N N 282 
LEU   OXT    O N N 283 
LEU   H      H N N 284 
LEU   H2     H N N 285 
LEU   HA     H N N 286 
LEU   HB2    H N N 287 
LEU   HB3    H N N 288 
LEU   HG     H N N 289 
LEU   HD11   H N N 290 
LEU   HD12   H N N 291 
LEU   HD13   H N N 292 
LEU   HD21   H N N 293 
LEU   HD22   H N N 294 
LEU   HD23   H N N 295 
LEU   HXT    H N N 296 
LYS   N      N N N 297 
LYS   CA     C N S 298 
LYS   C      C N N 299 
LYS   O      O N N 300 
LYS   CB     C N N 301 
LYS   CG     C N N 302 
LYS   CD     C N N 303 
LYS   CE     C N N 304 
LYS   NZ     N N N 305 
LYS   OXT    O N N 306 
LYS   H      H N N 307 
LYS   H2     H N N 308 
LYS   HA     H N N 309 
LYS   HB2    H N N 310 
LYS   HB3    H N N 311 
LYS   HG2    H N N 312 
LYS   HG3    H N N 313 
LYS   HD2    H N N 314 
LYS   HD3    H N N 315 
LYS   HE2    H N N 316 
LYS   HE3    H N N 317 
LYS   HZ1    H N N 318 
LYS   HZ2    H N N 319 
LYS   HZ3    H N N 320 
LYS   HXT    H N N 321 
MET   N      N N N 322 
MET   CA     C N S 323 
MET   C      C N N 324 
MET   O      O N N 325 
MET   CB     C N N 326 
MET   CG     C N N 327 
MET   SD     S N N 328 
MET   CE     C N N 329 
MET   OXT    O N N 330 
MET   H      H N N 331 
MET   H2     H N N 332 
MET   HA     H N N 333 
MET   HB2    H N N 334 
MET   HB3    H N N 335 
MET   HG2    H N N 336 
MET   HG3    H N N 337 
MET   HE1    H N N 338 
MET   HE2    H N N 339 
MET   HE3    H N N 340 
MET   HXT    H N N 341 
PHE   N      N N N 342 
PHE   CA     C N S 343 
PHE   C      C N N 344 
PHE   O      O N N 345 
PHE   CB     C N N 346 
PHE   CG     C Y N 347 
PHE   CD1    C Y N 348 
PHE   CD2    C Y N 349 
PHE   CE1    C Y N 350 
PHE   CE2    C Y N 351 
PHE   CZ     C Y N 352 
PHE   OXT    O N N 353 
PHE   H      H N N 354 
PHE   H2     H N N 355 
PHE   HA     H N N 356 
PHE   HB2    H N N 357 
PHE   HB3    H N N 358 
PHE   HD1    H N N 359 
PHE   HD2    H N N 360 
PHE   HE1    H N N 361 
PHE   HE2    H N N 362 
PHE   HZ     H N N 363 
PHE   HXT    H N N 364 
PRO   N      N N N 365 
PRO   CA     C N S 366 
PRO   C      C N N 367 
PRO   O      O N N 368 
PRO   CB     C N N 369 
PRO   CG     C N N 370 
PRO   CD     C N N 371 
PRO   OXT    O N N 372 
PRO   H      H N N 373 
PRO   HA     H N N 374 
PRO   HB2    H N N 375 
PRO   HB3    H N N 376 
PRO   HG2    H N N 377 
PRO   HG3    H N N 378 
PRO   HD2    H N N 379 
PRO   HD3    H N N 380 
PRO   HXT    H N N 381 
SER   N      N N N 382 
SER   CA     C N S 383 
SER   C      C N N 384 
SER   O      O N N 385 
SER   CB     C N N 386 
SER   OG     O N N 387 
SER   OXT    O N N 388 
SER   H      H N N 389 
SER   H2     H N N 390 
SER   HA     H N N 391 
SER   HB2    H N N 392 
SER   HB3    H N N 393 
SER   HG     H N N 394 
SER   HXT    H N N 395 
THR   N      N N N 396 
THR   CA     C N S 397 
THR   C      C N N 398 
THR   O      O N N 399 
THR   CB     C N R 400 
THR   OG1    O N N 401 
THR   CG2    C N N 402 
THR   OXT    O N N 403 
THR   H      H N N 404 
THR   H2     H N N 405 
THR   HA     H N N 406 
THR   HB     H N N 407 
THR   HG1    H N N 408 
THR   HG21   H N N 409 
THR   HG22   H N N 410 
THR   HG23   H N N 411 
THR   HXT    H N N 412 
TYR   N      N N N 413 
TYR   CA     C N S 414 
TYR   C      C N N 415 
TYR   O      O N N 416 
TYR   CB     C N N 417 
TYR   CG     C Y N 418 
TYR   CD1    C Y N 419 
TYR   CD2    C Y N 420 
TYR   CE1    C Y N 421 
TYR   CE2    C Y N 422 
TYR   CZ     C Y N 423 
TYR   OH     O N N 424 
TYR   OXT    O N N 425 
TYR   H      H N N 426 
TYR   H2     H N N 427 
TYR   HA     H N N 428 
TYR   HB2    H N N 429 
TYR   HB3    H N N 430 
TYR   HD1    H N N 431 
TYR   HD2    H N N 432 
TYR   HE1    H N N 433 
TYR   HE2    H N N 434 
TYR   HH     H N N 435 
TYR   HXT    H N N 436 
VAL   N      N N N 437 
VAL   CA     C N S 438 
VAL   C      C N N 439 
VAL   O      O N N 440 
VAL   CB     C N N 441 
VAL   CG1    C N N 442 
VAL   CG2    C N N 443 
VAL   OXT    O N N 444 
VAL   H      H N N 445 
VAL   H2     H N N 446 
VAL   HA     H N N 447 
VAL   HB     H N N 448 
VAL   HG11   H N N 449 
VAL   HG12   H N N 450 
VAL   HG13   H N N 451 
VAL   HG21   H N N 452 
VAL   HG22   H N N 453 
VAL   HG23   H N N 454 
VAL   HXT    H N N 455 
# 
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 
A1AVS O01   C02    doub N N 1   
A1AVS C02   N03    sing N N 2   
A1AVS C02   N21    sing N N 3   
A1AVS N03   C04    sing N N 4   
A1AVS N21   C22    sing N N 5   
A1AVS C04   O20    doub N N 6   
A1AVS C04   C05    sing N N 7   
A1AVS C22   O23    doub N N 8   
A1AVS C22   C05    sing N N 9   
A1AVS C05   C06    sing N N 10  
A1AVS C06   C14    sing N N 11  
A1AVS C14   C15    doub Y N 12  
A1AVS C14   C19    sing Y N 13  
A1AVS C15   C16    sing Y N 14  
A1AVS C19   C18    doub Y N 15  
A1AVS C16   C17    doub Y N 16  
A1AVS C18   C17    sing Y N 17  
A1AVS C05   H051   sing N N 18  
A1AVS C06   H1     sing N N 19  
A1AVS C06   H061   sing N N 20  
A1AVS C15   H151   sing N N 21  
A1AVS C16   H161   sing N N 22  
A1AVS C17   H171   sing N N 23  
A1AVS C18   H181   sing N N 24  
A1AVS C19   H191   sing N N 25  
A1AVS N03   H031   sing N N 26  
A1AVS N21   H211   sing N N 27  
ALA   N     CA     sing N N 28  
ALA   N     H      sing N N 29  
ALA   N     H2     sing N N 30  
ALA   CA    C      sing N N 31  
ALA   CA    CB     sing N N 32  
ALA   CA    HA     sing N N 33  
ALA   C     O      doub N N 34  
ALA   C     OXT    sing N N 35  
ALA   CB    HB1    sing N N 36  
ALA   CB    HB2    sing N N 37  
ALA   CB    HB3    sing N N 38  
ALA   OXT   HXT    sing N N 39  
ARG   N     CA     sing N N 40  
ARG   N     H      sing N N 41  
ARG   N     H2     sing N N 42  
ARG   CA    C      sing N N 43  
ARG   CA    CB     sing N N 44  
ARG   CA    HA     sing N N 45  
ARG   C     O      doub N N 46  
ARG   C     OXT    sing N N 47  
ARG   CB    CG     sing N N 48  
ARG   CB    HB2    sing N N 49  
ARG   CB    HB3    sing N N 50  
ARG   CG    CD     sing N N 51  
ARG   CG    HG2    sing N N 52  
ARG   CG    HG3    sing N N 53  
ARG   CD    NE     sing N N 54  
ARG   CD    HD2    sing N N 55  
ARG   CD    HD3    sing N N 56  
ARG   NE    CZ     sing N N 57  
ARG   NE    HE     sing N N 58  
ARG   CZ    NH1    sing N N 59  
ARG   CZ    NH2    doub N N 60  
ARG   NH1   HH11   sing N N 61  
ARG   NH1   HH12   sing N N 62  
ARG   NH2   HH21   sing N N 63  
ARG   NH2   HH22   sing N N 64  
ARG   OXT   HXT    sing N N 65  
ASN   N     CA     sing N N 66  
ASN   N     H      sing N N 67  
ASN   N     H2     sing N N 68  
ASN   CA    C      sing N N 69  
ASN   CA    CB     sing N N 70  
ASN   CA    HA     sing N N 71  
ASN   C     O      doub N N 72  
ASN   C     OXT    sing N N 73  
ASN   CB    CG     sing N N 74  
ASN   CB    HB2    sing N N 75  
ASN   CB    HB3    sing N N 76  
ASN   CG    OD1    doub N N 77  
ASN   CG    ND2    sing N N 78  
ASN   ND2   HD21   sing N N 79  
ASN   ND2   HD22   sing N N 80  
ASN   OXT   HXT    sing N N 81  
ASP   N     CA     sing N N 82  
ASP   N     H      sing N N 83  
ASP   N     H2     sing N N 84  
ASP   CA    C      sing N N 85  
ASP   CA    CB     sing N N 86  
ASP   CA    HA     sing N N 87  
ASP   C     O      doub N N 88  
ASP   C     OXT    sing N N 89  
ASP   CB    CG     sing N N 90  
ASP   CB    HB2    sing N N 91  
ASP   CB    HB3    sing N N 92  
ASP   CG    OD1    doub N N 93  
ASP   CG    OD2    sing N N 94  
ASP   OD2   HD2    sing N N 95  
ASP   OXT   HXT    sing N N 96  
CYS   N     CA     sing N N 97  
CYS   N     H      sing N N 98  
CYS   N     H2     sing N N 99  
CYS   CA    C      sing N N 100 
CYS   CA    CB     sing N N 101 
CYS   CA    HA     sing N N 102 
CYS   C     O      doub N N 103 
CYS   C     OXT    sing N N 104 
CYS   CB    SG     sing N N 105 
CYS   CB    HB2    sing N N 106 
CYS   CB    HB3    sing N N 107 
CYS   SG    HG     sing N N 108 
CYS   OXT   HXT    sing N N 109 
FMN   N1    C2     sing N N 110 
FMN   N1    C10    doub N N 111 
FMN   C2    O2     doub N N 112 
FMN   C2    N3     sing N N 113 
FMN   N3    C4     sing N N 114 
FMN   N3    HN3    sing N N 115 
FMN   C4    O4     doub N N 116 
FMN   C4    C4A    sing N N 117 
FMN   C4A   N5     doub N N 118 
FMN   C4A   C10    sing N N 119 
FMN   N5    C5A    sing N N 120 
FMN   C5A   C6     doub Y N 121 
FMN   C5A   C9A    sing Y N 122 
FMN   C6    C7     sing Y N 123 
FMN   C6    H6     sing N N 124 
FMN   C7    C7M    sing N N 125 
FMN   C7    C8     doub Y N 126 
FMN   C7M   HM71   sing N N 127 
FMN   C7M   HM72   sing N N 128 
FMN   C7M   HM73   sing N N 129 
FMN   C8    C8M    sing N N 130 
FMN   C8    C9     sing Y N 131 
FMN   C8M   HM81   sing N N 132 
FMN   C8M   HM82   sing N N 133 
FMN   C8M   HM83   sing N N 134 
FMN   C9    C9A    doub Y N 135 
FMN   C9    H9     sing N N 136 
FMN   C9A   N10    sing N N 137 
FMN   N10   C10    sing N N 138 
FMN   N10   "C1'"  sing N N 139 
FMN   "C1'" "C2'"  sing N N 140 
FMN   "C1'" "H1'1" sing N N 141 
FMN   "C1'" "H1'2" sing N N 142 
FMN   "C2'" "O2'"  sing N N 143 
FMN   "C2'" "C3'"  sing N N 144 
FMN   "C2'" "H2'"  sing N N 145 
FMN   "O2'" "HO2'" sing N N 146 
FMN   "C3'" "O3'"  sing N N 147 
FMN   "C3'" "C4'"  sing N N 148 
FMN   "C3'" "H3'"  sing N N 149 
FMN   "O3'" "HO3'" sing N N 150 
FMN   "C4'" "O4'"  sing N N 151 
FMN   "C4'" "C5'"  sing N N 152 
FMN   "C4'" "H4'"  sing N N 153 
FMN   "O4'" "HO4'" sing N N 154 
FMN   "C5'" "O5'"  sing N N 155 
FMN   "C5'" "H5'1" sing N N 156 
FMN   "C5'" "H5'2" sing N N 157 
FMN   "O5'" P      sing N N 158 
FMN   P     O1P    doub N N 159 
FMN   P     O2P    sing N N 160 
FMN   P     O3P    sing N N 161 
FMN   O2P   HOP2   sing N N 162 
FMN   O3P   HOP3   sing N N 163 
GLN   N     CA     sing N N 164 
GLN   N     H      sing N N 165 
GLN   N     H2     sing N N 166 
GLN   CA    C      sing N N 167 
GLN   CA    CB     sing N N 168 
GLN   CA    HA     sing N N 169 
GLN   C     O      doub N N 170 
GLN   C     OXT    sing N N 171 
GLN   CB    CG     sing N N 172 
GLN   CB    HB2    sing N N 173 
GLN   CB    HB3    sing N N 174 
GLN   CG    CD     sing N N 175 
GLN   CG    HG2    sing N N 176 
GLN   CG    HG3    sing N N 177 
GLN   CD    OE1    doub N N 178 
GLN   CD    NE2    sing N N 179 
GLN   NE2   HE21   sing N N 180 
GLN   NE2   HE22   sing N N 181 
GLN   OXT   HXT    sing N N 182 
GLU   N     CA     sing N N 183 
GLU   N     H      sing N N 184 
GLU   N     H2     sing N N 185 
GLU   CA    C      sing N N 186 
GLU   CA    CB     sing N N 187 
GLU   CA    HA     sing N N 188 
GLU   C     O      doub N N 189 
GLU   C     OXT    sing N N 190 
GLU   CB    CG     sing N N 191 
GLU   CB    HB2    sing N N 192 
GLU   CB    HB3    sing N N 193 
GLU   CG    CD     sing N N 194 
GLU   CG    HG2    sing N N 195 
GLU   CG    HG3    sing N N 196 
GLU   CD    OE1    doub N N 197 
GLU   CD    OE2    sing N N 198 
GLU   OE2   HE2    sing N N 199 
GLU   OXT   HXT    sing N N 200 
GLY   N     CA     sing N N 201 
GLY   N     H      sing N N 202 
GLY   N     H2     sing N N 203 
GLY   CA    C      sing N N 204 
GLY   CA    HA2    sing N N 205 
GLY   CA    HA3    sing N N 206 
GLY   C     O      doub N N 207 
GLY   C     OXT    sing N N 208 
GLY   OXT   HXT    sing N N 209 
GOL   C1    O1     sing N N 210 
GOL   C1    C2     sing N N 211 
GOL   C1    H11    sing N N 212 
GOL   C1    H12    sing N N 213 
GOL   O1    HO1    sing N N 214 
GOL   C2    O2     sing N N 215 
GOL   C2    C3     sing N N 216 
GOL   C2    H2     sing N N 217 
GOL   O2    HO2    sing N N 218 
GOL   C3    O3     sing N N 219 
GOL   C3    H31    sing N N 220 
GOL   C3    H32    sing N N 221 
GOL   O3    HO3    sing N N 222 
HIS   N     CA     sing N N 223 
HIS   N     H      sing N N 224 
HIS   N     H2     sing N N 225 
HIS   CA    C      sing N N 226 
HIS   CA    CB     sing N N 227 
HIS   CA    HA     sing N N 228 
HIS   C     O      doub N N 229 
HIS   C     OXT    sing N N 230 
HIS   CB    CG     sing N N 231 
HIS   CB    HB2    sing N N 232 
HIS   CB    HB3    sing N N 233 
HIS   CG    ND1    sing Y N 234 
HIS   CG    CD2    doub Y N 235 
HIS   ND1   CE1    doub Y N 236 
HIS   ND1   HD1    sing N N 237 
HIS   CD2   NE2    sing Y N 238 
HIS   CD2   HD2    sing N N 239 
HIS   CE1   NE2    sing Y N 240 
HIS   CE1   HE1    sing N N 241 
HIS   NE2   HE2    sing N N 242 
HIS   OXT   HXT    sing N N 243 
HOH   O     H1     sing N N 244 
HOH   O     H2     sing N N 245 
ILE   N     CA     sing N N 246 
ILE   N     H      sing N N 247 
ILE   N     H2     sing N N 248 
ILE   CA    C      sing N N 249 
ILE   CA    CB     sing N N 250 
ILE   CA    HA     sing N N 251 
ILE   C     O      doub N N 252 
ILE   C     OXT    sing N N 253 
ILE   CB    CG1    sing N N 254 
ILE   CB    CG2    sing N N 255 
ILE   CB    HB     sing N N 256 
ILE   CG1   CD1    sing N N 257 
ILE   CG1   HG12   sing N N 258 
ILE   CG1   HG13   sing N N 259 
ILE   CG2   HG21   sing N N 260 
ILE   CG2   HG22   sing N N 261 
ILE   CG2   HG23   sing N N 262 
ILE   CD1   HD11   sing N N 263 
ILE   CD1   HD12   sing N N 264 
ILE   CD1   HD13   sing N N 265 
ILE   OXT   HXT    sing N N 266 
LEU   N     CA     sing N N 267 
LEU   N     H      sing N N 268 
LEU   N     H2     sing N N 269 
LEU   CA    C      sing N N 270 
LEU   CA    CB     sing N N 271 
LEU   CA    HA     sing N N 272 
LEU   C     O      doub N N 273 
LEU   C     OXT    sing N N 274 
LEU   CB    CG     sing N N 275 
LEU   CB    HB2    sing N N 276 
LEU   CB    HB3    sing N N 277 
LEU   CG    CD1    sing N N 278 
LEU   CG    CD2    sing N N 279 
LEU   CG    HG     sing N N 280 
LEU   CD1   HD11   sing N N 281 
LEU   CD1   HD12   sing N N 282 
LEU   CD1   HD13   sing N N 283 
LEU   CD2   HD21   sing N N 284 
LEU   CD2   HD22   sing N N 285 
LEU   CD2   HD23   sing N N 286 
LEU   OXT   HXT    sing N N 287 
LYS   N     CA     sing N N 288 
LYS   N     H      sing N N 289 
LYS   N     H2     sing N N 290 
LYS   CA    C      sing N N 291 
LYS   CA    CB     sing N N 292 
LYS   CA    HA     sing N N 293 
LYS   C     O      doub N N 294 
LYS   C     OXT    sing N N 295 
LYS   CB    CG     sing N N 296 
LYS   CB    HB2    sing N N 297 
LYS   CB    HB3    sing N N 298 
LYS   CG    CD     sing N N 299 
LYS   CG    HG2    sing N N 300 
LYS   CG    HG3    sing N N 301 
LYS   CD    CE     sing N N 302 
LYS   CD    HD2    sing N N 303 
LYS   CD    HD3    sing N N 304 
LYS   CE    NZ     sing N N 305 
LYS   CE    HE2    sing N N 306 
LYS   CE    HE3    sing N N 307 
LYS   NZ    HZ1    sing N N 308 
LYS   NZ    HZ2    sing N N 309 
LYS   NZ    HZ3    sing N N 310 
LYS   OXT   HXT    sing N N 311 
MET   N     CA     sing N N 312 
MET   N     H      sing N N 313 
MET   N     H2     sing N N 314 
MET   CA    C      sing N N 315 
MET   CA    CB     sing N N 316 
MET   CA    HA     sing N N 317 
MET   C     O      doub N N 318 
MET   C     OXT    sing N N 319 
MET   CB    CG     sing N N 320 
MET   CB    HB2    sing N N 321 
MET   CB    HB3    sing N N 322 
MET   CG    SD     sing N N 323 
MET   CG    HG2    sing N N 324 
MET   CG    HG3    sing N N 325 
MET   SD    CE     sing N N 326 
MET   CE    HE1    sing N N 327 
MET   CE    HE2    sing N N 328 
MET   CE    HE3    sing N N 329 
MET   OXT   HXT    sing N N 330 
PHE   N     CA     sing N N 331 
PHE   N     H      sing N N 332 
PHE   N     H2     sing N N 333 
PHE   CA    C      sing N N 334 
PHE   CA    CB     sing N N 335 
PHE   CA    HA     sing N N 336 
PHE   C     O      doub N N 337 
PHE   C     OXT    sing N N 338 
PHE   CB    CG     sing N N 339 
PHE   CB    HB2    sing N N 340 
PHE   CB    HB3    sing N N 341 
PHE   CG    CD1    doub Y N 342 
PHE   CG    CD2    sing Y N 343 
PHE   CD1   CE1    sing Y N 344 
PHE   CD1   HD1    sing N N 345 
PHE   CD2   CE2    doub Y N 346 
PHE   CD2   HD2    sing N N 347 
PHE   CE1   CZ     doub Y N 348 
PHE   CE1   HE1    sing N N 349 
PHE   CE2   CZ     sing Y N 350 
PHE   CE2   HE2    sing N N 351 
PHE   CZ    HZ     sing N N 352 
PHE   OXT   HXT    sing N N 353 
PRO   N     CA     sing N N 354 
PRO   N     CD     sing N N 355 
PRO   N     H      sing N N 356 
PRO   CA    C      sing N N 357 
PRO   CA    CB     sing N N 358 
PRO   CA    HA     sing N N 359 
PRO   C     O      doub N N 360 
PRO   C     OXT    sing N N 361 
PRO   CB    CG     sing N N 362 
PRO   CB    HB2    sing N N 363 
PRO   CB    HB3    sing N N 364 
PRO   CG    CD     sing N N 365 
PRO   CG    HG2    sing N N 366 
PRO   CG    HG3    sing N N 367 
PRO   CD    HD2    sing N N 368 
PRO   CD    HD3    sing N N 369 
PRO   OXT   HXT    sing N N 370 
SER   N     CA     sing N N 371 
SER   N     H      sing N N 372 
SER   N     H2     sing N N 373 
SER   CA    C      sing N N 374 
SER   CA    CB     sing N N 375 
SER   CA    HA     sing N N 376 
SER   C     O      doub N N 377 
SER   C     OXT    sing N N 378 
SER   CB    OG     sing N N 379 
SER   CB    HB2    sing N N 380 
SER   CB    HB3    sing N N 381 
SER   OG    HG     sing N N 382 
SER   OXT   HXT    sing N N 383 
THR   N     CA     sing N N 384 
THR   N     H      sing N N 385 
THR   N     H2     sing N N 386 
THR   CA    C      sing N N 387 
THR   CA    CB     sing N N 388 
THR   CA    HA     sing N N 389 
THR   C     O      doub N N 390 
THR   C     OXT    sing N N 391 
THR   CB    OG1    sing N N 392 
THR   CB    CG2    sing N N 393 
THR   CB    HB     sing N N 394 
THR   OG1   HG1    sing N N 395 
THR   CG2   HG21   sing N N 396 
THR   CG2   HG22   sing N N 397 
THR   CG2   HG23   sing N N 398 
THR   OXT   HXT    sing N N 399 
TYR   N     CA     sing N N 400 
TYR   N     H      sing N N 401 
TYR   N     H2     sing N N 402 
TYR   CA    C      sing N N 403 
TYR   CA    CB     sing N N 404 
TYR   CA    HA     sing N N 405 
TYR   C     O      doub N N 406 
TYR   C     OXT    sing N N 407 
TYR   CB    CG     sing N N 408 
TYR   CB    HB2    sing N N 409 
TYR   CB    HB3    sing N N 410 
TYR   CG    CD1    doub Y N 411 
TYR   CG    CD2    sing Y N 412 
TYR   CD1   CE1    sing Y N 413 
TYR   CD1   HD1    sing N N 414 
TYR   CD2   CE2    doub Y N 415 
TYR   CD2   HD2    sing N N 416 
TYR   CE1   CZ     doub Y N 417 
TYR   CE1   HE1    sing N N 418 
TYR   CE2   CZ     sing Y N 419 
TYR   CE2   HE2    sing N N 420 
TYR   CZ    OH     sing N N 421 
TYR   OH    HH     sing N N 422 
TYR   OXT   HXT    sing N N 423 
VAL   N     CA     sing N N 424 
VAL   N     H      sing N N 425 
VAL   N     H2     sing N N 426 
VAL   CA    C      sing N N 427 
VAL   CA    CB     sing N N 428 
VAL   CA    HA     sing N N 429 
VAL   C     O      doub N N 430 
VAL   C     OXT    sing N N 431 
VAL   CB    CG1    sing N N 432 
VAL   CB    CG2    sing N N 433 
VAL   CB    HB     sing N N 434 
VAL   CG1   HG11   sing N N 435 
VAL   CG1   HG12   sing N N 436 
VAL   CG1   HG13   sing N N 437 
VAL   CG2   HG21   sing N N 438 
VAL   CG2   HG22   sing N N 439 
VAL   CG2   HG23   sing N N 440 
VAL   OXT   HXT    sing N N 441 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Sao Paulo Research Foundation (FAPESP)'                            Brazil          '2019/ 25532-1' 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' 1R01AI160379-01 2 
# 
_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   4wzh 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CB8 
_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]   0.016250 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009544 
_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]   0.009360 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . SER   A 1 34  ? -23.92800 -13.04900 -37.40600 1.000 71.73000  ? 0   SER   A N      1 
ATOM   2    C CA     . SER   A 1 34  ? -22.83100 -13.72700 -36.72100 1.000 74.23000  ? 0   SER   A CA     1 
ATOM   3    C C      . SER   A 1 34  ? -21.80500 -12.72200 -36.18700 1.000 67.46000  ? 0   SER   A C      1 
ATOM   4    O O      . SER   A 1 34  ? -20.69000 -13.09800 -35.82400 1.000 78.40000  ? 0   SER   A O      1 
ATOM   5    C CB     . SER   A 1 34  ? -22.15100 -14.73000 -37.66100 1.000 74.55000  ? 0   SER   A CB     1 
ATOM   6    O OG     . SER   A 1 34  ? -21.65400 -14.08900 -38.82800 1.000 76.17000  ? 0   SER   A OG     1 
ATOM   7    H H      . SER   A 1 34  ? -24.44800 -13.65200 -37.80200 1.000 71.73000  ? 0   SER   A H      1 
ATOM   8    H HA     . SER   A 1 34  ? -23.18800 -14.22000 -35.96600 1.000 74.23000  ? 0   SER   A HA     1 
ATOM   9    H HB2    . SER   A 1 34  ? -21.41100 -15.14800 -37.19300 1.000 74.55000  ? 0   SER   A HB2    1 
ATOM   10   H HB3    . SER   A 1 34  ? -22.79800 -15.40300 -37.92400 1.000 74.55000  ? 0   SER   A HB3    1 
ATOM   11   H HG     . SER   A 1 34  ? -21.28600 -14.65200 -39.33000 1.000 76.17000  ? 0   SER   A HG     1 
ATOM   12   N N      . MET   A 1 35  ? -22.18300 -11.44700 -36.13900 1.000 62.28000  ? 1   MET   A N      1 
ATOM   13   C CA     . MET   A 1 35  ? -21.29100 -10.39200 -35.68000 1.000 56.85000  ? 1   MET   A CA     1 
ATOM   14   C C      . MET   A 1 35  ? -21.84700 -9.72700  -34.42900 1.000 59.50000  ? 1   MET   A C      1 
ATOM   15   O O      . MET   A 1 35  ? -23.04500 -9.79100  -34.13200 1.000 51.42000  ? 1   MET   A O      1 
ATOM   16   C CB     . MET   A 1 35  ? -21.07000 -9.32300  -36.75100 1.000 54.05000  ? 1   MET   A CB     1 
ATOM   17   C CG     . MET   A 1 35  ? -20.70800 -9.84800  -38.12600 1.000 59.63000  ? 1   MET   A CG     1 
ATOM   18   S SD     . MET   A 1 35  ? -20.92600 -8.51000  -39.31500 1.000 68.41000  ? 1   MET   A SD     1 
ATOM   19   C CE     . MET   A 1 35  ? -22.54500 -7.92000  -38.84100 1.000 48.59000  ? 1   MET   A CE     1 
ATOM   20   H H      . MET   A 1 35  ? -22.96200 -11.16400 -36.36900 1.000 62.28000  ? 1   MET   A H      1 
ATOM   21   H HA     . MET   A 1 35  ? -20.42700 -10.77800 -35.46800 1.000 56.85000  ? 1   MET   A HA     1 
ATOM   22   H HB2    . MET   A 1 35  ? -21.88500 -8.81600  -36.77500 1.000 54.05000  ? 1   MET   A HB2    1 
ATOM   23   H HB3    . MET   A 1 35  ? -20.34300 -8.74900  -36.46200 1.000 54.05000  ? 1   MET   A HB3    1 
ATOM   24   H HG2    . MET   A 1 35  ? -19.78000 -10.13100 -38.13800 1.000 59.63000  ? 1   MET   A HG2    1 
ATOM   25   H HG3    . MET   A 1 35  ? -21.29600 -10.58000 -38.36900 1.000 59.63000  ? 1   MET   A HG3    1 
ATOM   26   H HE1    . MET   A 1 35  ? -22.95500 -7.49100  -39.60800 1.000 48.59000  ? 1   MET   A HE1    1 
ATOM   27   H HE2    . MET   A 1 35  ? -23.09000 -8.67100  -38.55900 1.000 48.59000  ? 1   MET   A HE2    1 
ATOM   28   H HE3    . MET   A 1 35  ? -22.45400 -7.27900  -38.12000 1.000 48.59000  ? 1   MET   A HE3    1 
ATOM   29   N N      . SER   A 1 36  ? -20.95700 -9.05500  -33.70900 1.000 46.02000  ? 2   SER   A N      1 
ATOM   30   C CA     . SER   A 1 36  ? -21.31600 -8.48300  -32.42700 1.000 42.25000  ? 2   SER   A CA     1 
ATOM   31   C C      . SER   A 1 36  ? -20.44100 -7.27000  -32.16100 1.000 40.17000  ? 2   SER   A C      1 
ATOM   32   O O      . SER   A 1 36  ? -19.25100 -7.27100  -32.49800 1.000 39.22000  ? 2   SER   A O      1 
ATOM   33   C CB     . SER   A 1 36  ? -21.14000 -9.50600  -31.30000 1.000 42.65000  ? 2   SER   A CB     1 
ATOM   34   O OG     . SER   A 1 36  ? -21.44600 -8.92600  -30.05500 1.000 44.90000  ? 2   SER   A OG     1 
ATOM   35   H H      . SER   A 1 36  ? -20.14100 -8.91800  -33.94300 1.000 46.02000  ? 2   SER   A H      1 
ATOM   36   H HA     . SER   A 1 36  ? -22.24300 -8.19800  -32.44400 1.000 42.25000  ? 2   SER   A HA     1 
ATOM   37   H HB2    . SER   A 1 36  ? -21.73700 -10.25500 -31.45600 1.000 42.65000  ? 2   SER   A HB2    1 
ATOM   38   H HB3    . SER   A 1 36  ? -20.21900 -9.81100  -31.29000 1.000 42.65000  ? 2   SER   A HB3    1 
ATOM   39   H HG     . SER   A 1 36  ? -21.34800 -9.49200  -29.44200 1.000 44.90000  ? 2   SER   A HG     1 
ATOM   40   N N      . LEU   A 1 37  ? -21.04300 -6.25100  -31.55600 1.000 37.59000  ? 3   LEU   A N      1 
ATOM   41   C CA     . LEU   A 1 37  ? -20.34200 -5.07800  -31.06200 1.000 37.76000  ? 3   LEU   A CA     1 
ATOM   42   C C      . LEU   A 1 37  ? -20.08000 -5.18200  -29.57800 1.000 36.89000  ? 3   LEU   A C      1 
ATOM   43   O O      . LEU   A 1 37  ? -19.64100 -4.21500  -28.96200 1.000 32.10000  ? 3   LEU   A O      1 
ATOM   44   C CB     . LEU   A 1 37  ? -21.14600 -3.81300  -31.36100 1.000 34.73000  ? 3   LEU   A CB     1 
ATOM   45   C CG     . LEU   A 1 37  ? -21.26300 -3.50700  -32.85500 1.000 38.82000  ? 3   LEU   A CG     1 
ATOM   46   C CD1    . LEU   A 1 37  ? -21.88400 -2.12300  -33.05800 1.000 36.90000  ? 3   LEU   A CD1    1 
ATOM   47   C CD2    . LEU   A 1 37  ? -19.91000 -3.60300  -33.53100 1.000 41.99000  ? 3   LEU   A CD2    1 
ATOM   48   H H      . LEU   A 1 37  ? -21.89100 -6.21900  -31.41700 1.000 37.59000  ? 3   LEU   A H      1 
ATOM   49   H HA     . LEU   A 1 37  ? -19.47800 -5.01800  -31.49600 1.000 37.76000  ? 3   LEU   A HA     1 
ATOM   50   H HB2    . LEU   A 1 37  ? -22.04300 -3.92000  -31.00800 1.000 34.73000  ? 3   LEU   A HB2    1 
ATOM   51   H HB3    . LEU   A 1 37  ? -20.71200 -3.05700  -30.93500 1.000 34.73000  ? 3   LEU   A HB3    1 
ATOM   52   H HG     . LEU   A 1 37  ? -21.85000 -4.16100  -33.26600 1.000 38.82000  ? 3   LEU   A HG     1 
ATOM   53   H HD11   . LEU   A 1 37  ? -21.94200 -1.93900  -34.00900 1.000 36.90000  ? 3   LEU   A HD11   1 
ATOM   54   H HD12   . LEU   A 1 37  ? -22.77000 -2.11400  -32.66400 1.000 36.90000  ? 3   LEU   A HD12   1 
ATOM   55   H HD13   . LEU   A 1 37  ? -21.32300 -1.46000  -32.62600 1.000 36.90000  ? 3   LEU   A HD13   1 
ATOM   56   H HD21   . LEU   A 1 37  ? -19.94500 -3.12700  -34.37500 1.000 41.99000  ? 3   LEU   A HD21   1 
ATOM   57   H HD22   . LEU   A 1 37  ? -19.24000 -3.20300  -32.95400 1.000 41.99000  ? 3   LEU   A HD22   1 
ATOM   58   H HD23   . LEU   A 1 37  ? -19.69800 -4.53700  -33.68700 1.000 41.99000  ? 3   LEU   A HD23   1 
ATOM   59   N N      . GLN   A 1 38  ? -20.35800 -6.33800  -28.98300 1.000 35.70000  ? 4   GLN   A N      1 
ATOM   60   C CA     . GLN   A 1 38  ? -20.24000 -6.45100  -27.54200 1.000 36.62000  ? 4   GLN   A CA     1 
ATOM   61   C C      . GLN   A 1 38  ? -18.81300 -6.18100  -27.10600 1.000 30.26000  ? 4   GLN   A C      1 
ATOM   62   O O      . GLN   A 1 38  ? -17.84900 -6.48400  -27.81600 1.000 34.39000  ? 4   GLN   A O      1 
ATOM   63   C CB     . GLN   A 1 38  ? -20.66000 -7.84500  -27.07700 1.000 33.53000  ? 4   GLN   A CB     1 
ATOM   64   C CG     . GLN   A 1 38  ? -22.16200 -7.99700  -27.00000 1.000 39.35000  ? 4   GLN   A CG     1 
ATOM   65   C CD     . GLN   A 1 38  ? -22.54600 -9.40800  -26.62900 1.000 44.17000  ? 4   GLN   A CD     1 
ATOM   66   O OE1    . GLN   A 1 38  ? -21.81300 -10.35700 -26.91600 1.000 47.32000  ? 4   GLN   A OE1    1 
ATOM   67   N NE2    . GLN   A 1 38  ? -23.68900 -9.55300  -25.97500 1.000 46.85000  ? 4   GLN   A NE2    1 
ATOM   68   H H      . GLN   A 1 38  ? -20.61000 -7.05700  -29.38200 1.000 35.70000  ? 4   GLN   A H      1 
ATOM   69   H HA     . GLN   A 1 38  ? -20.82000 -5.79800  -27.12000 1.000 36.62000  ? 4   GLN   A HA     1 
ATOM   70   H HB2    . GLN   A 1 38  ? -20.32200 -8.50300  -27.70400 1.000 33.53000  ? 4   GLN   A HB2    1 
ATOM   71   H HB3    . GLN   A 1 38  ? -20.29500 -8.00900  -26.19300 1.000 33.53000  ? 4   GLN   A HB3    1 
ATOM   72   H HG2    . GLN   A 1 38  ? -22.51200 -7.39700  -26.32300 1.000 39.35000  ? 4   GLN   A HG2    1 
ATOM   73   H HG3    . GLN   A 1 38  ? -22.55100 -7.79200  -27.86500 1.000 39.35000  ? 4   GLN   A HG3    1 
ATOM   74   H HE21   . GLN   A 1 38  ? -24.17000 -8.86400  -25.79200 1.000 46.85000  ? 4   GLN   A HE21   1 
ATOM   75   H HE22   . GLN   A 1 38  ? -23.95300 -10.33700 -25.73900 1.000 46.85000  ? 4   GLN   A HE22   1 
ATOM   76   N N      . VAL   A 1 39  ? -18.68700 -5.61300  -25.91500 1.000 32.51000  ? 5   VAL   A N      1 
ATOM   77   C CA     . VAL   A 1 39  ? -17.39200 -5.39400  -25.30300 1.000 37.46000  ? 5   VAL   A CA     1 
ATOM   78   C C      . VAL   A 1 39  ? -17.47200 -5.89300  -23.87000 1.000 35.46000  ? 5   VAL   A C      1 
ATOM   79   O O      . VAL   A 1 39  ? -18.32600 -5.44100  -23.09600 1.000 36.97000  ? 5   VAL   A O      1 
ATOM   80   C CB     . VAL   A 1 39  ? -17.00300 -3.91100  -25.34500 1.000 38.68000  ? 5   VAL   A CB     1 
ATOM   81   C CG1    . VAL   A 1 39  ? -15.60900 -3.71900  -24.78000 1.000 48.27000  ? 5   VAL   A CG1    1 
ATOM   82   C CG2    . VAL   A 1 39  ? -17.10200 -3.41400  -26.79500 1.000 40.78000  ? 5   VAL   A CG2    1 
ATOM   83   H H      . VAL   A 1 39  ? -19.34800 -5.34300  -25.43600 1.000 32.51000  ? 5   VAL   A H      1 
ATOM   84   H HA     . VAL   A 1 39  ? -16.71500 -5.90600  -25.77100 1.000 37.46000  ? 5   VAL   A HA     1 
ATOM   85   H HB     . VAL   A 1 39  ? -17.62500 -3.40000  -24.80400 1.000 38.68000  ? 5   VAL   A HB     1 
ATOM   86   H HG11   . VAL   A 1 39  ? -15.29400 -2.83200  -25.01400 1.000 48.27000  ? 5   VAL   A HG11   1 
ATOM   87   H HG12   . VAL   A 1 39  ? -15.64500 -3.81300  -23.81600 1.000 48.27000  ? 5   VAL   A HG12   1 
ATOM   88   H HG13   . VAL   A 1 39  ? -15.01900 -4.38900  -25.15900 1.000 48.27000  ? 5   VAL   A HG13   1 
ATOM   89   H HG21   . VAL   A 1 39  ? -16.74000 -2.51600  -26.84600 1.000 40.78000  ? 5   VAL   A HG21   1 
ATOM   90   H HG22   . VAL   A 1 39  ? -16.59100 -4.00900  -27.36600 1.000 40.78000  ? 5   VAL   A HG22   1 
ATOM   91   H HG23   . VAL   A 1 39  ? -18.03300 -3.41100  -27.06700 1.000 40.78000  ? 5   VAL   A HG23   1 
ATOM   92   N N      . GLY   A 1 40  ? -16.58900 -6.79900  -23.51200 1.000 41.88000  ? 6   GLY   A N      1 
ATOM   93   C CA     . GLY   A 1 40  ? -16.67300 -7.34700  -22.17900 1.000 41.89000  ? 6   GLY   A CA     1 
ATOM   94   C C      . GLY   A 1 40  ? -15.56500 -6.79500  -21.33000 1.000 44.83000  ? 6   GLY   A C      1 
ATOM   95   O O      . GLY   A 1 40  ? -14.44000 -7.29600  -21.39700 1.000 54.65000  ? 6   GLY   A O      1 
ATOM   96   H H      . GLY   A 1 40  ? -15.95200 -7.10500  -24.00200 1.000 41.88000  ? 6   GLY   A H      1 
ATOM   97   H HA2    . GLY   A 1 40  ? -17.52400 -7.12900  -21.77000 1.000 41.89000  ? 6   GLY   A HA2    1 
ATOM   98   H HA3    . GLY   A 1 40  ? -16.58400 -8.31200  -22.21600 1.000 41.89000  ? 6   GLY   A HA3    1 
ATOM   99   N N      . ILE   A 1 41  ? -15.85000 -5.76400  -20.53700 1.000 41.73000  ? 7   ILE   A N      1 
ATOM   100  C CA     . ILE   A 1 41  ? -14.81200 -5.12400  -19.74400 1.000 55.34000  ? 7   ILE   A CA     1 
ATOM   101  C C      . ILE   A 1 41  ? -15.34900 -4.69000  -18.38900 1.000 50.18000  ? 7   ILE   A C      1 
ATOM   102  O O      . ILE   A 1 41  ? -16.54800 -4.47000  -18.19800 1.000 47.87000  ? 7   ILE   A O      1 
ATOM   103  C CB     . ILE   A 1 41  ? -14.21400 -3.92100  -20.48500 1.000 51.42000  ? 7   ILE   A CB     1 
ATOM   104  C CG1    . ILE   A 1 41  ? -15.31700 -2.90200  -20.75100 1.000 49.55000  ? 7   ILE   A CG1    1 
ATOM   105  C CG2    . ILE   A 1 41  ? -13.53700 -4.40100  -21.77300 1.000 45.25000  ? 7   ILE   A CG2    1 
ATOM   106  C CD1    . ILE   A 1 41  ? -14.81600 -1.59600  -21.32800 1.000 42.07000  ? 7   ILE   A CD1    1 
ATOM   107  H H      . ILE   A 1 41  ? -16.63300 -5.42000  -20.44300 1.000 41.73000  ? 7   ILE   A H      1 
ATOM   108  H HA     . ILE   A 1 41  ? -14.09700 -5.76000  -19.58700 1.000 55.34000  ? 7   ILE   A HA     1 
ATOM   109  H HB     . ILE   A 1 41  ? -13.55000 -3.51400  -19.91300 1.000 51.42000  ? 7   ILE   A HB     1 
ATOM   110  H HG12   . ILE   A 1 41  ? -15.94700 -3.28100  -21.38400 1.000 49.55000  ? 7   ILE   A HG12   1 
ATOM   111  H HG13   . ILE   A 1 41  ? -15.77300 -2.69100  -19.92200 1.000 49.55000  ? 7   ILE   A HG13   1 
ATOM   112  H HG21   . ILE   A 1 41  ? -13.05400 -3.66000  -22.17000 1.000 45.25000  ? 7   ILE   A HG21   1 
ATOM   113  H HG22   . ILE   A 1 41  ? -12.92100 -5.11900  -21.55600 1.000 45.25000  ? 7   ILE   A HG22   1 
ATOM   114  H HG23   . ILE   A 1 41  ? -14.21400 -4.72200  -22.38800 1.000 45.25000  ? 7   ILE   A HG23   1 
ATOM   115  H HD11   . ILE   A 1 41  ? -15.56700 -0.99200  -21.44000 1.000 42.07000  ? 7   ILE   A HD11   1 
ATOM   116  H HD12   . ILE   A 1 41  ? -14.16900 -1.21000  -20.71800 1.000 42.07000  ? 7   ILE   A HD12   1 
ATOM   117  H HD13   . ILE   A 1 41  ? -14.40000 -1.76900  -22.18700 1.000 42.07000  ? 7   ILE   A HD13   1 
ATOM   118  N N      . LEU   A 1 42  ? -14.41700 -4.54600  -17.44500 1.000 41.56000  ? 8   LEU   A N      1 
ATOM   119  C CA     . LEU   A 1 42  ? -14.73500 -4.15100  -16.07800 1.000 36.90000  ? 8   LEU   A CA     1 
ATOM   120  C C      . LEU   A 1 42  ? -15.76300 -5.09400  -15.45900 1.000 37.75000  ? 8   LEU   A C      1 
ATOM   121  O O      . LEU   A 1 42  ? -16.56100 -4.68300  -14.61400 1.000 40.47000  ? 8   LEU   A O      1 
ATOM   122  C CB     . LEU   A 1 42  ? -15.22900 -2.70600  -16.02400 1.000 41.42000  ? 8   LEU   A CB     1 
ATOM   123  C CG     . LEU   A 1 42  ? -14.18100 -1.69400  -16.49700 1.000 47.28000  ? 8   LEU   A CG     1 
ATOM   124  C CD1    . LEU   A 1 42  ? -14.85400 -0.38800  -16.90500 1.000 46.36000  ? 8   LEU   A CD1    1 
ATOM   125  C CD2    . LEU   A 1 42  ? -13.16600 -1.45900  -15.38800 1.000 44.84000  ? 8   LEU   A CD2    1 
ATOM   126  H H      . LEU   A 1 42  ? -13.57700 -4.67500  -17.57800 1.000 41.56000  ? 8   LEU   A H      1 
ATOM   127  H HA     . LEU   A 1 42  ? -13.92700 -4.20700  -15.54400 1.000 36.90000  ? 8   LEU   A HA     1 
ATOM   128  H HB2    . LEU   A 1 42  ? -16.01000 -2.62000  -16.59300 1.000 41.42000  ? 8   LEU   A HB2    1 
ATOM   129  H HB3    . LEU   A 1 42  ? -15.46200 -2.48700  -15.10800 1.000 41.42000  ? 8   LEU   A HB3    1 
ATOM   130  H HG     . LEU   A 1 42  ? -13.71300 -2.05000  -17.26900 1.000 47.28000  ? 8   LEU   A HG     1 
ATOM   131  H HD11   . LEU   A 1 42  ? -14.23200 0.13400   -17.43500 1.000 46.36000  ? 8   LEU   A HD11   1 
ATOM   132  H HD12   . LEU   A 1 42  ? -15.64700 -0.58700  -17.42700 1.000 46.36000  ? 8   LEU   A HD12   1 
ATOM   133  H HD13   . LEU   A 1 42  ? -15.09800 0.10300   -16.10500 1.000 46.36000  ? 8   LEU   A HD13   1 
ATOM   134  H HD21   . LEU   A 1 42  ? -12.52100 -0.79900  -15.68600 1.000 44.84000  ? 8   LEU   A HD21   1 
ATOM   135  H HD22   . LEU   A 1 42  ? -13.62900 -1.13600  -14.60000 1.000 44.84000  ? 8   LEU   A HD22   1 
ATOM   136  H HD23   . LEU   A 1 42  ? -12.71600 -2.29500  -15.18800 1.000 44.84000  ? 8   LEU   A HD23   1 
ATOM   137  N N      . GLY   A 1 43  ? -15.76000 -6.35200  -15.90100 1.000 39.36000  ? 9   GLY   A N      1 
ATOM   138  C CA     . GLY   A 1 43  ? -16.72500 -7.32600  -15.42600 1.000 51.02000  ? 9   GLY   A CA     1 
ATOM   139  C C      . GLY   A 1 43  ? -18.14500 -7.15700  -15.92900 1.000 49.59000  ? 9   GLY   A C      1 
ATOM   140  O O      . GLY   A 1 43  ? -19.04900 -7.81100  -15.40500 1.000 50.32000  ? 9   GLY   A O      1 
ATOM   141  H H      . GLY   A 1 43  ? -15.20400 -6.66300  -16.47900 1.000 39.36000  ? 9   GLY   A H      1 
ATOM   142  H HA2    . GLY   A 1 43  ? -16.42500 -8.21200  -15.68400 1.000 51.02000  ? 9   GLY   A HA2    1 
ATOM   143  H HA3    . GLY   A 1 43  ? -16.75000 -7.29100  -14.45700 1.000 51.02000  ? 9   GLY   A HA3    1 
ATOM   144  N N      . ASN   A 1 44  ? -18.37400 -6.30300  -16.92500 1.000 41.87000  ? 10  ASN   A N      1 
ATOM   145  C CA     . ASN   A 1 44  ? -19.67800 -6.07700  -17.53600 1.000 36.94000  ? 10  ASN   A CA     1 
ATOM   146  C C      . ASN   A 1 44  ? -19.64100 -6.48200  -19.00500 1.000 36.09000  ? 10  ASN   A C      1 
ATOM   147  O O      . ASN   A 1 44  ? -18.60200 -6.38100  -19.66200 1.000 40.54000  ? 10  ASN   A O      1 
ATOM   148  C CB     . ASN   A 1 44  ? -20.08200 -4.59600  -17.48400 1.000 41.02000  ? 10  ASN   A CB     1 
ATOM   149  C CG     . ASN   A 1 44  ? -20.44800 -4.12000  -16.10000 1.000 52.79000  ? 10  ASN   A CG     1 
ATOM   150  O OD1    . ASN   A 1 44  ? -21.56800 -4.33500  -15.64800 1.000 61.20000  ? 10  ASN   A OD1    1 
ATOM   151  N ND2    . ASN   A 1 44  ? -19.52600 -3.41000  -15.44000 1.000 59.31000  ? 10  ASN   A ND2    1 
ATOM   152  H H      . ASN   A 1 44  ? -17.75600 -5.82100  -17.27900 1.000 41.87000  ? 10  ASN   A H      1 
ATOM   153  H HA     . ASN   A 1 44  ? -20.35400 -6.60300  -17.08200 1.000 36.94000  ? 10  ASN   A HA     1 
ATOM   154  H HB2    . ASN   A 1 44  ? -19.33800 -4.05700  -17.79700 1.000 41.02000  ? 10  ASN   A HB2    1 
ATOM   155  H HB3    . ASN   A 1 44  ? -20.85200 -4.46100  -18.05900 1.000 41.02000  ? 10  ASN   A HB3    1 
ATOM   156  H HD21   . ASN   A 1 44  ? -19.69500 -3.11400  -14.65000 1.000 59.31000  ? 10  ASN   A HD21   1 
ATOM   157  H HD22   . ASN   A 1 44  ? -18.75500 -3.27000  -15.79500 1.000 59.31000  ? 10  ASN   A HD22   1 
ATOM   158  N N      . THR   A 1 45  ? -20.79300 -6.86800  -19.54900 1.000 37.32000  ? 11  THR   A N      1 
ATOM   159  C CA     . THR   A 1 45  ? -20.94400 -7.00300  -20.99400 1.000 36.10000  ? 11  THR   A CA     1 
ATOM   160  C C      . THR   A 1 45  ? -21.65100 -5.74700  -21.48000 1.000 39.83000  ? 11  THR   A C      1 
ATOM   161  O O      . THR   A 1 45  ? -22.81500 -5.52200  -21.14700 1.000 41.69000  ? 11  THR   A O      1 
ATOM   162  C CB     . THR   A 1 45  ? -21.73500 -8.24700  -21.40000 1.000 40.85000  ? 11  THR   A CB     1 
ATOM   163  O OG1    . THR   A 1 45  ? -21.06600 -9.43200  -20.95200 1.000 39.30000  ? 11  THR   A OG1    1 
ATOM   164  C CG2    . THR   A 1 45  ? -21.86900 -8.30800  -22.94600 1.000 40.93000  ? 11  THR   A CG2    1 
ATOM   165  H H      . THR   A 1 45  ? -21.50300 -7.05800  -19.10200 1.000 37.32000  ? 11  THR   A H      1 
ATOM   166  H HA     . THR   A 1 45  ? -20.07100 -7.04600  -21.41300 1.000 36.10000  ? 11  THR   A HA     1 
ATOM   167  H HB     . THR   A 1 45  ? -22.62400 -8.20900  -21.01300 1.000 40.85000  ? 11  THR   A HB     1 
ATOM   168  H HG1    . THR   A 1 45  ? -21.50400 -10.11200 -21.17700 1.000 39.30000  ? 11  THR   A HG1    1 
ATOM   169  H HG21   . THR   A 1 45  ? -22.20800 -9.17700  -23.21300 1.000 40.93000  ? 11  THR   A HG21   1 
ATOM   170  H HG22   . THR   A 1 45  ? -22.48200 -7.62300  -23.25600 1.000 40.93000  ? 11  THR   A HG22   1 
ATOM   171  H HG23   . THR   A 1 45  ? -21.00300 -8.16800  -23.35900 1.000 40.93000  ? 11  THR   A HG23   1 
ATOM   172  N N      . PHE   A 1 46  ? -20.94700 -4.91500  -22.23900 1.000 36.54000  ? 12  PHE   A N      1 
ATOM   173  C CA     . PHE   A 1 46  ? -21.58000 -3.75600  -22.86200 1.000 38.59000  ? 12  PHE   A CA     1 
ATOM   174  C C      . PHE   A 1 46  ? -22.10800 -4.16000  -24.23300 1.000 30.84000  ? 12  PHE   A C      1 
ATOM   175  O O      . PHE   A 1 46  ? -21.43100 -4.86500  -24.98800 1.000 35.31000  ? 12  PHE   A O      1 
ATOM   176  C CB     . PHE   A 1 46  ? -20.59700 -2.58700  -23.00900 1.000 36.49000  ? 12  PHE   A CB     1 
ATOM   177  C CG     . PHE   A 1 46  ? -20.09500 -2.01900  -21.70200 1.000 36.04000  ? 12  PHE   A CG     1 
ATOM   178  C CD1    . PHE   A 1 46  ? -19.09500 -2.66700  -20.98100 1.000 40.13000  ? 12  PHE   A CD1    1 
ATOM   179  C CD2    . PHE   A 1 46  ? -20.57900 -0.81400  -21.22100 1.000 38.49000  ? 12  PHE   A CD2    1 
ATOM   180  C CE1    . PHE   A 1 46  ? -18.61200 -2.12600  -19.78300 1.000 45.36000  ? 12  PHE   A CE1    1 
ATOM   181  C CE2    . PHE   A 1 46  ? -20.10800 -0.26000  -20.03000 1.000 41.67000  ? 12  PHE   A CE2    1 
ATOM   182  C CZ     . PHE   A 1 46  ? -19.12100 -0.91600  -19.30700 1.000 38.44000  ? 12  PHE   A CZ     1 
ATOM   183  H H      . PHE   A 1 46  ? -20.10800 -4.99700  -22.40900 1.000 36.54000  ? 12  PHE   A H      1 
ATOM   184  H HA     . PHE   A 1 46  ? -22.32700 -3.46100  -22.31900 1.000 38.59000  ? 12  PHE   A HA     1 
ATOM   185  H HB2    . PHE   A 1 46  ? -19.82600 -2.89200  -23.51200 1.000 36.49000  ? 12  PHE   A HB2    1 
ATOM   186  H HB3    . PHE   A 1 46  ? -21.03800 -1.87000  -23.49100 1.000 36.49000  ? 12  PHE   A HB3    1 
ATOM   187  H HD1    . PHE   A 1 46  ? -18.75100 -3.47300  -21.29300 1.000 40.13000  ? 12  PHE   A HD1    1 
ATOM   188  H HD2    . PHE   A 1 46  ? -21.23900 -0.36700  -21.69900 1.000 38.49000  ? 12  PHE   A HD2    1 
ATOM   189  H HE1    . PHE   A 1 46  ? -17.95100 -2.57300  -19.30500 1.000 45.36000  ? 12  PHE   A HE1    1 
ATOM   190  H HE2    . PHE   A 1 46  ? -20.45500 0.54500   -19.72100 1.000 41.67000  ? 12  PHE   A HE2    1 
ATOM   191  H HZ     . PHE   A 1 46  ? -18.80500 -0.55500  -18.51000 1.000 38.44000  ? 12  PHE   A HZ     1 
ATOM   192  N N      . ALA   A 1 47  ? -23.31700 -3.69000  -24.56000 1.000 37.60000  ? 13  ALA   A N      1 
ATOM   193  C CA     . ALA   A 1 47  ? -23.95200 -4.07500  -25.81900 1.000 36.65000  ? 13  ALA   A CA     1 
ATOM   194  C C      . ALA   A 1 47  ? -23.13900 -3.63800  -27.02900 1.000 36.68000  ? 13  ALA   A C      1 
ATOM   195  O O      . ALA   A 1 47  ? -23.14400 -4.31000  -28.06900 1.000 37.76000  ? 13  ALA   A O      1 
ATOM   196  C CB     . ALA   A 1 47  ? -25.35900 -3.47800  -25.88200 1.000 43.58000  ? 13  ALA   A CB     1 
ATOM   197  H H      . ALA   A 1 47  ? -23.78300 -3.15400  -24.07500 1.000 37.60000  ? 13  ALA   A H      1 
ATOM   198  H HA     . ALA   A 1 47  ? -24.03500 -5.04100  -25.84800 1.000 36.65000  ? 13  ALA   A HA     1 
ATOM   199  H HB1    . ALA   A 1 47  ? -25.77400 -3.73700  -26.71900 1.000 43.58000  ? 13  ALA   A HB1    1 
ATOM   200  H HB2    . ALA   A 1 47  ? -25.87900 -3.81600  -25.13600 1.000 43.58000  ? 13  ALA   A HB2    1 
ATOM   201  H HB3    . ALA   A 1 47  ? -25.29400 -2.51200  -25.83000 1.000 43.58000  ? 13  ALA   A HB3    1 
ATOM   202  N N      . ASN   A 1 48  ? -22.46100 -2.50300  -26.91900 1.000 38.27000  ? 14  ASN   A N      1 
ATOM   203  C CA     . ASN   A 1 48  ? -21.63800 -1.95600  -27.98300 1.000 32.60000  ? 14  ASN   A CA     1 
ATOM   204  C C      . ASN   A 1 48  ? -20.68300 -0.95500  -27.34300 1.000 32.69000  ? 14  ASN   A C      1 
ATOM   205  O O      . ASN   A 1 48  ? -20.86300 -0.59100  -26.17300 1.000 34.27000  ? 14  ASN   A O      1 
ATOM   206  C CB     . ASN   A 1 48  ? -22.50700 -1.29100  -29.07400 1.000 35.92000  ? 14  ASN   A CB     1 
ATOM   207  C CG     . ASN   A 1 48  ? -23.31500 -0.12500  -28.53300 1.000 41.04000  ? 14  ASN   A CG     1 
ATOM   208  O OD1    . ASN   A 1 48  ? -22.74900 0.89700   -28.16200 1.000 37.59000  ? 14  ASN   A OD1    1 
ATOM   209  N ND2    . ASN   A 1 48  ? -24.63800 -0.28100  -28.45700 1.000 37.49000  ? 14  ASN   A ND2    1 
ATOM   210  H H      . ASN   A 1 48  ? -22.46400 -2.01600  -26.21000 1.000 38.27000  ? 14  ASN   A H      1 
ATOM   211  H HA     . ASN   A 1 48  ? -21.12400 -2.66300  -28.39100 1.000 32.60000  ? 14  ASN   A HA     1 
ATOM   212  H HB2    . ASN   A 1 48  ? -21.95600 -0.96500  -29.79700 1.000 35.92000  ? 14  ASN   A HB2    1 
ATOM   213  H HB3    . ASN   A 1 48  ? -23.13300 -1.94900  -29.41400 1.000 35.92000  ? 14  ASN   A HB3    1 
ATOM   214  H HD21   . ASN   A 1 48  ? -25.12900 0.35600   -28.15300 1.000 37.49000  ? 14  ASN   A HD21   1 
ATOM   215  H HD22   . ASN   A 1 48  ? -25.00000 -1.01400  -28.72200 1.000 37.49000  ? 14  ASN   A HD22   1 
ATOM   216  N N      . PRO   A 1 49  ? -19.66100 -0.49600  -28.06400 1.000 34.40000  ? 15  PRO   A N      1 
ATOM   217  C CA     . PRO   A 1 49  ? -18.63000 0.34200   -27.43100 1.000 34.19000  ? 15  PRO   A CA     1 
ATOM   218  C C      . PRO   A 1 49  ? -19.00400 1.80800   -27.23200 1.000 36.58000  ? 15  PRO   A C      1 
ATOM   219  O O      . PRO   A 1 49  ? -18.18000 2.55600   -26.69700 1.000 33.99000  ? 15  PRO   A O      1 
ATOM   220  C CB     . PRO   A 1 49  ? -17.44200 0.21900   -28.39500 1.000 36.46000  ? 15  PRO   A CB     1 
ATOM   221  C CG     . PRO   A 1 49  ? -18.04300 -0.10300  -29.71400 1.000 34.85000  ? 15  PRO   A CG     1 
ATOM   222  C CD     . PRO   A 1 49  ? -19.30000 -0.88800  -29.44300 1.000 35.12000  ? 15  PRO   A CD     1 
ATOM   223  H HA     . PRO   A 1 49  ? -18.37900 -0.03600  -26.57400 1.000 34.19000  ? 15  PRO   A HA     1 
ATOM   224  H HB2    . PRO   A 1 49  ? -16.96300 1.06200   -28.43300 1.000 36.46000  ? 15  PRO   A HB2    1 
ATOM   225  H HB3    . PRO   A 1 49  ? -16.85600 -0.49600  -28.10200 1.000 36.46000  ? 15  PRO   A HB3    1 
ATOM   226  H HG2    . PRO   A 1 49  ? -18.25300 0.72100   -30.18100 1.000 34.85000  ? 15  PRO   A HG2    1 
ATOM   227  H HG3    . PRO   A 1 49  ? -17.41800 -0.63500  -30.23100 1.000 34.85000  ? 15  PRO   A HG3    1 
ATOM   228  H HD2    . PRO   A 1 49  ? -19.98200 -0.61800  -30.07300 1.000 35.12000  ? 15  PRO   A HD2    1 
ATOM   229  H HD3    . PRO   A 1 49  ? -19.12300 -1.84000  -29.49200 1.000 35.12000  ? 15  PRO   A HD3    1 
ATOM   230  N N      . PHE   A 1 50  ? -20.20200 2.24700   -27.61500 1.000 36.62000  ? 16  PHE   A N      1 
ATOM   231  C CA     . PHE   A 1 50  ? -20.49100 3.67600   -27.71500 1.000 36.52000  ? 16  PHE   A CA     1 
ATOM   232  C C      . PHE   A 1 50  ? -21.09100 4.22500   -26.43300 1.000 40.36000  ? 16  PHE   A C      1 
ATOM   233  O O      . PHE   A 1 50  ? -21.88500 3.56200   -25.76200 1.000 41.23000  ? 16  PHE   A O      1 
ATOM   234  C CB     . PHE   A 1 50  ? -21.42800 3.96300   -28.89200 1.000 37.02000  ? 16  PHE   A CB     1 
ATOM   235  C CG     . PHE   A 1 50  ? -20.80900 3.70000   -30.22200 1.000 38.16000  ? 16  PHE   A CG     1 
ATOM   236  C CD1    . PHE   A 1 50  ? -19.84100 4.55100   -30.72700 1.000 33.70000  ? 16  PHE   A CD1    1 
ATOM   237  C CD2    . PHE   A 1 50  ? -21.17800 2.59100   -30.96100 1.000 32.74000  ? 16  PHE   A CD2    1 
ATOM   238  C CE1    . PHE   A 1 50  ? -19.26500 4.31200   -31.95300 1.000 36.09000  ? 16  PHE   A CE1    1 
ATOM   239  C CE2    . PHE   A 1 50  ? -20.60700 2.33000   -32.19400 1.000 37.17000  ? 16  PHE   A CE2    1 
ATOM   240  C CZ     . PHE   A 1 50  ? -19.64200 3.18600   -32.69900 1.000 43.13000  ? 16  PHE   A CZ     1 
ATOM   241  H H      . PHE   A 1 50  ? -20.86400 1.73800   -27.82200 1.000 36.62000  ? 16  PHE   A H      1 
ATOM   242  H HA     . PHE   A 1 50  ? -19.66100 4.14900   -27.87900 1.000 36.52000  ? 16  PHE   A HA     1 
ATOM   243  H HB2    . PHE   A 1 50  ? -22.21300 3.39900   -28.81200 1.000 37.02000  ? 16  PHE   A HB2    1 
ATOM   244  H HB3    . PHE   A 1 50  ? -21.68900 4.89700   -28.86500 1.000 37.02000  ? 16  PHE   A HB3    1 
ATOM   245  H HD1    . PHE   A 1 50  ? -19.58500 5.29900   -30.23700 1.000 33.70000  ? 16  PHE   A HD1    1 
ATOM   246  H HD2    . PHE   A 1 50  ? -21.82400 2.01300   -30.62500 1.000 32.74000  ? 16  PHE   A HD2    1 
ATOM   247  H HE1    . PHE   A 1 50  ? -18.61700 4.89200   -32.28200 1.000 36.09000  ? 16  PHE   A HE1    1 
ATOM   248  H HE2    . PHE   A 1 50  ? -20.86800 1.58200   -32.68100 1.000 37.17000  ? 16  PHE   A HE2    1 
ATOM   249  H HZ     . PHE   A 1 50  ? -19.25400 3.02000   -33.52800 1.000 43.13000  ? 16  PHE   A HZ     1 
ATOM   250  N N      . MET   A 1 51  ? -20.68700 5.44700   -26.09000 1.000 34.33000  ? 17  MET   A N      1 
ATOM   251  C CA     . MET   A 1 51  ? -21.25100 6.17100   -24.96900 1.000 31.32000  ? 17  MET   A CA     1 
ATOM   252  C C      . MET   A 1 51  ? -21.06500 7.64800   -25.25200 1.000 39.48000  ? 17  MET   A C      1 
ATOM   253  O O      . MET   A 1 51  ? -20.33500 8.03500   -26.16700 1.000 36.66000  ? 17  MET   A O      1 
ATOM   254  C CB     . MET   A 1 51  ? -20.58800 5.77900   -23.64500 1.000 37.08000  ? 17  MET   A CB     1 
ATOM   255  C CG     . MET   A 1 51  ? -19.10400 6.08800   -23.58800 1.000 41.43000  ? 17  MET   A CG     1 
ATOM   256  S SD     . MET   A 1 51  ? -18.26500 5.27200   -22.19200 1.000 41.46000  ? 17  MET   A SD     1 
ATOM   257  C CE     . MET   A 1 51  ? -18.81600 6.19900   -20.80000 1.000 40.34000  ? 17  MET   A CE     1 
ATOM   258  H H      . MET   A 1 51  ? -20.07300 5.88200   -26.50500 1.000 34.33000  ? 17  MET   A H      1 
ATOM   259  H HA     . MET   A 1 51  ? -22.19900 5.97400   -24.90400 1.000 31.32000  ? 17  MET   A HA     1 
ATOM   260  H HB2    . MET   A 1 51  ? -21.02000 6.26300   -22.92400 1.000 37.08000  ? 17  MET   A HB2    1 
ATOM   261  H HB3    . MET   A 1 51  ? -20.69700 4.82500   -23.51100 1.000 37.08000  ? 17  MET   A HB3    1 
ATOM   262  H HG2    . MET   A 1 51  ? -18.68500 5.78400   -24.40800 1.000 41.43000  ? 17  MET   A HG2    1 
ATOM   263  H HG3    . MET   A 1 51  ? -18.98500 7.04600   -23.49000 1.000 41.43000  ? 17  MET   A HG3    1 
ATOM   264  H HE1    . MET   A 1 51  ? -18.31600 5.92000   -20.01700 1.000 40.34000  ? 17  MET   A HE1    1 
ATOM   265  H HE2    . MET   A 1 51  ? -18.66500 7.14200   -20.97000 1.000 40.34000  ? 17  MET   A HE2    1 
ATOM   266  H HE3    . MET   A 1 51  ? -19.76300 6.03500   -20.66600 1.000 40.34000  ? 17  MET   A HE3    1 
ATOM   267  N N      . ASN   A 1 52  ? -21.73900 8.47500   -24.46500 1.000 37.20000  ? 18  ASN   A N      1 
ATOM   268  C CA     . ASN   A 1 52  ? -21.49800 9.90300   -24.56000 1.000 39.62000  ? 18  ASN   A CA     1 
ATOM   269  C C      . ASN   A 1 52  ? -20.17100 10.24500  -23.90000 1.000 39.09000  ? 18  ASN   A C      1 
ATOM   270  O O      . ASN   A 1 52  ? -19.68700 9.53700   -23.00600 1.000 36.98000  ? 18  ASN   A O      1 
ATOM   271  C CB     . ASN   A 1 52  ? -22.61900 10.70300  -23.89400 1.000 40.07000  ? 18  ASN   A CB     1 
ATOM   272  C CG     . ASN   A 1 52  ? -22.71100 10.43000  -22.41200 1.000 39.53000  ? 18  ASN   A CG     1 
ATOM   273  O OD1    . ASN   A 1 52  ? -22.85500 9.27800   -21.99200 1.000 42.79000  ? 18  ASN   A OD1    1 
ATOM   274  N ND2    . ASN   A 1 52  ? -22.57500 11.47800  -21.60100 1.000 37.71000  ? 18  ASN   A ND2    1 
ATOM   275  H H      . ASN   A 1 52  ? -22.32700 8.24100   -23.88200 1.000 37.20000  ? 18  ASN   A H      1 
ATOM   276  H HA     . ASN   A 1 52  ? -21.45100 10.16100  -25.49400 1.000 39.62000  ? 18  ASN   A HA     1 
ATOM   277  H HB2    . ASN   A 1 52  ? -22.45000 11.65000  -24.01700 1.000 40.07000  ? 18  ASN   A HB2    1 
ATOM   278  H HB3    . ASN   A 1 52  ? -23.46600 10.46000  -24.29900 1.000 40.07000  ? 18  ASN   A HB3    1 
ATOM   279  H HD21   . ASN   A 1 52  ? -22.61600 11.37000  -20.74900 1.000 37.71000  ? 18  ASN   A HD21   1 
ATOM   280  H HD22   . ASN   A 1 52  ? -22.46700 12.26500  -21.93000 1.000 37.71000  ? 18  ASN   A HD22   1 
ATOM   281  N N      . ALA   A 1 53  ? -19.58300 11.34600  -24.35800 1.000 36.98000  ? 19  ALA   A N      1 
ATOM   282  C CA     . ALA   A 1 53  ? -18.45100 11.95100  -23.68200 1.000 35.77000  ? 19  ALA   A CA     1 
ATOM   283  C C      . ALA   A 1 53  ? -18.93100 12.70800  -22.45300 1.000 39.37000  ? 19  ALA   A C      1 
ATOM   284  O O      . ALA   A 1 53  ? -20.01200 13.30800  -22.45200 1.000 38.67000  ? 19  ALA   A O      1 
ATOM   285  C CB     . ALA   A 1 53  ? -17.71200 12.89800  -24.64300 1.000 33.85000  ? 19  ALA   A CB     1 
ATOM   286  H H      . ALA   A 1 53  ? -19.82800 11.76400  -25.06900 1.000 36.98000  ? 19  ALA   A H      1 
ATOM   287  H HA     . ALA   A 1 53  ? -17.83500 11.25800  -23.39700 1.000 35.77000  ? 19  ALA   A HA     1 
ATOM   288  H HB1    . ALA   A 1 53  ? -16.79200 12.99300  -24.35300 1.000 33.85000  ? 19  ALA   A HB1    1 
ATOM   289  H HB2    . ALA   A 1 53  ? -17.73300 12.51300  -25.53300 1.000 33.85000  ? 19  ALA   A HB2    1 
ATOM   290  H HB3    . ALA   A 1 53  ? -18.16100 13.75800  -24.65100 1.000 33.85000  ? 19  ALA   A HB3    1 
ATOM   291  N N      . ALA   A 1 54  ? -18.12700 12.69100  -21.39900 1.000 38.31000  ? 20  ALA   A N      1 
ATOM   292  C CA     . ALA   A 1 54  ? -18.51000 13.42900  -20.20300 1.000 40.68000  ? 20  ALA   A CA     1 
ATOM   293  C C      . ALA   A 1 54  ? -18.76600 14.88800  -20.56300 1.000 42.40000  ? 20  ALA   A C      1 
ATOM   294  O O      . ALA   A 1 54  ? -18.02700 15.48400  -21.34900 1.000 42.29000  ? 20  ALA   A O      1 
ATOM   295  C CB     . ALA   A 1 54  ? -17.42400 13.32900  -19.13400 1.000 33.00000  ? 20  ALA   A CB     1 
ATOM   296  H H      . ALA   A 1 54  ? -17.37700 12.27400  -21.34900 1.000 38.31000  ? 20  ALA   A H      1 
ATOM   297  H HA     . ALA   A 1 54  ? -19.32900 13.05500  -19.84300 1.000 40.68000  ? 20  ALA   A HA     1 
ATOM   298  H HB1    . ALA   A 1 54  ? -17.70400 13.83100  -18.35200 1.000 33.00000  ? 20  ALA   A HB1    1 
ATOM   299  H HB2    . ALA   A 1 54  ? -17.29600 12.39600  -18.90100 1.000 33.00000  ? 20  ALA   A HB2    1 
ATOM   300  H HB3    . ALA   A 1 54  ? -16.59900 13.69800  -19.48700 1.000 33.00000  ? 20  ALA   A HB3    1 
ATOM   301  N N      . GLY   A 1 55  ? -19.84700 15.45400  -20.01300 1.000 42.74000  ? 21  GLY   A N      1 
ATOM   302  C CA     . GLY   A 1 55  ? -20.22300 16.82900  -20.28000 1.000 43.66000  ? 21  GLY   A CA     1 
ATOM   303  C C      . GLY   A 1 55  ? -21.22400 17.03300  -21.40100 1.000 47.59000  ? 21  GLY   A C      1 
ATOM   304  O O      . GLY   A 1 55  ? -21.76300 18.13600  -21.53400 1.000 50.72000  ? 21  GLY   A O      1 
ATOM   305  H H      . GLY   A 1 55  ? -20.38100 15.04800  -19.47500 1.000 42.74000  ? 21  GLY   A H      1 
ATOM   306  H HA2    . GLY   A 1 55  ? -20.59200 17.21700  -19.47600 1.000 43.66000  ? 21  GLY   A HA2    1 
ATOM   307  H HA3    . GLY   A 1 55  ? -19.43300 17.31500  -20.51800 1.000 43.66000  ? 21  GLY   A HA3    1 
ATOM   308  N N      . VAL   A 1 56  ? -21.48800 16.02600  -22.22400 1.000 44.66000  ? 22  VAL   A N      1 
ATOM   309  C CA     . VAL   A 1 56  ? -22.41300 16.15800  -23.34600 1.000 46.35000  ? 22  VAL   A CA     1 
ATOM   310  C C      . VAL   A 1 56  ? -23.65900 15.33700  -23.04200 1.000 54.94000  ? 22  VAL   A C      1 
ATOM   311  O O      . VAL   A 1 56  ? -23.57500 14.11600  -22.85400 1.000 45.41000  ? 22  VAL   A O      1 
ATOM   312  C CB     . VAL   A 1 56  ? -21.76900 15.71900  -24.67200 1.000 43.16000  ? 22  VAL   A CB     1 
ATOM   313  C CG1    . VAL   A 1 56  ? -22.77200 15.82300  -25.80900 1.000 44.53000  ? 22  VAL   A CG1    1 
ATOM   314  C CG2    . VAL   A 1 56  ? -20.52700 16.56200  -24.96100 1.000 46.05000  ? 22  VAL   A CG2    1 
ATOM   315  H H      . VAL   A 1 56  ? -21.13900 15.24300  -22.15400 1.000 44.66000  ? 22  VAL   A H      1 
ATOM   316  H HA     . VAL   A 1 56  ? -22.68000 17.08600  -23.43700 1.000 46.35000  ? 22  VAL   A HA     1 
ATOM   317  H HB     . VAL   A 1 56  ? -21.49300 14.79200  -24.59800 1.000 43.16000  ? 22  VAL   A HB     1 
ATOM   318  H HG11   . VAL   A 1 56  ? -22.30000 15.74800  -26.65200 1.000 44.53000  ? 22  VAL   A HG11   1 
ATOM   319  H HG12   . VAL   A 1 56  ? -23.42000 15.10600  -25.72900 1.000 44.53000  ? 22  VAL   A HG12   1 
ATOM   320  H HG13   . VAL   A 1 56  ? -23.21900 16.68200  -25.75700 1.000 44.53000  ? 22  VAL   A HG13   1 
ATOM   321  H HG21   . VAL   A 1 56  ? -20.17200 16.31400  -25.82900 1.000 46.05000  ? 22  VAL   A HG21   1 
ATOM   322  H HG22   . VAL   A 1 56  ? -20.77600 17.50000  -24.96100 1.000 46.05000  ? 22  VAL   A HG22   1 
ATOM   323  H HG23   . VAL   A 1 56  ? -19.86500 16.39600  -24.27200 1.000 46.05000  ? 22  VAL   A HG23   1 
ATOM   324  N N      . MET   A 1 57  ? -24.81400 16.01200  -22.99400 1.000 51.36000  ? 23  MET   A N      1 
ATOM   325  C CA     . MET   A 1 57  ? -26.11900 15.36100  -22.83700 1.000 56.67000  ? 23  MET   A CA     1 
ATOM   326  C C      . MET   A 1 57  ? -26.17500 14.51600  -21.56400 1.000 61.06000  ? 23  MET   A C      1 
ATOM   327  O O      . MET   A 1 57  ? -26.53000 13.33500  -21.58700 1.000 56.25000  ? 23  MET   A O      1 
ATOM   328  C CB     . MET   A 1 57  ? -26.45500 14.51400  -24.06800 1.000 54.91000  ? 23  MET   A CB     1 
ATOM   329  C CG     . MET   A 1 57  ? -27.79600 13.79500  -23.98900 1.000 67.36000  ? 23  MET   A CG     1 
ATOM   330  S SD     . MET   A 1 57  ? -28.44400 13.47000  -25.63700 1.000 75.18000  ? 23  MET   A SD     1 
ATOM   331  C CE     . MET   A 1 57  ? -28.23800 15.10900  -26.35200 1.000 69.27000  ? 23  MET   A CE     1 
ATOM   332  H H      . MET   A 1 57  ? -24.86700 16.86800  -23.05200 1.000 51.36000  ? 23  MET   A H      1 
ATOM   333  H HA     . MET   A 1 57  ? -26.79600 16.05200  -22.77100 1.000 56.67000  ? 23  MET   A HA     1 
ATOM   334  H HB2    . MET   A 1 57  ? -26.40900 15.09300  -24.83500 1.000 54.91000  ? 23  MET   A HB2    1 
ATOM   335  H HB3    . MET   A 1 57  ? -25.77400 13.82800  -24.15200 1.000 54.91000  ? 23  MET   A HB3    1 
ATOM   336  H HG2    . MET   A 1 57  ? -27.68400 12.94600  -23.54200 1.000 67.36000  ? 23  MET   A HG2    1 
ATOM   337  H HG3    . MET   A 1 57  ? -28.43300 14.34900  -23.51200 1.000 67.36000  ? 23  MET   A HG3    1 
ATOM   338  H HE1    . MET   A 1 57  ? -28.91800 15.24000  -27.03100 1.000 69.27000  ? 23  MET   A HE1    1 
ATOM   339  H HE2    . MET   A 1 57  ? -28.34000 15.77600  -25.65500 1.000 69.27000  ? 23  MET   A HE2    1 
ATOM   340  H HE3    . MET   A 1 57  ? -27.35700 15.17500  -26.75300 1.000 69.27000  ? 23  MET   A HE3    1 
ATOM   341  N N      . CYS   A 1 58  ? -25.82800 15.12900  -20.43700 1.000 49.07000  ? 24  CYS   A N      1 
ATOM   342  C CA     . CYS   A 1 58  ? -25.68400 14.31400  -19.24200 1.000 54.05000  ? 24  CYS   A CA     1 
ATOM   343  C C      . CYS   A 1 58  ? -25.76300 15.11300  -17.95300 1.000 67.76000  ? 24  CYS   A C      1 
ATOM   344  O O      . CYS   A 1 58  ? -25.41200 14.59900  -16.88600 1.000 70.50000  ? 24  CYS   A O      1 
ATOM   345  C CB     . CYS   A 1 58  ? -24.35400 13.55300  -19.29200 1.000 65.48000  ? 24  CYS   A CB     1 
ATOM   346  S SG     . CYS   A 1 58  ? -22.86900 14.57300  -19.09700 1.000 61.18000  ? 24  CYS   A SG     1 
ATOM   347  H H      . CYS   A 1 58  ? -25.67600 15.97000  -20.34200 1.000 49.07000  ? 24  CYS   A H      1 
ATOM   348  H HA     . CYS   A 1 58  ? -26.39900 13.65900  -19.22200 1.000 54.05000  ? 24  CYS   A HA     1 
ATOM   349  H HB2    . CYS   A 1 58  ? -24.35000 12.89500  -18.57900 1.000 65.48000  ? 24  CYS   A HB2    1 
ATOM   350  H HB3    . CYS   A 1 58  ? -24.28800 13.10200  -20.14800 1.000 65.48000  ? 24  CYS   A HB3    1 
ATOM   351  H HG     . CYS   A 1 58  ? -22.85600 15.39800  -19.96800 1.000 61.18000  ? 24  CYS   A HG     1 
ATOM   352  N N      . SER   A 1 59  ? -26.22700 16.35500  -18.02600 1.000 63.16000  ? 25  SER   A N      1 
ATOM   353  C CA     . SER   A 1 59  ? -26.28100 17.15900  -16.81200 1.000 77.31000  ? 25  SER   A CA     1 
ATOM   354  C C      . SER   A 1 59  ? -27.65300 17.09900  -16.14100 1.000 84.32000  ? 25  SER   A C      1 
ATOM   355  O O      . SER   A 1 59  ? -27.73100 16.94800  -14.91400 1.000 85.42000  ? 25  SER   A O      1 
ATOM   356  C CB     . SER   A 1 59  ? -25.88600 18.60600  -17.12500 1.000 76.02000  ? 25  SER   A CB     1 
ATOM   357  O OG     . SER   A 1 59  ? -24.50000 18.68400  -17.44900 1.000 76.37000  ? 25  SER   A OG     1 
ATOM   358  H H      . SER   A 1 59  ? -26.50900 16.74500  -18.73900 1.000 63.16000  ? 25  SER   A H      1 
ATOM   359  H HA     . SER   A 1 59  ? -25.63100 16.81400  -16.18200 1.000 77.31000  ? 25  SER   A HA     1 
ATOM   360  H HB2    . SER   A 1 59  ? -26.40700 18.92000  -17.88100 1.000 76.02000  ? 25  SER   A HB2    1 
ATOM   361  H HB3    . SER   A 1 59  ? -26.06100 19.15800  -16.34700 1.000 76.02000  ? 25  SER   A HB3    1 
ATOM   362  H HG     . SER   A 1 59  ? -24.28900 19.47900  -17.62000 1.000 76.37000  ? 25  SER   A HG     1 
ATOM   363  N N      . THR   A 1 60  ? -28.73400 17.18000  -16.92200 1.000 72.10000  ? 26  THR   A N      1 
ATOM   364  C CA     . THR   A 1 60  ? -30.09600 17.17100  -16.39900 1.000 79.81000  ? 26  THR   A CA     1 
ATOM   365  C C      . THR   A 1 60  ? -30.65500 15.75100  -16.35000 1.000 81.36000  ? 26  THR   A C      1 
ATOM   366  O O      . THR   A 1 60  ? -30.31800 14.90200  -17.17600 1.000 79.98000  ? 26  THR   A O      1 
ATOM   367  C CB     . THR   A 1 60  ? -31.00700 18.05100  -17.26300 1.000 78.67000  ? 26  THR   A CB     1 
ATOM   368  O OG1    . THR   A 1 60  ? -31.56300 17.26600  -18.32700 1.000 71.40000  ? 26  THR   A OG1    1 
ATOM   369  C CG2    . THR   A 1 60  ? -30.22500 19.21600  -17.86100 1.000 75.27000  ? 26  THR   A CG2    1 
ATOM   370  H H      . THR   A 1 60  ? -28.69700 17.23400  -17.77900 1.000 72.10000  ? 26  THR   A H      1 
ATOM   371  H HA     . THR   A 1 60  ? -30.09500 17.52800  -15.49700 1.000 79.81000  ? 26  THR   A HA     1 
ATOM   372  H HB     . THR   A 1 60  ? -31.72400 18.41000  -16.71700 1.000 78.67000  ? 26  THR   A HB     1 
ATOM   373  H HG1    . THR   A 1 60  ? -32.06300 17.74300  -18.80400 1.000 71.40000  ? 26  THR   A HG1    1 
ATOM   374  H HG21   . THR   A 1 60  ? -30.83900 19.88900  -18.19400 1.000 75.27000  ? 26  THR   A HG21   1 
ATOM   375  H HG22   . THR   A 1 60  ? -29.65700 19.61600  -17.18400 1.000 75.27000  ? 26  THR   A HG22   1 
ATOM   376  H HG23   . THR   A 1 60  ? -29.67200 18.90600  -18.59400 1.000 75.27000  ? 26  THR   A HG23   1 
ATOM   377  N N      . GLU   A 1 61  ? -31.53600 15.50500  -15.37600 1.000 81.14000  ? 27  GLU   A N      1 
ATOM   378  C CA     . GLU   A 1 61  ? -32.15200 14.18700  -15.24700 1.000 71.32000  ? 27  GLU   A CA     1 
ATOM   379  C C      . GLU   A 1 61  ? -32.80700 13.73500  -16.54900 1.000 73.78000  ? 27  GLU   A C      1 
ATOM   380  O O      . GLU   A 1 61  ? -32.86800 12.53000  -16.83100 1.000 68.90000  ? 27  GLU   A O      1 
ATOM   381  H H      . GLU   A 1 61  ? -31.78900 16.07700  -14.78600 1.000 81.14000  ? 27  GLU   A H      1 
ATOM   382  N N      . GLU   A 1 62  ? -33.30100 14.68300  -17.35500 1.000 67.93000  ? 28  GLU   A N      1 
ATOM   383  C CA     . GLU   A 1 62  ? -33.91700 14.33000  -18.63200 1.000 69.99000  ? 28  GLU   A CA     1 
ATOM   384  C C      . GLU   A 1 62  ? -32.87500 13.88100  -19.65100 1.000 69.06000  ? 28  GLU   A C      1 
ATOM   385  O O      . GLU   A 1 62  ? -33.14700 13.00400  -20.48000 1.000 68.07000  ? 28  GLU   A O      1 
ATOM   386  C CB     . GLU   A 1 62  ? -34.70500 15.51900  -19.17000 1.000 74.36000  ? 28  GLU   A CB     1 
ATOM   387  C CG     . GLU   A 1 62  ? -35.26300 15.32200  -20.57300 1.000 69.75000  ? 28  GLU   A CG     1 
ATOM   388  C CD     . GLU   A 1 62  ? -36.05000 16.53000  -21.05400 1.000 83.91000  ? 28  GLU   A CD     1 
ATOM   389  O OE1    . GLU   A 1 62  ? -36.05500 17.56000  -20.34400 1.000 98.56000  ? 28  GLU   A OE1    1 
ATOM   390  O OE2    . GLU   A 1 62  ? -36.67000 16.45500  -22.13800 1.000 91.53000  ? 28  GLU   A OE2    1 
ATOM   391  H H      . GLU   A 1 62  ? -33.29100 15.52600  -17.18500 1.000 67.93000  ? 28  GLU   A H      1 
ATOM   392  H HA     . GLU   A 1 62  ? -34.53700 13.59700  -18.49300 1.000 69.99000  ? 28  GLU   A HA     1 
ATOM   393  H HB2    . GLU   A 1 62  ? -35.45300 15.68900  -18.57700 1.000 74.36000  ? 28  GLU   A HB2    1 
ATOM   394  H HB3    . GLU   A 1 62  ? -34.12200 16.29400  -19.19100 1.000 74.36000  ? 28  GLU   A HB3    1 
ATOM   395  H HG2    . GLU   A 1 62  ? -34.53300 15.18100  -21.19600 1.000 69.75000  ? 28  GLU   A HG2    1 
ATOM   396  H HG3    . GLU   A 1 62  ? -35.85600 14.55500  -20.57500 1.000 69.75000  ? 28  GLU   A HG3    1 
ATOM   397  N N      . GLU   A 1 63  ? -31.68600 14.48900  -19.62600 1.000 63.68000  ? 29  GLU   A N      1 
ATOM   398  C CA     . GLU   A 1 63  ? -30.62000 14.04900  -20.52000 1.000 66.60000  ? 29  GLU   A CA     1 
ATOM   399  C C      . GLU   A 1 63  ? -30.13500 12.65600  -20.14000 1.000 59.05000  ? 29  GLU   A C      1 
ATOM   400  O O      . GLU   A 1 63  ? -29.99000 11.78600  -21.00400 1.000 60.50000  ? 29  GLU   A O      1 
ATOM   401  C CB     . GLU   A 1 63  ? -29.47200 15.05600  -20.50700 1.000 57.13000  ? 29  GLU   A CB     1 
ATOM   402  C CG     . GLU   A 1 63  ? -29.69600 16.24100  -21.43400 1.000 66.25000  ? 29  GLU   A CG     1 
ATOM   403  C CD     . GLU   A 1 63  ? -28.76400 17.39900  -21.14000 1.000 70.80000  ? 29  GLU   A CD     1 
ATOM   404  O OE1    . GLU   A 1 63  ? -28.25600 17.48900  -19.99900 1.000 71.46000  ? 29  GLU   A OE1    1 
ATOM   405  O OE2    . GLU   A 1 63  ? -28.54000 18.22200  -22.05400 1.000 71.48000  ? 29  GLU   A OE2    1 
ATOM   406  H H      . GLU   A 1 63  ? -31.47700 15.14500  -19.11100 1.000 63.68000  ? 29  GLU   A H      1 
ATOM   407  H HA     . GLU   A 1 63  ? -30.96700 14.00600  -21.42500 1.000 66.60000  ? 29  GLU   A HA     1 
ATOM   408  H HB2    . GLU   A 1 63  ? -29.36500 15.39500  -19.60500 1.000 57.13000  ? 29  GLU   A HB2    1 
ATOM   409  H HB3    . GLU   A 1 63  ? -28.66300 14.60500  -20.78800 1.000 57.13000  ? 29  GLU   A HB3    1 
ATOM   410  H HG2    . GLU   A 1 63  ? -29.54600 15.96000  -22.35000 1.000 66.25000  ? 29  GLU   A HG2    1 
ATOM   411  H HG3    . GLU   A 1 63  ? -30.60700 16.55600  -21.32900 1.000 66.25000  ? 29  GLU   A HG3    1 
ATOM   412  N N      . LEU   A 1 64  ? -29.88900 12.42000  -18.84800 1.000 59.35000  ? 30  LEU   A N      1 
ATOM   413  C CA     . LEU   A 1 64  ? -29.54400 11.07300  -18.40800 1.000 62.90000  ? 30  LEU   A CA     1 
ATOM   414  C C      . LEU   A 1 64  ? -30.58400 10.07000  -18.89800 1.000 65.76000  ? 30  LEU   A C      1 
ATOM   415  O O      . LEU   A 1 64  ? -30.24600 9.01700   -19.45200 1.000 59.40000  ? 30  LEU   A O      1 
ATOM   416  C CB     . LEU   A 1 64  ? -29.42100 11.02700  -16.88200 1.000 66.23000  ? 30  LEU   A CB     1 
ATOM   417  C CG     . LEU   A 1 64  ? -28.19600 11.59000  -16.14100 1.000 68.09000  ? 30  LEU   A CG     1 
ATOM   418  C CD1    . LEU   A 1 64  ? -26.88200 10.91800  -16.56900 1.000 60.62000  ? 30  LEU   A CD1    1 
ATOM   419  C CD2    . LEU   A 1 64  ? -28.10900 13.09700  -16.29900 1.000 75.97000  ? 30  LEU   A CD2    1 
ATOM   420  H H      . LEU   A 1 64  ? -29.91700 13.01000  -18.22300 1.000 59.35000  ? 30  LEU   A H      1 
ATOM   421  H HA     . LEU   A 1 64  ? -28.68600 10.82600  -18.78700 1.000 62.90000  ? 30  LEU   A HA     1 
ATOM   422  H HB2    . LEU   A 1 64  ? -30.18900 11.49700  -16.52200 1.000 66.23000  ? 30  LEU   A HB2    1 
ATOM   423  H HB3    . LEU   A 1 64  ? -29.48500 10.09500  -16.62200 1.000 66.23000  ? 30  LEU   A HB3    1 
ATOM   424  H HG     . LEU   A 1 64  ? -28.31000 11.41000  -15.19500 1.000 68.09000  ? 30  LEU   A HG     1 
ATOM   425  H HD11   . LEU   A 1 64  ? -26.15200 11.29800  -16.05600 1.000 60.62000  ? 30  LEU   A HD11   1 
ATOM   426  H HD12   . LEU   A 1 64  ? -26.94500 9.96500   -16.39900 1.000 60.62000  ? 30  LEU   A HD12   1 
ATOM   427  H HD13   . LEU   A 1 64  ? -26.74000 11.07700  -17.51500 1.000 60.62000  ? 30  LEU   A HD13   1 
ATOM   428  H HD21   . LEU   A 1 64  ? -27.31100 13.41400  -15.84900 1.000 75.97000  ? 30  LEU   A HD21   1 
ATOM   429  H HD22   . LEU   A 1 64  ? -28.06600 13.31600  -17.24200 1.000 75.97000  ? 30  LEU   A HD22   1 
ATOM   430  H HD23   . LEU   A 1 64  ? -28.89500 13.49900  -15.89800 1.000 75.97000  ? 30  LEU   A HD23   1 
ATOM   431  N N      . ALA   A 1 65  ? -31.86500 10.39800  -18.71500 1.000 64.19000  ? 31  ALA   A N      1 
ATOM   432  C CA     . ALA   A 1 65  ? -32.93200 9.50100   -19.14000 1.000 64.19000  ? 31  ALA   A CA     1 
ATOM   433  C C      . ALA   A 1 65  ? -32.86500 9.24200   -20.64100 1.000 60.26000  ? 31  ALA   A C      1 
ATOM   434  O O      . ALA   A 1 65  ? -32.97900 8.09500   -21.09300 1.000 64.01000  ? 31  ALA   A O      1 
ATOM   435  C CB     . ALA   A 1 65  ? -34.28600 10.08800  -18.74000 1.000 68.75000  ? 31  ALA   A CB     1 
ATOM   436  H H      . ALA   A 1 65  ? -32.13700 11.12800  -18.35000 1.000 64.19000  ? 31  ALA   A H      1 
ATOM   437  H HA     . ALA   A 1 65  ? -32.82900 8.65100   -18.68500 1.000 64.19000  ? 31  ALA   A HA     1 
ATOM   438  H HB1    . ALA   A 1 65  ? -34.98900 9.48400   -19.02700 1.000 68.75000  ? 31  ALA   A HB1    1 
ATOM   439  H HB2    . ALA   A 1 65  ? -34.31200 10.19200  -17.77600 1.000 68.75000  ? 31  ALA   A HB2    1 
ATOM   440  H HB3    . ALA   A 1 65  ? -34.39500 10.95100  -19.17000 1.000 68.75000  ? 31  ALA   A HB3    1 
ATOM   441  N N      . ALA   A 1 66  ? -32.66400 10.30100  -21.43100 1.000 58.75000  ? 32  ALA   A N      1 
ATOM   442  C CA     . ALA   A 1 66  ? -32.53300 10.13300  -22.87500 1.000 67.18000  ? 32  ALA   A CA     1 
ATOM   443  C C      . ALA   A 1 66  ? -31.33400 9.25300   -23.22600 1.000 60.65000  ? 32  ALA   A C      1 
ATOM   444  O O      . ALA   A 1 66  ? -31.40400 8.43000   -24.15000 1.000 55.47000  ? 32  ALA   A O      1 
ATOM   445  C CB     . ALA   A 1 66  ? -32.42200 11.50200  -23.54600 1.000 61.70000  ? 32  ALA   A CB     1 
ATOM   446  H H      . ALA   A 1 66  ? -32.60100 11.11400  -21.15800 1.000 58.75000  ? 32  ALA   A H      1 
ATOM   447  H HA     . ALA   A 1 66  ? -33.33100 9.69800   -23.21400 1.000 67.18000  ? 32  ALA   A HA     1 
ATOM   448  H HB1    . ALA   A 1 66  ? -32.33600 11.37700  -24.50400 1.000 61.70000  ? 32  ALA   A HB1    1 
ATOM   449  H HB2    . ALA   A 1 66  ? -33.22100 12.01500  -23.34900 1.000 61.70000  ? 32  ALA   A HB2    1 
ATOM   450  H HB3    . ALA   A 1 66  ? -31.64000 11.96000  -23.20000 1.000 61.70000  ? 32  ALA   A HB3    1 
ATOM   451  N N      . MET   A 1 67  ? -30.22400 9.41000   -22.50300 1.000 60.08000  ? 33  MET   A N      1 
ATOM   452  C CA     . MET   A 1 67  ? -29.06500 8.56400   -22.76800 1.000 57.96000  ? 33  MET   A CA     1 
ATOM   453  C C      . MET   A 1 67  ? -29.35500 7.10700   -22.41000 1.000 47.75000  ? 33  MET   A C      1 
ATOM   454  O O      . MET   A 1 67  ? -28.97300 6.19100   -23.15200 1.000 48.64000  ? 33  MET   A O      1 
ATOM   455  C CB     . MET   A 1 67  ? -27.84200 9.09300   -22.01100 1.000 48.23000  ? 33  MET   A CB     1 
ATOM   456  C CG     . MET   A 1 67  ? -27.03200 10.17300  -22.76700 1.000 47.51000  ? 33  MET   A CG     1 
ATOM   457  S SD     . MET   A 1 67  ? -26.44500 9.65700   -24.38600 1.000 51.44000  ? 33  MET   A SD     1 
ATOM   458  C CE     . MET   A 1 67  ? -25.48900 8.15600   -23.93800 1.000 42.66000  ? 33  MET   A CE     1 
ATOM   459  H H      . MET   A 1 67  ? -30.11900 9.98300   -21.87100 1.000 60.08000  ? 33  MET   A H      1 
ATOM   460  H HA     . MET   A 1 67  ? -28.86900 8.60800   -23.71600 1.000 57.96000  ? 33  MET   A HA     1 
ATOM   461  H HB2    . MET   A 1 67  ? -28.14200 9.48400   -21.17500 1.000 48.23000  ? 33  MET   A HB2    1 
ATOM   462  H HB3    . MET   A 1 67  ? -27.24600 8.35100   -21.82700 1.000 48.23000  ? 33  MET   A HB3    1 
ATOM   463  H HG2    . MET   A 1 67  ? -27.60200 10.94500  -22.89200 1.000 47.51000  ? 33  MET   A HG2    1 
ATOM   464  H HG3    . MET   A 1 67  ? -26.25900 10.41600  -22.23400 1.000 47.51000  ? 33  MET   A HG3    1 
ATOM   465  H HE1    . MET   A 1 67  ? -25.02800 7.82900   -24.72600 1.000 42.66000  ? 33  MET   A HE1    1 
ATOM   466  H HE2    . MET   A 1 67  ? -24.84500 8.38600   -23.25000 1.000 42.66000  ? 33  MET   A HE2    1 
ATOM   467  H HE3    . MET   A 1 67  ? -26.10000 7.47900   -23.60700 1.000 42.66000  ? 33  MET   A HE3    1 
ATOM   468  N N      . THR   A 1 68  ? -30.04300 6.87600   -21.28500 1.000 53.63000  ? 34  THR   A N      1 
ATOM   469  C CA     . THR   A 1 68  ? -30.38400 5.51100   -20.88200 1.000 51.49000  ? 34  THR   A CA     1 
ATOM   470  C C      . THR   A 1 68  ? -31.34300 4.86500   -21.87400 1.000 55.72000  ? 34  THR   A C      1 
ATOM   471  O O      . THR   A 1 68  ? -31.24400 3.66300   -22.15800 1.000 52.44000  ? 34  THR   A O      1 
ATOM   472  C CB     . THR   A 1 68  ? -30.99700 5.50400   -19.48000 1.000 57.22000  ? 34  THR   A CB     1 
ATOM   473  O OG1    . THR   A 1 68  ? -30.08700 6.10200   -18.55000 1.000 56.81000  ? 34  THR   A OG1    1 
ATOM   474  C CG2    . THR   A 1 68  ? -31.28900 4.07300   -19.03700 1.000 57.77000  ? 34  THR   A CG2    1 
ATOM   475  H H      . THR   A 1 68  ? -30.32000 7.48600   -20.74600 1.000 53.63000  ? 34  THR   A H      1 
ATOM   476  H HA     . THR   A 1 68  ? -29.57400 4.97800   -20.85800 1.000 51.49000  ? 34  THR   A HA     1 
ATOM   477  H HB     . THR   A 1 68  ? -31.83000 6.00200   -19.48600 1.000 57.22000  ? 34  THR   A HB     1 
ATOM   478  H HG1    . THR   A 1 68  ? -29.93200 6.89700   -18.77100 1.000 56.81000  ? 34  THR   A HG1    1 
ATOM   479  H HG21   . THR   A 1 68  ? -31.48700 4.05600   -18.08800 1.000 57.77000  ? 34  THR   A HG21   1 
ATOM   480  H HG22   . THR   A 1 68  ? -32.05100 3.72100   -19.52300 1.000 57.77000  ? 34  THR   A HG22   1 
ATOM   481  H HG23   . THR   A 1 68  ? -30.51800 3.51000   -19.20700 1.000 57.77000  ? 34  THR   A HG23   1 
ATOM   482  N N      . GLU   A 1 69  ? -32.28100 5.65000   -22.41200 0.880 55.14000  ? 35  GLU   A N      1 
ATOM   483  C CA     . GLU   A 1 69  ? -33.24200 5.13900   -23.38200 0.880 54.53000  ? 35  GLU   A CA     1 
ATOM   484  C C      . GLU   A 1 69  ? -32.60400 4.83600   -24.72700 0.880 57.72000  ? 35  GLU   A C      1 
ATOM   485  O O      . GLU   A 1 69  ? -33.16600 4.05700   -25.50800 0.880 50.60000  ? 35  GLU   A O      1 
ATOM   486  C CB     . GLU   A 1 69  ? -34.37400 6.14800   -23.57900 0.880 65.80000  ? 35  GLU   A CB     1 
ATOM   487  C CG     . GLU   A 1 69  ? -35.27800 6.33100   -22.37200 0.880 69.04000  ? 35  GLU   A CG     1 
ATOM   488  C CD     . GLU   A 1 69  ? -36.74500 6.18000   -22.73000 0.880 95.83000  ? 35  GLU   A CD     1 
ATOM   489  O OE1    . GLU   A 1 69  ? -37.07500 6.24800   -23.93600 0.880 103.48000 ? 35  GLU   A OE1    1 
ATOM   490  O OE2    . GLU   A 1 69  ? -37.56700 5.98300   -21.81000 0.880 106.07000 ? 35  GLU   A OE2    1 
ATOM   491  H H      . GLU   A 1 69  ? -32.37900 6.48400   -22.22800 0.880 55.14000  ? 35  GLU   A H      1 
ATOM   492  H HA     . GLU   A 1 69  ? -33.62800 4.31700   -23.04100 0.880 54.53000  ? 35  GLU   A HA     1 
ATOM   493  H HB2    . GLU   A 1 69  ? -33.98400 7.01200   -23.78400 0.880 65.80000  ? 35  GLU   A HB2    1 
ATOM   494  H HB3    . GLU   A 1 69  ? -34.91200 5.85000   -24.32700 0.880 65.80000  ? 35  GLU   A HB3    1 
ATOM   495  H HG2    . GLU   A 1 69  ? -35.05900 5.66100   -21.70600 0.880 69.04000  ? 35  GLU   A HG2    1 
ATOM   496  H HG3    . GLU   A 1 69  ? -35.14600 7.22000   -22.00800 0.880 69.04000  ? 35  GLU   A HG3    1 
ATOM   497  N N      . SER   A 1 70  ? -31.45000 5.43400   -25.01200 1.000 51.63000  ? 36  SER   A N      1 
ATOM   498  C CA     . SER   A 1 70  ? -30.81700 5.30600   -26.31300 1.000 47.83000  ? 36  SER   A CA     1 
ATOM   499  C C      . SER   A 1 70  ? -30.21100 3.91500   -26.48200 1.000 52.57000  ? 36  SER   A C      1 
ATOM   500  O O      . SER   A 1 70  ? -30.16000 3.11100   -25.54500 1.000 51.71000  ? 36  SER   A O      1 
ATOM   501  C CB     . SER   A 1 70  ? -29.73200 6.36800   -26.48400 1.000 51.52000  ? 36  SER   A CB     1 
ATOM   502  O OG     . SER   A 1 70  ? -28.53800 5.95200   -25.84800 1.000 49.63000  ? 36  SER   A OG     1 
ATOM   503  H H      . SER   A 1 70  ? -31.01100 5.92500   -24.46000 1.000 51.63000  ? 36  SER   A H      1 
ATOM   504  H HA     . SER   A 1 70  ? -31.48200 5.43500   -27.00700 1.000 47.83000  ? 36  SER   A HA     1 
ATOM   505  H HB2    . SER   A 1 70  ? -29.56000 6.49900   -27.43000 1.000 51.52000  ? 36  SER   A HB2    1 
ATOM   506  H HB3    . SER   A 1 70  ? -30.03400 7.19700   -26.08100 1.000 51.52000  ? 36  SER   A HB3    1 
ATOM   507  H HG     . SER   A 1 70  ? -28.67500 5.83400   -25.02800 1.000 49.63000  ? 36  SER   A HG     1 
ATOM   508  N N      . THR   A 1 71  ? -29.74200 3.63500   -27.70500 1.000 48.89000  ? 37  THR   A N      1 
ATOM   509  C CA     . THR   A 1 71  ? -29.07500 2.36800   -27.99700 1.000 49.96000  ? 37  THR   A CA     1 
ATOM   510  C C      . THR   A 1 71  ? -27.58800 2.37000   -27.63000 1.000 44.73000  ? 37  THR   A C      1 
ATOM   511  O O      . THR   A 1 71  ? -26.87400 1.44500   -28.03500 1.000 46.92000  ? 37  THR   A O      1 
ATOM   512  C CB     . THR   A 1 71  ? -29.21800 1.99600   -29.48400 1.000 54.38000  ? 37  THR   A CB     1 
ATOM   513  O OG1    . THR   A 1 71  ? -28.65200 3.02800   -30.30000 1.000 51.18000  ? 37  THR   A OG1    1 
ATOM   514  C CG2    . THR   A 1 71  ? -30.68700 1.78600   -29.87300 1.000 55.56000  ? 37  THR   A CG2    1 
ATOM   515  H H      . THR   A 1 71  ? -29.80000 4.16500   -28.38000 1.000 48.89000  ? 37  THR   A H      1 
ATOM   516  H HA     . THR   A 1 71  ? -29.50300 1.66900   -27.47900 1.000 49.96000  ? 37  THR   A HA     1 
ATOM   517  H HB     . THR   A 1 71  ? -28.74300 1.16600   -29.65000 1.000 54.38000  ? 37  THR   A HB     1 
ATOM   518  H HG1    . THR   A 1 71  ? -28.72900 2.82700   -31.11200 1.000 51.18000  ? 37  THR   A HG1    1 
ATOM   519  H HG21   . THR   A 1 71  ? -30.75000 1.54500   -30.81100 1.000 55.56000  ? 37  THR   A HG21   1 
ATOM   520  H HG22   . THR   A 1 71  ? -31.07300 1.07500   -29.33800 1.000 55.56000  ? 37  THR   A HG22   1 
ATOM   521  H HG23   . THR   A 1 71  ? -31.19000 2.60200   -29.72200 1.000 55.56000  ? 37  THR   A HG23   1 
ATOM   522  N N      . SER   A 1 72  ? -27.09800 3.37200   -26.90000 1.000 40.71000  ? 38  SER   A N      1 
ATOM   523  C CA     . SER   A 1 72  ? -25.68500 3.40000   -26.54600 1.000 45.20000  ? 38  SER   A CA     1 
ATOM   524  C C      . SER   A 1 72  ? -25.34900 2.26800   -25.58000 1.000 45.01000  ? 38  SER   A C      1 
ATOM   525  O O      . SER   A 1 72  ? -26.18300 1.83800   -24.77500 1.000 43.51000  ? 38  SER   A O      1 
ATOM   526  C CB     . SER   A 1 72  ? -25.32000 4.73700   -25.90700 1.000 42.20000  ? 38  SER   A CB     1 
ATOM   527  O OG     . SER   A 1 72  ? -25.87100 4.82400   -24.60700 1.000 48.82000  ? 38  SER   A OG     1 
ATOM   528  H H      . SER   A 1 72  ? -27.55600 4.03600   -26.60300 1.000 40.71000  ? 38  SER   A H      1 
ATOM   529  H HA     . SER   A 1 72  ? -25.15000 3.28800   -27.34700 1.000 45.20000  ? 38  SER   A HA     1 
ATOM   530  H HB2    . SER   A 1 72  ? -24.35400 4.80800   -25.84800 1.000 42.20000  ? 38  SER   A HB2    1 
ATOM   531  H HB3    . SER   A 1 72  ? -25.67500 5.45700   -26.45100 1.000 42.20000  ? 38  SER   A HB3    1 
ATOM   532  H HG     . SER   A 1 72  ? -25.45800 4.31400   -24.08300 1.000 48.82000  ? 38  SER   A HG     1 
ATOM   533  N N      . GLY   A 1 73  ? -24.10800 1.78400   -25.67300 1.000 44.22000  ? 39  GLY   A N      1 
ATOM   534  C CA     . GLY   A 1 73  ? -23.65600 0.73700   -24.76600 1.000 42.54000  ? 39  GLY   A CA     1 
ATOM   535  C C      . GLY   A 1 73  ? -23.54500 1.21000   -23.33000 1.000 42.29000  ? 39  GLY   A C      1 
ATOM   536  O O      . GLY   A 1 73  ? -23.69300 0.41600   -22.39300 1.000 46.49000  ? 39  GLY   A O      1 
ATOM   537  H H      . GLY   A 1 73  ? -23.52000 2.04300   -26.24400 1.000 44.22000  ? 39  GLY   A H      1 
ATOM   538  H HA2    . GLY   A 1 73  ? -24.27900 -0.00600  -24.79600 1.000 42.54000  ? 39  GLY   A HA2    1 
ATOM   539  H HA3    . GLY   A 1 73  ? -22.78600 0.41900   -25.05100 1.000 42.54000  ? 39  GLY   A HA3    1 
ATOM   540  N N      . SER   A 1 74  ? -23.30900 2.50400   -23.12900 1.000 38.17000  ? 40  SER   A N      1 
ATOM   541  C CA     . SER   A 1 74  ? -23.19500 3.02600   -21.77700 1.000 38.38000  ? 40  SER   A CA     1 
ATOM   542  C C      . SER   A 1 74  ? -23.44000 4.52600   -21.81500 1.000 38.77000  ? 40  SER   A C      1 
ATOM   543  O O      . SER   A 1 74  ? -23.80500 5.09000   -22.85200 1.000 42.16000  ? 40  SER   A O      1 
ATOM   544  C CB     . SER   A 1 74  ? -21.83100 2.67500   -21.17400 1.000 44.44000  ? 40  SER   A CB     1 
ATOM   545  O OG     . SER   A 1 74  ? -21.79500 2.95600   -19.78400 1.000 41.58000  ? 40  SER   A OG     1 
ATOM   546  H H      . SER   A 1 74  ? -23.21200 3.09100   -23.75000 1.000 38.17000  ? 40  SER   A H      1 
ATOM   547  H HA     . SER   A 1 74  ? -23.88100 2.62300   -21.22200 1.000 38.38000  ? 40  SER   A HA     1 
ATOM   548  H HB2    . SER   A 1 74  ? -21.66300 1.73000   -21.30800 1.000 44.44000  ? 40  SER   A HB2    1 
ATOM   549  H HB3    . SER   A 1 74  ? -21.14600 3.19900   -21.61900 1.000 44.44000  ? 40  SER   A HB3    1 
ATOM   550  H HG     . SER   A 1 74  ? -22.38300 2.50800   -19.38500 1.000 41.58000  ? 40  SER   A HG     1 
ATOM   551  N N      . LEU   A 1 75  ? -23.27100 5.15800   -20.65500 1.000 39.27000  ? 41  LEU   A N      1 
ATOM   552  C CA     . LEU   A 1 75  ? -23.37700 6.60400   -20.52700 1.000 41.56000  ? 41  LEU   A CA     1 
ATOM   553  C C      . LEU   A 1 75  ? -22.56300 7.02800   -19.31700 1.000 42.49000  ? 41  LEU   A C      1 
ATOM   554  O O      . LEU   A 1 75  ? -22.25100 6.21200   -18.44200 1.000 42.60000  ? 41  LEU   A O      1 
ATOM   555  C CB     . LEU   A 1 75  ? -24.83200 7.06500   -20.38100 1.000 51.13000  ? 41  LEU   A CB     1 
ATOM   556  C CG     . LEU   A 1 75  ? -25.43300 6.79500   -19.00100 1.000 46.89000  ? 41  LEU   A CG     1 
ATOM   557  C CD1    . LEU   A 1 75  ? -26.77100 7.48100   -18.86700 1.000 50.27000  ? 41  LEU   A CD1    1 
ATOM   558  C CD2    . LEU   A 1 75  ? -25.58300 5.29500   -18.77600 1.000 51.18000  ? 41  LEU   A CD2    1 
ATOM   559  H H      . LEU   A 1 75  ? -23.08900 4.76000   -19.91500 1.000 39.27000  ? 41  LEU   A H      1 
ATOM   560  H HA     . LEU   A 1 75  ? -22.99900 7.02200   -21.31500 1.000 41.56000  ? 41  LEU   A HA     1 
ATOM   561  H HB2    . LEU   A 1 75  ? -24.87300 8.02100   -20.54000 1.000 51.13000  ? 41  LEU   A HB2    1 
ATOM   562  H HB3    . LEU   A 1 75  ? -25.37400 6.60000   -21.03700 1.000 51.13000  ? 41  LEU   A HB3    1 
ATOM   563  H HG     . LEU   A 1 75  ? -24.85900 7.15000   -18.30600 1.000 46.89000  ? 41  LEU   A HG     1 
ATOM   564  H HD11   . LEU   A 1 75  ? -27.12700 7.30700   -17.98200 1.000 50.27000  ? 41  LEU   A HD11   1 
ATOM   565  H HD12   . LEU   A 1 75  ? -26.65000 8.43500   -18.99400 1.000 50.27000  ? 41  LEU   A HD12   1 
ATOM   566  H HD13   . LEU   A 1 75  ? -27.37400 7.13100   -19.54100 1.000 50.27000  ? 41  LEU   A HD13   1 
ATOM   567  H HD21   . LEU   A 1 75  ? -26.21000 5.14800   -18.05300 1.000 51.18000  ? 41  LEU   A HD21   1 
ATOM   568  H HD22   . LEU   A 1 75  ? -25.91300 4.88500   -19.59000 1.000 51.18000  ? 41  LEU   A HD22   1 
ATOM   569  H HD23   . LEU   A 1 75  ? -24.71900 4.92200   -18.54400 1.000 51.18000  ? 41  LEU   A HD23   1 
ATOM   570  N N      . ILE   A 1 76  ? -22.20600 8.31500   -19.28800 1.000 36.44000  ? 42  ILE   A N      1 
ATOM   571  C CA     . ILE   A 1 76  ? -21.43900 8.89800   -18.19500 1.000 38.53000  ? 42  ILE   A CA     1 
ATOM   572  C C      . ILE   A 1 76  ? -22.07400 10.23200  -17.83100 1.000 40.73000  ? 42  ILE   A C      1 
ATOM   573  O O      . ILE   A 1 76  ? -22.64700 10.92000  -18.68100 1.000 43.01000  ? 42  ILE   A O      1 
ATOM   574  C CB     . ILE   A 1 76  ? -19.94000 9.06800   -18.55500 1.000 38.24000  ? 42  ILE   A CB     1 
ATOM   575  C CG1    . ILE   A 1 76  ? -19.14600 9.63600   -17.37100 1.000 42.53000  ? 42  ILE   A CG1    1 
ATOM   576  C CG2    . ILE   A 1 76  ? -19.77800 9.96400   -19.76500 1.000 40.52000  ? 42  ILE   A CG2    1 
ATOM   577  C CD1    . ILE   A 1 76  ? -17.62800 9.48000   -17.51900 1.000 38.55000  ? 42  ILE   A CD1    1 
ATOM   578  H H      . ILE   A 1 76  ? -22.40300 8.87900   -19.90600 1.000 36.44000  ? 42  ILE   A H      1 
ATOM   579  H HA     . ILE   A 1 76  ? -21.49800 8.31600   -17.42200 1.000 38.53000  ? 42  ILE   A HA     1 
ATOM   580  H HB     . ILE   A 1 76  ? -19.57800 8.19500   -18.77400 1.000 38.24000  ? 42  ILE   A HB     1 
ATOM   581  H HG12   . ILE   A 1 76  ? -19.34000 10.58300  -17.28800 1.000 42.53000  ? 42  ILE   A HG12   1 
ATOM   582  H HG13   . ILE   A 1 76  ? -19.41500 9.17300   -16.56200 1.000 42.53000  ? 42  ILE   A HG13   1 
ATOM   583  H HG21   . ILE   A 1 76  ? -18.84300 9.97600   -20.02400 1.000 40.52000  ? 42  ILE   A HG21   1 
ATOM   584  H HG22   . ILE   A 1 76  ? -20.31700 9.61500   -20.49200 1.000 40.52000  ? 42  ILE   A HG22   1 
ATOM   585  H HG23   . ILE   A 1 76  ? -20.06900 10.86100  -19.53800 1.000 40.52000  ? 42  ILE   A HG23   1 
ATOM   586  H HD11   . ILE   A 1 76  ? -17.20200 9.73100   -16.68500 1.000 38.55000  ? 42  ILE   A HD11   1 
ATOM   587  H HD12   . ILE   A 1 76  ? -17.42600 8.55500   -17.72800 1.000 38.55000  ? 42  ILE   A HD12   1 
ATOM   588  H HD13   . ILE   A 1 76  ? -17.32000 10.05600  -18.23600 1.000 38.55000  ? 42  ILE   A HD13   1 
ATOM   589  N N      . THR   A 1 77  ? -21.96600 10.58800  -16.55300 1.000 42.54000  ? 43  THR   A N      1 
ATOM   590  C CA     . THR   A 1 77  ? -22.50900 11.83000  -16.01900 1.000 51.01000  ? 43  THR   A CA     1 
ATOM   591  C C      . THR   A 1 77  ? -21.56600 13.00800  -16.26400 1.000 66.12000  ? 43  THR   A C      1 
ATOM   592  O O      . THR   A 1 77  ? -20.36800 12.84300  -16.52200 1.000 64.13000  ? 43  THR   A O      1 
ATOM   593  C CB     . THR   A 1 77  ? -22.71800 11.71800  -14.51900 1.000 56.40000  ? 43  THR   A CB     1 
ATOM   594  O OG1    . THR   A 1 77  ? -21.42800 11.67500  -13.89200 1.000 57.73000  ? 43  THR   A OG1    1 
ATOM   595  C CG2    . THR   A 1 77  ? -23.49700 10.45400  -14.17700 1.000 47.58000  ? 43  THR   A CG2    1 
ATOM   596  H H      . THR   A 1 77  ? -21.56800 10.10900  -15.95900 1.000 42.54000  ? 43  THR   A H      1 
ATOM   597  H HA     . THR   A 1 77  ? -23.36200 12.02100  -16.43900 1.000 51.01000  ? 43  THR   A HA     1 
ATOM   598  H HB     . THR   A 1 77  ? -23.21400 12.48700  -14.19800 1.000 56.40000  ? 43  THR   A HB     1 
ATOM   599  H HG1    . THR   A 1 77  ? -21.51300 11.74800  -13.06000 1.000 57.73000  ? 43  THR   A HG1    1 
ATOM   600  H HG21   . THR   A 1 77  ? -23.75200 10.46500  -13.24100 1.000 47.58000  ? 43  THR   A HG21   1 
ATOM   601  H HG22   . THR   A 1 77  ? -24.29900 10.40200  -14.72100 1.000 47.58000  ? 43  THR   A HG22   1 
ATOM   602  H HG23   . THR   A 1 77  ? -22.95100 9.67000   -14.34500 1.000 47.58000  ? 43  THR   A HG23   1 
ATOM   603  N N      . LYS   A 1 78  ? -22.11700 14.21500  -16.13800 1.000 67.13000  ? 44  LYS   A N      1 
ATOM   604  C CA     . LYS   A 1 78  ? -21.29400 15.41900  -16.17700 1.000 61.10000  ? 44  LYS   A CA     1 
ATOM   605  C C      . LYS   A 1 78  ? -20.27900 15.40000  -15.04000 1.000 60.41000  ? 44  LYS   A C      1 
ATOM   606  O O      . LYS   A 1 78  ? -20.58200 14.95900  -13.92600 1.000 64.49000  ? 44  LYS   A O      1 
ATOM   607  C CB     . LYS   A 1 78  ? -22.17700 16.66600  -16.07900 1.000 71.89000  ? 44  LYS   A CB     1 
ATOM   608  C CG     . LYS   A 1 78  ? -21.41100 17.96800  -15.85100 1.000 73.74000  ? 44  LYS   A CG     1 
ATOM   609  C CD     . LYS   A 1 78  ? -20.48200 18.28500  -17.01200 1.000 63.69000  ? 44  LYS   A CD     1 
ATOM   610  C CE     . LYS   A 1 78  ? -19.70100 19.57700  -16.77100 1.000 73.10000  ? 44  LYS   A CE     1 
ATOM   611  N NZ     . LYS   A 1 78  ? -19.20200 20.19500  -18.04100 1.000 53.95000  ? 44  LYS   A NZ     1 
ATOM   612  H H      . LYS   A 1 78  ? -22.95800 14.36100  -16.03000 1.000 67.13000  ? 44  LYS   A H      1 
ATOM   613  H HA     . LYS   A 1 78  ? -20.81100 15.45100  -17.01800 1.000 61.10000  ? 44  LYS   A HA     1 
ATOM   614  H HB2    . LYS   A 1 78  ? -22.67500 16.75900  -16.90600 1.000 71.89000  ? 44  LYS   A HB2    1 
ATOM   615  H HB3    . LYS   A 1 78  ? -22.79200 16.55300  -15.33800 1.000 71.89000  ? 44  LYS   A HB3    1 
ATOM   616  H HG2    . LYS   A 1 78  ? -22.04800 18.69600  -15.77400 1.000 73.74000  ? 44  LYS   A HG2    1 
ATOM   617  H HG3    . LYS   A 1 78  ? -20.88200 17.90700  -15.04100 1.000 73.74000  ? 44  LYS   A HG3    1 
ATOM   618  H HD2    . LYS   A 1 78  ? -19.85100 17.56100  -17.14000 1.000 63.69000  ? 44  LYS   A HD2    1 
ATOM   619  H HD3    . LYS   A 1 78  ? -21.01900 18.41300  -17.80800 1.000 63.69000  ? 44  LYS   A HD3    1 
ATOM   620  H HE2    . LYS   A 1 78  ? -20.28000 20.21900  -16.33200 1.000 73.10000  ? 44  LYS   A HE2    1 
ATOM   621  H HE3    . LYS   A 1 78  ? -18.93400 19.38300  -16.21000 1.000 73.10000  ? 44  LYS   A HE3    1 
ATOM   622  H HZ1    . LYS   A 1 78  ? -18.91000 21.02100  -17.88200 1.000 53.95000  ? 44  LYS   A HZ1    1 
ATOM   623  H HZ2    . LYS   A 1 78  ? -18.53300 19.71100  -18.37000 1.000 53.95000  ? 44  LYS   A HZ2    1 
ATOM   624  H HZ3    . LYS   A 1 78  ? -19.85800 20.23100  -18.64100 1.000 53.95000  ? 44  LYS   A HZ3    1 
ATOM   625  N N      . SER   A 1 79  ? -19.06000 15.87200  -15.32700 1.000 63.76000  ? 45  SER   A N      1 
ATOM   626  C CA     . SER   A 1 79  ? -18.02900 15.97400  -14.29300 1.000 63.02000  ? 45  SER   A CA     1 
ATOM   627  C C      . SER   A 1 79  ? -18.51900 16.89600  -13.18400 1.000 67.22000  ? 45  SER   A C      1 
ATOM   628  O O      . SER   A 1 79  ? -18.75400 18.08600  -13.41600 1.000 67.16000  ? 45  SER   A O      1 
ATOM   629  C CB     . SER   A 1 79  ? -16.71100 16.50300  -14.87500 1.000 59.02000  ? 45  SER   A CB     1 
ATOM   630  O OG     . SER   A 1 79  ? -16.02400 15.54100  -15.65500 1.000 47.00000  ? 45  SER   A OG     1 
ATOM   631  H H      . SER   A 1 79  ? -18.80700 16.13300  -16.10600 1.000 63.76000  ? 45  SER   A H      1 
ATOM   632  H HA     . SER   A 1 79  ? -17.86400 15.09800  -13.91700 1.000 63.02000  ? 45  SER   A HA     1 
ATOM   633  H HB2    . SER   A 1 79  ? -16.90700 17.27100  -15.43400 1.000 59.02000  ? 45  SER   A HB2    1 
ATOM   634  H HB3    . SER   A 1 79  ? -16.13600 16.77300  -14.14200 1.000 59.02000  ? 45  SER   A HB3    1 
ATOM   635  H HG     . SER   A 1 79  ? -15.73900 14.92400  -15.16200 1.000 47.00000  ? 45  SER   A HG     1 
ATOM   636  N N      . CYS   A 1 80  ? -18.67700 16.35100  -11.98100 1.000 71.17000  ? 46  CYS   A N      1 
ATOM   637  C CA     . CYS   A 1 80  ? -19.27500 17.09000  -10.88000 1.000 79.36000  ? 46  CYS   A CA     1 
ATOM   638  C C      . CYS   A 1 80  ? -18.22100 17.49000  -9.85400  1.000 76.90000  ? 46  CYS   A C      1 
ATOM   639  O O      . CYS   A 1 80  ? -17.14400 16.89200  -9.75700  1.000 71.57000  ? 46  CYS   A O      1 
ATOM   640  C CB     . CYS   A 1 80  ? -20.39100 16.27600  -10.21000 1.000 78.61000  ? 46  CYS   A CB     1 
ATOM   641  S SG     . CYS   A 1 80  ? -19.88400 14.65200  -9.61600  1.000 73.09000  ? 46  CYS   A SG     1 
ATOM   642  H H      . CYS   A 1 80  ? -18.44300 15.54900  -11.77800 1.000 71.17000  ? 46  CYS   A H      1 
ATOM   643  H HA     . CYS   A 1 80  ? -19.67200 17.90100  -11.22800 1.000 79.36000  ? 46  CYS   A HA     1 
ATOM   644  H HB2    . CYS   A 1 80  ? -20.72900 16.77600  -9.45100  1.000 78.61000  ? 46  CYS   A HB2    1 
ATOM   645  H HB3    . CYS   A 1 80  ? -21.10000 16.14300  -10.85700 1.000 78.61000  ? 46  CYS   A HB3    1 
ATOM   646  H HG     . CYS   A 1 80  ? -19.52600 13.98600  -10.54700 1.000 73.09000  ? 46  CYS   A HG     1 
ATOM   647  N N      . THR   A 1 81  ? -18.54700 18.53100  -9.09900  1.000 79.69000  ? 47  THR   A N      1 
ATOM   648  C CA     . THR   A 1 81  ? -17.73700 19.03400  -8.00500  1.000 84.85000  ? 47  THR   A CA     1 
ATOM   649  C C      . THR   A 1 81  ? -18.54000 18.97600  -6.71100  1.000 89.61000  ? 47  THR   A C      1 
ATOM   650  O O      . THR   A 1 81  ? -19.77700 18.96300  -6.73700  1.000 80.96000  ? 47  THR   A O      1 
ATOM   651  C CB     . THR   A 1 81  ? -17.28100 20.47800  -8.26600  1.000 83.18000  ? 47  THR   A CB     1 
ATOM   652  O OG1    . THR   A 1 81  ? -18.42300 21.30100  -8.53700  1.000 71.80000  ? 47  THR   A OG1    1 
ATOM   653  C CG2    . THR   A 1 81  ? -16.31500 20.53800  -9.45100  1.000 77.81000  ? 47  THR   A CG2    1 
ATOM   654  H H      . THR   A 1 81  ? -19.27100 18.98200  -9.21100  1.000 79.69000  ? 47  THR   A H      1 
ATOM   655  H HA     . THR   A 1 81  ? -16.95000 18.47500  -7.91300  1.000 84.85000  ? 47  THR   A HA     1 
ATOM   656  H HB     . THR   A 1 81  ? -16.82500 20.82700  -7.48600  1.000 83.18000  ? 47  THR   A HB     1 
ATOM   657  H HG1    . THR   A 1 81  ? -18.18000 22.09200  -8.68100  1.000 71.80000  ? 47  THR   A HG1    1 
ATOM   658  H HG21   . THR   A 1 81  ? -16.22000 21.45500  -9.75400  1.000 77.81000  ? 47  THR   A HG21   1 
ATOM   659  H HG22   . THR   A 1 81  ? -15.44600 20.20400  -9.18200  1.000 77.81000  ? 47  THR   A HG22   1 
ATOM   660  H HG23   . THR   A 1 81  ? -16.65100 19.99800  -10.18300 1.000 77.81000  ? 47  THR   A HG23   1 
ATOM   661  N N      . PRO   A 1 82  ? -17.86500 18.93400  -5.55100  1.000 91.24000  ? 48  PRO   A N      1 
ATOM   662  C CA     . PRO   A 1 82  ? -18.53800 18.90800  -4.24700  1.000 87.09000  ? 48  PRO   A CA     1 
ATOM   663  C C      . PRO   A 1 82  ? -19.57200 20.02000  -4.10600  1.000 84.93000  ? 48  PRO   A C      1 
ATOM   664  O O      . PRO   A 1 82  ? -20.73000 19.77700  -4.44500  1.000 88.52000  ? 48  PRO   A O      1 
ATOM   665  C CB     . PRO   A 1 82  ? -17.38700 19.09400  -3.24700  1.000 90.60000  ? 48  PRO   A CB     1 
ATOM   666  C CG     . PRO   A 1 82  ? -16.20700 19.55500  -4.06400  1.000 89.26000  ? 48  PRO   A CG     1 
ATOM   667  C CD     . PRO   A 1 82  ? -16.40000 18.95500  -5.41600  1.000 83.40000  ? 48  PRO   A CD     1 
ATOM   668  H HA     . PRO   A 1 82  ? -18.96200 18.04800  -4.09900  1.000 87.09000  ? 48  PRO   A HA     1 
ATOM   669  H HB2    . PRO   A 1 82  ? -17.63100 19.76600  -2.59100  1.000 90.60000  ? 48  PRO   A HB2    1 
ATOM   670  H HB3    . PRO   A 1 82  ? -17.19300 18.24800  -2.81400  1.000 90.60000  ? 48  PRO   A HB3    1 
ATOM   671  H HG2    . PRO   A 1 82  ? -16.20600 20.52400  -4.11700  1.000 89.26000  ? 48  PRO   A HG2    1 
ATOM   672  H HG3    . PRO   A 1 82  ? -15.38600 19.23300  -3.66100  1.000 89.26000  ? 48  PRO   A HG3    1 
ATOM   673  H HD2    . PRO   A 1 82  ? -15.98400 19.51400  -6.08700  1.000 83.40000  ? 48  PRO   A HD2    1 
ATOM   674  H HD3    . PRO   A 1 82  ? -16.04100 18.05700  -5.43400  1.000 83.40000  ? 48  PRO   A HD3    1 
ATOM   675  N N      . PRO   A 1 91  ? -22.62000 32.86100  -23.60700 1.000 83.64000  ? 57  PRO   A N      1 
ATOM   676  C CA     . PRO   A 1 91  ? -22.23900 31.70500  -24.42600 1.000 79.83000  ? 57  PRO   A CA     1 
ATOM   677  C C      . PRO   A 1 91  ? -20.97200 31.01200  -23.91800 1.000 74.82000  ? 57  PRO   A C      1 
ATOM   678  O O      . PRO   A 1 91  ? -19.89000 31.60800  -23.91400 1.000 66.20000  ? 57  PRO   A O      1 
ATOM   679  C CB     . PRO   A 1 91  ? -22.00900 32.32300  -25.80500 1.000 72.00000  ? 57  PRO   A CB     1 
ATOM   680  C CG     . PRO   A 1 91  ? -21.51500 33.69700  -25.49800 1.000 77.09000  ? 57  PRO   A CG     1 
ATOM   681  C CD     . PRO   A 1 91  ? -22.24800 34.13500  -24.24900 1.000 79.25000  ? 57  PRO   A CD     1 
ATOM   682  H HA     . PRO   A 1 91  ? -22.96600 31.06400  -24.47300 1.000 79.83000  ? 57  PRO   A HA     1 
ATOM   683  H HB2    . PRO   A 1 91  ? -21.34000 31.81400  -26.28900 1.000 72.00000  ? 57  PRO   A HB2    1 
ATOM   684  H HB3    . PRO   A 1 91  ? -22.84500 32.35600  -26.29600 1.000 72.00000  ? 57  PRO   A HB3    1 
ATOM   685  H HG2    . PRO   A 1 91  ? -20.55800 33.67000  -25.33900 1.000 77.09000  ? 57  PRO   A HG2    1 
ATOM   686  H HG3    . PRO   A 1 91  ? -21.72100 34.28900  -26.23900 1.000 77.09000  ? 57  PRO   A HG3    1 
ATOM   687  H HD2    . PRO   A 1 91  ? -21.65800 34.64500  -23.67200 1.000 79.25000  ? 57  PRO   A HD2    1 
ATOM   688  H HD3    . PRO   A 1 91  ? -23.04200 34.64100  -24.48300 1.000 79.25000  ? 57  PRO   A HD3    1 
ATOM   689  N N      . ARG   A 1 92  ? -21.11900 29.76200  -23.47900 1.000 69.26000  ? 58  ARG   A N      1 
ATOM   690  C CA     . ARG   A 1 92  ? -19.99400 28.94100  -23.05600 1.000 73.05000  ? 58  ARG   A CA     1 
ATOM   691  C C      . ARG   A 1 92  ? -19.73500 27.76900  -24.00200 1.000 66.68000  ? 58  ARG   A C      1 
ATOM   692  O O      . ARG   A 1 92  ? -18.79100 27.00500  -23.77900 1.000 58.24000  ? 58  ARG   A O      1 
ATOM   693  C CB     . ARG   A 1 92  ? -20.22500 28.43400  -21.62600 1.000 65.39000  ? 58  ARG   A CB     1 
ATOM   694  H H      . ARG   A 1 92  ? -21.87800 29.36200  -23.41700 1.000 69.26000  ? 58  ARG   A H      1 
ATOM   695  H HA     . ARG   A 1 92  ? -19.19400 29.48900  -23.04500 1.000 73.05000  ? 58  ARG   A HA     1 
ATOM   696  N N      . TYR   A 1 93  ? -20.55200 27.60600  -25.04300 1.000 64.61000  ? 59  TYR   A N      1 
ATOM   697  C CA     . TYR   A 1 93  ? -20.36800 26.62500  -26.10500 1.000 64.53000  ? 59  TYR   A CA     1 
ATOM   698  C C      . TYR   A 1 93  ? -20.45500 27.36800  -27.43400 1.000 65.99000  ? 59  TYR   A C      1 
ATOM   699  O O      . TYR   A 1 93  ? -20.89900 28.51700  -27.49600 1.000 63.33000  ? 59  TYR   A O      1 
ATOM   700  C CB     . TYR   A 1 93  ? -21.42100 25.50100  -26.02200 1.000 56.90000  ? 59  TYR   A CB     1 
ATOM   701  C CG     . TYR   A 1 93  ? -21.32800 24.39900  -27.07800 1.000 52.00000  ? 59  TYR   A CG     1 
ATOM   702  C CD1    . TYR   A 1 93  ? -20.58200 23.24600  -26.84900 1.000 56.36000  ? 59  TYR   A CD1    1 
ATOM   703  C CD2    . TYR   A 1 93  ? -22.01200 24.49800  -28.29200 1.000 54.11000  ? 59  TYR   A CD2    1 
ATOM   704  C CE1    . TYR   A 1 93  ? -20.50300 22.22500  -27.80800 1.000 53.86000  ? 59  TYR   A CE1    1 
ATOM   705  C CE2    . TYR   A 1 93  ? -21.93500 23.48600  -29.26000 1.000 51.48000  ? 59  TYR   A CE2    1 
ATOM   706  C CZ     . TYR   A 1 93  ? -21.17700 22.34900  -29.00700 1.000 59.32000  ? 59  TYR   A CZ     1 
ATOM   707  O OH     . TYR   A 1 93  ? -21.09500 21.33600  -29.94600 1.000 56.59000  ? 59  TYR   A OH     1 
ATOM   708  H H      . TYR   A 1 93  ? -21.25900 28.08100  -25.15800 1.000 64.61000  ? 59  TYR   A H      1 
ATOM   709  H HA     . TYR   A 1 93  ? -19.48600 26.22700  -26.03100 1.000 64.53000  ? 59  TYR   A HA     1 
ATOM   710  H HB2    . TYR   A 1 93  ? -21.34200 25.07500  -25.15400 1.000 56.90000  ? 59  TYR   A HB2    1 
ATOM   711  H HB3    . TYR   A 1 93  ? -22.30000 25.90300  -26.10300 1.000 56.90000  ? 59  TYR   A HB3    1 
ATOM   712  H HD1    . TYR   A 1 93  ? -20.12300 23.15300  -26.04600 1.000 56.36000  ? 59  TYR   A HD1    1 
ATOM   713  H HD2    . TYR   A 1 93  ? -22.51900 25.25800  -28.46800 1.000 54.11000  ? 59  TYR   A HD2    1 
ATOM   714  H HE1    . TYR   A 1 93  ? -19.99400 21.46500  -27.63700 1.000 53.86000  ? 59  TYR   A HE1    1 
ATOM   715  H HE2    . TYR   A 1 93  ? -22.39400 23.57200  -30.06400 1.000 51.48000  ? 59  TYR   A HE2    1 
ATOM   716  H HH     . TYR   A 1 93  ? -20.60800 20.71500  -29.65700 1.000 56.59000  ? 59  TYR   A HH     1 
ATOM   717  N N      . TYR   A 1 94  ? -20.01500 26.72100  -28.51000 1.000 44.70000  ? 60  TYR   A N      1 
ATOM   718  C CA     . TYR   A 1 94  ? -20.15700 27.32200  -29.83000 1.000 55.22000  ? 60  TYR   A CA     1 
ATOM   719  C C      . TYR   A 1 94  ? -19.87800 26.30900  -30.93400 1.000 50.28000  ? 60  TYR   A C      1 
ATOM   720  O O      . TYR   A 1 94  ? -18.83700 25.64300  -30.92400 1.000 44.35000  ? 60  TYR   A O      1 
ATOM   721  C CB     . TYR   A 1 94  ? -19.23000 28.53600  -29.96400 1.000 45.10000  ? 60  TYR   A CB     1 
ATOM   722  C CG     . TYR   A 1 94  ? -19.49200 29.38100  -31.19500 1.000 55.86000  ? 60  TYR   A CG     1 
ATOM   723  C CD1    . TYR   A 1 94  ? -20.45000 30.39700  -31.18000 1.000 60.01000  ? 60  TYR   A CD1    1 
ATOM   724  C CD2    . TYR   A 1 94  ? -18.78100 29.17000  -32.37100 1.000 63.77000  ? 60  TYR   A CD2    1 
ATOM   725  C CE1    . TYR   A 1 94  ? -20.69000 31.18200  -32.31300 1.000 58.20000  ? 60  TYR   A CE1    1 
ATOM   726  C CE2    . TYR   A 1 94  ? -19.01500 29.94500  -33.50700 1.000 61.51000  ? 60  TYR   A CE2    1 
ATOM   727  C CZ     . TYR   A 1 94  ? -19.96900 30.94600  -33.47300 1.000 64.04000  ? 60  TYR   A CZ     1 
ATOM   728  O OH     . TYR   A 1 94  ? -20.19100 31.71100  -34.59900 1.000 67.21000  ? 60  TYR   A OH     1 
ATOM   729  H H      . TYR   A 1 94  ? -19.63800 25.94800  -28.50300 1.000 44.70000  ? 60  TYR   A H      1 
ATOM   730  H HA     . TYR   A 1 94  ? -21.07000 27.63200  -29.93600 1.000 55.22000  ? 60  TYR   A HA     1 
ATOM   731  H HB2    . TYR   A 1 94  ? -19.33800 29.10800  -29.18900 1.000 45.10000  ? 60  TYR   A HB2    1 
ATOM   732  H HB3    . TYR   A 1 94  ? -18.31400 28.22300  -30.01300 1.000 45.10000  ? 60  TYR   A HB3    1 
ATOM   733  H HD1    . TYR   A 1 94  ? -20.93500 30.55600  -30.40300 1.000 60.01000  ? 60  TYR   A HD1    1 
ATOM   734  H HD2    . TYR   A 1 94  ? -18.13900 28.49800  -32.40100 1.000 63.77000  ? 60  TYR   A HD2    1 
ATOM   735  H HE1    . TYR   A 1 94  ? -21.33200 31.85500  -32.28900 1.000 58.20000  ? 60  TYR   A HE1    1 
ATOM   736  H HE2    . TYR   A 1 94  ? -18.53000 29.79000  -34.28500 1.000 61.51000  ? 60  TYR   A HE2    1 
ATOM   737  H HH     . TYR   A 1 94  ? -20.78700 32.28200  -34.44500 1.000 67.21000  ? 60  TYR   A HH     1 
ATOM   738  N N      . THR   A 1 95  ? -20.80300 26.19100  -31.88900 1.000 55.07000  ? 61  THR   A N      1 
ATOM   739  C CA     . THR   A 1 95  ? -20.64500 25.28400  -33.02100 1.000 49.01000  ? 61  THR   A CA     1 
ATOM   740  C C      . THR   A 1 95  ? -19.73300 25.89900  -34.07000 1.000 56.82000  ? 61  THR   A C      1 
ATOM   741  O O      . THR   A 1 95  ? -19.98200 27.01100  -34.54300 1.000 52.60000  ? 61  THR   A O      1 
ATOM   742  C CB     . THR   A 1 95  ? -21.99800 24.96600  -33.65700 1.000 52.23000  ? 61  THR   A CB     1 
ATOM   743  O OG1    . THR   A 1 95  ? -22.79900 24.22800  -32.73200 1.000 51.60000  ? 61  THR   A OG1    1 
ATOM   744  C CG2    . THR   A 1 95  ? -21.81800 24.15000  -34.94800 1.000 54.87000  ? 61  THR   A CG2    1 
ATOM   745  H H      . THR   A 1 95  ? -21.54000 26.63300  -31.90100 1.000 55.07000  ? 61  THR   A H      1 
ATOM   746  H HA     . THR   A 1 95  ? -20.24600 24.45400  -32.71600 1.000 49.01000  ? 61  THR   A HA     1 
ATOM   747  H HB     . THR   A 1 95  ? -22.44900 25.79500  -33.88100 1.000 52.23000  ? 61  THR   A HB     1 
ATOM   748  H HG1    . THR   A 1 95  ? -23.54400 24.05000  -33.07600 1.000 51.60000  ? 61  THR   A HG1    1 
ATOM   749  H HG21   . THR   A 1 95  ? -22.65200 23.71200  -35.17900 1.000 54.87000  ? 61  THR   A HG21   1 
ATOM   750  H HG22   . THR   A 1 95  ? -21.55700 24.73200  -35.67900 1.000 54.87000  ? 61  THR   A HG22   1 
ATOM   751  H HG23   . THR   A 1 95  ? -21.13400 23.47400  -34.82000 1.000 54.87000  ? 61  THR   A HG23   1 
ATOM   752  N N      . LEU   A 1 96  ? -18.69000 25.17500  -34.44400 1.000 47.19000  ? 62  LEU   A N      1 
ATOM   753  C CA     . LEU   A 1 96  ? -17.78500 25.60100  -35.49400 1.000 43.32000  ? 62  LEU   A CA     1 
ATOM   754  C C      . LEU   A 1 96  ? -17.99500 24.76800  -36.75000 1.000 48.21000  ? 62  LEU   A C      1 
ATOM   755  O O      . LEU   A 1 96  ? -18.62000 23.70100  -36.70300 1.000 47.92000  ? 62  LEU   A O      1 
ATOM   756  C CB     . LEU   A 1 96  ? -16.33400 25.46800  -35.02800 1.000 40.61000  ? 62  LEU   A CB     1 
ATOM   757  C CG     . LEU   A 1 96  ? -16.06600 26.18700  -33.70700 1.000 46.12000  ? 62  LEU   A CG     1 
ATOM   758  C CD1    . LEU   A 1 96  ? -14.71100 25.79400  -33.13400 1.000 45.27000  ? 62  LEU   A CD1    1 
ATOM   759  C CD2    . LEU   A 1 96  ? -16.15700 27.68600  -33.95500 1.000 48.05000  ? 62  LEU   A CD2    1 
ATOM   760  H H      . LEU   A 1 96  ? -18.48200 24.41700  -34.09600 1.000 47.19000  ? 62  LEU   A H      1 
ATOM   761  H HA     . LEU   A 1 96  ? -17.95500 26.53000  -35.71200 1.000 43.32000  ? 62  LEU   A HA     1 
ATOM   762  H HB2    . LEU   A 1 96  ? -16.13000 24.52800  -34.90300 1.000 40.61000  ? 62  LEU   A HB2    1 
ATOM   763  H HB3    . LEU   A 1 96  ? -15.74000 25.84800  -35.69000 1.000 40.61000  ? 62  LEU   A HB3    1 
ATOM   764  H HG     . LEU   A 1 96  ? -16.74700 25.94400  -33.06000 1.000 46.12000  ? 62  LEU   A HG     1 
ATOM   765  H HD11   . LEU   A 1 96  ? -14.60300 26.21200  -32.26500 1.000 45.27000  ? 62  LEU   A HD11   1 
ATOM   766  H HD12   . LEU   A 1 96  ? -14.67500 24.82900  -33.04400 1.000 45.27000  ? 62  LEU   A HD12   1 
ATOM   767  H HD13   . LEU   A 1 96  ? -14.01400 26.09600  -33.73700 1.000 45.27000  ? 62  LEU   A HD13   1 
ATOM   768  H HD21   . LEU   A 1 96  ? -15.91600 28.15200  -33.13900 1.000 48.05000  ? 62  LEU   A HD21   1 
ATOM   769  H HD22   . LEU   A 1 96  ? -15.54500 27.92400  -34.66900 1.000 48.05000  ? 62  LEU   A HD22   1 
ATOM   770  H HD23   . LEU   A 1 96  ? -17.06500 27.91300  -34.20800 1.000 48.05000  ? 62  LEU   A HD23   1 
ATOM   771  N N      . PRO   A 1 97  ? -17.47800 25.21700  -37.89400 1.000 56.37000  ? 63  PRO   A N      1 
ATOM   772  C CA     . PRO   A 1 97  ? -17.63200 24.41400  -39.11800 1.000 66.69000  ? 63  PRO   A CA     1 
ATOM   773  C C      . PRO   A 1 97  ? -17.11700 22.98900  -38.94900 1.000 51.06000  ? 63  PRO   A C      1 
ATOM   774  O O      . PRO   A 1 97  ? -17.76100 22.03600  -39.40700 1.000 60.52000  ? 63  PRO   A O      1 
ATOM   775  C CB     . PRO   A 1 97  ? -16.82400 25.20100  -40.16600 1.000 56.16000  ? 63  PRO   A CB     1 
ATOM   776  C CG     . PRO   A 1 97  ? -16.61400 26.56700  -39.58800 1.000 63.03000  ? 63  PRO   A CG     1 
ATOM   777  C CD     . PRO   A 1 97  ? -16.61400 26.39300  -38.09600 1.000 66.94000  ? 63  PRO   A CD     1 
ATOM   778  H HA     . PRO   A 1 97  ? -18.56400 24.38800  -39.38700 1.000 66.69000  ? 63  PRO   A HA     1 
ATOM   779  H HB2    . PRO   A 1 97  ? -15.97300 24.76100  -40.31700 1.000 56.16000  ? 63  PRO   A HB2    1 
ATOM   780  H HB3    . PRO   A 1 97  ? -17.33000 25.25500  -40.99200 1.000 56.16000  ? 63  PRO   A HB3    1 
ATOM   781  H HG2    . PRO   A 1 97  ? -15.76200 26.91900  -39.88900 1.000 63.03000  ? 63  PRO   A HG2    1 
ATOM   782  H HG3    . PRO   A 1 97  ? -17.33900 27.15000  -39.86200 1.000 63.03000  ? 63  PRO   A HG3    1 
ATOM   783  H HD2    . PRO   A 1 97  ? -15.71300 26.21200  -37.78800 1.000 66.94000  ? 63  PRO   A HD2    1 
ATOM   784  H HD3    . PRO   A 1 97  ? -16.99200 27.17500  -37.66400 1.000 66.94000  ? 63  PRO   A HD3    1 
ATOM   785  N N      . LEU   A 1 98  ? -15.99500 22.81400  -38.25100 1.000 47.59000  ? 64  LEU   A N      1 
ATOM   786  C CA     . LEU   A 1 98  ? -15.34700 21.51600  -38.13900 1.000 45.51000  ? 64  LEU   A CA     1 
ATOM   787  C C      . LEU   A 1 98  ? -15.37500 20.95700  -36.71800 1.000 41.08000  ? 64  LEU   A C      1 
ATOM   788  O O      . LEU   A 1 98  ? -14.58600 20.06700  -36.39400 1.000 38.58000  ? 64  LEU   A O      1 
ATOM   789  C CB     . LEU   A 1 98  ? -13.91200 21.62000  -38.64600 1.000 41.27000  ? 64  LEU   A CB     1 
ATOM   790  C CG     . LEU   A 1 98  ? -13.78100 22.15900  -40.07000 1.000 47.61000  ? 64  LEU   A CG     1 
ATOM   791  C CD1    . LEU   A 1 98  ? -12.31200 22.19500  -40.47100 1.000 40.91000  ? 64  LEU   A CD1    1 
ATOM   792  C CD2    . LEU   A 1 98  ? -14.60800 21.32500  -41.04500 1.000 40.17000  ? 64  LEU   A CD2    1 
ATOM   793  H H      . LEU   A 1 98  ? -15.58700 23.44300  -37.82900 1.000 47.59000  ? 64  LEU   A H      1 
ATOM   794  H HA     . LEU   A 1 98  ? -15.81400 20.88200  -38.70400 1.000 45.51000  ? 64  LEU   A HA     1 
ATOM   795  H HB2    . LEU   A 1 98  ? -13.41800 22.21300  -38.06200 1.000 41.27000  ? 64  LEU   A HB2    1 
ATOM   796  H HB3    . LEU   A 1 98  ? -13.51200 20.73700  -38.62800 1.000 41.27000  ? 64  LEU   A HB3    1 
ATOM   797  H HG     . LEU   A 1 98  ? -14.11800 23.06800  -40.09500 1.000 47.61000  ? 64  LEU   A HG     1 
ATOM   798  H HD11   . LEU   A 1 98  ? -12.24100 22.53100  -41.37800 1.000 40.91000  ? 64  LEU   A HD11   1 
ATOM   799  H HD12   . LEU   A 1 98  ? -11.83400 22.78000  -39.86300 1.000 40.91000  ? 64  LEU   A HD12   1 
ATOM   800  H HD13   . LEU   A 1 98  ? -11.94900 21.29800  -40.42100 1.000 40.91000  ? 64  LEU   A HD13   1 
ATOM   801  H HD21   . LEU   A 1 98  ? -14.36800 21.57100  -41.95200 1.000 40.17000  ? 64  LEU   A HD21   1 
ATOM   802  H HD22   . LEU   A 1 98  ? -14.41800 20.38600  -40.89600 1.000 40.17000  ? 64  LEU   A HD22   1 
ATOM   803  H HD23   . LEU   A 1 98  ? -15.55000 21.50000  -40.89300 1.000 40.17000  ? 64  LEU   A HD23   1 
ATOM   804  N N      . GLY   A 1 99  ? -16.25800 21.46200  -35.86100 1.000 39.32000  ? 65  GLY   A N      1 
ATOM   805  C CA     . GLY   A 1 99  ? -16.32300 20.95000  -34.50600 1.000 44.22000  ? 65  GLY   A CA     1 
ATOM   806  C C      . GLY   A 1 99  ? -16.97200 21.88700  -33.50900 1.000 43.91000  ? 65  GLY   A C      1 
ATOM   807  O O      . GLY   A 1 99  ? -18.05500 22.42400  -33.76700 1.000 44.73000  ? 65  GLY   A O      1 
ATOM   808  H H      . GLY   A 1 99  ? -16.81900 22.08900  -36.03800 1.000 39.32000  ? 65  GLY   A H      1 
ATOM   809  H HA2    . GLY   A 1 99  ? -16.82300 20.11900  -34.50600 1.000 44.22000  ? 65  GLY   A HA2    1 
ATOM   810  H HA3    . GLY   A 1 99  ? -15.42400 20.76000  -34.19600 1.000 44.22000  ? 65  GLY   A HA3    1 
ATOM   811  N N      . SER   A 1 100 ? -16.31700 22.08500  -32.36200 1.000 36.85000  ? 66  SER   A N      1 
ATOM   812  C CA     . SER   A 1 100 ? -16.87400 22.88000  -31.27500 1.000 37.14000  ? 66  SER   A CA     1 
ATOM   813  C C      . SER   A 1 100 ? -15.75600 23.51500  -30.45800 1.000 38.24000  ? 66  SER   A C      1 
ATOM   814  O O      . SER   A 1 100 ? -14.59800 23.07700  -30.49400 1.000 35.67000  ? 66  SER   A O      1 
ATOM   815  C CB     . SER   A 1 100 ? -17.76700 22.02800  -30.36200 1.000 40.24000  ? 66  SER   A CB     1 
ATOM   816  O OG     . SER   A 1 100 ? -16.99900 21.07000  -29.65600 1.000 42.99000  ? 66  SER   A OG     1 
ATOM   817  H H      . SER   A 1 100 ? -15.53800 21.76300  -32.19100 1.000 36.85000  ? 66  SER   A H      1 
ATOM   818  H HA     . SER   A 1 100 ? -17.41700 23.59200  -31.64800 1.000 37.14000  ? 66  SER   A HA     1 
ATOM   819  H HB2    . SER   A 1 100 ? -18.21100 22.60800  -29.72400 1.000 40.24000  ? 66  SER   A HB2    1 
ATOM   820  H HB3    . SER   A 1 100 ? -18.42500 21.56700  -30.90500 1.000 40.24000  ? 66  SER   A HB3    1 
ATOM   821  H HG     . SER   A 1 100 ? -16.60800 20.56000  -30.19700 1.000 42.99000  ? 66  SER   A HG     1 
ATOM   822  N N      . ILE   A 1 101 ? -16.12200 24.56800  -29.71700 1.000 35.12000  ? 67  ILE   A N      1 
ATOM   823  C CA     . ILE   A 1 101 ? -15.26700 25.18300  -28.70300 1.000 31.90000  ? 67  ILE   A CA     1 
ATOM   824  C C      . ILE   A 1 101 ? -16.13300 25.44000  -27.47800 1.000 39.65000  ? 67  ILE   A C      1 
ATOM   825  O O      . ILE   A 1 101 ? -17.29800 25.82400  -27.61100 1.000 39.78000  ? 67  ILE   A O      1 
ATOM   826  C CB     . ILE   A 1 101 ? -14.60600 26.49100  -29.20900 1.000 34.81000  ? 67  ILE   A CB     1 
ATOM   827  C CG1    . ILE   A 1 101 ? -13.59600 27.02600  -28.17900 1.000 35.01000  ? 67  ILE   A CG1    1 
ATOM   828  C CG2    . ILE   A 1 101 ? -15.68400 27.53700  -29.57400 1.000 37.29000  ? 67  ILE   A CG2    1 
ATOM   829  C CD1    . ILE   A 1 101 ? -12.63000 28.13000  -28.72800 1.000 33.48000  ? 67  ILE   A CD1    1 
ATOM   830  H H      . ILE   A 1 101 ? -16.88800 24.95300  -29.79000 1.000 35.12000  ? 67  ILE   A H      1 
ATOM   831  H HA     . ILE   A 1 101 ? -14.56500 24.56300  -28.46400 1.000 31.90000  ? 67  ILE   A HA     1 
ATOM   832  H HB     . ILE   A 1 101 ? -14.11500 26.27900  -30.01800 1.000 34.81000  ? 67  ILE   A HB     1 
ATOM   833  H HG12   . ILE   A 1 101 ? -14.08600 27.40700  -27.43400 1.000 35.01000  ? 67  ILE   A HG12   1 
ATOM   834  H HG13   . ILE   A 1 101 ? -13.05100 26.28700  -27.86700 1.000 35.01000  ? 67  ILE   A HG13   1 
ATOM   835  H HG21   . ILE   A 1 101 ? -15.25300 28.30200  -29.98700 1.000 37.29000  ? 67  ILE   A HG21   1 
ATOM   836  H HG22   . ILE   A 1 101 ? -16.31200 27.13800  -30.19500 1.000 37.29000  ? 67  ILE   A HG22   1 
ATOM   837  H HG23   . ILE   A 1 101 ? -16.14600 27.81400  -28.76700 1.000 37.29000  ? 67  ILE   A HG23   1 
ATOM   838  H HD11   . ILE   A 1 101 ? -12.02900 28.40500  -28.01800 1.000 33.48000  ? 67  ILE   A HD11   1 
ATOM   839  H HD12   . ILE   A 1 101 ? -12.12200 27.76400  -29.46900 1.000 33.48000  ? 67  ILE   A HD12   1 
ATOM   840  H HD13   . ILE   A 1 101 ? -13.15600 28.88800  -29.02900 1.000 33.48000  ? 67  ILE   A HD13   1 
ATOM   841  N N      . ASN   A 1 102 ? -15.58300 25.20500  -26.28500 1.000 36.82000  ? 68  ASN   A N      1 
ATOM   842  C CA     . ASN   A 1 102 ? -16.39300 25.38800  -25.08700 1.000 44.46000  ? 68  ASN   A CA     1 
ATOM   843  C C      . ASN   A 1 102 ? -15.54700 25.88800  -23.92700 1.000 43.39000  ? 68  ASN   A C      1 
ATOM   844  O O      . ASN   A 1 102 ? -14.36900 25.54500  -23.79600 1.000 41.72000  ? 68  ASN   A O      1 
ATOM   845  C CB     . ASN   A 1 102 ? -17.09700 24.08800  -24.65500 1.000 43.06000  ? 68  ASN   A CB     1 
ATOM   846  C CG     . ASN   A 1 102 ? -16.17800 23.15800  -23.85400 1.000 47.79000  ? 68  ASN   A CG     1 
ATOM   847  O OD1    . ASN   A 1 102 ? -16.01900 23.31700  -22.64200 1.000 50.35000  ? 68  ASN   A OD1    1 
ATOM   848  N ND2    . ASN   A 1 102 ? -15.57600 22.18600  -24.53200 1.000 43.22000  ? 68  ASN   A ND2    1 
ATOM   849  H H      . ASN   A 1 102 ? -14.77400 24.94900  -26.14700 1.000 36.82000  ? 68  ASN   A H      1 
ATOM   850  H HA     . ASN   A 1 102 ? -17.07600 26.05400  -25.26300 1.000 53.36000  ? 68  ASN   A HA     1 
ATOM   851  H HB2    . ASN   A 1 102 ? -17.85900 24.31100  -24.09700 1.000 51.67000  ? 68  ASN   A HB2    1 
ATOM   852  H HB3    . ASN   A 1 102 ? -17.39200 23.61000  -25.44600 1.000 51.67000  ? 68  ASN   A HB3    1 
ATOM   853  H HD21   . ASN   A 1 102 ? -15.05100 21.63900  -24.12500 1.000 51.86000  ? 68  ASN   A HD21   1 
ATOM   854  H HD22   . ASN   A 1 102 ? -15.71000 22.10400  -25.37700 1.000 51.86000  ? 68  ASN   A HD22   1 
ATOM   855  N N      . SER   A 1 103 ? -16.17500 26.70100  -23.07400 1.000 47.29000  ? 69  SER   A N      1 
ATOM   856  C CA     . SER   A 1 103 ? -15.60700 27.09300  -21.79300 1.000 56.20000  ? 69  SER   A CA     1 
ATOM   857  C C      . SER   A 1 103 ? -16.67500 26.88700  -20.71100 1.000 63.36000  ? 69  SER   A C      1 
ATOM   858  O O      . SER   A 1 103 ? -17.03200 27.80400  -19.97400 1.000 69.48000  ? 69  SER   A O      1 
ATOM   859  C CB     . SER   A 1 103 ? -15.11600 28.53900  -21.81400 1.000 64.25000  ? 69  SER   A CB     1 
ATOM   860  O OG     . SER   A 1 103 ? -14.33400 28.81400  -20.66400 1.000 80.07000  ? 69  SER   A OG     1 
ATOM   861  H H      . SER   A 1 103 ? -16.94900 27.04400  -23.22400 1.000 56.75000  ? 69  SER   A H      1 
ATOM   862  H HA     . SER   A 1 103 ? -14.85300 26.52000  -21.58800 1.000 67.44000  ? 69  SER   A HA     1 
ATOM   863  H HB2    . SER   A 1 103 ? -14.57200 28.67600  -22.60500 1.000 77.10000  ? 69  SER   A HB2    1 
ATOM   864  H HB3    . SER   A 1 103 ? -15.88100 29.13500  -21.82800 1.000 77.10000  ? 69  SER   A HB3    1 
ATOM   865  H HG     . SER   A 1 103 ? -14.06700 29.61000  -20.68200 1.000 96.09000  ? 69  SER   A HG     1 
ATOM   866  N N      . MET   A 1 104 ? -17.18700 25.65200  -20.62200 1.000 65.96000  ? 70  MET   A N      1 
ATOM   867  C CA     . MET   A 1 104 ? -18.22500 25.34100  -19.64000 1.000 82.08000  ? 70  MET   A CA     1 
ATOM   868  C C      . MET   A 1 104 ? -17.81000 25.77400  -18.23500 1.000 84.25000  ? 70  MET   A C      1 
ATOM   869  O O      . MET   A 1 104 ? -18.58200 26.41800  -17.51400 1.000 77.12000  ? 70  MET   A O      1 
ATOM   870  C CB     . MET   A 1 104 ? -18.54000 23.84000  -19.65300 1.000 77.98000  ? 70  MET   A CB     1 
ATOM   871  C CG     . MET   A 1 104 ? -19.29400 23.35100  -20.89000 1.000 75.17000  ? 70  MET   A CG     1 
ATOM   872  S SD     . MET   A 1 104 ? -20.72400 24.36200  -21.36200 1.000 94.69000  ? 70  MET   A SD     1 
ATOM   873  C CE     . MET   A 1 104 ? -22.07100 23.51200  -20.53500 1.000 76.86000  ? 70  MET   A CE     1 
ATOM   874  H H      . MET   A 1 104 ? -16.95100 24.98700  -21.11400 1.000 79.15000  ? 70  MET   A H      1 
ATOM   875  H HA     . MET   A 1 104 ? -19.03100 25.82400  -19.87800 1.000 98.49000  ? 70  MET   A HA     1 
ATOM   876  H HB2    . MET   A 1 104 ? -17.70500 23.34900  -19.60600 1.000 93.58000  ? 70  MET   A HB2    1 
ATOM   877  H HB3    . MET   A 1 104 ? -19.08400 23.63200  -18.87700 1.000 93.58000  ? 70  MET   A HB3    1 
ATOM   878  H HG2    . MET   A 1 104 ? -18.68100 23.34200  -21.64200 1.000 90.20000  ? 70  MET   A HG2    1 
ATOM   879  H HG3    . MET   A 1 104 ? -19.61500 22.45100  -20.72000 1.000 90.20000  ? 70  MET   A HG3    1 
ATOM   880  H HE1    . MET   A 1 104 ? -22.90000 23.98100  -20.71900 1.000 92.23000  ? 70  MET   A HE1    1 
ATOM   881  H HE2    . MET   A 1 104 ? -22.12300 22.60300  -20.87000 1.000 92.23000  ? 70  MET   A HE2    1 
ATOM   882  H HE3    . MET   A 1 104 ? -21.90000 23.50400  -19.58000 1.000 92.23000  ? 70  MET   A HE3    1 
ATOM   883  N N      . GLY   A 1 105 ? -16.59500 25.41600  -17.82800 1.000 83.19000  ? 71  GLY   A N      1 
ATOM   884  C CA     . GLY   A 1 105 ? -16.12200 25.72100  -16.49100 1.000 87.46000  ? 71  GLY   A CA     1 
ATOM   885  C C      . GLY   A 1 105 ? -16.99500 25.08700  -15.42800 1.000 82.33000  ? 71  GLY   A C      1 
ATOM   886  O O      . GLY   A 1 105 ? -16.60200 24.97700  -14.26700 1.000 87.25000  ? 71  GLY   A O      1 
ATOM   887  H H      . GLY   A 1 105 ? -16.02500 24.99300  -18.31400 1.000 99.83000  ? 71  GLY   A H      1 
ATOM   888  H HA2    . GLY   A 1 105 ? -15.21600 25.39200  -16.38400 1.000 104.96000 ? 71  GLY   A HA2    1 
ATOM   889  H HA3    . GLY   A 1 105 ? -16.12100 26.68200  -16.35800 1.000 104.96000 ? 71  GLY   A HA3    1 
ATOM   890  N N      . PRO   A 1 107 ? -19.76400 23.72300  -14.59200 1.000 81.75000  ? 73  PRO   A N      1 
ATOM   891  C CA     . PRO   A 1 107 ? -21.17500 23.90400  -14.24300 1.000 82.06000  ? 73  PRO   A CA     1 
ATOM   892  C C      . PRO   A 1 107 ? -21.88900 22.56300  -14.08300 1.000 88.64000  ? 73  PRO   A C      1 
ATOM   893  O O      . PRO   A 1 107 ? -22.06300 21.82200  -15.05600 1.000 88.47000  ? 73  PRO   A O      1 
ATOM   894  C CB     . PRO   A 1 107 ? -21.73000 24.70200  -15.42900 1.000 76.99000  ? 73  PRO   A CB     1 
ATOM   895  H HA     . PRO   A 1 107 ? -21.26400 24.42300  -13.42800 1.000 82.06000  ? 73  PRO   A HA     1 
ATOM   896  N N      . ASN   A 1 108 ? -22.28900 22.25600  -12.85200 1.000 87.15000  ? 74  ASN   A N      1 
ATOM   897  C CA     . ASN   A 1 108 ? -22.87600 20.95900  -12.54600 1.000 87.69000  ? 74  ASN   A CA     1 
ATOM   898  C C      . ASN   A 1 108 ? -23.77900 21.08800  -11.32600 1.000 87.62000  ? 74  ASN   A C      1 
ATOM   899  O O      . ASN   A 1 108 ? -23.61700 21.98700  -10.49500 1.000 83.67000  ? 74  ASN   A O      1 
ATOM   900  C CB     . ASN   A 1 108 ? -21.79200 19.89900  -12.30600 1.000 79.25000  ? 74  ASN   A CB     1 
ATOM   901  C CG     . ASN   A 1 108 ? -20.95600 20.19200  -11.07200 1.000 82.82000  ? 74  ASN   A CG     1 
ATOM   902  O OD1    . ASN   A 1 108 ? -21.14700 19.58000  -10.02000 1.000 87.38000  ? 74  ASN   A OD1    1 
ATOM   903  N ND2    . ASN   A 1 108 ? -20.03000 21.14100  -11.19400 1.000 86.75000  ? 74  ASN   A ND2    1 
ATOM   904  H H      . ASN   A 1 108 ? -22.23000 22.78400  -12.17600 1.000 87.15000  ? 74  ASN   A H      1 
ATOM   905  H HA     . ASN   A 1 108 ? -23.42000 20.67100  -13.29500 1.000 87.69000  ? 74  ASN   A HA     1 
ATOM   906  H HB2    . ASN   A 1 108 ? -22.21500 19.03500  -12.18400 1.000 79.25000  ? 74  ASN   A HB2    1 
ATOM   907  H HB3    . ASN   A 1 108 ? -21.19800 19.87400  -13.07300 1.000 79.25000  ? 74  ASN   A HB3    1 
ATOM   908  H HD21   . ASN   A 1 108 ? -19.53200 21.34400  -10.52300 1.000 86.75000  ? 74  ASN   A HD21   1 
ATOM   909  H HD22   . ASN   A 1 108 ? -19.92800 21.54800  -11.94500 1.000 86.75000  ? 74  ASN   A HD22   1 
ATOM   910  N N      . LYS   A 1 109 ? -24.73600 20.16300  -11.23100 1.000 90.95000  ? 75  LYS   A N      1 
ATOM   911  C CA     . LYS   A 1 109 ? -25.69600 20.11100  -10.13600 1.000 87.09000  ? 75  LYS   A CA     1 
ATOM   912  C C      . LYS   A 1 109 ? -25.09700 19.55900  -8.84300  1.000 87.54000  ? 75  LYS   A C      1 
ATOM   913  O O      . LYS   A 1 109 ? -25.84400 19.28200  -7.89700  1.000 88.92000  ? 75  LYS   A O      1 
ATOM   914  C CB     . LYS   A 1 109 ? -26.90900 19.27300  -10.55100 1.000 79.04000  ? 75  LYS   A CB     1 
ATOM   915  H H      . LYS   A 1 109 ? -24.84900 19.53700  -11.81000 1.000 90.95000  ? 75  LYS   A H      1 
ATOM   916  H HA     . LYS   A 1 109 ? -26.00800 21.01100  -9.95400  1.000 87.09000  ? 75  LYS   A HA     1 
ATOM   917  N N      . GLY   A 1 110 ? -23.78100 19.39000  -8.77800  1.000 84.16000  ? 76  GLY   A N      1 
ATOM   918  C CA     . GLY   A 1 110 ? -23.12800 18.95400  -7.56300  1.000 84.63000  ? 76  GLY   A CA     1 
ATOM   919  C C      . GLY   A 1 110 ? -22.97400 17.44400  -7.47700  1.000 74.47000  ? 76  GLY   A C      1 
ATOM   920  O O      . GLY   A 1 110 ? -23.68100 16.67200  -8.12200  1.000 79.17000  ? 76  GLY   A O      1 
ATOM   921  H H      . GLY   A 1 110 ? -23.24100 19.52100  -9.43300  1.000 84.16000  ? 76  GLY   A H      1 
ATOM   922  H HA2    . GLY   A 1 110 ? -22.24500 19.35300  -7.51300  1.000 84.63000  ? 76  GLY   A HA2    1 
ATOM   923  H HA3    . GLY   A 1 110 ? -23.64100 19.25300  -6.79600  1.000 84.63000  ? 76  GLY   A HA3    1 
ATOM   924  N N      . PHE   A 1 111 ? -22.02200 17.03000  -6.63900  1.000 75.65000  ? 77  PHE   A N      1 
ATOM   925  C CA     . PHE   A 1 111 ? -21.73600 15.60900  -6.47500  1.000 80.65000  ? 77  PHE   A CA     1 
ATOM   926  C C      . PHE   A 1 111 ? -22.94000 14.85200  -5.92100  1.000 85.84000  ? 77  PHE   A C      1 
ATOM   927  O O      . PHE   A 1 111 ? -23.18800 13.70200  -6.30800  1.000 80.47000  ? 77  PHE   A O      1 
ATOM   928  C CB     . PHE   A 1 111 ? -20.51900 15.42900  -5.56600  1.000 77.94000  ? 77  PHE   A CB     1 
ATOM   929  C CG     . PHE   A 1 111 ? -20.22500 13.99900  -5.21900  1.000 83.57000  ? 77  PHE   A CG     1 
ATOM   930  C CD1    . PHE   A 1 111 ? -19.73100 13.12600  -6.17700  1.000 73.98000  ? 77  PHE   A CD1    1 
ATOM   931  C CD2    . PHE   A 1 111 ? -20.43300 13.52800  -3.93200  1.000 80.78000  ? 77  PHE   A CD2    1 
ATOM   932  C CE1    . PHE   A 1 111 ? -19.45800 11.81200  -5.86100  1.000 78.94000  ? 77  PHE   A CE1    1 
ATOM   933  C CE2    . PHE   A 1 111 ? -20.16000 12.21100  -3.60700  1.000 84.78000  ? 77  PHE   A CE2    1 
ATOM   934  C CZ     . PHE   A 1 111 ? -19.67100 11.35200  -4.57400  1.000 80.03000  ? 77  PHE   A CZ     1 
ATOM   935  H H      . PHE   A 1 111 ? -21.53300 17.54900  -6.15900  1.000 75.65000  ? 77  PHE   A H      1 
ATOM   936  H HA     . PHE   A 1 111 ? -21.52000 15.23000  -7.34100  1.000 80.65000  ? 77  PHE   A HA     1 
ATOM   937  H HB2    . PHE   A 1 111 ? -19.73900 15.79200  -6.01400  1.000 77.94000  ? 77  PHE   A HB2    1 
ATOM   938  H HB3    . PHE   A 1 111 ? -20.67500 15.90900  -4.73700  1.000 77.94000  ? 77  PHE   A HB3    1 
ATOM   939  H HD1    . PHE   A 1 111 ? -19.58600 13.43000  -7.04400  1.000 73.98000  ? 77  PHE   A HD1    1 
ATOM   940  H HD2    . PHE   A 1 111 ? -20.76200 14.10300  -3.28000  1.000 80.78000  ? 77  PHE   A HD2    1 
ATOM   941  H HE1    . PHE   A 1 111 ? -19.12900 11.23600  -6.51200  1.000 78.94000  ? 77  PHE   A HE1    1 
ATOM   942  H HE2    . PHE   A 1 111 ? -20.30500 11.90500  -2.74100  1.000 84.78000  ? 77  PHE   A HE2    1 
ATOM   943  H HZ     . PHE   A 1 111 ? -19.48700 10.46600  -4.36000  1.000 80.03000  ? 77  PHE   A HZ     1 
ATOM   944  N N      . ASP   A 1 112 ? -23.70600 15.48100  -5.01900  1.000 89.45000  ? 78  ASP   A N      1 
ATOM   945  C CA     . ASP   A 1 112 ? -24.80900 14.78100  -4.35800  1.000 88.57000  ? 78  ASP   A CA     1 
ATOM   946  C C      . ASP   A 1 112 ? -25.91600 14.42000  -5.34500  1.000 81.51000  ? 78  ASP   A C      1 
ATOM   947  O O      . ASP   A 1 112 ? -26.56400 13.37400  -5.20600  1.000 81.15000  ? 78  ASP   A O      1 
ATOM   948  C CB     . ASP   A 1 112 ? -25.37400 15.63300  -3.21700  1.000 87.98000  ? 78  ASP   A CB     1 
ATOM   949  C CG     . ASP   A 1 112 ? -24.41100 15.77100  -2.04900  1.000 98.04000  ? 78  ASP   A CG     1 
ATOM   950  O OD1    . ASP   A 1 112 ? -23.49900 14.92500  -1.91100  1.000 94.05000  ? 78  ASP   A OD1    1 
ATOM   951  O OD2    . ASP   A 1 112 ? -24.57600 16.72800  -1.26000  1.000 98.74000  ? 78  ASP   A OD2    1 
ATOM   952  H H      . ASP   A 1 112 ? -23.60800 16.30000  -4.77700  1.000 89.45000  ? 78  ASP   A H      1 
ATOM   953  H HA     . ASP   A 1 112 ? -24.47200 13.95600  -3.97500  1.000 88.57000  ? 78  ASP   A HA     1 
ATOM   954  H HB2    . ASP   A 1 112 ? -25.56700 16.52200  -3.55300  1.000 87.98000  ? 78  ASP   A HB2    1 
ATOM   955  H HB3    . ASP   A 1 112 ? -26.18700 15.22000  -2.88700  1.000 87.98000  ? 78  ASP   A HB3    1 
ATOM   956  N N      . PHE   A 1 113 ? -26.16200 15.28100  -6.33700  1.000 80.04000  ? 79  PHE   A N      1 
ATOM   957  C CA     . PHE   A 1 113 ? -27.18300 14.99500  -7.34400  1.000 80.19000  ? 79  PHE   A CA     1 
ATOM   958  C C      . PHE   A 1 113 ? -26.81200 13.78300  -8.19300  1.000 87.48000  ? 79  PHE   A C      1 
ATOM   959  O O      . PHE   A 1 113 ? -27.67600 12.95700  -8.51600  1.000 80.14000  ? 79  PHE   A O      1 
ATOM   960  C CB     . PHE   A 1 113 ? -27.39600 16.21900  -8.23800  1.000 79.25000  ? 79  PHE   A CB     1 
ATOM   961  C CG     . PHE   A 1 113 ? -28.24400 15.94500  -9.45800  1.000 87.90000  ? 79  PHE   A CG     1 
ATOM   962  C CD1    . PHE   A 1 113 ? -29.62100 15.82300  -9.34800  1.000 81.27000  ? 79  PHE   A CD1    1 
ATOM   963  C CD2    . PHE   A 1 113 ? -27.66300 15.82300  -10.71400 1.000 84.96000  ? 79  PHE   A CD2    1 
ATOM   964  C CE1    . PHE   A 1 113 ? -30.40600 15.57500  -10.46400 1.000 77.71000  ? 79  PHE   A CE1    1 
ATOM   965  C CE2    . PHE   A 1 113 ? -28.44300 15.57500  -11.83600 1.000 86.37000  ? 79  PHE   A CE2    1 
ATOM   966  C CZ     . PHE   A 1 113 ? -29.81700 15.45200  -11.70900 1.000 88.87000  ? 79  PHE   A CZ     1 
ATOM   967  H H      . PHE   A 1 113 ? -25.75500 16.03000  -6.44700  1.000 80.04000  ? 79  PHE   A H      1 
ATOM   968  H HA     . PHE   A 1 113 ? -28.02200 14.80100  -6.89600  1.000 80.19000  ? 79  PHE   A HA     1 
ATOM   969  H HB2    . PHE   A 1 113 ? -27.83700 16.91100  -7.72000  1.000 79.25000  ? 79  PHE   A HB2    1 
ATOM   970  H HB3    . PHE   A 1 113 ? -26.53200 16.53700  -8.54300  1.000 79.25000  ? 79  PHE   A HB3    1 
ATOM   971  H HD1    . PHE   A 1 113 ? -30.02300 15.90400  -8.51300  1.000 81.27000  ? 79  PHE   A HD1    1 
ATOM   972  H HD2    . PHE   A 1 113 ? -26.74100 15.90400  -10.80400 1.000 84.96000  ? 79  PHE   A HD2    1 
ATOM   973  H HE1    . PHE   A 1 113 ? -31.32800 15.49300  -10.37500 1.000 77.71000  ? 79  PHE   A HE1    1 
ATOM   974  H HE2    . PHE   A 1 113 ? -28.04300 15.49300  -12.67200 1.000 86.37000  ? 79  PHE   A HE2    1 
ATOM   975  H HZ     . PHE   A 1 113 ? -30.34200 15.28600  -12.45900 1.000 88.87000  ? 79  PHE   A HZ     1 
ATOM   976  N N      . TYR   A 1 114 ? -25.53600 13.67200  -8.58100  1.000 86.01000  ? 80  TYR   A N      1 
ATOM   977  C CA     . TYR   A 1 114 ? -25.10600 12.56800  -9.43400  1.000 81.62000  ? 80  TYR   A CA     1 
ATOM   978  C C      . TYR   A 1 114 ? -24.88700 11.29800  -8.61900  1.000 77.24000  ? 80  TYR   A C      1 
ATOM   979  O O      . TYR   A 1 114 ? -25.18600 10.19500  -9.09100  1.000 65.05000  ? 80  TYR   A O      1 
ATOM   980  C CB     . TYR   A 1 114 ? -23.84500 12.96300  -10.21400 1.000 77.04000  ? 80  TYR   A CB     1 
ATOM   981  C CG     . TYR   A 1 114 ? -24.09500 14.13700  -11.13200 1.000 76.41000  ? 80  TYR   A CG     1 
ATOM   982  C CD1    . TYR   A 1 114 ? -24.77300 13.96900  -12.33500 1.000 73.66000  ? 80  TYR   A CD1    1 
ATOM   983  C CD2    . TYR   A 1 114 ? -23.69000 15.41900  -10.78000 1.000 79.68000  ? 80  TYR   A CD2    1 
ATOM   984  C CE1    . TYR   A 1 114 ? -25.03000 15.04000  -13.16900 1.000 74.17000  ? 80  TYR   A CE1    1 
ATOM   985  C CE2    . TYR   A 1 114 ? -23.94400 16.49900  -11.61000 1.000 82.64000  ? 80  TYR   A CE2    1 
ATOM   986  C CZ     . TYR   A 1 114 ? -24.61500 16.30200  -12.80400 1.000 82.83000  ? 80  TYR   A CZ     1 
ATOM   987  O OH     . TYR   A 1 114 ? -24.87400 17.36400  -13.64300 1.000 85.99000  ? 80  TYR   A OH     1 
ATOM   988  H H      . TYR   A 1 114 ? -24.90900 14.21900  -8.36400  1.000 86.01000  ? 80  TYR   A H      1 
ATOM   989  H HA     . TYR   A 1 114 ? -25.80500 12.38500  -10.08100 1.000 81.62000  ? 80  TYR   A HA     1 
ATOM   990  H HB2    . TYR   A 1 114 ? -23.14700 13.21200  -9.58800  1.000 77.04000  ? 80  TYR   A HB2    1 
ATOM   991  H HB3    . TYR   A 1 114 ? -23.55600 12.21200  -10.75500 1.000 77.04000  ? 80  TYR   A HB3    1 
ATOM   992  H HD1    . TYR   A 1 114 ? -25.05900 13.11900  -12.58300 1.000 73.66000  ? 80  TYR   A HD1    1 
ATOM   993  H HD2    . TYR   A 1 114 ? -23.24200 15.55300  -9.97700  1.000 79.68000  ? 80  TYR   A HD2    1 
ATOM   994  H HE1    . TYR   A 1 114 ? -25.48000 14.91000  -13.97200 1.000 74.17000  ? 80  TYR   A HE1    1 
ATOM   995  H HE2    . TYR   A 1 114 ? -23.66300 17.35200  -11.36700 1.000 82.64000  ? 80  TYR   A HE2    1 
ATOM   996  H HH     . TYR   A 1 114 ? -25.46900 17.15300  -14.19500 1.000 85.99000  ? 80  TYR   A HH     1 
ATOM   997  N N      . LEU   A 1 115 ? -24.37400 11.43600  -7.39100  1.000 78.17000  ? 81  LEU   A N      1 
ATOM   998  C CA     . LEU   A 1 115 ? -24.31500 10.29300  -6.48500  1.000 76.15000  ? 81  LEU   A CA     1 
ATOM   999  C C      . LEU   A 1 115 ? -25.71100 9.75600   -6.19000  1.000 78.55000  ? 81  LEU   A C      1 
ATOM   1000 O O      . LEU   A 1 115 ? -25.92700 8.53900   -6.17300  1.000 79.04000  ? 81  LEU   A O      1 
ATOM   1001 C CB     . LEU   A 1 115 ? -23.60700 10.67800  -5.18500  1.000 73.01000  ? 81  LEU   A CB     1 
ATOM   1002 C CG     . LEU   A 1 115 ? -23.39400 9.51500   -4.20500  1.000 81.47000  ? 81  LEU   A CG     1 
ATOM   1003 C CD1    . LEU   A 1 115 ? -22.52300 8.42200   -4.82900  1.000 74.18000  ? 81  LEU   A CD1    1 
ATOM   1004 C CD2    . LEU   A 1 115 ? -22.80200 9.99100   -2.88200  1.000 80.57000  ? 81  LEU   A CD2    1 
ATOM   1005 H H      . LEU   A 1 115 ? -24.06000 12.16800  -7.06700  1.000 78.17000  ? 81  LEU   A H      1 
ATOM   1006 H HA     . LEU   A 1 115 ? -23.80600 9.58500   -6.90900  1.000 76.15000  ? 81  LEU   A HA     1 
ATOM   1007 H HB2    . LEU   A 1 115 ? -22.73500 11.04200  -5.40300  1.000 73.01000  ? 81  LEU   A HB2    1 
ATOM   1008 H HB3    . LEU   A 1 115 ? -24.13700 11.35200  -4.73100  1.000 73.01000  ? 81  LEU   A HB3    1 
ATOM   1009 H HG     . LEU   A 1 115 ? -24.25600 9.11800   -4.00600  1.000 81.47000  ? 81  LEU   A HG     1 
ATOM   1010 H HD11   . LEU   A 1 115 ? -22.25400 7.80000   -4.13500  1.000 74.18000  ? 81  LEU   A HD11   1 
ATOM   1011 H HD12   . LEU   A 1 115 ? -23.03600 7.95700   -5.50900  1.000 74.18000  ? 81  LEU   A HD12   1 
ATOM   1012 H HD13   . LEU   A 1 115 ? -21.73900 8.83200   -5.22600  1.000 74.18000  ? 81  LEU   A HD13   1 
ATOM   1013 H HD21   . LEU   A 1 115 ? -22.94700 9.30700   -2.20900  1.000 80.57000  ? 81  LEU   A HD21   1 
ATOM   1014 H HD22   . LEU   A 1 115 ? -21.85200 10.14300  -2.99800  1.000 80.57000  ? 81  LEU   A HD22   1 
ATOM   1015 H HD23   . LEU   A 1 115 ? -23.24200 10.81400  -2.61600  1.000 80.57000  ? 81  LEU   A HD23   1 
ATOM   1016 N N      . ALA   A 1 116 ? -26.67700 10.65200  -5.96400  1.000 77.43000  ? 82  ALA   A N      1 
ATOM   1017 C CA     . ALA   A 1 116 ? -28.05000 10.21500  -5.73300  1.000 77.02000  ? 82  ALA   A CA     1 
ATOM   1018 C C      . ALA   A 1 116 ? -28.62000 9.51600   -6.96300  1.000 83.75000  ? 82  ALA   A C      1 
ATOM   1019 O O      . ALA   A 1 116 ? -29.28200 8.47600   -6.84500  1.000 76.42000  ? 82  ALA   A O      1 
ATOM   1020 C CB     . ALA   A 1 116 ? -28.92000 11.40600  -5.33200  1.000 76.01000  ? 82  ALA   A CB     1 
ATOM   1021 H H      . ALA   A 1 116 ? -26.56300 11.50400  -5.94000  1.000 77.43000  ? 82  ALA   A H      1 
ATOM   1022 H HA     . ALA   A 1 116 ? -28.05800 9.58000   -5.00000  1.000 77.02000  ? 82  ALA   A HA     1 
ATOM   1023 H HB1    . ALA   A 1 116 ? -29.82700 11.09800  -5.18300  1.000 76.01000  ? 82  ALA   A HB1    1 
ATOM   1024 H HB2    . ALA   A 1 116 ? -28.56500 11.79600  -4.51800  1.000 76.01000  ? 82  ALA   A HB2    1 
ATOM   1025 H HB3    . ALA   A 1 116 ? -28.90600 12.06100  -6.04700  1.000 76.01000  ? 82  ALA   A HB3    1 
ATOM   1026 N N      . TYR   A 1 117 ? -28.37300 10.07300  -8.15400  1.000 77.26000  ? 83  TYR   A N      1 
ATOM   1027 C CA     . TYR   A 1 117 ? -28.81300 9.41200   -9.37800  1.000 74.95000  ? 83  TYR   A CA     1 
ATOM   1028 C C      . TYR   A 1 117 ? -28.18700 8.03000   -9.51000  1.000 77.41000  ? 83  TYR   A C      1 
ATOM   1029 O O      . TYR   A 1 117 ? -28.85200 7.07300   -9.92800  1.000 75.29000  ? 83  TYR   A O      1 
ATOM   1030 C CB     . TYR   A 1 117 ? -28.47300 10.26200  -10.60500 1.000 68.98000  ? 83  TYR   A CB     1 
ATOM   1031 C CG     . TYR   A 1 117 ? -28.73700 9.51700   -11.89600 1.000 72.68000  ? 83  TYR   A CG     1 
ATOM   1032 C CD1    . TYR   A 1 117 ? -30.02200 9.42600   -12.41400 1.000 71.78000  ? 83  TYR   A CD1    1 
ATOM   1033 C CD2    . TYR   A 1 117 ? -27.71000 8.86900   -12.57700 1.000 70.23000  ? 83  TYR   A CD2    1 
ATOM   1034 C CE1    . TYR   A 1 117 ? -30.28100 8.72800   -13.58100 1.000 76.81000  ? 83  TYR   A CE1    1 
ATOM   1035 C CE2    . TYR   A 1 117 ? -27.95800 8.16700   -13.74900 1.000 67.10000  ? 83  TYR   A CE2    1 
ATOM   1036 C CZ     . TYR   A 1 117 ? -29.24900 8.10000   -14.24700 1.000 73.56000  ? 83  TYR   A CZ     1 
ATOM   1037 O OH     . TYR   A 1 117 ? -29.51700 7.40700   -15.41000 1.000 62.43000  ? 83  TYR   A OH     1 
ATOM   1038 H H      . TYR   A 1 117 ? -27.96100 10.81800  -8.27500  1.000 77.26000  ? 83  TYR   A H      1 
ATOM   1039 H HA     . TYR   A 1 117 ? -29.77200 9.31400   -9.34000  1.000 74.95000  ? 83  TYR   A HA     1 
ATOM   1040 H HB2    . TYR   A 1 117 ? -29.02000 11.06300  -10.60000 1.000 68.98000  ? 83  TYR   A HB2    1 
ATOM   1041 H HB3    . TYR   A 1 117 ? -27.53300 10.49900  -10.57900 1.000 68.98000  ? 83  TYR   A HB3    1 
ATOM   1042 H HD1    . TYR   A 1 117 ? -30.72300 9.84500   -11.96900 1.000 71.78000  ? 83  TYR   A HD1    1 
ATOM   1043 H HD2    . TYR   A 1 117 ? -26.84300 8.91100   -12.24400 1.000 70.23000  ? 83  TYR   A HD2    1 
ATOM   1044 H HE1    . TYR   A 1 117 ? -31.14800 8.68400   -13.91600 1.000 76.81000  ? 83  TYR   A HE1    1 
ATOM   1045 H HE2    . TYR   A 1 117 ? -27.26100 7.74400   -14.19700 1.000 67.10000  ? 83  TYR   A HE2    1 
ATOM   1046 H HH     . TYR   A 1 117 ? -28.80500 7.27500   -15.83500 1.000 62.43000  ? 83  TYR   A HH     1 
ATOM   1047 N N      . SER   A 1 118 ? -26.90200 7.90700   -9.16700  1.000 69.25000  ? 84  SER   A N      1 
ATOM   1048 C CA     . SER   A 1 118 ? -26.22700 6.61600   -9.24800  1.000 77.36000  ? 84  SER   A CA     1 
ATOM   1049 C C      . SER   A 1 118 ? -26.77700 5.62800   -8.22800  1.000 81.87000  ? 84  SER   A C      1 
ATOM   1050 O O      . SER   A 1 118 ? -26.80900 4.41900   -8.49100  1.000 78.63000  ? 84  SER   A O      1 
ATOM   1051 C CB     . SER   A 1 118 ? -24.72300 6.79900   -9.04000  1.000 72.49000  ? 84  SER   A CB     1 
ATOM   1052 O OG     . SER   A 1 118 ? -24.19500 7.74700   -9.95300  1.000 79.20000  ? 84  SER   A OG     1 
ATOM   1053 H H      . SER   A 1 118 ? -26.40600 8.55100   -8.88700  1.000 69.25000  ? 84  SER   A H      1 
ATOM   1054 H HA     . SER   A 1 118 ? -26.36500 6.24200   -10.13200 1.000 77.36000  ? 84  SER   A HA     1 
ATOM   1055 H HB2    . SER   A 1 118 ? -24.56600 7.11100   -8.13500  1.000 72.49000  ? 84  SER   A HB2    1 
ATOM   1056 H HB3    . SER   A 1 118 ? -24.28000 5.94700   -9.17800  1.000 72.49000  ? 84  SER   A HB3    1 
ATOM   1057 H HG     . SER   A 1 118 ? -24.56200 8.49400   -9.83700  1.000 79.20000  ? 84  SER   A HG     1 
ATOM   1058 N N      . ALA   A 1 119 ? -27.21700 6.12200   -7.06600  1.000 81.45000  ? 85  ALA   A N      1 
ATOM   1059 C CA     . ALA   A 1 119 ? -27.60700 5.24400   -5.96800  1.000 83.56000  ? 85  ALA   A CA     1 
ATOM   1060 C C      . ALA   A 1 119 ? -29.00600 4.66900   -6.15600  1.000 81.62000  ? 85  ALA   A C      1 
ATOM   1061 O O      . ALA   A 1 119 ? -29.22300 3.47800   -5.90800  1.000 76.83000  ? 85  ALA   A O      1 
ATOM   1062 H H      . ALA   A 1 119 ? -27.29700 6.96000   -6.89200  1.000 81.45000  ? 85  ALA   A H      1 
ATOM   1063 N N      . ARG   A 1 120 ? -29.97100 5.48800   -6.60000  1.000 80.40000  ? 86  ARG   A N      1 
ATOM   1064 C CA     . ARG   A 1 120 ? -31.34900 5.00500   -6.61600  1.000 82.87000  ? 86  ARG   A CA     1 
ATOM   1065 C C      . ARG   A 1 120 ? -32.19500 5.51800   -7.78200  1.000 86.31000  ? 86  ARG   A C      1 
ATOM   1066 O O      . ARG   A 1 120 ? -33.42700 5.46600   -7.68700  1.000 92.12000  ? 86  ARG   A O      1 
ATOM   1067 C CB     . ARG   A 1 120 ? -32.04400 5.38000   -5.29500  1.000 82.10000  ? 86  ARG   A CB     1 
ATOM   1068 H H      . ARG   A 1 120 ? -29.85700 6.29200   -6.88400  1.000 80.40000  ? 86  ARG   A H      1 
ATOM   1069 H HA     . ARG   A 1 120 ? -31.34100 4.03700   -6.67600  1.000 82.87000  ? 86  ARG   A HA     1 
ATOM   1070 N N      . HIS   A 1 121 ? -31.59800 5.99600   -8.87800  1.000 85.04000  ? 87  HIS   A N      1 
ATOM   1071 C CA     . HIS   A 1 121 ? -32.38500 6.51000   -9.99700  1.000 76.02000  ? 87  HIS   A CA     1 
ATOM   1072 C C      . HIS   A 1 121 ? -31.97300 5.99000   -11.36400 1.000 74.47000  ? 87  HIS   A C      1 
ATOM   1073 O O      . HIS   A 1 121 ? -32.72600 6.18600   -12.32400 1.000 75.94000  ? 87  HIS   A O      1 
ATOM   1074 C CB     . HIS   A 1 121 ? -32.34400 8.04500   -10.02700 1.000 77.08000  ? 87  HIS   A CB     1 
ATOM   1075 C CG     . HIS   A 1 121 ? -33.22100 8.68600   -8.99800  1.000 88.22000  ? 87  HIS   A CG     1 
ATOM   1076 N ND1    . HIS   A 1 121 ? -32.76000 9.63700   -8.11400  1.000 84.71000  ? 87  HIS   A ND1    1 
ATOM   1077 C CD2    . HIS   A 1 121 ? -34.53200 8.50800   -8.71000  1.000 86.88000  ? 87  HIS   A CD2    1 
ATOM   1078 C CE1    . HIS   A 1 121 ? -33.75000 10.02000  -7.32700  1.000 91.61000  ? 87  HIS   A CE1    1 
ATOM   1079 N NE2    . HIS   A 1 121 ? -34.83700 9.35100   -7.66900  1.000 92.23000  ? 87  HIS   A NE2    1 
ATOM   1080 H H      . HIS   A 1 121 ? -30.74700 6.03300   -8.99600  1.000 85.04000  ? 87  HIS   A H      1 
ATOM   1081 H HA     . HIS   A 1 121 ? -33.31000 6.25100   -9.86800  1.000 76.02000  ? 87  HIS   A HA     1 
ATOM   1082 H HB2    . HIS   A 1 121 ? -31.43700 8.33000   -9.87000  1.000 77.08000  ? 87  HIS   A HB2    1 
ATOM   1083 H HB3    . HIS   A 1 121 ? -32.63800 8.34900   -10.90000 1.000 77.08000  ? 87  HIS   A HB3    1 
ATOM   1084 H HD2    . HIS   A 1 121 ? -35.11700 7.92700   -9.13900  1.000 86.88000  ? 87  HIS   A HD2    1 
ATOM   1085 H HE1    . HIS   A 1 121 ? -33.69200 10.65300  -6.64900  1.000 91.61000  ? 87  HIS   A HE1    1 
ATOM   1086 H HE2    . HIS   A 1 121 ? -35.60900 9.42900   -7.29800  1.000 92.23000  ? 87  HIS   A HE2    1 
ATOM   1087 N N      . HIS   A 1 122 ? -30.82600 5.33300   -11.49200 1.000 77.76000  ? 88  HIS   A N      1 
ATOM   1088 C CA     . HIS   A 1 122 ? -30.38200 4.80400   -12.77400 1.000 73.71000  ? 88  HIS   A CA     1 
ATOM   1089 C C      . HIS   A 1 122 ? -30.77400 3.33800   -12.91900 1.000 75.09000  ? 88  HIS   A C      1 
ATOM   1090 O O      . HIS   A 1 122 ? -30.45700 2.51500   -12.05000 1.000 69.71000  ? 88  HIS   A O      1 
ATOM   1091 C CB     . HIS   A 1 122 ? -28.87000 4.93400   -12.94900 1.000 70.76000  ? 88  HIS   A CB     1 
ATOM   1092 C CG     . HIS   A 1 122 ? -28.38900 4.34500   -14.23400 1.000 60.45000  ? 88  HIS   A CG     1 
ATOM   1093 N ND1    . HIS   A 1 122 ? -28.65500 4.92600   -15.45500 1.000 56.38000  ? 88  HIS   A ND1    1 
ATOM   1094 C CD2    . HIS   A 1 122 ? -27.72500 3.19600   -14.49800 1.000 55.33000  ? 88  HIS   A CD2    1 
ATOM   1095 C CE1    . HIS   A 1 122 ? -28.14600 4.17600   -16.41500 1.000 62.90000  ? 88  HIS   A CE1    1 
ATOM   1096 N NE2    . HIS   A 1 122 ? -27.57900 3.11800   -15.86200 1.000 64.74000  ? 88  HIS   A NE2    1 
ATOM   1097 H H      . HIS   A 1 122 ? -30.28200 5.17900   -10.84400 1.000 77.76000  ? 88  HIS   A H      1 
ATOM   1098 H HA     . HIS   A 1 122 ? -30.80900 5.30100   -13.48900 1.000 73.71000  ? 88  HIS   A HA     1 
ATOM   1099 H HB2    . HIS   A 1 122 ? -28.62100 5.86300   -12.91600 1.000 70.76000  ? 88  HIS   A HB2    1 
ATOM   1100 H HB3    . HIS   A 1 122 ? -28.43400 4.45600   -12.22700 1.000 70.76000  ? 88  HIS   A HB3    1 
ATOM   1101 H HD2    . HIS   A 1 122 ? -27.41600 2.58100   -13.87300 1.000 55.33000  ? 88  HIS   A HD2    1 
ATOM   1102 H HE1    . HIS   A 1 122 ? -28.18200 4.36000   -17.32600 1.000 62.90000  ? 88  HIS   A HE1    1 
ATOM   1103 H HE2    . HIS   A 1 122 ? -27.17600 2.48800   -16.28600 1.000 64.74000  ? 88  HIS   A HE2    1 
ATOM   1104 N N      . ASP   A 1 123 ? -31.42700 3.01000   -14.03400 1.000 70.87000  ? 89  ASP   A N      1 
ATOM   1105 C CA     . ASP   A 1 123 ? -31.77700 1.62600   -14.35600 1.000 72.14000  ? 89  ASP   A CA     1 
ATOM   1106 C C      . ASP   A 1 123 ? -30.53800 0.90200   -14.88000 1.000 67.04000  ? 89  ASP   A C      1 
ATOM   1107 O O      . ASP   A 1 123 ? -30.19400 1.00800   -16.06000 1.000 68.60000  ? 89  ASP   A O      1 
ATOM   1108 C CB     . ASP   A 1 123 ? -32.91200 1.58600   -15.37300 1.000 71.92000  ? 89  ASP   A CB     1 
ATOM   1109 C CG     . ASP   A 1 123 ? -33.34600 0.16700   -15.70900 1.000 78.90000  ? 89  ASP   A CG     1 
ATOM   1110 O OD1    . ASP   A 1 123 ? -32.95700 -0.76800  -14.97500 1.000 78.08000  ? 89  ASP   A OD1    1 
ATOM   1111 O OD2    . ASP   A 1 123 ? -34.07000 -0.01600  -16.71200 1.000 84.72000  ? 89  ASP   A OD2    1 
ATOM   1112 H H      . ASP   A 1 123 ? -31.68100 3.57800   -14.62700 1.000 70.87000  ? 89  ASP   A H      1 
ATOM   1113 H HA     . ASP   A 1 123 ? -32.07500 1.17500   -13.55000 1.000 72.14000  ? 89  ASP   A HA     1 
ATOM   1114 H HB2    . ASP   A 1 123 ? -33.67900 2.05700   -15.01000 1.000 71.92000  ? 89  ASP   A HB2    1 
ATOM   1115 H HB3    . ASP   A 1 123 ? -32.61700 2.01200   -16.19300 1.000 71.92000  ? 89  ASP   A HB3    1 
ATOM   1116 N N      . TYR   A 1 124 ? -29.87200 0.14200   -14.00000 1.000 66.67000  ? 90  TYR   A N      1 
ATOM   1117 C CA     . TYR   A 1 124 ? -28.67900 -0.61100  -14.38600 1.000 63.78000  ? 90  TYR   A CA     1 
ATOM   1118 C C      . TYR   A 1 124 ? -29.00100 -1.82800  -15.24200 1.000 71.14000  ? 90  TYR   A C      1 
ATOM   1119 O O      . TYR   A 1 124 ? -28.09500 -2.37600  -15.88200 1.000 64.86000  ? 90  TYR   A O      1 
ATOM   1120 C CB     . TYR   A 1 124 ? -27.90100 -1.04800  -13.14100 1.000 69.43000  ? 90  TYR   A CB     1 
ATOM   1121 C CG     . TYR   A 1 124 ? -27.22900 0.10500   -12.43800 1.000 71.68000  ? 90  TYR   A CG     1 
ATOM   1122 C CD1    . TYR   A 1 124 ? -27.94600 0.92500   -11.57700 1.000 70.98000  ? 90  TYR   A CD1    1 
ATOM   1123 C CD2    . TYR   A 1 124 ? -25.88300 0.38900   -12.65100 1.000 63.42000  ? 90  TYR   A CD2    1 
ATOM   1124 C CE1    . TYR   A 1 124 ? -27.34500 1.99200   -10.93900 1.000 74.60000  ? 90  TYR   A CE1    1 
ATOM   1125 C CE2    . TYR   A 1 124 ? -25.27000 1.45800   -12.01700 1.000 64.35000  ? 90  TYR   A CE2    1 
ATOM   1126 C CZ     . TYR   A 1 124 ? -26.01000 2.25600   -11.16000 1.000 69.97000  ? 90  TYR   A CZ     1 
ATOM   1127 O OH     . TYR   A 1 124 ? -25.42900 3.32100   -10.51500 1.000 67.47000  ? 90  TYR   A OH     1 
ATOM   1128 H H      . TYR   A 1 124 ? -30.09400 0.04800   -13.17400 1.000 66.67000  ? 90  TYR   A H      1 
ATOM   1129 H HA     . TYR   A 1 124 ? -28.10100 -0.03100  -14.90600 1.000 63.78000  ? 90  TYR   A HA     1 
ATOM   1130 H HB2    . TYR   A 1 124 ? -28.51400 -1.46400  -12.51500 1.000 69.43000  ? 90  TYR   A HB2    1 
ATOM   1131 H HB3    . TYR   A 1 124 ? -27.21400 -1.68100  -13.40400 1.000 69.43000  ? 90  TYR   A HB3    1 
ATOM   1132 H HD1    . TYR   A 1 124 ? -28.84700 0.75200   -11.42700 1.000 70.98000  ? 90  TYR   A HD1    1 
ATOM   1133 H HD2    . TYR   A 1 124 ? -25.38800 -0.14600  -13.22800 1.000 63.42000  ? 90  TYR   A HD2    1 
ATOM   1134 H HE1    . TYR   A 1 124 ? -27.83800 2.53000   -10.36300 1.000 74.60000  ? 90  TYR   A HE1    1 
ATOM   1135 H HE2    . TYR   A 1 124 ? -24.36900 1.63700   -12.16400 1.000 64.35000  ? 90  TYR   A HE2    1 
ATOM   1136 H HH     . TYR   A 1 124 ? -25.99600 3.70800   -10.03100 1.000 67.47000  ? 90  TYR   A HH     1 
ATOM   1137 N N      . SER   A 1 125 ? -30.26000 -2.27700  -15.25800 1.000 75.37000  ? 91  SER   A N      1 
ATOM   1138 C CA     . SER   A 1 125 ? -30.64200 -3.34800  -16.16700 1.000 77.89000  ? 91  SER   A CA     1 
ATOM   1139 C C      . SER   A 1 125 ? -30.63000 -2.88700  -17.62200 1.000 77.25000  ? 91  SER   A C      1 
ATOM   1140 O O      . SER   A 1 125 ? -30.55600 -3.73200  -18.52100 1.000 75.29000  ? 91  SER   A O      1 
ATOM   1141 C CB     . SER   A 1 125 ? -32.01900 -3.90800  -15.78800 1.000 71.47000  ? 91  SER   A CB     1 
ATOM   1142 O OG     . SER   A 1 125 ? -33.07300 -3.07400  -16.24000 1.000 76.73000  ? 91  SER   A OG     1 
ATOM   1143 H H      . SER   A 1 125 ? -30.89700 -1.98200  -14.76100 1.000 75.37000  ? 91  SER   A H      1 
ATOM   1144 H HA     . SER   A 1 125 ? -29.99900 -4.06900  -16.08300 1.000 77.89000  ? 91  SER   A HA     1 
ATOM   1145 H HB2    . SER   A 1 125 ? -32.12100 -4.78500  -16.19000 1.000 71.47000  ? 91  SER   A HB2    1 
ATOM   1146 H HB3    . SER   A 1 125 ? -32.07100 -3.98100  -14.82200 1.000 71.47000  ? 91  SER   A HB3    1 
ATOM   1147 H HG     . SER   A 1 125 ? -33.03900 -2.33300  -15.84800 1.000 76.73000  ? 91  SER   A HG     1 
ATOM   1148 N N      . ARG   A 1 126 ? -30.68000 -1.57000  -17.87400 1.000 69.15000  ? 92  ARG   A N      1 
ATOM   1149 C CA     . ARG   A 1 126 ? -30.57400 -1.06000  -19.24100 1.000 68.98000  ? 92  ARG   A CA     1 
ATOM   1150 C C      . ARG   A 1 126 ? -29.12300 -1.04400  -19.72500 1.000 66.89000  ? 92  ARG   A C      1 
ATOM   1151 O O      . ARG   A 1 126 ? -28.82600 -1.53200  -20.82300 1.000 61.50000  ? 92  ARG   A O      1 
ATOM   1152 C CB     . ARG   A 1 126 ? -31.18600 0.34200   -19.33700 1.000 74.07000  ? 92  ARG   A CB     1 
ATOM   1153 C CG     . ARG   A 1 126 ? -32.48300 0.41600   -20.14000 1.000 73.38000  ? 92  ARG   A CG     1 
ATOM   1154 H H      . ARG   A 1 126 ? -30.77300 -0.96100  -17.27400 1.000 69.15000  ? 92  ARG   A H      1 
ATOM   1155 H HA     . ARG   A 1 126 ? -31.07600 -1.64300  -19.83100 1.000 68.98000  ? 92  ARG   A HA     1 
ATOM   1156 H HB2    . ARG   A 1 126 ? -31.37700 0.66100   -18.44100 1.000 74.07000  ? 92  ARG   A HB2    1 
ATOM   1157 H HB3    . ARG   A 1 126 ? -30.54400 0.93100   -19.76300 1.000 74.07000  ? 92  ARG   A HB3    1 
ATOM   1158 N N      . LYS   A 1 127 ? -28.19900 -0.48500  -18.91300 1.000 69.24000  ? 93  LYS   A N      1 
ATOM   1159 C CA     . LYS   A 1 127 ? -26.78400 -0.35900  -19.27100 1.000 56.91000  ? 93  LYS   A CA     1 
ATOM   1160 C C      . LYS   A 1 127 ? -25.93700 0.10100   -18.08600 1.000 52.70000  ? 93  LYS   A C      1 
ATOM   1161 O O      . LYS   A 1 127 ? -26.45100 0.76500   -17.17200 1.000 52.96000  ? 93  LYS   A O      1 
ATOM   1162 C CB     . LYS   A 1 127 ? -26.61600 0.62200   -20.43600 1.000 48.42000  ? 93  LYS   A CB     1 
ATOM   1163 C CG     . LYS   A 1 127 ? -26.96700 2.05400   -20.08800 1.000 52.18000  ? 93  LYS   A CG     1 
ATOM   1164 C CD     . LYS   A 1 127 ? -27.03100 2.91700   -21.33900 1.000 53.05000  ? 93  LYS   A CD     1 
ATOM   1165 C CE     . LYS   A 1 127 ? -28.14100 2.47600   -22.28700 1.000 43.02000  ? 93  LYS   A CE     1 
ATOM   1166 N NZ     . LYS   A 1 127 ? -28.30900 3.44400   -23.42700 1.000 48.20000  ? 93  LYS   A NZ     1 
ATOM   1167 H H      . LYS   A 1 127 ? -28.38100 -0.16700  -18.13500 1.000 69.24000  ? 93  LYS   A H      1 
ATOM   1168 H HA     . LYS   A 1 127 ? -26.47000 -1.22700  -19.56400 1.000 56.91000  ? 93  LYS   A HA     1 
ATOM   1169 H HB2    . LYS   A 1 127 ? -25.69000 0.60700   -20.72400 1.000 48.42000  ? 93  LYS   A HB2    1 
ATOM   1170 H HB3    . LYS   A 1 127 ? -27.18800 0.32700   -21.15900 1.000 48.42000  ? 93  LYS   A HB3    1 
ATOM   1171 H HG2    . LYS   A 1 127 ? -27.83500 2.07700   -19.65600 1.000 52.18000  ? 93  LYS   A HG2    1 
ATOM   1172 H HG3    . LYS   A 1 127 ? -26.28700 2.42000   -19.50100 1.000 52.18000  ? 93  LYS   A HG3    1 
ATOM   1173 H HD2    . LYS   A 1 127 ? -27.20400 3.83600   -21.08300 1.000 53.05000  ? 93  LYS   A HD2    1 
ATOM   1174 H HD3    . LYS   A 1 127 ? -26.18700 2.85500   -21.81200 1.000 53.05000  ? 93  LYS   A HD3    1 
ATOM   1175 H HE2    . LYS   A 1 127 ? -27.92200 1.61200   -22.66800 1.000 43.02000  ? 93  LYS   A HE2    1 
ATOM   1176 H HE3    . LYS   A 1 127 ? -28.97900 2.42800   -21.80100 1.000 43.02000  ? 93  LYS   A HE3    1 
ATOM   1177 H HZ1    . LYS   A 1 127 ? -28.96100 3.16800   -23.96700 1.000 48.20000  ? 93  LYS   A HZ1    1 
ATOM   1178 H HZ2    . LYS   A 1 127 ? -28.51600 4.25100   -23.11300 1.000 48.20000  ? 93  LYS   A HZ2    1 
ATOM   1179 H HZ3    . LYS   A 1 127 ? -27.55200 3.50000   -23.89200 1.000 48.20000  ? 93  LYS   A HZ3    1 
ATOM   1180 N N      . PRO   A 1 128 ? -24.64200 -0.22000  -18.06800 1.000 47.72000  ? 94  PRO   A N      1 
ATOM   1181 C CA     . PRO   A 1 128 ? -23.77600 0.27400   -16.99100 1.000 50.29000  ? 94  PRO   A CA     1 
ATOM   1182 C C      . PRO   A 1 128 ? -23.63000 1.78900   -17.04700 1.000 51.82000  ? 94  PRO   A C      1 
ATOM   1183 O O      . PRO   A 1 128 ? -23.86400 2.43200   -18.07600 1.000 49.29000  ? 94  PRO   A O      1 
ATOM   1184 C CB     . PRO   A 1 128 ? -22.43600 -0.43100  -17.24500 1.000 43.57000  ? 94  PRO   A CB     1 
ATOM   1185 C CG     . PRO   A 1 128 ? -22.76000 -1.59400  -18.12200 1.000 40.09000  ? 94  PRO   A CG     1 
ATOM   1186 C CD     . PRO   A 1 128 ? -23.93500 -1.15700  -18.95800 1.000 47.29000  ? 94  PRO   A CD     1 
ATOM   1187 H HA     . PRO   A 1 128 ? -24.12400 0.01100   -16.12500 1.000 50.29000  ? 94  PRO   A HA     1 
ATOM   1188 H HB2    . PRO   A 1 128 ? -21.82800 0.17700   -17.69400 1.000 43.57000  ? 94  PRO   A HB2    1 
ATOM   1189 H HB3    . PRO   A 1 128 ? -22.06100 -0.73200  -16.40300 1.000 43.57000  ? 94  PRO   A HB3    1 
ATOM   1190 H HG2    . PRO   A 1 128 ? -21.99800 -1.80200  -18.68500 1.000 40.09000  ? 94  PRO   A HG2    1 
ATOM   1191 H HG3    . PRO   A 1 128 ? -22.99700 -2.35800  -17.57400 1.000 40.09000  ? 94  PRO   A HG3    1 
ATOM   1192 H HD2    . PRO   A 1 128 ? -23.63200 -0.70200  -19.75900 1.000 47.29000  ? 94  PRO   A HD2    1 
ATOM   1193 H HD3    . PRO   A 1 128 ? -24.49200 -1.92200  -19.16900 1.000 47.29000  ? 94  PRO   A HD3    1 
ATOM   1194 N N      . LEU   A 1 129 ? -23.24900 2.35400   -15.89800 1.000 45.26000  ? 95  LEU   A N      1 
ATOM   1195 C CA     . LEU   A 1 129 ? -23.17700 3.79400   -15.68800 1.000 44.40000  ? 95  LEU   A CA     1 
ATOM   1196 C C      . LEU   A 1 129 ? -21.79900 4.18300   -15.16900 1.000 49.64000  ? 95  LEU   A C      1 
ATOM   1197 O O      . LEU   A 1 129 ? -21.27900 3.54400   -14.25100 1.000 46.04000  ? 95  LEU   A O      1 
ATOM   1198 C CB     . LEU   A 1 129 ? -24.24900 4.25700   -14.69100 1.000 50.90000  ? 95  LEU   A CB     1 
ATOM   1199 C CG     . LEU   A 1 129 ? -24.10000 5.70700   -14.23200 1.000 49.83000  ? 95  LEU   A CG     1 
ATOM   1200 C CD1    . LEU   A 1 129 ? -24.63100 6.68100   -15.30500 1.000 44.37000  ? 95  LEU   A CD1    1 
ATOM   1201 C CD2    . LEU   A 1 129 ? -24.77600 5.94400   -12.88300 1.000 59.39000  ? 95  LEU   A CD2    1 
ATOM   1202 H H      . LEU   A 1 129 ? -23.02000 1.90200   -15.20300 1.000 45.26000  ? 95  LEU   A H      1 
ATOM   1203 H HA     . LEU   A 1 129 ? -23.32600 4.25100   -16.53000 1.000 44.40000  ? 95  LEU   A HA     1 
ATOM   1204 H HB2    . LEU   A 1 129 ? -25.12000 4.16900   -15.10900 1.000 50.90000  ? 95  LEU   A HB2    1 
ATOM   1205 H HB3    . LEU   A 1 129 ? -24.20500 3.69200   -13.90300 1.000 50.90000  ? 95  LEU   A HB3    1 
ATOM   1206 H HG     . LEU   A 1 129 ? -23.16600 5.92000   -14.10000 1.000 49.83000  ? 95  LEU   A HG     1 
ATOM   1207 H HD11   . LEU   A 1 129 ? -24.52400 7.59100   -14.98600 1.000 44.37000  ? 95  LEU   A HD11   1 
ATOM   1208 H HD12   . LEU   A 1 129 ? -24.12500 6.55500   -16.12300 1.000 44.37000  ? 95  LEU   A HD12   1 
ATOM   1209 H HD13   . LEU   A 1 129 ? -25.56900 6.49400   -15.46400 1.000 44.37000  ? 95  LEU   A HD13   1 
ATOM   1210 H HD21   . LEU   A 1 129 ? -24.66100 6.87400   -12.63200 1.000 59.39000  ? 95  LEU   A HD21   1 
ATOM   1211 H HD22   . LEU   A 1 129 ? -25.72000 5.73700   -12.96300 1.000 59.39000  ? 95  LEU   A HD22   1 
ATOM   1212 H HD23   . LEU   A 1 129 ? -24.36500 5.36800   -12.21900 1.000 59.39000  ? 95  LEU   A HD23   1 
ATOM   1213 N N      . PHE   A 1 130 ? -21.22300 5.23700   -15.75200 1.000 41.79000  ? 96  PHE   A N      1 
ATOM   1214 C CA     . PHE   A 1 130 ? -19.99500 5.87100   -15.29400 1.000 42.24000  ? 96  PHE   A CA     1 
ATOM   1215 C C      . PHE   A 1 130 ? -20.32600 7.22000   -14.67100 1.000 40.05000  ? 96  PHE   A C      1 
ATOM   1216 O O      . PHE   A 1 130 ? -21.27300 7.89600   -15.08200 1.000 49.22000  ? 96  PHE   A O      1 
ATOM   1217 C CB     . PHE   A 1 130 ? -19.00300 6.10700   -16.44400 1.000 39.51000  ? 96  PHE   A CB     1 
ATOM   1218 C CG     . PHE   A 1 130 ? -18.46800 4.85700   -17.06800 1.000 41.09000  ? 96  PHE   A CG     1 
ATOM   1219 C CD1    . PHE   A 1 130 ? -19.19800 4.17700   -18.01500 1.000 40.08000  ? 96  PHE   A CD1    1 
ATOM   1220 C CD2    . PHE   A 1 130 ? -17.21100 4.38800   -16.73400 1.000 38.13000  ? 96  PHE   A CD2    1 
ATOM   1221 C CE1    . PHE   A 1 130 ? -18.69700 3.03000   -18.60100 1.000 41.68000  ? 96  PHE   A CE1    1 
ATOM   1222 C CE2    . PHE   A 1 130 ? -16.70300 3.23700   -17.31300 1.000 39.09000  ? 96  PHE   A CE2    1 
ATOM   1223 C CZ     . PHE   A 1 130 ? -17.44500 2.55900   -18.24700 1.000 42.37000  ? 96  PHE   A CZ     1 
ATOM   1224 H H      . PHE   A 1 130 ? -21.54800 5.61700   -16.45100 1.000 41.79000  ? 96  PHE   A H      1 
ATOM   1225 H HA     . PHE   A 1 130 ? -19.57600 5.30900   -14.62800 1.000 42.24000  ? 96  PHE   A HA     1 
ATOM   1226 H HB2    . PHE   A 1 130 ? -19.45000 6.61400   -17.13900 1.000 39.51000  ? 96  PHE   A HB2    1 
ATOM   1227 H HB3    . PHE   A 1 130 ? -18.24800 6.61300   -16.10400 1.000 39.51000  ? 96  PHE   A HB3    1 
ATOM   1228 H HD1    . PHE   A 1 130 ? -20.04200 4.48500   -18.25500 1.000 40.08000  ? 96  PHE   A HD1    1 
ATOM   1229 H HD2    . PHE   A 1 130 ? -16.70700 4.84200   -16.09800 1.000 38.13000  ? 96  PHE   A HD2    1 
ATOM   1230 H HE1    . PHE   A 1 130 ? -19.20300 2.57300   -19.23300 1.000 41.68000  ? 96  PHE   A HE1    1 
ATOM   1231 H HE2    . PHE   A 1 130 ? -15.86000 2.92700   -17.07300 1.000 39.09000  ? 96  PHE   A HE2    1 
ATOM   1232 H HZ     . PHE   A 1 130 ? -17.10700 1.78800   -18.64200 1.000 42.37000  ? 96  PHE   A HZ     1 
ATOM   1233 N N      . ILE   A 1 131 ? -19.53000 7.62600   -13.69100 1.000 41.95000  ? 97  ILE   A N      1 
ATOM   1234 C CA     . ILE   A 1 131 ? -19.67500 8.94000   -13.08200 1.000 43.32000  ? 97  ILE   A CA     1 
ATOM   1235 C C      . ILE   A 1 131 ? -18.33300 9.65400   -13.16000 1.000 44.91000  ? 97  ILE   A C      1 
ATOM   1236 O O      . ILE   A 1 131 ? -17.30000 9.08300   -12.79500 1.000 43.92000  ? 97  ILE   A O      1 
ATOM   1237 C CB     . ILE   A 1 131 ? -20.17000 8.84800   -11.62400 1.000 50.02000  ? 97  ILE   A CB     1 
ATOM   1238 C CG1    . ILE   A 1 131 ? -20.09500 10.21100  -10.94200 1.000 50.62000  ? 97  ILE   A CG1    1 
ATOM   1239 C CG2    . ILE   A 1 131 ? -19.35700 7.85800   -10.83800 1.000 54.45000  ? 97  ILE   A CG2    1 
ATOM   1240 C CD1    . ILE   A 1 131 ? -20.74900 10.22900  -9.56800  1.000 69.20000  ? 97  ILE   A CD1    1 
ATOM   1241 H H      . ILE   A 1 131 ? -18.89100 7.15500   -13.36000 1.000 41.95000  ? 97  ILE   A H      1 
ATOM   1242 H HA     . ILE   A 1 131 ? -20.32000 9.46000   -13.58600 1.000 43.32000  ? 97  ILE   A HA     1 
ATOM   1243 H HB     . ILE   A 1 131 ? -21.09500 8.55500   -11.62900 1.000 50.02000  ? 97  ILE   A HB     1 
ATOM   1244 H HG12   . ILE   A 1 131 ? -19.16500 10.45800  -10.82200 1.000 50.62000  ? 97  ILE   A HG12   1 
ATOM   1245 H HG13   . ILE   A 1 131 ? -20.54400 10.86800  -11.49600 1.000 50.62000  ? 97  ILE   A HG13   1 
ATOM   1246 H HG21   . ILE   A 1 131 ? -19.76900 7.72700   -9.97000  1.000 54.45000  ? 97  ILE   A HG21   1 
ATOM   1247 H HG22   . ILE   A 1 131 ? -19.32600 7.01500   -11.31400 1.000 54.45000  ? 97  ILE   A HG22   1 
ATOM   1248 H HG23   . ILE   A 1 131 ? -18.45900 8.20600   -10.72800 1.000 54.45000  ? 97  ILE   A HG23   1 
ATOM   1249 H HD11   . ILE   A 1 131 ? -20.81300 11.14700  -9.26200  1.000 69.20000  ? 97  ILE   A HD11   1 
ATOM   1250 H HD12   . ILE   A 1 131 ? -21.63500 9.84100   -9.63600  1.000 69.20000  ? 97  ILE   A HD12   1 
ATOM   1251 H HD13   . ILE   A 1 131 ? -20.20700 9.71200   -8.95200  1.000 69.20000  ? 97  ILE   A HD13   1 
ATOM   1252 N N      . SER   A 1 132 ? -18.35100 10.89800  -13.63200 1.000 42.31000  ? 98  SER   A N      1 
ATOM   1253 C CA     . SER   A 1 132 ? -17.15000 11.70600  -13.77600 1.000 46.36000  ? 98  SER   A CA     1 
ATOM   1254 C C      . SER   A 1 132 ? -17.05500 12.70100  -12.63000 1.000 46.91000  ? 98  SER   A C      1 
ATOM   1255 O O      . SER   A 1 132 ? -18.02300 13.41500  -12.34200 1.000 49.36000  ? 98  SER   A O      1 
ATOM   1256 C CB     . SER   A 1 132 ? -17.16000 12.46700  -15.10000 1.000 48.09000  ? 98  SER   A CB     1 
ATOM   1257 O OG     . SER   A 1 132 ? -16.01700 13.29300  -15.16900 1.000 45.18000  ? 98  SER   A OG     1 
ATOM   1258 H H      . SER   A 1 132 ? -19.06700 11.30400  -13.88100 1.000 42.31000  ? 98  SER   A H      1 
ATOM   1259 H HA     . SER   A 1 132 ? -16.36900 11.13300  -13.75500 1.000 46.36000  ? 98  SER   A HA     1 
ATOM   1260 H HB2    . SER   A 1 132 ? -17.14300 11.83500  -15.83500 1.000 48.09000  ? 98  SER   A HB2    1 
ATOM   1261 H HB3    . SER   A 1 132 ? -17.95700 13.01800  -15.14800 1.000 48.09000  ? 98  SER   A HB3    1 
ATOM   1262 H HG     . SER   A 1 132 ? -15.32100 12.82500  -15.12200 1.000 45.18000  ? 98  SER   A HG     1 
ATOM   1263 N N      . ILE   A 1 133 ? -15.89100 12.76700  -11.98800 1.000 51.71000  ? 99  ILE   A N      1 
ATOM   1264 C CA     . ILE   A 1 133 ? -15.65900 13.74300  -10.92900 1.000 53.47000  ? 99  ILE   A CA     1 
ATOM   1265 C C      . ILE   A 1 133 ? -14.44000 14.58500  -11.28300 1.000 53.53000  ? 99  ILE   A C      1 
ATOM   1266 O O      . ILE   A 1 133 ? -13.42600 14.07500  -11.77500 1.000 46.94000  ? 99  ILE   A O      1 
ATOM   1267 C CB     . ILE   A 1 133 ? -15.49200 13.09200  -9.53700  1.000 58.07000  ? 99  ILE   A CB     1 
ATOM   1268 C CG1    . ILE   A 1 133 ? -14.04500 12.66100  -9.29900  1.000 65.76000  ? 99  ILE   A CG1    1 
ATOM   1269 C CG2    . ILE   A 1 133 ? -16.46100 11.91300  -9.35600  1.000 54.50000  ? 99  ILE   A CG2    1 
ATOM   1270 C CD1    . ILE   A 1 133 ? -13.68800 12.55200  -7.82900  1.000 71.73000  ? 99  ILE   A CD1    1 
ATOM   1271 H H      . ILE   A 1 133 ? -15.21800 12.25600  -12.14800 1.000 51.71000  ? 99  ILE   A H      1 
ATOM   1272 H HA     . ILE   A 1 133 ? -16.42100 14.34100  -10.88000 1.000 53.47000  ? 99  ILE   A HA     1 
ATOM   1273 H HB     . ILE   A 1 133 ? -15.71400 13.76100  -8.87000  1.000 58.07000  ? 99  ILE   A HB     1 
ATOM   1274 H HG12   . ILE   A 1 133 ? -13.90600 11.79300  -9.70500  1.000 65.76000  ? 99  ILE   A HG12   1 
ATOM   1275 H HG13   . ILE   A 1 133 ? -13.40500 13.28900  -9.64900  1.000 65.76000  ? 99  ILE   A HG13   1 
ATOM   1276 H HG21   . ILE   A 1 133 ? -16.37300 11.56800  -8.45400  1.000 54.50000  ? 99  ILE   A HG21   1 
ATOM   1277 H HG22   . ILE   A 1 133 ? -17.36700 12.22500  -9.50300  1.000 54.50000  ? 99  ILE   A HG22   1 
ATOM   1278 H HG23   . ILE   A 1 133 ? -16.24200 11.22000  -9.99800  1.000 54.50000  ? 99  ILE   A HG23   1 
ATOM   1279 H HD11   . ILE   A 1 133 ? -12.98200 11.89500  -7.72600  1.000 71.73000  ? 99  ILE   A HD11   1 
ATOM   1280 H HD12   . ILE   A 1 133 ? -13.38300 13.41700  -7.51500  1.000 71.73000  ? 99  ILE   A HD12   1 
ATOM   1281 H HD13   . ILE   A 1 133 ? -14.47300 12.27300  -7.33200  1.000 71.73000  ? 99  ILE   A HD13   1 
ATOM   1282 N N      . SER   A 1 134 ? -14.54700 15.88500  -11.03000 1.000 58.46000  ? 100 SER   A N      1 
ATOM   1283 C CA     . SER   A 1 134 ? -13.49200 16.82500  -11.33400 1.000 60.89000  ? 100 SER   A CA     1 
ATOM   1284 C C      . SER   A 1 134 ? -13.38500 17.81300  -10.17200 1.000 65.99000  ? 100 SER   A C      1 
ATOM   1285 O O      . SER   A 1 134 ? -13.75400 18.98300  -10.27600 1.000 74.90000  ? 100 SER   A O      1 
ATOM   1286 C CB     . SER   A 1 134 ? -13.75200 17.54300  -12.65800 1.000 57.53000  ? 100 SER   A CB     1 
ATOM   1287 O OG     . SER   A 1 134 ? -12.64300 18.36000  -12.99000 1.000 74.29000  ? 100 SER   A OG     1 
ATOM   1288 H H      . SER   A 1 134 ? -15.24000 16.24900  -10.67400 1.000 58.46000  ? 100 SER   A H      1 
ATOM   1289 H HA     . SER   A 1 134 ? -12.64900 16.35100  -11.40700 1.000 60.89000  ? 100 SER   A HA     1 
ATOM   1290 H HB2    . SER   A 1 134 ? -13.89100 16.88700  -13.35800 1.000 57.53000  ? 100 SER   A HB2    1 
ATOM   1291 H HB3    . SER   A 1 134 ? -14.53800 18.10000  -12.56000 1.000 57.53000  ? 100 SER   A HB3    1 
ATOM   1292 H HG     . SER   A 1 134 ? -12.78500 18.75500  -13.71800 1.000 74.29000  ? 100 SER   A HG     1 
ATOM   1293 N N      . GLY   A 1 135 ? -12.88000 17.32600  -9.04100  1.000 72.13000  ? 101 GLY   A N      1 
ATOM   1294 C CA     . GLY   A 1 135 ? -12.64300 18.19400  -7.90700  1.000 73.42000  ? 101 GLY   A CA     1 
ATOM   1295 C C      . GLY   A 1 135 ? -11.47700 19.13900  -8.13700  1.000 79.10000  ? 101 GLY   A C      1 
ATOM   1296 O O      . GLY   A 1 135 ? -10.57900 18.89500  -8.94700  1.000 71.70000  ? 101 GLY   A O      1 
ATOM   1297 H H      . GLY   A 1 135 ? -12.67000 16.50200  -8.91100  1.000 72.13000  ? 101 GLY   A H      1 
ATOM   1298 H HA2    . GLY   A 1 135 ? -13.43700 18.72300  -7.73300  1.000 73.42000  ? 101 GLY   A HA2    1 
ATOM   1299 H HA3    . GLY   A 1 135 ? -12.45300 17.65600  -7.12200  1.000 73.42000  ? 101 GLY   A HA3    1 
ATOM   1300 N N      . PHE   A 1 136 ? -11.49700 20.24700  -7.39600  1.000 75.59000  ? 102 PHE   A N      1 
ATOM   1301 C CA     . PHE   A 1 136 ? -10.48800 21.29200  -7.52500  1.000 85.75000  ? 102 PHE   A CA     1 
ATOM   1302 C C      . PHE   A 1 136 ? -9.21600  21.00600  -6.73600  1.000 84.10000  ? 102 PHE   A C      1 
ATOM   1303 O O      . PHE   A 1 136 ? -8.31100  21.84700  -6.73000  1.000 88.72000  ? 102 PHE   A O      1 
ATOM   1304 C CB     . PHE   A 1 136 ? -11.07800 22.63600  -7.09300  1.000 87.73000  ? 102 PHE   A CB     1 
ATOM   1305 C CG     . PHE   A 1 136 ? -12.24900 23.06800  -7.92400  1.000 94.98000  ? 102 PHE   A CG     1 
ATOM   1306 C CD1    . PHE   A 1 136 ? -12.38900 22.61800  -9.22800  1.000 95.25000  ? 102 PHE   A CD1    1 
ATOM   1307 C CD2    . PHE   A 1 136 ? -13.21400 23.91500  -7.40500  1.000 99.59000  ? 102 PHE   A CD2    1 
ATOM   1308 C CE1    . PHE   A 1 136 ? -13.46600 23.00700  -10.00300 1.000 93.76000  ? 102 PHE   A CE1    1 
ATOM   1309 C CE2    . PHE   A 1 136 ? -14.29500 24.31000  -8.17400  1.000 97.44000  ? 102 PHE   A CE2    1 
ATOM   1310 C CZ     . PHE   A 1 136 ? -14.42000 23.85400  -9.47500  1.000 92.94000  ? 102 PHE   A CZ     1 
ATOM   1311 H H      . PHE   A 1 136 ? -12.09600 20.41700  -6.80300  1.000 75.59000  ? 102 PHE   A H      1 
ATOM   1312 H HA     . PHE   A 1 136 ? -10.22400 21.35900  -8.45500  1.000 85.75000  ? 102 PHE   A HA     1 
ATOM   1313 H HB2    . PHE   A 1 136 ? -11.37600 22.56700  -6.17200  1.000 87.73000  ? 102 PHE   A HB2    1 
ATOM   1314 H HB3    . PHE   A 1 136 ? -10.39200 23.31800  -7.16700  1.000 87.73000  ? 102 PHE   A HB3    1 
ATOM   1315 H HD1    . PHE   A 1 136 ? -11.75100 22.04800  -9.59200  1.000 95.25000  ? 102 PHE   A HD1    1 
ATOM   1316 H HD2    . PHE   A 1 136 ? -13.13300 24.22400  -6.53100  1.000 99.59000  ? 102 PHE   A HD2    1 
ATOM   1317 H HE1    . PHE   A 1 136 ? -13.54700 22.69900  -10.87700 1.000 93.76000  ? 102 PHE   A HE1    1 
ATOM   1318 H HE2    . PHE   A 1 136 ? -14.93700 24.88000  -7.81700  1.000 97.44000  ? 102 PHE   A HE2    1 
ATOM   1319 H HZ     . PHE   A 1 136 ? -15.14600 24.11800  -9.99300  1.000 92.94000  ? 102 PHE   A HZ     1 
ATOM   1320 N N      . SER   A 1 137 ? -9.12000  19.85200  -6.08000  1.000 73.29000  ? 103 SER   A N      1 
ATOM   1321 C CA     . SER   A 1 137 ? -7.89400  19.44900  -5.40700  1.000 70.40000  ? 103 SER   A CA     1 
ATOM   1322 C C      . SER   A 1 137 ? -7.93100  17.94000  -5.21200  1.000 75.97000  ? 103 SER   A C      1 
ATOM   1323 O O      . SER   A 1 137 ? -8.97000  17.29600  -5.38600  1.000 67.42000  ? 103 SER   A O      1 
ATOM   1324 C CB     . SER   A 1 137 ? -7.72300  20.16100  -4.06200  1.000 70.11000  ? 103 SER   A CB     1 
ATOM   1325 O OG     . SER   A 1 137 ? -8.71200  19.73500  -3.13800  1.000 71.66000  ? 103 SER   A OG     1 
ATOM   1326 H H      . SER   A 1 137 ? -9.75900  19.28000  -6.01000  1.000 73.29000  ? 103 SER   A H      1 
ATOM   1327 H HA     . SER   A 1 137 ? -7.13300  19.66700  -5.96700  1.000 70.40000  ? 103 SER   A HA     1 
ATOM   1328 H HB2    . SER   A 1 137 ? -6.84600  19.95400  -3.70400  1.000 70.11000  ? 103 SER   A HB2    1 
ATOM   1329 H HB3    . SER   A 1 137 ? -7.80900  21.11800  -4.19800  1.000 70.11000  ? 103 SER   A HB3    1 
ATOM   1330 H HG     . SER   A 1 137 ? -8.60900  20.13100  -2.40400  1.000 71.66000  ? 103 SER   A HG     1 
ATOM   1331 N N      . ALA   A 1 138 ? -6.77100  17.38300  -4.85100  1.000 62.77000  ? 104 ALA   A N      1 
ATOM   1332 C CA     . ALA   A 1 138 ? -6.72500  15.98200  -4.45300  1.000 73.05000  ? 104 ALA   A CA     1 
ATOM   1333 C C      . ALA   A 1 138 ? -7.61700  15.73500  -3.24100  1.000 79.31000  ? 104 ALA   A C      1 
ATOM   1334 O O      . ALA   A 1 138 ? -8.30700  14.71000  -3.16800  1.000 78.06000  ? 104 ALA   A O      1 
ATOM   1335 C CB     . ALA   A 1 138 ? -5.28200  15.56100  -4.17000  1.000 60.57000  ? 104 ALA   A CB     1 
ATOM   1336 H H      . ALA   A 1 138 ? -6.01400  17.78600  -4.84300  1.000 62.77000  ? 104 ALA   A H      1 
ATOM   1337 H HA     . ALA   A 1 138 ? -7.05700  15.43700  -5.18300  1.000 73.05000  ? 104 ALA   A HA     1 
ATOM   1338 H HB1    . ALA   A 1 138 ? -5.27100  14.62500  -3.91500  1.000 60.57000  ? 104 ALA   A HB1    1 
ATOM   1339 H HB2    . ALA   A 1 138 ? -4.75200  15.69200  -4.97200  1.000 60.57000  ? 104 ALA   A HB2    1 
ATOM   1340 H HB3    . ALA   A 1 138 ? -4.93000  16.10500  -3.44800  1.000 60.57000  ? 104 ALA   A HB3    1 
ATOM   1341 N N      . GLU   A 1 139 ? -7.64000  16.67900  -2.29300  1.000 79.43000  ? 105 GLU   A N      1 
ATOM   1342 C CA     . GLU   A 1 139 ? -8.48800  16.53900  -1.11000  1.000 81.13000  ? 105 GLU   A CA     1 
ATOM   1343 C C      . GLU   A 1 139 ? -9.95900  16.42200  -1.49400  1.000 70.51000  ? 105 GLU   A C      1 
ATOM   1344 O O      . GLU   A 1 139 ? -10.66500 15.52300  -1.02100  1.000 75.18000  ? 105 GLU   A O      1 
ATOM   1345 C CB     . GLU   A 1 139 ? -8.27200  17.72400  -0.16400  1.000 64.58000  ? 105 GLU   A CB     1 
ATOM   1346 H H      . GLU   A 1 139 ? -7.17700  17.40300  -2.31300  1.000 79.43000  ? 105 GLU   A H      1 
ATOM   1347 H HA     . GLU   A 1 139 ? -8.23800  15.73000  -0.63700  1.000 81.13000  ? 105 GLU   A HA     1 
ATOM   1348 N N      . GLU   A 1 140 ? -10.44400 17.33400  -2.34200  1.000 68.55000  ? 106 GLU   A N      1 
ATOM   1349 C CA     . GLU   A 1 140 ? -11.84400 17.28800  -2.76000  1.000 75.49000  ? 106 GLU   A CA     1 
ATOM   1350 C C      . GLU   A 1 140 ? -12.16500 15.97200  -3.45400  1.000 76.88000  ? 106 GLU   A C      1 
ATOM   1351 O O      . GLU   A 1 140 ? -13.17100 15.32000  -3.14600  1.000 73.73000  ? 106 GLU   A O      1 
ATOM   1352 C CB     . GLU   A 1 140 ? -12.16100 18.46400  -3.68400  1.000 72.95000  ? 106 GLU   A CB     1 
ATOM   1353 C CG     . GLU   A 1 140 ? -12.11800 19.82400  -3.01600  1.000 82.29000  ? 106 GLU   A CG     1 
ATOM   1354 C CD     . GLU   A 1 140 ? -12.81400 20.89700  -3.84000  1.000 93.14000  ? 106 GLU   A CD     1 
ATOM   1355 O OE1    . GLU   A 1 140 ? -13.36400 20.57400  -4.91600  1.000 94.99000  ? 106 GLU   A OE1    1 
ATOM   1356 O OE2    . GLU   A 1 140 ? -12.81500 22.06800  -3.40800  1.000 99.43000  ? 106 GLU   A OE2    1 
ATOM   1357 H H      . GLU   A 1 140 ? -9.98900  17.97900  -2.68400  1.000 68.55000  ? 106 GLU   A H      1 
ATOM   1358 H HA     . GLU   A 1 140 ? -12.41100 17.36000  -1.97600  1.000 75.49000  ? 106 GLU   A HA     1 
ATOM   1359 H HB2    . GLU   A 1 140 ? -11.51600 18.47200  -4.40800  1.000 72.95000  ? 106 GLU   A HB2    1 
ATOM   1360 H HB3    . GLU   A 1 140 ? -13.05300 18.34000  -4.04300  1.000 72.95000  ? 106 GLU   A HB3    1 
ATOM   1361 H HG2    . GLU   A 1 140 ? -12.56300 19.76900  -2.15600  1.000 82.29000  ? 106 GLU   A HG2    1 
ATOM   1362 H HG3    . GLU   A 1 140 ? -11.19300 20.08900  -2.89600  1.000 82.29000  ? 106 GLU   A HG3    1 
ATOM   1363 N N      . ASN   A 1 141 ? -11.32400 15.57800  -4.41400  1.000 73.52000  ? 107 ASN   A N      1 
ATOM   1364 C CA     . ASN   A 1 141 ? -11.50800 14.31000  -5.11200  1.000 75.38000  ? 107 ASN   A CA     1 
ATOM   1365 C C      . ASN   A 1 141 ? -11.58900 13.14400  -4.13100  1.000 72.17000  ? 107 ASN   A C      1 
ATOM   1366 O O      . ASN   A 1 141 ? -12.47800 12.29000  -4.23500  1.000 65.53000  ? 107 ASN   A O      1 
ATOM   1367 C CB     . ASN   A 1 141 ? -10.36800 14.09500  -6.11300  1.000 60.92000  ? 107 ASN   A CB     1 
ATOM   1368 C CG     . ASN   A 1 141 ? -10.52100 14.93700  -7.36900  1.000 72.56000  ? 107 ASN   A CG     1 
ATOM   1369 O OD1    . ASN   A 1 141 ? -11.63400 15.26900  -7.77500  1.000 67.08000  ? 107 ASN   A OD1    1 
ATOM   1370 N ND2    . ASN   A 1 141 ? -9.39700  15.27200  -8.00100  1.000 70.23000  ? 107 ASN   A ND2    1 
ATOM   1371 H H      . ASN   A 1 141 ? -10.64100 16.02900  -4.67700  1.000 73.52000  ? 107 ASN   A H      1 
ATOM   1372 H HA     . ASN   A 1 141 ? -12.34000 14.34000  -5.60800  1.000 75.38000  ? 107 ASN   A HA     1 
ATOM   1373 H HB2    . ASN   A 1 141 ? -9.52000  14.31200  -5.69500  1.000 60.92000  ? 107 ASN   A HB2    1 
ATOM   1374 H HB3    . ASN   A 1 141 ? -10.38100 13.17200  -6.39700  1.000 60.92000  ? 107 ASN   A HB3    1 
ATOM   1375 H HD21   . ASN   A 1 141 ? -9.43100  15.74700  -8.71700  1.000 70.23000  ? 107 ASN   A HD21   1 
ATOM   1376 H HD22   . ASN   A 1 141 ? -8.63800  15.01800  -7.68800  1.000 70.23000  ? 107 ASN   A HD22   1 
ATOM   1377 N N      . ALA   A 1 142 ? -10.66400 13.09500  -3.16500  1.000 64.21000  ? 108 ALA   A N      1 
ATOM   1378 C CA     . ALA   A 1 142 ? -10.65400 11.98800  -2.21200  1.000 74.40000  ? 108 ALA   A CA     1 
ATOM   1379 C C      . ALA   A 1 142 ? -11.92200 11.97500  -1.36300  1.000 76.68000  ? 108 ALA   A C      1 
ATOM   1380 O O      . ALA   A 1 142 ? -12.47300 10.90500  -1.07200  1.000 77.99000  ? 108 ALA   A O      1 
ATOM   1381 C CB     . ALA   A 1 142 ? -9.41000  12.06000  -1.32700  1.000 64.41000  ? 108 ALA   A CB     1 
ATOM   1382 H H      . ALA   A 1 142 ? -10.04500 13.67900  -3.04400  1.000 64.21000  ? 108 ALA   A H      1 
ATOM   1383 H HA     . ALA   A 1 142 ? -10.61900 11.15300  -2.70400  1.000 74.40000  ? 108 ALA   A HA     1 
ATOM   1384 H HB1    . ALA   A 1 142 ? -9.42300  11.31700  -0.70300  1.000 64.41000  ? 108 ALA   A HB1    1 
ATOM   1385 H HB2    . ALA   A 1 142 ? -8.62000  12.00700  -1.88800  1.000 64.41000  ? 108 ALA   A HB2    1 
ATOM   1386 H HB3    . ALA   A 1 142 ? -9.41600  12.90000  -0.84200  1.000 64.41000  ? 108 ALA   A HB3    1 
ATOM   1387 N N      . GLU   A 1 143 ? -12.40400 13.15300  -0.95800  1.000 74.22000  ? 109 GLU   A N      1 
ATOM   1388 C CA     . GLU   A 1 143 ? -13.64000 13.21500  -0.18100  1.000 77.46000  ? 109 GLU   A CA     1 
ATOM   1389 C C      . GLU   A 1 143 ? -14.80700 12.63800  -0.97400  1.000 80.84000  ? 109 GLU   A C      1 
ATOM   1390 O O      . GLU   A 1 143 ? -15.55900 11.79400  -0.47000  1.000 82.29000  ? 109 GLU   A O      1 
ATOM   1391 C CB     . GLU   A 1 143 ? -13.92600 14.65800  0.24000   1.000 69.70000  ? 109 GLU   A CB     1 
ATOM   1392 H H      . GLU   A 1 143 ? -12.04100 13.91600  -1.11700  1.000 74.22000  ? 109 GLU   A H      1 
ATOM   1393 H HA     . GLU   A 1 143 ? -13.53300 12.68400  0.62400   1.000 77.46000  ? 109 GLU   A HA     1 
ATOM   1394 N N      . MET   A 1 144 ? -14.95900 13.07000  -2.23100  1.000 78.48000  ? 110 MET   A N      1 
ATOM   1395 C CA     . MET   A 1 144 ? -16.01900 12.53800  -3.08400  1.000 77.10000  ? 110 MET   A CA     1 
ATOM   1396 C C      . MET   A 1 144 ? -15.90800 11.03000  -3.26200  1.000 74.86000  ? 110 MET   A C      1 
ATOM   1397 O O      . MET   A 1 144 ? -16.93200 10.34600  -3.36200  1.000 72.36000  ? 110 MET   A O      1 
ATOM   1398 C CB     . MET   A 1 144 ? -16.00000 13.23300  -4.44900  1.000 73.17000  ? 110 MET   A CB     1 
ATOM   1399 C CG     . MET   A 1 144 ? -16.87300 14.48000  -4.51500  1.000 74.07000  ? 110 MET   A CG     1 
ATOM   1400 S SD     . MET   A 1 144 ? -16.61600 15.48400  -5.99000  1.000 71.32000  ? 110 MET   A SD     1 
ATOM   1401 C CE     . MET   A 1 144 ? -14.83900 15.69400  -5.93100  1.000 72.81000  ? 110 MET   A CE     1 
ATOM   1402 H H      . MET   A 1 144 ? -14.46500 13.66500  -2.60700  1.000 78.48000  ? 110 MET   A H      1 
ATOM   1403 H HA     . MET   A 1 144 ? -16.87300 12.73500  -2.66900  1.000 77.10000  ? 110 MET   A HA     1 
ATOM   1404 H HB2    . MET   A 1 144 ? -15.08600 13.48300  -4.64500  1.000 73.17000  ? 110 MET   A HB2    1 
ATOM   1405 H HB3    . MET   A 1 144 ? -16.32200 12.61100  -5.12000  1.000 73.17000  ? 110 MET   A HB3    1 
ATOM   1406 H HG2    . MET   A 1 144 ? -17.79700 14.21000  -4.48700  1.000 74.07000  ? 110 MET   A HG2    1 
ATOM   1407 H HG3    . MET   A 1 144 ? -16.67400 15.03600  -3.74500  1.000 74.07000  ? 110 MET   A HG3    1 
ATOM   1408 H HE1    . MET   A 1 144 ? -14.58800 16.41900  -6.52400  1.000 72.81000  ? 110 MET   A HE1    1 
ATOM   1409 H HE2    . MET   A 1 144 ? -14.57700 15.90500  -5.02200  1.000 72.81000  ? 110 MET   A HE2    1 
ATOM   1410 H HE3    . MET   A 1 144 ? -14.41600 14.87100  -6.21700  1.000 72.81000  ? 110 MET   A HE3    1 
ATOM   1411 N N      . CYS   A 1 145 ? -14.68400 10.49100  -3.30500  1.000 73.92000  ? 111 CYS   A N      1 
ATOM   1412 C CA     . CYS   A 1 145 ? -14.51600 9.05900   -3.54800  1.000 74.64000  ? 111 CYS   A CA     1 
ATOM   1413 C C      . CYS   A 1 145 ? -14.91600 8.23500   -2.33400  1.000 79.00000  ? 111 CYS   A C      1 
ATOM   1414 O O      . CYS   A 1 145 ? -15.46600 7.13400   -2.47500  1.000 65.59000  ? 111 CYS   A O      1 
ATOM   1415 C CB     . CYS   A 1 145 ? -13.07300 8.75300   -3.93600  1.000 68.18000  ? 111 CYS   A CB     1 
ATOM   1416 S SG     . CYS   A 1 145 ? -12.63500 9.32000   -5.58200  1.000 74.98000  ? 111 CYS   A SG     1 
ATOM   1417 H H      . CYS   A 1 145 ? -13.95000 10.92600  -3.19800  1.000 73.92000  ? 111 CYS   A H      1 
ATOM   1418 H HA     . CYS   A 1 145 ? -15.08600 8.79700   -4.28800  1.000 74.64000  ? 111 CYS   A HA     1 
ATOM   1419 H HB2    . CYS   A 1 145 ? -12.49000 9.21400   -3.31200  1.000 68.18000  ? 111 CYS   A HB2    1 
ATOM   1420 H HB3    . CYS   A 1 145 ? -12.90700 7.80700   -3.88100  1.000 68.18000  ? 111 CYS   A HB3    1 
ATOM   1421 H HG     . CYS   A 1 145 ? -12.88600 10.48700  -5.69500  1.000 74.98000  ? 111 CYS   A HG     1 
ATOM   1422 N N      . LYS   A 1 146 ? -14.62600 8.74400   -1.13300  1.000 80.52000  ? 112 LYS   A N      1 
ATOM   1423 C CA     . LYS   A 1 146 ? -15.04000 8.05600   0.08500   1.000 79.72000  ? 112 LYS   A CA     1 
ATOM   1424 C C      . LYS   A 1 146 ? -16.55000 7.82600   0.09800   1.000 78.94000  ? 112 LYS   A C      1 
ATOM   1425 O O      . LYS   A 1 146 ? -17.02400 6.78800   0.57700   1.000 80.12000  ? 112 LYS   A O      1 
ATOM   1426 C CB     . LYS   A 1 146 ? -14.58300 8.85500   1.30800   1.000 69.08000  ? 112 LYS   A CB     1 
ATOM   1427 C CG     . LYS   A 1 146 ? -13.11900 8.61600   1.66500   1.000 76.30000  ? 112 LYS   A CG     1 
ATOM   1428 C CD     . LYS   A 1 146 ? -12.49800 9.78700   2.41700   1.000 74.91000  ? 112 LYS   A CD     1 
ATOM   1429 C CE     . LYS   A 1 146 ? -11.03900 9.49800   2.76200   1.000 59.51000  ? 112 LYS   A CE     1 
ATOM   1430 N NZ     . LYS   A 1 146 ? -10.20800 10.74100  2.77700   1.000 74.80000  ? 112 LYS   A NZ     1 
ATOM   1431 H H      . LYS   A 1 146 ? -14.19600 9.47700   -1.00100  1.000 80.52000  ? 112 LYS   A H      1 
ATOM   1432 H HA     . LYS   A 1 146 ? -14.60700 7.18900   0.11800   1.000 79.72000  ? 112 LYS   A HA     1 
ATOM   1433 H HB2    . LYS   A 1 146 ? -14.69600 9.80100   1.12600   1.000 69.08000  ? 112 LYS   A HB2    1 
ATOM   1434 H HB3    . LYS   A 1 146 ? -15.12300 8.59800   2.07200   1.000 69.08000  ? 112 LYS   A HB3    1 
ATOM   1435 H HG2    . LYS   A 1 146 ? -13.05500 7.82900   2.22900   1.000 76.30000  ? 112 LYS   A HG2    1 
ATOM   1436 H HG3    . LYS   A 1 146 ? -12.61300 8.48100   0.84900   1.000 76.30000  ? 112 LYS   A HG3    1 
ATOM   1437 H HD2    . LYS   A 1 146 ? -12.53000 10.58100  1.86000   1.000 74.91000  ? 112 LYS   A HD2    1 
ATOM   1438 H HD3    . LYS   A 1 146 ? -12.98500 9.93400   3.24300   1.000 74.91000  ? 112 LYS   A HD3    1 
ATOM   1439 H HE2    . LYS   A 1 146 ? -10.99400 9.09400   3.64300   1.000 59.51000  ? 112 LYS   A HE2    1 
ATOM   1440 H HE3    . LYS   A 1 146 ? -10.66800 8.89500   2.09900   1.000 59.51000  ? 112 LYS   A HE3    1 
ATOM   1441 H HZ1    . LYS   A 1 146 ? -9.36500  10.54100  2.98100   1.000 74.80000  ? 112 LYS   A HZ1    1 
ATOM   1442 H HZ2    . LYS   A 1 146 ? -10.22800 11.12900  1.97700   1.000 74.80000  ? 112 LYS   A HZ2    1 
ATOM   1443 H HZ3    . LYS   A 1 146 ? -10.52400 11.31100  3.38300   1.000 74.80000  ? 112 LYS   A HZ3    1 
ATOM   1444 N N      . ARG   A 1 147 ? -17.32100 8.77100   -0.45800  1.000 70.41000  ? 113 ARG   A N      1 
ATOM   1445 C CA     . ARG   A 1 147 ? -18.77900 8.66100   -0.45800  1.000 79.53000  ? 113 ARG   A CA     1 
ATOM   1446 C C      . ARG   A 1 147 ? -19.31100 7.80300   -1.60400  1.000 84.57000  ? 113 ARG   A C      1 
ATOM   1447 O O      . ARG   A 1 147 ? -20.32800 7.11800   -1.44200  1.000 85.79000  ? 113 ARG   A O      1 
ATOM   1448 C CB     . ARG   A 1 147 ? -19.39500 10.05500  -0.50900  1.000 69.03000  ? 113 ARG   A CB     1 
ATOM   1449 C CG     . ARG   A 1 147 ? -19.07300 10.85400  0.73500   1.000 79.61000  ? 113 ARG   A CG     1 
ATOM   1450 C CD     . ARG   A 1 147 ? -19.37100 12.31200  0.54700   1.000 83.54000  ? 113 ARG   A CD     1 
ATOM   1451 N NE     . ARG   A 1 147 ? -20.78500 12.54400  0.29300   1.000 87.60000  ? 113 ARG   A NE     1 
ATOM   1452 C CZ     . ARG   A 1 147 ? -21.26600 13.65000  -0.25600  1.000 91.41000  ? 113 ARG   A CZ     1 
ATOM   1453 N NH1    . ARG   A 1 147 ? -20.46700 14.62800  -0.65100  1.000 86.49000  ? 113 ARG   A NH1    1 
ATOM   1454 N NH2    . ARG   A 1 147 ? -22.58100 13.77600  -0.41400  1.000 88.30000  ? 113 ARG   A NH2    1 
ATOM   1455 H H      . ARG   A 1 147 ? -17.02200 9.48100   -0.83900  1.000 70.41000  ? 113 ARG   A H      1 
ATOM   1456 H HA     . ARG   A 1 147 ? -19.05900 8.24600   0.37300   1.000 79.53000  ? 113 ARG   A HA     1 
ATOM   1457 H HB2    . ARG   A 1 147 ? -19.04200 10.53200  -1.27600  1.000 69.03000  ? 113 ARG   A HB2    1 
ATOM   1458 H HB3    . ARG   A 1 147 ? -20.35900 9.97600   -0.57800  1.000 69.03000  ? 113 ARG   A HB3    1 
ATOM   1459 H HG2    . ARG   A 1 147 ? -19.61100 10.52700  1.47300   1.000 79.61000  ? 113 ARG   A HG2    1 
ATOM   1460 H HG3    . ARG   A 1 147 ? -18.13000 10.76300  0.94200   1.000 79.61000  ? 113 ARG   A HG3    1 
ATOM   1461 H HD2    . ARG   A 1 147 ? -19.12300 12.79500  1.35100   1.000 83.54000  ? 113 ARG   A HD2    1 
ATOM   1462 H HD3    . ARG   A 1 147 ? -18.86600 12.64200  -0.21200  1.000 83.54000  ? 113 ARG   A HD3    1 
ATOM   1463 H HE     . ARG   A 1 147 ? -21.34700 11.96300  0.58600   1.000 87.60000  ? 113 ARG   A HE     1 
ATOM   1464 H HH11   . ARG   A 1 147 ? -19.61600 14.55800  -0.55500  1.000 86.49000  ? 113 ARG   A HH11   1 
ATOM   1465 H HH12   . ARG   A 1 147 ? -20.80100 15.33800  -1.00200  1.000 86.49000  ? 113 ARG   A HH12   1 
ATOM   1466 H HH21   . ARG   A 1 147 ? -23.11200 13.15000  -0.15700  1.000 88.30000  ? 113 ARG   A HH21   1 
ATOM   1467 H HH22   . ARG   A 1 147 ? -22.89200 14.49000  -0.75400  1.000 88.30000  ? 113 ARG   A HH22   1 
ATOM   1468 N N      . LEU   A 1 148 ? -18.65900 7.83300   -2.76600  1.000 72.04000  ? 114 LEU   A N      1 
ATOM   1469 C CA     . LEU   A 1 148 ? -19.08700 6.98800   -3.87400  1.000 69.63000  ? 114 LEU   A CA     1 
ATOM   1470 C C      . LEU   A 1 148 ? -18.80200 5.51300   -3.61900  1.000 70.32000  ? 114 LEU   A C      1 
ATOM   1471 O O      . LEU   A 1 148 ? -19.42400 4.65600   -4.25500  1.000 72.42000  ? 114 LEU   A O      1 
ATOM   1472 C CB     . LEU   A 1 148 ? -18.39700 7.44400   -5.15900  1.000 71.91000  ? 114 LEU   A CB     1 
ATOM   1473 C CG     . LEU   A 1 148 ? -18.69900 6.74300   -6.48200  1.000 63.54000  ? 114 LEU   A CG     1 
ATOM   1474 C CD1    . LEU   A 1 148 ? -20.10800 7.06400   -6.94900  1.000 55.54000  ? 114 LEU   A CD1    1 
ATOM   1475 C CD2    . LEU   A 1 148 ? -17.67400 7.18000   -7.51600  1.000 65.37000  ? 114 LEU   A CD2    1 
ATOM   1476 H H      . LEU   A 1 148 ? -17.97600 8.32700   -2.93500  1.000 72.04000  ? 114 LEU   A H      1 
ATOM   1477 H HA     . LEU   A 1 148 ? -20.04400 7.09000   -3.99600  1.000 69.63000  ? 114 LEU   A HA     1 
ATOM   1478 H HB2    . LEU   A 1 148 ? -18.61500 8.38000   -5.28900  1.000 71.91000  ? 114 LEU   A HB2    1 
ATOM   1479 H HB3    . LEU   A 1 148 ? -17.44100 7.36500   -5.01800  1.000 71.91000  ? 114 LEU   A HB3    1 
ATOM   1480 H HG     . LEU   A 1 148 ? -18.62500 5.78300   -6.36500  1.000 63.54000  ? 114 LEU   A HG     1 
ATOM   1481 H HD11   . LEU   A 1 148 ? -20.27000 6.61600   -7.79400  1.000 55.54000  ? 114 LEU   A HD11   1 
ATOM   1482 H HD12   . LEU   A 1 148 ? -20.74000 6.75200   -6.28200  1.000 55.54000  ? 114 LEU   A HD12   1 
ATOM   1483 H HD13   . LEU   A 1 148 ? -20.19200 8.02400   -7.06200  1.000 55.54000  ? 114 LEU   A HD13   1 
ATOM   1484 H HD21   . LEU   A 1 148 ? -17.87800 6.75200   -8.36200  1.000 65.37000  ? 114 LEU   A HD21   1 
ATOM   1485 H HD22   . LEU   A 1 148 ? -17.71600 8.14400   -7.61400  1.000 65.37000  ? 114 LEU   A HD22   1 
ATOM   1486 H HD23   . LEU   A 1 148 ? -16.79000 6.91600   -7.21500  1.000 65.37000  ? 114 LEU   A HD23   1 
ATOM   1487 N N      . ALA   A 1 149 ? -17.88500 5.20200   -2.70200  1.000 64.88000  ? 115 ALA   A N      1 
ATOM   1488 C CA     . ALA   A 1 149 ? -17.47800 3.81400   -2.48900  1.000 77.59000  ? 115 ALA   A CA     1 
ATOM   1489 C C      . ALA   A 1 149 ? -18.64600 2.89700   -2.15200  1.000 80.07000  ? 115 ALA   A C      1 
ATOM   1490 O O      . ALA   A 1 149 ? -18.78800 1.85100   -2.80700  1.000 66.31000  ? 115 ALA   A O      1 
ATOM   1491 C CB     . ALA   A 1 149 ? -16.39600 3.75800   -1.40600  1.000 69.71000  ? 115 ALA   A CB     1 
ATOM   1492 H H      . ALA   A 1 149 ? -17.48600 5.77000   -2.19500  1.000 64.88000  ? 115 ALA   A H      1 
ATOM   1493 H HA     . ALA   A 1 149 ? -17.08100 3.48400   -3.31000  1.000 77.59000  ? 115 ALA   A HA     1 
ATOM   1494 H HB1    . ALA   A 1 149 ? -16.17100 2.83000   -1.23400  1.000 69.71000  ? 115 ALA   A HB1    1 
ATOM   1495 H HB2    . ALA   A 1 149 ? -15.61200 4.23500   -1.72000  1.000 69.71000  ? 115 ALA   A HB2    1 
ATOM   1496 H HB3    . ALA   A 1 149 ? -16.73100 4.17100   -0.59600  1.000 69.71000  ? 115 ALA   A HB3    1 
ATOM   1497 N N      . PRO   A 1 150 ? -19.48900 3.19600   -1.15700  1.000 76.23000  ? 116 PRO   A N      1 
ATOM   1498 C CA     . PRO   A 1 150 ? -20.67200 2.34000   -0.93500  1.000 79.11000  ? 116 PRO   A CA     1 
ATOM   1499 C C      . PRO   A 1 150 ? -21.57900 2.23500   -2.15200  1.000 72.70000  ? 116 PRO   A C      1 
ATOM   1500 O O      . PRO   A 1 150 ? -22.01000 1.12800   -2.50800  1.000 69.62000  ? 116 PRO   A O      1 
ATOM   1501 C CB     . PRO   A 1 150 ? -21.37200 3.01700   0.25700   1.000 72.83000  ? 116 PRO   A CB     1 
ATOM   1502 C CG     . PRO   A 1 150 ? -20.74900 4.38200   0.37200   1.000 74.15000  ? 116 PRO   A CG     1 
ATOM   1503 C CD     . PRO   A 1 150 ? -19.34500 4.21800   -0.11000  1.000 76.55000  ? 116 PRO   A CD     1 
ATOM   1504 H HA     . PRO   A 1 150 ? -20.39200 1.44900   -0.67200  1.000 79.11000  ? 116 PRO   A HA     1 
ATOM   1505 H HB2    . PRO   A 1 150 ? -22.32300 3.08900   0.07800   1.000 72.83000  ? 116 PRO   A HB2    1 
ATOM   1506 H HB3    . PRO   A 1 150 ? -21.21400 2.50100   1.06300   1.000 72.83000  ? 116 PRO   A HB3    1 
ATOM   1507 H HG2    . PRO   A 1 150 ? -21.23200 5.00900   -0.18800  1.000 74.15000  ? 116 PRO   A HG2    1 
ATOM   1508 H HG3    . PRO   A 1 150 ? -20.76200 4.66900   1.29800   1.000 74.15000  ? 116 PRO   A HG3    1 
ATOM   1509 H HD2    . PRO   A 1 150 ? -19.01700 5.05100   -0.48100  1.000 76.55000  ? 116 PRO   A HD2    1 
ATOM   1510 H HD3    . PRO   A 1 150 ? -18.77500 3.89500   0.60500   1.000 76.55000  ? 116 PRO   A HD3    1 
ATOM   1511 N N      . VAL   A 1 151 ? -21.88100 3.36100   -2.80400  1.000 69.47000  ? 117 VAL   A N      1 
ATOM   1512 C CA     . VAL   A 1 151 ? -22.78300 3.33400   -3.95400  1.000 66.90000  ? 117 VAL   A CA     1 
ATOM   1513 C C      . VAL   A 1 151 ? -22.17800 2.52900   -5.09600  1.000 75.08000  ? 117 VAL   A C      1 
ATOM   1514 O O      . VAL   A 1 151 ? -22.89700 1.86200   -5.85300  1.000 71.44000  ? 117 VAL   A O      1 
ATOM   1515 C CB     . VAL   A 1 151 ? -23.12600 4.76200   -4.40600  1.000 62.85000  ? 117 VAL   A CB     1 
ATOM   1516 C CG1    . VAL   A 1 151 ? -24.12500 4.71300   -5.55700  1.000 68.18000  ? 117 VAL   A CG1    1 
ATOM   1517 C CG2    . VAL   A 1 151 ? -23.66600 5.56900   -3.24100  1.000 71.74000  ? 117 VAL   A CG2    1 
ATOM   1518 H H      . VAL   A 1 151 ? -21.57900 4.14100   -2.60300  1.000 69.47000  ? 117 VAL   A H      1 
ATOM   1519 H HA     . VAL   A 1 151 ? -23.61000 2.90000   -3.69200  1.000 66.90000  ? 117 VAL   A HA     1 
ATOM   1520 H HB     . VAL   A 1 151 ? -22.31900 5.19600   -4.72500  1.000 62.85000  ? 117 VAL   A HB     1 
ATOM   1521 H HG11   . VAL   A 1 151 ? -24.47200 5.60600   -5.71000  1.000 68.18000  ? 117 VAL   A HG11   1 
ATOM   1522 H HG12   . VAL   A 1 151 ? -23.67600 4.39300   -6.35500  1.000 68.18000  ? 117 VAL   A HG12   1 
ATOM   1523 H HG13   . VAL   A 1 151 ? -24.85000 4.11400   -5.32000  1.000 68.18000  ? 117 VAL   A HG13   1 
ATOM   1524 H HG21   . VAL   A 1 151 ? -24.03400 6.40100   -3.57700  1.000 71.74000  ? 117 VAL   A HG21   1 
ATOM   1525 H HG22   . VAL   A 1 151 ? -24.36000 5.05600   -2.79800  1.000 71.74000  ? 117 VAL   A HG22   1 
ATOM   1526 H HG23   . VAL   A 1 151 ? -22.94400 5.75300   -2.62000  1.000 71.74000  ? 117 VAL   A HG23   1 
ATOM   1527 N N      . ALA   A 1 152 ? -20.85200 2.60000   -5.25900  1.000 75.54000  ? 118 ALA   A N      1 
ATOM   1528 C CA     . ALA   A 1 152 ? -20.19100 1.81600   -6.29800  1.000 73.99000  ? 118 ALA   A CA     1 
ATOM   1529 C C      . ALA   A 1 152 ? -20.24800 0.32900   -5.97900  1.000 65.17000  ? 118 ALA   A C      1 
ATOM   1530 O O      . ALA   A 1 152 ? -20.39700 -0.50200  -6.88200  1.000 55.70000  ? 118 ALA   A O      1 
ATOM   1531 C CB     . ALA   A 1 152 ? -18.73900 2.26900   -6.46400  1.000 65.11000  ? 118 ALA   A CB     1 
ATOM   1532 H H      . ALA   A 1 152 ? -20.32300 3.08800   -4.78700  1.000 75.54000  ? 118 ALA   A H      1 
ATOM   1533 H HA     . ALA   A 1 152 ? -20.64900 1.95900   -7.14100  1.000 73.99000  ? 118 ALA   A HA     1 
ATOM   1534 H HB1    . ALA   A 1 152 ? -18.31900 1.73500   -7.15600  1.000 65.11000  ? 118 ALA   A HB1    1 
ATOM   1535 H HB2    . ALA   A 1 152 ? -18.72800 3.20600   -6.71600  1.000 65.11000  ? 118 ALA   A HB2    1 
ATOM   1536 H HB3    . ALA   A 1 152 ? -18.27200 2.14600   -5.62300  1.000 65.11000  ? 118 ALA   A HB3    1 
ATOM   1537 N N      . ALA   A 1 153 ? -20.13400 -0.02000  -4.69500  1.000 66.05000  ? 119 ALA   A N      1 
ATOM   1538 C CA     . ALA   A 1 153 ? -20.15400 -1.42200  -4.29800  1.000 75.42000  ? 119 ALA   A CA     1 
ATOM   1539 C C      . ALA   A 1 153 ? -21.55300 -2.01800  -4.42200  1.000 62.95000  ? 119 ALA   A C      1 
ATOM   1540 O O      . ALA   A 1 153 ? -21.69900 -3.18800  -4.79200  1.000 68.29000  ? 119 ALA   A O      1 
ATOM   1541 C CB     . ALA   A 1 153 ? -19.62600 -1.56600  -2.86900  1.000 72.07000  ? 119 ALA   A CB     1 
ATOM   1542 H H      . ALA   A 1 153 ? -20.04500 0.53300   -4.04300  1.000 66.05000  ? 119 ALA   A H      1 
ATOM   1543 H HA     . ALA   A 1 153 ? -19.56500 -1.92200  -4.88400  1.000 75.42000  ? 119 ALA   A HA     1 
ATOM   1544 H HB1    . ALA   A 1 153 ? -19.63600 -2.50400  -2.62200  1.000 72.07000  ? 119 ALA   A HB1    1 
ATOM   1545 H HB2    . ALA   A 1 153 ? -18.72000 -1.22400  -2.83100  1.000 72.07000  ? 119 ALA   A HB2    1 
ATOM   1546 H HB3    . ALA   A 1 153 ? -20.19600 -1.05900  -2.27000  1.000 72.07000  ? 119 ALA   A HB3    1 
ATOM   1547 N N      . GLU   A 1 154 ? -22.59200 -1.22600  -4.13600  0.860 68.97000  ? 120 GLU   A N      1 
ATOM   1548 C CA     . GLU   A 1 154 ? -23.96300 -1.72600  -4.08600  0.860 68.85000  ? 120 GLU   A CA     1 
ATOM   1549 C C      . GLU   A 1 154 ? -24.69900 -1.62700  -5.41500  0.860 77.83000  ? 120 GLU   A C      1 
ATOM   1550 O O      . GLU   A 1 154 ? -25.73600 -2.28200  -5.58000  0.860 78.12000  ? 120 GLU   A O      1 
ATOM   1551 C CB     . GLU   A 1 154 ? -24.76700 -0.96700  -3.02400  0.860 68.67000  ? 120 GLU   A CB     1 
ATOM   1552 H H      . GLU   A 1 154 ? -22.52400 -0.38600  -3.96600  0.860 68.97000  ? 120 GLU   A H      1 
ATOM   1553 H HA     . GLU   A 1 154 ? -23.94400 -2.66100  -3.82900  0.860 68.85000  ? 120 GLU   A HA     1 
ATOM   1554 N N      . LYS   A 1 155 ? -24.20500 -0.82100  -6.35600  1.000 74.22000  ? 121 LYS   A N      1 
ATOM   1555 C CA     . LYS   A 1 155 ? -24.87400 -0.63200  -7.63900  1.000 69.62000  ? 121 LYS   A CA     1 
ATOM   1556 C C      . LYS   A 1 155 ? -23.97700 -0.84800  -8.85100  1.000 69.85000  ? 121 LYS   A C      1 
ATOM   1557 O O      . LYS   A 1 155 ? -24.50800 -1.09200  -9.94100  1.000 65.67000  ? 121 LYS   A O      1 
ATOM   1558 C CB     . LYS   A 1 155 ? -25.49400 0.77400   -7.72000  1.000 69.25000  ? 121 LYS   A CB     1 
ATOM   1559 C CG     . LYS   A 1 155 ? -26.73700 0.97100   -6.84200  1.000 69.08000  ? 121 LYS   A CG     1 
ATOM   1560 C CD     . LYS   A 1 155 ? -27.85100 -0.00400  -7.23800  1.000 76.67000  ? 121 LYS   A CD     1 
ATOM   1561 C CE     . LYS   A 1 155 ? -29.06400 0.07000   -6.30900  1.000 82.90000  ? 121 LYS   A CE     1 
ATOM   1562 N NZ     . LYS   A 1 155 ? -30.16500 0.95300   -6.80700  1.000 79.20000  ? 121 LYS   A NZ     1 
ATOM   1563 H H      . LYS   A 1 155 ? -23.47800 -0.36900  -6.27300  1.000 74.22000  ? 121 LYS   A H      1 
ATOM   1564 H HA     . LYS   A 1 155 ? -25.58200 -1.28600  -7.71300  1.000 69.62000  ? 121 LYS   A HA     1 
ATOM   1565 H HB2    . LYS   A 1 155 ? -24.83000 1.42300   -7.44000  1.000 69.25000  ? 121 LYS   A HB2    1 
ATOM   1566 H HB3    . LYS   A 1 155 ? -25.75200 0.94600   -8.63900  1.000 69.25000  ? 121 LYS   A HB3    1 
ATOM   1567 H HG2    . LYS   A 1 155 ? -26.50400 0.80900   -5.91400  1.000 69.08000  ? 121 LYS   A HG2    1 
ATOM   1568 H HG3    . LYS   A 1 155 ? -27.06900 1.87600   -6.95300  1.000 69.08000  ? 121 LYS   A HG3    1 
ATOM   1569 H HD2    . LYS   A 1 155 ? -28.14800 0.20300   -8.13800  1.000 76.67000  ? 121 LYS   A HD2    1 
ATOM   1570 H HD3    . LYS   A 1 155 ? -27.52400 -0.91400  -7.19800  1.000 76.67000  ? 121 LYS   A HD3    1 
ATOM   1571 H HE2    . LYS   A 1 155 ? -29.42800 -0.82300  -6.20100  1.000 82.90000  ? 121 LYS   A HE2    1 
ATOM   1572 H HE3    . LYS   A 1 155 ? -28.77700 0.41300   -5.44800  1.000 82.90000  ? 121 LYS   A HE3    1 
ATOM   1573 H HZ1    . LYS   A 1 155 ? -30.83900 0.95500   -6.22600  1.000 79.20000  ? 121 LYS   A HZ1    1 
ATOM   1574 H HZ2    . LYS   A 1 155 ? -29.86600 1.78500   -6.90600  1.000 79.20000  ? 121 LYS   A HZ2    1 
ATOM   1575 H HZ3    . LYS   A 1 155 ? -30.46100 0.65700   -7.59200  1.000 79.20000  ? 121 LYS   A HZ3    1 
ATOM   1576 N N      . GLY   A 1 156 ? -22.65600 -0.77400  -8.70900  1.000 58.43000  ? 122 GLY   A N      1 
ATOM   1577 C CA     . GLY   A 1 156 ? -21.75300 -1.02900  -9.81300  1.000 59.83000  ? 122 GLY   A CA     1 
ATOM   1578 C C      . GLY   A 1 156 ? -21.39400 0.16700   -10.67700 1.000 57.46000  ? 122 GLY   A C      1 
ATOM   1579 O O      . GLY   A 1 156 ? -20.81200 -0.03000  -11.75200 1.000 53.34000  ? 122 GLY   A O      1 
ATOM   1580 H H      . GLY   A 1 156 ? -22.25900 -0.57500  -7.97200  1.000 58.43000  ? 122 GLY   A H      1 
ATOM   1581 H HA2    . GLY   A 1 156 ? -20.92700 -1.39400  -9.45900  1.000 59.83000  ? 122 GLY   A HA2    1 
ATOM   1582 H HA3    . GLY   A 1 156 ? -22.14900 -1.70100  -10.39000 1.000 59.83000  ? 122 GLY   A HA3    1 
ATOM   1583 N N      . VAL   A 1 157 ? -21.72600 1.39300   -10.25400 1.000 54.42000  ? 123 VAL   A N      1 
ATOM   1584 C CA     . VAL   A 1 157 ? -21.31500 2.58200   -10.99800 1.000 55.61000  ? 123 VAL   A CA     1 
ATOM   1585 C C      . VAL   A 1 157 ? -19.78200 2.67900   -11.01700 1.000 56.24000  ? 123 VAL   A C      1 
ATOM   1586 O O      . VAL   A 1 157 ? -19.09500 2.24700   -10.08100 1.000 53.23000  ? 123 VAL   A O      1 
ATOM   1587 C CB     . VAL   A 1 157 ? -21.96700 3.84200   -10.39400 1.000 57.10000  ? 123 VAL   A CB     1 
ATOM   1588 C CG1    . VAL   A 1 157 ? -21.77900 3.89000   -8.88200  1.000 55.17000  ? 123 VAL   A CG1    1 
ATOM   1589 C CG2    . VAL   A 1 157 ? -21.43400 5.12200   -11.04000 1.000 55.45000  ? 123 VAL   A CG2    1 
ATOM   1590 H H      . VAL   A 1 157 ? -22.18900 1.55200   -9.54900  1.000 54.42000  ? 123 VAL   A H      1 
ATOM   1591 H HA     . VAL   A 1 157 ? -21.62000 2.50000   -11.91500 1.000 55.61000  ? 123 VAL   A HA     1 
ATOM   1592 H HB     . VAL   A 1 157 ? -22.92100 3.80600   -10.56700 1.000 57.10000  ? 123 VAL   A HB     1 
ATOM   1593 H HG11   . VAL   A 1 157 ? -21.97400 4.78800   -8.57100  1.000 55.17000  ? 123 VAL   A HG11   1 
ATOM   1594 H HG12   . VAL   A 1 157 ? -22.38500 3.25900   -8.46400  1.000 55.17000  ? 123 VAL   A HG12   1 
ATOM   1595 H HG13   . VAL   A 1 157 ? -20.86100 3.66100   -8.67000  1.000 55.17000  ? 123 VAL   A HG13   1 
ATOM   1596 H HG21   . VAL   A 1 157 ? -21.99500 5.86700   -10.77200 1.000 55.45000  ? 123 VAL   A HG21   1 
ATOM   1597 H HG22   . VAL   A 1 157 ? -20.52400 5.26900   -10.74000 1.000 55.45000  ? 123 VAL   A HG22   1 
ATOM   1598 H HG23   . VAL   A 1 157 ? -21.45600 5.02200   -12.00500 1.000 55.45000  ? 123 VAL   A HG23   1 
ATOM   1599 N N      . ILE   A 1 158 ? -19.23600 3.23400   -12.10400 1.000 49.58000  ? 124 ILE   A N      1 
ATOM   1600 C CA     . ILE   A 1 158 ? -17.79400 3.22500   -12.35200 1.000 47.75000  ? 124 ILE   A CA     1 
ATOM   1601 C C      . ILE   A 1 158 ? -17.28200 4.66000   -12.43900 1.000 49.04000  ? 124 ILE   A C      1 
ATOM   1602 O O      . ILE   A 1 158 ? -17.83700 5.47900   -13.18200 1.000 43.04000  ? 124 ILE   A O      1 
ATOM   1603 C CB     . ILE   A 1 158 ? -17.44200 2.44900   -13.63400 1.000 42.12000  ? 124 ILE   A CB     1 
ATOM   1604 C CG1    . ILE   A 1 158 ? -17.96500 1.00700   -13.57100 1.000 43.97000  ? 124 ILE   A CG1    1 
ATOM   1605 C CG2    . ILE   A 1 158 ? -15.93700 2.44000   -13.84700 1.000 36.50000  ? 124 ILE   A CG2    1 
ATOM   1606 C CD1    . ILE   A 1 158 ? -18.01100 0.33100   -14.92500 1.000 46.66000  ? 124 ILE   A CD1    1 
ATOM   1607 H H      . ILE   A 1 158 ? -19.68900 3.62700   -12.72000 1.000 49.58000  ? 124 ILE   A H      1 
ATOM   1608 H HA     . ILE   A 1 158 ? -17.34500 2.79200   -11.60900 1.000 47.75000  ? 124 ILE   A HA     1 
ATOM   1609 H HB     . ILE   A 1 158 ? -17.85800 2.89500   -14.38800 1.000 42.12000  ? 124 ILE   A HB     1 
ATOM   1610 H HG12   . ILE   A 1 158 ? -17.38100 0.48600   -12.99800 1.000 43.97000  ? 124 ILE   A HG12   1 
ATOM   1611 H HG13   . ILE   A 1 158 ? -18.86500 1.00900   -13.21100 1.000 43.97000  ? 124 ILE   A HG13   1 
ATOM   1612 H HG21   . ILE   A 1 158 ? -15.72000 1.80700   -14.54800 1.000 36.50000  ? 124 ILE   A HG21   1 
ATOM   1613 H HG22   . ILE   A 1 158 ? -15.64600 3.32800   -14.10600 1.000 36.50000  ? 124 ILE   A HG22   1 
ATOM   1614 H HG23   . ILE   A 1 158 ? -15.50400 2.17700   -13.02000 1.000 36.50000  ? 124 ILE   A HG23   1 
ATOM   1615 H HD11   . ILE   A 1 158 ? -18.51700 -0.49300  -14.84900 1.000 46.66000  ? 124 ILE   A HD11   1 
ATOM   1616 H HD12   . ILE   A 1 158 ? -18.44100 0.92500   -15.56000 1.000 46.66000  ? 124 ILE   A HD12   1 
ATOM   1617 H HD13   . ILE   A 1 158 ? -17.10600 0.13800   -15.21300 1.000 46.66000  ? 124 ILE   A HD13   1 
ATOM   1618 N N      . LEU   A 1 159 ? -16.19900 4.94400   -11.71800 1.000 42.29000  ? 125 LEU   A N      1 
ATOM   1619 C CA     . LEU   A 1 159 ? -15.63600 6.28600   -11.62200 1.000 44.55000  ? 125 LEU   A CA     1 
ATOM   1620 C C      . LEU   A 1 159 ? -14.63600 6.55800   -12.75200 1.000 42.73000  ? 125 LEU   A C      1 
ATOM   1621 O O      . LEU   A 1 159 ? -13.79000 5.71000   -13.05300 1.000 40.55000  ? 125 LEU   A O      1 
ATOM   1622 C CB     . LEU   A 1 159 ? -14.95300 6.44300   -10.26500 1.000 42.69000  ? 125 LEU   A CB     1 
ATOM   1623 C CG     . LEU   A 1 159 ? -14.01500 7.63200   -10.08100 1.000 48.93000  ? 125 LEU   A CG     1 
ATOM   1624 C CD1    . LEU   A 1 159 ? -14.82600 8.91400   -10.08500 1.000 54.61000  ? 125 LEU   A CD1    1 
ATOM   1625 C CD2    . LEU   A 1 159 ? -13.19700 7.47900   -8.79400  1.000 50.94000  ? 125 LEU   A CD2    1 
ATOM   1626 H H      . LEU   A 1 159 ? -15.76200 4.35800   -11.26400 1.000 42.29000  ? 125 LEU   A H      1 
ATOM   1627 H HA     . LEU   A 1 159 ? -16.35000 6.94000   -11.68200 1.000 44.55000  ? 125 LEU   A HA     1 
ATOM   1628 H HB2    . LEU   A 1 159 ? -15.64400 6.52000   -9.58900  1.000 42.69000  ? 125 LEU   A HB2    1 
ATOM   1629 H HB3    . LEU   A 1 159 ? -14.43200 5.64200   -10.09700 1.000 42.69000  ? 125 LEU   A HB3    1 
ATOM   1630 H HG     . LEU   A 1 159 ? -13.38700 7.67300   -10.81800 1.000 48.93000  ? 125 LEU   A HG     1 
ATOM   1631 H HD11   . LEU   A 1 159 ? -14.22200 9.66400   -9.98200  1.000 54.61000  ? 125 LEU   A HD11   1 
ATOM   1632 H HD12   . LEU   A 1 159 ? -15.30200 8.98500   -10.92700 1.000 54.61000  ? 125 LEU   A HD12   1 
ATOM   1633 H HD13   . LEU   A 1 159 ? -15.45700 8.89200   -9.34800  1.000 54.61000  ? 125 LEU   A HD13   1 
ATOM   1634 H HD21   . LEU   A 1 159 ? -12.60100 8.24000   -8.70700  1.000 50.94000  ? 125 LEU   A HD21   1 
ATOM   1635 H HD22   . LEU   A 1 159 ? -13.80300 7.44500   -8.03700  1.000 50.94000  ? 125 LEU   A HD22   1 
ATOM   1636 H HD23   . LEU   A 1 159 ? -12.68200 6.65900   -8.84300  1.000 50.94000  ? 125 LEU   A HD23   1 
ATOM   1637 N N      . GLU   A 1 160 ? -14.74700 7.73900   -13.37800 1.000 43.05000  ? 126 GLU   A N      1 
ATOM   1638 C CA     . GLU   A 1 160 ? -13.74100 8.29000   -14.29100 1.000 43.83000  ? 126 GLU   A CA     1 
ATOM   1639 C C      . GLU   A 1 160 ? -13.27400 9.60500   -13.67500 1.000 42.43000  ? 126 GLU   A C      1 
ATOM   1640 O O      . GLU   A 1 160 ? -14.07900 10.52700  -13.50300 1.000 46.88000  ? 126 GLU   A O      1 
ATOM   1641 C CB     . GLU   A 1 160 ? -14.30700 8.50500   -15.71700 1.000 39.99000  ? 126 GLU   A CB     1 
ATOM   1642 C CG     . GLU   A 1 160 ? -13.31400 9.07400   -16.82300 1.000 40.79000  ? 126 GLU   A CG     1 
ATOM   1643 C CD     . GLU   A 1 160 ? -13.98900 9.38000   -18.20700 1.000 50.51000  ? 126 GLU   A CD     1 
ATOM   1644 O OE1    . GLU   A 1 160 ? -14.53800 10.51000  -18.41400 1.000 43.88000  ? 126 GLU   A OE1    1 
ATOM   1645 O OE2    . GLU   A 1 160 ? -13.94100 8.53100   -19.12200 1.000 43.64000  ? 126 GLU   A OE2    1 
ATOM   1646 H H      . GLU   A 1 160 ? -15.42700 8.25700   -13.28200 1.000 43.05000  ? 126 GLU   A H      1 
ATOM   1647 H HA     . GLU   A 1 160 ? -12.98300 7.68700   -14.34600 1.000 43.83000  ? 126 GLU   A HA     1 
ATOM   1648 H HB2    . GLU   A 1 160 ? -14.63400 7.65100   -16.04100 1.000 39.99000  ? 126 GLU   A HB2    1 
ATOM   1649 H HB3    . GLU   A 1 160 ? -15.04900 9.12700   -15.65500 1.000 39.99000  ? 126 GLU   A HB3    1 
ATOM   1650 H HG2    . GLU   A 1 160 ? -12.92600 9.90100   -16.49600 1.000 40.79000  ? 126 GLU   A HG2    1 
ATOM   1651 H HG3    . GLU   A 1 160 ? -12.61300 8.42200   -16.97500 1.000 40.79000  ? 126 GLU   A HG3    1 
ATOM   1652 N N      . LEU   A 1 161 ? -11.99200 9.68300   -13.32000 1.000 38.42000  ? 127 LEU   A N      1 
ATOM   1653 C CA     . LEU   A 1 161 ? -11.42300 10.87000  -12.68300 1.000 40.12000  ? 127 LEU   A CA     1 
ATOM   1654 C C      . LEU   A 1 161 ? -10.93600 11.82900  -13.76700 1.000 43.67000  ? 127 LEU   A C      1 
ATOM   1655 O O      . LEU   A 1 161 ? -10.11500 11.45200  -14.60100 1.000 39.24000  ? 127 LEU   A O      1 
ATOM   1656 C CB     . LEU   A 1 161 ? -10.27600 10.47100  -11.75200 1.000 38.65000  ? 127 LEU   A CB     1 
ATOM   1657 C CG     . LEU   A 1 161 ? -9.52900  11.57900  -11.00700 1.000 43.35000  ? 127 LEU   A CG     1 
ATOM   1658 C CD1    . LEU   A 1 161 ? -10.38700 12.18300  -9.89500  1.000 48.21000  ? 127 LEU   A CD1    1 
ATOM   1659 C CD2    . LEU   A 1 161 ? -8.23500  11.03300  -10.44200 1.000 46.11000  ? 127 LEU   A CD2    1 
ATOM   1660 H H      . LEU   A 1 161 ? -11.42200 9.05000   -13.44000 1.000 38.42000  ? 127 LEU   A H      1 
ATOM   1661 H HA     . LEU   A 1 161 ? -12.10600 11.31700  -12.15800 1.000 40.12000  ? 127 LEU   A HA     1 
ATOM   1662 H HB2    . LEU   A 1 161 ? -10.63500 9.87200   -11.07900 1.000 38.65000  ? 127 LEU   A HB2    1 
ATOM   1663 H HB3    . LEU   A 1 161 ? -9.61700  9.99400   -12.28000 1.000 38.65000  ? 127 LEU   A HB3    1 
ATOM   1664 H HG     . LEU   A 1 161 ? -9.30600  12.28700  -11.63100 1.000 43.35000  ? 127 LEU   A HG     1 
ATOM   1665 H HD11   . LEU   A 1 161 ? -9.88000  12.87900  -9.44800  1.000 48.21000  ? 127 LEU   A HD11   1 
ATOM   1666 H HD12   . LEU   A 1 161 ? -11.19100 12.55800  -10.28600 1.000 48.21000  ? 127 LEU   A HD12   1 
ATOM   1667 H HD13   . LEU   A 1 161 ? -10.62100 11.48500  -9.26300  1.000 48.21000  ? 127 LEU   A HD13   1 
ATOM   1668 H HD21   . LEU   A 1 161 ? -7.79000  11.73300  -9.93900  1.000 46.11000  ? 127 LEU   A HD21   1 
ATOM   1669 H HD22   . LEU   A 1 161 ? -8.43700  10.28400  -9.85900  1.000 46.11000  ? 127 LEU   A HD22   1 
ATOM   1670 H HD23   . LEU   A 1 161 ? -7.67000  10.74000  -11.17400 1.000 46.11000  ? 127 LEU   A HD23   1 
ATOM   1671 N N      . ASN   A 1 162 ? -11.44100 13.06100  -13.76500 1.000 41.16000  ? 128 ASN   A N      1 
ATOM   1672 C CA     . ASN   A 1 162 ? -11.10300 14.02500  -14.81700 1.000 41.37000  ? 128 ASN   A CA     1 
ATOM   1673 C C      . ASN   A 1 162 ? -9.84200  14.76500  -14.38000 1.000 45.01000  ? 128 ASN   A C      1 
ATOM   1674 O O      . ASN   A 1 162 ? -9.88000  15.61200  -13.48800 1.000 44.59000  ? 128 ASN   A O      1 
ATOM   1675 C CB     . ASN   A 1 162 ? -12.27200 14.97200  -15.08400 1.000 42.81000  ? 128 ASN   A CB     1 
ATOM   1676 C CG     . ASN   A 1 162 ? -11.97200 15.98500  -16.18500 1.000 52.13000  ? 128 ASN   A CG     1 
ATOM   1677 O OD1    . ASN   A 1 162 ? -10.86600 16.01600  -16.73700 1.000 46.50000  ? 128 ASN   A OD1    1 
ATOM   1678 N ND2    . ASN   A 1 162 ? -12.95800 16.81700  -16.50900 1.000 50.36000  ? 128 ASN   A ND2    1 
ATOM   1679 H H      . ASN   A 1 162 ? -11.98100 13.36500  -13.16800 1.000 41.16000  ? 128 ASN   A H      1 
ATOM   1680 H HA     . ASN   A 1 162 ? -10.90600 13.54800  -15.63700 1.000 41.37000  ? 128 ASN   A HA     1 
ATOM   1681 H HB2    . ASN   A 1 162 ? -13.04500 14.45300  -15.35600 1.000 42.81000  ? 128 ASN   A HB2    1 
ATOM   1682 H HB3    . ASN   A 1 162 ? -12.47000 15.46200  -14.27100 1.000 42.81000  ? 128 ASN   A HB3    1 
ATOM   1683 H HD21   . ASN   A 1 162 ? -12.83900 17.40600  -17.12400 1.000 50.36000  ? 128 ASN   A HD21   1 
ATOM   1684 H HD22   . ASN   A 1 162 ? -13.71500 16.76600  -16.10300 1.000 50.36000  ? 128 ASN   A HD22   1 
ATOM   1685 N N      . LEU   A 1 163 ? -8.70700  14.43000  -14.99500 1.000 39.58000  ? 129 LEU   A N      1 
ATOM   1686 C CA     . LEU   A 1 163 ? -7.44500  15.11000  -14.72800 1.000 44.36000  ? 129 LEU   A CA     1 
ATOM   1687 C C      . LEU   A 1 163 ? -7.07000  16.10100  -15.81200 1.000 41.26000  ? 129 LEU   A C      1 
ATOM   1688 O O      . LEU   A 1 163 ? -5.89300  16.45300  -15.93500 1.000 45.07000  ? 129 LEU   A O      1 
ATOM   1689 C CB     . LEU   A 1 163 ? -6.30800  14.10600  -14.59400 1.000 35.41000  ? 129 LEU   A CB     1 
ATOM   1690 C CG     . LEU   A 1 163 ? -6.42600  13.02300  -13.51300 1.000 49.66000  ? 129 LEU   A CG     1 
ATOM   1691 C CD1    . LEU   A 1 163 ? -5.20400  12.11400  -13.57200 1.000 49.59000  ? 129 LEU   A CD1    1 
ATOM   1692 C CD2    . LEU   A 1 163 ? -6.58200  13.66300  -12.14800 1.000 50.08000  ? 129 LEU   A CD2    1 
ATOM   1693 H H      . LEU   A 1 163 ? -8.64400  13.80200  -15.57900 1.000 39.58000  ? 129 LEU   A H      1 
ATOM   1694 H HA     . LEU   A 1 163 ? -7.51500  15.59600  -13.89200 1.000 44.36000  ? 129 LEU   A HA     1 
ATOM   1695 H HB2    . LEU   A 1 163 ? -6.21300  13.64800  -15.44400 1.000 35.41000  ? 129 LEU   A HB2    1 
ATOM   1696 H HB3    . LEU   A 1 163 ? -5.49400  14.59900  -14.40800 1.000 35.41000  ? 129 LEU   A HB3    1 
ATOM   1697 H HG     . LEU   A 1 163 ? -7.21300  12.48400  -13.68600 1.000 49.66000  ? 129 LEU   A HG     1 
ATOM   1698 H HD11   . LEU   A 1 163 ? -5.28500  11.43200  -12.88700 1.000 49.59000  ? 129 LEU   A HD11   1 
ATOM   1699 H HD12   . LEU   A 1 163 ? -5.16100  11.70000  -14.44800 1.000 49.59000  ? 129 LEU   A HD12   1 
ATOM   1700 H HD13   . LEU   A 1 163 ? -4.40800  12.64600  -13.41800 1.000 49.59000  ? 129 LEU   A HD13   1 
ATOM   1701 H HD21   . LEU   A 1 163 ? -6.52300  12.97400  -11.46800 1.000 50.08000  ? 129 LEU   A HD21   1 
ATOM   1702 H HD22   . LEU   A 1 163 ? -5.87300  14.31300  -12.02200 1.000 50.08000  ? 129 LEU   A HD22   1 
ATOM   1703 H HD23   . LEU   A 1 163 ? -7.44500  14.10200  -12.10200 1.000 50.08000  ? 129 LEU   A HD23   1 
ATOM   1704 N N      . SER   A 1 164 ? -8.03100  16.56400  -16.62300 1.000 39.52000  ? 130 SER   A N      1 
ATOM   1705 C CA     . SER   A 1 164 ? -7.71400  17.35700  -17.84600 1.000 47.66000  ? 130 SER   A CA     1 
ATOM   1706 C C      . SER   A 1 164 ? -8.67400  18.51500  -18.16500 1.000 47.34000  ? 130 SER   A C      1 
ATOM   1707 O O      . SER   A 1 164 ? -8.63400  18.98600  -19.31100 1.000 48.54000  ? 130 SER   A O      1 
ATOM   1708 C CB     . SER   A 1 164 ? -7.67100  16.38400  -18.98700 1.000 46.57000  ? 130 SER   A CB     1 
ATOM   1709 O OG     . SER   A 1 164 ? -8.64200  15.36600  -18.84800 1.000 39.96000  ? 130 SER   A OG     1 
ATOM   1710 H H      . SER   A 1 164 ? -8.90800  16.41900  -16.46900 1.000 39.52000  ? 130 SER   A H      1 
ATOM   1711 H HA     . SER   A 1 164 ? -6.81200  17.74600  -17.74400 1.000 47.66000  ? 130 SER   A HA     1 
ATOM   1712 H HB2    . SER   A 1 164 ? -7.79600  16.84000  -19.83600 1.000 46.57000  ? 130 SER   A HB2    1 
ATOM   1713 H HB3    . SER   A 1 164 ? -6.80000  15.98600  -18.99600 1.000 46.57000  ? 130 SER   A HB3    1 
ATOM   1714 H HG     . SER   A 1 164 ? -8.25800  14.67600  -18.57300 1.000 39.96000  ? 130 SER   A HG     1 
ATOM   1715 N N      . CYS   A 1 165 ? -9.47600  19.02500  -17.11000 0.850 47.84000  ? 131 CYS   A N      1 
ATOM   1716 C CA     . CYS   A 1 165 ? -10.32000 20.18800  -17.48900 0.850 59.58000  ? 131 CYS   A CA     1 
ATOM   1717 C C      . CYS   A 1 165 ? -9.52400  21.16100  -17.94500 0.850 56.45000  ? 131 CYS   A C      1 
ATOM   1718 O O      . CYS   A 1 165 ? -8.58700  21.44000  -17.30200 0.850 78.78000  ? 131 CYS   A O      1 
ATOM   1719 C CB     . CYS   A 1 165 ? -11.31900 20.60800  -16.41000 0.850 57.45000  ? 131 CYS   A CB     1 
ATOM   1720 S SG     . CYS   A 1 165 ? -12.54700 21.81800  -17.01100 0.850 54.68000  ? 131 CYS   A SG     1 
ATOM   1721 H H      . CYS   A 1 165 ? -9.12300  19.43100  -16.27300 0.850 57.41000  ? 131 CYS   A H      1 
ATOM   1722 H HA     . CYS   A 1 165 ? -10.61300 19.53900  -18.14500 0.850 71.50000  ? 131 CYS   A HA     1 
ATOM   1723 H HB2    . CYS   A 1 165 ? -11.78400 19.81500  -16.10000 0.850 68.94000  ? 131 CYS   A HB2    1 
ATOM   1724 H HB3    . CYS   A 1 165 ? -10.81900 20.97100  -15.67100 0.850 68.94000  ? 131 CYS   A HB3    1 
ATOM   1725 N N      . PRO   A 1 166 ? -9.79400  21.78300  -19.11700 0.810 57.31000  ? 132 PRO   A N      1 
ATOM   1726 C CA     . PRO   A 1 166 ? -8.96000  22.85300  -19.64300 0.810 51.84000  ? 132 PRO   A CA     1 
ATOM   1727 C C      . PRO   A 1 166 ? -9.47900  24.25600  -19.37500 0.810 60.11000  ? 132 PRO   A C      1 
ATOM   1728 O O      . PRO   A 1 166 ? -8.80100  25.21300  -19.78800 0.810 51.79000  ? 132 PRO   A O      1 
ATOM   1729 C CB     . PRO   A 1 166 ? -9.04900  22.48700  -21.12400 0.810 50.65000  ? 132 PRO   A CB     1 
ATOM   1730 C CG     . PRO   A 1 166 ? -10.50600 22.15900  -21.31600 0.810 53.28000  ? 132 PRO   A CG     1 
ATOM   1731 C CD     . PRO   A 1 166 ? -10.88700 21.45900  -20.02500 0.810 55.56000  ? 132 PRO   A CD     1 
ATOM   1732 H HA     . PRO   A 1 166 ? -8.02600  22.76000  -19.33100 0.810 62.20000  ? 132 PRO   A HA     1 
ATOM   1733 H HB2    . PRO   A 1 166 ? -8.77600  23.24200  -21.69400 0.810 60.78000  ? 132 PRO   A HB2    1 
ATOM   1734 H HB3    . PRO   A 1 166 ? -8.48300  21.70700  -21.32700 0.810 60.78000  ? 132 PRO   A HB3    1 
ATOM   1735 H HG2    . PRO   A 1 166 ? -11.03800 22.97200  -21.44500 0.810 63.94000  ? 132 PRO   A HG2    1 
ATOM   1736 H HG3    . PRO   A 1 166 ? -10.63600 21.56800  -22.08600 0.810 63.94000  ? 132 PRO   A HG3    1 
ATOM   1737 H HD2    . PRO   A 1 166 ? -11.74100 21.80000  -19.68500 0.810 66.67000  ? 132 PRO   A HD2    1 
ATOM   1738 H HD3    . PRO   A 1 166 ? -10.96100 20.48900  -20.16200 0.810 66.67000  ? 132 PRO   A HD3    1 
ATOM   1739 N N      . ASN   A 1 167 ? -10.61500 24.38000  -18.69300 1.000 53.18000  ? 133 ASN   A N      1 
ATOM   1740 C CA     . ASN   A 1 167 ? -11.27200 25.69100  -18.46000 1.000 62.66000  ? 133 ASN   A CA     1 
ATOM   1741 C C      . ASN   A 1 167 ? -11.28200 26.02900  -16.96600 1.000 69.00000  ? 133 ASN   A C      1 
ATOM   1742 O O      . ASN   A 1 167 ? -12.07400 26.90800  -16.59000 1.000 74.21000  ? 133 ASN   A O      1 
ATOM   1743 C CB     . ASN   A 1 167 ? -12.67800 25.66500  -19.04600 1.000 55.75000  ? 133 ASN   A CB     1 
ATOM   1744 C CG     . ASN   A 1 167 ? -12.67600 25.34900  -20.52100 1.000 59.25000  ? 133 ASN   A CG     1 
ATOM   1745 O OD1    . ASN   A 1 167 ? -13.41000 24.46500  -20.96900 1.000 54.18000  ? 133 ASN   A OD1    1 
ATOM   1746 N ND2    . ASN   A 1 167 ? -11.88500 26.07200  -21.29600 1.000 48.70000  ? 133 ASN   A ND2    1 
ATOM   1747 H H      . ASN   A 1 167 ? -11.03300 23.66500  -18.33600 1.000 63.81000  ? 133 ASN   A H      1 
ATOM   1748 H HA     . ASN   A 1 167 ? -10.77000 26.39000  -18.92900 1.000 75.20000  ? 133 ASN   A HA     1 
ATOM   1749 H HB2    . ASN   A 1 167 ? -13.20900 24.99200  -18.57500 1.000 66.90000  ? 133 ASN   A HB2    1 
ATOM   1750 H HB3    . ASN   A 1 167 ? -13.10200 26.53500  -18.91200 1.000 66.90000  ? 133 ASN   A HB3    1 
ATOM   1751 H HD21   . ASN   A 1 167 ? -11.51900 25.70200  -22.01400 1.000 58.44000  ? 133 ASN   A HD21   1 
ATOM   1752 H HD22   . ASN   A 1 167 ? -11.72400 26.92200  -21.09900 1.000 58.44000  ? 133 ASN   A HD22   1 
ATOM   1753 N N      . VAL   A 1 168 ? -10.44800 25.38400  -16.14200 1.000 79.47000  ? 134 VAL   A N      1 
ATOM   1754 C CA     . VAL   A 1 168 ? -10.47100 25.60700  -14.69600 1.000 82.05000  ? 134 VAL   A CA     1 
ATOM   1755 C C      . VAL   A 1 168 ? -9.70600  26.88900  -14.37900 1.000 75.21000  ? 134 VAL   A C      1 
ATOM   1756 O O      . VAL   A 1 168 ? -8.47200  26.91500  -14.50300 1.000 70.45000  ? 134 VAL   A O      1 
ATOM   1757 C CB     . VAL   A 1 168 ? -9.87900  24.40200  -13.94100 1.000 79.32000  ? 134 VAL   A CB     1 
ATOM   1758 C CG1    . VAL   A 1 168 ? -9.61000  24.75500  -12.47700 1.000 82.45000  ? 134 VAL   A CG1    1 
ATOM   1759 C CG2    . VAL   A 1 168 ? -10.80900 23.18600  -14.04300 1.000 70.32000  ? 134 VAL   A CG2    1 
ATOM   1760 H H      . VAL   A 1 168 ? -9.91000  24.75900  -16.38400 1.000 95.36000  ? 134 VAL   A H      1 
ATOM   1761 H HA     . VAL   A 1 168 ? -11.38900 25.72400  -14.40600 1.000 98.46000  ? 134 VAL   A HA     1 
ATOM   1762 H HB     . VAL   A 1 168 ? -9.03200  24.16300  -14.34900 1.000 95.19000  ? 134 VAL   A HB     1 
ATOM   1763 H HG11   . VAL   A 1 168 ? -9.33400  23.95400  -12.00500 1.000 98.94000  ? 134 VAL   A HG11   1 
ATOM   1764 H HG12   . VAL   A 1 168 ? -8.90700  25.41800  -12.44100 1.000 98.94000  ? 134 VAL   A HG12   1 
ATOM   1765 H HG13   . VAL   A 1 168 ? -10.42200 25.10900  -12.08200 1.000 98.94000  ? 134 VAL   A HG13   1 
ATOM   1766 H HG21   . VAL   A 1 168 ? -10.49300 22.49500  -13.44000 1.000 84.38000  ? 134 VAL   A HG21   1 
ATOM   1767 H HG22   . VAL   A 1 168 ? -11.70900 23.45400  -13.79900 1.000 84.38000  ? 134 VAL   A HG22   1 
ATOM   1768 H HG23   . VAL   A 1 168 ? -10.79600 22.86200  -14.95500 1.000 84.38000  ? 134 VAL   A HG23   1 
ATOM   1769 N N      . PRO   A 1 169 ? -10.38100 27.95300  -13.93900 1.000 81.51000  ? 135 PRO   A N      1 
ATOM   1770 C CA     . PRO   A 1 169 ? -9.70700  29.25600  -13.77300 1.000 76.69000  ? 135 PRO   A CA     1 
ATOM   1771 C C      . PRO   A 1 169 ? -8.51500  29.18300  -12.82600 1.000 81.15000  ? 135 PRO   A C      1 
ATOM   1772 O O      . PRO   A 1 169 ? -8.64600  28.81600  -11.65400 1.000 80.37000  ? 135 PRO   A O      1 
ATOM   1773 C CB     . PRO   A 1 169 ? -10.82000 30.15300  -13.21900 1.000 72.19000  ? 135 PRO   A CB     1 
ATOM   1774 H HA     . PRO   A 1 169 ? -9.41600  29.59800  -14.63300 1.000 76.69000  ? 135 PRO   A HA     1 
ATOM   1775 N N      . GLY   A 1 170 ? -7.33800  29.54000  -13.34900 1.000 69.50000  ? 136 GLY   A N      1 
ATOM   1776 C CA     . GLY   A 1 170 ? -6.10800  29.58700  -12.58100 1.000 74.42000  ? 136 GLY   A CA     1 
ATOM   1777 C C      . GLY   A 1 170 ? -5.37500  28.27200  -12.40600 1.000 79.38000  ? 136 GLY   A C      1 
ATOM   1778 O O      . GLY   A 1 170 ? -4.32700  28.25400  -11.74700 1.000 76.92000  ? 136 GLY   A O      1 
ATOM   1779 H H      . GLY   A 1 170 ? -7.23300  29.76500  -14.17200 1.000 69.50000  ? 136 GLY   A H      1 
ATOM   1780 H HA2    . GLY   A 1 170 ? -5.49900  30.20800  -13.01000 1.000 74.42000  ? 136 GLY   A HA2    1 
ATOM   1781 H HA3    . GLY   A 1 170 ? -6.30800  29.93200  -11.69700 1.000 74.42000  ? 136 GLY   A HA3    1 
ATOM   1782 N N      . LYS   A 1 171 ? -5.87600  27.17700  -12.96800 1.000 84.68000  ? 137 LYS   A N      1 
ATOM   1783 C CA     . LYS   A 1 171 ? -5.29100  25.85000  -12.76300 1.000 81.58000  ? 137 LYS   A CA     1 
ATOM   1784 C C      . LYS   A 1 171 ? -5.14700  25.12600  -14.09700 1.000 74.76000  ? 137 LYS   A C      1 
ATOM   1785 O O      . LYS   A 1 171 ? -6.16800  24.67100  -14.66000 1.000 70.05000  ? 137 LYS   A O      1 
ATOM   1786 C CB     . LYS   A 1 171 ? -6.14900  25.02700  -11.80200 1.000 74.18000  ? 137 LYS   A CB     1 
ATOM   1787 C CG     . LYS   A 1 171 ? -6.93100  25.83800  -10.76600 1.000 81.17000  ? 137 LYS   A CG     1 
ATOM   1788 C CD     . LYS   A 1 171 ? -6.25600  25.83800  -9.39900  1.000 86.94000  ? 137 LYS   A CD     1 
ATOM   1789 C CE     . LYS   A 1 171 ? -7.21400  26.28900  -8.29800  1.000 85.17000  ? 137 LYS   A CE     1 
ATOM   1790 N NZ     . LYS   A 1 171 ? -8.38100  25.36800  -8.14900  1.000 90.03000  ? 137 LYS   A NZ     1 
ATOM   1791 H H      . LYS   A 1 171 ? -6.56600  27.17400  -13.48100 1.000 84.68000  ? 137 LYS   A H      1 
ATOM   1792 H HA     . LYS   A 1 171 ? -4.42200  25.94900  -12.35200 1.000 81.58000  ? 137 LYS   A HA     1 
ATOM   1793 H HB2    . LYS   A 1 171 ? -6.79300  24.52000  -12.32000 1.000 74.18000  ? 137 LYS   A HB2    1 
ATOM   1794 H HB3    . LYS   A 1 171 ? -5.56900  24.41600  -11.32100 1.000 74.18000  ? 137 LYS   A HB3    1 
ATOM   1795 H HG2    . LYS   A 1 171 ? -7.05500  26.75600  -11.04000 1.000 81.17000  ? 137 LYS   A HG2    1 
ATOM   1796 H HG3    . LYS   A 1 171 ? -7.79500  25.41900  -10.64300 1.000 81.17000  ? 137 LYS   A HG3    1 
ATOM   1797 H HD2    . LYS   A 1 171 ? -5.95600  24.94000  -9.18800  1.000 86.94000  ? 137 LYS   A HD2    1 
ATOM   1798 H HD3    . LYS   A 1 171 ? -5.50200  26.44800  -9.41500  1.000 86.94000  ? 137 LYS   A HD3    1 
ATOM   1799 H HE2    . LYS   A 1 171 ? -6.73800  26.31200  -7.45300  1.000 85.17000  ? 137 LYS   A HE2    1 
ATOM   1800 H HE3    . LYS   A 1 171 ? -7.55300  27.17200  -8.51400  1.000 85.17000  ? 137 LYS   A HE3    1 
ATOM   1801 H HZ1    . LYS   A 1 171 ? -8.86100  25.60000  -7.43600  1.000 90.03000  ? 137 LYS   A HZ1    1 
ATOM   1802 H HZ2    . LYS   A 1 171 ? -8.89900  25.41100  -8.87100  1.000 90.03000  ? 137 LYS   A HZ2    1 
ATOM   1803 H HZ3    . LYS   A 1 171 ? -8.09600  24.53100  -8.04600  1.000 90.03000  ? 137 LYS   A HZ3    1 
ATOM   1804 N N      . PRO   A 1 172 ? -3.93400  24.98600  -14.63900 0.900 73.24000  ? 138 PRO   A N      1 
ATOM   1805 C CA     . PRO   A 1 172 ? -3.75800  24.18100  -15.85700 0.900 67.63000  ? 138 PRO   A CA     1 
ATOM   1806 C C      . PRO   A 1 172 ? -4.18600  22.73300  -15.64700 0.900 68.73000  ? 138 PRO   A C      1 
ATOM   1807 O O      . PRO   A 1 172 ? -4.33300  22.25100  -14.52000 0.900 52.50000  ? 138 PRO   A O      1 
ATOM   1808 C CB     . PRO   A 1 172 ? -2.25100  24.27700  -16.14000 0.900 64.04000  ? 138 PRO   A CB     1 
ATOM   1809 C CG     . PRO   A 1 172 ? -1.63100  24.73500  -14.84100 0.900 69.29000  ? 138 PRO   A CG     1 
ATOM   1810 C CD     . PRO   A 1 172 ? -2.67000  25.60200  -14.19500 0.900 60.99000  ? 138 PRO   A CD     1 
ATOM   1811 H HA     . PRO   A 1 172 ? -4.25400  24.56500  -16.59600 0.900 67.63000  ? 138 PRO   A HA     1 
ATOM   1812 H HB2    . PRO   A 1 172 ? -1.91000  23.40500  -16.39400 0.900 64.04000  ? 138 PRO   A HB2    1 
ATOM   1813 H HB3    . PRO   A 1 172 ? -2.09200  24.92600  -16.84300 0.900 64.04000  ? 138 PRO   A HB3    1 
ATOM   1814 H HG2    . PRO   A 1 172 ? -1.43200  23.96600  -14.28500 0.900 69.29000  ? 138 PRO   A HG2    1 
ATOM   1815 H HG3    . PRO   A 1 172 ? -0.82600  25.24400  -15.02500 0.900 69.29000  ? 138 PRO   A HG3    1 
ATOM   1816 H HD2    . PRO   A 1 172 ? -2.57600  25.55700  -13.23200 0.900 60.99000  ? 138 PRO   A HD2    1 
ATOM   1817 H HD3    . PRO   A 1 172 ? -2.60200  26.51300  -14.52000 0.900 60.99000  ? 138 PRO   A HD3    1 
ATOM   1818 N N      . GLN   A 1 173 ? -4.39300  22.04000  -16.76700 1.000 59.43000  ? 139 GLN   A N      1 
ATOM   1819 C CA     . GLN   A 1 173 ? -4.71600  20.62000  -16.76500 1.000 55.28000  ? 139 GLN   A CA     1 
ATOM   1820 C C      . GLN   A 1 173 ? -3.81200  19.86100  -15.79100 1.000 59.22000  ? 139 GLN   A C      1 
ATOM   1821 O O      . GLN   A 1 173 ? -2.58100  19.91700  -15.89400 1.000 47.46000  ? 139 GLN   A O      1 
ATOM   1822 C CB     . GLN   A 1 173 ? -4.57400  20.05100  -18.19200 1.000 51.41000  ? 139 GLN   A CB     1 
ATOM   1823 C CG     . GLN   A 1 173 ? -5.52600  20.64800  -19.27500 1.000 47.66000  ? 139 GLN   A CG     1 
ATOM   1824 C CD     . GLN   A 1 173 ? -5.03600  21.98500  -19.87800 1.000 61.07000  ? 139 GLN   A CD     1 
ATOM   1825 O OE1    . GLN   A 1 173 ? -4.75200  22.93900  -19.14800 1.000 51.49000  ? 139 GLN   A OE1    1 
ATOM   1826 N NE2    . GLN   A 1 173 ? -4.94000  22.05100  -21.22000 1.000 46.23000  ? 139 GLN   A NE2    1 
ATOM   1827 H H      . GLN   A 1 173 ? -4.34700  22.38200  -17.55300 1.000 59.43000  ? 139 GLN   A H      1 
ATOM   1828 H HA     . GLN   A 1 173 ? -5.63600  20.50200  -16.48100 1.000 55.28000  ? 139 GLN   A HA     1 
ATOM   1829 H HB2    . GLN   A 1 173 ? -3.66500  20.20600  -18.49100 1.000 51.41000  ? 139 GLN   A HB2    1 
ATOM   1830 H HB3    . GLN   A 1 173 ? -4.74200  19.09600  -18.15600 1.000 51.41000  ? 139 GLN   A HB3    1 
ATOM   1831 H HG2    . GLN   A 1 173 ? -5.61100  20.01000  -20.00100 1.000 47.66000  ? 139 GLN   A HG2    1 
ATOM   1832 H HG3    . GLN   A 1 173 ? -6.39500  20.80600  -18.87300 1.000 47.66000  ? 139 GLN   A HG3    1 
ATOM   1833 H HE21   . GLN   A 1 173 ? -5.14600  21.36800  -21.70000 1.000 46.23000  ? 139 GLN   A HE21   1 
ATOM   1834 H HE22   . GLN   A 1 173 ? -4.67200  22.77600  -21.59700 1.000 46.23000  ? 139 GLN   A HE22   1 
ATOM   1835 N N      . VAL   A 1 174 ? -4.42800  19.17600  -14.81500 1.000 49.39000  ? 140 VAL   A N      1 
ATOM   1836 C CA     . VAL   A 1 174 ? -3.66500  18.47200  -13.78000 1.000 49.76000  ? 140 VAL   A CA     1 
ATOM   1837 C C      . VAL   A 1 174 ? -2.63100  17.53200  -14.39100 1.000 49.39000  ? 140 VAL   A C      1 
ATOM   1838 O O      . VAL   A 1 174 ? -1.51000  17.39900  -13.88400 1.000 46.52000  ? 140 VAL   A O      1 
ATOM   1839 C CB     . VAL   A 1 174 ? -4.61300  17.69400  -12.84400 1.000 49.89000  ? 140 VAL   A CB     1 
ATOM   1840 C CG1    . VAL   A 1 174 ? -3.80700  17.01500  -11.73800 1.000 48.68000  ? 140 VAL   A CG1    1 
ATOM   1841 C CG2    . VAL   A 1 174 ? -5.69500  18.60500  -12.27100 1.000 62.71000  ? 140 VAL   A CG2    1 
ATOM   1842 H H      . VAL   A 1 174 ? -5.28100  19.10500  -14.73600 1.000 49.39000  ? 140 VAL   A H      1 
ATOM   1843 H HA     . VAL   A 1 174 ? -3.19000  19.12600  -13.24400 1.000 49.76000  ? 140 VAL   A HA     1 
ATOM   1844 H HB     . VAL   A 1 174 ? -5.05400  16.99900  -13.35700 1.000 49.89000  ? 140 VAL   A HB     1 
ATOM   1845 H HG11   . VAL   A 1 174 ? -4.41700  16.68800  -11.05900 1.000 48.68000  ? 140 VAL   A HG11   1 
ATOM   1846 H HG12   . VAL   A 1 174 ? -3.30800  16.27400  -12.11600 1.000 48.68000  ? 140 VAL   A HG12   1 
ATOM   1847 H HG13   . VAL   A 1 174 ? -3.19800  17.66200  -11.34900 1.000 48.68000  ? 140 VAL   A HG13   1 
ATOM   1848 H HG21   . VAL   A 1 174 ? -6.05300  18.20300  -11.46400 1.000 62.71000  ? 140 VAL   A HG21   1 
ATOM   1849 H HG22   . VAL   A 1 174 ? -5.30400  19.46800  -12.06600 1.000 62.71000  ? 140 VAL   A HG22   1 
ATOM   1850 H HG23   . VAL   A 1 174 ? -6.39900  18.70900  -12.92800 1.000 62.71000  ? 140 VAL   A HG23   1 
ATOM   1851 N N      . ALA   A 1 175 ? -3.00000  16.83100  -15.46200 1.000 41.34000  ? 141 ALA   A N      1 
ATOM   1852 C CA     . ALA   A 1 175 ? -2.08000  15.84900  -16.01800 1.000 39.51000  ? 141 ALA   A CA     1 
ATOM   1853 C C      . ALA   A 1 175 ? -0.99000  16.47500  -16.89000 1.000 39.58000  ? 141 ALA   A C      1 
ATOM   1854 O O      . ALA   A 1 175 ? -0.15600  15.74100  -17.42500 1.000 38.90000  ? 141 ALA   A O      1 
ATOM   1855 C CB     . ALA   A 1 175 ? -2.85600  14.77900  -16.79500 1.000 42.99000  ? 141 ALA   A CB     1 
ATOM   1856 H H      . ALA   A 1 175 ? -3.75300  16.90300  -15.87200 1.000 41.34000  ? 141 ALA   A H      1 
ATOM   1857 H HA     . ALA   A 1 175 ? -1.63500  15.40000  -15.28200 1.000 39.51000  ? 141 ALA   A HA     1 
ATOM   1858 H HB1    . ALA   A 1 175 ? -2.23000  14.13400  -17.15900 1.000 42.99000  ? 141 ALA   A HB1    1 
ATOM   1859 H HB2    . ALA   A 1 175 ? -3.47600  14.33800  -16.19300 1.000 42.99000  ? 141 ALA   A HB2    1 
ATOM   1860 H HB3    . ALA   A 1 175 ? -3.34000  15.21300  -17.51100 1.000 42.99000  ? 141 ALA   A HB3    1 
ATOM   1861 N N      . TYR   A 1 176 ? -0.95400  17.80300  -17.03200 1.000 41.39000  ? 142 TYR   A N      1 
ATOM   1862 C CA     . TYR   A 1 176 ? 0.21800   18.46000  -17.60100 1.000 46.17000  ? 142 TYR   A CA     1 
ATOM   1863 C C      . TYR   A 1 176 ? 1.27600   18.75300  -16.54100 1.000 50.68000  ? 142 TYR   A C      1 
ATOM   1864 O O      . TYR   A 1 176 ? 2.31700   19.33100  -16.86000 1.000 50.23000  ? 142 TYR   A O      1 
ATOM   1865 C CB     . TYR   A 1 176 ? -0.18700  19.75300  -18.33400 1.000 44.28000  ? 142 TYR   A CB     1 
ATOM   1866 C CG     . TYR   A 1 176 ? -0.87900  19.51700  -19.67600 1.000 43.41000  ? 142 TYR   A CG     1 
ATOM   1867 C CD1    . TYR   A 1 176 ? -0.85900  18.26300  -20.29400 1.000 38.56000  ? 142 TYR   A CD1    1 
ATOM   1868 C CD2    . TYR   A 1 176 ? -1.54800  20.55400  -20.32600 1.000 46.16000  ? 142 TYR   A CD2    1 
ATOM   1869 C CE1    . TYR   A 1 176 ? -1.49900  18.04900  -21.52500 1.000 35.15000  ? 142 TYR   A CE1    1 
ATOM   1870 C CE2    . TYR   A 1 176 ? -2.17800  20.35600  -21.54700 1.000 44.82000  ? 142 TYR   A CE2    1 
ATOM   1871 C CZ     . TYR   A 1 176 ? -2.15500  19.11300  -22.14200 1.000 39.18000  ? 142 TYR   A CZ     1 
ATOM   1872 O OH     . TYR   A 1 176 ? -2.79400  18.95000  -23.35700 1.000 32.93000  ? 142 TYR   A OH     1 
ATOM   1873 H H      . TYR   A 1 176 ? -1.58900  18.33800  -16.80900 1.000 41.39000  ? 142 TYR   A H      1 
ATOM   1874 H HA     . TYR   A 1 176 ? 0.63700   17.86200  -18.23700 1.000 46.17000  ? 142 TYR   A HA     1 
ATOM   1875 H HB2    . TYR   A 1 176 ? -0.79800  20.25300  -17.77000 1.000 44.28000  ? 142 TYR   A HB2    1 
ATOM   1876 H HB3    . TYR   A 1 176 ? 0.61000   20.28000  -18.50100 1.000 44.28000  ? 142 TYR   A HB3    1 
ATOM   1877 H HD1    . TYR   A 1 176 ? -0.42300  17.55300  -19.88400 1.000 38.56000  ? 142 TYR   A HD1    1 
ATOM   1878 H HD2    . TYR   A 1 176 ? -1.57100  21.39700  -19.93400 1.000 46.16000  ? 142 TYR   A HD2    1 
ATOM   1879 H HE1    . TYR   A 1 176 ? -1.47900  17.21100  -21.92700 1.000 35.15000  ? 142 TYR   A HE1    1 
ATOM   1880 H HE2    . TYR   A 1 176 ? -2.62000  21.06200  -21.96200 1.000 44.82000  ? 142 TYR   A HE2    1 
ATOM   1881 H HH     . TYR   A 1 176 ? -2.71400  18.15600  -23.62000 1.000 32.93000  ? 142 TYR   A HH     1 
ATOM   1882 N N      . ASP   A 1 177 ? 1.03400   18.34200  -15.29900 1.000 43.43000  ? 143 ASP   A N      1 
ATOM   1883 C CA     . ASP   A 1 177 ? 1.95100   18.51500  -14.16900 1.000 43.21000  ? 143 ASP   A CA     1 
ATOM   1884 C C      . ASP   A 1 177 ? 2.13500   17.12700  -13.56100 1.000 42.71000  ? 143 ASP   A C      1 
ATOM   1885 O O      . ASP   A 1 177 ? 1.28600   16.67600  -12.79000 1.000 45.70000  ? 143 ASP   A O      1 
ATOM   1886 C CB     . ASP   A 1 177 ? 1.36700   19.50700  -13.16300 1.000 47.19000  ? 143 ASP   A CB     1 
ATOM   1887 C CG     . ASP   A 1 177 ? 2.22500   19.68200  -11.90300 1.000 56.76000  ? 143 ASP   A CG     1 
ATOM   1888 O OD1    . ASP   A 1 177 ? 3.25400   18.98800  -11.72800 1.000 48.05000  ? 143 ASP   A OD1    1 
ATOM   1889 O OD2    . ASP   A 1 177 ? 1.84800   20.54300  -11.07900 1.000 60.65000  ? 143 ASP   A OD2    1 
ATOM   1890 H H      . ASP   A 1 177 ? 0.30900   17.94000  -15.07100 1.000 43.43000  ? 143 ASP   A H      1 
ATOM   1891 H HA     . ASP   A 1 177 ? 2.80900   18.84300  -14.48000 1.000 43.21000  ? 143 ASP   A HA     1 
ATOM   1892 H HB2    . ASP   A 1 177 ? 1.28500   20.37400  -13.59000 1.000 47.19000  ? 143 ASP   A HB2    1 
ATOM   1893 H HB3    . ASP   A 1 177 ? 0.49200   19.19300  -12.88500 1.000 47.19000  ? 143 ASP   A HB3    1 
ATOM   1894 N N      . PHE   A 1 178 ? 3.22500   16.43900  -13.90900 1.000 40.54000  ? 144 PHE   A N      1 
ATOM   1895 C CA     . PHE   A 1 178 ? 3.32200   15.02000  -13.56400 1.000 48.56000  ? 144 PHE   A CA     1 
ATOM   1896 C C      . PHE   A 1 178 ? 3.43800   14.78600  -12.06300 1.000 55.53000  ? 144 PHE   A C      1 
ATOM   1897 O O      . PHE   A 1 178 ? 3.04900   13.71400  -11.58400 1.000 48.37000  ? 144 PHE   A O      1 
ATOM   1898 C CB     . PHE   A 1 178 ? 4.48700   14.37000  -14.31400 1.000 46.04000  ? 144 PHE   A CB     1 
ATOM   1899 C CG     . PHE   A 1 178 ? 4.23400   14.23000  -15.78700 1.000 49.37000  ? 144 PHE   A CG     1 
ATOM   1900 C CD1    . PHE   A 1 178 ? 3.05800   13.65300  -16.24300 1.000 49.57000  ? 144 PHE   A CD1    1 
ATOM   1901 C CD2    . PHE   A 1 178 ? 5.14500   14.70900  -16.71400 1.000 45.68000  ? 144 PHE   A CD2    1 
ATOM   1902 C CE1    . PHE   A 1 178 ? 2.80000   13.53200  -17.60200 1.000 38.33000  ? 144 PHE   A CE1    1 
ATOM   1903 C CE2    . PHE   A 1 178 ? 4.90200   14.59700  -18.07400 1.000 53.59000  ? 144 PHE   A CE2    1 
ATOM   1904 C CZ     . PHE   A 1 178 ? 3.72300   14.01600  -18.52400 1.000 42.70000  ? 144 PHE   A CZ     1 
ATOM   1905 H H      . PHE   A 1 178 ? 3.90200   16.75900  -14.33200 1.000 40.54000  ? 144 PHE   A H      1 
ATOM   1906 H HA     . PHE   A 1 178 ? 2.50400   14.58500  -13.84800 1.000 48.56000  ? 144 PHE   A HA     1 
ATOM   1907 H HB2    . PHE   A 1 178 ? 5.27900   14.91800  -14.19900 1.000 46.04000  ? 144 PHE   A HB2    1 
ATOM   1908 H HB3    . PHE   A 1 178 ? 4.64200   13.48600  -13.95000 1.000 46.04000  ? 144 PHE   A HB3    1 
ATOM   1909 H HD1    . PHE   A 1 178 ? 2.43600   13.33400  -15.62900 1.000 49.57000  ? 144 PHE   A HD1    1 
ATOM   1910 H HD2    . PHE   A 1 178 ? 5.93300   15.10500  -16.42000 1.000 45.68000  ? 144 PHE   A HD2    1 
ATOM   1911 H HE1    . PHE   A 1 178 ? 2.01000   13.13900  -17.89400 1.000 38.33000  ? 144 PHE   A HE1    1 
ATOM   1912 H HE2    . PHE   A 1 178 ? 5.52500   14.91800  -18.68500 1.000 53.59000  ? 144 PHE   A HE2    1 
ATOM   1913 H HZ     . PHE   A 1 178 ? 3.56000   13.93400  -19.43600 1.000 42.70000  ? 144 PHE   A HZ     1 
ATOM   1914 N N      . ASP   A 1 179 ? 3.92200   15.76800  -11.30200 1.000 49.73000  ? 145 ASP   A N      1 
ATOM   1915 C CA     . ASP   A 1 179 ? 3.94900   15.60900  -9.85000  1.000 49.86000  ? 145 ASP   A CA     1 
ATOM   1916 C C      . ASP   A 1 179 ? 2.55100   15.71500  -9.25500  1.000 51.58000  ? 145 ASP   A C      1 
ATOM   1917 O O      . ASP   A 1 179 ? 2.19200   14.94200  -8.35800  1.000 51.78000  ? 145 ASP   A O      1 
ATOM   1918 C CB     . ASP   A 1 179 ? 4.86900   16.64700  -9.21600  1.000 55.57000  ? 145 ASP   A CB     1 
ATOM   1919 C CG     . ASP   A 1 179 ? 6.30600   16.20100  -9.19500  1.000 72.81000  ? 145 ASP   A CG     1 
ATOM   1920 O OD1    . ASP   A 1 179 ? 6.54800   14.98500  -9.39500  1.000 82.57000  ? 145 ASP   A OD1    1 
ATOM   1921 O OD2    . ASP   A 1 179 ? 7.19000   17.05700  -8.98900  1.000 84.70000  ? 145 ASP   A OD2    1 
ATOM   1922 H H      . ASP   A 1 179 ? 4.23200   16.51600  -11.59200 1.000 49.73000  ? 145 ASP   A H      1 
ATOM   1923 H HA     . ASP   A 1 179 ? 4.28700   14.72600  -9.63700  1.000 49.86000  ? 145 ASP   A HA     1 
ATOM   1924 H HB2    . ASP   A 1 179 ? 4.81700   17.47100  -9.72500  1.000 55.57000  ? 145 ASP   A HB2    1 
ATOM   1925 H HB3    . ASP   A 1 179 ? 4.58900   16.80300  -8.30100  1.000 55.57000  ? 145 ASP   A HB3    1 
ATOM   1926 N N      . ALA   A 1 180 ? 1.75300   16.67800  -9.72600  1.000 47.28000  ? 146 ALA   A N      1 
ATOM   1927 C CA     . ALA   A 1 180 ? 0.36500   16.75200  -9.28500  1.000 47.09000  ? 146 ALA   A CA     1 
ATOM   1928 C C      . ALA   A 1 180 ? -0.40000  15.49900  -9.68900  1.000 50.79000  ? 146 ALA   A C      1 
ATOM   1929 O O      . ALA   A 1 180 ? -1.18400  14.95800  -8.89800  1.000 48.09000  ? 146 ALA   A O      1 
ATOM   1930 C CB     . ALA   A 1 180 ? -0.31000  17.99800  -9.85900  1.000 50.81000  ? 146 ALA   A CB     1 
ATOM   1931 H H      . ALA   A 1 180 ? 1.98700   17.28500  -10.28800 1.000 47.28000  ? 146 ALA   A H      1 
ATOM   1932 H HA     . ALA   A 1 180 ? 0.34400   16.81800  -8.31700  1.000 47.09000  ? 146 ALA   A HA     1 
ATOM   1933 H HB1    . ALA   A 1 180 ? -1.23000  18.02700  -9.55400  1.000 50.81000  ? 146 ALA   A HB1    1 
ATOM   1934 H HB2    . ALA   A 1 180 ? 0.16600   18.78500  -9.55100  1.000 50.81000  ? 146 ALA   A HB2    1 
ATOM   1935 H HB3    . ALA   A 1 180 ? -0.28400  17.95300  -10.82800 1.000 50.81000  ? 146 ALA   A HB3    1 
ATOM   1936 N N      . MET   A 1 181 ? -0.19300  15.03300  -10.92500 1.000 45.00000  ? 147 MET   A N      1 
ATOM   1937 C CA     . MET   A 1 181 ? -0.84200  13.80600  -11.38500 1.000 45.63000  ? 147 MET   A CA     1 
ATOM   1938 C C      . MET   A 1 181 ? -0.55700  12.65000  -10.43100 1.000 44.23000  ? 147 MET   A C      1 
ATOM   1939 O O      . MET   A 1 181 ? -1.47600  11.95300  -9.97600  1.000 42.48000  ? 147 MET   A O      1 
ATOM   1940 C CB     . MET   A 1 181 ? -0.37600  13.47200  -12.80600 1.000 42.31000  ? 147 MET   A CB     1 
ATOM   1941 C CG     . MET   A 1 181 ? -0.85600  12.10900  -13.33100 1.000 47.49000  ? 147 MET   A CG     1 
ATOM   1942 S SD     . MET   A 1 181 ? -0.42900  11.92100  -15.07100 1.000 50.70000  ? 147 MET   A SD     1 
ATOM   1943 C CE     . MET   A 1 181 ? -1.25600  10.37100  -15.48700 1.000 57.47000  ? 147 MET   A CE     1 
ATOM   1944 H H      . MET   A 1 181 ? 0.31500   15.40700  -11.51000 1.000 45.00000  ? 147 MET   A H      1 
ATOM   1945 H HA     . MET   A 1 181 ? -1.80000  13.95400  -11.41600 1.000 45.63000  ? 147 MET   A HA     1 
ATOM   1946 H HB2    . MET   A 1 181 ? -0.70900  14.15400  -13.41000 1.000 42.31000  ? 147 MET   A HB2    1 
ATOM   1947 H HB3    . MET   A 1 181 ? 0.59400   13.46800  -12.82100 1.000 42.31000  ? 147 MET   A HB3    1 
ATOM   1948 H HG2    . MET   A 1 181 ? -0.42400  11.39800  -12.83300 1.000 47.49000  ? 147 MET   A HG2    1 
ATOM   1949 H HG3    . MET   A 1 181 ? -1.82000  12.04900  -13.24200 1.000 47.49000  ? 147 MET   A HG3    1 
ATOM   1950 H HE1    . MET   A 1 181 ? -0.99900  10.10700  -16.38400 1.000 57.47000  ? 147 MET   A HE1    1 
ATOM   1951 H HE2    . MET   A 1 181 ? -0.98600  9.69000   -14.85200 1.000 57.47000  ? 147 MET   A HE2    1 
ATOM   1952 H HE3    . MET   A 1 181 ? -2.21600  10.50300  -15.44100 1.000 57.47000  ? 147 MET   A HE3    1 
ATOM   1953 N N      . ARG   A 1 182 ? 0.71900   12.44700  -10.09500 1.000 44.53000  ? 148 ARG   A N      1 
ATOM   1954 C CA     . ARG   A 1 182 ? 1.07300   11.35100  -9.19900  1.000 43.75000  ? 148 ARG   A CA     1 
ATOM   1955 C C      . ARG   A 1 182 ? 0.39600   11.49300  -7.83600  1.000 54.56000  ? 148 ARG   A C      1 
ATOM   1956 O O      . ARG   A 1 182 ? 0.01000   10.49200  -7.22200  1.000 49.82000  ? 148 ARG   A O      1 
ATOM   1957 C CB     . ARG   A 1 182 ? 2.58700   11.26900  -9.03300  1.000 43.31000  ? 148 ARG   A CB     1 
ATOM   1958 C CG     . ARG   A 1 182 ? 2.99600   10.05300  -8.21500  1.000 50.98000  ? 148 ARG   A CG     1 
ATOM   1959 C CD     . ARG   A 1 182 ? 4.47200   10.06700  -7.88900  1.000 55.30000  ? 148 ARG   A CD     1 
ATOM   1960 N NE     . ARG   A 1 182 ? 5.27100   10.53600  -9.01400  1.000 76.60000  ? 148 ARG   A NE     1 
ATOM   1961 C CZ     . ARG   A 1 182 ? 5.81000   9.74900   -9.93700  1.000 75.92000  ? 148 ARG   A CZ     1 
ATOM   1962 N NH1    . ARG   A 1 182 ? 5.65200   8.43300   -9.90600  1.000 75.32000  ? 148 ARG   A NH1    1 
ATOM   1963 N NH2    . ARG   A 1 182 ? 6.52500   10.29700  -10.91700 1.000 75.56000  ? 148 ARG   A NH2    1 
ATOM   1964 H H      . ARG   A 1 182 ? 1.38400   12.92000  -10.36700 1.000 44.53000  ? 148 ARG   A H      1 
ATOM   1965 H HA     . ARG   A 1 182 ? 0.77300   10.51700  -9.59300  1.000 43.75000  ? 148 ARG   A HA     1 
ATOM   1966 H HB2    . ARG   A 1 182 ? 2.99700   11.20000  -9.90900  1.000 43.31000  ? 148 ARG   A HB2    1 
ATOM   1967 H HB3    . ARG   A 1 182 ? 2.90300   12.06400  -8.57500  1.000 43.31000  ? 148 ARG   A HB3    1 
ATOM   1968 H HG2    . ARG   A 1 182 ? 2.50900   10.04200  -7.37700  1.000 50.98000  ? 148 ARG   A HG2    1 
ATOM   1969 H HG3    . ARG   A 1 182 ? 2.80600   9.24900   -8.72300  1.000 50.98000  ? 148 ARG   A HG3    1 
ATOM   1970 H HD2    . ARG   A 1 182 ? 4.62300   10.67000  -7.14400  1.000 55.30000  ? 148 ARG   A HD2    1 
ATOM   1971 H HD3    . ARG   A 1 182 ? 4.75800   9.17200   -7.65200  1.000 55.30000  ? 148 ARG   A HD3    1 
ATOM   1972 H HE     . ARG   A 1 182 ? 5.40300   11.38300  -9.08500  1.000 76.60000  ? 148 ARG   A HE     1 
ATOM   1973 H HH11   . ARG   A 1 182 ? 5.19300   8.06500   -9.28000  1.000 75.32000  ? 148 ARG   A HH11   1 
ATOM   1974 H HH12   . ARG   A 1 182 ? 6.01100   7.94500   -10.51600 1.000 75.32000  ? 148 ARG   A HH12   1 
ATOM   1975 H HH21   . ARG   A 1 182 ? 6.63300   11.15000  -10.94500 1.000 75.56000  ? 148 ARG   A HH21   1 
ATOM   1976 H HH22   . ARG   A 1 182 ? 6.87900   9.79800   -11.52100 1.000 75.56000  ? 148 ARG   A HH22   1 
ATOM   1977 N N      . ARG   A 1 183 ? 0.26900   12.72200  -7.32300  1.000 52.15000  ? 149 ARG   A N      1 
ATOM   1978 C CA     . ARG   A 1 183 ? -0.32700  12.90100  -5.99900  1.000 46.13000  ? 149 ARG   A CA     1 
ATOM   1979 C C      . ARG   A 1 183 ? -1.83600  12.70400  -6.02700  1.000 50.75000  ? 149 ARG   A C      1 
ATOM   1980 O O      . ARG   A 1 183 ? -2.40900  12.18200  -5.06800  1.000 55.29000  ? 149 ARG   A O      1 
ATOM   1981 C CB     . ARG   A 1 183 ? -0.00900  14.29400  -5.43200  1.000 49.36000  ? 149 ARG   A CB     1 
ATOM   1982 C CG     . ARG   A 1 183 ? 1.44800   14.55700  -5.06600  1.000 63.66000  ? 149 ARG   A CG     1 
ATOM   1983 C CD     . ARG   A 1 183 ? 1.58300   15.92800  -4.38500  1.000 72.39000  ? 149 ARG   A CD     1 
ATOM   1984 N NE     . ARG   A 1 183 ? 0.52400   16.84900  -4.79700  1.000 65.96000  ? 149 ARG   A NE     1 
ATOM   1985 C CZ     . ARG   A 1 183 ? 0.69500   17.89700  -5.59300  1.000 66.51000  ? 149 ARG   A CZ     1 
ATOM   1986 N NH1    . ARG   A 1 183 ? 1.89400   18.24300  -6.03900  1.000 69.02000  ? 149 ARG   A NH1    1 
ATOM   1987 N NH2    . ARG   A 1 183 ? -0.36400  18.62400  -5.94400  1.000 67.33000  ? 149 ARG   A NH2    1 
ATOM   1988 H H      . ARG   A 1 183 ? 0.51400   13.44900  -7.71100  1.000 52.15000  ? 149 ARG   A H      1 
ATOM   1989 H HA     . ARG   A 1 183 ? 0.04800   12.24100  -5.39500  1.000 46.13000  ? 149 ARG   A HA     1 
ATOM   1990 H HB2    . ARG   A 1 183 ? -0.26500  14.94600  -6.10300  1.000 49.36000  ? 149 ARG   A HB2    1 
ATOM   1991 H HB3    . ARG   A 1 183 ? -0.53900  14.42800  -4.63100  1.000 49.36000  ? 149 ARG   A HB3    1 
ATOM   1992 H HG2    . ARG   A 1 183 ? 1.75600   13.87500  -4.44900  1.000 63.66000  ? 149 ARG   A HG2    1 
ATOM   1993 H HG3    . ARG   A 1 183 ? 1.99000   14.55800  -5.87000  1.000 63.66000  ? 149 ARG   A HG3    1 
ATOM   1994 H HD2    . ARG   A 1 183 ? 1.51100   15.80600  -3.42500  1.000 72.39000  ? 149 ARG   A HD2    1 
ATOM   1995 H HD3    . ARG   A 1 183 ? 2.44700   16.30700  -4.60100  1.000 72.39000  ? 149 ARG   A HD3    1 
ATOM   1996 H HE     . ARG   A 1 183 ? -0.25700  16.73300  -4.45700  1.000 65.96000  ? 149 ARG   A HE     1 
ATOM   1997 H HH11   . ARG   A 1 183 ? 2.59000   17.78800  -5.82600  1.000 69.02000  ? 149 ARG   A HH11   1 
ATOM   1998 H HH12   . ARG   A 1 183 ? 1.97500   18.92900  -6.55200  1.000 69.02000  ? 149 ARG   A HH12   1 
ATOM   1999 H HH21   . ARG   A 1 183 ? -1.14600  18.41000  -5.65900  1.000 67.33000  ? 149 ARG   A HH21   1 
ATOM   2000 H HH22   . ARG   A 1 183 ? -0.26500  19.30800  -6.45600  1.000 67.33000  ? 149 ARG   A HH22   1 
ATOM   2001 N N      . TYR   A 1 184 ? -2.50100  13.13500  -7.10100  1.000 43.99000  ? 150 TYR   A N      1 
ATOM   2002 C CA     . TYR   A 1 184 ? -3.92400  12.85100  -7.24300  1.000 52.97000  ? 150 TYR   A CA     1 
ATOM   2003 C C      . TYR   A 1 184 ? -4.17700  11.35100  -7.25500  1.000 49.17000  ? 150 TYR   A C      1 
ATOM   2004 O O      . TYR   A 1 184 ? -5.06800  10.85500  -6.55600  1.000 51.67000  ? 150 TYR   A O      1 
ATOM   2005 C CB     . TYR   A 1 184 ? -4.46800  13.47800  -8.52200  1.000 45.80000  ? 150 TYR   A CB     1 
ATOM   2006 C CG     . TYR   A 1 184 ? -4.93400  14.91200  -8.40400  1.000 54.35000  ? 150 TYR   A CG     1 
ATOM   2007 C CD1    . TYR   A 1 184 ? -4.05300  15.92500  -8.04600  1.000 62.56000  ? 150 TYR   A CD1    1 
ATOM   2008 C CD2    . TYR   A 1 184 ? -6.24900  15.25900  -8.70100  1.000 58.54000  ? 150 TYR   A CD2    1 
ATOM   2009 C CE1    . TYR   A 1 184 ? -4.47300  17.24400  -7.96200  1.000 58.52000  ? 150 TYR   A CE1    1 
ATOM   2010 C CE2    . TYR   A 1 184 ? -6.67900  16.57600  -8.62600  1.000 65.60000  ? 150 TYR   A CE2    1 
ATOM   2011 C CZ     . TYR   A 1 184 ? -5.78600  17.56400  -8.25500  1.000 66.25000  ? 150 TYR   A CZ     1 
ATOM   2012 O OH     . TYR   A 1 184 ? -6.20300  18.87400  -8.17400  1.000 69.64000  ? 150 TYR   A OH     1 
ATOM   2013 H H      . TYR   A 1 184 ? -2.15700  13.58500  -7.74800  1.000 43.99000  ? 150 TYR   A H      1 
ATOM   2014 H HA     . TYR   A 1 184 ? -4.40200  13.23300  -6.49100  1.000 52.97000  ? 150 TYR   A HA     1 
ATOM   2015 H HB2    . TYR   A 1 184 ? -3.77000  13.45400  -9.19500  1.000 45.80000  ? 150 TYR   A HB2    1 
ATOM   2016 H HB3    . TYR   A 1 184 ? -5.22500  12.95100  -8.82300  1.000 45.80000  ? 150 TYR   A HB3    1 
ATOM   2017 H HD1    . TYR   A 1 184 ? -3.16900  15.71400  -7.85100  1.000 62.56000  ? 150 TYR   A HD1    1 
ATOM   2018 H HD2    . TYR   A 1 184 ? -6.85000  14.59600  -8.95400  1.000 58.54000  ? 150 TYR   A HD2    1 
ATOM   2019 H HE1    . TYR   A 1 184 ? -3.87400  17.91100  -7.71400  1.000 58.52000  ? 150 TYR   A HE1    1 
ATOM   2020 H HE2    . TYR   A 1 184 ? -7.56300  16.79200  -8.82000  1.000 65.60000  ? 150 TYR   A HE2    1 
ATOM   2021 H HH     . TYR   A 1 184 ? -7.01600  18.93000  -8.37600  1.000 69.64000  ? 150 TYR   A HH     1 
ATOM   2022 N N      . LEU   A 1 185 ? -3.40800  10.61200  -8.06500  1.000 49.96000  ? 151 LEU   A N      1 
ATOM   2023 C CA     . LEU   A 1 185 ? -3.62800  9.17000   -8.19700  1.000 52.89000  ? 151 LEU   A CA     1 
ATOM   2024 C C      . LEU   A 1 185 ? -3.33700  8.44300   -6.89100  1.000 54.63000  ? 151 LEU   A C      1 
ATOM   2025 O O      . LEU   A 1 185 ? -4.06400  7.51100   -6.51700  1.000 49.84000  ? 151 LEU   A O      1 
ATOM   2026 C CB     . LEU   A 1 185 ? -2.77100  8.59700   -9.33600  1.000 40.35000  ? 151 LEU   A CB     1 
ATOM   2027 C CG     . LEU   A 1 185 ? -3.12600  9.13500   -10.73400 1.000 44.35000  ? 151 LEU   A CG     1 
ATOM   2028 C CD1    . LEU   A 1 185 ? -2.26700  8.51600   -11.82500 1.000 41.19000  ? 151 LEU   A CD1    1 
ATOM   2029 C CD2    . LEU   A 1 185 ? -4.59600  8.93400   -11.02600 1.000 42.21000  ? 151 LEU   A CD2    1 
ATOM   2030 H H      . LEU   A 1 185 ? -2.76100  10.91900  -8.54200  1.000 49.96000  ? 151 LEU   A H      1 
ATOM   2031 H HA     . LEU   A 1 185 ? -4.56100  9.01500   -8.40900  1.000 52.89000  ? 151 LEU   A HA     1 
ATOM   2032 H HB2    . LEU   A 1 185 ? -1.84100  8.81400   -9.16400  1.000 40.35000  ? 151 LEU   A HB2    1 
ATOM   2033 H HB3    . LEU   A 1 185 ? -2.88300  7.63400   -9.35400  1.000 40.35000  ? 151 LEU   A HB3    1 
ATOM   2034 H HG     . LEU   A 1 185 ? -2.95900  10.09000  -10.74400 1.000 44.35000  ? 151 LEU   A HG     1 
ATOM   2035 H HD11   . LEU   A 1 185 ? -2.51200  8.90600   -12.67900 1.000 41.19000  ? 151 LEU   A HD11   1 
ATOM   2036 H HD12   . LEU   A 1 185 ? -1.33400  8.69900   -11.63300 1.000 41.19000  ? 151 LEU   A HD12   1 
ATOM   2037 H HD13   . LEU   A 1 185 ? -2.42000  7.55800   -11.84200 1.000 41.19000  ? 151 LEU   A HD13   1 
ATOM   2038 H HD21   . LEU   A 1 185 ? -4.75000  9.07800   -11.97200 1.000 42.21000  ? 151 LEU   A HD21   1 
ATOM   2039 H HD22   . LEU   A 1 185 ? -4.84500  8.02800   -10.78400 1.000 42.21000  ? 151 LEU   A HD22   1 
ATOM   2040 H HD23   . LEU   A 1 185 ? -5.11300  9.57000   -10.50700 1.000 42.21000  ? 151 LEU   A HD23   1 
ATOM   2041 N N      . ALA   A 1 186 ? -2.27200  8.84100   -6.19100  1.000 46.95000  ? 152 ALA   A N      1 
ATOM   2042 C CA     . ALA   A 1 186 ? -1.98500  8.23600   -4.89500  1.000 46.70000  ? 152 ALA   A CA     1 
ATOM   2043 C C      . ALA   A 1 186 ? -3.10500  8.52800   -3.90400  1.000 51.23000  ? 152 ALA   A C      1 
ATOM   2044 O O      . ALA   A 1 186 ? -3.58900  7.62800   -3.21400  1.000 46.83000  ? 152 ALA   A O      1 
ATOM   2045 C CB     . ALA   A 1 186 ? -0.64600  8.74000   -4.35800  1.000 52.03000  ? 152 ALA   A CB     1 
ATOM   2046 H H      . ALA   A 1 186 ? -1.71300  9.44600   -6.44000  1.000 46.95000  ? 152 ALA   A H      1 
ATOM   2047 H HA     . ALA   A 1 186 ? -1.92200  7.27400   -5.00200  1.000 46.70000  ? 152 ALA   A HA     1 
ATOM   2048 H HB1    . ALA   A 1 186 ? -0.47500  8.32600   -3.49800  1.000 52.03000  ? 152 ALA   A HB1    1 
ATOM   2049 H HB2    . ALA   A 1 186 ? 0.05500   8.50200   -4.98500  1.000 52.03000  ? 152 ALA   A HB2    1 
ATOM   2050 H HB3    . ALA   A 1 186 ? -0.68900  9.70400   -4.25900  1.000 52.03000  ? 152 ALA   A HB3    1 
ATOM   2051 N N      . ALA   A 1 187 ? -3.54900  9.78400   -3.83500  1.000 49.52000  ? 153 ALA   A N      1 
ATOM   2052 C CA     . ALA   A 1 187 ? -4.62000  10.12600  -2.90600  1.000 56.84000  ? 153 ALA   A CA     1 
ATOM   2053 C C      . ALA   A 1 187 ? -5.89800  9.35600   -3.21600  1.000 62.42000  ? 153 ALA   A C      1 
ATOM   2054 O O      . ALA   A 1 187 ? -6.56900  8.86500   -2.29800  1.000 57.65000  ? 153 ALA   A O      1 
ATOM   2055 C CB     . ALA   A 1 187 ? -4.87900  11.63200  -2.92900  1.000 57.37000  ? 153 ALA   A CB     1 
ATOM   2056 H H      . ALA   A 1 187 ? -3.25300  10.44100  -4.30500  1.000 49.52000  ? 153 ALA   A H      1 
ATOM   2057 H HA     . ALA   A 1 187 ? -4.34200  9.88700   -2.00800  1.000 56.84000  ? 153 ALA   A HA     1 
ATOM   2058 H HB1    . ALA   A 1 187 ? -5.59300  11.83900  -2.30600  1.000 57.37000  ? 153 ALA   A HB1    1 
ATOM   2059 H HB2    . ALA   A 1 187 ? -4.06800  12.09500  -2.66900  1.000 57.37000  ? 153 ALA   A HB2    1 
ATOM   2060 H HB3    . ALA   A 1 187 ? -5.13700  11.89400  -3.82700  1.000 57.37000  ? 153 ALA   A HB3    1 
ATOM   2061 N N      . ILE   A 1 188 ? -6.25900  9.24100   -4.49900  1.000 51.96000  ? 154 ILE   A N      1 
ATOM   2062 C CA     . ILE   A 1 188 ? -7.47500  8.51100   -4.84900  1.000 46.21000  ? 154 ILE   A CA     1 
ATOM   2063 C C      . ILE   A 1 188 ? -7.30300  7.01600   -4.57000  1.000 51.96000  ? 154 ILE   A C      1 
ATOM   2064 O O      . ILE   A 1 188 ? -8.21800  6.35900   -4.05700  1.000 56.06000  ? 154 ILE   A O      1 
ATOM   2065 C CB     . ILE   A 1 188 ? -7.87300  8.78800   -6.31300  1.000 49.13000  ? 154 ILE   A CB     1 
ATOM   2066 C CG1    . ILE   A 1 188 ? -8.08600  10.28000  -6.53400  1.000 55.40000  ? 154 ILE   A CG1    1 
ATOM   2067 C CG2    . ILE   A 1 188 ? -9.16700  8.06800   -6.67700  1.000 44.03000  ? 154 ILE   A CG2    1 
ATOM   2068 C CD1    . ILE   A 1 188 ? -9.39300  10.80100  -5.97400  1.000 62.70000  ? 154 ILE   A CD1    1 
ATOM   2069 H H      . ILE   A 1 188 ? -5.82700  9.56800   -5.16700  1.000 51.96000  ? 154 ILE   A H      1 
ATOM   2070 H HA     . ILE   A 1 188 ? -8.19700  8.83000   -4.28500  1.000 46.21000  ? 154 ILE   A HA     1 
ATOM   2071 H HB     . ILE   A 1 188 ? -7.16300  8.47900   -6.89800  1.000 49.13000  ? 154 ILE   A HB     1 
ATOM   2072 H HG12   . ILE   A 1 188 ? -7.37000  10.77400  -6.10800  1.000 55.40000  ? 154 ILE   A HG12   1 
ATOM   2073 H HG13   . ILE   A 1 188 ? -8.08200  10.45700  -7.48800  1.000 55.40000  ? 154 ILE   A HG13   1 
ATOM   2074 H HG21   . ILE   A 1 188 ? -9.57400  8.51300   -7.43600  1.000 44.03000  ? 154 ILE   A HG21   1 
ATOM   2075 H HG22   . ILE   A 1 188 ? -8.95900  7.14900   -6.90800  1.000 44.03000  ? 154 ILE   A HG22   1 
ATOM   2076 H HG23   . ILE   A 1 188 ? -9.77000  8.08800   -5.91800  1.000 44.03000  ? 154 ILE   A HG23   1 
ATOM   2077 H HD11   . ILE   A 1 188 ? -9.22000  11.66300  -5.56800  1.000 62.70000  ? 154 ILE   A HD11   1 
ATOM   2078 H HD12   . ILE   A 1 188 ? -10.03800 10.88900  -6.69300  1.000 62.70000  ? 154 ILE   A HD12   1 
ATOM   2079 H HD13   . ILE   A 1 188 ? -9.72500  10.19400  -5.29500  1.000 62.70000  ? 154 ILE   A HD13   1 
ATOM   2080 N N      . SER   A 1 189 ? -6.12500  6.45500   -4.87000  1.000 46.68000  ? 155 SER   A N      1 
ATOM   2081 C CA     . SER   A 1 189 ? -5.93300  5.02300   -4.64000  1.000 48.11000  ? 155 SER   A CA     1 
ATOM   2082 C C      . SER   A 1 189 ? -5.98100  4.67700   -3.16000  1.000 61.48000  ? 155 SER   A C      1 
ATOM   2083 O O      . SER   A 1 189 ? -6.35800  3.55500   -2.79900  1.000 54.66000  ? 155 SER   A O      1 
ATOM   2084 C CB     . SER   A 1 189 ? -4.60700  4.54700   -5.22700  1.000 49.29000  ? 155 SER   A CB     1 
ATOM   2085 O OG     . SER   A 1 189 ? -4.54600  4.78900   -6.61200  1.000 45.12000  ? 155 SER   A OG     1 
ATOM   2086 H H      . SER   A 1 189 ? -5.44500  6.86700   -5.19600  1.000 46.68000  ? 155 SER   A H      1 
ATOM   2087 H HA     . SER   A 1 189 ? -6.64600  4.53700   -5.08200  1.000 48.11000  ? 155 SER   A HA     1 
ATOM   2088 H HB2    . SER   A 1 189 ? -3.88200  5.02300   -4.79200  1.000 49.29000  ? 155 SER   A HB2    1 
ATOM   2089 H HB3    . SER   A 1 189 ? -4.51800  3.59400   -5.07000  1.000 49.29000  ? 155 SER   A HB3    1 
ATOM   2090 H HG     . SER   A 1 189 ? -4.62000  5.61200   -6.76300  1.000 45.12000  ? 155 SER   A HG     1 
ATOM   2091 N N      . GLU   A 1 190 ? -5.58100  5.60500   -2.29100  1.000 59.83000  ? 156 GLU   A N      1 
ATOM   2092 C CA     . GLU   A 1 190 ? -5.64400  5.32100   -0.86400  1.000 62.34000  ? 156 GLU   A CA     1 
ATOM   2093 C C      . GLU   A 1 190 ? -7.05000  5.51800   -0.31300  1.000 57.21000  ? 156 GLU   A C      1 
ATOM   2094 O O      . GLU   A 1 190 ? -7.44500  4.81400   0.62100   1.000 67.20000  ? 156 GLU   A O      1 
ATOM   2095 C CB     . GLU   A 1 190 ? -4.63700  6.18900   -0.10500  1.000 53.94000  ? 156 GLU   A CB     1 
ATOM   2096 C CG     . GLU   A 1 190 ? -4.42200  5.74600   1.33100   1.000 72.94000  ? 156 GLU   A CG     1 
ATOM   2097 H H      . GLU   A 1 190 ? -5.27800  6.38300   -2.49600  1.000 59.83000  ? 156 GLU   A H      1 
ATOM   2098 H HA     . GLU   A 1 190 ? -5.39900  4.39400   -0.72000  1.000 62.34000  ? 156 GLU   A HA     1 
ATOM   2099 H HB2    . GLU   A 1 190 ? -3.78200  6.14900   -0.56000  1.000 53.94000  ? 156 GLU   A HB2    1 
ATOM   2100 H HB3    . GLU   A 1 190 ? -4.96000  7.10400   -0.08900  1.000 53.94000  ? 156 GLU   A HB3    1 
ATOM   2101 N N      . ALA   A 1 191 ? -7.82400  6.43600   -0.88700  1.000 57.51000  ? 157 ALA   A N      1 
ATOM   2102 C CA     . ALA   A 1 191 ? -9.16000  6.73000   -0.38300  1.000 63.75000  ? 157 ALA   A CA     1 
ATOM   2103 C C      . ALA   A 1 191 ? -10.25000 5.87200   -1.00900  1.000 67.79000  ? 157 ALA   A C      1 
ATOM   2104 O O      . ALA   A 1 191 ? -11.32400 5.73500   -0.41200  1.000 65.89000  ? 157 ALA   A O      1 
ATOM   2105 C CB     . ALA   A 1 191 ? -9.50400  8.20600   -0.61800  1.000 56.56000  ? 157 ALA   A CB     1 
ATOM   2106 H H      . ALA   A 1 191 ? -7.59700  6.90400   -1.57200  1.000 57.51000  ? 157 ALA   A H      1 
ATOM   2107 H HA     . ALA   A 1 191 ? -9.17400  6.57300   0.57400   1.000 63.75000  ? 157 ALA   A HA     1 
ATOM   2108 H HB1    . ALA   A 1 191 ? -10.39500 8.38000   -0.27600  1.000 56.56000  ? 157 ALA   A HB1    1 
ATOM   2109 H HB2    . ALA   A 1 191 ? -8.85700  8.75900   -0.15300  1.000 56.56000  ? 157 ALA   A HB2    1 
ATOM   2110 H HB3    . ALA   A 1 191 ? -9.47300  8.38900   -1.57000  1.000 56.56000  ? 157 ALA   A HB3    1 
ATOM   2111 N N      . TYR   A 1 192 ? -10.00400 5.30100   -2.18600  1.000 63.31000  ? 158 TYR   A N      1 
ATOM   2112 C CA     . TYR   A 1 192 ? -11.04000 4.67900   -2.99700  1.000 63.37000  ? 158 TYR   A CA     1 
ATOM   2113 C C      . TYR   A 1 192 ? -10.73000 3.20000   -3.17900  1.000 68.55000  ? 158 TYR   A C      1 
ATOM   2114 O O      . TYR   A 1 192 ? -9.72200  2.85400   -3.81700  1.000 63.78000  ? 158 TYR   A O      1 
ATOM   2115 C CB     . TYR   A 1 192 ? -11.15100 5.38300   -4.35100  1.000 64.97000  ? 158 TYR   A CB     1 
ATOM   2116 C CG     . TYR   A 1 192 ? -12.41400 5.05900   -5.10600  1.000 63.18000  ? 158 TYR   A CG     1 
ATOM   2117 C CD1    . TYR   A 1 192 ? -13.64700 5.51600   -4.66000  1.000 63.01000  ? 158 TYR   A CD1    1 
ATOM   2118 C CD2    . TYR   A 1 192 ? -12.37400 4.30800   -6.26900  1.000 49.68000  ? 158 TYR   A CD2    1 
ATOM   2119 C CE1    . TYR   A 1 192 ? -14.80400 5.22300   -5.34800  1.000 65.76000  ? 158 TYR   A CE1    1 
ATOM   2120 C CE2    . TYR   A 1 192 ? -13.52300 4.01200   -6.96400  1.000 52.91000  ? 158 TYR   A CE2    1 
ATOM   2121 C CZ     . TYR   A 1 192 ? -14.73700 4.46800   -6.50200  1.000 56.17000  ? 158 TYR   A CZ     1 
ATOM   2122 O OH     . TYR   A 1 192 ? -15.88700 4.16300   -7.19600  1.000 54.39000  ? 158 TYR   A OH     1 
ATOM   2123 H H      . TYR   A 1 192 ? -9.22300  5.26200   -2.54300  1.000 63.31000  ? 158 TYR   A H      1 
ATOM   2124 H HA     . TYR   A 1 192 ? -11.88900 4.78900   -2.55000  1.000 63.37000  ? 158 TYR   A HA     1 
ATOM   2125 H HB2    . TYR   A 1 192 ? -11.12900 6.34200   -4.20700  1.000 64.97000  ? 158 TYR   A HB2    1 
ATOM   2126 H HB3    . TYR   A 1 192 ? -10.39900 5.11700   -4.90300  1.000 64.97000  ? 158 TYR   A HB3    1 
ATOM   2127 H HD1    . TYR   A 1 192 ? -13.69600 6.01900   -3.88100  1.000 63.01000  ? 158 TYR   A HD1    1 
ATOM   2128 H HD2    . TYR   A 1 192 ? -11.55600 3.99600   -6.58400  1.000 49.68000  ? 158 TYR   A HD2    1 
ATOM   2129 H HE1    . TYR   A 1 192 ? -15.62500 5.52900   -5.03600  1.000 65.76000  ? 158 TYR   A HE1    1 
ATOM   2130 H HE2    . TYR   A 1 192 ? -13.48100 3.50300   -7.74100  1.000 52.91000  ? 158 TYR   A HE2    1 
ATOM   2131 H HH     . TYR   A 1 192 ? -15.70000 3.70200   -7.87300  1.000 54.39000  ? 158 TYR   A HH     1 
ATOM   2132 N N      . PRO   A 1 193 ? -11.55900 2.29500   -2.65400  1.000 68.70000  ? 159 PRO   A N      1 
ATOM   2133 C CA     . PRO   A 1 193 ? -11.21600 0.86600   -2.71000  1.000 65.35000  ? 159 PRO   A CA     1 
ATOM   2134 C C      . PRO   A 1 193 ? -11.45200 0.23000   -4.06400  1.000 69.99000  ? 159 PRO   A C      1 
ATOM   2135 O O      . PRO   A 1 193 ? -10.86500 -0.82600  -4.34800  1.000 74.19000  ? 159 PRO   A O      1 
ATOM   2136 C CB     . PRO   A 1 193 ? -12.12700 0.24100   -1.63600  1.000 73.82000  ? 159 PRO   A CB     1 
ATOM   2137 C CG     . PRO   A 1 193 ? -13.19200 1.28500   -1.32800  1.000 65.90000  ? 159 PRO   A CG     1 
ATOM   2138 C CD     . PRO   A 1 193 ? -12.90900 2.53200   -2.12100  1.000 69.06000  ? 159 PRO   A CD     1 
ATOM   2139 H HA     . PRO   A 1 193 ? -10.28900 0.73500   -2.45500  1.000 65.35000  ? 159 PRO   A HA     1 
ATOM   2140 H HB2    . PRO   A 1 193 ? -12.53400 -0.56700  -1.98600  1.000 73.82000  ? 159 PRO   A HB2    1 
ATOM   2141 H HB3    . PRO   A 1 193 ? -11.60500 0.04300   -0.84300  1.000 73.82000  ? 159 PRO   A HB3    1 
ATOM   2142 H HG2    . PRO   A 1 193 ? -14.06100 0.92900   -1.57100  1.000 65.90000  ? 159 PRO   A HG2    1 
ATOM   2143 H HG3    . PRO   A 1 193 ? -13.17100 1.48500   -0.37900  1.000 65.90000  ? 159 PRO   A HG3    1 
ATOM   2144 H HD2    . PRO   A 1 193 ? -13.54900 2.62800   -2.84400  1.000 69.06000  ? 159 PRO   A HD2    1 
ATOM   2145 H HD3    . PRO   A 1 193 ? -12.92100 3.29900   -1.52900  1.000 69.06000  ? 159 PRO   A HD3    1 
ATOM   2146 N N      . HIS   A 1 194 ? -12.24400 0.84500   -4.90700  1.000 63.96000  ? 160 HIS   A N      1 
ATOM   2147 C CA     . HIS   A 1 194 ? -12.61500 0.21100   -6.15200  1.000 58.56000  ? 160 HIS   A CA     1 
ATOM   2148 C C      . HIS   A 1 194 ? -11.72100 0.67100   -7.28500  1.000 55.20000  ? 160 HIS   A C      1 
ATOM   2149 O O      . HIS   A 1 194 ? -10.98400 1.65100   -7.16600  1.000 49.88000  ? 160 HIS   A O      1 
ATOM   2150 C CB     . HIS   A 1 194 ? -14.07200 0.52400   -6.48900  1.000 58.65000  ? 160 HIS   A CB     1 
ATOM   2151 C CG     . HIS   A 1 194 ? -15.01100 0.28600   -5.35100  1.000 68.11000  ? 160 HIS   A CG     1 
ATOM   2152 N ND1    . HIS   A 1 194 ? -15.26000 -0.97200  -4.84600  1.000 63.47000  ? 160 HIS   A ND1    1 
ATOM   2153 C CD2    . HIS   A 1 194 ? -15.75500 1.14300   -4.61500  1.000 62.34000  ? 160 HIS   A CD2    1 
ATOM   2154 C CE1    . HIS   A 1 194 ? -16.12200 -0.87900  -3.85000  1.000 66.43000  ? 160 HIS   A CE1    1 
ATOM   2155 N NE2    . HIS   A 1 194 ? -16.43900 0.39300   -3.69000  1.000 63.00000  ? 160 HIS   A NE2    1 
ATOM   2156 H H      . HIS   A 1 194 ? -12.58200 1.62700   -4.78700  1.000 63.96000  ? 160 HIS   A H      1 
ATOM   2157 H HA     . HIS   A 1 194 ? -12.52800 -0.74600  -6.04100  1.000 58.56000  ? 160 HIS   A HA     1 
ATOM   2158 H HB2    . HIS   A 1 194 ? -14.14600 1.45400   -6.74500  1.000 58.65000  ? 160 HIS   A HB2    1 
ATOM   2159 H HB3    . HIS   A 1 194 ? -14.35300 -0.04200  -7.22500  1.000 58.65000  ? 160 HIS   A HB3    1 
ATOM   2160 H HD2    . HIS   A 1 194 ? -15.79800 2.06600   -4.71900  1.000 62.34000  ? 160 HIS   A HD2    1 
ATOM   2161 H HE1    . HIS   A 1 194 ? -16.45000 -1.58900  -3.34700  1.000 66.43000  ? 160 HIS   A HE1    1 
ATOM   2162 H HE2    . HIS   A 1 194 ? -16.98400 0.70200   -3.10100  1.000 63.00000  ? 160 HIS   A HE2    1 
ATOM   2163 N N      . PRO   A 1 195 ? -11.75000 -0.04400  -8.39300  1.000 53.15000  ? 161 PRO   A N      1 
ATOM   2164 C CA     . PRO   A 1 195 ? -11.06000 0.41900   -9.59500  1.000 44.48000  ? 161 PRO   A CA     1 
ATOM   2165 C C      . PRO   A 1 195 ? -11.71200 1.68600   -10.13600 1.000 46.03000  ? 161 PRO   A C      1 
ATOM   2166 O O      . PRO   A 1 195 ? -12.88200 1.98700   -9.87000  1.000 41.62000  ? 161 PRO   A O      1 
ATOM   2167 C CB     . PRO   A 1 195 ? -11.21700 -0.76100  -10.56000 1.000 46.72000  ? 161 PRO   A CB     1 
ATOM   2168 C CG     . PRO   A 1 195 ? -11.53500 -1.96700  -9.61600  1.000 42.58000  ? 161 PRO   A CG     1 
ATOM   2169 C CD     . PRO   A 1 195 ? -12.37500 -1.36200  -8.56600  1.000 45.01000  ? 161 PRO   A CD     1 
ATOM   2170 H HA     . PRO   A 1 195 ? -10.12000 0.57800   -9.41600  1.000 44.48000  ? 161 PRO   A HA     1 
ATOM   2171 H HB2    . PRO   A 1 195 ? -11.94600 -0.59500  -11.17800 1.000 46.72000  ? 161 PRO   A HB2    1 
ATOM   2172 H HB3    . PRO   A 1 195 ? -10.38400 -0.89500  -11.02500 1.000 46.72000  ? 161 PRO   A HB3    1 
ATOM   2173 H HG2    . PRO   A 1 195 ? -12.02300 -2.64900  -10.10300 1.000 42.58000  ? 161 PRO   A HG2    1 
ATOM   2174 H HG3    . PRO   A 1 195 ? -10.71300 -2.32300  -9.24300  1.000 42.58000  ? 161 PRO   A HG3    1 
ATOM   2175 H HD2    . PRO   A 1 195 ? -13.29100 -1.27000  -8.87300  1.000 45.01000  ? 161 PRO   A HD2    1 
ATOM   2176 H HD3    . PRO   A 1 195 ? -12.31700 -1.89500  -7.75900  1.000 45.01000  ? 161 PRO   A HD3    1 
ATOM   2177 N N      . PHE   A 1 196 ? -10.91300 2.45500   -10.87700 1.000 41.16000  ? 162 PHE   A N      1 
ATOM   2178 C CA     . PHE   A 1 196 ? -11.40800 3.67500   -11.50300 1.000 37.69000  ? 162 PHE   A CA     1 
ATOM   2179 C C      . PHE   A 1 196 ? -10.61800 3.93000   -12.78600 1.000 36.76000  ? 162 PHE   A C      1 
ATOM   2180 O O      . PHE   A 1 196 ? -9.63000  3.25800   -13.07800 1.000 37.22000  ? 162 PHE   A O      1 
ATOM   2181 C CB     . PHE   A 1 196 ? -11.34800 4.86700   -10.53000 1.000 36.23000  ? 162 PHE   A CB     1 
ATOM   2182 C CG     . PHE   A 1 196 ? -9.94800  5.23600   -10.07100 1.000 43.12000  ? 162 PHE   A CG     1 
ATOM   2183 C CD1    . PHE   A 1 196 ? -9.31200  4.50900   -9.06600  1.000 40.05000  ? 162 PHE   A CD1    1 
ATOM   2184 C CD2    . PHE   A 1 196 ? -9.29700  6.34900   -10.60200 1.000 38.79000  ? 162 PHE   A CD2    1 
ATOM   2185 C CE1    . PHE   A 1 196 ? -8.03700  4.84700   -8.62300  1.000 38.55000  ? 162 PHE   A CE1    1 
ATOM   2186 C CE2    . PHE   A 1 196 ? -8.01700  6.70600   -10.15900 1.000 39.38000  ? 162 PHE   A CE2    1 
ATOM   2187 C CZ     . PHE   A 1 196 ? -7.38700  5.94700   -9.16700  1.000 43.94000  ? 162 PHE   A CZ     1 
ATOM   2188 H H      . PHE   A 1 196 ? -10.08300 2.29100   -11.03100 1.000 41.16000  ? 162 PHE   A H      1 
ATOM   2189 H HA     . PHE   A 1 196 ? -12.33700 3.54400   -11.75000 1.000 37.69000  ? 162 PHE   A HA     1 
ATOM   2190 H HB2    . PHE   A 1 196 ? -11.72900 5.64400   -10.96800 1.000 36.23000  ? 162 PHE   A HB2    1 
ATOM   2191 H HB3    . PHE   A 1 196 ? -11.86800 4.64900   -9.74100  1.000 36.23000  ? 162 PHE   A HB3    1 
ATOM   2192 H HD1    . PHE   A 1 196 ? -9.73900  3.76900   -8.70000  1.000 40.05000  ? 162 PHE   A HD1    1 
ATOM   2193 H HD2    . PHE   A 1 196 ? -9.71200  6.85300   -11.26400 1.000 38.79000  ? 162 PHE   A HD2    1 
ATOM   2194 H HE1    . PHE   A 1 196 ? -7.62400  4.34200   -7.96000  1.000 38.55000  ? 162 PHE   A HE1    1 
ATOM   2195 H HE2    . PHE   A 1 196 ? -7.58400  7.44100   -10.52900 1.000 39.38000  ? 162 PHE   A HE2    1 
ATOM   2196 H HZ     . PHE   A 1 196 ? -6.53600  6.17900   -8.87200  1.000 43.94000  ? 162 PHE   A HZ     1 
ATOM   2197 N N      . GLY   A 1 197 ? -11.07700 4.90400   -13.57800 1.000 36.72000  ? 163 GLY   A N      1 
ATOM   2198 C CA     . GLY   A 1 197 ? -10.37100 5.31300   -14.77300 1.000 34.02000  ? 163 GLY   A CA     1 
ATOM   2199 C C      . GLY   A 1 197 ? -9.98900  6.78500   -14.67700 1.000 35.22000  ? 163 GLY   A C      1 
ATOM   2200 O O      . GLY   A 1 197 ? -10.42500 7.50300   -13.76100 1.000 36.08000  ? 163 GLY   A O      1 
ATOM   2201 H H      . GLY   A 1 197 ? -11.80300 5.34200   -13.43500 1.000 36.72000  ? 163 GLY   A H      1 
ATOM   2202 H HA2    . GLY   A 1 197 ? -9.55700  4.79400   -14.86100 1.000 34.02000  ? 163 GLY   A HA2    1 
ATOM   2203 H HA3    . GLY   A 1 197 ? -10.90000 5.18200   -15.56100 1.000 34.02000  ? 163 GLY   A HA3    1 
ATOM   2204 N N      . VAL   A 1 198 ? -9.15200  7.22800   -15.61900 1.000 32.82000  ? 164 VAL   A N      1 
ATOM   2205 C CA     . VAL   A 1 198 ? -8.71400  8.62600   -15.66900 1.000 32.35000  ? 164 VAL   A CA     1 
ATOM   2206 C C      . VAL   A 1 198 ? -8.97200  9.18000   -17.06400 1.000 35.29000  ? 164 VAL   A C      1 
ATOM   2207 O O      . VAL   A 1 198 ? -8.70300  8.51400   -18.06800 1.000 35.44000  ? 164 VAL   A O      1 
ATOM   2208 C CB     . VAL   A 1 198 ? -7.22500  8.77800   -15.29000 1.000 36.97000  ? 164 VAL   A CB     1 
ATOM   2209 C CG1    . VAL   A 1 198 ? -6.99500  8.31100   -13.86300 1.000 36.07000  ? 164 VAL   A CG1    1 
ATOM   2210 C CG2    . VAL   A 1 198 ? -6.35500  7.98900   -16.25400 1.000 43.85000  ? 164 VAL   A CG2    1 
ATOM   2211 H H      . VAL   A 1 198 ? -8.82300  6.73700   -16.24300 1.000 32.82000  ? 164 VAL   A H      1 
ATOM   2212 H HA     . VAL   A 1 198 ? -9.23700  9.14700   -15.04000 1.000 32.35000  ? 164 VAL   A HA     1 
ATOM   2213 H HB     . VAL   A 1 198 ? -6.97300  9.71300   -15.34900 1.000 36.97000  ? 164 VAL   A HB     1 
ATOM   2214 H HG11   . VAL   A 1 198 ? -6.04800  8.36600   -13.66400 1.000 36.07000  ? 164 VAL   A HG11   1 
ATOM   2215 H HG12   . VAL   A 1 198 ? -7.49400  8.88300   -13.25900 1.000 36.07000  ? 164 VAL   A HG12   1 
ATOM   2216 H HG13   . VAL   A 1 198 ? -7.29800  7.39300   -13.77800 1.000 36.07000  ? 164 VAL   A HG13   1 
ATOM   2217 H HG21   . VAL   A 1 198 ? -5.44200  7.99200   -15.92600 1.000 43.85000  ? 164 VAL   A HG21   1 
ATOM   2218 H HG22   . VAL   A 1 198 ? -6.68300  7.07800   -16.30500 1.000 43.85000  ? 164 VAL   A HG22   1 
ATOM   2219 H HG23   . VAL   A 1 198 ? -6.39200  8.40400   -17.13000 1.000 43.85000  ? 164 VAL   A HG23   1 
ATOM   2220 N N      . LYS   A 1 199 ? -9.48200  10.41400  -17.12300 1.000 36.73000  ? 165 LYS   A N      1 
ATOM   2221 C CA     . LYS   A 1 199 ? -9.65500  11.13400  -18.38200 1.000 33.95000  ? 165 LYS   A CA     1 
ATOM   2222 C C      . LYS   A 1 199 ? -8.41600  12.00800  -18.59800 1.000 33.54000  ? 165 LYS   A C      1 
ATOM   2223 O O      . LYS   A 1 199 ? -8.12700  12.89700  -17.79000 1.000 34.16000  ? 165 LYS   A O      1 
ATOM   2224 C CB     . LYS   A 1 199 ? -10.93800 11.97900  -18.34100 1.000 34.83000  ? 165 LYS   A CB     1 
ATOM   2225 C CG     . LYS   A 1 199 ? -11.28000 12.81200  -19.60200 1.000 35.10000  ? 165 LYS   A CG     1 
ATOM   2226 C CD     . LYS   A 1 199 ? -11.95400 11.99400  -20.70400 1.000 36.52000  ? 165 LYS   A CD     1 
ATOM   2227 C CE     . LYS   A 1 199 ? -12.62200 12.90400  -21.77700 1.000 39.23000  ? 165 LYS   A CE     1 
ATOM   2228 N NZ     . LYS   A 1 199 ? -13.89900 13.57900  -21.33200 1.000 32.61000  ? 165 LYS   A NZ     1 
ATOM   2229 H H      . LYS   A 1 199 ? -9.73900  10.86000  -16.43400 1.000 36.73000  ? 165 LYS   A H      1 
ATOM   2230 H HA     . LYS   A 1 199 ? -9.72100  10.50300  -19.11500 1.000 33.95000  ? 165 LYS   A HA     1 
ATOM   2231 H HB2    . LYS   A 1 199 ? -11.68600 11.38300  -18.18000 1.000 34.83000  ? 165 LYS   A HB2    1 
ATOM   2232 H HB3    . LYS   A 1 199 ? -10.86300 12.60200  -17.60300 1.000 34.83000  ? 165 LYS   A HB3    1 
ATOM   2233 H HG2    . LYS   A 1 199 ? -11.88500 13.52700  -19.35000 1.000 35.10000  ? 165 LYS   A HG2    1 
ATOM   2234 H HG3    . LYS   A 1 199 ? -10.46200 13.18500  -19.96600 1.000 35.10000  ? 165 LYS   A HG3    1 
ATOM   2235 H HD2    . LYS   A 1 199 ? -11.28600 11.44600  -21.14500 1.000 36.52000  ? 165 LYS   A HD2    1 
ATOM   2236 H HD3    . LYS   A 1 199 ? -12.64100 11.43400  -20.31100 1.000 36.52000  ? 165 LYS   A HD3    1 
ATOM   2237 H HE2    . LYS   A 1 199 ? -11.99400 13.60000  -22.02400 1.000 39.23000  ? 165 LYS   A HE2    1 
ATOM   2238 H HE3    . LYS   A 1 199 ? -12.83100 12.36300  -22.55500 1.000 39.23000  ? 165 LYS   A HE3    1 
ATOM   2239 H HZ1    . LYS   A 1 199 ? -14.21600 14.09200  -21.98700 1.000 32.61000  ? 165 LYS   A HZ1    1 
ATOM   2240 H HZ2    . LYS   A 1 199 ? -14.51000 12.96600  -21.12300 1.000 32.61000  ? 165 LYS   A HZ2    1 
ATOM   2241 H HZ3    . LYS   A 1 199 ? -13.74100 14.08600  -20.61800 1.000 32.61000  ? 165 LYS   A HZ3    1 
ATOM   2242 N N      . MET   A 1 200 ? -7.68000  11.75000  -19.69800 1.000 32.45000  ? 166 MET   A N      1 
ATOM   2243 C CA     . MET   A 1 200 ? -6.40200  12.41400  -19.92300 1.000 29.05000  ? 166 MET   A CA     1 
ATOM   2244 C C      . MET   A 1 200 ? -6.54300  13.56600  -20.91800 1.000 31.19000  ? 166 MET   A C      1 
ATOM   2245 O O      . MET   A 1 200 ? -7.36900  13.51400  -21.83500 1.000 31.31000  ? 166 MET   A O      1 
ATOM   2246 C CB     . MET   A 1 200 ? -5.36600  11.42400  -20.45900 1.000 30.63000  ? 166 MET   A CB     1 
ATOM   2247 C CG     . MET   A 1 200 ? -5.05000  10.28100  -19.46700 1.000 39.31000  ? 166 MET   A CG     1 
ATOM   2248 S SD     . MET   A 1 200 ? -4.34000  10.80600  -17.90200 1.000 40.98000  ? 166 MET   A SD     1 
ATOM   2249 C CE     . MET   A 1 200 ? -2.59700  11.16000  -18.39100 1.000 33.64000  ? 166 MET   A CE     1 
ATOM   2250 H H      . MET   A 1 200 ? -7.90500  11.19800  -20.31800 1.000 32.45000  ? 166 MET   A H      1 
ATOM   2251 H HA     . MET   A 1 200 ? -6.08400  12.74700  -19.07100 1.000 29.05000  ? 166 MET   A HA     1 
ATOM   2252 H HB2    . MET   A 1 200 ? -5.70500  11.02500  -21.27600 1.000 30.63000  ? 166 MET   A HB2    1 
ATOM   2253 H HB3    . MET   A 1 200 ? -4.54000  11.89900  -20.64000 1.000 30.63000  ? 166 MET   A HB3    1 
ATOM   2254 H HG2    . MET   A 1 200 ? -5.87300  9.80800   -19.27000 1.000 39.31000  ? 166 MET   A HG2    1 
ATOM   2255 H HG3    . MET   A 1 200 ? -4.41900  9.67500   -19.88600 1.000 39.31000  ? 166 MET   A HG3    1 
ATOM   2256 H HE1    . MET   A 1 200 ? -2.17300  11.68100  -17.69100 1.000 33.64000  ? 166 MET   A HE1    1 
ATOM   2257 H HE2    . MET   A 1 200 ? -2.12600  10.32100  -18.51300 1.000 33.64000  ? 166 MET   A HE2    1 
ATOM   2258 H HE3    . MET   A 1 200 ? -2.59900  11.66300  -19.22000 1.000 33.64000  ? 166 MET   A HE3    1 
ATOM   2259 N N      . PRO   A 1 201 ? -5.70800  14.58800  -20.76100 1.000 31.69000  ? 167 PRO   A N      1 
ATOM   2260 C CA     . PRO   A 1 201 ? -5.56600  15.60300  -21.80600 1.000 33.27000  ? 167 PRO   A CA     1 
ATOM   2261 C C      . PRO   A 1 201 ? -4.69300  15.07300  -22.92600 1.000 34.76000  ? 167 PRO   A C      1 
ATOM   2262 O O      . PRO   A 1 201 ? -3.96700  14.08500  -22.73100 1.000 32.50000  ? 167 PRO   A O      1 
ATOM   2263 C CB     . PRO   A 1 201 ? -4.88000  16.75400  -21.06100 1.000 34.05000  ? 167 PRO   A CB     1 
ATOM   2264 C CG     . PRO   A 1 201 ? -3.94000  16.02300  -20.10900 1.000 38.66000  ? 167 PRO   A CG     1 
ATOM   2265 C CD     . PRO   A 1 201 ? -4.70400  14.75300  -19.68600 1.000 35.57000  ? 167 PRO   A CD     1 
ATOM   2266 H HA     . PRO   A 1 201 ? -6.43100  15.88300  -22.14300 1.000 33.27000  ? 167 PRO   A HA     1 
ATOM   2267 H HB2    . PRO   A 1 201 ? -4.38400  17.30500  -21.68600 1.000 34.05000  ? 167 PRO   A HB2    1 
ATOM   2268 H HB3    . PRO   A 1 201 ? -5.53400  17.27900  -20.57400 1.000 34.05000  ? 167 PRO   A HB3    1 
ATOM   2269 H HG2    . PRO   A 1 201 ? -3.12000  15.79200  -20.57300 1.000 38.66000  ? 167 PRO   A HG2    1 
ATOM   2270 H HG3    . PRO   A 1 201 ? -3.75300  16.58400  -19.34000 1.000 38.66000  ? 167 PRO   A HG3    1 
ATOM   2271 H HD2    . PRO   A 1 201 ? -4.09600  13.99700  -19.69600 1.000 35.57000  ? 167 PRO   A HD2    1 
ATOM   2272 H HD3    . PRO   A 1 201 ? -5.09600  14.85600  -18.81000 1.000 35.57000  ? 167 PRO   A HD3    1 
ATOM   2273 N N      . PRO   A 1 202 ? -4.73800  15.67700  -24.11600 1.000 34.37000  ? 168 PRO   A N      1 
ATOM   2274 C CA     . PRO   A 1 202 ? -3.83600  15.24200  -25.18800 1.000 30.43000  ? 168 PRO   A CA     1 
ATOM   2275 C C      . PRO   A 1 202 ? -2.37900  15.56600  -24.87300 1.000 32.08000  ? 168 PRO   A C      1 
ATOM   2276 O O      . PRO   A 1 202 ? -2.06600  16.61300  -24.29700 1.000 31.26000  ? 168 PRO   A O      1 
ATOM   2277 C CB     . PRO   A 1 202 ? -4.33500  16.02000  -26.41800 1.000 32.08000  ? 168 PRO   A CB     1 
ATOM   2278 C CG     . PRO   A 1 202 ? -5.11400  17.21100  -25.84400 1.000 31.46000  ? 168 PRO   A CG     1 
ATOM   2279 C CD     . PRO   A 1 202 ? -5.70900  16.70200  -24.56200 1.000 34.84000  ? 168 PRO   A CD     1 
ATOM   2280 H HA     . PRO   A 1 202 ? -3.93000  14.29000  -25.34700 1.000 30.43000  ? 168 PRO   A HA     1 
ATOM   2281 H HB2    . PRO   A 1 202 ? -3.57800  16.32400  -26.94200 1.000 32.08000  ? 168 PRO   A HB2    1 
ATOM   2282 H HB3    . PRO   A 1 202 ? -4.91600  15.45400  -26.95000 1.000 32.08000  ? 168 PRO   A HB3    1 
ATOM   2283 H HG2    . PRO   A 1 202 ? -4.50700  17.94800  -25.67200 1.000 31.46000  ? 168 PRO   A HG2    1 
ATOM   2284 H HG3    . PRO   A 1 202 ? -5.81100  17.47600  -26.46400 1.000 31.46000  ? 168 PRO   A HG3    1 
ATOM   2285 H HD2    . PRO   A 1 202 ? -5.76900  17.41800  -23.91000 1.000 34.84000  ? 168 PRO   A HD2    1 
ATOM   2286 H HD3    . PRO   A 1 202 ? -6.57500  16.29800  -24.72800 1.000 34.84000  ? 168 PRO   A HD3    1 
ATOM   2287 N N      . TYR   A 1 203 ? -1.48100  14.65100  -25.24500 1.000 31.34000  ? 169 TYR   A N      1 
ATOM   2288 C CA     . TYR   A 1 203 ? -0.05900  14.95600  -25.30500 1.000 33.95000  ? 169 TYR   A CA     1 
ATOM   2289 C C      . TYR   A 1 203 ? 0.39400   14.97500  -26.75700 1.000 34.52000  ? 169 TYR   A C      1 
ATOM   2290 O O      . TYR   A 1 203 ? -0.27600  14.44200  -27.65000 1.000 32.24000  ? 169 TYR   A O      1 
ATOM   2291 C CB     . TYR   A 1 203 ? 0.78700   13.95000  -24.50700 1.000 31.29000  ? 169 TYR   A CB     1 
ATOM   2292 C CG     . TYR   A 1 203 ? 0.41100   13.87700  -23.04900 1.000 31.28000  ? 169 TYR   A CG     1 
ATOM   2293 C CD1    . TYR   A 1 203 ? 0.85500   14.83600  -22.13400 1.000 33.55000  ? 169 TYR   A CD1    1 
ATOM   2294 C CD2    . TYR   A 1 203 ? -0.40500  12.84500  -22.57300 1.000 35.50000  ? 169 TYR   A CD2    1 
ATOM   2295 C CE1    . TYR   A 1 203 ? 0.48700   14.75900  -20.78000 1.000 32.90000  ? 169 TYR   A CE1    1 
ATOM   2296 C CE2    . TYR   A 1 203 ? -0.78000  12.78100  -21.23300 1.000 34.29000  ? 169 TYR   A CE2    1 
ATOM   2297 C CZ     . TYR   A 1 203 ? -0.32400  13.71800  -20.34100 1.000 38.47000  ? 169 TYR   A CZ     1 
ATOM   2298 O OH     . TYR   A 1 203 ? -0.69200  13.62100  -19.01700 1.000 39.37000  ? 169 TYR   A OH     1 
ATOM   2299 H H      . TYR   A 1 203 ? -1.67500  13.84300  -25.46800 1.000 31.34000  ? 169 TYR   A H      1 
ATOM   2300 H HA     . TYR   A 1 203 ? 0.09600   15.83800  -24.93200 1.000 33.95000  ? 169 TYR   A HA     1 
ATOM   2301 H HB2    . TYR   A 1 203 ? 0.66800   13.06900  -24.88700 1.000 31.29000  ? 169 TYR   A HB2    1 
ATOM   2302 H HB3    . TYR   A 1 203 ? 1.72000   14.21100  -24.56200 1.000 31.29000  ? 169 TYR   A HB3    1 
ATOM   2303 H HD1    . TYR   A 1 203 ? 1.40000   15.53200  -22.42400 1.000 33.55000  ? 169 TYR   A HD1    1 
ATOM   2304 H HD2    . TYR   A 1 203 ? -0.71900  12.20100  -23.16600 1.000 35.50000  ? 169 TYR   A HD2    1 
ATOM   2305 H HE1    . TYR   A 1 203 ? 0.79200   15.39800  -20.17700 1.000 32.90000  ? 169 TYR   A HE1    1 
ATOM   2306 H HE2    . TYR   A 1 203 ? -1.31600  12.08200  -20.93600 1.000 34.29000  ? 169 TYR   A HE2    1 
ATOM   2307 H HH     . TYR   A 1 203 ? -0.35900  14.25500  -18.57900 1.000 39.37000  ? 169 TYR   A HH     1 
ATOM   2308 N N      . PHE   A 1 204 ? 1.56400   15.58800  -26.97400 1.000 32.26000  ? 170 PHE   A N      1 
ATOM   2309 C CA     . PHE   A 1 204 ? 2.04600   15.90000  -28.30700 1.000 34.10000  ? 170 PHE   A CA     1 
ATOM   2310 C C      . PHE   A 1 204 ? 3.50000   15.50300  -28.53800 1.000 36.67000  ? 170 PHE   A C      1 
ATOM   2311 O O      . PHE   A 1 204 ? 4.08100   15.91300  -29.54800 1.000 32.52000  ? 170 PHE   A O      1 
ATOM   2312 C CB     . PHE   A 1 204 ? 1.84400   17.40900  -28.56500 1.000 30.64000  ? 170 PHE   A CB     1 
ATOM   2313 C CG     . PHE   A 1 204 ? 0.41000   17.83200  -28.43200 1.000 32.89000  ? 170 PHE   A CG     1 
ATOM   2314 C CD1    . PHE   A 1 204 ? -0.47800  17.64900  -29.48400 1.000 29.63000  ? 170 PHE   A CD1    1 
ATOM   2315 C CD2    . PHE   A 1 204 ? -0.07400  18.32300  -27.22900 1.000 28.77000  ? 170 PHE   A CD2    1 
ATOM   2316 C CE1    . PHE   A 1 204 ? -1.82300  17.99300  -29.34300 1.000 28.03000  ? 170 PHE   A CE1    1 
ATOM   2317 C CE2    . PHE   A 1 204 ? -1.41300  18.66900  -27.09000 1.000 29.82000  ? 170 PHE   A CE2    1 
ATOM   2318 C CZ     . PHE   A 1 204 ? -2.27500  18.49900  -28.14300 1.000 30.00000  ? 170 PHE   A CZ     1 
ATOM   2319 H H      . PHE   A 1 204 ? 2.10000   15.83400  -26.34800 1.000 32.26000  ? 170 PHE   A H      1 
ATOM   2320 H HA     . PHE   A 1 204 ? 1.50700   15.41800  -28.95400 1.000 34.10000  ? 170 PHE   A HA     1 
ATOM   2321 H HB2    . PHE   A 1 204 ? 2.36600   17.91300  -27.92100 1.000 30.64000  ? 170 PHE   A HB2    1 
ATOM   2322 H HB3    . PHE   A 1 204 ? 2.13600   17.61800  -29.46600 1.000 30.64000  ? 170 PHE   A HB3    1 
ATOM   2323 H HD1    . PHE   A 1 204 ? -0.17200  17.30300  -30.29100 1.000 29.63000  ? 170 PHE   A HD1    1 
ATOM   2324 H HD2    . PHE   A 1 204 ? 0.50700   18.43500  -26.51100 1.000 28.77000  ? 170 PHE   A HD2    1 
ATOM   2325 H HE1    . PHE   A 1 204 ? -2.41000  17.88500  -30.05600 1.000 28.03000  ? 170 PHE   A HE1    1 
ATOM   2326 H HE2    . PHE   A 1 204 ? -1.72400  19.01300  -26.28400 1.000 29.82000  ? 170 PHE   A HE2    1 
ATOM   2327 H HZ     . PHE   A 1 204 ? -3.16900  18.73900  -28.05100 1.000 30.00000  ? 170 PHE   A HZ     1 
ATOM   2328 N N      . ASP   A 1 205 ? 4.09100   14.68800  -27.66600 1.000 37.99000  ? 171 ASP   A N      1 
ATOM   2329 C CA     . ASP   A 1 205 ? 5.42800   14.15900  -27.91400 1.000 36.66000  ? 171 ASP   A CA     1 
ATOM   2330 C C      . ASP   A 1 205 ? 5.64600   12.92800  -27.04800 1.000 33.90000  ? 171 ASP   A C      1 
ATOM   2331 O O      . ASP   A 1 205 ? 5.03500   12.77900  -25.98400 1.000 35.52000  ? 171 ASP   A O      1 
ATOM   2332 C CB     . ASP   A 1 205 ? 6.51800   15.18400  -27.61000 1.000 42.29000  ? 171 ASP   A CB     1 
ATOM   2333 C CG     . ASP   A 1 205 ? 6.46300   15.66300  -26.18500 1.000 51.35000  ? 171 ASP   A CG     1 
ATOM   2334 O OD1    . ASP   A 1 205 ? 6.87100   14.90000  -25.27200 1.000 55.74000  ? 171 ASP   A OD1    1 
ATOM   2335 O OD2    . ASP   A 1 205 ? 5.97700   16.78800  -25.97100 1.000 67.54000  ? 171 ASP   A OD2    1 
ATOM   2336 H H      . ASP   A 1 205 ? 3.74000   14.42700  -26.92600 1.000 37.99000  ? 171 ASP   A H      1 
ATOM   2337 H HA     . ASP   A 1 205 ? 5.50500   13.89500  -28.84200 1.000 36.66000  ? 171 ASP   A HA     1 
ATOM   2338 H HB2    . ASP   A 1 205 ? 7.38000   14.79000  -27.75400 1.000 42.29000  ? 171 ASP   A HB2    1 
ATOM   2339 H HB3    . ASP   A 1 205 ? 6.40000   15.95100  -28.19000 1.000 42.29000  ? 171 ASP   A HB3    1 
ATOM   2340 N N      . PHE   A 1 206 ? 6.57700   12.07500  -27.50000 1.000 39.57000  ? 172 PHE   A N      1 
ATOM   2341 C CA     . PHE   A 1 206 ? 6.78500   10.77300  -26.86300 1.000 39.63000  ? 172 PHE   A CA     1 
ATOM   2342 C C      . PHE   A 1 206 ? 7.37800   10.89400  -25.45900 1.000 42.34000  ? 172 PHE   A C      1 
ATOM   2343 O O      . PHE   A 1 206 ? 7.16700   10.00800  -24.62700 1.000 42.92000  ? 172 PHE   A O      1 
ATOM   2344 C CB     . PHE   A 1 206 ? 7.67900   9.87800   -27.73700 1.000 35.54000  ? 172 PHE   A CB     1 
ATOM   2345 C CG     . PHE   A 1 206 ? 6.97600   9.28100   -28.95100 1.000 55.32000  ? 172 PHE   A CG     1 
ATOM   2346 C CD1    . PHE   A 1 206 ? 5.86300   9.89600   -29.49900 1.000 52.01000  ? 172 PHE   A CD1    1 
ATOM   2347 C CD2    . PHE   A 1 206 ? 7.45100   8.11300   -29.55300 1.000 62.11000  ? 172 PHE   A CD2    1 
ATOM   2348 C CE1    . PHE   A 1 206 ? 5.21400   9.35900   -30.60900 1.000 50.09000  ? 172 PHE   A CE1    1 
ATOM   2349 C CE2    . PHE   A 1 206 ? 6.81100   7.56500   -30.66800 1.000 59.54000  ? 172 PHE   A CE2    1 
ATOM   2350 C CZ     . PHE   A 1 206 ? 5.68900   8.18800   -31.19600 1.000 58.52000  ? 172 PHE   A CZ     1 
ATOM   2351 H H      . PHE   A 1 206 ? 7.08500   12.22700  -28.15300 1.000 39.57000  ? 172 PHE   A H      1 
ATOM   2352 H HA     . PHE   A 1 206 ? 5.92500   10.33300  -26.77500 1.000 39.63000  ? 172 PHE   A HA     1 
ATOM   2353 H HB2    . PHE   A 1 206 ? 8.45200   10.34700  -28.04500 1.000 35.54000  ? 172 PHE   A HB2    1 
ATOM   2354 H HB3    . PHE   A 1 206 ? 7.96800   9.13100   -27.19000 1.000 35.54000  ? 172 PHE   A HB3    1 
ATOM   2355 H HD1    . PHE   A 1 206 ? 5.53300   10.67400  -29.11400 1.000 52.01000  ? 172 PHE   A HD1    1 
ATOM   2356 H HD2    . PHE   A 1 206 ? 8.19900   7.68800   -29.20000 1.000 62.11000  ? 172 PHE   A HD2    1 
ATOM   2357 H HE1    . PHE   A 1 206 ? 4.46400   9.78300   -30.95900 1.000 50.09000  ? 172 PHE   A HE1    1 
ATOM   2358 H HE2    . PHE   A 1 206 ? 7.13500   6.78400   -31.05400 1.000 59.54000  ? 172 PHE   A HE2    1 
ATOM   2359 H HZ     . PHE   A 1 206 ? 5.26100   7.83000   -31.94000 1.000 58.52000  ? 172 PHE   A HZ     1 
ATOM   2360 N N      . ALA   A 1 207 ? 8.12500   11.95700  -25.16000 1.000 36.30000  ? 173 ALA   A N      1 
ATOM   2361 C CA     . ALA   A 1 207 ? 8.61200   12.09300  -23.79200 1.000 38.92000  ? 173 ALA   A CA     1 
ATOM   2362 C C      . ALA   A 1 207 ? 7.46200   12.29000  -22.81000 1.000 43.30000  ? 173 ALA   A C      1 
ATOM   2363 O O      . ALA   A 1 207 ? 7.51900   11.79600  -21.67900 1.000 39.98000  ? 173 ALA   A O      1 
ATOM   2364 C CB     . ALA   A 1 207 ? 9.62100   13.24100  -23.68800 1.000 42.10000  ? 173 ALA   A CB     1 
ATOM   2365 H H      . ALA   A 1 207 ? 8.35400   12.58400  -25.70200 1.000 36.30000  ? 173 ALA   A H      1 
ATOM   2366 H HA     . ALA   A 1 207 ? 9.07200   11.27500  -23.54500 1.000 38.92000  ? 173 ALA   A HA     1 
ATOM   2367 H HB1    . ALA   A 1 207 ? 9.92800   13.30900  -22.77000 1.000 42.10000  ? 173 ALA   A HB1    1 
ATOM   2368 H HB2    . ALA   A 1 207 ? 10.37100  13.05600  -24.27500 1.000 42.10000  ? 173 ALA   A HB2    1 
ATOM   2369 H HB3    . ALA   A 1 207 ? 9.18800   14.06700  -23.95400 1.000 42.10000  ? 173 ALA   A HB3    1 
ATOM   2370 N N      . HIS   A 1 208 ? 6.40100   12.99600  -23.21500 1.000 33.46000  ? 174 HIS   A N      1 
ATOM   2371 C CA     . HIS   A 1 208 ? 5.25300   13.14200  -22.32500 1.000 38.17000  ? 174 HIS   A CA     1 
ATOM   2372 C C      . HIS   A 1 208 ? 4.42300   11.85400  -22.27000 1.000 32.96000  ? 174 HIS   A C      1 
ATOM   2373 O O      . HIS   A 1 208 ? 3.96200   11.45700  -21.19400 1.000 35.37000  ? 174 HIS   A O      1 
ATOM   2374 C CB     . HIS   A 1 208 ? 4.38700   14.33000  -22.75000 1.000 36.92000  ? 174 HIS   A CB     1 
ATOM   2375 C CG     . HIS   A 1 208 ? 5.01500   15.65700  -22.46200 1.000 41.78000  ? 174 HIS   A CG     1 
ATOM   2376 N ND1    . HIS   A 1 208 ? 6.20000   16.05300  -23.04500 1.000 55.31000  ? 174 HIS   A ND1    1 
ATOM   2377 C CD2    . HIS   A 1 208 ? 4.62400   16.68200  -21.66900 1.000 60.77000  ? 174 HIS   A CD2    1 
ATOM   2378 C CE1    . HIS   A 1 208 ? 6.51400   17.26400  -22.62300 1.000 57.65000  ? 174 HIS   A CE1    1 
ATOM   2379 N NE2    . HIS   A 1 208 ? 5.57200   17.66800  -21.79300 1.000 56.64000  ? 174 HIS   A NE2    1 
ATOM   2380 H H      . HIS   A 1 208 ? 6.32400   13.38800  -23.97700 1.000 33.46000  ? 174 HIS   A H      1 
ATOM   2381 H HA     . HIS   A 1 208 ? 5.57700   13.32100  -21.42800 1.000 38.17000  ? 174 HIS   A HA     1 
ATOM   2382 H HB2    . HIS   A 1 208 ? 4.22600   14.27700  -23.70500 1.000 36.92000  ? 174 HIS   A HB2    1 
ATOM   2383 H HB3    . HIS   A 1 208 ? 3.54600   14.28900  -22.27000 1.000 36.92000  ? 174 HIS   A HB3    1 
ATOM   2384 H HD1    . HIS   A 1 208 ? 6.66200   15.58400  -23.59800 1.000 55.31000  ? 174 HIS   A HD1    1 
ATOM   2385 H HD2    . HIS   A 1 208 ? 3.85600   16.71500  -21.14600 1.000 60.77000  ? 174 HIS   A HD2    1 
ATOM   2386 H HE1    . HIS   A 1 208 ? 7.26800   17.74900  -22.87000 1.000 57.65000  ? 174 HIS   A HE1    1 
ATOM   2387 N N      . PHE   A 1 209 ? 4.20800   11.19700  -23.41100 1.000 33.74000  ? 175 PHE   A N      1 
ATOM   2388 C CA     . PHE   A 1 209 ? 3.55100   9.88900   -23.38200 1.000 36.17000  ? 175 PHE   A CA     1 
ATOM   2389 C C      . PHE   A 1 209 ? 4.25900   8.94200   -22.42000 1.000 40.33000  ? 175 PHE   A C      1 
ATOM   2390 O O      . PHE   A 1 209 ? 3.61900   8.29200   -21.58600 1.000 34.00000  ? 175 PHE   A O      1 
ATOM   2391 C CB     . PHE   A 1 209 ? 3.52000   9.26500   -24.77700 1.000 33.90000  ? 175 PHE   A CB     1 
ATOM   2392 C CG     . PHE   A 1 209 ? 2.55700   9.93400   -25.73300 1.000 40.00000  ? 175 PHE   A CG     1 
ATOM   2393 C CD1    . PHE   A 1 209 ? 1.25300   10.22300  -25.35100 1.000 41.56000  ? 175 PHE   A CD1    1 
ATOM   2394 C CD2    . PHE   A 1 209 ? 2.95800   10.24400  -27.01900 1.000 45.39000  ? 175 PHE   A CD2    1 
ATOM   2395 C CE1    . PHE   A 1 209 ? 0.36900   10.81400  -26.24400 1.000 41.06000  ? 175 PHE   A CE1    1 
ATOM   2396 C CE2    . PHE   A 1 209 ? 2.08500   10.84300  -27.91500 1.000 50.70000  ? 175 PHE   A CE2    1 
ATOM   2397 C CZ     . PHE   A 1 209 ? 0.79600   11.14200  -27.52100 1.000 29.65000  ? 175 PHE   A CZ     1 
ATOM   2398 H H      . PHE   A 1 209 ? 4.42600   11.47700  -24.19400 1.000 33.74000  ? 175 PHE   A H      1 
ATOM   2399 H HA     . PHE   A 1 209 ? 2.63900   9.99900   -23.07100 1.000 36.17000  ? 175 PHE   A HA     1 
ATOM   2400 H HB2    . PHE   A 1 209 ? 4.40800   9.32300   -25.16400 1.000 33.90000  ? 175 PHE   A HB2    1 
ATOM   2401 H HB3    . PHE   A 1 209 ? 3.25700   8.33500   -24.69600 1.000 33.90000  ? 175 PHE   A HB3    1 
ATOM   2402 H HD1    . PHE   A 1 209 ? 0.96700   10.01200  -24.49200 1.000 41.56000  ? 175 PHE   A HD1    1 
ATOM   2403 H HD2    . PHE   A 1 209 ? 3.82800   10.05300  -27.28600 1.000 45.39000  ? 175 PHE   A HD2    1 
ATOM   2404 H HE1    . PHE   A 1 209 ? -0.49900  11.01500  -25.97700 1.000 41.06000  ? 175 PHE   A HE1    1 
ATOM   2405 H HE2    . PHE   A 1 209 ? 2.37100   11.05500  -28.77400 1.000 50.70000  ? 175 PHE   A HE2    1 
ATOM   2406 H HZ     . PHE   A 1 209 ? 0.20600   11.53800  -28.12100 1.000 29.65000  ? 175 PHE   A HZ     1 
ATOM   2407 N N      . ASP   A 1 210 ? 5.59000   8.83900   -22.55000 1.000 38.43000  ? 176 ASP   A N      1 
ATOM   2408 C CA     . ASP   A 1 210 ? 6.38100   7.91500   -21.73200 1.000 41.45000  ? 176 ASP   A CA     1 
ATOM   2409 C C      . ASP   A 1 210 ? 6.29700   8.25700   -20.25500 1.000 43.74000  ? 176 ASP   A C      1 
ATOM   2410 O O      . ASP   A 1 210 ? 6.20600   7.35900   -19.40400 1.000 40.76000  ? 176 ASP   A O      1 
ATOM   2411 C CB     . ASP   A 1 210 ? 7.84500   7.92100   -22.17300 1.000 41.40000  ? 176 ASP   A CB     1 
ATOM   2412 C CG     . ASP   A 1 210 ? 8.06200   7.19900   -23.47600 1.000 46.04000  ? 176 ASP   A CG     1 
ATOM   2413 O OD1    . ASP   A 1 210 ? 7.18300   6.40100   -23.86100 1.000 47.36000  ? 176 ASP   A OD1    1 
ATOM   2414 O OD2    . ASP   A 1 210 ? 9.11600   7.40800   -24.11700 1.000 44.04000  ? 176 ASP   A OD2    1 
ATOM   2415 H H      . ASP   A 1 210 ? 6.05700   9.29700   -23.10800 1.000 38.43000  ? 176 ASP   A H      1 
ATOM   2416 H HA     . ASP   A 1 210 ? 6.03500   7.01700   -21.84800 1.000 41.45000  ? 176 ASP   A HA     1 
ATOM   2417 H HB2    . ASP   A 1 210 ? 8.13700   8.83900   -22.28600 1.000 41.40000  ? 176 ASP   A HB2    1 
ATOM   2418 H HB3    . ASP   A 1 210 ? 8.38200   7.48300   -21.49400 1.000 41.40000  ? 176 ASP   A HB3    1 
ATOM   2419 N N      . ALA   A 1 211 ? 6.34400   9.54600   -19.92500 1.000 35.37000  ? 177 ALA   A N      1 
ATOM   2420 C CA     . ALA   A 1 211 ? 6.27700   9.94300   -18.52700 1.000 38.35000  ? 177 ALA   A CA     1 
ATOM   2421 C C      . ALA   A 1 211 ? 4.88500   9.71300   -17.95900 1.000 39.30000  ? 177 ALA   A C      1 
ATOM   2422 O O      . ALA   A 1 211 ? 4.74100   9.21900   -16.83700 1.000 38.95000  ? 177 ALA   A O      1 
ATOM   2423 C CB     . ALA   A 1 211 ? 6.69400   11.40500  -18.38500 1.000 43.15000  ? 177 ALA   A CB     1 
ATOM   2424 H H      . ALA   A 1 211 ? 6.41300   10.19700  -20.48200 1.000 35.37000  ? 177 ALA   A H      1 
ATOM   2425 H HA     . ALA   A 1 211 ? 6.90100   9.40300   -18.01600 1.000 38.35000  ? 177 ALA   A HA     1 
ATOM   2426 H HB1    . ALA   A 1 211 ? 6.64500   11.65700  -17.45000 1.000 43.15000  ? 177 ALA   A HB1    1 
ATOM   2427 H HB2    . ALA   A 1 211 ? 7.60300   11.50700  -18.70900 1.000 43.15000  ? 177 ALA   A HB2    1 
ATOM   2428 H HB3    . ALA   A 1 211 ? 6.09200   11.95700  -18.90900 1.000 43.15000  ? 177 ALA   A HB3    1 
ATOM   2429 N N      . ALA   A 1 212 ? 3.84600   10.06000  -18.71900 1.000 32.60000  ? 178 ALA   A N      1 
ATOM   2430 C CA     . ALA   A 1 212 ? 2.48200   9.83100   -18.25400 1.000 35.92000  ? 178 ALA   A CA     1 
ATOM   2431 C C      . ALA   A 1 212 ? 2.21700   8.33800   -18.04000 1.000 35.56000  ? 178 ALA   A C      1 
ATOM   2432 O O      . ALA   A 1 212 ? 1.64600   7.94300   -17.01800 1.000 39.74000  ? 178 ALA   A O      1 
ATOM   2433 C CB     . ALA   A 1 212 ? 1.48000   10.42000  -19.25700 1.000 34.36000  ? 178 ALA   A CB     1 
ATOM   2434 H H      . ALA   A 1 212 ? 3.90400   10.42400  -19.49600 1.000 32.60000  ? 178 ALA   A H      1 
ATOM   2435 H HA     . ALA   A 1 212 ? 2.35700   10.28300  -17.40500 1.000 35.92000  ? 178 ALA   A HA     1 
ATOM   2436 H HB1    . ALA   A 1 212 ? 0.57900   10.26000  -18.93400 1.000 34.36000  ? 178 ALA   A HB1    1 
ATOM   2437 H HB2    . ALA   A 1 212 ? 1.63800   11.37400  -19.33800 1.000 34.36000  ? 178 ALA   A HB2    1 
ATOM   2438 H HB3    . ALA   A 1 212 ? 1.60500   9.98900   -20.11700 1.000 34.36000  ? 178 ALA   A HB3    1 
ATOM   2439 N N      . ALA   A 1 213 ? 2.64200   7.49500   -18.98400 1.000 38.69000  ? 179 ALA   A N      1 
ATOM   2440 C CA     . ALA   A 1 213 ? 2.35700   6.06500   -18.86500 1.000 37.70000  ? 179 ALA   A CA     1 
ATOM   2441 C C      . ALA   A 1 213 ? 3.12400   5.44300   -17.70800 1.000 43.30000  ? 179 ALA   A C      1 
ATOM   2442 O O      . ALA   A 1 213 ? 2.59300   4.58200   -16.99800 1.000 41.50000  ? 179 ALA   A O      1 
ATOM   2443 C CB     . ALA   A 1 213 ? 2.69300   5.34400   -20.16400 1.000 36.35000  ? 179 ALA   A CB     1 
ATOM   2444 H H      . ALA   A 1 213 ? 3.08600   7.71900   -19.68600 1.000 38.69000  ? 179 ALA   A H      1 
ATOM   2445 H HA     . ALA   A 1 213 ? 1.41000   5.94600   -18.69400 1.000 37.70000  ? 179 ALA   A HA     1 
ATOM   2446 H HB1    . ALA   A 1 213 ? 2.49600   4.40000   -20.06100 1.000 36.35000  ? 179 ALA   A HB1    1 
ATOM   2447 H HB2    . ALA   A 1 213 ? 2.15600   5.71800   -20.88000 1.000 36.35000  ? 179 ALA   A HB2    1 
ATOM   2448 H HB3    . ALA   A 1 213 ? 3.63500   5.46700   -20.35800 1.000 36.35000  ? 179 ALA   A HB3    1 
ATOM   2449 N N      . GLU   A 1 214 ? 4.38300   5.84400   -17.51700 0.900 37.91000  ? 180 GLU   A N      1 
ATOM   2450 C CA     . GLU   A 1 214 ? 5.15900   5.30600   -16.41100 0.900 39.61000  ? 180 GLU   A CA     1 
ATOM   2451 C C      . GLU   A 1 214 ? 4.50900   5.61500   -15.06200 0.900 41.63000  ? 180 GLU   A C      1 
ATOM   2452 O O      . GLU   A 1 214 ? 4.56000   4.78600   -14.14800 0.900 45.38000  ? 180 GLU   A O      1 
ATOM   2453 C CB     . GLU   A 1 214 ? 6.58400   5.85000   -16.48100 0.900 39.84000  ? 180 GLU   A CB     1 
ATOM   2454 C CG     . GLU   A 1 214 ? 7.17200   6.10100   -15.12800 0.900 60.85000  ? 180 GLU   A CG     1 
ATOM   2455 C CD     . GLU   A 1 214 ? 8.68100   6.12200   -15.15000 0.900 83.44000  ? 180 GLU   A CD     1 
ATOM   2456 O OE1    . GLU   A 1 214 ? 9.26300   6.49800   -16.19300 0.900 83.84000  ? 180 GLU   A OE1    1 
ATOM   2457 O OE2    . GLU   A 1 214 ? 9.28100   5.74700   -14.11800 0.900 94.60000  ? 180 GLU   A OE2    1 
ATOM   2458 H H      . GLU   A 1 214 ? 4.79900   6.41500   -18.00700 0.900 37.91000  ? 180 GLU   A H      1 
ATOM   2459 H HA     . GLU   A 1 214 ? 5.20500   4.34100   -16.50300 0.900 39.61000  ? 180 GLU   A HA     1 
ATOM   2460 H HB2    . GLU   A 1 214 ? 7.14700   5.20500   -16.93800 0.900 39.84000  ? 180 GLU   A HB2    1 
ATOM   2461 H HB3    . GLU   A 1 214 ? 6.58100   6.69000   -16.96600 0.900 39.84000  ? 180 GLU   A HB3    1 
ATOM   2462 H HG2    . GLU   A 1 214 ? 6.86000   6.95600   -14.79200 0.900 60.85000  ? 180 GLU   A HG2    1 
ATOM   2463 H HG3    . GLU   A 1 214 ? 6.92200   5.38700   -14.52200 0.900 60.85000  ? 180 GLU   A HG3    1 
ATOM   2464 N N      . ILE   A 1 215 ? 3.86800   6.78000   -14.92500 1.000 38.14000  ? 181 ILE   A N      1 
ATOM   2465 C CA     . ILE   A 1 215 ? 3.14400   7.10000   -13.69600 1.000 40.20000  ? 181 ILE   A CA     1 
ATOM   2466 C C      . ILE   A 1 215 ? 1.88400   6.24900   -13.57200 1.000 45.91000  ? 181 ILE   A C      1 
ATOM   2467 O O      . ILE   A 1 215 ? 1.59900   5.69700   -12.50200 1.000 41.47000  ? 181 ILE   A O      1 
ATOM   2468 C CB     . ILE   A 1 215 ? 2.80800   8.60100   -13.63700 1.000 37.90000  ? 181 ILE   A CB     1 
ATOM   2469 C CG1    . ILE   A 1 215 ? 4.08700   9.41100   -13.40000 1.000 41.02000  ? 181 ILE   A CG1    1 
ATOM   2470 C CG2    . ILE   A 1 215 ? 1.79400   8.88000   -12.51800 1.000 38.54000  ? 181 ILE   A CG2    1 
ATOM   2471 C CD1    . ILE   A 1 215 ? 3.97100   10.85400  -13.78400 1.000 39.73000  ? 181 ILE   A CD1    1 
ATOM   2472 H H      . ILE   A 1 215 ? 3.83800   7.39600   -15.52500 1.000 38.14000  ? 181 ILE   A H      1 
ATOM   2473 H HA     . ILE   A 1 215 ? 3.71300   6.89600   -12.93800 1.000 40.20000  ? 181 ILE   A HA     1 
ATOM   2474 H HB     . ILE   A 1 215 ? 2.42000   8.86900   -14.48500 1.000 37.90000  ? 181 ILE   A HB     1 
ATOM   2475 H HG12   . ILE   A 1 215 ? 4.31000   9.37300   -12.45700 1.000 41.02000  ? 181 ILE   A HG12   1 
ATOM   2476 H HG13   . ILE   A 1 215 ? 4.80500   9.02200   -13.92300 1.000 41.02000  ? 181 ILE   A HG13   1 
ATOM   2477 H HG21   . ILE   A 1 215 ? 1.81800   9.82500   -12.30000 1.000 38.54000  ? 181 ILE   A HG21   1 
ATOM   2478 H HG22   . ILE   A 1 215 ? 0.90600   8.63600   -12.82400 1.000 38.54000  ? 181 ILE   A HG22   1 
ATOM   2479 H HG23   . ILE   A 1 215 ? 2.03300   8.35600   -11.73700 1.000 38.54000  ? 181 ILE   A HG23   1 
ATOM   2480 H HD11   . ILE   A 1 215 ? 4.83900   11.27500  -13.68100 1.000 39.73000  ? 181 ILE   A HD11   1 
ATOM   2481 H HD12   . ILE   A 1 215 ? 3.68200   10.91200  -14.70800 1.000 39.73000  ? 181 ILE   A HD12   1 
ATOM   2482 H HD13   . ILE   A 1 215 ? 3.32200   11.28500  -13.20600 1.000 39.73000  ? 181 ILE   A HD13   1 
ATOM   2483 N N      . LEU   A 1 216 ? 1.09600   6.15400   -14.64900 1.000 39.87000  ? 182 LEU   A N      1 
ATOM   2484 C CA     . LEU   A 1 216 ? -0.15200  5.39200   -14.58500 1.000 42.18000  ? 182 LEU   A CA     1 
ATOM   2485 C C      . LEU   A 1 216 ? 0.10600   3.91400   -14.31100 1.000 34.94000  ? 182 LEU   A C      1 
ATOM   2486 O O      . LEU   A 1 216 ? -0.67100  3.25600   -13.61000 1.000 41.03000  ? 182 LEU   A O      1 
ATOM   2487 C CB     . LEU   A 1 216 ? -0.94200  5.56000   -15.88500 1.000 38.99000  ? 182 LEU   A CB     1 
ATOM   2488 C CG     . LEU   A 1 216 ? -1.47000  6.96700   -16.18100 1.000 38.53000  ? 182 LEU   A CG     1 
ATOM   2489 C CD1    . LEU   A 1 216 ? -1.83600  7.09400   -17.65400 1.000 39.57000  ? 182 LEU   A CD1    1 
ATOM   2490 C CD2    . LEU   A 1 216 ? -2.64700  7.30100   -15.30800 1.000 42.44000  ? 182 LEU   A CD2    1 
ATOM   2491 H H      . LEU   A 1 216 ? 1.25900   6.51400   -15.41300 1.000 39.87000  ? 182 LEU   A H      1 
ATOM   2492 H HA     . LEU   A 1 216 ? -0.69400  5.73900   -13.85900 1.000 42.18000  ? 182 LEU   A HA     1 
ATOM   2493 H HB2    . LEU   A 1 216 ? -0.36800  5.30600   -16.62400 1.000 38.99000  ? 182 LEU   A HB2    1 
ATOM   2494 H HB3    . LEU   A 1 216 ? -1.70800  4.96600   -15.85400 1.000 38.99000  ? 182 LEU   A HB3    1 
ATOM   2495 H HG     . LEU   A 1 216 ? -0.76900  7.61000   -15.99300 1.000 38.53000  ? 182 LEU   A HG     1 
ATOM   2496 H HD11   . LEU   A 1 216 ? -2.17400  7.98800   -17.81900 1.000 39.57000  ? 182 LEU   A HD11   1 
ATOM   2497 H HD12   . LEU   A 1 216 ? -1.04400  6.93500   -18.19100 1.000 39.57000  ? 182 LEU   A HD12   1 
ATOM   2498 H HD13   . LEU   A 1 216 ? -2.51800  6.43800   -17.86700 1.000 39.57000  ? 182 LEU   A HD13   1 
ATOM   2499 H HD21   . LEU   A 1 216 ? -2.97900  8.18000   -15.54800 1.000 42.44000  ? 182 LEU   A HD21   1 
ATOM   2500 H HD22   . LEU   A 1 216 ? -3.34000  6.63600   -15.44600 1.000 42.44000  ? 182 LEU   A HD22   1 
ATOM   2501 H HD23   . LEU   A 1 216 ? -2.36300  7.29600   -14.38100 1.000 42.44000  ? 182 LEU   A HD23   1 
ATOM   2502 N N      . ASN   A 1 217 ? 1.19200   3.37300   -14.85600 1.000 34.73000  ? 183 ASN   A N      1 
ATOM   2503 C CA     . ASN   A 1 217 ? 1.50200   1.96400   -14.66200 1.000 34.83000  ? 183 ASN   A CA     1 
ATOM   2504 C C      . ASN   A 1 217 ? 1.88800   1.61700   -13.23000 1.000 39.29000  ? 183 ASN   A C      1 
ATOM   2505 O O      . ASN   A 1 217 ? 2.02400   0.42900   -12.92000 1.000 39.53000  ? 183 ASN   A O      1 
ATOM   2506 C CB     . ASN   A 1 217 ? 2.60400   1.56100   -15.62300 1.000 35.26000  ? 183 ASN   A CB     1 
ATOM   2507 C CG     . ASN   A 1 217 ? 2.07700   1.30600   -17.01300 1.000 47.09000  ? 183 ASN   A CG     1 
ATOM   2508 O OD1    . ASN   A 1 217 ? 0.89500   1.00900   -17.18800 1.000 42.10000  ? 183 ASN   A OD1    1 
ATOM   2509 N ND2    . ASN   A 1 217 ? 2.94500   1.40700   -18.00700 1.000 39.43000  ? 183 ASN   A ND2    1 
ATOM   2510 H H      . ASN   A 1 217 ? 1.76100   3.79900   -15.34000 1.000 34.73000  ? 183 ASN   A H      1 
ATOM   2511 H HA     . ASN   A 1 217 ? 0.71300   1.44400   -14.87900 1.000 34.83000  ? 183 ASN   A HA     1 
ATOM   2512 H HB2    . ASN   A 1 217 ? 3.25900   2.27400   -15.67400 1.000 35.26000  ? 183 ASN   A HB2    1 
ATOM   2513 H HB3    . ASN   A 1 217 ? 3.02200   0.74600   -15.30400 1.000 35.26000  ? 183 ASN   A HB3    1 
ATOM   2514 H HD21   . ASN   A 1 217 ? 2.69000   1.26900   -18.81700 1.000 39.43000  ? 183 ASN   A HD21   1 
ATOM   2515 H HD22   . ASN   A 1 217 ? 3.76300   1.61500   -17.84400 1.000 39.43000  ? 183 ASN   A HD22   1 
ATOM   2516 N N      . GLN   A 1 218 ? 2.06400   2.60200   -12.35400 1.000 36.88000  ? 184 GLN   A N      1 
ATOM   2517 C CA     . GLN   A 1 218 ? 2.35800   2.34200   -10.95200 1.000 43.38000  ? 184 GLN   A CA     1 
ATOM   2518 C C      . GLN   A 1 218 ? 1.10600   2.24200   -10.10400 1.000 43.69000  ? 184 GLN   A C      1 
ATOM   2519 O O      . GLN   A 1 218 ? 1.19700   1.92100   -8.91900  1.000 43.52000  ? 184 GLN   A O      1 
ATOM   2520 C CB     . GLN   A 1 218 ? 3.24600   3.44500   -10.37800 1.000 42.51000  ? 184 GLN   A CB     1 
ATOM   2521 C CG     . GLN   A 1 218 ? 4.70600   3.20000   -10.69000 1.000 56.74000  ? 184 GLN   A CG     1 
ATOM   2522 C CD     . GLN   A 1 218 ? 5.51200   4.47600   -10.82500 1.000 66.17000  ? 184 GLN   A CD     1 
ATOM   2523 O OE1    . GLN   A 1 218 ? 5.12700   5.52000   -10.29200 1.000 73.88000  ? 184 GLN   A OE1    1 
ATOM   2524 N NE2    . GLN   A 1 218 ? 6.63200   4.40400   -11.54000 1.000 78.26000  ? 184 GLN   A NE2    1 
ATOM   2525 H H      . GLN   A 1 218 ? 2.01800   3.43800   -12.55000 1.000 36.88000  ? 184 GLN   A H      1 
ATOM   2526 H HA     . GLN   A 1 218 ? 2.83800   1.50200   -10.87900 1.000 43.38000  ? 184 GLN   A HA     1 
ATOM   2527 H HB2    . GLN   A 1 218 ? 2.99000   4.29600   -10.76700 1.000 42.51000  ? 184 GLN   A HB2    1 
ATOM   2528 H HB3    . GLN   A 1 218 ? 3.14100   3.47100   -9.41400  1.000 42.51000  ? 184 GLN   A HB3    1 
ATOM   2529 H HG2    . GLN   A 1 218 ? 5.09700   2.67500   -9.97400  1.000 56.74000  ? 184 GLN   A HG2    1 
ATOM   2530 H HG3    . GLN   A 1 218 ? 4.77100   2.71600   -11.52800 1.000 56.74000  ? 184 GLN   A HG3    1 
ATOM   2531 H HE21   . GLN   A 1 218 ? 6.86700   3.65800   -11.89700 1.000 78.26000  ? 184 GLN   A HE21   1 
ATOM   2532 H HE22   . GLN   A 1 218 ? 7.12200   5.10300   -11.64400 1.000 78.26000  ? 184 GLN   A HE22   1 
ATOM   2533 N N      . PHE   A 1 219 ? -0.06100  2.48700   -10.69000 1.000 35.96000  ? 185 PHE   A N      1 
ATOM   2534 C CA     . PHE   A 1 219 ? -1.33300  2.53700   -9.97600  1.000 32.37000  ? 185 PHE   A CA     1 
ATOM   2535 C C      . PHE   A 1 219 ? -2.26400  1.46300   -10.51900 1.000 40.32000  ? 185 PHE   A C      1 
ATOM   2536 O O      . PHE   A 1 219 ? -3.02400  1.70400   -11.46600 1.000 37.09000  ? 185 PHE   A O      1 
ATOM   2537 C CB     . PHE   A 1 219 ? -1.93700  3.93100   -10.09100 1.000 35.64000  ? 185 PHE   A CB     1 
ATOM   2538 C CG     . PHE   A 1 219 ? -1.12200  4.94200   -9.37600  1.000 43.62000  ? 185 PHE   A CG     1 
ATOM   2539 C CD1    . PHE   A 1 219 ? -1.23500  5.06800   -8.00300  1.000 42.84000  ? 185 PHE   A CD1    1 
ATOM   2540 C CD2    . PHE   A 1 219 ? -0.15800  5.68500   -10.04400 1.000 46.90000  ? 185 PHE   A CD2    1 
ATOM   2541 C CE1    . PHE   A 1 219 ? -0.44900  5.98100   -7.30600  1.000 43.09000  ? 185 PHE   A CE1    1 
ATOM   2542 C CE2    . PHE   A 1 219 ? 0.63800   6.58400   -9.35900  1.000 46.82000  ? 185 PHE   A CE2    1 
ATOM   2543 C CZ     . PHE   A 1 219 ? 0.49100   6.73400   -7.99000  1.000 41.15000  ? 185 PHE   A CZ     1 
ATOM   2544 H H      . PHE   A 1 219 ? -0.14700  2.63300   -11.53300 1.000 35.96000  ? 185 PHE   A H      1 
ATOM   2545 H HA     . PHE   A 1 219 ? -1.17800  2.37300   -9.03400  1.000 32.37000  ? 185 PHE   A HA     1 
ATOM   2546 H HB2    . PHE   A 1 219 ? -1.98200  4.18400   -11.02600 1.000 35.64000  ? 185 PHE   A HB2    1 
ATOM   2547 H HB3    . PHE   A 1 219 ? -2.82600  3.92700   -9.70200  1.000 35.64000  ? 185 PHE   A HB3    1 
ATOM   2548 H HD1    . PHE   A 1 219 ? -1.86800  4.56300   -7.54600  1.000 42.84000  ? 185 PHE   A HD1    1 
ATOM   2549 H HD2    . PHE   A 1 219 ? -0.05800  5.58800   -10.96300 1.000 46.90000  ? 185 PHE   A HD2    1 
ATOM   2550 H HE1    . PHE   A 1 219 ? -0.54600  6.07600   -6.38600  1.000 43.09000  ? 185 PHE   A HE1    1 
ATOM   2551 H HE2    . PHE   A 1 219 ? 1.26400   7.09600   -9.81900  1.000 46.82000  ? 185 PHE   A HE2    1 
ATOM   2552 H HZ     . PHE   A 1 219 ? 1.02000   7.34500   -7.53000  1.000 41.15000  ? 185 PHE   A HZ     1 
ATOM   2553 N N      . PRO   A 1 220 ? -2.24000  0.26500   -9.93800  1.000 40.75000  ? 186 PRO   A N      1 
ATOM   2554 C CA     . PRO   A 1 220 ? -3.07000  -0.83300  -10.47800 1.000 36.38000  ? 186 PRO   A CA     1 
ATOM   2555 C C      . PRO   A 1 220 ? -4.56800  -0.57600  -10.38900 1.000 31.72000  ? 186 PRO   A C      1 
ATOM   2556 O O      . PRO   A 1 220 ? -5.32900  -1.20900  -11.13500 1.000 41.51000  ? 186 PRO   A O      1 
ATOM   2557 C CB     . PRO   A 1 220 ? -2.65500  -2.04900  -9.62400  1.000 38.05000  ? 186 PRO   A CB     1 
ATOM   2558 C CG     . PRO   A 1 220 ? -1.33600  -1.64800  -8.96100  1.000 38.75000  ? 186 PRO   A CG     1 
ATOM   2559 C CD     . PRO   A 1 220 ? -1.34600  -0.15100  -8.84400  1.000 35.01000  ? 186 PRO   A CD     1 
ATOM   2560 H HA     . PRO   A 1 220 ? -2.83400  -1.00200  -11.40300 1.000 36.38000  ? 186 PRO   A HA     1 
ATOM   2561 H HB2    . PRO   A 1 220 ? -3.33500  -2.22500  -8.95500  1.000 38.05000  ? 186 PRO   A HB2    1 
ATOM   2562 H HB3    . PRO   A 1 220 ? -2.52900  -2.82200  -10.19600 1.000 38.05000  ? 186 PRO   A HB3    1 
ATOM   2563 H HG2    . PRO   A 1 220 ? -1.28000  -2.05500  -8.08300  1.000 38.75000  ? 186 PRO   A HG2    1 
ATOM   2564 H HG3    . PRO   A 1 220 ? -0.59500  -1.93900  -9.51600  1.000 38.75000  ? 186 PRO   A HG3    1 
ATOM   2565 H HD2    . PRO   A 1 220 ? -1.70900  0.12000   -7.98600  1.000 35.01000  ? 186 PRO   A HD2    1 
ATOM   2566 H HD3    . PRO   A 1 220 ? -0.45200  0.19800   -8.98100  1.000 35.01000  ? 186 PRO   A HD3    1 
ATOM   2567 N N      . LYS   A 1 221 ? -5.02900  0.31500   -9.50500  1.000 31.57000  ? 187 LYS   A N      1 
ATOM   2568 C CA     . LYS   A 1 221 ? -6.46000  0.61500   -9.45300  1.000 37.06000  ? 187 LYS   A CA     1 
ATOM   2569 C C      . LYS   A 1 221 ? -6.94400  1.40700   -10.65700 1.000 37.66000  ? 187 LYS   A C      1 
ATOM   2570 O O      . LYS   A 1 221 ? -8.15200  1.43300   -10.91900 1.000 37.06000  ? 187 LYS   A O      1 
ATOM   2571 C CB     . LYS   A 1 221 ? -6.80800  1.37400   -8.18200  1.000 40.75000  ? 187 LYS   A CB     1 
ATOM   2572 C CG     . LYS   A 1 221 ? -6.73200  0.49200   -6.95500  1.000 47.17000  ? 187 LYS   A CG     1 
ATOM   2573 C CD     . LYS   A 1 221 ? -7.63900  1.00700   -5.88000  1.000 52.48000  ? 187 LYS   A CD     1 
ATOM   2574 C CE     . LYS   A 1 221 ? -7.24800  0.43300   -4.54200  1.000 57.64000  ? 187 LYS   A CE     1 
ATOM   2575 N NZ     . LYS   A 1 221 ? -7.66700  1.39000   -3.48900  1.000 62.45000  ? 187 LYS   A NZ     1 
ATOM   2576 H H      . LYS   A 1 221 ? -4.54700  0.74800   -8.93900  1.000 31.57000  ? 187 LYS   A H      1 
ATOM   2577 H HA     . LYS   A 1 221 ? -6.95000  -0.22200  -9.44000  1.000 37.06000  ? 187 LYS   A HA     1 
ATOM   2578 H HB2    . LYS   A 1 221 ? -6.18200  2.10600   -8.06700  1.000 40.75000  ? 187 LYS   A HB2    1 
ATOM   2579 H HB3    . LYS   A 1 221 ? -7.71300  1.71600   -8.25300  1.000 40.75000  ? 187 LYS   A HB3    1 
ATOM   2580 H HG2    . LYS   A 1 221 ? -7.01000  -0.40800  -7.18400  1.000 47.17000  ? 187 LYS   A HG2    1 
ATOM   2581 H HG3    . LYS   A 1 221 ? -5.82200  0.49000   -6.62000  1.000 47.17000  ? 187 LYS   A HG3    1 
ATOM   2582 H HD2    . LYS   A 1 221 ? -7.56800  1.97300   -5.83200  1.000 52.48000  ? 187 LYS   A HD2    1 
ATOM   2583 H HD3    . LYS   A 1 221 ? -8.55200  0.74300   -6.07300  1.000 52.48000  ? 187 LYS   A HD3    1 
ATOM   2584 H HE2    . LYS   A 1 221 ? -7.70500  -0.41100  -4.39900  1.000 57.64000  ? 187 LYS   A HE2    1 
ATOM   2585 H HE3    . LYS   A 1 221 ? -6.28600  0.31800   -4.49300  1.000 57.64000  ? 187 LYS   A HE3    1 
ATOM   2586 H HZ1    . LYS   A 1 221 ? -7.45400  1.07100   -2.68600  1.000 62.45000  ? 187 LYS   A HZ1    1 
ATOM   2587 H HZ2    . LYS   A 1 221 ? -7.25700  2.17100   -3.60800  1.000 62.45000  ? 187 LYS   A HZ2    1 
ATOM   2588 H HZ3    . LYS   A 1 221 ? -8.54700  1.51700   -3.52600  1.000 62.45000  ? 187 LYS   A HZ3    1 
ATOM   2589 N N      . VAL   A 1 222 ? -6.04400  2.06200   -11.38400 1.000 36.31000  ? 188 VAL   A N      1 
ATOM   2590 C CA     . VAL   A 1 222 ? -6.42300  2.73100   -12.62900 1.000 37.01000  ? 188 VAL   A CA     1 
ATOM   2591 C C      . VAL   A 1 222 ? -6.59200  1.64500   -13.69000 1.000 33.14000  ? 188 VAL   A C      1 
ATOM   2592 O O      . VAL   A 1 222 ? -5.60500  1.15600   -14.24600 1.000 34.08000  ? 188 VAL   A O      1 
ATOM   2593 C CB     . VAL   A 1 222 ? -5.39300  3.77900   -13.05200 1.000 37.89000  ? 188 VAL   A CB     1 
ATOM   2594 C CG1    . VAL   A 1 222 ? -5.79000  4.38600   -14.40900 1.000 38.59000  ? 188 VAL   A CG1    1 
ATOM   2595 C CG2    . VAL   A 1 222 ? -5.27600  4.85500   -12.00000 1.000 36.95000  ? 188 VAL   A CG2    1 
ATOM   2596 H H      . VAL   A 1 222 ? -5.21100  2.13500   -11.18200 1.000 36.31000  ? 188 VAL   A H      1 
ATOM   2597 H HA     . VAL   A 1 222 ? -7.27600  3.17600   -12.50700 1.000 37.01000  ? 188 VAL   A HA     1 
ATOM   2598 H HB     . VAL   A 1 222 ? -4.52600  3.35500   -13.15100 1.000 37.89000  ? 188 VAL   A HB     1 
ATOM   2599 H HG11   . VAL   A 1 222 ? -5.25700  5.18100   -14.56500 1.000 38.59000  ? 188 VAL   A HG11   1 
ATOM   2600 H HG12   . VAL   A 1 222 ? -5.62400  3.73600   -15.11000 1.000 38.59000  ? 188 VAL   A HG12   1 
ATOM   2601 H HG13   . VAL   A 1 222 ? -6.73100  4.61900   -14.38700 1.000 38.59000  ? 188 VAL   A HG13   1 
ATOM   2602 H HG21   . VAL   A 1 222 ? -4.64300  5.52500   -12.30300 1.000 36.95000  ? 188 VAL   A HG21   1 
ATOM   2603 H HG22   . VAL   A 1 222 ? -6.14700  5.26000   -11.86500 1.000 36.95000  ? 188 VAL   A HG22   1 
ATOM   2604 H HG23   . VAL   A 1 222 ? -4.96400  4.45600   -11.17300 1.000 36.95000  ? 188 VAL   A HG23   1 
ATOM   2605 N N      . GLN   A 1 223 ? -7.84400  1.25700   -13.97300 1.000 33.36000  ? 189 GLN   A N      1 
ATOM   2606 C CA     . GLN   A 1 223 ? -8.11900  0.17800   -14.91900 1.000 34.19000  ? 189 GLN   A CA     1 
ATOM   2607 C C      . GLN   A 1 223 ? -8.43100  0.66800   -16.32200 1.000 34.70000  ? 189 GLN   A C      1 
ATOM   2608 O O      . GLN   A 1 223 ? -8.44600  -0.14500  -17.25800 1.000 33.63000  ? 189 GLN   A O      1 
ATOM   2609 C CB     . GLN   A 1 223 ? -9.26100  -0.70000  -14.36900 1.000 35.67000  ? 189 GLN   A CB     1 
ATOM   2610 C CG     . GLN   A 1 223 ? -8.80900  -1.45400  -13.12700 1.000 41.59000  ? 189 GLN   A CG     1 
ATOM   2611 C CD     . GLN   A 1 223 ? -9.66200  -2.67300  -12.72500 1.000 45.01000  ? 189 GLN   A CD     1 
ATOM   2612 O OE1    . GLN   A 1 223 ? -9.68300  -3.11700  -11.57200 1.000 35.35000  ? 189 GLN   A OE1    1 
ATOM   2613 N NE2    . GLN   A 1 223 ? -10.36100 -3.22400  -13.71000 1.000 44.17000  ? 189 GLN   A NE2    1 
ATOM   2614 H H      . GLN   A 1 223 ? -8.54900  1.60700   -13.62700 1.000 33.36000  ? 189 GLN   A H      1 
ATOM   2615 H HA     . GLN   A 1 223 ? -7.33000  -0.38200  -14.98100 1.000 34.19000  ? 189 GLN   A HA     1 
ATOM   2616 H HB2    . GLN   A 1 223 ? -10.01500 -0.13900  -14.13100 1.000 35.67000  ? 189 GLN   A HB2    1 
ATOM   2617 H HB3    . GLN   A 1 223 ? -9.51100  -1.32900  -15.06000 1.000 35.67000  ? 189 GLN   A HB3    1 
ATOM   2618 H HG2    . GLN   A 1 223 ? -7.91000  -1.78000  -13.28600 1.000 41.59000  ? 189 GLN   A HG2    1 
ATOM   2619 H HG3    . GLN   A 1 223 ? -8.79300  -0.83600  -12.38200 1.000 41.59000  ? 189 GLN   A HG3    1 
ATOM   2620 H HE21   . GLN   A 1 223 ? -10.33400 -2.91000  -14.50600 1.000 44.17000  ? 189 GLN   A HE21   1 
ATOM   2621 H HE22   . GLN   A 1 223 ? -10.85100 -3.90800  -13.54300 1.000 44.17000  ? 189 GLN   A HE22   1 
ATOM   2622 N N      . PHE   A 1 224 ? -8.68700  1.96000   -16.50600 1.000 29.15000  ? 190 PHE   A N      1 
ATOM   2623 C CA     . PHE   A 1 224 ? -8.86700  2.43300   -17.86500 1.000 28.13000  ? 190 PHE   A CA     1 
ATOM   2624 C C      . PHE   A 1 224 ? -8.42700  3.88300   -17.94200 1.000 29.04000  ? 190 PHE   A C      1 
ATOM   2625 O O      . PHE   A 1 224 ? -8.42500  4.61000   -16.94300 1.000 32.82000  ? 190 PHE   A O      1 
ATOM   2626 C CB     . PHE   A 1 224 ? -10.31100 2.30400   -18.38000 1.000 28.17000  ? 190 PHE   A CB     1 
ATOM   2627 C CG     . PHE   A 1 224 ? -11.31000 3.17300   -17.67300 1.000 35.34000  ? 190 PHE   A CG     1 
ATOM   2628 C CD1    . PHE   A 1 224 ? -11.98300 2.71200   -16.54700 1.000 41.06000  ? 190 PHE   A CD1    1 
ATOM   2629 C CD2    . PHE   A 1 224 ? -11.63500 4.42900   -18.16900 1.000 36.40000  ? 190 PHE   A CD2    1 
ATOM   2630 C CE1    . PHE   A 1 224 ? -12.93800 3.50100   -15.90800 1.000 39.96000  ? 190 PHE   A CE1    1 
ATOM   2631 C CE2    . PHE   A 1 224 ? -12.58600 5.21500   -17.53300 1.000 36.83000  ? 190 PHE   A CE2    1 
ATOM   2632 C CZ     . PHE   A 1 224 ? -13.24600 4.75600   -16.40200 1.000 38.44000  ? 190 PHE   A CZ     1 
ATOM   2633 H H      . PHE   A 1 224 ? -8.75800  2.55600   -15.89000 1.000 29.15000  ? 190 PHE   A H      1 
ATOM   2634 H HA     . PHE   A 1 224 ? -8.29300  1.91600   -18.44700 1.000 28.13000  ? 190 PHE   A HA     1 
ATOM   2635 H HB2    . PHE   A 1 224 ? -10.32700 2.54400   -19.32000 1.000 28.17000  ? 190 PHE   A HB2    1 
ATOM   2636 H HB3    . PHE   A 1 224 ? -10.59600 1.38300   -18.27400 1.000 28.17000  ? 190 PHE   A HB3    1 
ATOM   2637 H HD1    . PHE   A 1 224 ? -11.78600 1.86800   -16.21000 1.000 41.06000  ? 190 PHE   A HD1    1 
ATOM   2638 H HD2    . PHE   A 1 224 ? -11.20500 4.75000   -18.92900 1.000 36.40000  ? 190 PHE   A HD2    1 
ATOM   2639 H HE1    . PHE   A 1 224 ? -13.37000 3.18200   -15.14900 1.000 39.96000  ? 190 PHE   A HE1    1 
ATOM   2640 H HE2    . PHE   A 1 224 ? -12.78400 6.05900   -17.87000 1.000 36.83000  ? 190 PHE   A HE2    1 
ATOM   2641 H HZ     . PHE   A 1 224 ? -13.87700 5.28900   -15.97500 1.000 38.44000  ? 190 PHE   A HZ     1 
ATOM   2642 N N      . ILE   A 1 225 ? -8.03100  4.26200   -19.15000 1.000 32.59000  ? 191 ILE   A N      1 
ATOM   2643 C CA     . ILE   A 1 225 ? -7.53500  5.59500   -19.47700 1.000 29.80000  ? 191 ILE   A CA     1 
ATOM   2644 C C      . ILE   A 1 225 ? -8.39400  6.08900   -20.62600 1.000 32.05000  ? 191 ILE   A C      1 
ATOM   2645 O O      . ILE   A 1 225 ? -8.48200  5.40200   -21.64500 1.000 29.77000  ? 191 ILE   A O      1 
ATOM   2646 C CB     . ILE   A 1 225 ? -6.05600  5.52600   -19.91000 1.000 34.67000  ? 191 ILE   A CB     1 
ATOM   2647 C CG1    . ILE   A 1 225 ? -5.18900  4.86800   -18.82700 1.000 31.65000  ? 191 ILE   A CG1    1 
ATOM   2648 C CG2    . ILE   A 1 225 ? -5.51200  6.89100   -20.32700 1.000 37.16000  ? 191 ILE   A CG2    1 
ATOM   2649 C CD1    . ILE   A 1 225 ? -3.83900  4.36900   -19.36800 1.000 40.27000  ? 191 ILE   A CD1    1 
ATOM   2650 H H      . ILE   A 1 225 ? -8.04100  3.73700   -19.83100 1.000 32.59000  ? 191 ILE   A H      1 
ATOM   2651 H HA     . ILE   A 1 225 ? -7.62700  6.19200   -18.71800 1.000 29.80000  ? 191 ILE   A HA     1 
ATOM   2652 H HB     . ILE   A 1 225 ? -6.01600  4.95400   -20.69200 1.000 34.67000  ? 191 ILE   A HB     1 
ATOM   2653 H HG12   . ILE   A 1 225 ? -5.01000  5.51800   -18.12900 1.000 31.65000  ? 191 ILE   A HG12   1 
ATOM   2654 H HG13   . ILE   A 1 225 ? -5.65800  4.10500   -18.45600 1.000 31.65000  ? 191 ILE   A HG13   1 
ATOM   2655 H HG21   . ILE   A 1 225 ? -4.56800  6.81100   -20.53300 1.000 37.16000  ? 191 ILE   A HG21   1 
ATOM   2656 H HG22   . ILE   A 1 225 ? -5.99300  7.19900   -21.11100 1.000 37.16000  ? 191 ILE   A HG22   1 
ATOM   2657 H HG23   . ILE   A 1 225 ? -5.63800  7.51500   -19.59500 1.000 37.16000  ? 191 ILE   A HG23   1 
ATOM   2658 H HD11   . ILE   A 1 225 ? -3.21700  4.28600   -18.62900 1.000 40.27000  ? 191 ILE   A HD11   1 
ATOM   2659 H HD12   . ILE   A 1 225 ? -3.96800  3.50500   -19.79000 1.000 40.27000  ? 191 ILE   A HD12   1 
ATOM   2660 H HD13   . ILE   A 1 225 ? -3.49600  5.00500   -20.01400 1.000 40.27000  ? 191 ILE   A HD13   1 
ATOM   2661 N N      . THR   A 1 226 ? -9.01200  7.27100   -20.48300 1.000 32.24000  ? 192 THR   A N      1 
ATOM   2662 C CA     . THR   A 1 226 ? -9.80900  7.85900   -21.56000 1.000 32.20000  ? 192 THR   A CA     1 
ATOM   2663 C C      . THR   A 1 226 ? -8.99700  8.95200   -22.26000 1.000 31.34000  ? 192 THR   A C      1 
ATOM   2664 O O      . THR   A 1 226 ? -8.57800  9.92300   -21.62000 1.000 31.40000  ? 192 THR   A O      1 
ATOM   2665 C CB     . THR   A 1 226 ? -11.12800 8.42300   -21.03000 1.000 34.03000  ? 192 THR   A CB     1 
ATOM   2666 O OG1    . THR   A 1 226 ? -11.85600 7.38000   -20.36300 1.000 36.64000  ? 192 THR   A OG1    1 
ATOM   2667 C CG2    . THR   A 1 226 ? -11.98300 8.94800   -22.19300 1.000 30.60000  ? 192 THR   A CG2    1 
ATOM   2668 H H      . THR   A 1 226 ? -8.98200  7.75000   -19.76900 1.000 32.24000  ? 192 THR   A H      1 
ATOM   2669 H HA     . THR   A 1 226 ? -10.01800 7.17400   -22.21400 1.000 32.20000  ? 192 THR   A HA     1 
ATOM   2670 H HB     . THR   A 1 226 ? -10.95400 9.15100   -20.41400 1.000 34.03000  ? 192 THR   A HB     1 
ATOM   2671 H HG1    . THR   A 1 226 ? -12.58300 7.68000   -20.06800 1.000 36.64000  ? 192 THR   A HG1    1 
ATOM   2672 H HG21   . THR   A 1 226 ? -12.85700 9.21200   -21.86600 1.000 30.60000  ? 192 THR   A HG21   1 
ATOM   2673 H HG22   . THR   A 1 226 ? -11.55600 9.71600   -22.60400 1.000 30.60000  ? 192 THR   A HG22   1 
ATOM   2674 H HG23   . THR   A 1 226 ? -12.09400 8.25400   -22.86100 1.000 30.60000  ? 192 THR   A HG23   1 
ATOM   2675 N N      . CYS   A 1 227 ? -8.75300  8.76000   -23.55900 1.000 31.16000  ? 193 CYS   A N      1 
ATOM   2676 C CA     . CYS   A 1 227 ? -8.04500  9.71100   -24.41500 1.000 36.55000  ? 193 CYS   A CA     1 
ATOM   2677 C C      . CYS   A 1 227 ? -8.98400  10.11600  -25.54300 1.000 30.12000  ? 193 CYS   A C      1 
ATOM   2678 O O      . CYS   A 1 227 ? -9.30300  9.27200   -26.38900 1.000 31.83000  ? 193 CYS   A O      1 
ATOM   2679 C CB     . CYS   A 1 227 ? -6.79400  9.06400   -25.01800 1.000 29.30000  ? 193 CYS   A CB     1 
ATOM   2680 S SG     . CYS   A 1 227 ? -5.62300  8.31800   -23.83500 1.000 34.99000  ? 193 CYS   A SG     1 
ATOM   2681 H H      . CYS   A 1 227 ? -9.00000  8.05300   -23.98200 1.000 31.16000  ? 193 CYS   A H      1 
ATOM   2682 H HA     . CYS   A 1 227 ? -7.76300  10.46300  -23.88400 1.000 36.55000  ? 193 CYS   A HA     1 
ATOM   2683 H HB2    . CYS   A 1 227 ? -7.07700  8.36200   -25.62500 1.000 29.30000  ? 193 CYS   A HB2    1 
ATOM   2684 H HB3    . CYS   A 1 227 ? -6.31000  9.74200   -25.51400 1.000 29.30000  ? 193 CYS   A HB3    1 
ATOM   2685 H HG     . CYS   A 1 227 ? -4.71200  7.83300   -24.44700 1.000 34.99000  ? 193 CYS   A HG     1 
ATOM   2686 N N      . ILE   A 1 228 ? -9.36900  11.40400  -25.62600 1.000 29.64000  ? 194 ILE   A N      1 
ATOM   2687 C CA     . ILE   A 1 228 ? -8.79200  12.55900  -24.93400 1.000 30.12000  ? 194 ILE   A CA     1 
ATOM   2688 C C      . ILE   A 1 228 ? -9.88900  13.52100  -24.47900 1.000 29.85000  ? 194 ILE   A C      1 
ATOM   2689 O O      . ILE   A 1 228 ? -10.99800 13.50800  -25.01000 1.000 31.27000  ? 194 ILE   A O      1 
ATOM   2690 C CB     . ILE   A 1 228 ? -7.83200  13.35400  -25.85700 1.000 31.16000  ? 194 ILE   A CB     1 
ATOM   2691 C CG1    . ILE   A 1 228 ? -8.53800  13.67800  -27.19600 1.000 29.04000  ? 194 ILE   A CG1    1 
ATOM   2692 C CG2    . ILE   A 1 228 ? -6.54600  12.59500  -26.06600 1.000 33.00000  ? 194 ILE   A CG2    1 
ATOM   2693 C CD1    . ILE   A 1 228 ? -7.77900  14.71700  -28.09700 1.000 29.02000  ? 194 ILE   A CD1    1 
ATOM   2694 H H      . ILE   A 1 228 ? -10.02600 11.64200  -26.12800 1.000 29.64000  ? 194 ILE   A H      1 
ATOM   2695 H HA     . ILE   A 1 228 ? -8.30200  12.30400  -24.14400 1.000 30.12000  ? 194 ILE   A HA     1 
ATOM   2696 H HB     . ILE   A 1 228 ? -7.61800  14.19300  -25.41900 1.000 31.16000  ? 194 ILE   A HB     1 
ATOM   2697 H HG12   . ILE   A 1 228 ? -8.62500  12.85800  -27.70600 1.000 29.04000  ? 194 ILE   A HG12   1 
ATOM   2698 H HG13   . ILE   A 1 228 ? -9.41700  14.04200  -27.01200 1.000 29.04000  ? 194 ILE   A HG13   1 
ATOM   2699 H HG21   . ILE   A 1 228 ? -5.93700  13.14200  -26.58600 1.000 33.00000  ? 194 ILE   A HG21   1 
ATOM   2700 H HG22   . ILE   A 1 228 ? -6.15400  12.39400  -25.20200 1.000 33.00000  ? 194 ILE   A HG22   1 
ATOM   2701 H HG23   . ILE   A 1 228 ? -6.74000  11.77200  -26.54100 1.000 33.00000  ? 194 ILE   A HG23   1 
ATOM   2702 H HD11   . ILE   A 1 228 ? -8.29800  14.87500  -28.90100 1.000 29.02000  ? 194 ILE   A HD11   1 
ATOM   2703 H HD12   . ILE   A 1 228 ? -7.67300  15.54500  -27.60300 1.000 29.02000  ? 194 ILE   A HD12   1 
ATOM   2704 H HD13   . ILE   A 1 228 ? -6.90900  14.35700  -28.33000 1.000 29.02000  ? 194 ILE   A HD13   1 
ATOM   2705 N N      . ASN   A 1 229 ? -9.56600  14.37100  -23.51100 1.000 29.54000  ? 195 ASN   A N      1 
ATOM   2706 C CA     . ASN   A 1 229 ? -10.36600 15.55300  -23.27800 1.000 31.38000  ? 195 ASN   A CA     1 
ATOM   2707 C C      . ASN   A 1 229 ? -10.13000 16.51400  -24.44300 1.000 38.88000  ? 195 ASN   A C      1 
ATOM   2708 O O      . ASN   A 1 229 ? -9.34200  16.24900  -25.35100 1.000 35.02000  ? 195 ASN   A O      1 
ATOM   2709 C CB     . ASN   A 1 229 ? -9.99200  16.17600  -21.93700 1.000 31.01000  ? 195 ASN   A CB     1 
ATOM   2710 C CG     . ASN   A 1 229 ? -11.16900 16.84000  -21.25300 1.000 40.87000  ? 195 ASN   A CG     1 
ATOM   2711 O OD1    . ASN   A 1 229 ? -11.96300 17.54600  -21.89200 1.000 41.40000  ? 195 ASN   A OD1    1 
ATOM   2712 N ND2    . ASN   A 1 229 ? -11.29900 16.61100  -19.95000 1.000 43.38000  ? 195 ASN   A ND2    1 
ATOM   2713 H H      . ASN   A 1 229 ? -8.89300  14.28300  -22.98200 1.000 29.54000  ? 195 ASN   A H      1 
ATOM   2714 H HA     . ASN   A 1 229 ? -11.30400 15.31500  -23.25500 1.000 31.38000  ? 195 ASN   A HA     1 
ATOM   2715 H HB2    . ASN   A 1 229 ? -9.65600  15.48200  -21.34900 1.000 31.01000  ? 195 ASN   A HB2    1 
ATOM   2716 H HB3    . ASN   A 1 229 ? -9.30900  16.85000  -22.08100 1.000 31.01000  ? 195 ASN   A HB3    1 
ATOM   2717 H HD21   . ASN   A 1 229 ? -11.95100 16.96400  -19.51400 1.000 43.38000  ? 195 ASN   A HD21   1 
ATOM   2718 H HD22   . ASN   A 1 229 ? -10.72800 16.11400  -19.54200 1.000 43.38000  ? 195 ASN   A HD22   1 
ATOM   2719 N N      A SER   A 1 230 ? -10.82900 17.63800  -24.42000 0.780 38.52000  ? 196 SER   A N      1 
ATOM   2720 N N      B SER   A 1 230 ? -10.82400 17.64500  -24.41900 0.220 38.39000  ? 196 SER   A N      1 
ATOM   2721 C CA     A SER   A 1 230 ? -10.70600 18.60500  -25.50100 0.780 34.88000  ? 196 SER   A CA     1 
ATOM   2722 C CA     B SER   A 1 230 ? -10.69300 18.61500  -25.49500 0.220 35.04000  ? 196 SER   A CA     1 
ATOM   2723 C C      A SER   A 1 230 ? -9.26600  19.10700  -25.61500 0.780 37.65000  ? 196 SER   A C      1 
ATOM   2724 C C      B SER   A 1 230 ? -9.24900  19.09900  -25.61600 0.220 37.56000  ? 196 SER   A C      1 
ATOM   2725 O O      A SER   A 1 230 ? -8.50100  19.09000  -24.64500 0.780 38.68000  ? 196 SER   A O      1 
ATOM   2726 O O      B SER   A 1 230 ? -8.47000  19.06700  -24.65900 0.220 38.49000  ? 196 SER   A O      1 
ATOM   2727 C CB     A SER   A 1 230 ? -11.67000 19.77100  -25.25800 0.780 36.31000  ? 196 SER   A CB     1 
ATOM   2728 C CB     B SER   A 1 230 ? -11.61700 19.80900  -25.25500 0.220 36.41000  ? 196 SER   A CB     1 
ATOM   2729 O OG     A SER   A 1 230 ? -11.49900 20.30800  -23.96000 0.780 37.87000  ? 196 SER   A OG     1 
ATOM   2730 O OG     B SER   A 1 230 ? -12.97400 19.41100  -25.25000 0.220 36.89000  ? 196 SER   A OG     1 
ATOM   2731 H H      A SER   A 1 230 ? -11.37700 17.86500  -23.79700 0.780 38.39000  ? 196 SER   A H      1 
ATOM   2732 H H      B SER   A 1 230 ? -11.37200 17.87300  -23.79700 0.220 38.39000  ? 196 SER   A H      1 
ATOM   2733 H HA     A SER   A 1 230 ? -10.94700 18.18100  -26.33900 0.780 35.04000  ? 196 SER   A HA     1 
ATOM   2734 H HA     B SER   A 1 230 ? -10.94600 18.19900  -26.33400 0.220 35.04000  ? 196 SER   A HA     1 
ATOM   2735 H HB2    A SER   A 1 230 ? -11.49500 20.46600  -25.91100 0.780 36.41000  ? 196 SER   A HB2    1 
ATOM   2736 H HB2    B SER   A 1 230 ? -11.40300 20.20400  -24.39500 0.220 36.41000  ? 196 SER   A HB2    1 
ATOM   2737 H HB3    A SER   A 1 230 ? -12.58100 19.45100  -25.35000 0.780 36.41000  ? 196 SER   A HB3    1 
ATOM   2738 H HB3    B SER   A 1 230 ? -11.48100 20.46100  -25.96000 0.220 36.41000  ? 196 SER   A HB3    1 
ATOM   2739 H HG     A SER   A 1 230 ? -12.03800 20.94100  -23.83700 0.780 36.89000  ? 196 SER   A HG     1 
ATOM   2740 H HG     B SER   A 1 230 ? -13.46800 20.07700  -25.11700 0.220 36.89000  ? 196 SER   A HG     1 
ATOM   2741 N N      . ILE   A 1 231 ? -8.89200  19.55500  -26.81700 1.000 34.98000  ? 197 ILE   A N      1 
ATOM   2742 C CA     . ILE   A 1 231 ? -7.60100  20.22700  -27.00400 1.000 35.53000  ? 197 ILE   A CA     1 
ATOM   2743 C C      . ILE   A 1 231 ? -7.70800  21.61900  -26.39600 1.000 41.39000  ? 197 ILE   A C      1 
ATOM   2744 O O      . ILE   A 1 231 ? -8.52500  22.43800  -26.83000 1.000 34.87000  ? 197 ILE   A O      1 
ATOM   2745 C CB     . ILE   A 1 231 ? -7.20400  20.29800  -28.49000 1.000 35.84000  ? 197 ILE   A CB     1 
ATOM   2746 C CG1    . ILE   A 1 231 ? -6.94700  18.89300  -29.06500 1.000 32.06000  ? 197 ILE   A CG1    1 
ATOM   2747 C CG2    . ILE   A 1 231 ? -5.92900  21.12500  -28.66700 1.000 32.98000  ? 197 ILE   A CG2    1 
ATOM   2748 C CD1    . ILE   A 1 231 ? -6.49000  18.89500  -30.51800 1.000 31.74000  ? 197 ILE   A CD1    1 
ATOM   2749 H H      A ILE   A 1 231 ? -9.36200  19.48400  -27.53400 0.780 34.98000  ? 197 ILE   A H      1 
ATOM   2750 H H      B ILE   A 1 231 ? -9.36900  19.49100  -27.53000 0.220 34.98000  ? 197 ILE   A H      1 
ATOM   2751 H HA     . ILE   A 1 231 ? -6.91200  19.73800  -26.52800 1.000 35.53000  ? 197 ILE   A HA     1 
ATOM   2752 H HB     . ILE   A 1 231 ? -7.92300  20.71600  -28.98900 1.000 35.84000  ? 197 ILE   A HB     1 
ATOM   2753 H HG12   . ILE   A 1 231 ? -6.25600  18.46200  -28.53800 1.000 32.06000  ? 197 ILE   A HG12   1 
ATOM   2754 H HG13   . ILE   A 1 231 ? -7.76800  18.37900  -29.01300 1.000 32.06000  ? 197 ILE   A HG13   1 
ATOM   2755 H HG21   . ILE   A 1 231 ? -5.70800  21.18200  -29.60900 1.000 32.98000  ? 197 ILE   A HG21   1 
ATOM   2756 H HG22   . ILE   A 1 231 ? -6.07000  22.01900  -28.32100 1.000 32.98000  ? 197 ILE   A HG22   1 
ATOM   2757 H HG23   . ILE   A 1 231 ? -5.20600  20.69500  -28.18400 1.000 32.98000  ? 197 ILE   A HG23   1 
ATOM   2758 H HD11   . ILE   A 1 231 ? -6.62100  18.00900  -30.89100 1.000 31.74000  ? 197 ILE   A HD11   1 
ATOM   2759 H HD12   . ILE   A 1 231 ? -7.01600  19.54300  -31.01300 1.000 31.74000  ? 197 ILE   A HD12   1 
ATOM   2760 H HD13   . ILE   A 1 231 ? -5.55100  19.13400  -30.55500 1.000 31.74000  ? 197 ILE   A HD13   1 
ATOM   2761 N N      . GLY   A 1 232 ? -6.88600  21.89100  -25.39100 1.000 34.13000  ? 198 GLY   A N      1 
ATOM   2762 C CA     . GLY   A 1 232 ? -7.11600  23.03300  -24.52700 1.000 37.03000  ? 198 GLY   A CA     1 
ATOM   2763 C C      . GLY   A 1 232 ? -6.76700  24.37000  -25.15500 1.000 40.89000  ? 198 GLY   A C      1 
ATOM   2764 O O      . GLY   A 1 232 ? -5.86800  24.49100  -25.97400 1.000 32.85000  ? 198 GLY   A O      1 
ATOM   2765 H H      . GLY   A 1 232 ? -6.18900  21.42900  -25.19000 1.000 34.13000  ? 198 GLY   A H      1 
ATOM   2766 H HA2    . GLY   A 1 232 ? -8.05200  23.05500  -24.27300 1.000 37.03000  ? 198 GLY   A HA2    1 
ATOM   2767 H HA3    . GLY   A 1 232 ? -6.58700  22.93200  -23.72100 1.000 37.03000  ? 198 GLY   A HA3    1 
ATOM   2768 N N      . ASN   A 1 233 ? -7.54100  25.37700  -24.76700 1.000 34.33000  ? 199 ASN   A N      1 
ATOM   2769 C CA     . ASN   A 1 233 ? -7.22300  26.78600  -24.99100 1.000 36.05000  ? 199 ASN   A CA     1 
ATOM   2770 C C      . ASN   A 1 233 ? -6.94300  27.10800  -26.46000 1.000 34.04000  ? 199 ASN   A C      1 
ATOM   2771 O O      . ASN   A 1 233 ? -5.98000  27.79600  -26.80100 1.000 34.59000  ? 199 ASN   A O      1 
ATOM   2772 C CB     . ASN   A 1 233 ? -6.06800  27.20300  -24.08500 1.000 38.43000  ? 199 ASN   A CB     1 
ATOM   2773 C CG     . ASN   A 1 233 ? -6.47900  27.18400  -22.63300 1.000 48.12000  ? 199 ASN   A CG     1 
ATOM   2774 O OD1    . ASN   A 1 233 ? -7.33000  27.97000  -22.22600 1.000 40.55000  ? 199 ASN   A OD1    1 
ATOM   2775 N ND2    . ASN   A 1 233 ? -5.94000  26.24000  -21.86300 1.000 40.87000  ? 199 ASN   A ND2    1 
ATOM   2776 H H      . ASN   A 1 233 ? -8.28700  25.26500  -24.35500 1.000 34.33000  ? 199 ASN   A H      1 
ATOM   2777 H HA     . ASN   A 1 233 ? -7.99400  27.31200  -24.72800 1.000 36.05000  ? 199 ASN   A HA     1 
ATOM   2778 H HB2    . ASN   A 1 233 ? -5.32900  26.58600  -24.20100 1.000 38.43000  ? 199 ASN   A HB2    1 
ATOM   2779 H HB3    . ASN   A 1 233 ? -5.79200  28.10500  -24.31100 1.000 38.43000  ? 199 ASN   A HB3    1 
ATOM   2780 H HD21   . ASN   A 1 233 ? -6.15300  26.19000  -21.03100 1.000 40.87000  ? 199 ASN   A HD21   1 
ATOM   2781 H HD22   . ASN   A 1 233 ? -5.35700  25.69900  -22.19000 1.000 40.87000  ? 199 ASN   A HD22   1 
ATOM   2782 N N      . GLY   A 1 234 ? -7.83600  26.62400  -27.33500 1.000 33.67000  ? 200 GLY   A N      1 
ATOM   2783 C CA     . GLY   A 1 234 ? -7.94000  27.19100  -28.66400 1.000 35.21000  ? 200 GLY   A CA     1 
ATOM   2784 C C      . GLY   A 1 234 ? -8.67400  28.53000  -28.61700 1.000 34.46000  ? 200 GLY   A C      1 
ATOM   2785 O O      . GLY   A 1 234 ? -9.20100  28.93400  -27.58600 1.000 30.54000  ? 200 GLY   A O      1 
ATOM   2786 H H      . GLY   A 1 234 ? -8.38100  25.97700  -27.17700 1.000 33.67000  ? 200 GLY   A H      1 
ATOM   2787 H HA2    . GLY   A 1 234 ? -7.05400  27.33100  -29.03300 1.000 35.21000  ? 200 GLY   A HA2    1 
ATOM   2788 H HA3    . GLY   A 1 234 ? -8.42900  26.58600  -29.24300 1.000 35.21000  ? 200 GLY   A HA3    1 
ATOM   2789 N N      . LEU   A 1 235 ? -8.70500  29.21500  -29.76000 1.000 30.26000  ? 201 LEU   A N      1 
ATOM   2790 C CA     . LEU   A 1 235 ? -9.31400  30.54300  -29.83100 1.000 32.05000  ? 201 LEU   A CA     1 
ATOM   2791 C C      . LEU   A 1 235 ? -10.08200 30.66700  -31.13600 1.000 34.75000  ? 201 LEU   A C      1 
ATOM   2792 O O      . LEU   A 1 235 ? -9.51900  30.41100  -32.19900 1.000 38.48000  ? 201 LEU   A O      1 
ATOM   2793 C CB     . LEU   A 1 235 ? -8.24300  31.62800  -29.74200 1.000 34.03000  ? 201 LEU   A CB     1 
ATOM   2794 C CG     . LEU   A 1 235 ? -8.76200  33.07200  -29.70900 1.000 36.49000  ? 201 LEU   A CG     1 
ATOM   2795 C CD1    . LEU   A 1 235 ? -9.56700  33.29500  -28.43800 1.000 33.04000  ? 201 LEU   A CD1    1 
ATOM   2796 C CD2    . LEU   A 1 235 ? -7.58900  34.04500  -29.81400 1.000 33.29000  ? 201 LEU   A CD2    1 
ATOM   2797 H H      . LEU   A 1 235 ? -8.38200  28.93400  -30.50600 1.000 30.26000  ? 201 LEU   A H      1 
ATOM   2798 H HA     . LEU   A 1 235 ? -9.93600  30.65700  -29.09600 1.000 32.05000  ? 201 LEU   A HA     1 
ATOM   2799 H HB2    . LEU   A 1 235 ? -7.73000  31.48600  -28.93100 1.000 34.03000  ? 201 LEU   A HB2    1 
ATOM   2800 H HB3    . LEU   A 1 235 ? -7.65900  31.54600  -30.51200 1.000 34.03000  ? 201 LEU   A HB3    1 
ATOM   2801 H HG     . LEU   A 1 235 ? -9.34700  33.22100  -30.46800 1.000 36.49000  ? 201 LEU   A HG     1 
ATOM   2802 H HD11   . LEU   A 1 235 ? -9.76700  34.24100  -28.35500 1.000 33.04000  ? 201 LEU   A HD11   1 
ATOM   2803 H HD12   . LEU   A 1 235 ? -10.39100 32.78700  -28.49100 1.000 33.04000  ? 201 LEU   A HD12   1 
ATOM   2804 H HD13   . LEU   A 1 235 ? -9.04300  33.00000  -27.67700 1.000 33.04000  ? 201 LEU   A HD13   1 
ATOM   2805 H HD21   . LEU   A 1 235 ? -7.93000  34.95300  -29.79100 1.000 33.29000  ? 201 LEU   A HD21   1 
ATOM   2806 H HD22   . LEU   A 1 235 ? -6.98900  33.89700  -29.06600 1.000 33.29000  ? 201 LEU   A HD22   1 
ATOM   2807 H HD23   . LEU   A 1 235 ? -7.12200  33.88700  -30.64900 1.000 33.29000  ? 201 LEU   A HD23   1 
ATOM   2808 N N      . VAL   A 1 236 ? -11.36600 31.03600  -31.06600 1.000 34.39000  ? 202 VAL   A N      1 
ATOM   2809 C CA     . VAL   A 1 236 ? -12.17100 31.24900  -32.26400 1.000 32.82000  ? 202 VAL   A CA     1 
ATOM   2810 C C      . VAL   A 1 236 ? -12.65900 32.69200  -32.27700 1.000 37.68000  ? 202 VAL   A C      1 
ATOM   2811 O O      . VAL   A 1 236 ? -13.07300 33.23000  -31.24100 1.000 34.87000  ? 202 VAL   A O      1 
ATOM   2812 C CB     . VAL   A 1 236 ? -13.35000 30.25600  -32.35900 1.000 37.30000  ? 202 VAL   A CB     1 
ATOM   2813 C CG1    . VAL   A 1 236 ? -14.26100 30.61900  -33.51900 1.000 38.70000  ? 202 VAL   A CG1    1 
ATOM   2814 C CG2    . VAL   A 1 236 ? -12.82100 28.84600  -32.55900 1.000 39.94000  ? 202 VAL   A CG2    1 
ATOM   2815 H H      . VAL   A 1 236 ? -11.79200 31.16900  -30.33100 1.000 34.39000  ? 202 VAL   A H      1 
ATOM   2816 H HA     . VAL   A 1 236 ? -11.61400 31.12000  -33.04700 1.000 32.82000  ? 202 VAL   A HA     1 
ATOM   2817 H HB     . VAL   A 1 236 ? -13.86600 30.28100  -31.53800 1.000 37.30000  ? 202 VAL   A HB     1 
ATOM   2818 H HG11   . VAL   A 1 236 ? -14.65000 29.81200  -33.88000 1.000 38.70000  ? 202 VAL   A HG11   1 
ATOM   2819 H HG12   . VAL   A 1 236 ? -14.95900 31.21200  -33.20000 1.000 38.70000  ? 202 VAL   A HG12   1 
ATOM   2820 H HG13   . VAL   A 1 236 ? -13.73600 31.06000  -34.20500 1.000 38.70000  ? 202 VAL   A HG13   1 
ATOM   2821 H HG21   . VAL   A 1 236 ? -13.56900 28.23100  -32.58600 1.000 39.94000  ? 202 VAL   A HG21   1 
ATOM   2822 H HG22   . VAL   A 1 236 ? -12.33000 28.80900  -33.39500 1.000 39.94000  ? 202 VAL   A HG22   1 
ATOM   2823 H HG23   . VAL   A 1 236 ? -12.23400 28.62100  -31.82000 1.000 39.94000  ? 202 VAL   A HG23   1 
ATOM   2824 N N      . ILE   A 1 237 ? -12.55600 33.33000  -33.44500 1.000 34.16000  ? 203 ILE   A N      1 
ATOM   2825 C CA     . ILE   A 1 237 ? -12.93900 34.72900  -33.65000 1.000 37.59000  ? 203 ILE   A CA     1 
ATOM   2826 C C      . ILE   A 1 237 ? -13.91400 34.79600  -34.81800 1.000 41.12000  ? 203 ILE   A C      1 
ATOM   2827 O O      . ILE   A 1 237 ? -13.71700 34.12300  -35.83700 1.000 39.68000  ? 203 ILE   A O      1 
ATOM   2828 C CB     . ILE   A 1 237 ? -11.71800 35.62800  -33.95100 1.000 32.41000  ? 203 ILE   A CB     1 
ATOM   2829 C CG1    . ILE   A 1 237 ? -10.60800 35.42900  -32.91900 1.000 34.25000  ? 203 ILE   A CG1    1 
ATOM   2830 C CG2    . ILE   A 1 237 ? -12.14700 37.13000  -34.06700 1.000 33.86000  ? 203 ILE   A CG2    1 
ATOM   2831 C CD1    . ILE   A 1 237 ? -9.30400  36.14100  -33.29600 1.000 31.98000  ? 203 ILE   A CD1    1 
ATOM   2832 H H      . ILE   A 1 237 ? -12.25500 32.95800  -34.16000 1.000 34.16000  ? 203 ILE   A H      1 
ATOM   2833 H HA     . ILE   A 1 237 ? -13.38300 35.06600  -32.85600 1.000 37.59000  ? 203 ILE   A HA     1 
ATOM   2834 H HB     . ILE   A 1 237 ? -11.36400 35.35800  -34.81300 1.000 32.41000  ? 203 ILE   A HB     1 
ATOM   2835 H HG12   . ILE   A 1 237 ? -10.90500 35.78100  -32.06500 1.000 34.25000  ? 203 ILE   A HG12   1 
ATOM   2836 H HG13   . ILE   A 1 237 ? -10.41300 34.48300  -32.83700 1.000 34.25000  ? 203 ILE   A HG13   1 
ATOM   2837 H HG21   . ILE   A 1 237 ? -11.35600 37.68100  -34.16200 1.000 33.86000  ? 203 ILE   A HG21   1 
ATOM   2838 H HG22   . ILE   A 1 237 ? -12.71800 37.23800  -34.84400 1.000 33.86000  ? 203 ILE   A HG22   1 
ATOM   2839 H HG23   . ILE   A 1 237 ? -12.63000 37.38200  -33.26400 1.000 33.86000  ? 203 ILE   A HG23   1 
ATOM   2840 H HD11   . ILE   A 1 237 ? -8.59600  35.83300  -32.70900 1.000 31.98000  ? 203 ILE   A HD11   1 
ATOM   2841 H HD12   . ILE   A 1 237 ? -9.08500  35.93000  -34.21700 1.000 31.98000  ? 203 ILE   A HD12   1 
ATOM   2842 H HD13   . ILE   A 1 237 ? -9.42400  37.09800  -33.19500 1.000 31.98000  ? 203 ILE   A HD13   1 
ATOM   2843 N N      . ASP   A 1 238 ? -14.95100 35.62500  -34.68500 1.000 39.19000  ? 204 ASP   A N      1 
ATOM   2844 C CA     . ASP   A 1 238 ? -15.94100 35.80300  -35.73800 1.000 43.33000  ? 204 ASP   A CA     1 
ATOM   2845 C C      . ASP   A 1 238 ? -15.50800 36.93600  -36.66600 1.000 38.78000  ? 204 ASP   A C      1 
ATOM   2846 O O      . ASP   A 1 238 ? -15.19800 38.04000  -36.19800 1.000 41.53000  ? 204 ASP   A O      1 
ATOM   2847 C CB     . ASP   A 1 238 ? -17.31000 36.09300  -35.12100 1.000 45.17000  ? 204 ASP   A CB     1 
ATOM   2848 C CG     . ASP   A 1 238 ? -18.39400 36.29200  -36.16400 1.000 51.95000  ? 204 ASP   A CG     1 
ATOM   2849 O OD1    . ASP   A 1 238 ? -18.78100 35.31600  -36.84200 1.000 63.14000  ? 204 ASP   A OD1    1 
ATOM   2850 O OD2    . ASP   A 1 238 ? -18.87200 37.43000  -36.29600 1.000 54.78000  ? 204 ASP   A OD2    1 
ATOM   2851 H H      . ASP   A 1 238 ? -15.10100 36.10000  -33.98400 1.000 39.19000  ? 204 ASP   A H      1 
ATOM   2852 H HA     . ASP   A 1 238 ? -16.00800 34.98800  -36.26000 1.000 43.33000  ? 204 ASP   A HA     1 
ATOM   2853 H HB2    . ASP   A 1 238 ? -17.56800 35.34600  -34.55900 1.000 45.17000  ? 204 ASP   A HB2    1 
ATOM   2854 H HB3    . ASP   A 1 238 ? -17.25200 36.90300  -34.59000 1.000 45.17000  ? 204 ASP   A HB3    1 
ATOM   2855 N N      . VAL   A 1 239 ? -15.47900 36.65500  -37.97800 1.000 35.79000  ? 205 VAL   A N      1 
ATOM   2856 C CA     . VAL   A 1 239 ? -15.01400 37.64200  -38.95500 1.000 39.49000  ? 205 VAL   A CA     1 
ATOM   2857 C C      . VAL   A 1 239 ? -15.90200 38.88600  -38.93300 1.000 36.54000  ? 205 VAL   A C      1 
ATOM   2858 O O      . VAL   A 1 239 ? -15.41200 40.02700  -38.95300 1.000 39.61000  ? 205 VAL   A O      1 
ATOM   2859 C CB     . VAL   A 1 239 ? -14.96200 37.04000  -40.37400 1.000 41.56000  ? 205 VAL   A CB     1 
ATOM   2860 C CG1    . VAL   A 1 239 ? -14.51100 38.12900  -41.37200 1.000 42.88000  ? 205 VAL   A CG1    1 
ATOM   2861 C CG2    . VAL   A 1 239 ? -14.06000 35.80000  -40.45300 1.000 48.23000  ? 205 VAL   A CG2    1 
ATOM   2862 H H      . VAL   A 1 239 ? -15.72200 35.90500  -38.32200 1.000 35.79000  ? 205 VAL   A H      1 
ATOM   2863 H HA     . VAL   A 1 239 ? -14.11500 37.91600  -38.71700 1.000 39.49000  ? 205 VAL   A HA     1 
ATOM   2864 H HB     . VAL   A 1 239 ? -15.85800 36.76600  -40.62600 1.000 41.56000  ? 205 VAL   A HB     1 
ATOM   2865 H HG11   . VAL   A 1 239 ? -14.23300 37.70200  -42.19700 1.000 42.88000  ? 205 VAL   A HG11   1 
ATOM   2866 H HG12   . VAL   A 1 239 ? -15.25300 38.72900  -41.54600 1.000 42.88000  ? 205 VAL   A HG12   1 
ATOM   2867 H HG13   . VAL   A 1 239 ? -13.76700 38.62000  -40.98800 1.000 42.88000  ? 205 VAL   A HG13   1 
ATOM   2868 H HG21   . VAL   A 1 239 ? -14.04400 35.48000  -41.36900 1.000 48.23000  ? 205 VAL   A HG21   1 
ATOM   2869 H HG22   . VAL   A 1 239 ? -13.16400 36.04300  -40.17100 1.000 48.23000  ? 205 VAL   A HG22   1 
ATOM   2870 H HG23   . VAL   A 1 239 ? -14.41600 35.11300  -39.86800 1.000 48.23000  ? 205 VAL   A HG23   1 
ATOM   2871 N N      . GLU   A 1 240 ? -17.22500 38.68700  -38.91300 1.000 40.74000  ? 206 GLU   A N      1 
ATOM   2872 C CA     . GLU   A 1 240 ? -18.13700 39.83200  -38.98400 1.000 43.85000  ? 206 GLU   A CA     1 
ATOM   2873 C C      . GLU   A 1 240 ? -17.99600 40.73800  -37.76300 1.000 46.05000  ? 206 GLU   A C      1 
ATOM   2874 O O      . GLU   A 1 240 ? -17.80700 41.94900  -37.89800 1.000 45.42000  ? 206 GLU   A O      1 
ATOM   2875 C CB     . GLU   A 1 240 ? -19.58500 39.36400  -39.13800 1.000 49.93000  ? 206 GLU   A CB     1 
ATOM   2876 C CG     . GLU   A 1 240 ? -19.91700 38.77900  -40.50300 1.000 64.71000  ? 206 GLU   A CG     1 
ATOM   2877 H H      . GLU   A 1 240 ? -17.61000 37.92000  -38.86000 1.000 40.74000  ? 206 GLU   A H      1 
ATOM   2878 H HA     . GLU   A 1 240 ? -17.91300 40.35800  -39.76800 1.000 43.85000  ? 206 GLU   A HA     1 
ATOM   2879 H HB2    . GLU   A 1 240 ? -19.76200 38.68000  -38.47400 1.000 49.93000  ? 206 GLU   A HB2    1 
ATOM   2880 H HB3    . GLU   A 1 240 ? -20.17300 40.12100  -38.99200 1.000 49.93000  ? 206 GLU   A HB3    1 
ATOM   2881 N N      . THR   A 1 241 ? -18.08400 40.17600  -36.56000 1.000 40.36000  ? 207 THR   A N      1 
ATOM   2882 C CA     . THR   A 1 241 ? -18.02600 40.99300  -35.35100 1.000 42.62000  ? 207 THR   A CA     1 
ATOM   2883 C C      . THR   A 1 241 ? -16.60700 41.29000  -34.88700 1.000 46.65000  ? 207 THR   A C      1 
ATOM   2884 O O      . THR   A 1 241 ? -16.43000 42.12600  -34.00100 1.000 39.90000  ? 207 THR   A O      1 
ATOM   2885 C CB     . THR   A 1 241 ? -18.78200 40.31900  -34.19100 1.000 49.01000  ? 207 THR   A CB     1 
ATOM   2886 O OG1    . THR   A 1 241 ? -18.05100 39.17600  -33.73200 1.000 44.66000  ? 207 THR   A OG1    1 
ATOM   2887 C CG2    . THR   A 1 241 ? -20.17600 39.87900  -34.62300 1.000 45.91000  ? 207 THR   A CG2    1 
ATOM   2888 H H      . THR   A 1 241 ? -18.17700 39.33300  -36.41700 1.000 40.36000  ? 207 THR   A H      1 
ATOM   2889 H HA     . THR   A 1 241 ? -18.46000 41.84200  -35.53000 1.000 42.62000  ? 207 THR   A HA     1 
ATOM   2890 H HB     . THR   A 1 241 ? -18.87600 40.95100  -33.46200 1.000 49.01000  ? 207 THR   A HB     1 
ATOM   2891 H HG1    . THR   A 1 241 ? -18.46200 38.80700  -33.09900 1.000 44.66000  ? 207 THR   A HG1    1 
ATOM   2892 H HG21   . THR   A 1 241 ? -20.65100 39.49800  -33.86800 1.000 45.91000  ? 207 THR   A HG21   1 
ATOM   2893 H HG22   . THR   A 1 241 ? -20.67500 40.64200  -34.95600 1.000 45.91000  ? 207 THR   A HG22   1 
ATOM   2894 H HG23   . THR   A 1 241 ? -20.11600 39.21300  -35.32400 1.000 45.91000  ? 207 THR   A HG23   1 
ATOM   2895 N N      . GLU   A 1 242 ? -15.59600 40.63400  -35.45500 1.000 42.75000  ? 208 GLU   A N      1 
ATOM   2896 C CA     . GLU   A 1 242 ? -14.21400 40.76000  -34.97200 1.000 35.51000  ? 208 GLU   A CA     1 
ATOM   2897 C C      . GLU   A 1 242 ? -14.11100 40.46000  -33.48000 1.000 33.77000  ? 208 GLU   A C      1 
ATOM   2898 O O      . GLU   A 1 242 ? -13.22500 40.97100  -32.79300 1.000 39.79000  ? 208 GLU   A O      1 
ATOM   2899 C CB     . GLU   A 1 242 ? -13.64000 42.14300  -35.29900 1.000 34.52000  ? 208 GLU   A CB     1 
ATOM   2900 C CG     . GLU   A 1 242 ? -13.78800 42.43500  -36.76500 1.000 32.69000  ? 208 GLU   A CG     1 
ATOM   2901 C CD     . GLU   A 1 242 ? -13.32200 43.81200  -37.19100 1.000 36.97000  ? 208 GLU   A CD     1 
ATOM   2902 O OE1    . GLU   A 1 242 ? -12.58400 44.48800  -36.44100 1.000 46.82000  ? 208 GLU   A OE1    1 
ATOM   2903 O OE2    . GLU   A 1 242 ? -13.71000 44.20600  -38.31100 1.000 43.95000  ? 208 GLU   A OE2    1 
ATOM   2904 H H      . GLU   A 1 242 ? -15.68100 40.10500  -36.12700 1.000 42.75000  ? 208 GLU   A H      1 
ATOM   2905 H HA     . GLU   A 1 242 ? -13.67100 40.10400  -35.43600 1.000 35.51000  ? 208 GLU   A HA     1 
ATOM   2906 H HB2    . GLU   A 1 242 ? -14.12300 42.82000  -34.80000 1.000 34.52000  ? 208 GLU   A HB2    1 
ATOM   2907 H HB3    . GLU   A 1 242 ? -12.69700 42.16400  -35.07500 1.000 34.52000  ? 208 GLU   A HB3    1 
ATOM   2908 H HG2    . GLU   A 1 242 ? -13.27100 41.78300  -37.26400 1.000 32.69000  ? 208 GLU   A HG2    1 
ATOM   2909 H HG3    . GLU   A 1 242 ? -14.72400 42.36200  -37.00700 1.000 32.69000  ? 208 GLU   A HG3    1 
ATOM   2910 N N      . SER   A 1 243 ? -14.99900 39.60300  -32.96900 1.000 35.54000  ? 209 SER   A N      1 
ATOM   2911 C CA     . SER   A 1 243 ? -15.03000 39.27000  -31.55100 1.000 41.73000  ? 209 SER   A CA     1 
ATOM   2912 C C      . SER   A 1 243 ? -14.87800 37.76800  -31.35100 1.000 35.65000  ? 209 SER   A C      1 
ATOM   2913 O O      . SER   A 1 243 ? -15.28700 36.96600  -32.19800 1.000 36.94000  ? 209 SER   A O      1 
ATOM   2914 C CB     . SER   A 1 243 ? -16.34100 39.72000  -30.88400 1.000 44.73000  ? 209 SER   A CB     1 
ATOM   2915 O OG     . SER   A 1 243 ? -16.65700 41.04600  -31.27000 1.000 59.00000  ? 209 SER   A OG     1 
ATOM   2916 H H      . SER   A 1 243 ? -15.60000 39.19800  -33.43300 1.000 35.54000  ? 209 SER   A H      1 
ATOM   2917 H HA     . SER   A 1 243 ? -14.29400 39.71000  -31.09800 1.000 41.73000  ? 209 SER   A HA     1 
ATOM   2918 H HB2    . SER   A 1 243 ? -17.05800 39.12900  -31.16200 1.000 44.73000  ? 209 SER   A HB2    1 
ATOM   2919 H HB3    . SER   A 1 243 ? -16.23500 39.68600  -29.92000 1.000 44.73000  ? 209 SER   A HB3    1 
ATOM   2920 H HG     . SER   A 1 243 ? -16.77900 41.08300  -32.10000 1.000 59.00000  ? 209 SER   A HG     1 
ATOM   2921 N N      . VAL   A 1 244 ? -14.31000 37.40100  -30.20000 1.000 38.08000  ? 210 VAL   A N      1 
ATOM   2922 C CA     . VAL   A 1 244 ? -14.28200 35.99700  -29.80200 1.000 38.48000  ? 210 VAL   A CA     1 
ATOM   2923 C C      . VAL   A 1 244 ? -15.71100 35.49900  -29.59200 1.000 47.48000  ? 210 VAL   A C      1 
ATOM   2924 O O      . VAL   A 1 244 ? -16.63000 36.27500  -29.30100 1.000 48.04000  ? 210 VAL   A O      1 
ATOM   2925 C CB     . VAL   A 1 244 ? -13.43900 35.81500  -28.53100 1.000 37.10000  ? 210 VAL   A CB     1 
ATOM   2926 C CG1    . VAL   A 1 244 ? -12.05200 36.35100  -28.75800 1.000 38.27000  ? 210 VAL   A CG1    1 
ATOM   2927 C CG2    . VAL   A 1 244 ? -14.11100 36.51400  -27.32800 1.000 47.11000  ? 210 VAL   A CG2    1 
ATOM   2928 H H      . VAL   A 1 244 ? -13.94100 37.94000  -29.64100 1.000 38.08000  ? 210 VAL   A H      1 
ATOM   2929 H HA     . VAL   A 1 244 ? -13.87900 35.47200  -30.51100 1.000 38.48000  ? 210 VAL   A HA     1 
ATOM   2930 H HB     . VAL   A 1 244 ? -13.36800 34.86900  -28.33000 1.000 37.10000  ? 210 VAL   A HB     1 
ATOM   2931 H HG11   . VAL   A 1 244 ? -11.49100 36.10000  -28.00800 1.000 38.27000  ? 210 VAL   A HG11   1 
ATOM   2932 H HG12   . VAL   A 1 244 ? -11.69800 35.97100  -29.57700 1.000 38.27000  ? 210 VAL   A HG12   1 
ATOM   2933 H HG13   . VAL   A 1 244 ? -12.09300 37.31700  -28.83200 1.000 38.27000  ? 210 VAL   A HG13   1 
ATOM   2934 H HG21   . VAL   A 1 244 ? -13.48200 36.54300  -26.59000 1.000 47.11000  ? 210 VAL   A HG21   1 
ATOM   2935 H HG22   . VAL   A 1 244 ? -14.36100 37.41500  -27.58500 1.000 47.11000  ? 210 VAL   A HG22   1 
ATOM   2936 H HG23   . VAL   A 1 244 ? -14.90000 36.01300  -27.06900 1.000 47.11000  ? 210 VAL   A HG23   1 
ATOM   2937 N N      . VAL   A 1 245 ? -15.90600 34.19100  -29.74000 1.000 45.04000  ? 211 VAL   A N      1 
ATOM   2938 C CA     . VAL   A 1 245 ? -17.26000 33.64600  -29.76800 1.000 44.52000  ? 211 VAL   A CA     1 
ATOM   2939 C C      . VAL   A 1 245 ? -17.73200 33.11700  -28.41800 1.000 54.71000  ? 211 VAL   A C      1 
ATOM   2940 O O      . VAL   A 1 245 ? -18.92400 32.79300  -28.28200 1.000 53.24000  ? 211 VAL   A O      1 
ATOM   2941 C CB     . VAL   A 1 245 ? -17.39800 32.54900  -30.84300 1.000 52.20000  ? 211 VAL   A CB     1 
ATOM   2942 C CG1    . VAL   A 1 245 ? -17.15700 33.15200  -32.20600 1.000 49.66000  ? 211 VAL   A CG1    1 
ATOM   2943 C CG2    . VAL   A 1 245 ? -16.43000 31.40500  -30.56800 1.000 42.93000  ? 211 VAL   A CG2    1 
ATOM   2944 H H      . VAL   A 1 245 ? -15.28000 33.60800  -29.82300 1.000 45.04000  ? 211 VAL   A H      1 
ATOM   2945 H HA     . VAL   A 1 245 ? -17.86700 34.36000  -30.01800 1.000 44.52000  ? 211 VAL   A HA     1 
ATOM   2946 H HB     . VAL   A 1 245 ? -18.30000 32.19500  -30.82300 1.000 52.20000  ? 211 VAL   A HB     1 
ATOM   2947 H HG11   . VAL   A 1 245 ? -17.28900 32.46800  -32.88100 1.000 49.66000  ? 211 VAL   A HG11   1 
ATOM   2948 H HG12   . VAL   A 1 245 ? -17.78400 33.87900  -32.34500 1.000 49.66000  ? 211 VAL   A HG12   1 
ATOM   2949 H HG13   . VAL   A 1 245 ? -16.24800 33.48700  -32.24700 1.000 49.66000  ? 211 VAL   A HG13   1 
ATOM   2950 H HG21   . VAL   A 1 245 ? -16.56900 30.71200  -31.23200 1.000 42.93000  ? 211 VAL   A HG21   1 
ATOM   2951 H HG22   . VAL   A 1 245 ? -15.52100 31.73600  -30.62600 1.000 42.93000  ? 211 VAL   A HG22   1 
ATOM   2952 H HG23   . VAL   A 1 245 ? -16.59800 31.04900  -29.68200 1.000 42.93000  ? 211 VAL   A HG23   1 
ATOM   2953 N N      . ILE   A 1 246 ? -16.85300 33.01100  -27.42500 1.000 42.11000  ? 212 ILE   A N      1 
ATOM   2954 C CA     . ILE   A 1 246 ? -17.26200 32.63400  -26.07900 1.000 54.52000  ? 212 ILE   A CA     1 
ATOM   2955 C C      . ILE   A 1 246 ? -16.69500 33.66600  -25.12600 1.000 48.65000  ? 212 ILE   A C      1 
ATOM   2956 O O      . ILE   A 1 246 ? -15.63400 34.24800  -25.37500 1.000 54.44000  ? 212 ILE   A O      1 
ATOM   2957 C CB     . ILE   A 1 246 ? -16.80500 31.21100  -25.68600 1.000 53.47000  ? 212 ILE   A CB     1 
ATOM   2958 C CG1    . ILE   A 1 246 ? -15.27300 31.12600  -25.71100 1.000 53.15000  ? 212 ILE   A CG1    1 
ATOM   2959 C CG2    . ILE   A 1 246 ? -17.48500 30.17000  -26.58400 1.000 54.95000  ? 212 ILE   A CG2    1 
ATOM   2960 C CD1    . ILE   A 1 246 ? -14.71200 29.74600  -25.45300 1.000 46.52000  ? 212 ILE   A CD1    1 
ATOM   2961 H H      . ILE   A 1 246 ? -16.00900 33.15300  -27.50700 1.000 42.11000  ? 212 ILE   A H      1 
ATOM   2962 H HA     . ILE   A 1 246 ? -18.22900 32.66700  -26.01500 1.000 54.52000  ? 212 ILE   A HA     1 
ATOM   2963 H HB     . ILE   A 1 246 ? -17.09500 31.04900  -24.77500 1.000 53.47000  ? 212 ILE   A HB     1 
ATOM   2964 H HG12   . ILE   A 1 246 ? -14.96000 31.41100  -26.58400 1.000 53.15000  ? 212 ILE   A HG12   1 
ATOM   2965 H HG13   . ILE   A 1 246 ? -14.91500 31.71400  -25.02800 1.000 53.15000  ? 212 ILE   A HG13   1 
ATOM   2966 H HG21   . ILE   A 1 246 ? -17.28900 29.28200  -26.24600 1.000 54.95000  ? 212 ILE   A HG21   1 
ATOM   2967 H HG22   . ILE   A 1 246 ? -18.44300 30.32300  -26.57300 1.000 54.95000  ? 212 ILE   A HG22   1 
ATOM   2968 H HG23   . ILE   A 1 246 ? -17.14600 30.26400  -27.48800 1.000 54.95000  ? 212 ILE   A HG23   1 
ATOM   2969 H HD11   . ILE   A 1 246 ? -13.75300 29.81400  -25.32100 1.000 46.52000  ? 212 ILE   A HD11   1 
ATOM   2970 H HD12   . ILE   A 1 246 ? -15.13200 29.38000  -24.65900 1.000 46.52000  ? 212 ILE   A HD12   1 
ATOM   2971 H HD13   . ILE   A 1 246 ? -14.90200 29.18000  -26.21700 1.000 46.52000  ? 212 ILE   A HD13   1 
ATOM   2972 N N      . LYS   A 1 247 ? -17.41000 33.89500  -24.03100 1.000 58.47000  ? 213 LYS   A N      1 
ATOM   2973 C CA     . LYS   A 1 247 ? -17.15300 35.06200  -23.19200 1.000 57.33000  ? 213 LYS   A CA     1 
ATOM   2974 C C      . LYS   A 1 247 ? -16.02100 34.83600  -22.18900 1.000 54.63000  ? 213 LYS   A C      1 
ATOM   2975 O O      . LYS   A 1 247 ? -15.12300 35.68200  -22.08600 1.000 58.69000  ? 213 LYS   A O      1 
ATOM   2976 C CB     . LYS   A 1 247 ? -18.43800 35.47300  -22.46800 1.000 58.71000  ? 213 LYS   A CB     1 
ATOM   2977 H H      . LYS   A 1 247 ? -18.05000 33.39300  -23.75300 1.000 58.47000  ? 213 LYS   A H      1 
ATOM   2978 H HA     . LYS   A 1 247 ? -16.89100 35.80000  -23.76400 1.000 57.33000  ? 213 LYS   A HA     1 
ATOM   2979 N N      . PRO   A 1 248 ? -16.01000 33.72900  -21.44200 1.000 55.78000  ? 214 PRO   A N      1 
ATOM   2980 C CA     . PRO   A 1 248 ? -14.98400 33.56000  -20.39900 1.000 45.18000  ? 214 PRO   A CA     1 
ATOM   2981 C C      . PRO   A 1 248 ? -13.57800 33.41100  -20.97500 1.000 53.36000  ? 214 PRO   A C      1 
ATOM   2982 O O      . PRO   A 1 248 ? -13.38400 32.92500  -22.09400 1.000 50.93000  ? 214 PRO   A O      1 
ATOM   2983 C CB     . PRO   A 1 248 ? -15.41300 32.27400  -19.67400 1.000 47.52000  ? 214 PRO   A CB     1 
ATOM   2984 C CG     . PRO   A 1 248 ? -16.78800 31.92700  -20.20200 1.000 57.22000  ? 214 PRO   A CG     1 
ATOM   2985 C CD     . PRO   A 1 248 ? -16.88600 32.55000  -21.56000 1.000 53.63000  ? 214 PRO   A CD     1 
ATOM   2986 H HA     . PRO   A 1 248 ? -15.00400 34.30500  -19.77800 1.000 45.18000  ? 214 PRO   A HA     1 
ATOM   2987 H HB2    . PRO   A 1 248 ? -14.78300 31.56400  -19.87500 1.000 47.52000  ? 214 PRO   A HB2    1 
ATOM   2988 H HB3    . PRO   A 1 248 ? -15.44800 32.43800  -18.71900 1.000 47.52000  ? 214 PRO   A HB3    1 
ATOM   2989 H HG2    . PRO   A 1 248 ? -16.87700 30.96300  -20.26300 1.000 57.22000  ? 214 PRO   A HG2    1 
ATOM   2990 H HG3    . PRO   A 1 248 ? -17.46400 32.29400  -19.61100 1.000 57.22000  ? 214 PRO   A HG3    1 
ATOM   2991 H HD2    . PRO   A 1 248 ? -16.55100 31.94300  -22.23900 1.000 53.63000  ? 214 PRO   A HD2    1 
ATOM   2992 H HD3    . PRO   A 1 248 ? -17.80000 32.81900  -21.73800 1.000 53.63000  ? 214 PRO   A HD3    1 
ATOM   2993 N N      . LYS   A 1 249 ? -12.58600 33.83300  -20.18600 0.850 43.67000  ? 215 LYS   A N      1 
ATOM   2994 C CA     . LYS   A 1 249 ? -11.17500 33.53500  -20.47100 0.850 57.39000  ? 215 LYS   A CA     1 
ATOM   2995 C C      . LYS   A 1 249 ? -10.69900 34.18700  -21.76900 0.850 55.85000  ? 215 LYS   A C      1 
ATOM   2996 O O      . LYS   A 1 249 ? -9.87900  33.62300  -22.49700 0.850 42.45000  ? 215 LYS   A O      1 
ATOM   2997 C CB     . LYS   A 1 249 ? -10.92700 32.02300  -20.52900 0.850 51.73000  ? 215 LYS   A CB     1 
ATOM   2998 C CG     . LYS   A 1 249 ? -10.25700 31.40700  -19.31600 0.850 56.36000  ? 215 LYS   A CG     1 
ATOM   2999 C CD     . LYS   A 1 249 ? -10.25100 29.87000  -19.40700 0.850 63.82000  ? 215 LYS   A CD     1 
ATOM   3000 C CE     . LYS   A 1 249 ? -8.98100  29.36200  -20.07400 0.850 62.16000  ? 215 LYS   A CE     1 
ATOM   3001 N NZ     . LYS   A 1 249 ? -7.81900  30.18800  -19.62800 0.850 68.86000  ? 215 LYS   A NZ     1 
ATOM   3002 H H      . LYS   A 1 249 ? -12.70400 34.29800  -19.47200 0.850 43.67000  ? 215 LYS   A H      1 
ATOM   3003 H HA     . LYS   A 1 249 ? -10.63400 33.89200  -19.75000 0.850 57.39000  ? 215 LYS   A HA     1 
ATOM   3004 H HB2    . LYS   A 1 249 ? -11.77900 31.57400  -20.63600 0.850 51.73000  ? 215 LYS   A HB2    1 
ATOM   3005 H HB3    . LYS   A 1 249 ? -10.36700 31.81700  -21.29100 0.850 51.73000  ? 215 LYS   A HB3    1 
ATOM   3006 H HG2    . LYS   A 1 249 ? -9.36800  31.77100  -19.22500 0.850 56.36000  ? 215 LYS   A HG2    1 
ATOM   3007 H HG3    . LYS   A 1 249 ? -10.77700 31.64300  -18.53200 0.850 56.36000  ? 215 LYS   A HG3    1 
ATOM   3008 H HD2    . LYS   A 1 249 ? -10.29500 29.49600  -18.51300 0.850 63.82000  ? 215 LYS   A HD2    1 
ATOM   3009 H HD3    . LYS   A 1 249 ? -11.01000 29.57400  -19.93300 0.850 63.82000  ? 215 LYS   A HD3    1 
ATOM   3010 H HE2    . LYS   A 1 249 ? -8.82300  28.44000  -19.81700 0.850 62.16000  ? 215 LYS   A HE2    1 
ATOM   3011 H HE3    . LYS   A 1 249 ? -9.06500  29.43900  -21.03700 0.850 62.16000  ? 215 LYS   A HE3    1 
ATOM   3012 H HZ1    . LYS   A 1 249 ? -7.06400  29.73100  -19.74300 0.850 68.86000  ? 215 LYS   A HZ1    1 
ATOM   3013 H HZ2    . LYS   A 1 249 ? -7.77400  30.93800  -20.10400 0.850 68.86000  ? 215 LYS   A HZ2    1 
ATOM   3014 H HZ3    . LYS   A 1 249 ? -7.90100  30.39100  -18.76500 0.850 68.86000  ? 215 LYS   A HZ3    1 
ATOM   3015 N N      . GLN   A 1 250 ? -11.21100 35.38400  -22.06900 1.000 49.77000  ? 216 GLN   A N      1 
ATOM   3016 C CA     . GLN   A 1 250 ? -10.81900 36.11600  -23.28000 1.000 46.38000  ? 216 GLN   A CA     1 
ATOM   3017 C C      . GLN   A 1 250 ? -11.03400 35.28900  -24.54800 1.000 39.88000  ? 216 GLN   A C      1 
ATOM   3018 O O      . GLN   A 1 250 ? -10.30900 35.45000  -25.53600 1.000 44.08000  ? 216 GLN   A O      1 
ATOM   3019 C CB     . GLN   A 1 250 ? -9.36200  36.57700  -23.20800 1.000 38.55000  ? 216 GLN   A CB     1 
ATOM   3020 C CG     . GLN   A 1 250 ? -9.12000  37.65200  -22.17700 1.000 60.15000  ? 216 GLN   A CG     1 
ATOM   3021 C CD     . GLN   A 1 250 ? -7.89400  37.37500  -21.34500 1.000 69.77000  ? 216 GLN   A CD     1 
ATOM   3022 O OE1    . GLN   A 1 250 ? -6.76200  37.53300  -21.80900 1.000 76.16000  ? 216 GLN   A OE1    1 
ATOM   3023 N NE2    . GLN   A 1 250 ? -8.10900  36.94700  -20.10500 1.000 71.56000  ? 216 GLN   A NE2    1 
ATOM   3024 H H      . GLN   A 1 250 ? -11.79000 35.79700  -21.58500 1.000 49.77000  ? 216 GLN   A H      1 
ATOM   3025 H HA     . GLN   A 1 250 ? -11.37300 36.90900  -23.35200 1.000 46.38000  ? 216 GLN   A HA     1 
ATOM   3026 H HB2    . GLN   A 1 250 ? -8.80200  35.81800  -22.98300 1.000 38.55000  ? 216 GLN   A HB2    1 
ATOM   3027 H HB3    . GLN   A 1 250 ? -9.10200  36.93400  -24.07100 1.000 38.55000  ? 216 GLN   A HB3    1 
ATOM   3028 H HG2    . GLN   A 1 250 ? -8.99400  38.50200  -22.62700 1.000 60.15000  ? 216 GLN   A HG2    1 
ATOM   3029 H HG3    . GLN   A 1 250 ? -9.88500  37.70000  -21.58200 1.000 60.15000  ? 216 GLN   A HG3    1 
ATOM   3030 H HE21   . GLN   A 1 250 ? -8.91300  36.84700  -19.81800 1.000 71.56000  ? 216 GLN   A HE21   1 
ATOM   3031 H HE22   . GLN   A 1 250 ? -7.44400  36.77300  -19.58900 1.000 71.56000  ? 216 GLN   A HE22   1 
ATOM   3032 N N      . GLY   A 1 251 ? -12.01800 34.39700  -24.52900 1.000 36.86000  ? 217 GLY   A N      1 
ATOM   3033 C CA     . GLY   A 1 251 ? -12.38600 33.62700  -25.70000 1.000 40.44000  ? 217 GLY   A CA     1 
ATOM   3034 C C      . GLY   A 1 251 ? -11.67300 32.29700  -25.86800 1.000 35.95000  ? 217 GLY   A C      1 
ATOM   3035 O O      . GLY   A 1 251 ? -12.01900 31.54300  -26.79400 1.000 37.98000  ? 217 GLY   A O      1 
ATOM   3036 H H      . GLY   A 1 251 ? -12.49400 34.22000  -23.83500 1.000 36.86000  ? 217 GLY   A H      1 
ATOM   3037 H HA2    . GLY   A 1 251 ? -13.33900 33.44900  -25.66900 1.000 40.44000  ? 217 GLY   A HA2    1 
ATOM   3038 H HA3    . GLY   A 1 251 ? -12.20900 34.15900  -26.49100 1.000 40.44000  ? 217 GLY   A HA3    1 
ATOM   3039 N N      . PHE   A 1 252 ? -10.68800 31.98900  -25.02500 1.000 35.25000  ? 218 PHE   A N      1 
ATOM   3040 C CA     . PHE   A 1 252 ? -9.98000  30.71000  -25.11500 1.000 34.72000  ? 218 PHE   A CA     1 
ATOM   3041 C C      . PHE   A 1 252 ? -10.86100 29.60000  -24.53900 1.000 42.11000  ? 218 PHE   A C      1 
ATOM   3042 O O      . PHE   A 1 252 ? -11.52700 29.79800  -23.51900 1.000 43.03000  ? 218 PHE   A O      1 
ATOM   3043 C CB     . PHE   A 1 252 ? -8.64600  30.78500  -24.36100 1.000 32.67000  ? 218 PHE   A CB     1 
ATOM   3044 C CG     . PHE   A 1 252 ? -7.63900  31.74700  -24.97400 1.000 37.92000  ? 218 PHE   A CG     1 
ATOM   3045 C CD1    . PHE   A 1 252 ? -7.74500  33.12600  -24.75700 1.000 35.61000  ? 218 PHE   A CD1    1 
ATOM   3046 C CD2    . PHE   A 1 252 ? -6.58000  31.27600  -25.75700 1.000 42.33000  ? 218 PHE   A CD2    1 
ATOM   3047 C CE1    . PHE   A 1 252 ? -6.82500  34.01000  -25.31400 1.000 38.55000  ? 218 PHE   A CE1    1 
ATOM   3048 C CE2    . PHE   A 1 252 ? -5.65000  32.17200  -26.33100 1.000 35.19000  ? 218 PHE   A CE2    1 
ATOM   3049 C CZ     . PHE   A 1 252 ? -5.78100  33.53900  -26.10700 1.000 33.52000  ? 218 PHE   A CZ     1 
ATOM   3050 H H      . PHE   A 1 252 ? -10.41000 32.50100  -24.39300 1.000 35.25000  ? 218 PHE   A H      1 
ATOM   3051 H HA     . PHE   A 1 252 ? -9.79800  30.51300  -26.04500 1.000 34.72000  ? 218 PHE   A HA     1 
ATOM   3052 H HB2    . PHE   A 1 252 ? -8.81800  31.07700  -23.45200 1.000 32.67000  ? 218 PHE   A HB2    1 
ATOM   3053 H HB3    . PHE   A 1 252 ? -8.24400  29.90200  -24.35100 1.000 32.67000  ? 218 PHE   A HB3    1 
ATOM   3054 H HD1    . PHE   A 1 252 ? -8.44100  33.45600  -24.23700 1.000 35.61000  ? 218 PHE   A HD1    1 
ATOM   3055 H HD2    . PHE   A 1 252 ? -6.49600  30.36300  -25.91400 1.000 42.33000  ? 218 PHE   A HD2    1 
ATOM   3056 H HE1    . PHE   A 1 252 ? -6.91400  34.92300  -25.16400 1.000 38.55000  ? 218 PHE   A HE1    1 
ATOM   3057 H HE2    . PHE   A 1 252 ? -4.95100  31.84900  -26.85300 1.000 35.19000  ? 218 PHE   A HE2    1 
ATOM   3058 H HZ     . PHE   A 1 252 ? -5.16700  34.13400  -26.47400 1.000 33.52000  ? 218 PHE   A HZ     1 
ATOM   3059 N N      . GLY   A 1 253 ? -10.86900 28.43100  -25.19800 1.000 36.62000  ? 219 GLY   A N      1 
ATOM   3060 C CA     . GLY   A 1 253 ? -11.69600 27.31900  -24.75100 1.000 37.08000  ? 219 GLY   A CA     1 
ATOM   3061 C C      . GLY   A 1 253 ? -11.24200 26.01100  -25.36000 1.000 36.80000  ? 219 GLY   A C      1 
ATOM   3062 O O      . GLY   A 1 253 ? -10.35200 25.97900  -26.21200 1.000 37.45000  ? 219 GLY   A O      1 
ATOM   3063 H H      . GLY   A 1 253 ? -10.40400 28.26500  -25.90200 1.000 36.62000  ? 219 GLY   A H      1 
ATOM   3064 H HA2    . GLY   A 1 253 ? -11.64800 27.24500  -23.78500 1.000 37.08000  ? 219 GLY   A HA2    1 
ATOM   3065 H HA3    . GLY   A 1 253 ? -12.61900 27.47600  -25.00500 1.000 37.08000  ? 219 GLY   A HA3    1 
ATOM   3066 N N      . GLY   A 1 254 ? -11.88100 24.92200  -24.92200 1.000 38.52000  ? 220 GLY   A N      1 
ATOM   3067 C CA     . GLY   A 1 254 ? -11.47900 23.59100  -25.38400 1.000 34.63000  ? 220 GLY   A CA     1 
ATOM   3068 C C      . GLY   A 1 254 ? -12.10500 23.23300  -26.72900 1.000 36.24000  ? 220 GLY   A C      1 
ATOM   3069 O O      . GLY   A 1 254 ? -13.29800 23.44300  -26.97100 1.000 36.89000  ? 220 GLY   A O      1 
ATOM   3070 H H      . GLY   A 1 254 ? -12.53800 24.92600  -24.36700 1.000 38.52000  ? 220 GLY   A H      1 
ATOM   3071 H HA2    . GLY   A 1 254 ? -10.51400 23.55700  -25.47500 1.000 34.63000  ? 220 GLY   A HA2    1 
ATOM   3072 H HA3    . GLY   A 1 254 ? -11.75000 22.92600  -24.73200 1.000 34.63000  ? 220 GLY   A HA3    1 
ATOM   3073 N N      . LEU   A 1 255 ? -11.28200 22.64800  -27.59900 1.000 32.70000  ? 221 LEU   A N      1 
ATOM   3074 C CA     . LEU   A 1 255 ? -11.70400 22.23600  -28.93400 1.000 30.83000  ? 221 LEU   A CA     1 
ATOM   3075 C C      . LEU   A 1 255 ? -12.15800 20.78700  -28.93300 1.000 36.10000  ? 221 LEU   A C      1 
ATOM   3076 O O      . LEU   A 1 255 ? -11.50800 19.92600  -28.32600 1.000 33.25000  ? 221 LEU   A O      1 
ATOM   3077 C CB     . LEU   A 1 255 ? -10.55000 22.37300  -29.92700 1.000 34.31000  ? 221 LEU   A CB     1 
ATOM   3078 C CG     . LEU   A 1 255 ? -9.93100  23.75400  -30.01300 1.000 43.07000  ? 221 LEU   A CG     1 
ATOM   3079 C CD1    . LEU   A 1 255 ? -8.67900  23.69300  -30.89300 1.000 32.97000  ? 221 LEU   A CD1    1 
ATOM   3080 C CD2    . LEU   A 1 255 ? -10.98900 24.71600  -30.58900 1.000 38.59000  ? 221 LEU   A CD2    1 
ATOM   3081 H H      . LEU   A 1 255 ? -10.45600 22.47600  -27.43300 1.000 32.70000  ? 221 LEU   A H      1 
ATOM   3082 H HA     . LEU   A 1 255 ? -12.44100 22.79100  -29.23100 1.000 30.83000  ? 221 LEU   A HA     1 
ATOM   3083 H HB2    . LEU   A 1 255 ? -9.84900  21.75500  -29.67000 1.000 34.31000  ? 221 LEU   A HB2    1 
ATOM   3084 H HB3    . LEU   A 1 255 ? -10.87600 22.14400  -30.81100 1.000 34.31000  ? 221 LEU   A HB3    1 
ATOM   3085 H HG     . LEU   A 1 255 ? -9.67800  24.05900  -29.12800 1.000 43.07000  ? 221 LEU   A HG     1 
ATOM   3086 H HD11   . LEU   A 1 255 ? -8.25500  24.56500  -30.89900 1.000 32.97000  ? 221 LEU   A HD11   1 
ATOM   3087 H HD12   . LEU   A 1 255 ? -8.07000  23.03100  -30.52900 1.000 32.97000  ? 221 LEU   A HD12   1 
ATOM   3088 H HD13   . LEU   A 1 255 ? -8.93800  23.44400  -31.79400 1.000 32.97000  ? 221 LEU   A HD13   1 
ATOM   3089 H HD21   . LEU   A 1 255 ? -10.57100 25.57300  -30.76900 1.000 38.59000  ? 221 LEU   A HD21   1 
ATOM   3090 H HD22   . LEU   A 1 255 ? -11.34200 24.34100  -31.41100 1.000 38.59000  ? 221 LEU   A HD22   1 
ATOM   3091 H HD23   . LEU   A 1 255 ? -11.70300 24.82600  -29.94200 1.000 38.59000  ? 221 LEU   A HD23   1 
ATOM   3092 N N      . GLY   A 1 256 ? -13.26000 20.52400  -29.64400 1.000 32.33000  ? 222 GLY   A N      1 
ATOM   3093 C CA     . GLY   A 1 256 ? -13.71800 19.17000  -29.86700 1.000 32.66000  ? 222 GLY   A CA     1 
ATOM   3094 C C      . GLY   A 1 256 ? -14.16300 18.99800  -31.30700 1.000 36.62000  ? 222 GLY   A C      1 
ATOM   3095 O O      . GLY   A 1 256 ? -14.25800 19.96400  -32.07400 1.000 39.39000  ? 222 GLY   A O      1 
ATOM   3096 H H      . GLY   A 1 256 ? -13.75700 21.12500  -30.00700 1.000 32.33000  ? 222 GLY   A H      1 
ATOM   3097 H HA2    . GLY   A 1 256 ? -13.00200 18.54300  -29.68300 1.000 32.66000  ? 222 GLY   A HA2    1 
ATOM   3098 H HA3    . GLY   A 1 256 ? -14.46600 18.97400  -29.28100 1.000 32.66000  ? 222 GLY   A HA3    1 
ATOM   3099 N N      . GLY   A 1 257 ? -14.42800 17.74900  -31.67400 1.000 33.85000  ? 223 GLY   A N      1 
ATOM   3100 C CA     . GLY   A 1 257 ? -14.90200 17.49600  -33.02300 1.000 36.22000  ? 223 GLY   A CA     1 
ATOM   3101 C C      . GLY   A 1 257 ? -13.82600 17.16700  -34.03800 1.000 35.10000  ? 223 GLY   A C      1 
ATOM   3102 O O      . GLY   A 1 257 ? -12.79500 16.58200  -33.69100 1.000 36.56000  ? 223 GLY   A O      1 
ATOM   3103 H H      . GLY   A 1 257 ? -14.34400 17.05200  -31.17700 1.000 33.85000  ? 223 GLY   A H      1 
ATOM   3104 H HA2    . GLY   A 1 257 ? -15.52300 16.75100  -33.00000 1.000 36.22000  ? 223 GLY   A HA2    1 
ATOM   3105 H HA3    . GLY   A 1 257 ? -15.38400 18.27500  -33.34100 1.000 36.22000  ? 223 GLY   A HA3    1 
ATOM   3106 N N      . ARG   A 1 258 ? -14.05100 17.55200  -35.30400 1.000 30.29000  ? 224 ARG   A N      1 
ATOM   3107 C CA     . ARG   A 1 258 ? -13.17100 17.09600  -36.37500 1.000 36.46000  ? 224 ARG   A CA     1 
ATOM   3108 C C      . ARG   A 1 258 ? -11.74800 17.60200  -36.17900 1.000 31.76000  ? 224 ARG   A C      1 
ATOM   3109 O O      . ARG   A 1 258 ? -10.79100 16.95100  -36.63000 1.000 37.16000  ? 224 ARG   A O      1 
ATOM   3110 C CB     . ARG   A 1 258 ? -13.72400 17.52400  -37.73200 1.000 39.15000  ? 224 ARG   A CB     1 
ATOM   3111 C CG     . ARG   A 1 258 ? -14.97200 16.74400  -38.10100 1.000 37.72000  ? 224 ARG   A CG     1 
ATOM   3112 C CD     . ARG   A 1 258 ? -15.42600 17.04500  -39.50100 1.000 53.76000  ? 224 ARG   A CD     1 
ATOM   3113 N NE     . ARG   A 1 258 ? -16.88200 17.07100  -39.57700 1.000 62.36000  ? 224 ARG   A NE     1 
ATOM   3114 C CZ     . ARG   A 1 258 ? -17.64200 16.01900  -39.85500 1.000 71.03000  ? 224 ARG   A CZ     1 
ATOM   3115 N NH1    . ARG   A 1 258 ? -17.11700 14.82100  -40.07600 1.000 59.92000  ? 224 ARG   A NH1    1 
ATOM   3116 N NH2    . ARG   A 1 258 ? -18.96200 16.17300  -39.91900 1.000 64.68000  ? 224 ARG   A NH2    1 
ATOM   3117 H H      . ARG   A 1 258 ? -14.69300 18.06500  -35.55800 1.000 30.29000  ? 224 ARG   A H      1 
ATOM   3118 H HA     . ARG   A 1 258 ? -13.14300 16.12700  -36.36100 1.000 36.46000  ? 224 ARG   A HA     1 
ATOM   3119 H HB2    . ARG   A 1 258 ? -13.93900 18.46400  -37.72800 1.000 39.15000  ? 224 ARG   A HB2    1 
ATOM   3120 H HB3    . ARG   A 1 258 ? -13.05400 17.34500  -38.41000 1.000 39.15000  ? 224 ARG   A HB3    1 
ATOM   3121 H HG2    . ARG   A 1 258 ? -14.78500 15.79400  -38.04100 1.000 37.72000  ? 224 ARG   A HG2    1 
ATOM   3122 H HG3    . ARG   A 1 258 ? -15.68900 16.98400  -37.49300 1.000 37.72000  ? 224 ARG   A HG3    1 
ATOM   3123 H HD2    . ARG   A 1 258 ? -15.09400 17.91800  -39.76300 1.000 53.76000  ? 224 ARG   A HD2    1 
ATOM   3124 H HD3    . ARG   A 1 258 ? -15.09100 16.36500  -40.10500 1.000 53.76000  ? 224 ARG   A HD3    1 
ATOM   3125 H HE     . ARG   A 1 258 ? -17.27600 17.82100  -39.43100 1.000 62.36000  ? 224 ARG   A HE     1 
ATOM   3126 H HH11   . ARG   A 1 258 ? -16.26600 14.70600  -40.03900 1.000 59.92000  ? 224 ARG   A HH11   1 
ATOM   3127 H HH12   . ARG   A 1 258 ? -17.63100 14.15500  -40.25400 1.000 59.92000  ? 224 ARG   A HH12   1 
ATOM   3128 H HH21   . ARG   A 1 258 ? -19.31200 16.94600  -39.77800 1.000 64.68000  ? 224 ARG   A HH21   1 
ATOM   3129 H HH22   . ARG   A 1 258 ? -19.46500 15.49900  -40.09800 1.000 64.68000  ? 224 ARG   A HH22   1 
ATOM   3130 N N      . TYR   A 1 259 ? -11.58600 18.74400  -35.49500 1.000 28.79000  ? 225 TYR   A N      1 
ATOM   3131 C CA     . TYR   A 1 259 ? -10.24300 19.27100  -35.24200 1.000 34.86000  ? 225 TYR   A CA     1 
ATOM   3132 C C      . TYR   A 1 259 ? -9.34100  18.28300  -34.52700 1.000 32.31000  ? 225 TYR   A C      1 
ATOM   3133 O O      . TYR   A 1 259 ? -8.11800  18.33200  -34.70600 1.000 33.83000  ? 225 TYR   A O      1 
ATOM   3134 C CB     . TYR   A 1 259 ? -10.28700 20.51200  -34.37200 1.000 31.39000  ? 225 TYR   A CB     1 
ATOM   3135 C CG     . TYR   A 1 259 ? -11.02000 21.64600  -34.99100 1.000 35.36000  ? 225 TYR   A CG     1 
ATOM   3136 C CD1    . TYR   A 1 259 ? -10.44200 22.40500  -36.00100 1.000 34.86000  ? 225 TYR   A CD1    1 
ATOM   3137 C CD2    . TYR   A 1 259 ? -12.29600 21.97400  -34.55300 1.000 39.89000  ? 225 TYR   A CD2    1 
ATOM   3138 C CE1    . TYR   A 1 259 ? -11.12800 23.47700  -36.57100 1.000 36.35000  ? 225 TYR   A CE1    1 
ATOM   3139 C CE2    . TYR   A 1 259 ? -12.99300 23.04100  -35.11600 1.000 44.37000  ? 225 TYR   A CE2    1 
ATOM   3140 C CZ     . TYR   A 1 259 ? -12.40900 23.77900  -36.12600 1.000 47.53000  ? 225 TYR   A CZ     1 
ATOM   3141 O OH     . TYR   A 1 259 ? -13.12200 24.82800  -36.68300 1.000 43.93000  ? 225 TYR   A OH     1 
ATOM   3142 H H      . TYR   A 1 259 ? -12.22500 19.22200  -35.17400 1.000 28.79000  ? 225 TYR   A H      1 
ATOM   3143 H HA     . TYR   A 1 259 ? -9.82800  19.50600  -36.08700 1.000 34.86000  ? 225 TYR   A HA     1 
ATOM   3144 H HB2    . TYR   A 1 259 ? -10.72900 20.29300  -33.53600 1.000 31.39000  ? 225 TYR   A HB2    1 
ATOM   3145 H HB3    . TYR   A 1 259 ? -9.37900  20.80500  -34.19800 1.000 31.39000  ? 225 TYR   A HB3    1 
ATOM   3146 H HD1    . TYR   A 1 259 ? -9.58600  22.19700  -36.29900 1.000 34.86000  ? 225 TYR   A HD1    1 
ATOM   3147 H HD2    . TYR   A 1 259 ? -12.69100 21.47400  -33.87600 1.000 39.89000  ? 225 TYR   A HD2    1 
ATOM   3148 H HE1    . TYR   A 1 259 ? -10.73800 23.97500  -37.25300 1.000 36.35000  ? 225 TYR   A HE1    1 
ATOM   3149 H HE2    . TYR   A 1 259 ? -13.85100 23.24700  -34.82200 1.000 44.37000  ? 225 TYR   A HE2    1 
ATOM   3150 H HH     . TYR   A 1 259 ? -13.87600 24.88900  -36.31700 1.000 43.93000  ? 225 TYR   A HH     1 
ATOM   3151 N N      . VAL   A 1 260 ? -9.90000  17.45700  -33.63800 1.000 32.69000  ? 226 VAL   A N      1 
ATOM   3152 C CA     . VAL   A 1 260 ? -9.08200  16.73600  -32.66500 1.000 36.72000  ? 226 VAL   A CA     1 
ATOM   3153 C C      . VAL   A 1 260 ? -8.89900  15.26500  -33.01500 1.000 31.30000  ? 226 VAL   A C      1 
ATOM   3154 O O      . VAL   A 1 260 ? -8.25000  14.53500  -32.25300 1.000 31.56000  ? 226 VAL   A O      1 
ATOM   3155 C CB     . VAL   A 1 260 ? -9.67300  16.86300  -31.24200 1.000 32.65000  ? 226 VAL   A CB     1 
ATOM   3156 C CG1    . VAL   A 1 260 ? -10.03900 18.32000  -30.91800 1.000 32.01000  ? 226 VAL   A CG1    1 
ATOM   3157 C CG2    . VAL   A 1 260 ? -10.87800 15.93800  -31.07800 1.000 33.63000  ? 226 VAL   A CG2    1 
ATOM   3158 H H      . VAL   A 1 260 ? -10.74300 17.29900  -33.57900 1.000 32.69000  ? 226 VAL   A H      1 
ATOM   3159 H HA     . VAL   A 1 260 ? -8.20000  17.13900  -32.64500 1.000 36.72000  ? 226 VAL   A HA     1 
ATOM   3160 H HB     . VAL   A 1 260 ? -9.00000  16.58200  -30.60300 1.000 32.65000  ? 226 VAL   A HB     1 
ATOM   3161 H HG11   . VAL   A 1 260 ? -10.28700 18.38200  -29.98200 1.000 32.01000  ? 226 VAL   A HG11   1 
ATOM   3162 H HG12   . VAL   A 1 260 ? -9.27100  18.88500  -31.09500 1.000 32.01000  ? 226 VAL   A HG12   1 
ATOM   3163 H HG13   . VAL   A 1 260 ? -10.78400 18.59100  -31.47600 1.000 32.01000  ? 226 VAL   A HG13   1 
ATOM   3164 H HG21   . VAL   A 1 260 ? -11.42800 16.26400  -30.34900 1.000 33.63000  ? 226 VAL   A HG21   1 
ATOM   3165 H HG22   . VAL   A 1 260 ? -11.38800 15.93600  -31.90200 1.000 33.63000  ? 226 VAL   A HG22   1 
ATOM   3166 H HG23   . VAL   A 1 260 ? -10.56500 15.04100  -30.88200 1.000 33.63000  ? 226 VAL   A HG23   1 
ATOM   3167 N N      . PHE   A 1 261 ? -9.42700  14.81300  -34.14900 1.000 29.94000  ? 227 PHE   A N      1 
ATOM   3168 C CA     . PHE   A 1 261 ? -9.46500  13.37200  -34.40700 1.000 30.03000  ? 227 PHE   A CA     1 
ATOM   3169 C C      . PHE   A 1 261 ? -8.07000  12.76300  -34.56000 1.000 34.36000  ? 227 PHE   A C      1 
ATOM   3170 O O      . PHE   A 1 261 ? -7.77800  11.76900  -33.87100 1.000 33.19000  ? 227 PHE   A O      1 
ATOM   3171 C CB     . PHE   A 1 261 ? -10.36900 13.09800  -35.61300 1.000 31.27000  ? 227 PHE   A CB     1 
ATOM   3172 C CG     . PHE   A 1 261 ? -10.50900 11.63100  -35.96700 1.000 30.10000  ? 227 PHE   A CG     1 
ATOM   3173 C CD1    . PHE   A 1 261 ? -11.01400 10.71800  -35.05100 1.000 36.02000  ? 227 PHE   A CD1    1 
ATOM   3174 C CD2    . PHE   A 1 261 ? -10.18600 11.19100  -37.23500 1.000 38.33000  ? 227 PHE   A CD2    1 
ATOM   3175 C CE1    . PHE   A 1 261 ? -11.16800 9.37600   -35.39700 1.000 33.74000  ? 227 PHE   A CE1    1 
ATOM   3176 C CE2    . PHE   A 1 261 ? -10.33700 9.85400   -37.59200 1.000 43.19000  ? 227 PHE   A CE2    1 
ATOM   3177 C CZ     . PHE   A 1 261 ? -10.82900 8.95400   -36.67100 1.000 38.36000  ? 227 PHE   A CZ     1 
ATOM   3178 H H      . PHE   A 1 261 ? -9.76200  15.30200  -34.77200 1.000 29.94000  ? 227 PHE   A H      1 
ATOM   3179 H HA     . PHE   A 1 261 ? -9.87700  12.94200  -33.64100 1.000 30.03000  ? 227 PHE   A HA     1 
ATOM   3180 H HB2    . PHE   A 1 261 ? -11.25600 13.43700  -35.41700 1.000 31.27000  ? 227 PHE   A HB2    1 
ATOM   3181 H HB3    . PHE   A 1 261 ? -10.01200 13.55500  -36.38900 1.000 31.27000  ? 227 PHE   A HB3    1 
ATOM   3182 H HD1    . PHE   A 1 261 ? -11.24500 11.00300  -34.19600 1.000 36.02000  ? 227 PHE   A HD1    1 
ATOM   3183 H HD2    . PHE   A 1 261 ? -9.85800  11.79700  -37.86000 1.000 38.33000  ? 227 PHE   A HD2    1 
ATOM   3184 H HE1    . PHE   A 1 261 ? -11.49800 8.76800   -34.77500 1.000 33.74000  ? 227 PHE   A HE1    1 
ATOM   3185 H HE2    . PHE   A 1 261 ? -10.10600 9.56900   -38.44700 1.000 43.19000  ? 227 PHE   A HE2    1 
ATOM   3186 H HZ     . PHE   A 1 261 ? -10.92400 8.05900   -36.90300 1.000 38.36000  ? 227 PHE   A HZ     1 
ATOM   3187 N N      . PRO   A 1 262 ? -7.16600  13.28300  -35.40100 1.000 30.70000  ? 228 PRO   A N      1 
ATOM   3188 C CA     . PRO   A 1 262 ? -5.82500  12.67600  -35.44400 1.000 30.02000  ? 228 PRO   A CA     1 
ATOM   3189 C C      . PRO   A 1 262 ? -5.09200  12.78200  -34.12100 1.000 28.73000  ? 228 PRO   A C      1 
ATOM   3190 O O      . PRO   A 1 262 ? -4.29900  11.89100  -33.80400 1.000 29.51000  ? 228 PRO   A O      1 
ATOM   3191 C CB     . PRO   A 1 262 ? -5.08500  13.46100  -36.54400 1.000 32.27000  ? 228 PRO   A CB     1 
ATOM   3192 C CG     . PRO   A 1 262 ? -6.14100  14.26300  -37.26700 1.000 38.28000  ? 228 PRO   A CG     1 
ATOM   3193 C CD     . PRO   A 1 262 ? -7.26300  14.46500  -36.28200 1.000 32.47000  ? 228 PRO   A CD     1 
ATOM   3194 H HA     . PRO   A 1 262 ? -5.88600  11.74300  -35.70300 1.000 30.02000  ? 228 PRO   A HA     1 
ATOM   3195 H HB2    . PRO   A 1 262 ? -4.43000  14.04900  -36.13700 1.000 32.27000  ? 228 PRO   A HB2    1 
ATOM   3196 H HB3    . PRO   A 1 262 ? -4.65400  12.84000  -37.15200 1.000 32.27000  ? 228 PRO   A HB3    1 
ATOM   3197 H HG2    . PRO   A 1 262 ? -5.77000  15.11700  -37.53900 1.000 38.28000  ? 228 PRO   A HG2    1 
ATOM   3198 H HG3    . PRO   A 1 262 ? -6.45200  13.76600  -38.04000 1.000 38.28000  ? 228 PRO   A HG3    1 
ATOM   3199 H HD2    . PRO   A 1 262 ? -7.12700  15.27900  -35.77600 1.000 32.47000  ? 228 PRO   A HD2    1 
ATOM   3200 H HD3    . PRO   A 1 262 ? -8.11300  14.47700  -36.74600 1.000 32.47000  ? 228 PRO   A HD3    1 
ATOM   3201 N N      . THR   A 1 263 ? -5.30200  13.85900  -33.35100 1.000 28.21000  ? 229 THR   A N      1 
ATOM   3202 C CA     . THR   A 1 263 ? -4.66700  13.92600  -32.03900 1.000 29.69000  ? 229 THR   A CA     1 
ATOM   3203 C C      . THR   A 1 263 ? -5.23400  12.86200  -31.10300 1.000 32.45000  ? 229 THR   A C      1 
ATOM   3204 O O      . THR   A 1 263 ? -4.48600  12.22700  -30.35000 1.000 31.09000  ? 229 THR   A O      1 
ATOM   3205 C CB     . THR   A 1 263 ? -4.83400  15.31600  -31.43300 1.000 31.04000  ? 229 THR   A CB     1 
ATOM   3206 O OG1    . THR   A 1 263 ? -4.18600  16.28400  -32.27800 1.000 30.45000  ? 229 THR   A OG1    1 
ATOM   3207 C CG2    . THR   A 1 263 ? -4.20700  15.33700  -30.05000 1.000 29.17000  ? 229 THR   A CG2    1 
ATOM   3208 H H      . THR   A 1 263 ? -5.78900  14.53600  -33.55900 1.000 28.21000  ? 229 THR   A H      1 
ATOM   3209 H HA     . THR   A 1 263 ? -3.71700  13.75800  -32.14100 1.000 29.69000  ? 229 THR   A HA     1 
ATOM   3210 H HB     . THR   A 1 263 ? -5.77700  15.52900  -31.35200 1.000 31.04000  ? 229 THR   A HB     1 
ATOM   3211 H HG1    . THR   A 1 263 ? -4.53000  16.27300  -33.04400 1.000 30.45000  ? 229 THR   A HG1    1 
ATOM   3212 H HG21   . THR   A 1 263 ? -4.05700  16.25400  -29.77100 1.000 29.17000  ? 229 THR   A HG21   1 
ATOM   3213 H HG22   . THR   A 1 263 ? -4.79400  14.90700  -29.40900 1.000 29.17000  ? 229 THR   A HG22   1 
ATOM   3214 H HG23   . THR   A 1 263 ? -3.35600  14.87100  -30.06400 1.000 29.17000  ? 229 THR   A HG23   1 
ATOM   3215 N N      . ALA   A 1 264 ? -6.55400  12.65500  -31.14300 1.000 30.68000  ? 230 ALA   A N      1 
ATOM   3216 C CA     . ALA   A 1 264 ? -7.18100  11.62900  -30.30800 1.000 34.06000  ? 230 ALA   A CA     1 
ATOM   3217 C C      . ALA   A 1 264 ? -6.66800  10.23600  -30.65500 1.000 29.45000  ? 230 ALA   A C      1 
ATOM   3218 O O      . ALA   A 1 264 ? -6.32700  9.45700   -29.75300 1.000 30.65000  ? 230 ALA   A O      1 
ATOM   3219 C CB     . ALA   A 1 264 ? -8.71000  11.69400  -30.43800 1.000 30.97000  ? 230 ALA   A CB     1 
ATOM   3220 H H      . ALA   A 1 264 ? -7.10300  13.09200  -31.64100 1.000 30.68000  ? 230 ALA   A H      1 
ATOM   3221 H HA     . ALA   A 1 264 ? -6.95600  11.80300  -29.38100 1.000 34.06000  ? 230 ALA   A HA     1 
ATOM   3222 H HB1    . ALA   A 1 264 ? -9.10400  11.00700  -29.87800 1.000 30.97000  ? 230 ALA   A HB1    1 
ATOM   3223 H HB2    . ALA   A 1 264 ? -9.01400  12.56900  -30.15200 1.000 30.97000  ? 230 ALA   A HB2    1 
ATOM   3224 H HB3    . ALA   A 1 264 ? -8.95400  11.54600  -31.36500 1.000 30.97000  ? 230 ALA   A HB3    1 
ATOM   3225 N N      . LEU   A 1 265 ? -6.61600  9.89200   -31.95800 1.000 27.87000  ? 231 LEU   A N      1 
ATOM   3226 C CA     . LEU   A 1 265 ? -6.11600  8.56900   -32.34800 1.000 29.82000  ? 231 LEU   A CA     1 
ATOM   3227 C C      . LEU   A 1 265 ? -4.68500  8.35800   -31.86600 1.000 30.55000  ? 231 LEU   A C      1 
ATOM   3228 O O      . LEU   A 1 265 ? -4.32300  7.26300   -31.39500 1.000 28.86000  ? 231 LEU   A O      1 
ATOM   3229 C CB     . LEU   A 1 265 ? -6.17000  8.38800   -33.87000 1.000 31.71000  ? 231 LEU   A CB     1 
ATOM   3230 C CG     . LEU   A 1 265 ? -7.50700  8.18300   -34.58100 1.000 41.54000  ? 231 LEU   A CG     1 
ATOM   3231 C CD1    . LEU   A 1 265 ? -7.29900  7.90700   -36.07500 1.000 37.53000  ? 231 LEU   A CD1    1 
ATOM   3232 C CD2    . LEU   A 1 265 ? -8.34700  7.07400   -33.91300 1.000 33.49000  ? 231 LEU   A CD2    1 
ATOM   3233 H H      . LEU   A 1 265 ? -6.85800  10.39400  -32.61300 1.000 27.87000  ? 231 LEU   A H      1 
ATOM   3234 H HA     . LEU   A 1 265 ? -6.67200  7.88700   -31.94000 1.000 29.82000  ? 231 LEU   A HA     1 
ATOM   3235 H HB2    . LEU   A 1 265 ? -5.76700  9.17500   -34.26900 1.000 31.71000  ? 231 LEU   A HB2    1 
ATOM   3236 H HB3    . LEU   A 1 265 ? -5.62400  7.61700   -34.08800 1.000 31.71000  ? 231 LEU   A HB3    1 
ATOM   3237 H HG     . LEU   A 1 265 ? -8.01500  9.00700   -34.51100 1.000 41.54000  ? 231 LEU   A HG     1 
ATOM   3238 H HD11   . LEU   A 1 265 ? -8.16400  7.78000   -36.49600 1.000 37.53000  ? 231 LEU   A HD11   1 
ATOM   3239 H HD12   . LEU   A 1 265 ? -6.84400  8.66400   -36.47500 1.000 37.53000  ? 231 LEU   A HD12   1 
ATOM   3240 H HD13   . LEU   A 1 265 ? -6.76100  7.10600   -36.17600 1.000 37.53000  ? 231 LEU   A HD13   1 
ATOM   3241 H HD21   . LEU   A 1 265 ? -9.13400  6.90600   -34.45400 1.000 33.49000  ? 231 LEU   A HD21   1 
ATOM   3242 H HD22   . LEU   A 1 265 ? -7.81100  6.26800   -33.84900 1.000 33.49000  ? 231 LEU   A HD22   1 
ATOM   3243 H HD23   . LEU   A 1 265 ? -8.61100  7.36800   -33.02700 1.000 33.49000  ? 231 LEU   A HD23   1 
ATOM   3244 N N      . ALA   A 1 266 ? -3.84300  9.39200   -32.00600 1.000 28.41000  ? 232 ALA   A N      1 
ATOM   3245 C CA     . ALA   A 1 266 ? -2.45800  9.28200   -31.57000 1.000 27.12000  ? 232 ALA   A CA     1 
ATOM   3246 C C      . ALA   A 1 266 ? -2.38300  8.99500   -30.08700 1.000 28.15000  ? 232 ALA   A C      1 
ATOM   3247 O O      . ALA   A 1 266 ? -1.57600  8.17400   -29.64900 1.000 28.67000  ? 232 ALA   A O      1 
ATOM   3248 C CB     . ALA   A 1 266 ? -1.67100  10.56900  -31.87800 1.000 25.83000  ? 232 ALA   A CB     1 
ATOM   3249 H H      . ALA   A 1 266 ? -4.05200  10.15400  -32.34600 1.000 28.41000  ? 232 ALA   A H      1 
ATOM   3250 H HA     . ALA   A 1 266 ? -2.03400  8.54800   -32.04200 1.000 27.12000  ? 232 ALA   A HA     1 
ATOM   3251 H HB1    . ALA   A 1 266 ? -0.75500  10.45800  -31.58000 1.000 25.83000  ? 232 ALA   A HB1    1 
ATOM   3252 H HB2    . ALA   A 1 266 ? -1.69100  10.72900  -32.83400 1.000 25.83000  ? 232 ALA   A HB2    1 
ATOM   3253 H HB3    . ALA   A 1 266 ? -2.08400  11.31100  -31.40900 1.000 25.83000  ? 232 ALA   A HB3    1 
ATOM   3254 N N      . ASN   A 1 267 ? -3.19700  9.68300   -29.29500 1.000 27.69000  ? 233 ASN   A N      1 
ATOM   3255 C CA     . ASN   A 1 267 ? -3.15200  9.48200   -27.85800 1.000 28.75000  ? 233 ASN   A CA     1 
ATOM   3256 C C      . ASN   A 1 267 ? -3.69900  8.10800   -27.48500 1.000 30.04000  ? 233 ASN   A C      1 
ATOM   3257 O O      . ASN   A 1 267 ? -3.11300  7.40500   -26.65400 1.000 28.77000  ? 233 ASN   A O      1 
ATOM   3258 C CB     . ASN   A 1 267 ? -3.91300  10.61100  -27.15800 1.000 27.88000  ? 233 ASN   A CB     1 
ATOM   3259 C CG     . ASN   A 1 267 ? -3.03000  11.82900  -26.92500 1.000 30.93000  ? 233 ASN   A CG     1 
ATOM   3260 O OD1    . ASN   A 1 267 ? -2.56300  12.05400  -25.82300 1.000 31.45000  ? 233 ASN   A OD1    1 
ATOM   3261 N ND2    . ASN   A 1 267 ? -2.77000  12.58800  -27.98400 1.000 27.78000  ? 233 ASN   A ND2    1 
ATOM   3262 H H      . ASN   A 1 267 ? -3.77400  10.26200  -29.56200 1.000 27.69000  ? 233 ASN   A H      1 
ATOM   3263 H HA     . ASN   A 1 267 ? -2.22800  9.52200   -27.56600 1.000 28.75000  ? 233 ASN   A HA     1 
ATOM   3264 H HB2    . ASN   A 1 267 ? -4.66400  10.88100  -27.71000 1.000 27.88000  ? 233 ASN   A HB2    1 
ATOM   3265 H HB3    . ASN   A 1 267 ? -4.22700  10.29600  -26.29600 1.000 27.88000  ? 233 ASN   A HB3    1 
ATOM   3266 H HD21   . ASN   A 1 267 ? -2.27300  13.28500  -27.90200 1.000 27.78000  ? 233 ASN   A HD21   1 
ATOM   3267 H HD22   . ASN   A 1 267 ? -3.11300  12.39200  -28.74800 1.000 27.78000  ? 233 ASN   A HD22   1 
ATOM   3268 N N      . VAL   A 1 268 ? -4.80700  7.70100   -28.09900 1.000 27.80000  ? 234 VAL   A N      1 
ATOM   3269 C CA     . VAL   A 1 268 ? -5.31600  6.34400   -27.86500 1.000 27.80000  ? 234 VAL   A CA     1 
ATOM   3270 C C      . VAL   A 1 268 ? -4.23400  5.31100   -28.16200 1.000 31.34000  ? 234 VAL   A C      1 
ATOM   3271 O O      . VAL   A 1 268 ? -3.95000  4.42900   -27.34800 1.000 31.37000  ? 234 VAL   A O      1 
ATOM   3272 C CB     . VAL   A 1 268 ? -6.58000  6.07100   -28.70100 1.000 28.98000  ? 234 VAL   A CB     1 
ATOM   3273 C CG1    . VAL   A 1 268 ? -6.89800  4.56100   -28.68300 1.000 26.65000  ? 234 VAL   A CG1    1 
ATOM   3274 C CG2    . VAL   A 1 268 ? -7.77700  6.84600   -28.14300 1.000 28.71000  ? 234 VAL   A CG2    1 
ATOM   3275 H H      . VAL   A 1 268 ? -5.27500  8.17500   -28.64300 1.000 27.80000  ? 234 VAL   A H      1 
ATOM   3276 H HA     . VAL   A 1 268 ? -5.55700  6.25900   -26.92900 1.000 27.80000  ? 234 VAL   A HA     1 
ATOM   3277 H HB     . VAL   A 1 268 ? -6.43100  6.34700   -29.61900 1.000 28.98000  ? 234 VAL   A HB     1 
ATOM   3278 H HG11   . VAL   A 1 268 ? -7.82600  4.43400   -28.93500 1.000 26.65000  ? 234 VAL   A HG11   1 
ATOM   3279 H HG12   . VAL   A 1 268 ? -6.32100  4.10500   -29.31600 1.000 26.65000  ? 234 VAL   A HG12   1 
ATOM   3280 H HG13   . VAL   A 1 268 ? -6.75100  4.21700   -27.78800 1.000 26.65000  ? 234 VAL   A HG13   1 
ATOM   3281 H HG21   . VAL   A 1 268 ? -8.55500  6.66400   -28.69300 1.000 28.71000  ? 234 VAL   A HG21   1 
ATOM   3282 H HG22   . VAL   A 1 268 ? -7.94200  6.55800   -27.23100 1.000 28.71000  ? 234 VAL   A HG22   1 
ATOM   3283 H HG23   . VAL   A 1 268 ? -7.57400  7.79400   -28.16000 1.000 28.71000  ? 234 VAL   A HG23   1 
ATOM   3284 N N      . ASN   A 1 269 ? -3.61700  5.39900   -29.33600 1.000 29.66000  ? 235 ASN   A N      1 
ATOM   3285 C CA     . ASN   A 1 269 ? -2.61400  4.39800   -29.68500 1.000 29.28000  ? 235 ASN   A CA     1 
ATOM   3286 C C      . ASN   A 1 269 ? -1.38100  4.48800   -28.79000 1.000 33.36000  ? 235 ASN   A C      1 
ATOM   3287 O O      . ASN   A 1 269 ? -0.83300  3.45200   -28.38000 1.000 30.21000  ? 235 ASN   A O      1 
ATOM   3288 C CB     . ASN   A 1 269 ? -2.22300  4.51900   -31.16100 1.000 27.92000  ? 235 ASN   A CB     1 
ATOM   3289 C CG     . ASN   A 1 269 ? -1.35000  3.35300   -31.62200 1.000 34.37000  ? 235 ASN   A CG     1 
ATOM   3290 O OD1    . ASN   A 1 269 ? -0.21300  3.54300   -32.04600 1.000 33.52000  ? 235 ASN   A OD1    1 
ATOM   3291 N ND2    . ASN   A 1 269 ? -1.87400  2.14000   -31.50500 1.000 29.09000  ? 235 ASN   A ND2    1 
ATOM   3292 H H      . ASN   A 1 269 ? -3.75400  6.00600   -29.93000 1.000 29.66000  ? 235 ASN   A H      1 
ATOM   3293 H HA     . ASN   A 1 269 ? -3.00200  3.51800   -29.55700 1.000 29.28000  ? 235 ASN   A HA     1 
ATOM   3294 H HB2    . ASN   A 1 269 ? -3.02700  4.52800   -31.70400 1.000 27.92000  ? 235 ASN   A HB2    1 
ATOM   3295 H HB3    . ASN   A 1 269 ? -1.72300  5.34000   -31.29100 1.000 27.92000  ? 235 ASN   A HB3    1 
ATOM   3296 H HD21   . ASN   A 1 269 ? -1.42100  1.45100   -31.74800 1.000 29.09000  ? 235 ASN   A HD21   1 
ATOM   3297 H HD22   . ASN   A 1 269 ? -2.67200  2.04400   -31.19800 1.000 29.09000  ? 235 ASN   A HD22   1 
ATOM   3298 N N      . ALA   A 1 270 ? -0.92000  5.70500   -28.46700 1.000 27.81000  ? 236 ALA   A N      1 
ATOM   3299 C CA     . ALA   A 1 270 ? 0.26800   5.82400   -27.62100 1.000 35.39000  ? 236 ALA   A CA     1 
ATOM   3300 C C      . ALA   A 1 270 ? 0.06200   5.17400   -26.25000 1.000 33.97000  ? 236 ALA   A C      1 
ATOM   3301 O O      . ALA   A 1 270 ? 0.98100   4.54400   -25.71100 1.000 32.62000  ? 236 ALA   A O      1 
ATOM   3302 C CB     . ALA   A 1 270 ? 0.65600   7.29700   -27.45800 1.000 30.19000  ? 236 ALA   A CB     1 
ATOM   3303 H H      . ALA   A 1 270 ? -1.26600  6.45100   -28.71700 1.000 27.81000  ? 236 ALA   A H      1 
ATOM   3304 H HA     . ALA   A 1 270 ? 1.00700   5.37000   -28.05600 1.000 35.39000  ? 236 ALA   A HA     1 
ATOM   3305 H HB1    . ALA   A 1 270 ? 1.44400   7.35500   -26.89500 1.000 30.19000  ? 236 ALA   A HB1    1 
ATOM   3306 H HB2    . ALA   A 1 270 ? 0.84500   7.67200   -28.33200 1.000 30.19000  ? 236 ALA   A HB2    1 
ATOM   3307 H HB3    . ALA   A 1 270 ? -0.08100  7.77400   -27.04600 1.000 30.19000  ? 236 ALA   A HB3    1 
ATOM   3308 N N      . PHE   A 1 271 ? -1.12300  5.33700   -25.65300 1.000 29.83000  ? 237 PHE   A N      1 
ATOM   3309 C CA     . PHE   A 1 271 ? -1.33500  4.74500   -24.34000 1.000 29.03000  ? 237 PHE   A CA     1 
ATOM   3310 C C      . PHE   A 1 271 ? -1.70600  3.27900   -24.45500 1.000 35.43000  ? 237 PHE   A C      1 
ATOM   3311 O O      . PHE   A 1 271 ? -1.35600  2.48300   -23.57200 1.000 30.88000  ? 237 PHE   A O      1 
ATOM   3312 C CB     . PHE   A 1 271 ? -2.38900  5.53300   -23.56300 1.000 30.01000  ? 237 PHE   A CB     1 
ATOM   3313 C CG     . PHE   A 1 271 ? -1.83100  6.77100   -22.93600 1.000 33.90000  ? 237 PHE   A CG     1 
ATOM   3314 C CD1    . PHE   A 1 271 ? -1.03300  6.69400   -21.80300 1.000 36.77000  ? 237 PHE   A CD1    1 
ATOM   3315 C CD2    . PHE   A 1 271 ? -2.04100  8.00300   -23.52100 1.000 30.41000  ? 237 PHE   A CD2    1 
ATOM   3316 C CE1    . PHE   A 1 271 ? -0.48200  7.85400   -21.23000 1.000 38.97000  ? 237 PHE   A CE1    1 
ATOM   3317 C CE2    . PHE   A 1 271 ? -1.49800  9.16800   -22.96500 1.000 30.86000  ? 237 PHE   A CE2    1 
ATOM   3318 C CZ     . PHE   A 1 271 ? -0.71400  9.08500   -21.82200 1.000 35.71000  ? 237 PHE   A CZ     1 
ATOM   3319 H H      . PHE   A 1 271 ? -1.79300  5.76900   -25.97600 1.000 29.83000  ? 237 PHE   A H      1 
ATOM   3320 H HA     . PHE   A 1 271 ? -0.50600  4.79700   -23.83900 1.000 29.03000  ? 237 PHE   A HA     1 
ATOM   3321 H HB2    . PHE   A 1 271 ? -3.09900  5.79700   -24.17000 1.000 30.01000  ? 237 PHE   A HB2    1 
ATOM   3322 H HB3    . PHE   A 1 271 ? -2.74600  4.97300   -22.85600 1.000 30.01000  ? 237 PHE   A HB3    1 
ATOM   3323 H HD1    . PHE   A 1 271 ? -0.87500  5.86700   -21.40800 1.000 36.77000  ? 237 PHE   A HD1    1 
ATOM   3324 H HD2    . PHE   A 1 271 ? -2.56300  8.06200   -24.28800 1.000 30.41000  ? 237 PHE   A HD2    1 
ATOM   3325 H HE1    . PHE   A 1 271 ? 0.04100   7.79400   -20.46300 1.000 38.97000  ? 237 PHE   A HE1    1 
ATOM   3326 H HE2    . PHE   A 1 271 ? -1.65800  9.99300   -23.36200 1.000 30.86000  ? 237 PHE   A HE2    1 
ATOM   3327 H HZ     . PHE   A 1 271 ? -0.35600  9.85700   -21.44600 1.000 35.71000  ? 237 PHE   A HZ     1 
ATOM   3328 N N      . TYR   A 1 272 ? -2.34600  2.89400   -25.55800 1.000 27.20000  ? 238 TYR   A N      1 
ATOM   3329 C CA     . TYR   A 1 272 ? -2.56900  1.46400   -25.80900 1.000 30.42000  ? 238 TYR   A CA     1 
ATOM   3330 C C      . TYR   A 1 272 ? -1.25100  0.68800   -25.81500 1.000 34.46000  ? 238 TYR   A C      1 
ATOM   3331 O O      . TYR   A 1 272 ? -1.13100  -0.37800  -25.19300 1.000 33.71000  ? 238 TYR   A O      1 
ATOM   3332 C CB     . TYR   A 1 272 ? -3.31100  1.27700   -27.12700 1.000 29.11000  ? 238 TYR   A CB     1 
ATOM   3333 C CG     . TYR   A 1 272 ? -3.54500  -0.19200  -27.42700 1.000 28.07000  ? 238 TYR   A CG     1 
ATOM   3334 C CD1    . TYR   A 1 272 ? -4.60200  -0.87500  -26.83300 1.000 35.15000  ? 238 TYR   A CD1    1 
ATOM   3335 C CD2    . TYR   A 1 272 ? -2.70900  -0.88800  -28.29200 1.000 36.09000  ? 238 TYR   A CD2    1 
ATOM   3336 C CE1    . TYR   A 1 272 ? -4.82400  -2.22700  -27.09300 1.000 38.04000  ? 238 TYR   A CE1    1 
ATOM   3337 C CE2    . TYR   A 1 272 ? -2.92400  -2.24000  -28.55800 1.000 38.66000  ? 238 TYR   A CE2    1 
ATOM   3338 C CZ     . TYR   A 1 272 ? -3.97600  -2.90100  -27.95200 1.000 42.86000  ? 238 TYR   A CZ     1 
ATOM   3339 O OH     . TYR   A 1 272 ? -4.19000  -4.24900  -28.20400 1.000 37.71000  ? 238 TYR   A OH     1 
ATOM   3340 H H      . TYR   A 1 272 ? -2.65500  3.42100   -26.16300 1.000 27.20000  ? 238 TYR   A H      1 
ATOM   3341 H HA     . TYR   A 1 272 ? -3.12400  1.10300   -25.10000 1.000 30.42000  ? 238 TYR   A HA     1 
ATOM   3342 H HB2    . TYR   A 1 272 ? -4.17300  1.71800   -27.07500 1.000 29.11000  ? 238 TYR   A HB2    1 
ATOM   3343 H HB3    . TYR   A 1 272 ? -2.78300  1.65500   -27.84800 1.000 29.11000  ? 238 TYR   A HB3    1 
ATOM   3344 H HD1    . TYR   A 1 272 ? -5.16800  -0.42300  -26.25000 1.000 35.15000  ? 238 TYR   A HD1    1 
ATOM   3345 H HD2    . TYR   A 1 272 ? -1.99700  -0.44800  -28.69600 1.000 36.09000  ? 238 TYR   A HD2    1 
ATOM   3346 H HE1    . TYR   A 1 272 ? -5.53100  -2.67300  -26.68600 1.000 38.04000  ? 238 TYR   A HE1    1 
ATOM   3347 H HE2    . TYR   A 1 272 ? -2.35600  -2.69800  -29.13400 1.000 38.66000  ? 238 TYR   A HE2    1 
ATOM   3348 H HH     . TYR   A 1 272 ? -3.60900  -4.53700  -28.73800 1.000 37.71000  ? 238 TYR   A HH     1 
ATOM   3349 N N      . ARG   A 1 273 ? -0.24400  1.21700   -26.51100 1.000 29.86000  ? 239 ARG   A N      1 
ATOM   3350 C CA     . ARG   A 1 273 ? 1.06700   0.57100   -26.57600 1.000 33.27000  ? 239 ARG   A CA     1 
ATOM   3351 C C      . ARG   A 1 273 ? 1.78900   0.59900   -25.23300 1.000 36.79000  ? 239 ARG   A C      1 
ATOM   3352 O O      . ARG   A 1 273 ? 2.48200   -0.36300  -24.88600 1.000 37.34000  ? 239 ARG   A O      1 
ATOM   3353 C CB     . ARG   A 1 273 ? 1.95300   1.23800   -27.63900 1.000 33.53000  ? 239 ARG   A CB     1 
ATOM   3354 C CG     . ARG   A 1 273 ? 1.54000   1.03000   -29.10200 1.000 37.24000  ? 239 ARG   A CG     1 
ATOM   3355 C CD     . ARG   A 1 273 ? 2.30300   2.01500   -30.01300 1.000 40.41000  ? 239 ARG   A CD     1 
ATOM   3356 N NE     . ARG   A 1 273 ? 1.97800   1.90700   -31.43700 1.000 39.31000  ? 239 ARG   A NE     1 
ATOM   3357 C CZ     . ARG   A 1 273 ? 2.42500   0.95000   -32.24000 1.000 50.73000  ? 239 ARG   A CZ     1 
ATOM   3358 N NH1    . ARG   A 1 273 ? 3.18700   -0.02900  -31.78600 1.000 54.47000  ? 239 ARG   A NH1    1 
ATOM   3359 N NH2    . ARG   A 1 273 ? 2.09100   0.97100   -33.53000 1.000 42.68000  ? 239 ARG   A NH2    1 
ATOM   3360 H H      . ARG   A 1 273 ? -0.29500  1.95100   -26.95600 1.000 29.86000  ? 239 ARG   A H      1 
ATOM   3361 H HA     . ARG   A 1 273 ? 0.94600   -0.35800  -26.82900 1.000 33.27000  ? 239 ARG   A HA     1 
ATOM   3362 H HB2    . ARG   A 1 273 ? 1.95700   2.19400   -27.47400 1.000 33.53000  ? 239 ARG   A HB2    1 
ATOM   3363 H HB3    . ARG   A 1 273 ? 2.85400   0.89300   -27.54300 1.000 33.53000  ? 239 ARG   A HB3    1 
ATOM   3364 H HG2    . ARG   A 1 273 ? 1.75800   0.12500   -29.37500 1.000 37.24000  ? 239 ARG   A HG2    1 
ATOM   3365 H HG3    . ARG   A 1 273 ? 0.58900   1.19500   -29.19700 1.000 37.24000  ? 239 ARG   A HG3    1 
ATOM   3366 H HD2    . ARG   A 1 273 ? 2.09500   2.92000   -29.73300 1.000 40.41000  ? 239 ARG   A HD2    1 
ATOM   3367 H HD3    . ARG   A 1 273 ? 3.25500   1.85400   -29.91500 1.000 40.41000  ? 239 ARG   A HD3    1 
ATOM   3368 H HE     . ARG   A 1 273 ? 1.46200   2.50500   -31.77600 1.000 39.31000  ? 239 ARG   A HE     1 
ATOM   3369 H HH11   . ARG   A 1 273 ? 3.41000   -0.05400  -30.95600 1.000 54.47000  ? 239 ARG   A HH11   1 
ATOM   3370 H HH12   . ARG   A 1 273 ? 3.46400   -0.64100  -32.32300 1.000 54.47000  ? 239 ARG   A HH12   1 
ATOM   3371 H HH21   . ARG   A 1 273 ? 1.59300   1.60300   -33.83500 1.000 42.68000  ? 239 ARG   A HH21   1 
ATOM   3372 H HH22   . ARG   A 1 273 ? 2.37300   0.35300   -34.05700 1.000 42.68000  ? 239 ARG   A HH22   1 
ATOM   3373 N N      . ARG   A 1 274 ? 1.68600   1.69400   -24.48100 1.000 28.79000  ? 240 ARG   A N      1 
ATOM   3374 C CA     . ARG   A 1 274 ? 2.48400   1.81100   -23.26200 1.000 28.84000  ? 240 ARG   A CA     1 
ATOM   3375 C C      . ARG   A 1 274 ? 1.79300   1.27800   -22.01000 1.000 35.79000  ? 240 ARG   A C      1 
ATOM   3376 O O      . ARG   A 1 274 ? 2.45100   1.13200   -20.97400 1.000 38.04000  ? 240 ARG   A O      1 
ATOM   3377 C CB     . ARG   A 1 274 ? 2.87700   3.27900   -23.04600 1.000 34.14000  ? 240 ARG   A CB     1 
ATOM   3378 C CG     . ARG   A 1 274 ? 3.80100   3.82400   -24.12100 1.000 30.29000  ? 240 ARG   A CG     1 
ATOM   3379 C CD     . ARG   A 1 274 ? 3.83200   5.36600   -24.08000 1.000 35.92000  ? 240 ARG   A CD     1 
ATOM   3380 N NE     . ARG   A 1 274 ? 4.82900   5.89400   -25.00100 1.000 40.36000  ? 240 ARG   A NE     1 
ATOM   3381 C CZ     . ARG   A 1 274 ? 4.71200   5.87200   -26.32100 1.000 45.89000  ? 240 ARG   A CZ     1 
ATOM   3382 N NH1    . ARG   A 1 274 ? 3.63200   5.38000   -26.91200 1.000 41.43000  ? 240 ARG   A NH1    1 
ATOM   3383 N NH2    . ARG   A 1 274 ? 5.71000   6.33600   -27.06600 1.000 46.78000  ? 240 ARG   A NH2    1 
ATOM   3384 H H      . ARG   A 1 274 ? 1.17600   2.36600   -24.64800 1.000 28.79000  ? 240 ARG   A H      1 
ATOM   3385 H HA     . ARG   A 1 274 ? 3.30400   1.30600   -23.37900 1.000 28.84000  ? 240 ARG   A HA     1 
ATOM   3386 H HB2    . ARG   A 1 274 ? 2.07300   3.82100   -23.04200 1.000 34.14000  ? 240 ARG   A HB2    1 
ATOM   3387 H HB3    . ARG   A 1 274 ? 3.33300   3.35900   -22.19300 1.000 34.14000  ? 240 ARG   A HB3    1 
ATOM   3388 H HG2    . ARG   A 1 274 ? 4.70100   3.49500   -23.97000 1.000 30.29000  ? 240 ARG   A HG2    1 
ATOM   3389 H HG3    . ARG   A 1 274 ? 3.48100   3.54600   -24.99400 1.000 30.29000  ? 240 ARG   A HG3    1 
ATOM   3390 H HD2    . ARG   A 1 274 ? 2.96300   5.71200   -24.33800 1.000 35.92000  ? 240 ARG   A HD2    1 
ATOM   3391 H HD3    . ARG   A 1 274 ? 4.05900   5.65900   -23.18400 1.000 35.92000  ? 240 ARG   A HD3    1 
ATOM   3392 H HE     . ARG   A 1 274 ? 5.54000   6.24300   -24.66600 1.000 40.36000  ? 240 ARG   A HE     1 
ATOM   3393 H HH11   . ARG   A 1 274 ? 2.98200   5.07300   -26.44000 1.000 41.43000  ? 240 ARG   A HH11   1 
ATOM   3394 H HH12   . ARG   A 1 274 ? 3.57800   5.37400   -27.77000 1.000 41.43000  ? 240 ARG   A HH12   1 
ATOM   3395 H HH21   . ARG   A 1 274 ? 6.41400   6.65600   -26.69000 1.000 46.78000  ? 240 ARG   A HH21   1 
ATOM   3396 H HH22   . ARG   A 1 274 ? 5.64600   6.32800   -27.92400 1.000 46.78000  ? 240 ARG   A HH22   1 
ATOM   3397 N N      . CYS   A 1 275 ? 0.49300   1.00600   -22.05500 1.000 32.87000  ? 241 CYS   A N      1 
ATOM   3398 C CA     . CYS   A 1 275 ? -0.25300  0.55700   -20.87800 1.000 33.86000  ? 241 CYS   A CA     1 
ATOM   3399 C C      . CYS   A 1 275 ? -1.03600  -0.68700  -21.25400 1.000 32.80000  ? 241 CYS   A C      1 
ATOM   3400 O O      . CYS   A 1 275 ? -2.26400  -0.69900  -21.19700 1.000 32.38000  ? 241 CYS   A O      1 
ATOM   3401 C CB     . CYS   A 1 275 ? -1.18300  1.65100   -20.34700 1.000 33.67000  ? 241 CYS   A CB     1 
ATOM   3402 S SG     . CYS   A 1 275 ? -0.39400  3.17100   -19.77000 1.000 37.24000  ? 241 CYS   A SG     1 
ATOM   3403 H H      . CYS   A 1 275 ? 0.01100   1.07400   -22.76400 1.000 32.87000  ? 241 CYS   A H      1 
ATOM   3404 H HA     . CYS   A 1 275 ? 0.36800   0.32000   -20.17100 1.000 33.86000  ? 241 CYS   A HA     1 
ATOM   3405 H HB2    . CYS   A 1 275 ? -1.79700  1.89700   -21.05600 1.000 33.67000  ? 241 CYS   A HB2    1 
ATOM   3406 H HB3    . CYS   A 1 275 ? -1.68500  1.28700   -19.60100 1.000 33.67000  ? 241 CYS   A HB3    1 
ATOM   3407 H HG     . CYS   A 1 275 ? 0.35500   2.90500   -18.87100 1.000 37.24000  ? 241 CYS   A HG     1 
ATOM   3408 N N      . PRO   A 1 276 ? -0.34200  -1.75800  -21.65500 1.000 32.99000  ? 242 PRO   A N      1 
ATOM   3409 C CA     . PRO   A 1 276 ? -1.04700  -2.99300  -22.05800 1.000 41.64000  ? 242 PRO   A CA     1 
ATOM   3410 C C      . PRO   A 1 276 ? -1.87300  -3.62200  -20.94900 1.000 42.26000  ? 242 PRO   A C      1 
ATOM   3411 O O      . PRO   A 1 276 ? -2.74300  -4.44300  -21.24200 1.000 34.87000  ? 242 PRO   A O      1 
ATOM   3412 C CB     . PRO   A 1 276 ? 0.09400   -3.92600  -22.49500 1.000 37.17000  ? 242 PRO   A CB     1 
ATOM   3413 C CG     . PRO   A 1 276 ? 1.32100   -3.39600  -21.77800 1.000 37.47000  ? 242 PRO   A CG     1 
ATOM   3414 C CD     . PRO   A 1 276 ? 1.12200   -1.88900  -21.77800 1.000 34.18000  ? 242 PRO   A CD     1 
ATOM   3415 H HA     . PRO   A 1 276 ? -1.62100  -2.81600  -22.82000 1.000 41.64000  ? 242 PRO   A HA     1 
ATOM   3416 H HB2    . PRO   A 1 276 ? -0.10100  -4.83500  -22.21800 1.000 37.17000  ? 242 PRO   A HB2    1 
ATOM   3417 H HB3    . PRO   A 1 276 ? 0.20900   -3.87600  -23.45700 1.000 37.17000  ? 242 PRO   A HB3    1 
ATOM   3418 H HG2    . PRO   A 1 276 ? 1.34900   -3.74200  -20.87200 1.000 37.47000  ? 242 PRO   A HG2    1 
ATOM   3419 H HG3    . PRO   A 1 276 ? 2.12100   -3.64000  -22.26900 1.000 37.47000  ? 242 PRO   A HG3    1 
ATOM   3420 H HD2    . PRO   A 1 276 ? 1.56700   -1.48900  -21.01500 1.000 34.18000  ? 242 PRO   A HD2    1 
ATOM   3421 H HD3    . PRO   A 1 276 ? 1.42900   -1.50500  -22.61400 1.000 34.18000  ? 242 PRO   A HD3    1 
ATOM   3422 N N      . GLY   A 1 277 ? -1.64100  -3.26600  -19.69600 1.000 35.02000  ? 243 GLY   A N      1 
ATOM   3423 C CA     . GLY   A 1 277 ? -2.42300  -3.78200  -18.58800 1.000 37.58000  ? 243 GLY   A CA     1 
ATOM   3424 C C      . GLY   A 1 277 ? -3.66900  -2.99900  -18.26100 1.000 38.24000  ? 243 GLY   A C      1 
ATOM   3425 O O      . GLY   A 1 277 ? -4.36100  -3.32200  -17.29900 1.000 35.55000  ? 243 GLY   A O      1 
ATOM   3426 H H      . GLY   A 1 277 ? -1.02400  -2.71600  -19.45800 1.000 35.02000  ? 243 GLY   A H      1 
ATOM   3427 H HA2    . GLY   A 1 277 ? -2.68800  -4.69400  -18.78700 1.000 37.58000  ? 243 GLY   A HA2    1 
ATOM   3428 H HA3    . GLY   A 1 277 ? -1.86600  -3.80000  -17.79400 1.000 37.58000  ? 243 GLY   A HA3    1 
ATOM   3429 N N      . LYS   A 1 278 ? -3.97800  -1.95800  -19.02600 1.000 30.39000  ? 244 LYS   A N      1 
ATOM   3430 C CA     . LYS   A 1 278 ? -5.15200  -1.13500  -18.79700 1.000 32.42000  ? 244 LYS   A CA     1 
ATOM   3431 C C      . LYS   A 1 278 ? -5.99300  -1.12000  -20.06700 1.000 28.52000  ? 244 LYS   A C      1 
ATOM   3432 O O      . LYS   A 1 278 ? -5.52600  -1.48700  -21.14400 1.000 34.36000  ? 244 LYS   A O      1 
ATOM   3433 C CB     . LYS   A 1 278 ? -4.77000  0.31200   -18.40300 1.000 33.69000  ? 244 LYS   A CB     1 
ATOM   3434 C CG     . LYS   A 1 278 ? -3.71500  0.38700   -17.31300 1.000 36.24000  ? 244 LYS   A CG     1 
ATOM   3435 C CD     . LYS   A 1 278 ? -3.61600  1.79000   -16.74700 1.000 40.78000  ? 244 LYS   A CD     1 
ATOM   3436 C CE     . LYS   A 1 278 ? -2.54800  1.86100   -15.66800 1.000 42.91000  ? 244 LYS   A CE     1 
ATOM   3437 N NZ     . LYS   A 1 278 ? -2.94200  1.15700   -14.42600 1.000 33.88000  ? 244 LYS   A NZ     1 
ATOM   3438 H H      . LYS   A 1 278 ? -3.50900  -1.70400  -19.70100 1.000 30.39000  ? 244 LYS   A H      1 
ATOM   3439 H HA     . LYS   A 1 278 ? -5.68500  -1.51600  -18.08200 1.000 32.42000  ? 244 LYS   A HA     1 
ATOM   3440 H HB2    . LYS   A 1 278 ? -4.42200  0.76800   -19.18500 1.000 33.69000  ? 244 LYS   A HB2    1 
ATOM   3441 H HB3    . LYS   A 1 278 ? -5.56300  0.76900   -18.08100 1.000 33.69000  ? 244 LYS   A HB3    1 
ATOM   3442 H HG2    . LYS   A 1 278 ? -3.95400  -0.21700  -16.59200 1.000 36.24000  ? 244 LYS   A HG2    1 
ATOM   3443 H HG3    . LYS   A 1 278 ? -2.85200  0.14600   -17.68400 1.000 36.24000  ? 244 LYS   A HG3    1 
ATOM   3444 H HD2    . LYS   A 1 278 ? -3.37500  2.40500   -17.45600 1.000 40.78000  ? 244 LYS   A HD2    1 
ATOM   3445 H HD3    . LYS   A 1 278 ? -4.46700  2.04100   -16.35400 1.000 40.78000  ? 244 LYS   A HD3    1 
ATOM   3446 H HE2    . LYS   A 1 278 ? -1.73500  1.45000   -16.00100 1.000 42.91000  ? 244 LYS   A HE2    1 
ATOM   3447 H HE3    . LYS   A 1 278 ? -2.38400  2.79100   -15.44600 1.000 42.91000  ? 244 LYS   A HE3    1 
ATOM   3448 H HZ1    . LYS   A 1 278 ? -2.29300  1.22300   -13.82000 1.000 33.88000  ? 244 LYS   A HZ1    1 
ATOM   3449 H HZ2    . LYS   A 1 278 ? -3.68500  1.51800   -14.09400 1.000 33.88000  ? 244 LYS   A HZ2    1 
ATOM   3450 H HZ3    . LYS   A 1 278 ? -3.09100  0.29700   -14.59800 1.000 33.88000  ? 244 LYS   A HZ3    1 
ATOM   3451 N N      . LEU   A 1 279 ? -7.25500  -0.73200  -19.91300 1.000 27.31000  ? 245 LEU   A N      1 
ATOM   3452 C CA     . LEU   A 1 279 ? -8.12000  -0.47500  -21.05700 1.000 28.89000  ? 245 LEU   A CA     1 
ATOM   3453 C C      . LEU   A 1 279 ? -7.94200  0.97600   -21.48800 1.000 31.32000  ? 245 LEU   A C      1 
ATOM   3454 O O      . LEU   A 1 279 ? -7.73700  1.84400   -20.64600 1.000 29.65000  ? 245 LEU   A O      1 
ATOM   3455 C CB     . LEU   A 1 279 ? -9.58500  -0.69500  -20.69100 1.000 30.47000  ? 245 LEU   A CB     1 
ATOM   3456 C CG     . LEU   A 1 279 ? -9.95500  -2.05600  -20.08600 1.000 33.03000  ? 245 LEU   A CG     1 
ATOM   3457 C CD1    . LEU   A 1 279 ? -11.41200 -2.04500  -19.62900 1.000 36.90000  ? 245 LEU   A CD1    1 
ATOM   3458 C CD2    . LEU   A 1 279 ? -9.72000  -3.08300  -21.16900 1.000 34.77000  ? 245 LEU   A CD2    1 
ATOM   3459 H H      . LEU   A 1 279 ? -7.63600  -0.61000  -19.15200 1.000 27.31000  ? 245 LEU   A H      1 
ATOM   3460 H HA     . LEU   A 1 279 ? -7.88400  -1.05800  -21.79500 1.000 28.89000  ? 245 LEU   A HA     1 
ATOM   3461 H HB2    . LEU   A 1 279 ? -9.83800  -0.01700  -20.04500 1.000 30.47000  ? 245 LEU   A HB2    1 
ATOM   3462 H HB3    . LEU   A 1 279 ? -10.11700 -0.58400  -21.49400 1.000 30.47000  ? 245 LEU   A HB3    1 
ATOM   3463 H HG     . LEU   A 1 279 ? -9.38300  -2.25300  -19.32800 1.000 33.03000  ? 245 LEU   A HG     1 
ATOM   3464 H HD11   . LEU   A 1 279 ? -11.59300 -2.86300  -19.14100 1.000 36.90000  ? 245 LEU   A HD11   1 
ATOM   3465 H HD12   . LEU   A 1 279 ? -11.55600 -1.27800  -19.05300 1.000 36.90000  ? 245 LEU   A HD12   1 
ATOM   3466 H HD13   . LEU   A 1 279 ? -11.98600 -1.98600  -20.40900 1.000 36.90000  ? 245 LEU   A HD13   1 
ATOM   3467 H HD21   . LEU   A 1 279 ? -10.03900 -3.94500  -20.85900 1.000 34.77000  ? 245 LEU   A HD21   1 
ATOM   3468 H HD22   . LEU   A 1 279 ? -10.20500 -2.81900  -21.96600 1.000 34.77000  ? 245 LEU   A HD22   1 
ATOM   3469 H HD23   . LEU   A 1 279 ? -8.77000  -3.13100  -21.36000 1.000 34.77000  ? 245 LEU   A HD23   1 
ATOM   3470 N N      . ILE   A 1 280 ? -8.06000  1.23200   -22.79500 1.000 29.42000  ? 246 ILE   A N      1 
ATOM   3471 C CA     . ILE   A 1 280 ? -8.10400  2.60400   -23.32800 1.000 31.38000  ? 246 ILE   A CA     1 
ATOM   3472 C C      . ILE   A 1 280 ? -9.51600  2.86800   -23.81700 1.000 31.61000  ? 246 ILE   A C      1 
ATOM   3473 O O      . ILE   A 1 280 ? -10.07700 2.04500   -24.55200 1.000 35.64000  ? 246 ILE   A O      1 
ATOM   3474 C CB     . ILE   A 1 280 ? -7.10900  2.82300   -24.48100 1.000 32.23000  ? 246 ILE   A CB     1 
ATOM   3475 C CG1    . ILE   A 1 280 ? -5.75900  2.16100   -24.19000 1.000 29.78000  ? 246 ILE   A CG1    1 
ATOM   3476 C CG2    . ILE   A 1 280 ? -6.96500  4.35400   -24.79200 1.000 31.55000  ? 246 ILE   A CG2    1 
ATOM   3477 C CD1    . ILE   A 1 280 ? -5.03900  2.73000   -22.97700 1.000 31.71000  ? 246 ILE   A CD1    1 
ATOM   3478 H H      . ILE   A 1 280 ? -8.11700  0.62400   -23.40100 1.000 29.42000  ? 246 ILE   A H      1 
ATOM   3479 H HA     . ILE   A 1 280 ? -7.89900  3.23500   -22.62100 1.000 31.38000  ? 246 ILE   A HA     1 
ATOM   3480 H HB     . ILE   A 1 280 ? -7.47800  2.39800   -25.27100 1.000 32.23000  ? 246 ILE   A HB     1 
ATOM   3481 H HG12   . ILE   A 1 280 ? -5.89400  1.21300   -24.04000 1.000 29.78000  ? 246 ILE   A HG12   1 
ATOM   3482 H HG13   . ILE   A 1 280 ? -5.18200  2.28900   -24.95900 1.000 29.78000  ? 246 ILE   A HG13   1 
ATOM   3483 H HG21   . ILE   A 1 280 ? -6.28700  4.47400   -25.47600 1.000 31.55000  ? 246 ILE   A HG21   1 
ATOM   3484 H HG22   . ILE   A 1 280 ? -7.81700  4.69400   -25.10700 1.000 31.55000  ? 246 ILE   A HG22   1 
ATOM   3485 H HG23   . ILE   A 1 280 ? -6.70300  4.81800   -23.98100 1.000 31.55000  ? 246 ILE   A HG23   1 
ATOM   3486 H HD11   . ILE   A 1 280 ? -4.20300  2.25300   -22.85500 1.000 31.71000  ? 246 ILE   A HD11   1 
ATOM   3487 H HD12   . ILE   A 1 280 ? -4.86300  3.67200   -23.12600 1.000 31.71000  ? 246 ILE   A HD12   1 
ATOM   3488 H HD13   . ILE   A 1 280 ? -5.60000  2.61800   -22.19400 1.000 31.71000  ? 246 ILE   A HD13   1 
ATOM   3489 N N      . PHE   A 1 281 ? -10.09700 3.99700   -23.40700 1.000 31.22000  ? 247 PHE   A N      1 
ATOM   3490 C CA     . PHE   A 1 281 ? -11.33600 4.47900   -24.00500 1.000 30.76000  ? 247 PHE   A CA     1 
ATOM   3491 C C      . PHE   A 1 281 ? -10.96400 5.61400   -24.95500 1.000 34.78000  ? 247 PHE   A C      1 
ATOM   3492 O O      . PHE   A 1 281 ? -10.17700 6.49000   -24.59000 1.000 32.19000  ? 247 PHE   A O      1 
ATOM   3493 C CB     . PHE   A 1 281 ? -12.33400 4.99800   -22.97200 1.000 27.55000  ? 247 PHE   A CB     1 
ATOM   3494 C CG     . PHE   A 1 281 ? -12.88700 3.95600   -22.00700 1.000 32.00000  ? 247 PHE   A CG     1 
ATOM   3495 C CD1    . PHE   A 1 281 ? -12.45300 2.63700   -22.02100 1.000 36.49000  ? 247 PHE   A CD1    1 
ATOM   3496 C CD2    . PHE   A 1 281 ? -13.87400 4.32900   -21.09000 1.000 37.80000  ? 247 PHE   A CD2    1 
ATOM   3497 C CE1    . PHE   A 1 281 ? -12.97200 1.71400   -21.12200 1.000 34.95000  ? 247 PHE   A CE1    1 
ATOM   3498 C CE2    . PHE   A 1 281 ? -14.40700 3.41100   -20.19500 1.000 35.80000  ? 247 PHE   A CE2    1 
ATOM   3499 C CZ     . PHE   A 1 281 ? -13.95300 2.09900   -20.20900 1.000 36.70000  ? 247 PHE   A CZ     1 
ATOM   3500 H H      . PHE   A 1 281 ? -9.79000  4.50100   -22.78200 1.000 31.22000  ? 247 PHE   A H      1 
ATOM   3501 H HA     . PHE   A 1 281 ? -11.75600 3.77000   -24.51600 1.000 30.76000  ? 247 PHE   A HA     1 
ATOM   3502 H HB2    . PHE   A 1 281 ? -11.89700 5.68200   -22.44100 1.000 27.55000  ? 247 PHE   A HB2    1 
ATOM   3503 H HB3    . PHE   A 1 281 ? -13.08800 5.38700   -23.44300 1.000 27.55000  ? 247 PHE   A HB3    1 
ATOM   3504 H HD1    . PHE   A 1 281 ? -11.79500 2.37300   -22.62200 1.000 36.49000  ? 247 PHE   A HD1    1 
ATOM   3505 H HD2    . PHE   A 1 281 ? -14.17500 5.20900   -21.07600 1.000 37.80000  ? 247 PHE   A HD2    1 
ATOM   3506 H HE1    . PHE   A 1 281 ? -12.67200 0.83400   -21.13700 1.000 34.95000  ? 247 PHE   A HE1    1 
ATOM   3507 H HE2    . PHE   A 1 281 ? -15.05900 3.67500   -19.58600 1.000 35.80000  ? 247 PHE   A HE2    1 
ATOM   3508 H HZ     . PHE   A 1 281 ? -14.30500 1.47700   -19.61400 1.000 36.70000  ? 247 PHE   A HZ     1 
ATOM   3509 N N      . GLY   A 1 282 ? -11.49900 5.58200   -26.17100 1.000 30.77000  ? 248 GLY   A N      1 
ATOM   3510 C CA     . GLY   A 1 282 ? -11.22600 6.63200   -27.14000 1.000 36.63000  ? 248 GLY   A CA     1 
ATOM   3511 C C      . GLY   A 1 282 ? -12.29900 7.70600   -27.05700 1.000 38.08000  ? 248 GLY   A C      1 
ATOM   3512 O O      . GLY   A 1 282 ? -13.47900 7.41300   -26.88000 1.000 33.87000  ? 248 GLY   A O      1 
ATOM   3513 H H      . GLY   A 1 282 ? -12.02300 4.96300   -26.45800 1.000 30.77000  ? 248 GLY   A H      1 
ATOM   3514 H HA2    . GLY   A 1 282 ? -10.36200 7.03400   -26.96100 1.000 36.63000  ? 248 GLY   A HA2    1 
ATOM   3515 H HA3    . GLY   A 1 282 ? -11.22100 6.26100   -28.03600 1.000 36.63000  ? 248 GLY   A HA3    1 
ATOM   3516 N N      . CYS   A 1 283 ? -11.86800 8.96200   -27.16100 1.000 32.74000  ? 249 CYS   A N      1 
ATOM   3517 C CA     . CYS   A 1 283 ? -12.80600 10.06900  -27.19000 1.000 29.21000  ? 249 CYS   A CA     1 
ATOM   3518 C C      . CYS   A 1 283 ? -12.19100 11.13800  -28.07800 1.000 36.25000  ? 249 CYS   A C      1 
ATOM   3519 O O      . CYS   A 1 283 ? -11.04200 11.52300  -27.85800 1.000 34.31000  ? 249 CYS   A O      1 
ATOM   3520 C CB     . CYS   A 1 283 ? -13.06500 10.61600  -25.78900 1.000 27.79000  ? 249 CYS   A CB     1 
ATOM   3521 S SG     . CYS   A 1 283 ? -14.34000 11.88900  -25.77700 1.000 37.00000  ? 249 CYS   A SG     1 
ATOM   3522 H H      . CYS   A 1 283 ? -11.04200 9.19400   -27.21600 1.000 32.74000  ? 249 CYS   A H      1 
ATOM   3523 H HA     . CYS   A 1 283 ? -13.64700 9.78200   -27.57800 1.000 29.21000  ? 249 CYS   A HA     1 
ATOM   3524 H HB2    . CYS   A 1 283 ? -13.35700 9.89100   -25.21400 1.000 27.79000  ? 249 CYS   A HB2    1 
ATOM   3525 H HB3    . CYS   A 1 283 ? -12.24700 11.00600  -25.44400 1.000 27.79000  ? 249 CYS   A HB3    1 
ATOM   3526 H HG     . CYS   A 1 283 ? -13.99400 12.76600  -26.51900 1.000 37.00000  ? 249 CYS   A HG     1 
ATOM   3527 N N      . GLY   A 1 284 ? -12.93500 11.59700  -29.07700 1.000 33.22000  ? 250 GLY   A N      1 
ATOM   3528 C CA     . GLY   A 1 284 ? -12.42900 12.69500  -29.88000 1.000 29.63000  ? 250 GLY   A CA     1 
ATOM   3529 C C      . GLY   A 1 284 ? -12.70500 12.51800  -31.35300 1.000 34.31000  ? 250 GLY   A C      1 
ATOM   3530 O O      . GLY   A 1 284 ? -12.17900 11.60100  -31.99500 1.000 35.23000  ? 250 GLY   A O      1 
ATOM   3531 H H      . GLY   A 1 284 ? -13.71000 11.30100  -29.30300 1.000 33.22000  ? 250 GLY   A H      1 
ATOM   3532 H HA2    . GLY   A 1 284 ? -12.84400 13.52200  -29.58900 1.000 29.63000  ? 250 GLY   A HA2    1 
ATOM   3533 H HA3    . GLY   A 1 284 ? -11.47000 12.77600  -29.76200 1.000 29.63000  ? 250 GLY   A HA3    1 
ATOM   3534 N N      . GLY   A 1 285 ? -13.54500 13.39800  -31.90000 1.000 34.46000  ? 251 GLY   A N      1 
ATOM   3535 C CA     . GLY   A 1 285 ? -13.71100 13.44400  -33.33600 1.000 31.33000  ? 251 GLY   A CA     1 
ATOM   3536 C C      . GLY   A 1 285 ? -14.53500 12.35600  -33.96800 1.000 33.57000  ? 251 GLY   A C      1 
ATOM   3537 O O      . GLY   A 1 285 ? -14.44600 12.17600  -35.18300 1.000 30.39000  ? 251 GLY   A O      1 
ATOM   3538 H H      . GLY   A 1 285 ? -14.01900 13.96700  -31.46300 1.000 34.46000  ? 251 GLY   A H      1 
ATOM   3539 H HA2    . GLY   A 1 285 ? -14.12000 14.29200  -33.57000 1.000 31.33000  ? 251 GLY   A HA2    1 
ATOM   3540 H HA3    . GLY   A 1 285 ? -12.83300 13.41900  -33.74600 1.000 31.33000  ? 251 GLY   A HA3    1 
ATOM   3541 N N      . VAL   A 1 286 ? -15.33600 11.62000  -33.19900 1.000 34.35000  ? 252 VAL   A N      1 
ATOM   3542 C CA     . VAL   A 1 286 ? -16.14300 10.54700  -33.77400 1.000 33.19000  ? 252 VAL   A CA     1 
ATOM   3543 C C      . VAL   A 1 286 ? -17.45100 11.11500  -34.32300 1.000 33.97000  ? 252 VAL   A C      1 
ATOM   3544 O O      . VAL   A 1 286 ? -18.25400 11.69400  -33.58600 1.000 36.92000  ? 252 VAL   A O      1 
ATOM   3545 C CB     . VAL   A 1 286 ? -16.40900 9.43800   -32.74800 1.000 35.13000  ? 252 VAL   A CB     1 
ATOM   3546 C CG1    . VAL   A 1 286 ? -17.33500 8.34600   -33.33300 1.000 33.39000  ? 252 VAL   A CG1    1 
ATOM   3547 C CG2    . VAL   A 1 286 ? -15.07600 8.85200   -32.27600 1.000 33.32000  ? 252 VAL   A CG2    1 
ATOM   3548 H H      . VAL   A 1 286 ? -15.42900 11.72100  -32.35000 1.000 34.35000  ? 252 VAL   A H      1 
ATOM   3549 H HA     . VAL   A 1 286 ? -15.65700 10.15200  -34.51500 1.000 33.19000  ? 252 VAL   A HA     1 
ATOM   3550 H HB     . VAL   A 1 286 ? -16.85400 9.82400   -31.97700 1.000 35.13000  ? 252 VAL   A HB     1 
ATOM   3551 H HG11   . VAL   A 1 286 ? -17.31900 7.57400   -32.74600 1.000 33.39000  ? 252 VAL   A HG11   1 
ATOM   3552 H HG12   . VAL   A 1 286 ? -18.23800 8.69400   -33.39500 1.000 33.39000  ? 252 VAL   A HG12   1 
ATOM   3553 H HG13   . VAL   A 1 286 ? -17.01200 8.09800   -34.21300 1.000 33.39000  ? 252 VAL   A HG13   1 
ATOM   3554 H HG21   . VAL   A 1 286 ? -15.25200 8.12300   -31.66200 1.000 33.32000  ? 252 VAL   A HG21   1 
ATOM   3555 H HG22   . VAL   A 1 286 ? -14.58600 8.52500   -33.04600 1.000 33.32000  ? 252 VAL   A HG22   1 
ATOM   3556 H HG23   . VAL   A 1 286 ? -14.56600 9.54500   -31.82900 1.000 33.32000  ? 252 VAL   A HG23   1 
ATOM   3557 N N      . TYR   A 1 287 ? -17.65300 10.96000  -35.62600 1.000 37.88000  ? 253 TYR   A N      1 
ATOM   3558 C CA     . TYR   A 1 287 ? -18.92000 11.25800  -36.27600 1.000 37.55000  ? 253 TYR   A CA     1 
ATOM   3559 C C      . TYR   A 1 287 ? -19.52100 10.07000  -37.00000 1.000 38.76000  ? 253 TYR   A C      1 
ATOM   3560 O O      . TYR   A 1 287 ? -20.73200 10.06300  -37.22700 1.000 42.09000  ? 253 TYR   A O      1 
ATOM   3561 C CB     . TYR   A 1 287 ? -18.75600 12.39800  -37.29500 1.000 36.21000  ? 253 TYR   A CB     1 
ATOM   3562 C CG     . TYR   A 1 287 ? -18.45900 13.73200  -36.67800 1.000 35.54000  ? 253 TYR   A CG     1 
ATOM   3563 C CD1    . TYR   A 1 287 ? -17.19200 14.01700  -36.19100 1.000 38.58000  ? 253 TYR   A CD1    1 
ATOM   3564 C CD2    . TYR   A 1 287 ? -19.43700 14.72300  -36.59300 1.000 41.25000  ? 253 TYR   A CD2    1 
ATOM   3565 C CE1    . TYR   A 1 287 ? -16.90000 15.24100  -35.62500 1.000 34.92000  ? 253 TYR   A CE1    1 
ATOM   3566 C CE2    . TYR   A 1 287 ? -19.15500 15.96700  -36.02000 1.000 39.36000  ? 253 TYR   A CE2    1 
ATOM   3567 C CZ     . TYR   A 1 287 ? -17.88300 16.22100  -35.55100 1.000 46.57000  ? 253 TYR   A CZ     1 
ATOM   3568 O OH     . TYR   A 1 287 ? -17.57100 17.43700  -34.99500 1.000 42.61000  ? 253 TYR   A OH     1 
ATOM   3569 H H      . TYR   A 1 287 ? -17.05100 10.67400  -36.17000 1.000 37.88000  ? 253 TYR   A H      1 
ATOM   3570 H HA     . TYR   A 1 287 ? -19.55800 11.54900  -35.60600 1.000 37.55000  ? 253 TYR   A HA     1 
ATOM   3571 H HB2    . TYR   A 1 287 ? -18.02400 12.17900  -37.89200 1.000 36.21000  ? 253 TYR   A HB2    1 
ATOM   3572 H HB3    . TYR   A 1 287 ? -19.57800 12.48300  -37.80200 1.000 36.21000  ? 253 TYR   A HB3    1 
ATOM   3573 H HD1    . TYR   A 1 287 ? -16.52700 13.36900  -36.24300 1.000 38.58000  ? 253 TYR   A HD1    1 
ATOM   3574 H HD2    . TYR   A 1 287 ? -20.29200 14.55100  -36.91600 1.000 41.25000  ? 253 TYR   A HD2    1 
ATOM   3575 H HE1    . TYR   A 1 287 ? -16.04300 15.41500  -35.30700 1.000 34.92000  ? 253 TYR   A HE1    1 
ATOM   3576 H HE2    . TYR   A 1 287 ? -19.81300 16.62200  -35.97200 1.000 39.36000  ? 253 TYR   A HE2    1 
ATOM   3577 H HH     . TYR   A 1 287 ? -18.24400 17.94000  -35.00800 1.000 42.61000  ? 253 TYR   A HH     1 
ATOM   3578 N N      . THR   A 1 288 ? -18.72100 9.07700   -37.38000 1.000 36.95000  ? 254 THR   A N      1 
ATOM   3579 C CA     . THR   A 1 288 ? -19.20800 7.95500   -38.16800 1.000 32.37000  ? 254 THR   A CA     1 
ATOM   3580 C C      . THR   A 1 288 ? -18.72400 6.65200   -37.54400 1.000 38.62000  ? 254 THR   A C      1 
ATOM   3581 O O      . THR   A 1 288 ? -17.84500 6.65400   -36.68200 1.000 36.24000  ? 254 THR   A O      1 
ATOM   3582 C CB     . THR   A 1 288 ? -18.74700 8.05700   -39.64200 1.000 42.54000  ? 254 THR   A CB     1 
ATOM   3583 O OG1    . THR   A 1 288 ? -17.33600 7.83400   -39.72600 1.000 43.24000  ? 254 THR   A OG1    1 
ATOM   3584 C CG2    . THR   A 1 288 ? -19.07100 9.45700   -40.23500 1.000 38.79000  ? 254 THR   A CG2    1 
ATOM   3585 H H      . THR   A 1 288 ? -17.88300 9.03200   -37.19100 1.000 36.95000  ? 254 THR   A H      1 
ATOM   3586 H HA     . THR   A 1 288 ? -20.17800 7.95000   -38.15700 1.000 32.37000  ? 254 THR   A HA     1 
ATOM   3587 H HB     . THR   A 1 288 ? -19.21000 7.38800   -40.17000 1.000 42.54000  ? 254 THR   A HB     1 
ATOM   3588 H HG1    . THR   A 1 288 ? -17.08400 7.88900   -40.52500 1.000 43.24000  ? 254 THR   A HG1    1 
ATOM   3589 H HG21   . THR   A 1 288 ? -18.83600 9.48100   -41.17600 1.000 38.79000  ? 254 THR   A HG21   1 
ATOM   3590 H HG22   . THR   A 1 288 ? -20.01800 9.64500   -40.14200 1.000 38.79000  ? 254 THR   A HG22   1 
ATOM   3591 H HG23   . THR   A 1 288 ? -18.56700 10.14100  -39.76700 1.000 38.79000  ? 254 THR   A HG23   1 
ATOM   3592 N N      . GLY   A 1 289 ? -19.33900 5.53600   -37.96100 1.000 38.30000  ? 255 GLY   A N      1 
ATOM   3593 C CA     . GLY   A 1 289 ? -18.84100 4.23800   -37.53500 1.000 36.48000  ? 255 GLY   A CA     1 
ATOM   3594 C C      . GLY   A 1 289 ? -17.43800 3.97400   -38.04500 1.000 39.57000  ? 255 GLY   A C      1 
ATOM   3595 O O      . GLY   A 1 289 ? -16.66600 3.24000   -37.41700 1.000 39.74000  ? 255 GLY   A O      1 
ATOM   3596 H H      . GLY   A 1 289 ? -20.02700 5.51000   -38.47600 1.000 38.30000  ? 255 GLY   A H      1 
ATOM   3597 H HA2    . GLY   A 1 289 ? -18.83000 4.19600   -36.56600 1.000 36.48000  ? 255 GLY   A HA2    1 
ATOM   3598 H HA3    . GLY   A 1 289 ? -19.42700 3.54000   -37.86800 1.000 36.48000  ? 255 GLY   A HA3    1 
ATOM   3599 N N      . GLU   A 1 290 ? -17.08200 4.58000   -39.18200 1.000 41.72000  ? 256 GLU   A N      1 
ATOM   3600 C CA     . GLU   A 1 290 ? -15.71200 4.48400   -39.67100 1.000 47.06000  ? 256 GLU   A CA     1 
ATOM   3601 C C      . GLU   A 1 290 ? -14.73800 5.19700   -38.73600 1.000 33.13000  ? 256 GLU   A C      1 
ATOM   3602 O O      . GLU   A 1 290 ? -13.62900 4.69600   -38.49900 1.000 37.05000  ? 256 GLU   A O      1 
ATOM   3603 C CB     . GLU   A 1 290 ? -15.61100 5.03200   -41.10000 1.000 43.94000  ? 256 GLU   A CB     1 
ATOM   3604 C CG     . GLU   A 1 290 ? -15.88500 3.94100   -42.14900 1.000 47.67000  ? 256 GLU   A CG     1 
ATOM   3605 C CD     . GLU   A 1 290 ? -15.58300 4.35000   -43.59300 1.000 61.18000  ? 256 GLU   A CD     1 
ATOM   3606 O OE1    . GLU   A 1 290 ? -15.06800 5.46500   -43.81700 1.000 56.03000  ? 256 GLU   A OE1    1 
ATOM   3607 O OE2    . GLU   A 1 290 ? -15.86600 3.53600   -44.50400 1.000 67.25000  ? 256 GLU   A OE2    1 
ATOM   3608 H H      . GLU   A 1 290 ? -17.60900 5.04400   -39.67900 1.000 41.72000  ? 256 GLU   A H      1 
ATOM   3609 H HA     . GLU   A 1 290 ? -15.45900 3.54800   -39.69700 1.000 47.06000  ? 256 GLU   A HA     1 
ATOM   3610 H HB2    . GLU   A 1 290 ? -16.26500 5.73800   -41.21900 1.000 43.94000  ? 256 GLU   A HB2    1 
ATOM   3611 H HB3    . GLU   A 1 290 ? -14.71600 5.37600   -41.24700 1.000 43.94000  ? 256 GLU   A HB3    1 
ATOM   3612 H HG2    . GLU   A 1 290 ? -15.33600 3.16800   -41.94400 1.000 47.67000  ? 256 GLU   A HG2    1 
ATOM   3613 H HG3    . GLU   A 1 290 ? -16.82200 3.69600   -42.10300 1.000 47.67000  ? 256 GLU   A HG3    1 
ATOM   3614 N N      . ASP   A 1 291 ? -15.12700 6.35500   -38.19200 1.000 34.59000  ? 257 ASP   A N      1 
ATOM   3615 C CA     . ASP   A 1 291 ? -14.28800 6.98100   -37.17100 1.000 36.34000  ? 257 ASP   A CA     1 
ATOM   3616 C C      . ASP   A 1 291 ? -14.12700 6.06500   -35.95900 1.000 38.83000  ? 257 ASP   A C      1 
ATOM   3617 O O      . ASP   A 1 291 ? -13.02900 5.94100   -35.40000 1.000 31.54000  ? 257 ASP   A O      1 
ATOM   3618 C CB     . ASP   A 1 291 ? -14.88100 8.31700   -36.73100 1.000 34.02000  ? 257 ASP   A CB     1 
ATOM   3619 C CG     . ASP   A 1 291 ? -14.95500 9.35200   -37.88000 1.000 37.82000  ? 257 ASP   A CG     1 
ATOM   3620 O OD1    . ASP   A 1 291 ? -14.19400 9.24200   -38.86500 1.000 40.81000  ? 257 ASP   A OD1    1 
ATOM   3621 O OD2    . ASP   A 1 291 ? -15.79500 10.26000  -37.78400 1.000 37.17000  ? 257 ASP   A OD2    1 
ATOM   3622 H H      . ASP   A 1 291 ? -15.84600 6.78300   -38.38900 1.000 34.59000  ? 257 ASP   A H      1 
ATOM   3623 H HA     . ASP   A 1 291 ? -13.40800 7.14900   -37.54200 1.000 36.34000  ? 257 ASP   A HA     1 
ATOM   3624 H HB2    . ASP   A 1 291 ? -15.78200 8.16900   -36.40300 1.000 34.02000  ? 257 ASP   A HB2    1 
ATOM   3625 H HB3    . ASP   A 1 291 ? -14.32900 8.69100   -36.02700 1.000 34.02000  ? 257 ASP   A HB3    1 
ATOM   3626 N N      . ALA   A 1 292 ? -15.22500 5.44300   -35.52200 1.000 35.92000  ? 258 ALA   A N      1 
ATOM   3627 C CA     . ALA   A 1 292 ? -15.16800 4.53900   -34.37700 1.000 36.27000  ? 258 ALA   A CA     1 
ATOM   3628 C C      . ALA   A 1 292 ? -14.28400 3.33800   -34.67200 1.000 38.88000  ? 258 ALA   A C      1 
ATOM   3629 O O      . ALA   A 1 292 ? -13.51900 2.89000   -33.80500 1.000 36.52000  ? 258 ALA   A O      1 
ATOM   3630 C CB     . ALA   A 1 292 ? -16.57700 4.08200   -34.00200 1.000 36.85000  ? 258 ALA   A CB     1 
ATOM   3631 H H      . ALA   A 1 292 ? -16.00700 5.52800   -35.86900 1.000 35.92000  ? 258 ALA   A H      1 
ATOM   3632 H HA     . ALA   A 1 292 ? -14.79200 5.01100   -33.61800 1.000 36.27000  ? 258 ALA   A HA     1 
ATOM   3633 H HB1    . ALA   A 1 292 ? -16.52400 3.49400   -33.23200 1.000 36.85000  ? 258 ALA   A HB1    1 
ATOM   3634 H HB2    . ALA   A 1 292 ? -17.11300 4.86100   -33.78800 1.000 36.85000  ? 258 ALA   A HB2    1 
ATOM   3635 H HB3    . ALA   A 1 292 ? -16.96600 3.60900   -34.75400 1.000 36.85000  ? 258 ALA   A HB3    1 
ATOM   3636 N N      . PHE   A 1 293 ? -14.39100 2.79600   -35.89000 1.000 32.98000  ? 259 PHE   A N      1 
ATOM   3637 C CA     . PHE   A 1 293 ? -13.52900 1.70200   -36.31900 1.000 34.73000  ? 259 PHE   A CA     1 
ATOM   3638 C C      . PHE   A 1 293 ? -12.05400 2.06200   -36.17400 1.000 37.04000  ? 259 PHE   A C      1 
ATOM   3639 O O      . PHE   A 1 293 ? -11.25600 1.25200   -35.68900 1.000 32.20000  ? 259 PHE   A O      1 
ATOM   3640 C CB     . PHE   A 1 293 ? -13.86500 1.32700   -37.76600 1.000 33.01000  ? 259 PHE   A CB     1 
ATOM   3641 C CG     . PHE   A 1 293 ? -12.96400 0.29200   -38.35500 1.000 33.41000  ? 259 PHE   A CG     1 
ATOM   3642 C CD1    . PHE   A 1 293 ? -13.16200 -1.04700  -38.08100 1.000 36.28000  ? 259 PHE   A CD1    1 
ATOM   3643 C CD2    . PHE   A 1 293 ? -11.93600 0.65400   -39.20300 1.000 35.22000  ? 259 PHE   A CD2    1 
ATOM   3644 C CE1    . PHE   A 1 293 ? -12.33200 -2.02400  -38.62300 1.000 35.36000  ? 259 PHE   A CE1    1 
ATOM   3645 C CE2    . PHE   A 1 293 ? -11.10300 -0.31000  -39.76300 1.000 35.04000  ? 259 PHE   A CE2    1 
ATOM   3646 C CZ     . PHE   A 1 293 ? -11.29800 -1.65800  -39.46500 1.000 38.40000  ? 259 PHE   A CZ     1 
ATOM   3647 H H      . PHE   A 1 293 ? -14.95800 3.04800   -36.48500 1.000 32.98000  ? 259 PHE   A H      1 
ATOM   3648 H HA     . PHE   A 1 293 ? -13.70300 0.92700   -35.76200 1.000 34.73000  ? 259 PHE   A HA     1 
ATOM   3649 H HB2    . PHE   A 1 293 ? -14.77100 0.98100   -37.79600 1.000 33.01000  ? 259 PHE   A HB2    1 
ATOM   3650 H HB3    . PHE   A 1 293 ? -13.80000 2.12300   -38.31700 1.000 33.01000  ? 259 PHE   A HB3    1 
ATOM   3651 H HD1    . PHE   A 1 293 ? -13.85200 -1.29900  -37.51000 1.000 36.28000  ? 259 PHE   A HD1    1 
ATOM   3652 H HD2    . PHE   A 1 293 ? -11.79800 1.55200   -39.40100 1.000 35.22000  ? 259 PHE   A HD2    1 
ATOM   3653 H HE1    . PHE   A 1 293 ? -12.47500 -2.92100  -38.42300 1.000 35.36000  ? 259 PHE   A HE1    1 
ATOM   3654 H HE2    . PHE   A 1 293 ? -10.40900 -0.05400  -40.32600 1.000 35.04000  ? 259 PHE   A HE2    1 
ATOM   3655 H HZ     . PHE   A 1 293 ? -10.74400 -2.30600  -39.83600 1.000 38.40000  ? 259 PHE   A HZ     1 
ATOM   3656 N N      . LEU   A 1 294 ? -11.66500 3.27900   -36.57600 1.000 30.98000  ? 260 LEU   A N      1 
ATOM   3657 C CA     . LEU   A 1 294 ? -10.26100 3.67200   -36.44200 1.000 30.53000  ? 260 LEU   A CA     1 
ATOM   3658 C C      . LEU   A 1 294 ? -9.85000  3.79900   -34.98200 1.000 29.22000  ? 260 LEU   A C      1 
ATOM   3659 O O      . LEU   A 1 294 ? -8.71900  3.43600   -34.62100 1.000 31.20000  ? 260 LEU   A O      1 
ATOM   3660 C CB     . LEU   A 1 294 ? -9.99800  4.99100   -37.17900 1.000 33.67000  ? 260 LEU   A CB     1 
ATOM   3661 C CG     . LEU   A 1 294 ? -10.14800 4.90600   -38.71300 1.000 37.24000  ? 260 LEU   A CG     1 
ATOM   3662 C CD1    . LEU   A 1 294 ? -9.86400  6.26900   -39.32300 1.000 37.19000  ? 260 LEU   A CD1    1 
ATOM   3663 C CD2    . LEU   A 1 294 ? -9.23500  3.82700   -39.28600 1.000 34.89000  ? 260 LEU   A CD2    1 
ATOM   3664 H H      . LEU   A 1 294 ? -12.17900 3.87700   -36.91900 1.000 30.98000  ? 260 LEU   A H      1 
ATOM   3665 H HA     . LEU   A 1 294 ? -9.70500  2.98400   -36.84000 1.000 30.53000  ? 260 LEU   A HA     1 
ATOM   3666 H HB2    . LEU   A 1 294 ? -10.62700 5.65700   -36.85800 1.000 33.67000  ? 260 LEU   A HB2    1 
ATOM   3667 H HB3    . LEU   A 1 294 ? -9.09200  5.27800   -36.98700 1.000 33.67000  ? 260 LEU   A HB3    1 
ATOM   3668 H HG     . LEU   A 1 294 ? -11.06400 4.66800   -38.92700 1.000 37.24000  ? 260 LEU   A HG     1 
ATOM   3669 H HD11   . LEU   A 1 294 ? -9.96200  6.21000   -40.28600 1.000 37.19000  ? 260 LEU   A HD11   1 
ATOM   3670 H HD12   . LEU   A 1 294 ? -10.49500 6.91200   -38.96500 1.000 37.19000  ? 260 LEU   A HD12   1 
ATOM   3671 H HD13   . LEU   A 1 294 ? -8.95800  6.53300   -39.09700 1.000 37.19000  ? 260 LEU   A HD13   1 
ATOM   3672 H HD21   . LEU   A 1 294 ? -9.15400  3.95800   -40.24400 1.000 34.89000  ? 260 LEU   A HD21   1 
ATOM   3673 H HD22   . LEU   A 1 294 ? -8.36300  3.89700   -38.86700 1.000 34.89000  ? 260 LEU   A HD22   1 
ATOM   3674 H HD23   . LEU   A 1 294 ? -9.62000  2.95600   -39.10200 1.000 34.89000  ? 260 LEU   A HD23   1 
ATOM   3675 N N      . HIS   A 1 295 ? -10.73600 4.33200   -34.13400 1.000 28.83000  ? 261 HIS   A N      1 
ATOM   3676 C CA     . HIS   A 1 295 ? -10.44900 4.38700   -32.70000 1.000 30.51000  ? 261 HIS   A CA     1 
ATOM   3677 C C      . HIS   A 1 295 ? -10.16700 2.98800   -32.14400 1.000 28.99000  ? 261 HIS   A C      1 
ATOM   3678 O O      . HIS   A 1 295 ? -9.21200  2.79600   -31.38700 1.000 28.31000  ? 261 HIS   A O      1 
ATOM   3679 C CB     . HIS   A 1 295 ? -11.60700 5.03700   -31.93500 1.000 32.98000  ? 261 HIS   A CB     1 
ATOM   3680 C CG     . HIS   A 1 295 ? -11.42000 6.50300   -31.66000 1.000 30.90000  ? 261 HIS   A CG     1 
ATOM   3681 N ND1    . HIS   A 1 295 ? -10.60700 6.98000   -30.64700 1.000 37.18000  ? 261 HIS   A ND1    1 
ATOM   3682 C CD2    . HIS   A 1 295 ? -11.97700 7.59800   -32.23700 1.000 33.73000  ? 261 HIS   A CD2    1 
ATOM   3683 C CE1    . HIS   A 1 295 ? -10.65800 8.30300   -30.62400 1.000 38.60000  ? 261 HIS   A CE1    1 
ATOM   3684 N NE2    . HIS   A 1 295 ? -11.47200 8.70400   -31.58800 1.000 33.30000  ? 261 HIS   A NE2    1 
ATOM   3685 H H      . HIS   A 1 295 ? -11.49700 4.66300   -34.36100 1.000 28.83000  ? 261 HIS   A H      1 
ATOM   3686 H HA     . HIS   A 1 295 ? -9.65700  4.92900   -32.55900 1.000 30.51000  ? 261 HIS   A HA     1 
ATOM   3687 H HB2    . HIS   A 1 295 ? -12.42000 4.93600   -32.45400 1.000 32.98000  ? 261 HIS   A HB2    1 
ATOM   3688 H HB3    . HIS   A 1 295 ? -11.70600 4.58700   -31.08100 1.000 32.98000  ? 261 HIS   A HB3    1 
ATOM   3689 H HD2    . HIS   A 1 295 ? -12.57100 7.60200   -32.95300 1.000 33.73000  ? 261 HIS   A HD2    1 
ATOM   3690 H HE1    . HIS   A 1 295 ? -10.19000 8.85600   -30.04100 1.000 38.60000  ? 261 HIS   A HE1    1 
ATOM   3691 H HE2    . HIS   A 1 295 ? -11.66700 9.52200   -31.76900 1.000 33.30000  ? 261 HIS   A HE2    1 
ATOM   3692 N N      . VAL   A 1 296 ? -11.00100 2.00700   -32.49700 1.000 30.33000  ? 262 VAL   A N      1 
ATOM   3693 C CA     . VAL   A 1 296 ? -10.79900 0.63000   -32.03200 1.000 29.89000  ? 262 VAL   A CA     1 
ATOM   3694 C C      . VAL   A 1 296 ? -9.49500  0.05100   -32.58300 1.000 31.66000  ? 262 VAL   A C      1 
ATOM   3695 O O      . VAL   A 1 296 ? -8.72100  -0.59500  -31.86100 1.000 29.91000  ? 262 VAL   A O      1 
ATOM   3696 C CB     . VAL   A 1 296 ? -12.00500 -0.24900  -32.41500 1.000 32.44000  ? 262 VAL   A CB     1 
ATOM   3697 C CG1    . VAL   A 1 296 ? -11.74400 -1.71100  -31.99600 1.000 28.41000  ? 262 VAL   A CG1    1 
ATOM   3698 C CG2    . VAL   A 1 296 ? -13.27100 0.29700   -31.77700 1.000 31.74000  ? 262 VAL   A CG2    1 
ATOM   3699 H H      . VAL   A 1 296 ? -11.68800 2.11100   -33.00300 1.000 30.33000  ? 262 VAL   A H      1 
ATOM   3700 H HA     . VAL   A 1 296 ? -10.73300 0.63500   -31.06400 1.000 29.89000  ? 262 VAL   A HA     1 
ATOM   3701 H HB     . VAL   A 1 296 ? -12.12000 -0.22800  -33.37800 1.000 32.44000  ? 262 VAL   A HB     1 
ATOM   3702 H HG11   . VAL   A 1 296 ? -12.58300 -2.19700  -32.01500 1.000 28.41000  ? 262 VAL   A HG11   1 
ATOM   3703 H HG12   . VAL   A 1 296 ? -11.11600 -2.11300  -32.61600 1.000 28.41000  ? 262 VAL   A HG12   1 
ATOM   3704 H HG13   . VAL   A 1 296 ? -11.37800 -1.72100  -31.09800 1.000 28.41000  ? 262 VAL   A HG13   1 
ATOM   3705 H HG21   . VAL   A 1 296 ? -14.01700 -0.27400  -32.02000 1.000 31.74000  ? 262 VAL   A HG21   1 
ATOM   3706 H HG22   . VAL   A 1 296 ? -13.16000 0.30400   -30.81300 1.000 31.74000  ? 262 VAL   A HG22   1 
ATOM   3707 H HG23   . VAL   A 1 296 ? -13.42700 1.19800   -32.09800 1.000 31.74000  ? 262 VAL   A HG23   1 
ATOM   3708 N N      . LEU   A 1 297 ? -9.24500  0.24800   -33.88000 1.000 31.41000  ? 263 LEU   A N      1 
ATOM   3709 C CA     . LEU   A 1 297 ? -7.97300  -0.16700  -34.47900 1.000 33.37000  ? 263 LEU   A CA     1 
ATOM   3710 C C      . LEU   A 1 297 ? -6.77200  0.39000   -33.71700 1.000 36.62000  ? 263 LEU   A C      1 
ATOM   3711 O O      . LEU   A 1 297 ? -5.74200  -0.27800  -33.57900 1.000 34.25000  ? 263 LEU   A O      1 
ATOM   3712 C CB     . LEU   A 1 297 ? -7.91900  0.30100   -35.93400 1.000 33.58000  ? 263 LEU   A CB     1 
ATOM   3713 C CG     . LEU   A 1 297 ? -7.27700  -0.51100  -37.05400 1.000 41.97000  ? 263 LEU   A CG     1 
ATOM   3714 C CD1    . LEU   A 1 297 ? -7.56800  -2.02600  -36.94700 1.000 36.31000  ? 263 LEU   A CD1    1 
ATOM   3715 C CD2    . LEU   A 1 297 ? -7.76200  0.05000   -38.39200 1.000 43.08000  ? 263 LEU   A CD2    1 
ATOM   3716 H H      . LEU   A 1 297 ? -9.79300  0.61800   -34.42900 1.000 31.41000  ? 263 LEU   A H      1 
ATOM   3717 H HA     . LEU   A 1 297 ? -7.91700  -1.13500  -34.46200 1.000 33.37000  ? 263 LEU   A HA     1 
ATOM   3718 H HB2    . LEU   A 1 297 ? -8.83500  0.45100   -36.21500 1.000 33.58000  ? 263 LEU   A HB2    1 
ATOM   3719 H HB3    . LEU   A 1 297 ? -7.46000  1.15500   -35.93400 1.000 33.58000  ? 263 LEU   A HB3    1 
ATOM   3720 H HG     . LEU   A 1 297 ? -6.31500  -0.39100  -37.01400 1.000 41.97000  ? 263 LEU   A HG     1 
ATOM   3721 H HD11   . LEU   A 1 297 ? -7.25200  -2.46500  -37.75200 1.000 36.31000  ? 263 LEU   A HD11   1 
ATOM   3722 H HD12   . LEU   A 1 297 ? -7.10600  -2.38300  -36.17300 1.000 36.31000  ? 263 LEU   A HD12   1 
ATOM   3723 H HD13   . LEU   A 1 297 ? -8.52400  -2.15800  -36.85300 1.000 36.31000  ? 263 LEU   A HD13   1 
ATOM   3724 H HD21   . LEU   A 1 297 ? -7.08200  -0.11600  -39.06100 1.000 43.08000  ? 263 LEU   A HD21   1 
ATOM   3725 H HD22   . LEU   A 1 297 ? -8.58800  -0.39300  -38.63900 1.000 43.08000  ? 263 LEU   A HD22   1 
ATOM   3726 H HD23   . LEU   A 1 297 ? -7.90800  1.00500   -38.30100 1.000 43.08000  ? 263 LEU   A HD23   1 
ATOM   3727 N N      . ALA   A 1 298 ? -6.87400  1.63400   -33.25100 1.000 32.35000  ? 264 ALA   A N      1 
ATOM   3728 C CA     . ALA   A 1 298 ? -5.80200  2.25800   -32.49000 1.000 33.80000  ? 264 ALA   A CA     1 
ATOM   3729 C C      . ALA   A 1 298 ? -5.70200  1.70200   -31.08300 1.000 33.80000  ? 264 ALA   A C      1 
ATOM   3730 O O      . ALA   A 1 298 ? -4.66700  1.88300   -30.43300 1.000 30.99000  ? 264 ALA   A O      1 
ATOM   3731 C CB     . ALA   A 1 298 ? -6.01200  3.77600   -32.40900 1.000 31.23000  ? 264 ALA   A CB     1 
ATOM   3732 H H      . ALA   A 1 298 ? -7.56100  2.13900   -33.36500 1.000 32.35000  ? 264 ALA   A H      1 
ATOM   3733 H HA     . ALA   A 1 298 ? -4.95800  2.09400   -32.93900 1.000 33.80000  ? 264 ALA   A HA     1 
ATOM   3734 H HB1    . ALA   A 1 298 ? -5.29200  4.16700   -31.88900 1.000 31.23000  ? 264 ALA   A HB1    1 
ATOM   3735 H HB2    . ALA   A 1 298 ? -6.01000  4.14300   -33.30700 1.000 31.23000  ? 264 ALA   A HB2    1 
ATOM   3736 H HB3    . ALA   A 1 298 ? -6.86400  3.95400   -31.98000 1.000 31.23000  ? 264 ALA   A HB3    1 
ATOM   3737 N N      . GLY   A 1 299 ? -6.76800  1.08300   -30.57700 1.000 32.02000  ? 265 GLY   A N      1 
ATOM   3738 C CA     . GLY   A 1 299 ? -6.70300  0.44100   -29.28300 1.000 31.58000  ? 265 GLY   A CA     1 
ATOM   3739 C C      . GLY   A 1 299 ? -7.90300  0.64800   -28.38200 1.000 33.25000  ? 265 GLY   A C      1 
ATOM   3740 O O      . GLY   A 1 299 ? -7.91300  0.13100   -27.27000 1.000 32.78000  ? 265 GLY   A O      1 
ATOM   3741 H H      . GLY   A 1 299 ? -7.53300  1.02500   -30.96500 1.000 32.02000  ? 265 GLY   A H      1 
ATOM   3742 H HA2    . GLY   A 1 299 ? -6.59600  -0.51400  -29.41600 1.000 31.58000  ? 265 GLY   A HA2    1 
ATOM   3743 H HA3    . GLY   A 1 299 ? -5.92200  0.76300   -28.80700 1.000 31.58000  ? 265 GLY   A HA3    1 
ATOM   3744 N N      . ALA   A 1 300 ? -8.91700  1.39500   -28.81600 1.000 28.93000  ? 266 ALA   A N      1 
ATOM   3745 C CA     . ALA   A 1 300 ? -10.01000 1.74400   -27.91500 1.000 30.21000  ? 266 ALA   A CA     1 
ATOM   3746 C C      . ALA   A 1 300 ? -10.91000 0.54700   -27.60700 1.000 30.13000  ? 266 ALA   A C      1 
ATOM   3747 O O      . ALA   A 1 300 ? -11.30500 -0.19800  -28.50600 1.000 30.99000  ? 266 ALA   A O      1 
ATOM   3748 C CB     . ALA   A 1 300 ? -10.87000 2.85900   -28.51900 1.000 28.55000  ? 266 ALA   A CB     1 
ATOM   3749 H H      . ALA   A 1 300 ? -8.99500  1.70700   -29.61400 1.000 28.93000  ? 266 ALA   A H      1 
ATOM   3750 H HA     . ALA   A 1 300 ? -9.64100  2.06700   -27.07800 1.000 30.21000  ? 266 ALA   A HA     1 
ATOM   3751 H HB1    . ALA   A 1 300 ? -11.58700 3.07300   -27.90200 1.000 28.55000  ? 266 ALA   A HB1    1 
ATOM   3752 H HB2    . ALA   A 1 300 ? -10.31500 3.64100   -28.66500 1.000 28.55000  ? 266 ALA   A HB2    1 
ATOM   3753 H HB3    . ALA   A 1 300 ? -11.23800 2.55200   -29.36200 1.000 28.55000  ? 266 ALA   A HB3    1 
ATOM   3754 N N      . SER   A 1 301 ? -11.26200 0.39900   -26.33000 1.000 30.23000  ? 267 SER   A N      1 
ATOM   3755 C CA     . SER   A 1 301 ? -12.27000 -0.56500  -25.88000 1.000 33.79000  ? 267 SER   A CA     1 
ATOM   3756 C C      . SER   A 1 301 ? -13.67600 0.02600   -25.96900 1.000 38.26000  ? 267 SER   A C      1 
ATOM   3757 O O      . SER   A 1 301 ? -14.57400 -0.60200  -26.54200 1.000 38.56000  ? 267 SER   A O      1 
ATOM   3758 C CB     . SER   A 1 301 ? -11.98400 -1.02500  -24.44000 1.000 32.99000  ? 267 SER   A CB     1 
ATOM   3759 O OG     . SER   A 1 301 ? -10.85700 -1.87500  -24.39900 1.000 37.20000  ? 267 SER   A OG     1 
ATOM   3760 H H      . SER   A 1 301 ? -10.92200 0.85800   -25.68700 1.000 30.23000  ? 267 SER   A H      1 
ATOM   3761 H HA     . SER   A 1 301 ? -12.23800 -1.34500  -26.45400 1.000 33.79000  ? 267 SER   A HA     1 
ATOM   3762 H HB2    . SER   A 1 301 ? -11.81200 -0.24600  -23.88800 1.000 32.99000  ? 267 SER   A HB2    1 
ATOM   3763 H HB3    . SER   A 1 301 ? -12.75600 -1.50700  -24.10300 1.000 32.99000  ? 267 SER   A HB3    1 
ATOM   3764 H HG     . SER   A 1 301 ? -10.18100 -1.47000  -24.68900 1.000 37.20000  ? 267 SER   A HG     1 
ATOM   3765 N N      . MET   A 1 302 ? -13.87700 1.22000   -25.40500 1.000 32.04000  ? 268 MET   A N      1 
ATOM   3766 C CA     . MET   A 1 302 ? -15.09300 2.00900   -25.55500 1.000 32.44000  ? 268 MET   A CA     1 
ATOM   3767 C C      . MET   A 1 302 ? -14.78400 3.22200   -26.42000 1.000 35.98000  ? 268 MET   A C      1 
ATOM   3768 O O      . MET   A 1 302 ? -13.62900 3.64300   -26.53400 1.000 31.95000  ? 268 MET   A O      1 
ATOM   3769 C CB     . MET   A 1 302 ? -15.64900 2.49900   -24.20900 1.000 33.25000  ? 268 MET   A CB     1 
ATOM   3770 C CG     . MET   A 1 302 ? -16.15500 1.40700   -23.21700 1.000 37.59000  ? 268 MET   A CG     1 
ATOM   3771 S SD     . MET   A 1 302 ? -17.45000 0.32300   -23.81100 1.000 40.64000  ? 268 MET   A SD     1 
ATOM   3772 C CE     . MET   A 1 302 ? -18.90600 1.35600   -23.47400 1.000 41.80000  ? 268 MET   A CE     1 
ATOM   3773 H H      . MET   A 1 302 ? -13.29100 1.60700   -24.90800 1.000 32.04000  ? 268 MET   A H      1 
ATOM   3774 H HA     . MET   A 1 302 ? -15.77400 1.47100   -25.98800 1.000 32.44000  ? 268 MET   A HA     1 
ATOM   3775 H HB2    . MET   A 1 302 ? -14.95000 2.99500   -23.75600 1.000 33.25000  ? 268 MET   A HB2    1 
ATOM   3776 H HB3    . MET   A 1 302 ? -16.39600 3.09100   -24.38800 1.000 33.25000  ? 268 MET   A HB3    1 
ATOM   3777 H HG2    . MET   A 1 302 ? -15.40200 0.84700   -22.97300 1.000 37.59000  ? 268 MET   A HG2    1 
ATOM   3778 H HG3    . MET   A 1 302 ? -16.49400 1.85200   -22.42400 1.000 37.59000  ? 268 MET   A HG3    1 
ATOM   3779 H HE1    . MET   A 1 302 ? -19.70300 0.87900   -23.75500 1.000 41.80000  ? 268 MET   A HE1    1 
ATOM   3780 H HE2    . MET   A 1 302 ? -18.94800 1.54100   -22.52300 1.000 41.80000  ? 268 MET   A HE2    1 
ATOM   3781 H HE3    . MET   A 1 302 ? -18.82500 2.18600   -23.96900 1.000 41.80000  ? 268 MET   A HE3    1 
ATOM   3782 N N      . VAL   A 1 303 ? -15.83300 3.79300   -27.01500 1.000 33.75000  ? 269 VAL   A N      1 
ATOM   3783 C CA     . VAL   A 1 303 ? -15.70900 4.95300   -27.90300 1.000 32.67000  ? 269 VAL   A CA     1 
ATOM   3784 C C      . VAL   A 1 303 ? -16.73400 5.98600   -27.44700 1.000 35.33000  ? 269 VAL   A C      1 
ATOM   3785 O O      . VAL   A 1 303 ? -17.94500 5.73200   -27.49900 1.000 35.71000  ? 269 VAL   A O      1 
ATOM   3786 C CB     . VAL   A 1 303 ? -15.90900 4.57800   -29.38700 1.000 34.00000  ? 269 VAL   A CB     1 
ATOM   3787 C CG1    . VAL   A 1 303 ? -15.77600 5.81600   -30.28800 1.000 29.98000  ? 269 VAL   A CG1    1 
ATOM   3788 C CG2    . VAL   A 1 303 ? -14.88600 3.53000   -29.82200 1.000 33.52000  ? 269 VAL   A CG2    1 
ATOM   3789 H H      . VAL   A 1 303 ? -16.64300 3.52100   -26.91800 1.000 33.75000  ? 269 VAL   A H      1 
ATOM   3790 H HA     . VAL   A 1 303 ? -14.82500 5.34000   -27.80500 1.000 32.67000  ? 269 VAL   A HA     1 
ATOM   3791 H HB     . VAL   A 1 303 ? -16.79700 4.20600   -29.50800 1.000 34.00000  ? 269 VAL   A HB     1 
ATOM   3792 H HG11   . VAL   A 1 303 ? -15.76800 5.53000   -31.21500 1.000 29.98000  ? 269 VAL   A HG11   1 
ATOM   3793 H HG12   . VAL   A 1 303 ? -16.53000 6.40600   -30.13100 1.000 29.98000  ? 269 VAL   A HG12   1 
ATOM   3794 H HG13   . VAL   A 1 303 ? -14.94700 6.27300   -30.07600 1.000 29.98000  ? 269 VAL   A HG13   1 
ATOM   3795 H HG21   . VAL   A 1 303 ? -15.01800 3.33200   -30.76200 1.000 33.52000  ? 269 VAL   A HG21   1 
ATOM   3796 H HG22   . VAL   A 1 303 ? -13.99400 3.88300   -29.68000 1.000 33.52000  ? 269 VAL   A HG22   1 
ATOM   3797 H HG23   . VAL   A 1 303 ? -15.01200 2.72700   -29.29300 1.000 33.52000  ? 269 VAL   A HG23   1 
ATOM   3798 N N      . GLN   A 1 304 ? -16.25600 7.13400   -26.98100 1.000 36.16000  ? 270 GLN   A N      1 
ATOM   3799 C CA     . GLN   A 1 304 ? -17.11500 8.19800   -26.48100 1.000 33.18000  ? 270 GLN   A CA     1 
ATOM   3800 C C      . GLN   A 1 304 ? -17.35600 9.22600   -27.57400 1.000 38.63000  ? 270 GLN   A C      1 
ATOM   3801 O O      . GLN   A 1 304 ? -16.50600 9.44100   -28.44100 1.000 36.89000  ? 270 GLN   A O      1 
ATOM   3802 C CB     . GLN   A 1 304 ? -16.49600 8.86900   -25.26400 1.000 31.08000  ? 270 GLN   A CB     1 
ATOM   3803 C CG     . GLN   A 1 304 ? -16.02000 7.88300   -24.21900 1.000 38.42000  ? 270 GLN   A CG     1 
ATOM   3804 C CD     . GLN   A 1 304 ? -15.62000 8.56300   -22.93400 1.000 37.97000  ? 270 GLN   A CD     1 
ATOM   3805 O OE1    . GLN   A 1 304 ? -15.23100 9.73000   -22.93600 1.000 42.85000  ? 270 GLN   A OE1    1 
ATOM   3806 N NE2    . GLN   A 1 304 ? -15.72200 7.83800   -21.80900 1.000 38.16000  ? 270 GLN   A NE2    1 
ATOM   3807 H H      . GLN   A 1 304 ? -15.41800 7.32400   -26.94400 1.000 36.16000  ? 270 GLN   A H      1 
ATOM   3808 H HA     . GLN   A 1 304 ? -17.96900 7.82300   -26.21900 1.000 33.18000  ? 270 GLN   A HA     1 
ATOM   3809 H HB2    . GLN   A 1 304 ? -15.73200 9.39300   -25.54900 1.000 31.08000  ? 270 GLN   A HB2    1 
ATOM   3810 H HB3    . GLN   A 1 304 ? -17.15800 9.44600   -24.85100 1.000 31.08000  ? 270 GLN   A HB3    1 
ATOM   3811 H HG2    . GLN   A 1 304 ? -16.73400 7.25800   -24.02100 1.000 38.42000  ? 270 GLN   A HG2    1 
ATOM   3812 H HG3    . GLN   A 1 304 ? -15.24600 7.40700   -24.56000 1.000 38.42000  ? 270 GLN   A HG3    1 
ATOM   3813 H HE21   . GLN   A 1 304 ? -16.00000 7.02500   -21.84500 1.000 38.16000  ? 270 GLN   A HE21   1 
ATOM   3814 H HE22   . GLN   A 1 304 ? -15.50600 8.18500   -21.05300 1.000 38.16000  ? 270 GLN   A HE22   1 
ATOM   3815 N N      . VAL   A 1 305 ? -18.52400 9.86300   -27.52500 1.000 35.51000  ? 271 VAL   A N      1 
ATOM   3816 C CA     . VAL   A 1 305 ? -18.99400 10.75000  -28.59000 1.000 37.07000  ? 271 VAL   A CA     1 
ATOM   3817 C C      . VAL   A 1 305 ? -19.47800 12.04100  -27.93700 1.000 37.97000  ? 271 VAL   A C      1 
ATOM   3818 O O      . VAL   A 1 305 ? -20.39900 12.01500  -27.10800 1.000 35.09000  ? 271 VAL   A O      1 
ATOM   3819 C CB     . VAL   A 1 305 ? -20.11000 10.10400  -29.43300 1.000 37.39000  ? 271 VAL   A CB     1 
ATOM   3820 C CG1    . VAL   A 1 305 ? -20.51800 11.02300  -30.59600 1.000 40.39000  ? 271 VAL   A CG1    1 
ATOM   3821 C CG2    . VAL   A 1 305 ? -19.67300 8.74200   -29.97800 1.000 38.26000  ? 271 VAL   A CG2    1 
ATOM   3822 H H      . VAL   A 1 305 ? -19.07600 9.79600   -26.86900 1.000 35.51000  ? 271 VAL   A H      1 
ATOM   3823 H HA     . VAL   A 1 305 ? -18.25500 10.96600  -29.17900 1.000 37.07000  ? 271 VAL   A HA     1 
ATOM   3824 H HB     . VAL   A 1 305 ? -20.88900 9.96600   -28.87200 1.000 37.39000  ? 271 VAL   A HB     1 
ATOM   3825 H HG11   . VAL   A 1 305 ? -21.14100 10.54800  -31.16800 1.000 40.39000  ? 271 VAL   A HG11   1 
ATOM   3826 H HG12   . VAL   A 1 305 ? -20.94000 11.82000  -30.23800 1.000 40.39000  ? 271 VAL   A HG12   1 
ATOM   3827 H HG13   . VAL   A 1 305 ? -19.72500 11.26400  -31.10000 1.000 40.39000  ? 271 VAL   A HG13   1 
ATOM   3828 H HG21   . VAL   A 1 305 ? -20.37600 8.38900   -30.54500 1.000 38.26000  ? 271 VAL   A HG21   1 
ATOM   3829 H HG22   . VAL   A 1 305 ? -18.85800 8.85500   -30.49200 1.000 38.26000  ? 271 VAL   A HG22   1 
ATOM   3830 H HG23   . VAL   A 1 305 ? -19.51500 8.14000   -29.23400 1.000 38.26000  ? 271 VAL   A HG23   1 
ATOM   3831 N N      . GLY   A 1 306 ? -18.84100 13.16500  -28.28700 1.000 33.72000  ? 272 GLY   A N      1 
ATOM   3832 C CA     . GLY   A 1 306 ? -19.11300 14.42800  -27.64100 1.000 31.36000  ? 272 GLY   A CA     1 
ATOM   3833 C C      . GLY   A 1 306 ? -19.76700 15.40900  -28.59000 1.000 40.93000  ? 272 GLY   A C      1 
ATOM   3834 O O      . GLY   A 1 306 ? -20.99100 15.48100  -28.63600 1.000 37.55000  ? 272 GLY   A O      1 
ATOM   3835 H H      . GLY   A 1 306 ? -18.24300 13.21000  -28.90300 1.000 33.72000  ? 272 GLY   A H      1 
ATOM   3836 H HA2    . GLY   A 1 306 ? -19.70200 14.29100  -26.88300 1.000 31.36000  ? 272 GLY   A HA2    1 
ATOM   3837 H HA3    . GLY   A 1 306 ? -18.28300 14.81400  -27.32100 1.000 31.36000  ? 272 GLY   A HA3    1 
ATOM   3838 N N      . THR   A 1 307 ? -18.96100 16.13300  -29.37800 1.000 38.36000  ? 273 THR   A N      1 
ATOM   3839 C CA     . THR   A 1 307 ? -19.48300 17.14700  -30.30300 1.000 37.31000  ? 273 THR   A CA     1 
ATOM   3840 C C      . THR   A 1 307 ? -20.56900 16.59400  -31.23300 1.000 38.79000  ? 273 THR   A C      1 
ATOM   3841 O O      . THR   A 1 307 ? -21.63200 17.20000  -31.38400 1.000 41.34000  ? 273 THR   A O      1 
ATOM   3842 C CB     . THR   A 1 307 ? -18.32700 17.74200  -31.12500 1.000 33.96000  ? 273 THR   A CB     1 
ATOM   3843 O OG1    . THR   A 1 307 ? -17.40400 18.40900  -30.25000 1.000 35.04000  ? 273 THR   A OG1    1 
ATOM   3844 C CG2    . THR   A 1 307 ? -18.85500 18.73100  -32.18700 1.000 36.71000  ? 273 THR   A CG2    1 
ATOM   3845 H H      . THR   A 1 307 ? -18.10500 16.05500  -29.39500 1.000 38.36000  ? 273 THR   A H      1 
ATOM   3846 H HA     . THR   A 1 307 ? -19.87700 17.86600  -29.78500 1.000 37.31000  ? 273 THR   A HA     1 
ATOM   3847 H HB     . THR   A 1 307 ? -17.86400 17.02500  -31.58600 1.000 33.96000  ? 273 THR   A HB     1 
ATOM   3848 H HG1    . THR   A 1 307 ? -17.09200 17.86400  -29.69200 1.000 35.04000  ? 273 THR   A HG1    1 
ATOM   3849 H HG21   . THR   A 1 307 ? -18.12400 19.27100  -32.52600 1.000 36.71000  ? 273 THR   A HG21   1 
ATOM   3850 H HG22   . THR   A 1 307 ? -19.25600 18.24700  -32.92600 1.000 36.71000  ? 273 THR   A HG22   1 
ATOM   3851 H HG23   . THR   A 1 307 ? -19.52100 19.31600  -31.79300 1.000 36.71000  ? 273 THR   A HG23   1 
ATOM   3852 N N      . ALA   A 1 308 ? -20.31500 15.45300  -31.89000 1.000 37.92000  ? 274 ALA   A N      1 
ATOM   3853 C CA     . ALA   A 1 308 ? -21.30200 14.92700  -32.83600 1.000 35.12000  ? 274 ALA   A CA     1 
ATOM   3854 C C      . ALA   A 1 308 ? -22.62200 14.57300  -32.15000 1.000 46.51000  ? 274 ALA   A C      1 
ATOM   3855 O O      . ALA   A 1 308 ? -23.68800 14.68200  -32.76600 1.000 42.52000  ? 274 ALA   A O      1 
ATOM   3856 C CB     . ALA   A 1 308 ? -20.74800 13.71000  -33.57800 1.000 39.20000  ? 274 ALA   A CB     1 
ATOM   3857 H H      . ALA   A 1 308 ? -19.60100 14.98000  -31.80800 1.000 37.92000  ? 274 ALA   A H      1 
ATOM   3858 H HA     . ALA   A 1 308 ? -21.49100 15.61200  -33.49700 1.000 35.12000  ? 274 ALA   A HA     1 
ATOM   3859 H HB1    . ALA   A 1 308 ? -21.39100 13.42700  -34.24700 1.000 39.20000  ? 274 ALA   A HB1    1 
ATOM   3860 H HB2    . ALA   A 1 308 ? -19.91200 13.95500  -34.00200 1.000 39.20000  ? 274 ALA   A HB2    1 
ATOM   3861 H HB3    . ALA   A 1 308 ? -20.59500 12.99500  -32.94000 1.000 39.20000  ? 274 ALA   A HB3    1 
ATOM   3862 N N      . LEU   A 1 309 ? -22.56700 14.14000  -30.88400 1.000 40.79000  ? 275 LEU   A N      1 
ATOM   3863 C CA     . LEU   A 1 309 ? -23.77300 13.85500  -30.10100 1.000 40.54000  ? 275 LEU   A CA     1 
ATOM   3864 C C      . LEU   A 1 309 ? -24.51200 15.13200  -29.71900 1.000 46.39000  ? 275 LEU   A C      1 
ATOM   3865 O O      . LEU   A 1 309 ? -25.74700 15.17400  -29.74300 1.000 47.21000  ? 275 LEU   A O      1 
ATOM   3866 C CB     . LEU   A 1 309 ? -23.40400 13.07200  -28.83700 1.000 40.26000  ? 275 LEU   A CB     1 
ATOM   3867 C CG     . LEU   A 1 309 ? -24.49200 12.94100  -27.76600 1.000 45.39000  ? 275 LEU   A CG     1 
ATOM   3868 C CD1    . LEU   A 1 309 ? -25.71900 12.21500  -28.31100 1.000 43.17000  ? 275 LEU   A CD1    1 
ATOM   3869 C CD2    . LEU   A 1 309 ? -23.94300 12.22900  -26.53600 1.000 39.21000  ? 275 LEU   A CD2    1 
ATOM   3870 H H      . LEU   A 1 309 ? -21.83500 14.00300  -30.45400 1.000 40.79000  ? 275 LEU   A H      1 
ATOM   3871 H HA     . LEU   A 1 309 ? -24.37300 13.30700  -30.63100 1.000 40.54000  ? 275 LEU   A HA     1 
ATOM   3872 H HB2    . LEU   A 1 309 ? -23.15200 12.17300  -29.10100 1.000 40.26000  ? 275 LEU   A HB2    1 
ATOM   3873 H HB3    . LEU   A 1 309 ? -22.64400 13.50900  -28.42200 1.000 40.26000  ? 275 LEU   A HB3    1 
ATOM   3874 H HG     . LEU   A 1 309 ? -24.77200 13.82500  -27.48400 1.000 45.39000  ? 275 LEU   A HG     1 
ATOM   3875 H HD11   . LEU   A 1 309 ? -26.37200 12.12200  -27.60000 1.000 43.17000  ? 275 LEU   A HD11   1 
ATOM   3876 H HD12   . LEU   A 1 309 ? -26.09500 12.73300  -29.03900 1.000 43.17000  ? 275 LEU   A HD12   1 
ATOM   3877 H HD13   . LEU   A 1 309 ? -25.45100 11.33900  -28.63100 1.000 43.17000  ? 275 LEU   A HD13   1 
ATOM   3878 H HD21   . LEU   A 1 309 ? -24.64700 12.15800  -25.87300 1.000 39.21000  ? 275 LEU   A HD21   1 
ATOM   3879 H HD22   . LEU   A 1 309 ? -23.63900 11.34400  -26.79300 1.000 39.21000  ? 275 LEU   A HD22   1 
ATOM   3880 H HD23   . LEU   A 1 309 ? -23.20200 12.74300  -26.17900 1.000 39.21000  ? 275 LEU   A HD23   1 
ATOM   3881 N N      . HIS   A 1 310 ? -23.77000 16.16900  -29.32400 1.000 38.96000  ? 276 HIS   A N      1 
ATOM   3882 C CA     . HIS   A 1 310 ? -24.37100 17.46600  -29.03600 1.000 47.35000  ? 276 HIS   A CA     1 
ATOM   3883 C C      . HIS   A 1 310 ? -25.12500 18.01300  -30.24500 1.000 49.87000  ? 276 HIS   A C      1 
ATOM   3884 O O      . HIS   A 1 310 ? -26.13200 18.70800  -30.08600 1.000 49.43000  ? 276 HIS   A O      1 
ATOM   3885 C CB     . HIS   A 1 310 ? -23.27500 18.43800  -28.59900 1.000 51.05000  ? 276 HIS   A CB     1 
ATOM   3886 C CG     . HIS   A 1 310 ? -23.78100 19.72700  -28.03900 1.000 62.54000  ? 276 HIS   A CG     1 
ATOM   3887 N ND1    . HIS   A 1 310 ? -24.34700 20.70900  -28.82400 1.000 63.89000  ? 276 HIS   A ND1    1 
ATOM   3888 C CD2    . HIS   A 1 310 ? -23.77300 20.21200  -26.77400 1.000 58.04000  ? 276 HIS   A CD2    1 
ATOM   3889 C CE1    . HIS   A 1 310 ? -24.68300 21.73700  -28.06300 1.000 58.91000  ? 276 HIS   A CE1    1 
ATOM   3890 N NE2    . HIS   A 1 310 ? -24.34600 21.46100  -26.81500 1.000 61.79000  ? 276 HIS   A NE2    1 
ATOM   3891 H H      . HIS   A 1 310 ? -22.91700 16.14400  -29.21600 1.000 38.96000  ? 276 HIS   A H      1 
ATOM   3892 H HA     . HIS   A 1 310 ? -25.00100 17.37000  -28.30400 1.000 47.35000  ? 276 HIS   A HA     1 
ATOM   3893 H HB2    . HIS   A 1 310 ? -22.73600 18.01100  -27.91500 1.000 51.05000  ? 276 HIS   A HB2    1 
ATOM   3894 H HB3    . HIS   A 1 310 ? -22.72200 18.64800  -29.36700 1.000 51.05000  ? 276 HIS   A HB3    1 
ATOM   3895 H HD2    . HIS   A 1 310 ? -23.45000 19.77700  -26.01800 1.000 58.04000  ? 276 HIS   A HD2    1 
ATOM   3896 H HE1    . HIS   A 1 310 ? -25.08800 22.52100  -28.35600 1.000 58.91000  ? 276 HIS   A HE1    1 
ATOM   3897 H HE2    . HIS   A 1 310 ? -24.46600 21.97900  -26.13900 1.000 61.79000  ? 276 HIS   A HE2    1 
ATOM   3898 N N      . GLU   A 1 311 ? -24.66400 17.69600  -31.45500 0.900 42.45000  ? 277 GLU   A N      1 
ATOM   3899 C CA     . GLU   A 1 311 ? -25.29900 18.21800  -32.65700 0.900 48.06000  ? 277 GLU   A CA     1 
ATOM   3900 C C      . GLU   A 1 311 ? -26.49000 17.36300  -33.06900 0.900 56.95000  ? 277 GLU   A C      1 
ATOM   3901 O O      . GLU   A 1 311 ? -27.51900 17.88500  -33.51200 0.900 51.24000  ? 277 GLU   A O      1 
ATOM   3902 C CB     . GLU   A 1 311 ? -24.26600 18.30100  -33.77900 0.900 48.42000  ? 277 GLU   A CB     1 
ATOM   3903 C CG     . GLU   A 1 311 ? -23.09400 19.18800  -33.40000 0.900 47.51000  ? 277 GLU   A CG     1 
ATOM   3904 C CD     . GLU   A 1 311 ? -22.13500 19.44100  -34.54400 0.900 63.73000  ? 277 GLU   A CD     1 
ATOM   3905 O OE1    . GLU   A 1 311 ? -22.14000 18.64500  -35.50600 0.900 64.72000  ? 277 GLU   A OE1    1 
ATOM   3906 O OE2    . GLU   A 1 311 ? -21.37100 20.43500  -34.47400 0.900 74.02000  ? 277 GLU   A OE2    1 
ATOM   3907 H H      . GLU   A 1 311 ? -23.98900 17.18400  -31.60300 0.900 42.45000  ? 277 GLU   A H      1 
ATOM   3908 H HA     . GLU   A 1 311 ? -25.62100 19.11600  -32.48000 0.900 48.06000  ? 277 GLU   A HA     1 
ATOM   3909 H HB2    . GLU   A 1 311 ? -23.92600 17.41200  -33.96600 0.900 48.42000  ? 277 GLU   A HB2    1 
ATOM   3910 H HB3    . GLU   A 1 311 ? -24.68400 18.67300  -34.57100 0.900 48.42000  ? 277 GLU   A HB3    1 
ATOM   3911 H HG2    . GLU   A 1 311 ? -23.44100 20.04600  -33.11000 0.900 47.51000  ? 277 GLU   A HG2    1 
ATOM   3912 H HG3    . GLU   A 1 311 ? -22.59900 18.77500  -32.68000 0.900 47.51000  ? 277 GLU   A HG3    1 
ATOM   3913 N N      . GLU   A 1 312 ? -26.37700 16.04800  -32.91600 1.000 41.92000  ? 278 GLU   A N      1 
ATOM   3914 C CA     . GLU   A 1 312 ? -27.33900 15.11600  -33.48100 1.000 44.01000  ? 278 GLU   A CA     1 
ATOM   3915 C C      . GLU   A 1 312 ? -28.27400 14.47200  -32.45600 1.000 51.94000  ? 278 GLU   A C      1 
ATOM   3916 O O      . GLU   A 1 312 ? -29.28000 13.87500  -32.85500 1.000 50.80000  ? 278 GLU   A O      1 
ATOM   3917 C CB     . GLU   A 1 312 ? -26.58500 14.02700  -34.24800 1.000 54.35000  ? 278 GLU   A CB     1 
ATOM   3918 C CG     . GLU   A 1 312 ? -27.41500 13.14700  -35.15100 1.000 50.03000  ? 278 GLU   A CG     1 
ATOM   3919 C CD     . GLU   A 1 312 ? -26.53000 12.24100  -35.98000 1.000 58.17000  ? 278 GLU   A CD     1 
ATOM   3920 O OE1    . GLU   A 1 312 ? -25.41000 12.69100  -36.32900 1.000 58.37000  ? 278 GLU   A OE1    1 
ATOM   3921 O OE2    . GLU   A 1 312 ? -26.93400 11.08500  -36.26800 1.000 59.66000  ? 278 GLU   A OE2    1 
ATOM   3922 H H      . GLU   A 1 312 ? -25.74000 15.66700  -32.48100 1.000 41.92000  ? 278 GLU   A H      1 
ATOM   3923 H HA     . GLU   A 1 312 ? -27.89200 15.59100  -34.12000 1.000 44.01000  ? 278 GLU   A HA     1 
ATOM   3924 H HB2    . GLU   A 1 312 ? -25.91400 14.45900  -34.80000 1.000 54.35000  ? 278 GLU   A HB2    1 
ATOM   3925 H HB3    . GLU   A 1 312 ? -26.14800 13.44800  -33.60400 1.000 54.35000  ? 278 GLU   A HB3    1 
ATOM   3926 H HG2    . GLU   A 1 312 ? -28.00100 12.59300  -34.61200 1.000 50.03000  ? 278 GLU   A HG2    1 
ATOM   3927 H HG3    . GLU   A 1 312 ? -27.93500 13.70200  -35.75300 1.000 50.03000  ? 278 GLU   A HG3    1 
ATOM   3928 N N      . GLY   A 1 313 ? -27.98300 14.56500  -31.16100 1.000 50.77000  ? 279 GLY   A N      1 
ATOM   3929 C CA     . GLY   A 1 313 ? -28.80700 13.89600  -30.16200 1.000 42.22000  ? 279 GLY   A CA     1 
ATOM   3930 C C      . GLY   A 1 313 ? -28.65300 12.37600  -30.18700 1.000 44.74000  ? 279 GLY   A C      1 
ATOM   3931 O O      . GLY   A 1 313 ? -27.97500 11.79100  -31.03200 1.000 45.44000  ? 279 GLY   A O      1 
ATOM   3932 H H      . GLY   A 1 313 ? -27.31900 15.00600  -30.83800 1.000 50.77000  ? 279 GLY   A H      1 
ATOM   3933 H HA2    . GLY   A 1 313 ? -28.56300 14.21400  -29.27900 1.000 42.22000  ? 279 GLY   A HA2    1 
ATOM   3934 H HA3    . GLY   A 1 313 ? -29.74000 14.11100  -30.31800 1.000 42.22000  ? 279 GLY   A HA3    1 
ATOM   3935 N N      . ALA   A 1 314 ? -29.35300 11.73100  -29.24300 1.000 44.31000  ? 280 ALA   A N      1 
ATOM   3936 C CA     . ALA   A 1 314 ? -29.11700 10.32400  -28.91600 1.000 43.63000  ? 280 ALA   A CA     1 
ATOM   3937 C C      . ALA   A 1 314 ? -29.43700 9.36400   -30.05700 1.000 54.07000  ? 280 ALA   A C      1 
ATOM   3938 O O      . ALA   A 1 314 ? -29.00900 8.20400   -30.00500 1.000 50.33000  ? 280 ALA   A O      1 
ATOM   3939 C CB     . ALA   A 1 314 ? -29.92300 9.94000   -27.67100 1.000 51.28000  ? 280 ALA   A CB     1 
ATOM   3940 H H      . ALA   A 1 314 ? -29.97600 12.09400  -28.77500 1.000 44.31000  ? 280 ALA   A H      1 
ATOM   3941 H HA     . ALA   A 1 314 ? -28.17800 10.21400  -28.70000 1.000 43.63000  ? 280 ALA   A HA     1 
ATOM   3942 H HB1    . ALA   A 1 314 ? -29.75900 9.00700   -27.46600 1.000 51.28000  ? 280 ALA   A HB1    1 
ATOM   3943 H HB2    . ALA   A 1 314 ? -29.64100 10.49700  -26.92900 1.000 51.28000  ? 280 ALA   A HB2    1 
ATOM   3944 H HB3    . ALA   A 1 314 ? -30.86600 10.07900  -27.85000 1.000 51.28000  ? 280 ALA   A HB3    1 
ATOM   3945 N N      . ALA   A 1 315 ? -30.17200 9.80100   -31.08300 1.000 48.82000  ? 281 ALA   A N      1 
ATOM   3946 C CA     . ALA   A 1 315 ? -30.40500 8.93800   -32.23900 1.000 46.03000  ? 281 ALA   A CA     1 
ATOM   3947 C C      . ALA   A 1 315 ? -29.11200 8.57600   -32.96100 1.000 47.29000  ? 281 ALA   A C      1 
ATOM   3948 O O      . ALA   A 1 315 ? -29.08300 7.59200   -33.71200 1.000 44.81000  ? 281 ALA   A O      1 
ATOM   3949 C CB     . ALA   A 1 315 ? -31.37100 9.60800   -33.22200 1.000 48.69000  ? 281 ALA   A CB     1 
ATOM   3950 H H      . ALA   A 1 315 ? -30.53900 10.57700  -31.13300 1.000 48.82000  ? 281 ALA   A H      1 
ATOM   3951 H HA     . ALA   A 1 315 ? -30.81600 8.11300   -31.93500 1.000 46.03000  ? 281 ALA   A HA     1 
ATOM   3952 H HB1    . ALA   A 1 315 ? -31.51000 9.01800   -33.97900 1.000 48.69000  ? 281 ALA   A HB1    1 
ATOM   3953 H HB2    . ALA   A 1 315 ? -32.21400 9.77400   -32.77200 1.000 48.69000  ? 281 ALA   A HB2    1 
ATOM   3954 H HB3    . ALA   A 1 315 ? -30.98500 10.44600  -33.52200 1.000 48.69000  ? 281 ALA   A HB3    1 
ATOM   3955 N N      . ILE   A 1 316 ? -28.04300 9.35000   -32.75400 1.000 46.06000  ? 282 ILE   A N      1 
ATOM   3956 C CA     . ILE   A 1 316 ? -26.77800 9.07300   -33.42900 1.000 42.81000  ? 282 ILE   A CA     1 
ATOM   3957 C C      . ILE   A 1 316 ? -26.27700 7.66100   -33.12900 1.000 36.92000  ? 282 ILE   A C      1 
ATOM   3958 O O      . ILE   A 1 316 ? -25.66600 7.01600   -33.99000 1.000 42.65000  ? 282 ILE   A O      1 
ATOM   3959 C CB     . ILE   A 1 316 ? -25.73200 10.12800  -33.03300 1.000 41.29000  ? 282 ILE   A CB     1 
ATOM   3960 C CG1    . ILE   A 1 316 ? -24.52400 10.05500  -33.96600 1.000 42.66000  ? 282 ILE   A CG1    1 
ATOM   3961 C CG2    . ILE   A 1 316 ? -25.30400 9.94300   -31.58800 1.000 41.39000  ? 282 ILE   A CG2    1 
ATOM   3962 C CD1    . ILE   A 1 316 ? -23.45700 11.06400  -33.64500 1.000 44.73000  ? 282 ILE   A CD1    1 
ATOM   3963 H H      . ILE   A 1 316 ? -28.02600 10.03400  -32.23300 1.000 46.06000  ? 282 ILE   A H      1 
ATOM   3964 H HA     . ILE   A 1 316 ? -26.91600 9.13900   -34.38700 1.000 42.81000  ? 282 ILE   A HA     1 
ATOM   3965 H HB     . ILE   A 1 316 ? -26.13500 11.00600  -33.12200 1.000 41.29000  ? 282 ILE   A HB     1 
ATOM   3966 H HG12   . ILE   A 1 316 ? -24.12700 9.17300   -33.89700 1.000 42.66000  ? 282 ILE   A HG12   1 
ATOM   3967 H HG13   . ILE   A 1 316 ? -24.82100 10.21300  -34.87500 1.000 42.66000  ? 282 ILE   A HG13   1 
ATOM   3968 H HG21   . ILE   A 1 316 ? -24.86500 10.75200  -31.28200 1.000 41.39000  ? 282 ILE   A HG21   1 
ATOM   3969 H HG22   . ILE   A 1 316 ? -26.09000 9.76900   -31.04600 1.000 41.39000  ? 282 ILE   A HG22   1 
ATOM   3970 H HG23   . ILE   A 1 316 ? -24.69200 9.19300   -31.53200 1.000 41.39000  ? 282 ILE   A HG23   1 
ATOM   3971 H HD11   . ILE   A 1 316 ? -22.80100 11.06600  -34.35900 1.000 44.73000  ? 282 ILE   A HD11   1 
ATOM   3972 H HD12   . ILE   A 1 316 ? -23.86500 11.94000  -33.56800 1.000 44.73000  ? 282 ILE   A HD12   1 
ATOM   3973 H HD13   . ILE   A 1 316 ? -23.03300 10.82200  -32.80700 1.000 44.73000  ? 282 ILE   A HD13   1 
ATOM   3974 N N      . PHE   A 1 317 ? -26.53100 7.15000   -31.92200 1.000 39.42000  ? 283 PHE   A N      1 
ATOM   3975 C CA     . PHE   A 1 317 ? -26.01500 5.82100   -31.58700 1.000 43.44000  ? 283 PHE   A CA     1 
ATOM   3976 C C      . PHE   A 1 317 ? -26.64200 4.72500   -32.45000 1.000 54.39000  ? 283 PHE   A C      1 
ATOM   3977 O O      . PHE   A 1 317 ? -25.97800 3.72200   -32.75800 1.000 49.78000  ? 283 PHE   A O      1 
ATOM   3978 C CB     . PHE   A 1 317 ? -26.22000 5.55000   -30.09800 1.000 43.49000  ? 283 PHE   A CB     1 
ATOM   3979 C CG     . PHE   A 1 317 ? -25.47400 6.50500   -29.21000 1.000 42.07000  ? 283 PHE   A CG     1 
ATOM   3980 C CD1    . PHE   A 1 317 ? -24.09200 6.47100   -29.14000 1.000 44.08000  ? 283 PHE   A CD1    1 
ATOM   3981 C CD2    . PHE   A 1 317 ? -26.15500 7.43500   -28.44400 1.000 40.12000  ? 283 PHE   A CD2    1 
ATOM   3982 C CE1    . PHE   A 1 317 ? -23.40300 7.36500   -28.31500 1.000 42.30000  ? 283 PHE   A CE1    1 
ATOM   3983 C CE2    . PHE   A 1 317 ? -25.48300 8.31200   -27.61300 1.000 41.19000  ? 283 PHE   A CE2    1 
ATOM   3984 C CZ     . PHE   A 1 317 ? -24.10500 8.28300   -27.54700 1.000 46.17000  ? 283 PHE   A CZ     1 
ATOM   3985 H H      . PHE   A 1 317 ? -26.98300 7.53600   -31.30000 1.000 39.42000  ? 283 PHE   A H      1 
ATOM   3986 H HA     . PHE   A 1 317 ? -25.06000 5.81200   -31.75600 1.000 43.44000  ? 283 PHE   A HA     1 
ATOM   3987 H HB2    . PHE   A 1 317 ? -27.16500 5.62800   -29.89200 1.000 43.49000  ? 283 PHE   A HB2    1 
ATOM   3988 H HB3    . PHE   A 1 317 ? -25.91100 4.65300   -29.89700 1.000 43.49000  ? 283 PHE   A HB3    1 
ATOM   3989 H HD1    . PHE   A 1 317 ? -23.61800 5.85600   -29.65200 1.000 44.08000  ? 283 PHE   A HD1    1 
ATOM   3990 H HD2    . PHE   A 1 317 ? -27.08400 7.46100   -28.47900 1.000 40.12000  ? 283 PHE   A HD2    1 
ATOM   3991 H HE1    . PHE   A 1 317 ? -22.47400 7.33600   -28.27100 1.000 42.30000  ? 283 PHE   A HE1    1 
ATOM   3992 H HE2    . PHE   A 1 317 ? -25.95900 8.93000   -27.10700 1.000 41.19000  ? 283 PHE   A HE2    1 
ATOM   3993 H HZ     . PHE   A 1 317 ? -23.65000 8.87700   -26.99500 1.000 46.17000  ? 283 PHE   A HZ     1 
ATOM   3994 N N      . GLU   A 1 318 ? -27.90300 4.89100   -32.86700 1.000 50.14000  ? 284 GLU   A N      1 
ATOM   3995 C CA     . GLU   A 1 318 ? -28.47900 3.95600   -33.83100 1.000 48.45000  ? 284 GLU   A CA     1 
ATOM   3996 C C      . GLU   A 1 318 ? -27.68400 3.95900   -35.12900 1.000 44.73000  ? 284 GLU   A C      1 
ATOM   3997 O O      . GLU   A 1 318 ? -27.40400 2.90300   -35.70900 1.000 46.03000  ? 284 GLU   A O      1 
ATOM   3998 C CB     . GLU   A 1 318 ? -29.94800 4.31000   -34.09800 1.000 52.02000  ? 284 GLU   A CB     1 
ATOM   3999 C CG     . GLU   A 1 318 ? -30.87200 4.00900   -32.91400 1.000 61.49000  ? 284 GLU   A CG     1 
ATOM   4000 C CD     . GLU   A 1 318 ? -32.10500 4.91700   -32.84300 1.000 84.69000  ? 284 GLU   A CD     1 
ATOM   4001 O OE1    . GLU   A 1 318 ? -32.67800 5.25800   -33.90600 1.000 74.37000  ? 284 GLU   A OE1    1 
ATOM   4002 O OE2    . GLU   A 1 318 ? -32.50000 5.29200   -31.71100 1.000 82.20000  ? 284 GLU   A OE2    1 
ATOM   4003 H H      . GLU   A 1 318 ? -28.43100 5.52100   -32.61300 1.000 50.14000  ? 284 GLU   A H      1 
ATOM   4004 H HA     . GLU   A 1 318 ? -28.44800 3.06000   -33.46100 1.000 48.45000  ? 284 GLU   A HA     1 
ATOM   4005 H HB2    . GLU   A 1 318 ? -30.01200 5.25800   -34.29200 1.000 52.02000  ? 284 GLU   A HB2    1 
ATOM   4006 H HB3    . GLU   A 1 318 ? -30.26100 3.79600   -34.85800 1.000 52.02000  ? 284 GLU   A HB3    1 
ATOM   4007 H HG2    . GLU   A 1 318 ? -31.18300 3.09300   -32.98500 1.000 61.49000  ? 284 GLU   A HG2    1 
ATOM   4008 H HG3    . GLU   A 1 318 ? -30.37200 4.12300   -32.09100 1.000 61.49000  ? 284 GLU   A HG3    1 
ATOM   4009 N N      . ARG   A 1 319 ? -27.30000 5.14500   -35.59200 1.000 47.10000  ? 285 ARG   A N      1 
ATOM   4010 C CA     . ARG   A 1 319 ? -26.53600 5.25400   -36.82600 1.000 44.22000  ? 285 ARG   A CA     1 
ATOM   4011 C C      . ARG   A 1 319 ? -25.11400 4.73300   -36.64700 1.000 41.94000  ? 285 ARG   A C      1 
ATOM   4012 O O      . ARG   A 1 319 ? -24.59100 4.04000   -37.52800 1.000 40.91000  ? 285 ARG   A O      1 
ATOM   4013 C CB     . ARG   A 1 319 ? -26.53000 6.71600   -37.28600 1.000 47.77000  ? 285 ARG   A CB     1 
ATOM   4014 C CG     . ARG   A 1 319 ? -25.64800 6.98800   -38.47200 1.000 43.68000  ? 285 ARG   A CG     1 
ATOM   4015 C CD     . ARG   A 1 319 ? -25.85300 8.40000   -39.00300 1.000 44.00000  ? 285 ARG   A CD     1 
ATOM   4016 N NE     . ARG   A 1 319 ? -25.29400 9.41600   -38.11800 1.000 46.18000  ? 285 ARG   A NE     1 
ATOM   4017 C CZ     . ARG   A 1 319 ? -23.99900 9.68700   -38.02100 1.000 45.17000  ? 285 ARG   A CZ     1 
ATOM   4018 N NH1    . ARG   A 1 319 ? -23.10100 9.03700   -38.74800 1.000 39.65000  ? 285 ARG   A NH1    1 
ATOM   4019 N NH2    . ARG   A 1 319 ? -23.59500 10.63100  -37.17100 1.000 45.72000  ? 285 ARG   A NH2    1 
ATOM   4020 H H      . ARG   A 1 319 ? -27.46900 5.89700   -35.21100 1.000 47.10000  ? 285 ARG   A H      1 
ATOM   4021 H HA     . ARG   A 1 319 ? -26.96700 4.72300   -37.51400 1.000 44.22000  ? 285 ARG   A HA     1 
ATOM   4022 H HB2    . ARG   A 1 319 ? -27.43500 6.96900   -37.52700 1.000 47.77000  ? 285 ARG   A HB2    1 
ATOM   4023 H HB3    . ARG   A 1 319 ? -26.21900 7.27100   -36.55400 1.000 47.77000  ? 285 ARG   A HB3    1 
ATOM   4024 H HG2    . ARG   A 1 319 ? -24.71800 6.89700   -38.21100 1.000 43.68000  ? 285 ARG   A HG2    1 
ATOM   4025 H HG3    . ARG   A 1 319 ? -25.86200 6.36200   -39.18100 1.000 43.68000  ? 285 ARG   A HG3    1 
ATOM   4026 H HD2    . ARG   A 1 319 ? -25.42000 8.48000   -39.86700 1.000 44.00000  ? 285 ARG   A HD2    1 
ATOM   4027 H HD3    . ARG   A 1 319 ? -26.80400 8.57000   -39.09200 1.000 44.00000  ? 285 ARG   A HD3    1 
ATOM   4028 H HE     . ARG   A 1 319 ? -25.83300 9.83400   -37.59400 1.000 46.18000  ? 285 ARG   A HE     1 
ATOM   4029 H HH11   . ARG   A 1 319 ? -23.35000 8.42500   -39.29900 1.000 39.65000  ? 285 ARG   A HH11   1 
ATOM   4030 H HH12   . ARG   A 1 319 ? -22.26600 9.22800   -38.66900 1.000 39.65000  ? 285 ARG   A HH12   1 
ATOM   4031 H HH21   . ARG   A 1 319 ? -24.17100 11.05700  -36.69600 1.000 45.72000  ? 285 ARG   A HH21   1 
ATOM   4032 H HH22   . ARG   A 1 319 ? -22.75800 10.81600  -37.10000 1.000 45.72000  ? 285 ARG   A HH22   1 
ATOM   4033 N N      . LEU   A 1 320 ? -24.47200 5.06400   -35.51800 1.000 39.89000  ? 286 LEU   A N      1 
ATOM   4034 C CA     . LEU   A 1 320 ? -23.08400 4.64200   -35.29300 1.000 43.52000  ? 286 LEU   A CA     1 
ATOM   4035 C C      . LEU   A 1 320 ? -22.94800 3.11900   -35.21900 1.000 39.50000  ? 286 LEU   A C      1 
ATOM   4036 O O      . LEU   A 1 320 ? -22.03200 2.54500   -35.82000 1.000 41.34000  ? 286 LEU   A O      1 
ATOM   4037 C CB     . LEU   A 1 320 ? -22.53300 5.29200   -34.02300 1.000 39.51000  ? 286 LEU   A CB     1 
ATOM   4038 C CG     . LEU   A 1 320 ? -22.29600 6.81300   -34.09600 1.000 36.44000  ? 286 LEU   A CG     1 
ATOM   4039 C CD1    . LEU   A 1 320 ? -21.90000 7.38600   -32.75200 1.000 38.97000  ? 286 LEU   A CD1    1 
ATOM   4040 C CD2    . LEU   A 1 320 ? -21.26000 7.13100   -35.15900 1.000 40.36000  ? 286 LEU   A CD2    1 
ATOM   4041 H H      . LEU   A 1 320 ? -24.81300 5.52500   -34.87700 1.000 39.89000  ? 286 LEU   A H      1 
ATOM   4042 H HA     . LEU   A 1 320 ? -22.54500 4.94300   -36.04100 1.000 43.52000  ? 286 LEU   A HA     1 
ATOM   4043 H HB2    . LEU   A 1 320 ? -23.16000 5.13100   -33.30000 1.000 39.51000  ? 286 LEU   A HB2    1 
ATOM   4044 H HB3    . LEU   A 1 320 ? -21.68300 4.87600   -33.81100 1.000 39.51000  ? 286 LEU   A HB3    1 
ATOM   4045 H HG     . LEU   A 1 320 ? -23.12500 7.23800   -34.36200 1.000 36.44000  ? 286 LEU   A HG     1 
ATOM   4046 H HD11   . LEU   A 1 320 ? -21.76800 8.34300   -32.84400 1.000 38.97000  ? 286 LEU   A HD11   1 
ATOM   4047 H HD12   . LEU   A 1 320 ? -22.60800 7.20900   -32.11300 1.000 38.97000  ? 286 LEU   A HD12   1 
ATOM   4048 H HD13   . LEU   A 1 320 ? -21.07700 6.96400   -32.46000 1.000 38.97000  ? 286 LEU   A HD13   1 
ATOM   4049 H HD21   . LEU   A 1 320 ? -20.97800 8.05400   -35.05800 1.000 40.36000  ? 286 LEU   A HD21   1 
ATOM   4050 H HD22   . LEU   A 1 320 ? -20.50000 6.53900   -35.04600 1.000 40.36000  ? 286 LEU   A HD22   1 
ATOM   4051 H HD23   . LEU   A 1 320 ? -21.65400 7.00000   -36.03500 1.000 40.36000  ? 286 LEU   A HD23   1 
ATOM   4052 N N      . THR   A 1 321 ? -23.84300 2.43800   -34.49600 1.000 41.03000  ? 287 THR   A N      1 
ATOM   4053 C CA     . THR   A 1 321 ? -23.72000 0.97700   -34.43500 1.000 41.19000  ? 287 THR   A CA     1 
ATOM   4054 C C      . THR   A 1 321 ? -23.88400 0.35000   -35.81400 1.000 46.62000  ? 287 THR   A C      1 
ATOM   4055 O O      . THR   A 1 321 ? -23.15700 -0.58500  -36.17000 1.000 43.77000  ? 287 THR   A O      1 
ATOM   4056 C CB     . THR   A 1 321 ? -24.73300 0.37000   -33.46000 1.000 46.40000  ? 287 THR   A CB     1 
ATOM   4057 O OG1    . THR   A 1 321 ? -26.03100 0.92900   -33.69000 1.000 56.17000  ? 287 THR   A OG1    1 
ATOM   4058 C CG2    . THR   A 1 321 ? -24.31600 0.60500   -32.03600 1.000 43.45000  ? 287 THR   A CG2    1 
ATOM   4059 H H      . THR   A 1 321 ? -24.49700 2.77700   -34.05300 1.000 41.03000  ? 287 THR   A H      1 
ATOM   4060 H HA     . THR   A 1 321 ? -22.83200 0.75400   -34.11400 1.000 41.19000  ? 287 THR   A HA     1 
ATOM   4061 H HB     . THR   A 1 321 ? -24.77300 -0.58800  -33.60500 1.000 46.40000  ? 287 THR   A HB     1 
ATOM   4062 H HG1    . THR   A 1 321 ? -26.03100 1.74600   -33.49700 1.000 56.17000  ? 287 THR   A HG1    1 
ATOM   4063 H HG21   . THR   A 1 321 ? -24.96800 0.21700   -31.43200 1.000 43.45000  ? 287 THR   A HG21   1 
ATOM   4064 H HG22   . THR   A 1 321 ? -23.45200 0.19600   -31.87200 1.000 43.45000  ? 287 THR   A HG22   1 
ATOM   4065 H HG23   . THR   A 1 321 ? -24.25300 1.55700   -31.86200 1.000 43.45000  ? 287 THR   A HG23   1 
ATOM   4066 N N      . ALA   A 1 322 ? -24.82900 0.85400   -36.61500 1.000 45.18000  ? 288 ALA   A N      1 
ATOM   4067 C CA     . ALA   A 1 322 ? -25.04700 0.25400   -37.92600 1.000 44.09000  ? 288 ALA   A CA     1 
ATOM   4068 C C      . ALA   A 1 322 ? -23.86100 0.49900   -38.85200 1.000 40.16000  ? 288 ALA   A C      1 
ATOM   4069 O O      . ALA   A 1 322 ? -23.46500 -0.39100  -39.61800 1.000 45.27000  ? 288 ALA   A O      1 
ATOM   4070 C CB     . ALA   A 1 322 ? -26.33800 0.79200   -38.54200 1.000 53.20000  ? 288 ALA   A CB     1 
ATOM   4071 H H      . ALA   A 1 322 ? -25.33900 1.52000   -36.42800 1.000 45.18000  ? 288 ALA   A H      1 
ATOM   4072 H HA     . ALA   A 1 322 ? -25.14600 -0.70500  -37.81900 1.000 44.09000  ? 288 ALA   A HA     1 
ATOM   4073 H HB1    . ALA   A 1 322 ? -26.46700 0.38300   -39.41200 1.000 53.20000  ? 288 ALA   A HB1    1 
ATOM   4074 H HB2    . ALA   A 1 322 ? -27.08100 0.57200   -37.95900 1.000 53.20000  ? 288 ALA   A HB2    1 
ATOM   4075 H HB3    . ALA   A 1 322 ? -26.26500 1.75500   -38.63600 1.000 53.20000  ? 288 ALA   A HB3    1 
ATOM   4076 N N      . GLU   A 1 323 ? -23.27200 1.69800   -38.78900 1.000 47.07000  ? 289 GLU   A N      1 
ATOM   4077 C CA     . GLU   A 1 323 ? -22.11900 1.99700   -39.63400 1.000 40.06000  ? 289 GLU   A CA     1 
ATOM   4078 C C      . GLU   A 1 323 ? -20.90900 1.15600   -39.24400 1.000 35.94000  ? 289 GLU   A C      1 
ATOM   4079 O O      . GLU   A 1 323 ? -20.18700 0.65600   -40.11600 1.000 43.85000  ? 289 GLU   A O      1 
ATOM   4080 C CB     . GLU   A 1 323 ? -21.79700 3.48800   -39.55400 1.000 43.59000  ? 289 GLU   A CB     1 
ATOM   4081 C CG     . GLU   A 1 323 ? -22.75800 4.35100   -40.37500 1.000 45.59000  ? 289 GLU   A CG     1 
ATOM   4082 C CD     . GLU   A 1 323 ? -22.61100 5.84000   -40.09500 1.000 55.80000  ? 289 GLU   A CD     1 
ATOM   4083 O OE1    . GLU   A 1 323 ? -21.75200 6.20800   -39.27500 1.000 49.25000  ? 289 GLU   A OE1    1 
ATOM   4084 O OE2    . GLU   A 1 323 ? -23.36300 6.64200   -40.69300 1.000 54.37000  ? 289 GLU   A OE2    1 
ATOM   4085 H H      . GLU   A 1 323 ? -23.51700 2.34200   -38.27500 1.000 47.07000  ? 289 GLU   A H      1 
ATOM   4086 H HA     . GLU   A 1 323 ? -22.34200 1.78900   -40.55500 1.000 40.06000  ? 289 GLU   A HA     1 
ATOM   4087 H HB2    . GLU   A 1 323 ? -21.85400 3.77300   -38.62900 1.000 43.59000  ? 289 GLU   A HB2    1 
ATOM   4088 H HB3    . GLU   A 1 323 ? -20.90000 3.63500   -39.89100 1.000 43.59000  ? 289 GLU   A HB3    1 
ATOM   4089 H HG2    . GLU   A 1 323 ? -22.58400 4.20600   -41.31800 1.000 45.59000  ? 289 GLU   A HG2    1 
ATOM   4090 H HG3    . GLU   A 1 323 ? -23.67000 4.09600   -40.16300 1.000 45.59000  ? 289 GLU   A HG3    1 
ATOM   4091 N N      . LEU   A 1 324 ? -20.66800 0.98800   -37.93900 1.000 39.50000  ? 290 LEU   A N      1 
ATOM   4092 C CA     . LEU   A 1 324 ? -19.55600 0.14800   -37.49100 1.000 39.11000  ? 290 LEU   A CA     1 
ATOM   4093 C C      . LEU   A 1 324 ? -19.75800 -1.30300  -37.92000 1.000 38.44000  ? 290 LEU   A C      1 
ATOM   4094 O O      . LEU   A 1 324 ? -18.83500 -1.94700  -38.43900 1.000 39.96000  ? 290 LEU   A O      1 
ATOM   4095 C CB     . LEU   A 1 324 ? -19.40200 0.26000   -35.97200 1.000 39.23000  ? 290 LEU   A CB     1 
ATOM   4096 C CG     . LEU   A 1 324 ? -18.23800 -0.49900  -35.32800 1.000 38.06000  ? 290 LEU   A CG     1 
ATOM   4097 C CD1    . LEU   A 1 324 ? -16.94200 -0.25500  -36.11000 1.000 35.19000  ? 290 LEU   A CD1    1 
ATOM   4098 C CD2    . LEU   A 1 324 ? -18.10700 -0.10100  -33.84900 1.000 36.81000  ? 290 LEU   A CD2    1 
ATOM   4099 H H      . LEU   A 1 324 ? -21.12600 1.34400   -37.30400 1.000 39.50000  ? 290 LEU   A H      1 
ATOM   4100 H HA     . LEU   A 1 324 ? -18.74100 0.47100   -37.90400 1.000 39.11000  ? 290 LEU   A HA     1 
ATOM   4101 H HB2    . LEU   A 1 324 ? -19.28900 1.19700   -35.75000 1.000 39.23000  ? 290 LEU   A HB2    1 
ATOM   4102 H HB3    . LEU   A 1 324 ? -20.21800 -0.06800  -35.56200 1.000 39.23000  ? 290 LEU   A HB3    1 
ATOM   4103 H HG     . LEU   A 1 324 ? -18.42900 -1.44900  -35.36200 1.000 38.06000  ? 290 LEU   A HG     1 
ATOM   4104 H HD11   . LEU   A 1 324 ? -16.19500 -0.59900  -35.59500 1.000 35.19000  ? 290 LEU   A HD11   1 
ATOM   4105 H HD12   . LEU   A 1 324 ? -16.99400 -0.71500  -36.96300 1.000 35.19000  ? 290 LEU   A HD12   1 
ATOM   4106 H HD13   . LEU   A 1 324 ? -16.83400 0.69800   -36.25200 1.000 35.19000  ? 290 LEU   A HD13   1 
ATOM   4107 H HD21   . LEU   A 1 324 ? -17.36800 -0.59000  -33.45500 1.000 36.81000  ? 290 LEU   A HD21   1 
ATOM   4108 H HD22   . LEU   A 1 324 ? -17.94100 0.85300   -33.79300 1.000 36.81000  ? 290 LEU   A HD22   1 
ATOM   4109 H HD23   . LEU   A 1 324 ? -18.93200 -0.32100  -33.38900 1.000 36.81000  ? 290 LEU   A HD23   1 
ATOM   4110 N N      . LEU   A 1 325 ? -20.96600 -1.83800  -37.71600 1.000 39.98000  ? 291 LEU   A N      1 
ATOM   4111 C CA     . LEU   A 1 325 ? -21.24100 -3.20200  -38.17000 1.000 47.06000  ? 291 LEU   A CA     1 
ATOM   4112 C C      . LEU   A 1 325 ? -21.06900 -3.33400  -39.67500 1.000 44.28000  ? 291 LEU   A C      1 
ATOM   4113 O O      . LEU   A 1 325 ? -20.63300 -4.38700  -40.16900 1.000 44.52000  ? 291 LEU   A O      1 
ATOM   4114 C CB     . LEU   A 1 325 ? -22.65400 -3.61000  -37.76300 1.000 43.25000  ? 291 LEU   A CB     1 
ATOM   4115 C CG     . LEU   A 1 325 ? -22.79000 -4.05000  -36.30800 1.000 48.17000  ? 291 LEU   A CG     1 
ATOM   4116 C CD1    . LEU   A 1 325 ? -24.24000 -4.01000  -35.87300 1.000 43.75000  ? 291 LEU   A CD1    1 
ATOM   4117 C CD2    . LEU   A 1 325 ? -22.19300 -5.45400  -36.12600 1.000 42.05000  ? 291 LEU   A CD2    1 
ATOM   4118 H H      . LEU   A 1 325 ? -21.62500 -1.44400  -37.32800 1.000 39.98000  ? 291 LEU   A H      1 
ATOM   4119 H HA     . LEU   A 1 325 ? -20.61500 -3.80700  -37.74400 1.000 47.06000  ? 291 LEU   A HA     1 
ATOM   4120 H HB2    . LEU   A 1 325 ? -23.24600 -2.85400  -37.89900 1.000 43.25000  ? 291 LEU   A HB2    1 
ATOM   4121 H HB3    . LEU   A 1 325 ? -22.93600 -4.35100  -38.32200 1.000 43.25000  ? 291 LEU   A HB3    1 
ATOM   4122 H HG     . LEU   A 1 325 ? -22.29100 -3.43700  -35.74500 1.000 48.17000  ? 291 LEU   A HG     1 
ATOM   4123 H HD11   . LEU   A 1 325 ? -24.30000 -4.30200  -34.95000 1.000 43.75000  ? 291 LEU   A HD11   1 
ATOM   4124 H HD12   . LEU   A 1 325 ? -24.56900 -3.10100  -35.95500 1.000 43.75000  ? 291 LEU   A HD12   1 
ATOM   4125 H HD13   . LEU   A 1 325 ? -24.75600 -4.60200  -36.44200 1.000 43.75000  ? 291 LEU   A HD13   1 
ATOM   4126 H HD21   . LEU   A 1 325 ? -21.83200 -5.52700  -35.22900 1.000 42.05000  ? 291 LEU   A HD21   1 
ATOM   4127 H HD22   . LEU   A 1 325 ? -22.89400 -6.11200  -36.25300 1.000 42.05000  ? 291 LEU   A HD22   1 
ATOM   4128 H HD23   . LEU   A 1 325 ? -21.48700 -5.59000  -36.77700 1.000 42.05000  ? 291 LEU   A HD23   1 
ATOM   4129 N N      . ASP   A 1 326 ? -21.41700 -2.27800  -40.40800 1.000 45.41000  ? 292 ASP   A N      1 
ATOM   4130 C CA     . ASP   A 1 326 ? -21.23200 -2.23600  -41.85300 1.000 44.00000  ? 292 ASP   A CA     1 
ATOM   4131 C C      . ASP   A 1 326 ? -19.76300 -2.36800  -42.23400 1.000 47.52000  ? 292 ASP   A C      1 
ATOM   4132 O O      . ASP   A 1 326 ? -19.40500 -3.14600  -43.12700 1.000 47.56000  ? 292 ASP   A O      1 
ATOM   4133 C CB     . ASP   A 1 326 ? -21.79600 -0.91700  -42.37600 1.000 61.65000  ? 292 ASP   A CB     1 
ATOM   4134 C CG     . ASP   A 1 326 ? -22.64600 -1.09300  -43.58800 1.000 73.04000  ? 292 ASP   A CG     1 
ATOM   4135 O OD1    . ASP   A 1 326 ? -22.29700 -1.94200  -44.43900 1.000 79.11000  ? 292 ASP   A OD1    1 
ATOM   4136 O OD2    . ASP   A 1 326 ? -23.66700 -0.37700  -43.68600 1.000 83.18000  ? 292 ASP   A OD2    1 
ATOM   4137 H H      . ASP   A 1 326 ? -21.76600 -1.56400  -40.08100 1.000 45.41000  ? 292 ASP   A H      1 
ATOM   4138 H HA     . ASP   A 1 326 ? -21.72300 -2.96600  -42.26300 1.000 44.00000  ? 292 ASP   A HA     1 
ATOM   4139 H HB2    . ASP   A 1 326 ? -22.34100 -0.50300  -41.69100 1.000 61.65000  ? 292 ASP   A HB2    1 
ATOM   4140 H HB3    . ASP   A 1 326 ? -21.05900 -0.33100  -42.61100 1.000 61.65000  ? 292 ASP   A HB3    1 
ATOM   4141 N N      . VAL   A 1 327 ? -18.89300 -1.59500  -41.58000 1.000 45.81000  ? 293 VAL   A N      1 
ATOM   4142 C CA     . VAL   A 1 327 ? -17.47000 -1.68800  -41.88600 1.000 40.39000  ? 293 VAL   A CA     1 
ATOM   4143 C C      . VAL   A 1 327 ? -16.94600 -3.07400  -41.54200 1.000 37.13000  ? 293 VAL   A C      1 
ATOM   4144 O O      . VAL   A 1 327 ? -16.17400 -3.66500  -42.30300 1.000 45.56000  ? 293 VAL   A O      1 
ATOM   4145 C CB     . VAL   A 1 327 ? -16.67700 -0.59400  -41.14100 1.000 45.80000  ? 293 VAL   A CB     1 
ATOM   4146 C CG1    . VAL   A 1 327 ? -15.20900 -0.70300  -41.49400 1.000 44.12000  ? 293 VAL   A CG1    1 
ATOM   4147 C CG2    . VAL   A 1 327 ? -17.18700 0.78000   -41.49600 1.000 44.25000  ? 293 VAL   A CG2    1 
ATOM   4148 H H      . VAL   A 1 327 ? -19.09700 -1.02400  -40.97000 1.000 45.81000  ? 293 VAL   A H      1 
ATOM   4149 H HA     . VAL   A 1 327 ? -17.34400 -1.55000  -42.83800 1.000 40.39000  ? 293 VAL   A HA     1 
ATOM   4150 H HB     . VAL   A 1 327 ? -16.77300 -0.72000  -40.18400 1.000 45.80000  ? 293 VAL   A HB     1 
ATOM   4151 H HG11   . VAL   A 1 327 ? -14.75600 0.10400   -41.20400 1.000 44.12000  ? 293 VAL   A HG11   1 
ATOM   4152 H HG12   . VAL   A 1 327 ? -14.82900 -1.47300  -41.04400 1.000 44.12000  ? 293 VAL   A HG12   1 
ATOM   4153 H HG13   . VAL   A 1 327 ? -15.12200 -0.80300  -42.45500 1.000 44.12000  ? 293 VAL   A HG13   1 
ATOM   4154 H HG21   . VAL   A 1 327 ? -16.66600 1.44300   -41.01600 1.000 44.25000  ? 293 VAL   A HG21   1 
ATOM   4155 H HG22   . VAL   A 1 327 ? -17.09200 0.91300   -42.45200 1.000 44.25000  ? 293 VAL   A HG22   1 
ATOM   4156 H HG23   . VAL   A 1 327 ? -18.12000 0.84900   -41.24400 1.000 44.25000  ? 293 VAL   A HG23   1 
ATOM   4157 N N      . MET   A 1 328 ? -17.35300 -3.61000  -40.38500 1.000 45.31000  ? 294 MET   A N      1 
ATOM   4158 C CA     . MET   A 1 328 ? -16.91700 -4.94500  -39.98200 1.000 45.13000  ? 294 MET   A CA     1 
ATOM   4159 C C      . MET   A 1 328 ? -17.38300 -6.00600  -40.97200 1.000 43.88000  ? 294 MET   A C      1 
ATOM   4160 O O      . MET   A 1 328 ? -16.61300 -6.89800  -41.34900 1.000 47.09000  ? 294 MET   A O      1 
ATOM   4161 C CB     . MET   A 1 328 ? -17.43500 -5.26000  -38.58000 1.000 46.93000  ? 294 MET   A CB     1 
ATOM   4162 C CG     . MET   A 1 328 ? -16.68300 -4.55100  -37.46100 1.000 39.37000  ? 294 MET   A CG     1 
ATOM   4163 S SD     . MET   A 1 328 ? -17.55500 -4.70500  -35.88900 1.000 45.66000  ? 294 MET   A SD     1 
ATOM   4164 C CE     . MET   A 1 328 ? -17.30200 -6.41700  -35.43300 1.000 37.33000  ? 294 MET   A CE     1 
ATOM   4165 H H      . MET   A 1 328 ? -17.87600 -3.22300  -39.82300 1.000 45.31000  ? 294 MET   A H      1 
ATOM   4166 H HA     . MET   A 1 328 ? -15.94800 -4.95800  -39.94800 1.000 45.13000  ? 294 MET   A HA     1 
ATOM   4167 H HB2    . MET   A 1 328 ? -18.36600 -4.99300  -38.52500 1.000 46.93000  ? 294 MET   A HB2    1 
ATOM   4168 H HB3    . MET   A 1 328 ? -17.35900 -6.21500  -38.42800 1.000 46.93000  ? 294 MET   A HB3    1 
ATOM   4169 H HG2    . MET   A 1 328 ? -15.80400 -4.94900  -37.36200 1.000 39.37000  ? 294 MET   A HG2    1 
ATOM   4170 H HG3    . MET   A 1 328 ? -16.60400 -3.60800  -37.67500 1.000 39.37000  ? 294 MET   A HG3    1 
ATOM   4171 H HE1    . MET   A 1 328 ? -17.74500 -6.58700  -34.58700 1.000 37.33000  ? 294 MET   A HE1    1 
ATOM   4172 H HE2    . MET   A 1 328 ? -17.67700 -6.98600  -36.12300 1.000 37.33000  ? 294 MET   A HE2    1 
ATOM   4173 H HE3    . MET   A 1 328 ? -16.35000 -6.58300  -35.34800 1.000 37.33000  ? 294 MET   A HE3    1 
ATOM   4174 N N      . ALA   A 1 329 ? -18.64100 -5.91900  -41.41100 1.000 44.52000  ? 295 ALA   A N      1 
ATOM   4175 C CA     . ALA   A 1 329 ? -19.14500 -6.85300  -42.41700 1.000 46.99000  ? 295 ALA   A CA     1 
ATOM   4176 C C      . ALA   A 1 329 ? -18.26700 -6.84200  -43.65900 1.000 46.09000  ? 295 ALA   A C      1 
ATOM   4177 O O      . ALA   A 1 329 ? -17.83700 -7.89700  -44.14200 1.000 52.52000  ? 295 ALA   A O      1 
ATOM   4178 C CB     . ALA   A 1 329 ? -20.59000 -6.50200  -42.77500 1.000 44.42000  ? 295 ALA   A CB     1 
ATOM   4179 H H      . ALA   A 1 329 ? -19.21500 -5.33600  -41.14600 1.000 44.52000  ? 295 ALA   A H      1 
ATOM   4180 H HA     . ALA   A 1 329 ? -19.13500 -7.75100  -42.04900 1.000 46.99000  ? 295 ALA   A HA     1 
ATOM   4181 H HB1    . ALA   A 1 329 ? -20.91100 -7.12900  -43.44200 1.000 44.42000  ? 295 ALA   A HB1    1 
ATOM   4182 H HB2    . ALA   A 1 329 ? -21.13600 -6.56100  -41.97600 1.000 44.42000  ? 295 ALA   A HB2    1 
ATOM   4183 H HB3    . ALA   A 1 329 ? -20.61700 -5.59900  -43.12900 1.000 44.42000  ? 295 ALA   A HB3    1 
ATOM   4184 N N      . LYS   A 1 330 ? -17.97600 -5.64700  -44.18100 1.000 46.52000  ? 296 LYS   A N      1 
ATOM   4185 C CA     . LYS   A 1 330 ? -17.17100 -5.53000  -45.39300 1.000 42.44000  ? 296 LYS   A CA     1 
ATOM   4186 C C      . LYS   A 1 330 ? -15.79300 -6.15400  -45.22300 1.000 54.09000  ? 296 LYS   A C      1 
ATOM   4187 O O      . LYS   A 1 330 ? -15.19600 -6.61900  -46.19800 1.000 52.30000  ? 296 LYS   A O      1 
ATOM   4188 C CB     . LYS   A 1 330 ? -17.04700 -4.05700  -45.78900 1.000 50.79000  ? 296 LYS   A CB     1 
ATOM   4189 C CG     . LYS   A 1 330 ? -16.17400 -3.81400  -47.00300 1.000 67.08000  ? 296 LYS   A CG     1 
ATOM   4190 H H      . LYS   A 1 330 ? -18.23200 -4.89500  -43.85200 1.000 46.52000  ? 296 LYS   A H      1 
ATOM   4191 H HA     . LYS   A 1 330 ? -17.62100 -5.99600  -46.11500 1.000 42.44000  ? 296 LYS   A HA     1 
ATOM   4192 H HB2    . LYS   A 1 330 ? -17.93200 -3.71200  -45.98700 1.000 50.79000  ? 296 LYS   A HB2    1 
ATOM   4193 H HB3    . LYS   A 1 330 ? -16.66300 -3.56600  -45.04600 1.000 50.79000  ? 296 LYS   A HB3    1 
ATOM   4194 N N      . LYS   A 1 331 ? -15.26900 -6.18300  -44.00600 1.000 48.68000  ? 297 LYS   A N      1 
ATOM   4195 C CA     . LYS   A 1 331 ? -13.94600 -6.74800  -43.78700 1.000 41.15000  ? 297 LYS   A CA     1 
ATOM   4196 C C      . LYS   A 1 331 ? -13.98800 -8.17300  -43.26500 1.000 48.80000  ? 297 LYS   A C      1 
ATOM   4197 O O      . LYS   A 1 331 ? -12.93200 -8.81000  -43.16000 1.000 48.76000  ? 297 LYS   A O      1 
ATOM   4198 C CB     . LYS   A 1 331 ? -13.15800 -5.86500  -42.81400 1.000 44.55000  ? 297 LYS   A CB     1 
ATOM   4199 C CG     . LYS   A 1 331 ? -12.83800 -4.52400  -43.41300 1.000 42.46000  ? 297 LYS   A CG     1 
ATOM   4200 C CD     . LYS   A 1 331 ? -12.51300 -3.49500  -42.35300 1.000 43.22000  ? 297 LYS   A CD     1 
ATOM   4201 C CE     . LYS   A 1 331 ? -11.91500 -2.25900  -43.00000 1.000 40.79000  ? 297 LYS   A CE     1 
ATOM   4202 N NZ     . LYS   A 1 331 ? -10.69600 -2.64600  -43.76700 1.000 42.48000  ? 297 LYS   A NZ     1 
ATOM   4203 H H      . LYS   A 1 331 ? -15.65400 -5.88500  -43.29700 1.000 48.68000  ? 297 LYS   A H      1 
ATOM   4204 H HA     . LYS   A 1 331 ? -13.46200 -6.75700  -44.62700 1.000 41.15000  ? 297 LYS   A HA     1 
ATOM   4205 H HB2    . LYS   A 1 331 ? -13.68700 -5.72100  -42.01400 1.000 44.55000  ? 297 LYS   A HB2    1 
ATOM   4206 H HB3    . LYS   A 1 331 ? -12.32300 -6.30400  -42.58900 1.000 44.55000  ? 297 LYS   A HB3    1 
ATOM   4207 H HG2    . LYS   A 1 331 ? -12.07400 -4.62600  -44.00000 1.000 42.46000  ? 297 LYS   A HG2    1 
ATOM   4208 H HG3    . LYS   A 1 331 ? -13.60500 -4.20700  -43.91500 1.000 42.46000  ? 297 LYS   A HG3    1 
ATOM   4209 H HD2    . LYS   A 1 331 ? -13.32500 -3.23900  -41.88900 1.000 43.22000  ? 297 LYS   A HD2    1 
ATOM   4210 H HD3    . LYS   A 1 331 ? -11.86600 -3.86200  -41.73100 1.000 43.22000  ? 297 LYS   A HD3    1 
ATOM   4211 H HE2    . LYS   A 1 331 ? -12.55700 -1.86800  -43.61300 1.000 40.79000  ? 297 LYS   A HE2    1 
ATOM   4212 H HE3    . LYS   A 1 331 ? -11.66200 -1.62100  -42.31500 1.000 40.79000  ? 297 LYS   A HE3    1 
ATOM   4213 H HZ1    . LYS   A 1 331 ? -10.19500 -1.92700  -43.92400 1.000 42.48000  ? 297 LYS   A HZ1    1 
ATOM   4214 H HZ2    . LYS   A 1 331 ? -10.21800 -3.23500  -43.30100 1.000 42.48000  ? 297 LYS   A HZ2    1 
ATOM   4215 H HZ3    . LYS   A 1 331 ? -10.92700 -3.01300  -44.54400 1.000 42.48000  ? 297 LYS   A HZ3    1 
ATOM   4216 N N      . GLY   A 1 332 ? -15.17400 -8.68200  -42.93700 1.000 46.16000  ? 298 GLY   A N      1 
ATOM   4217 C CA     . GLY   A 1 332 ? -15.29300 -10.03800 -42.45000 1.000 49.46000  ? 298 GLY   A CA     1 
ATOM   4218 C C      . GLY   A 1 332 ? -15.00900 -10.19500 -40.97700 1.000 55.11000  ? 298 GLY   A C      1 
ATOM   4219 O O      . GLY   A 1 332 ? -14.76400 -11.31600 -40.51800 1.000 52.92000  ? 298 GLY   A O      1 
ATOM   4220 H H      . GLY   A 1 332 ? -15.92100 -8.25900  -42.98900 1.000 46.16000  ? 298 GLY   A H      1 
ATOM   4221 H HA2    . GLY   A 1 332 ? -16.19400 -10.35700 -42.61800 1.000 49.46000  ? 298 GLY   A HA2    1 
ATOM   4222 H HA3    . GLY   A 1 332 ? -14.67600 -10.60600 -42.93800 1.000 49.46000  ? 298 GLY   A HA3    1 
ATOM   4223 N N      . TYR   A 1 333 ? -15.01700 -9.09900  -40.22100 1.000 44.42000  ? 299 TYR   A N      1 
ATOM   4224 C CA     . TYR   A 1 333 ? -14.81600 -9.16500  -38.78100 1.000 44.68000  ? 299 TYR   A CA     1 
ATOM   4225 C C      . TYR   A 1 333 ? -16.11100 -9.54200  -38.08400 1.000 47.78000  ? 299 TYR   A C      1 
ATOM   4226 O O      . TYR   A 1 333 ? -17.19000 -9.04800  -38.43100 1.000 44.87000  ? 299 TYR   A O      1 
ATOM   4227 C CB     . TYR   A 1 333 ? -14.32100 -7.81800  -38.24100 1.000 39.51000  ? 299 TYR   A CB     1 
ATOM   4228 C CG     . TYR   A 1 333 ? -12.88600 -7.49000  -38.57700 1.000 40.89000  ? 299 TYR   A CG     1 
ATOM   4229 C CD1    . TYR   A 1 333 ? -11.85800 -8.37200  -38.26200 1.000 43.97000  ? 299 TYR   A CD1    1 
ATOM   4230 C CD2    . TYR   A 1 333 ? -12.55400 -6.28100  -39.18600 1.000 42.49000  ? 299 TYR   A CD2    1 
ATOM   4231 C CE1    . TYR   A 1 333 ? -10.53800 -8.06800  -38.54900 1.000 43.56000  ? 299 TYR   A CE1    1 
ATOM   4232 C CE2    . TYR   A 1 333 ? -11.24100 -5.97100  -39.48400 1.000 38.32000  ? 299 TYR   A CE2    1 
ATOM   4233 C CZ     . TYR   A 1 333 ? -10.23700 -6.86000  -39.16400 1.000 40.42000  ? 299 TYR   A CZ     1 
ATOM   4234 O OH     . TYR   A 1 333 ? -8.93400  -6.54800  -39.46300 1.000 47.58000  ? 299 TYR   A OH     1 
ATOM   4235 H H      . TYR   A 1 333 ? -15.13800 -8.30200  -40.52100 1.000 44.42000  ? 299 TYR   A H      1 
ATOM   4236 H HA     . TYR   A 1 333 ? -14.15300 -9.84300  -38.57800 1.000 44.68000  ? 299 TYR   A HA     1 
ATOM   4237 H HB2    . TYR   A 1 333 ? -14.87700 -7.11400  -38.61000 1.000 39.51000  ? 299 TYR   A HB2    1 
ATOM   4238 H HB3    . TYR   A 1 333 ? -14.40200 -7.82400  -37.27400 1.000 39.51000  ? 299 TYR   A HB3    1 
ATOM   4239 H HD1    . TYR   A 1 333 ? -12.06100 -9.18000  -37.84800 1.000 43.97000  ? 299 TYR   A HD1    1 
ATOM   4240 H HD2    . TYR   A 1 333 ? -13.22700 -5.67700  -39.40200 1.000 42.49000  ? 299 TYR   A HD2    1 
ATOM   4241 H HE1    . TYR   A 1 333 ? -9.86100  -8.66900  -38.33800 1.000 43.56000  ? 299 TYR   A HE1    1 
ATOM   4242 H HE2    . TYR   A 1 333 ? -11.03400 -5.16200  -39.89400 1.000 38.32000  ? 299 TYR   A HE2    1 
ATOM   4243 H HH     . TYR   A 1 333 ? -8.89400  -5.78400  -39.80800 1.000 47.58000  ? 299 TYR   A HH     1 
ATOM   4244 N N      . LYS   A 1 334 ? -15.99800 -10.40400 -37.07300 1.000 42.92000  ? 300 LYS   A N      1 
ATOM   4245 C CA     . LYS   A 1 334 ? -17.15000 -10.81600 -36.28800 1.000 44.19000  ? 300 LYS   A CA     1 
ATOM   4246 C C      . LYS   A 1 334 ? -17.17400 -10.23300 -34.88300 1.000 47.22000  ? 300 LYS   A C      1 
ATOM   4247 O O      . LYS   A 1 334 ? -18.25000 -10.16600 -34.28300 1.000 40.58000  ? 300 LYS   A O      1 
ATOM   4248 C CB     . LYS   A 1 334 ? -17.20700 -12.35200 -36.21600 1.000 50.52000  ? 300 LYS   A CB     1 
ATOM   4249 C CG     . LYS   A 1 334 ? -17.10300 -12.99500 -37.60200 1.000 50.10000  ? 300 LYS   A CG     1 
ATOM   4250 C CD     . LYS   A 1 334 ? -18.07000 -14.14800 -37.77600 1.000 71.26000  ? 300 LYS   A CD     1 
ATOM   4251 C CE     . LYS   A 1 334 ? -17.55400 -15.41700 -37.11600 1.000 66.14000  ? 300 LYS   A CE     1 
ATOM   4252 N NZ     . LYS   A 1 334 ? -17.55600 -16.55900 -38.07300 1.000 71.88000  ? 300 LYS   A NZ     1 
ATOM   4253 H H      . LYS   A 1 334 ? -15.25800 -10.76400 -36.82400 1.000 42.92000  ? 300 LYS   A H      1 
ATOM   4254 H HA     . LYS   A 1 334 ? -17.95600 -10.51800 -36.73800 1.000 44.19000  ? 300 LYS   A HA     1 
ATOM   4255 H HB2    . LYS   A 1 334 ? -16.46600 -12.67200 -35.67900 1.000 50.52000  ? 300 LYS   A HB2    1 
ATOM   4256 H HB3    . LYS   A 1 334 ? -18.04900 -12.62000 -35.81600 1.000 50.52000  ? 300 LYS   A HB3    1 
ATOM   4257 H HG2    . LYS   A 1 334 ? -17.31000 -12.32800 -38.27500 1.000 50.10000  ? 300 LYS   A HG2    1 
ATOM   4258 H HG3    . LYS   A 1 334 ? -16.20200 -13.32800 -37.73300 1.000 50.10000  ? 300 LYS   A HG3    1 
ATOM   4259 H HD2    . LYS   A 1 334 ? -18.92300 -13.92000 -37.37400 1.000 71.26000  ? 300 LYS   A HD2    1 
ATOM   4260 H HD3    . LYS   A 1 334 ? -18.18500 -14.32600 -38.72300 1.000 71.26000  ? 300 LYS   A HD3    1 
ATOM   4261 H HE2    . LYS   A 1 334 ? -16.65300 -15.27500 -36.80400 1.000 66.14000  ? 300 LYS   A HE2    1 
ATOM   4262 H HE3    . LYS   A 1 334 ? -18.13200 -15.64600 -36.37200 1.000 66.14000  ? 300 LYS   A HE3    1 
ATOM   4263 H HZ1    . LYS   A 1 334 ? -17.25200 -17.29300 -37.67100 1.000 71.88000  ? 300 LYS   A HZ1    1 
ATOM   4264 H HZ2    . LYS   A 1 334 ? -18.38300 -16.71000 -38.36400 1.000 71.88000  ? 300 LYS   A HZ2    1 
ATOM   4265 H HZ3    . LYS   A 1 334 ? -17.03400 -16.37300 -38.76900 1.000 71.88000  ? 300 LYS   A HZ3    1 
ATOM   4266 N N      . ALA   A 1 335 ? -16.03300 -9.79300  -34.35200 1.000 36.71000  ? 301 ALA   A N      1 
ATOM   4267 C CA     . ALA   A 1 335 ? -15.99400 -9.19700  -33.02700 1.000 39.33000  ? 301 ALA   A CA     1 
ATOM   4268 C C      . ALA   A 1 335 ? -14.91100 -8.12700  -32.99600 1.000 35.74000  ? 301 ALA   A C      1 
ATOM   4269 O O      . ALA   A 1 335 ? -13.91100 -8.21400  -33.70900 1.000 38.09000  ? 301 ALA   A O      1 
ATOM   4270 C CB     . ALA   A 1 335 ? -15.72700 -10.24200 -31.93100 1.000 36.52000  ? 301 ALA   A CB     1 
ATOM   4271 H H      . ALA   A 1 335 ? -15.26800 -9.83000  -34.74300 1.000 36.71000  ? 301 ALA   A H      1 
ATOM   4272 H HA     . ALA   A 1 335 ? -16.84600 -8.77200  -32.84100 1.000 39.33000  ? 301 ALA   A HA     1 
ATOM   4273 H HB1    . ALA   A 1 335 ? -15.71000 -9.79800  -31.06900 1.000 36.52000  ? 301 ALA   A HB1    1 
ATOM   4274 H HB2    . ALA   A 1 335 ? -16.43500 -10.90500 -31.94800 1.000 36.52000  ? 301 ALA   A HB2    1 
ATOM   4275 H HB3    . ALA   A 1 335 ? -14.87200 -10.66600 -32.10200 1.000 36.52000  ? 301 ALA   A HB3    1 
ATOM   4276 N N      . LEU   A 1 336 ? -15.10500 -7.14200  -32.12600 1.000 33.41000  ? 302 LEU   A N      1 
ATOM   4277 C CA     . LEU   A 1 336 ? -14.11100 -6.08000  -31.97800 1.000 36.68000  ? 302 LEU   A CA     1 
ATOM   4278 C C      . LEU   A 1 336 ? -12.75900 -6.61700  -31.51200 1.000 47.59000  ? 302 LEU   A C      1 
ATOM   4279 O O      . LEU   A 1 336 ? -11.71700 -6.08000  -31.90600 1.000 40.54000  ? 302 LEU   A O      1 
ATOM   4280 C CB     . LEU   A 1 336 ? -14.64000 -5.02300  -31.00100 1.000 35.49000  ? 302 LEU   A CB     1 
ATOM   4281 C CG     . LEU   A 1 336 ? -15.95300 -4.39100  -31.46200 1.000 38.47000  ? 302 LEU   A CG     1 
ATOM   4282 C CD1    . LEU   A 1 336 ? -16.58000 -3.52700  -30.38700 1.000 36.25000  ? 302 LEU   A CD1    1 
ATOM   4283 C CD2    . LEU   A 1 336 ? -15.73600 -3.59900  -32.75800 1.000 44.21000  ? 302 LEU   A CD2    1 
ATOM   4284 H H      . LEU   A 1 336 ? -15.79200 -7.06500  -31.61500 1.000 33.41000  ? 302 LEU   A H      1 
ATOM   4285 H HA     . LEU   A 1 336 ? -13.97600 -5.65500  -32.83900 1.000 36.68000  ? 302 LEU   A HA     1 
ATOM   4286 H HB2    . LEU   A 1 336 ? -14.79500 -5.44000  -30.13900 1.000 35.49000  ? 302 LEU   A HB2    1 
ATOM   4287 H HB3    . LEU   A 1 336 ? -13.98200 -4.31600  -30.91400 1.000 35.49000  ? 302 LEU   A HB3    1 
ATOM   4288 H HG     . LEU   A 1 336 ? -16.58300 -5.10100  -31.66100 1.000 38.47000  ? 302 LEU   A HG     1 
ATOM   4289 H HD11   . LEU   A 1 336 ? -17.37700 -3.10600  -30.74600 1.000 36.25000  ? 302 LEU   A HD11   1 
ATOM   4290 H HD12   . LEU   A 1 336 ? -16.81300 -4.08700  -29.63000 1.000 36.25000  ? 302 LEU   A HD12   1 
ATOM   4291 H HD13   . LEU   A 1 336 ? -15.94200 -2.84900  -30.11500 1.000 36.25000  ? 302 LEU   A HD13   1 
ATOM   4292 H HD21   . LEU   A 1 336 ? -16.52600 -3.06500  -32.93700 1.000 44.21000  ? 302 LEU   A HD21   1 
ATOM   4293 H HD22   . LEU   A 1 336 ? -14.96400 -3.02200  -32.64900 1.000 44.21000  ? 302 LEU   A HD22   1 
ATOM   4294 H HD23   . LEU   A 1 336 ? -15.58500 -4.22000  -33.48800 1.000 44.21000  ? 302 LEU   A HD23   1 
ATOM   4295 N N      . ASP   A 1 337 ? -12.74600 -7.66800  -30.67000 1.000 38.39000  ? 303 ASP   A N      1 
ATOM   4296 C CA     . ASP   A 1 337 ? -11.48400 -8.25500  -30.21100 1.000 40.70000  ? 303 ASP   A CA     1 
ATOM   4297 C C      . ASP   A 1 337 ? -10.60700 -8.70500  -31.36500 1.000 40.47000  ? 303 ASP   A C      1 
ATOM   4298 O O      . ASP   A 1 337 ? -9.42200  -8.98400  -31.14900 1.000 44.51000  ? 303 ASP   A O      1 
ATOM   4299 C CB     . ASP   A 1 337 ? -11.71900 -9.48500  -29.30300 1.000 35.68000  ? 303 ASP   A CB     1 
ATOM   4300 C CG     . ASP   A 1 337 ? -12.05600 -9.12900  -27.83700 1.000 49.87000  ? 303 ASP   A CG     1 
ATOM   4301 O OD1    . ASP   A 1 337 ? -11.97000 -7.95200  -27.43200 1.000 47.71000  ? 303 ASP   A OD1    1 
ATOM   4302 O OD2    . ASP   A 1 337 ? -12.41600 -10.06300 -27.07000 1.000 50.25000  ? 303 ASP   A OD2    1 
ATOM   4303 H H      . ASP   A 1 337 ? -13.44900 -8.05100  -30.35700 1.000 38.39000  ? 303 ASP   A H      1 
ATOM   4304 H HA     . ASP   A 1 337 ? -10.99300 -7.59200  -29.70100 1.000 40.70000  ? 303 ASP   A HA     1 
ATOM   4305 H HB2    . ASP   A 1 337 ? -12.46000 -9.99900  -29.66000 1.000 35.68000  ? 303 ASP   A HB2    1 
ATOM   4306 H HB3    . ASP   A 1 337 ? -10.91500 -10.02700 -29.29800 1.000 35.68000  ? 303 ASP   A HB3    1 
ATOM   4307 N N      . GLU   A 1 338 ? -11.16800 -8.86000  -32.57200 1.000 40.59000  ? 304 GLU   A N      1 
ATOM   4308 C CA     . GLU   A 1 338 ? -10.36300 -9.32300  -33.69500 1.000 32.87000  ? 304 GLU   A CA     1 
ATOM   4309 C C      . GLU   A 1 338 ? -9.44500  -8.24700  -34.25800 1.000 44.91000  ? 304 GLU   A C      1 
ATOM   4310 O O      . GLU   A 1 338 ? -8.45900  -8.57800  -34.92400 1.000 45.16000  ? 304 GLU   A O      1 
ATOM   4311 C CB     . GLU   A 1 338 ? -11.24100 -9.84100  -34.82000 1.000 46.15000  ? 304 GLU   A CB     1 
ATOM   4312 C CG     . GLU   A 1 338 ? -11.70200 -11.25200 -34.58000 1.000 45.08000  ? 304 GLU   A CG     1 
ATOM   4313 C CD     . GLU   A 1 338 ? -12.59100 -11.73900 -35.68000 1.000 45.60000  ? 304 GLU   A CD     1 
ATOM   4314 O OE1    . GLU   A 1 338 ? -13.64800 -11.11200 -35.89600 1.000 51.93000  ? 304 GLU   A OE1    1 
ATOM   4315 O OE2    . GLU   A 1 338 ? -12.22900 -12.74100 -36.33200 1.000 58.90000  ? 304 GLU   A OE2    1 
ATOM   4316 H H      . GLU   A 1 338 ? -11.99400 -8.70900  -32.75900 1.000 40.59000  ? 304 GLU   A H      1 
ATOM   4317 H HA     . GLU   A 1 338 ? -9.80500  -10.05800 -33.39400 1.000 32.87000  ? 304 GLU   A HA     1 
ATOM   4318 H HB2    . GLU   A 1 338 ? -12.02500 -9.27600  -34.89700 1.000 46.15000  ? 304 GLU   A HB2    1 
ATOM   4319 H HB3    . GLU   A 1 338 ? -10.73700 -9.82600  -35.64800 1.000 46.15000  ? 304 GLU   A HB3    1 
ATOM   4320 H HG2    . GLU   A 1 338 ? -10.92900 -11.83700 -34.53300 1.000 45.08000  ? 304 GLU   A HG2    1 
ATOM   4321 H HG3    . GLU   A 1 338 ? -12.20100 -11.28800 -33.74900 1.000 45.08000  ? 304 GLU   A HG3    1 
ATOM   4322 N N      . PHE   A 1 339 ? -9.74800  -6.97200  -34.04300 1.000 40.66000  ? 305 PHE   A N      1 
ATOM   4323 C CA     . PHE   A 1 339 ? -8.90500  -5.92500  -34.61600 1.000 41.43000  ? 305 PHE   A CA     1 
ATOM   4324 C C      . PHE   A 1 339 ? -8.57200  -4.79400  -33.64700 1.000 34.03000  ? 305 PHE   A C      1 
ATOM   4325 O O      . PHE   A 1 339 ? -7.80600  -3.89700  -34.02300 1.000 36.91000  ? 305 PHE   A O      1 
ATOM   4326 C CB     . PHE   A 1 339 ? -9.55200  -5.35700  -35.89400 1.000 36.38000  ? 305 PHE   A CB     1 
ATOM   4327 C CG     . PHE   A 1 339 ? -10.89300 -4.71100  -35.67600 1.000 38.22000  ? 305 PHE   A CG     1 
ATOM   4328 C CD1    . PHE   A 1 339 ? -12.06000 -5.46500  -35.73700 1.000 38.65000  ? 305 PHE   A CD1    1 
ATOM   4329 C CD2    . PHE   A 1 339 ? -10.99600 -3.34200  -35.47400 1.000 37.68000  ? 305 PHE   A CD2    1 
ATOM   4330 C CE1    . PHE   A 1 339 ? -13.29300 -4.87400  -35.55200 1.000 35.37000  ? 305 PHE   A CE1    1 
ATOM   4331 C CE2    . PHE   A 1 339 ? -12.23200 -2.74700  -35.28600 1.000 37.60000  ? 305 PHE   A CE2    1 
ATOM   4332 C CZ     . PHE   A 1 339 ? -13.38500 -3.51000  -35.32300 1.000 38.50000  ? 305 PHE   A CZ     1 
ATOM   4333 H H      . PHE   A 1 339 ? -10.41700 -6.69000  -33.58200 1.000 40.66000  ? 305 PHE   A H      1 
ATOM   4334 H HA     . PHE   A 1 339 ? -8.06300  -6.31900  -34.88400 1.000 41.43000  ? 305 PHE   A HA     1 
ATOM   4335 H HB2    . PHE   A 1 339 ? -8.96000  -4.68800  -36.27100 1.000 36.38000  ? 305 PHE   A HB2    1 
ATOM   4336 H HB3    . PHE   A 1 339 ? -9.67300  -6.08100  -36.52800 1.000 36.38000  ? 305 PHE   A HB3    1 
ATOM   4337 H HD1    . PHE   A 1 339 ? -12.00700 -6.38200  -35.88000 1.000 38.65000  ? 305 PHE   A HD1    1 
ATOM   4338 H HD2    . PHE   A 1 339 ? -10.22500 -2.82300  -35.43800 1.000 37.68000  ? 305 PHE   A HD2    1 
ATOM   4339 H HE1    . PHE   A 1 339 ? -14.06500 -5.39200  -35.58000 1.000 35.37000  ? 305 PHE   A HE1    1 
ATOM   4340 H HE2    . PHE   A 1 339 ? -12.28700 -1.83100  -35.13700 1.000 37.60000  ? 305 PHE   A HE2    1 
ATOM   4341 H HZ     . PHE   A 1 339 ? -14.21600 -3.11000  -35.20400 1.000 38.50000  ? 305 PHE   A HZ     1 
ATOM   4342 N N      . ARG   A 1 340 ? -9.10200  -4.80800  -32.41900 1.000 30.40000  ? 306 ARG   A N      1 
ATOM   4343 C CA     . ARG   A 1 340 ? -8.74600  -3.76500  -31.46400 1.000 35.28000  ? 306 ARG   A CA     1 
ATOM   4344 C C      . ARG   A 1 340 ? -7.23300  -3.72400  -31.30300 1.000 40.04000  ? 306 ARG   A C      1 
ATOM   4345 O O      . ARG   A 1 340 ? -6.59400  -4.75300  -31.04100 1.000 36.06000  ? 306 ARG   A O      1 
ATOM   4346 C CB     . ARG   A 1 340 ? -9.41800  -3.98700  -30.10900 1.000 35.57000  ? 306 ARG   A CB     1 
ATOM   4347 C CG     . ARG   A 1 340 ? -9.03700  -2.92000  -29.09000 1.000 34.36000  ? 306 ARG   A CG     1 
ATOM   4348 C CD     . ARG   A 1 340 ? -9.77900  -3.05900  -27.77600 1.000 32.12000  ? 306 ARG   A CD     1 
ATOM   4349 N NE     . ARG   A 1 340 ? -11.22100 -3.17900  -27.96000 1.000 43.06000  ? 306 ARG   A NE     1 
ATOM   4350 C CZ     . ARG   A 1 340 ? -11.88800 -4.32700  -27.86200 1.000 49.73000  ? 306 ARG   A CZ     1 
ATOM   4351 N NH1    . ARG   A 1 340 ? -11.26800 -5.46700  -27.60900 1.000 50.21000  ? 306 ARG   A NH1    1 
ATOM   4352 N NH2    . ARG   A 1 340 ? -13.20800 -4.32900  -28.02400 1.000 46.58000  ? 306 ARG   A NH2    1 
ATOM   4353 H H      . ARG   A 1 340 ? -9.65600  -5.39600  -32.12400 1.000 30.40000  ? 306 ARG   A H      1 
ATOM   4354 H HA     . ARG   A 1 340 ? -9.03900  -2.90900  -31.81000 1.000 35.28000  ? 306 ARG   A HA     1 
ATOM   4355 H HB2    . ARG   A 1 340 ? -10.38000 -3.96400  -30.22900 1.000 35.57000  ? 306 ARG   A HB2    1 
ATOM   4356 H HB3    . ARG   A 1 340 ? -9.14700  -4.85000  -29.75800 1.000 35.57000  ? 306 ARG   A HB3    1 
ATOM   4357 H HG2    . ARG   A 1 340 ? -8.08800  -2.98500  -28.89900 1.000 34.36000  ? 306 ARG   A HG2    1 
ATOM   4358 H HG3    . ARG   A 1 340 ? -9.24100  -2.04600  -29.45800 1.000 34.36000  ? 306 ARG   A HG3    1 
ATOM   4359 H HD2    . ARG   A 1 340 ? -9.44600  -3.83400  -27.30000 1.000 32.12000  ? 306 ARG   A HD2    1 
ATOM   4360 H HD3    . ARG   A 1 340 ? -9.61900  -2.26200  -27.24700 1.000 32.12000  ? 306 ARG   A HD3    1 
ATOM   4361 H HE     . ARG   A 1 340 ? -11.64800 -2.48900  -28.24500 1.000 43.06000  ? 306 ARG   A HE     1 
ATOM   4362 H HH11   . ARG   A 1 340 ? -10.41700 -5.49000  -27.50200 1.000 50.21000  ? 306 ARG   A HH11   1 
ATOM   4363 H HH12   . ARG   A 1 340 ? -11.72300 -6.19500  -27.55200 1.000 50.21000  ? 306 ARG   A HH12   1 
ATOM   4364 H HH21   . ARG   A 1 340 ? -13.62200 -3.59400  -28.18900 1.000 46.58000  ? 306 ARG   A HH21   1 
ATOM   4365 H HH22   . ARG   A 1 340 ? -13.64700 -5.06600  -27.96400 1.000 46.58000  ? 306 ARG   A HH22   1 
ATOM   4366 N N      . GLY   A 1 341 ? -6.66000  -2.54000  -31.51700 1.000 38.85000  ? 307 GLY   A N      1 
ATOM   4367 C CA     . GLY   A 1 341 ? -5.22900  -2.31100  -31.39700 1.000 34.01000  ? 307 GLY   A CA     1 
ATOM   4368 C C      . GLY   A 1 341 ? -4.37200  -2.83800  -32.52300 1.000 38.17000  ? 307 GLY   A C      1 
ATOM   4369 O O      . GLY   A 1 341 ? -3.14200  -2.75000  -32.43500 1.000 38.18000  ? 307 GLY   A O      1 
ATOM   4370 H H      . GLY   A 1 341 ? -7.09800  -1.83400  -31.74000 1.000 38.85000  ? 307 GLY   A H      1 
ATOM   4371 H HA2    . GLY   A 1 341 ? -5.07200  -1.35600  -31.32900 1.000 34.01000  ? 307 GLY   A HA2    1 
ATOM   4372 H HA3    . GLY   A 1 341 ? -4.91800  -2.72100  -30.57500 1.000 34.01000  ? 307 GLY   A HA3    1 
ATOM   4373 N N      . LYS   A 1 342 ? -4.96800  -3.39300  -33.58500 1.000 31.64000  ? 308 LYS   A N      1 
ATOM   4374 C CA     . LYS   A 1 342 ? -4.20800  -4.03900  -34.64300 1.000 39.96000  ? 308 LYS   A CA     1 
ATOM   4375 C C      . LYS   A 1 342 ? -3.87700  -3.10700  -35.80200 1.000 36.17000  ? 308 LYS   A C      1 
ATOM   4376 O O      . LYS   A 1 342 ? -3.71400  -3.57100  -36.94400 1.000 40.75000  ? 308 LYS   A O      1 
ATOM   4377 C CB     . LYS   A 1 342 ? -4.96000  -5.27700  -35.14300 1.000 36.63000  ? 308 LYS   A CB     1 
ATOM   4378 C CG     . LYS   A 1 342 ? -5.22800  -6.29400  -34.03500 1.000 54.29000  ? 308 LYS   A CG     1 
ATOM   4379 C CD     . LYS   A 1 342 ? -4.16200  -7.38700  -33.98700 1.000 72.28000  ? 308 LYS   A CD     1 
ATOM   4380 H H      . LYS   A 1 342 ? -5.81900  -3.40500  -33.71100 1.000 31.64000  ? 308 LYS   A H      1 
ATOM   4381 H HA     . LYS   A 1 342 ? -3.36600  -4.34500  -34.27100 1.000 39.96000  ? 308 LYS   A HA     1 
ATOM   4382 H HB2    . LYS   A 1 342 ? -5.81400  -5.00100  -35.51000 1.000 36.63000  ? 308 LYS   A HB2    1 
ATOM   4383 H HB3    . LYS   A 1 342 ? -4.43000  -5.71300  -35.82800 1.000 36.63000  ? 308 LYS   A HB3    1 
ATOM   4384 H HG2    . LYS   A 1 342 ? -5.23600  -5.84500  -33.17600 1.000 54.29000  ? 308 LYS   A HG2    1 
ATOM   4385 H HG3    . LYS   A 1 342 ? -6.08200  -6.72200  -34.19400 1.000 54.29000  ? 308 LYS   A HG3    1 
ATOM   4386 N N      . VAL   A 1 343 ? -3.76700  -1.80300  -35.55200 1.000 39.04000  ? 309 VAL   A N      1 
ATOM   4387 C CA     . VAL   A 1 343 ? -3.29200  -0.91200  -36.60200 1.000 36.27000  ? 309 VAL   A CA     1 
ATOM   4388 C C      . VAL   A 1 343 ? -1.94300  -1.42100  -37.09800 1.000 40.35000  ? 309 VAL   A C      1 
ATOM   4389 O O      . VAL   A 1 343 ? -1.09200  -1.85000  -36.31000 1.000 41.64000  ? 309 VAL   A O      1 
ATOM   4390 C CB     . VAL   A 1 343 ? -3.21600  0.53700   -36.08300 1.000 39.34000  ? 309 VAL   A CB     1 
ATOM   4391 C CG1    . VAL   A 1 343 ? -2.46200  0.60000   -34.76500 1.000 35.08000  ? 309 VAL   A CG1    1 
ATOM   4392 C CG2    . VAL   A 1 343 ? -2.55900  1.43300   -37.12100 1.000 39.43000  ? 309 VAL   A CG2    1 
ATOM   4393 H H      . VAL   A 1 343 ? -3.96100  -1.42300  -34.80600 1.000 39.04000  ? 309 VAL   A H      1 
ATOM   4394 H HA     . VAL   A 1 343 ? -3.91500  -0.93400  -37.34500 1.000 36.27000  ? 309 VAL   A HA     1 
ATOM   4395 H HB     . VAL   A 1 343 ? -4.11600  0.86500   -35.93000 1.000 39.34000  ? 309 VAL   A HB     1 
ATOM   4396 H HG11   . VAL   A 1 343 ? -2.25200  1.52700   -34.57000 1.000 35.08000  ? 309 VAL   A HG11   1 
ATOM   4397 H HG12   . VAL   A 1 343 ? -3.01900  0.23400   -34.06100 1.000 35.08000  ? 309 VAL   A HG12   1 
ATOM   4398 H HG13   . VAL   A 1 343 ? -1.64300  0.08700   -34.84200 1.000 35.08000  ? 309 VAL   A HG13   1 
ATOM   4399 H HG21   . VAL   A 1 343 ? -2.70800  2.35900   -36.87400 1.000 39.43000  ? 309 VAL   A HG21   1 
ATOM   4400 H HG22   . VAL   A 1 343 ? -1.60700  1.24800   -37.14600 1.000 39.43000  ? 309 VAL   A HG22   1 
ATOM   4401 H HG23   . VAL   A 1 343 ? -2.95600  1.25500   -37.98800 1.000 39.43000  ? 309 VAL   A HG23   1 
ATOM   4402 N N      . LYS   A 1 344 ? -1.75500  -1.41600  -38.41600 1.000 38.48000  ? 310 LYS   A N      1 
ATOM   4403 C CA     . LYS   A 1 344 ? -0.53200  -1.92400  -39.02400 1.000 48.11000  ? 310 LYS   A CA     1 
ATOM   4404 C C      . LYS   A 1 344 ? 0.44600   -0.79900  -39.35200 1.000 53.93000  ? 310 LYS   A C      1 
ATOM   4405 O O      . LYS   A 1 344 ? 0.04800   0.30700   -39.72300 1.000 44.43000  ? 310 LYS   A O      1 
ATOM   4406 C CB     . LYS   A 1 344 ? -0.83700  -2.69200  -40.31300 1.000 44.69000  ? 310 LYS   A CB     1 
ATOM   4407 C CG     . LYS   A 1 344 ? -1.90700  -3.76000  -40.17900 1.000 52.32000  ? 310 LYS   A CG     1 
ATOM   4408 C CD     . LYS   A 1 344 ? -2.11400  -4.49700  -41.49200 1.000 63.57000  ? 310 LYS   A CD     1 
ATOM   4409 C CE     . LYS   A 1 344 ? -3.45200  -5.22200  -41.51100 1.000 63.72000  ? 310 LYS   A CE     1 
ATOM   4410 N NZ     . LYS   A 1 344 ? -3.95400  -5.40400  -42.90400 1.000 78.39000  ? 310 LYS   A NZ     1 
ATOM   4411 H H      . LYS   A 1 344 ? -2.32900  -1.12000  -38.98400 1.000 38.48000  ? 310 LYS   A H      1 
ATOM   4412 H HA     . LYS   A 1 344 ? -0.09600  -2.53300  -38.40700 1.000 48.11000  ? 310 LYS   A HA     1 
ATOM   4413 H HB2    . LYS   A 1 344 ? -1.13900  -2.06300  -40.98500 1.000 44.69000  ? 310 LYS   A HB2    1 
ATOM   4414 H HB3    . LYS   A 1 344 ? -0.02400  -3.12700  -40.61500 1.000 44.69000  ? 310 LYS   A HB3    1 
ATOM   4415 H HG2    . LYS   A 1 344 ? -1.63500  -4.40500  -39.50700 1.000 52.32000  ? 310 LYS   A HG2    1 
ATOM   4416 H HG3    . LYS   A 1 344 ? -2.74500  -3.34200  -39.92500 1.000 52.32000  ? 310 LYS   A HG3    1 
ATOM   4417 H HD2    . LYS   A 1 344 ? -2.10200  -3.86000  -42.22300 1.000 63.57000  ? 310 LYS   A HD2    1 
ATOM   4418 H HD3    . LYS   A 1 344 ? -1.41000  -5.15400  -41.60600 1.000 63.57000  ? 310 LYS   A HD3    1 
ATOM   4419 H HE2    . LYS   A 1 344 ? -3.34600  -6.09900  -41.10900 1.000 63.72000  ? 310 LYS   A HE2    1 
ATOM   4420 H HE3    . LYS   A 1 344 ? -4.10800  -4.70400  -41.01900 1.000 63.72000  ? 310 LYS   A HE3    1 
ATOM   4421 H HZ1    . LYS   A 1 344 ? -4.73600  -5.82900  -42.89200 1.000 78.39000  ? 310 LYS   A HZ1    1 
ATOM   4422 H HZ2    . LYS   A 1 344 ? -4.06200  -4.61100  -43.29400 1.000 78.39000  ? 310 LYS   A HZ2    1 
ATOM   4423 H HZ3    . LYS   A 1 344 ? -3.37100  -5.88300  -43.37700 1.000 78.39000  ? 310 LYS   A HZ3    1 
ATOM   4424 N N      . ALA   A 1 345 ? 1.73500   -1.10100  -39.21800 1.000 70.46000  ? 311 ALA   A N      1 
ATOM   4425 C CA     . ALA   A 1 345 ? 2.75500   -0.34200  -39.92700 1.000 68.07000  ? 311 ALA   A CA     1 
ATOM   4426 C C      . ALA   A 1 345 ? 2.69300   -0.71000  -41.40700 1.000 74.65000  ? 311 ALA   A C      1 
ATOM   4427 O O      . ALA   A 1 345 ? 2.40800   -1.85700  -41.76400 1.000 87.14000  ? 311 ALA   A O      1 
ATOM   4428 C CB     . ALA   A 1 345 ? 4.14000   -0.63500  -39.35000 1.000 60.64000  ? 311 ALA   A CB     1 
ATOM   4429 H H      . ALA   A 1 345 ? 2.04100   -1.73600  -38.72600 1.000 70.46000  ? 311 ALA   A H      1 
ATOM   4430 H HA     . ALA   A 1 345 ? 2.57700   0.60700   -39.83600 1.000 68.07000  ? 311 ALA   A HA     1 
ATOM   4431 H HB1    . ALA   A 1 345 ? 4.80100   -0.11900  -39.83800 1.000 60.64000  ? 311 ALA   A HB1    1 
ATOM   4432 H HB2    . ALA   A 1 345 ? 4.15000   -0.38500  -38.41300 1.000 60.64000  ? 311 ALA   A HB2    1 
ATOM   4433 H HB3    . ALA   A 1 345 ? 4.32600   -1.58300  -39.44200 1.000 60.64000  ? 311 ALA   A HB3    1 
ATOM   4434 N N      . MET   A 1 346 ? 2.93200   0.26800   -42.27300 1.000 80.65000  ? 312 MET   A N      1 
ATOM   4435 C CA     . MET   A 1 346 ? 2.73200   0.06000   -43.70900 1.000 84.92000  ? 312 MET   A CA     1 
ATOM   4436 C C      . MET   A 1 346 ? 3.93300   -0.59700  -44.39300 1.000 83.66000  ? 312 MET   A C      1 
ATOM   4437 O O      . MET   A 1 346 ? 3.82000   -1.12200  -45.50400 1.000 84.91000  ? 312 MET   A O      1 
ATOM   4438 C CB     . MET   A 1 346 ? 2.42200   1.39000   -44.37500 1.000 71.00000  ? 312 MET   A CB     1 
ATOM   4439 C CG     . MET   A 1 346 ? 3.42600   2.45100   -44.01200 1.000 68.13000  ? 312 MET   A CG     1 
ATOM   4440 S SD     . MET   A 1 346 ? 3.07700   3.97900   -44.88100 1.000 87.01000  ? 312 MET   A SD     1 
ATOM   4441 C CE     . MET   A 1 346 ? 2.18000   3.36400   -46.29800 1.000 75.73000  ? 312 MET   A CE     1 
ATOM   4442 H H      . MET   A 1 346 ? 3.21100   1.04600   -42.04900 1.000 80.65000  ? 312 MET   A H      1 
ATOM   4443 H HA     . MET   A 1 346 ? 1.95900   -0.51300  -43.83100 1.000 84.92000  ? 312 MET   A HA     1 
ATOM   4444 H HB2    . MET   A 1 346 ? 2.46600   1.20500   -45.32100 1.000 71.00000  ? 312 MET   A HB2    1 
ATOM   4445 H HB3    . MET   A 1 346 ? 1.53600   1.69000   -44.11900 1.000 71.00000  ? 312 MET   A HB3    1 
ATOM   4446 H HG2    . MET   A 1 346 ? 3.38000   2.64400   -43.06400 1.000 68.13000  ? 312 MET   A HG2    1 
ATOM   4447 H HG3    . MET   A 1 346 ? 4.31600   2.15400   -44.25700 1.000 68.13000  ? 312 MET   A HG3    1 
ATOM   4448 H HE1    . MET   A 1 346 ? 2.02100   4.10700   -46.90000 1.000 75.73000  ? 312 MET   A HE1    1 
ATOM   4449 H HE2    . MET   A 1 346 ? 2.71300   2.69400   -46.75400 1.000 75.73000  ? 312 MET   A HE2    1 
ATOM   4450 H HE3    . MET   A 1 346 ? 1.32800   2.99500   -46.01800 1.000 75.73000  ? 312 MET   A HE3    1 
ATOM   4451 N N      . SER   B 1 34  ? -6.36900  53.43800  -52.10900 1.000 67.63000  ? 0   SER   B N      1 
ATOM   4452 C CA     . SER   B 1 34  ? -6.10800  53.92300  -50.76200 1.000 71.30000  ? 0   SER   B CA     1 
ATOM   4453 C C      . SER   B 1 34  ? -5.99700  52.76800  -49.74900 1.000 66.75000  ? 0   SER   B C      1 
ATOM   4454 O O      . SER   B 1 34  ? -5.56200  52.97800  -48.61600 1.000 77.46000  ? 0   SER   B O      1 
ATOM   4455 C CB     . SER   B 1 34  ? -7.19500  54.92700  -50.33000 1.000 71.98000  ? 0   SER   B CB     1 
ATOM   4456 O OG     . SER   B 1 34  ? -8.50100  54.37800  -50.43300 1.000 75.96000  ? 0   SER   B OG     1 
ATOM   4457 H H      . SER   B 1 34  ? -6.33400  54.11900  -52.68100 1.000 67.63000  ? 0   SER   B H      1 
ATOM   4458 H HA     . SER   B 1 34  ? -5.26000  54.39300  -50.76300 1.000 71.30000  ? 0   SER   B HA     1 
ATOM   4459 H HB2    . SER   B 1 34  ? -7.03600  55.18100  -49.40800 1.000 71.98000  ? 0   SER   B HB2    1 
ATOM   4460 H HB3    . SER   B 1 34  ? -7.14000  55.71000  -50.90000 1.000 71.98000  ? 0   SER   B HB3    1 
ATOM   4461 H HG     . SER   B 1 34  ? -9.07100  54.94600  -50.19200 1.000 75.96000  ? 0   SER   B HG     1 
ATOM   4462 N N      . MET   B 1 35  ? -6.36700  51.55300  -50.15400 1.000 63.11000  ? 1   MET   B N      1 
ATOM   4463 C CA     . MET   B 1 35  ? -6.19300  50.36600  -49.31800 1.000 69.57000  ? 1   MET   B CA     1 
ATOM   4464 C C      . MET   B 1 35  ? -4.80300  49.77000  -49.51700 1.000 59.85000  ? 1   MET   B C      1 
ATOM   4465 O O      . MET   B 1 35  ? -4.24000  49.79800  -50.61800 1.000 56.45000  ? 1   MET   B O      1 
ATOM   4466 C CB     . MET   B 1 35  ? -7.24300  49.29700  -49.62900 1.000 69.55000  ? 1   MET   B CB     1 
ATOM   4467 C CG     . MET   B 1 35  ? -8.64700  49.59500  -49.15000 1.000 64.13000  ? 1   MET   B CG     1 
ATOM   4468 S SD     . MET   B 1 35  ? -9.59700  48.06600  -49.21200 1.000 71.82000  ? 1   MET   B SD     1 
ATOM   4469 C CE     . MET   B 1 35  ? -9.40500  47.61300  -50.93000 1.000 58.20000  ? 1   MET   B CE     1 
ATOM   4470 H H      . MET   B 1 35  ? -6.72600  51.38700  -50.91700 1.000 63.11000  ? 1   MET   B H      1 
ATOM   4471 H HA     . MET   B 1 35  ? -6.29500  50.62000  -48.38700 1.000 69.57000  ? 1   MET   B HA     1 
ATOM   4472 H HB2    . MET   B 1 35  ? -7.27900  49.18800  -50.59200 1.000 69.55000  ? 1   MET   B HB2    1 
ATOM   4473 H HB3    . MET   B 1 35  ? -6.96500  48.46400  -49.21800 1.000 69.55000  ? 1   MET   B HB3    1 
ATOM   4474 H HG2    . MET   B 1 35  ? -8.62300  49.91400  -48.23400 1.000 64.13000  ? 1   MET   B HG2    1 
ATOM   4475 H HG3    . MET   B 1 35  ? -9.06400  50.24800  -49.73400 1.000 64.13000  ? 1   MET   B HG3    1 
ATOM   4476 H HE1    . MET   B 1 35  ? -9.98600  46.86000  -51.12300 1.000 58.20000  ? 1   MET   B HE1    1 
ATOM   4477 H HE2    . MET   B 1 35  ? -9.65100  48.37000  -51.48400 1.000 58.20000  ? 1   MET   B HE2    1 
ATOM   4478 H HE3    . MET   B 1 35  ? -8.48200  47.36900  -51.09600 1.000 58.20000  ? 1   MET   B HE3    1 
ATOM   4479 N N      . SER   B 1 36  ? -4.25800  49.20600  -48.44100 1.000 55.86000  ? 2   SER   B N      1 
ATOM   4480 C CA     . SER   B 1 36  ? -2.87000  48.77700  -48.46700 1.000 38.95000  ? 2   SER   B CA     1 
ATOM   4481 C C      . SER   B 1 36  ? -2.66400  47.56300  -47.56300 1.000 40.03000  ? 2   SER   B C      1 
ATOM   4482 O O      . SER   B 1 36  ? -3.16300  47.50600  -46.43200 1.000 35.55000  ? 2   SER   B O      1 
ATOM   4483 C CB     . SER   B 1 36  ? -1.93700  49.90600  -48.04500 1.000 42.70000  ? 2   SER   B CB     1 
ATOM   4484 O OG     . SER   B 1 36  ? -0.61600  49.43800  -47.90400 1.000 47.04000  ? 2   SER   B OG     1 
ATOM   4485 H H      . SER   B 1 36  ? -4.66600  49.06400  -47.69700 1.000 55.86000  ? 2   SER   B H      1 
ATOM   4486 H HA     . SER   B 1 36  ? -2.63500  48.51700  -49.37100 1.000 38.95000  ? 2   SER   B HA     1 
ATOM   4487 H HB2    . SER   B 1 36  ? -1.95500  50.60100  -48.72200 1.000 42.70000  ? 2   SER   B HB2    1 
ATOM   4488 H HB3    . SER   B 1 36  ? -2.23800  50.26300  -47.19500 1.000 42.70000  ? 2   SER   B HB3    1 
ATOM   4489 H HG     . SER   B 1 36  ? -0.11100  50.06800  -47.67100 1.000 47.04000  ? 2   SER   B HG     1 
ATOM   4490 N N      . LEU   B 1 37  ? -1.92700  46.59400  -48.09000 1.000 31.53000  ? 3   LEU   B N      1 
ATOM   4491 C CA     . LEU   B 1 37  ? -1.49100  45.42500  -47.33400 1.000 27.78000  ? 3   LEU   B CA     1 
ATOM   4492 C C      . LEU   B 1 37  ? -0.04100  45.54200  -46.88700 1.000 30.92000  ? 3   LEU   B C      1 
ATOM   4493 O O      . LEU   B 1 37  ? 0.51300   44.57000  -46.35900 1.000 27.64000  ? 3   LEU   B O      1 
ATOM   4494 C CB     . LEU   B 1 37  ? -1.68400  44.15800  -48.18000 1.000 29.40000  ? 3   LEU   B CB     1 
ATOM   4495 C CG     . LEU   B 1 37  ? -3.10700  43.74200  -48.55900 1.000 34.38000  ? 3   LEU   B CG     1 
ATOM   4496 C CD1    . LEU   B 1 37  ? -3.06100  42.34600  -49.14900 1.000 38.63000  ? 3   LEU   B CD1    1 
ATOM   4497 C CD2    . LEU   B 1 37  ? -4.02800  43.77600  -47.35400 1.000 28.48000  ? 3   LEU   B CD2    1 
ATOM   4498 H H      . LEU   B 1 37  ? -1.65900  46.59000  -48.90700 1.000 31.53000  ? 3   LEU   B H      1 
ATOM   4499 H HA     . LEU   B 1 37  ? -2.03700  45.34300  -46.53700 1.000 27.78000  ? 3   LEU   B HA     1 
ATOM   4500 H HB2    . LEU   B 1 37  ? -1.19700  44.27900  -49.01000 1.000 29.40000  ? 3   LEU   B HB2    1 
ATOM   4501 H HB3    . LEU   B 1 37  ? -1.29500  43.41500  -47.69300 1.000 29.40000  ? 3   LEU   B HB3    1 
ATOM   4502 H HG     . LEU   B 1 37  ? -3.45500  44.34900  -49.23100 1.000 34.38000  ? 3   LEU   B HG     1 
ATOM   4503 H HD11   . LEU   B 1 37  ? -3.95800  42.08400  -49.40800 1.000 38.63000  ? 3   LEU   B HD11   1 
ATOM   4504 H HD12   . LEU   B 1 37  ? -2.48000  42.35100  -49.92600 1.000 38.63000  ? 3   LEU   B HD12   1 
ATOM   4505 H HD13   . LEU   B 1 37  ? -2.71700  41.73200  -48.48100 1.000 38.63000  ? 3   LEU   B HD13   1 
ATOM   4506 H HD21   . LEU   B 1 37  ? -4.87600  43.37000  -47.59400 1.000 28.48000  ? 3   LEU   B HD21   1 
ATOM   4507 H HD22   . LEU   B 1 37  ? -3.61700  43.28000  -46.62900 1.000 28.48000  ? 3   LEU   B HD22   1 
ATOM   4508 H HD23   . LEU   B 1 37  ? -4.16700  44.69800  -47.08700 1.000 28.48000  ? 3   LEU   B HD23   1 
ATOM   4509 N N      . GLN   B 1 38  ? 0.59100   46.71000  -47.07200 1.000 30.22000  ? 4   GLN   B N      1 
ATOM   4510 C CA     . GLN   B 1 38  ? 1.99900   46.85100  -46.69700 1.000 30.05000  ? 4   GLN   B CA     1 
ATOM   4511 C C      . GLN   B 1 38  ? 2.21900   46.62900  -45.20600 1.000 29.34000  ? 4   GLN   B C      1 
ATOM   4512 O O      . GLN   B 1 38  ? 1.36500   46.92900  -44.36600 1.000 33.02000  ? 4   GLN   B O      1 
ATOM   4513 C CB     . GLN   B 1 38  ? 2.53900   48.23800  -47.08300 1.000 29.71000  ? 4   GLN   B CB     1 
ATOM   4514 C CG     . GLN   B 1 38  ? 3.03700   48.30400  -48.49200 1.000 41.69000  ? 4   GLN   B CG     1 
ATOM   4515 C CD     . GLN   B 1 38  ? 3.61200   49.67100  -48.81400 1.000 48.01000  ? 4   GLN   B CD     1 
ATOM   4516 O OE1    . GLN   B 1 38  ? 3.69400   50.53600  -47.94700 1.000 51.21000  ? 4   GLN   B OE1    1 
ATOM   4517 N NE2    . GLN   B 1 38  ? 4.02100   49.86300  -50.05500 1.000 47.55000  ? 4   GLN   B NE2    1 
ATOM   4518 H H      . GLN   B 1 38  ? 0.23500   47.41900  -47.40400 1.000 30.22000  ? 4   GLN   B H      1 
ATOM   4519 H HA     . GLN   B 1 38  ? 2.51600   46.18600  -47.17700 1.000 30.05000  ? 4   GLN   B HA     1 
ATOM   4520 H HB2    . GLN   B 1 38  ? 1.82700   48.88900  -46.98900 1.000 29.71000  ? 4   GLN   B HB2    1 
ATOM   4521 H HB3    . GLN   B 1 38  ? 3.27600   48.46500  -46.49400 1.000 29.71000  ? 4   GLN   B HB3    1 
ATOM   4522 H HG2    . GLN   B 1 38  ? 3.73600   47.64300  -48.61600 1.000 41.69000  ? 4   GLN   B HG2    1 
ATOM   4523 H HG3    . GLN   B 1 38  ? 2.30100   48.13300  -49.10000 1.000 41.69000  ? 4   GLN   B HG3    1 
ATOM   4524 H HE21   . GLN   B 1 38  ? 3.94900   49.23100  -50.63400 1.000 47.55000  ? 4   GLN   B HE21   1 
ATOM   4525 H HE22   . GLN   B 1 38  ? 4.35500   50.62100  -50.28500 1.000 47.55000  ? 4   GLN   B HE22   1 
ATOM   4526 N N      . VAL   B 1 39  ? 3.37800   46.05200  -44.89200 1.000 29.37000  ? 5   VAL   B N      1 
ATOM   4527 C CA     . VAL   B 1 39  ? 3.82200   45.81500  -43.52900 1.000 28.53000  ? 5   VAL   B CA     1 
ATOM   4528 C C      . VAL   B 1 39  ? 5.20300   46.43900  -43.41200 1.000 35.43000  ? 5   VAL   B C      1 
ATOM   4529 O O      . VAL   B 1 39  ? 6.07700   46.17600  -44.24300 1.000 34.51000  ? 5   VAL   B O      1 
ATOM   4530 C CB     . VAL   B 1 39  ? 3.87800   44.30900  -43.18500 1.000 31.65000  ? 5   VAL   B CB     1 
ATOM   4531 C CG1    . VAL   B 1 39  ? 4.24200   44.11200  -41.72300 1.000 29.62000  ? 5   VAL   B CG1    1 
ATOM   4532 C CG2    . VAL   B 1 39  ? 2.54500   43.65600  -43.48400 1.000 28.77000  ? 5   VAL   B CG2    1 
ATOM   4533 H H      . VAL   B 1 39  ? 3.94300   45.78000  -45.48000 1.000 29.37000  ? 5   VAL   B H      1 
ATOM   4534 H HA     . VAL   B 1 39  ? 3.22500   46.25700  -42.90500 1.000 28.53000  ? 5   VAL   B HA     1 
ATOM   4535 H HB     . VAL   B 1 39  ? 4.55700   43.88000  -43.72900 1.000 31.65000  ? 5   VAL   B HB     1 
ATOM   4536 H HG11   . VAL   B 1 39  ? 4.14200   43.17400  -41.49700 1.000 29.62000  ? 5   VAL   B HG11   1 
ATOM   4537 H HG12   . VAL   B 1 39  ? 5.16100   44.38800  -41.58600 1.000 29.62000  ? 5   VAL   B HG12   1 
ATOM   4538 H HG13   . VAL   B 1 39  ? 3.64800   44.64900  -41.17500 1.000 29.62000  ? 5   VAL   B HG13   1 
ATOM   4539 H HG21   . VAL   B 1 39  ? 2.57300   42.73300  -43.18800 1.000 28.77000  ? 5   VAL   B HG21   1 
ATOM   4540 H HG22   . VAL   B 1 39  ? 1.84700   44.13400  -43.01000 1.000 28.77000  ? 5   VAL   B HG22   1 
ATOM   4541 H HG23   . VAL   B 1 39  ? 2.38200   43.69200  -44.43900 1.000 28.77000  ? 5   VAL   B HG23   1 
ATOM   4542 N N      . GLY   B 1 40  ? 5.38400   47.30200  -42.42700 1.000 31.15000  ? 6   GLY   B N      1 
ATOM   4543 C CA     . GLY   B 1 40  ? 6.68500   47.90600  -42.24000 1.000 32.87000  ? 6   GLY   B CA     1 
ATOM   4544 C C      . GLY   B 1 40  ? 7.23500   47.40600  -40.92800 1.000 34.78000  ? 6   GLY   B C      1 
ATOM   4545 O O      . GLY   B 1 40  ? 6.81800   47.87400  -39.87000 1.000 34.82000  ? 6   GLY   B O      1 
ATOM   4546 H H      . GLY   B 1 40  ? 4.78200   47.55000  -41.86500 1.000 31.15000  ? 6   GLY   B H      1 
ATOM   4547 H HA2    . GLY   B 1 40  ? 7.29100   47.66100  -42.95600 1.000 32.87000  ? 6   GLY   B HA2    1 
ATOM   4548 H HA3    . GLY   B 1 40  ? 6.60500   48.87200  -42.20600 1.000 32.87000  ? 6   GLY   B HA3    1 
ATOM   4549 N N      . ILE   B 1 41  ? 8.13200   46.41700  -40.97100 1.000 30.12000  ? 7   ILE   B N      1 
ATOM   4550 C CA     . ILE   B 1 41  ? 8.68900   45.80700  -39.77000 1.000 27.75000  ? 7   ILE   B CA     1 
ATOM   4551 C C      . ILE   B 1 41  ? 10.14800  45.45900  -40.04300 1.000 28.75000  ? 7   ILE   B C      1 
ATOM   4552 O O      . ILE   B 1 41  ? 10.56800  45.28500  -41.19100 1.000 31.48000  ? 7   ILE   B O      1 
ATOM   4553 C CB     . ILE   B 1 41  ? 7.92900   44.52400  -39.34500 1.000 29.36000  ? 7   ILE   B CB     1 
ATOM   4554 C CG1    . ILE   B 1 41  ? 7.98000   43.48000  -40.47600 1.000 30.53000  ? 7   ILE   B CG1    1 
ATOM   4555 C CG2    . ILE   B 1 41  ? 6.46200   44.84300  -38.88700 1.000 30.85000  ? 7   ILE   B CG2    1 
ATOM   4556 C CD1    . ILE   B 1 41  ? 7.44200   42.08600  -40.04600 1.000 28.20000  ? 7   ILE   B CD1    1 
ATOM   4557 H H      . ILE   B 1 41  ? 8.43700   46.07900  -41.70100 1.000 30.12000  ? 7   ILE   B H      1 
ATOM   4558 H HA     . ILE   B 1 41  ? 8.65600   46.44200  -39.03700 1.000 27.75000  ? 7   ILE   B HA     1 
ATOM   4559 H HB     . ILE   B 1 41  ? 8.39600   44.14900  -38.58300 1.000 29.36000  ? 7   ILE   B HB     1 
ATOM   4560 H HG12   . ILE   B 1 41  ? 7.43700   43.79300  -41.21600 1.000 30.53000  ? 7   ILE   B HG12   1 
ATOM   4561 H HG13   . ILE   B 1 41  ? 8.89500   43.35600  -40.76900 1.000 30.53000  ? 7   ILE   B HG13   1 
ATOM   4562 H HG21   . ILE   B 1 41  ? 6.03300   44.02100  -38.60200 1.000 30.85000  ? 7   ILE   B HG21   1 
ATOM   4563 H HG22   . ILE   B 1 41  ? 6.49300   45.47200  -38.14900 1.000 30.85000  ? 7   ILE   B HG22   1 
ATOM   4564 H HG23   . ILE   B 1 41  ? 5.97600   45.23100  -39.63100 1.000 30.85000  ? 7   ILE   B HG23   1 
ATOM   4565 H HD11   . ILE   B 1 41  ? 7.56700   41.46100  -40.77700 1.000 28.20000  ? 7   ILE   B HD11   1 
ATOM   4566 H HD12   . ILE   B 1 41  ? 7.93400   41.78500  -39.26600 1.000 28.20000  ? 7   ILE   B HD12   1 
ATOM   4567 H HD13   . ILE   B 1 41  ? 6.49900   42.16200  -39.83400 1.000 28.20000  ? 7   ILE   B HD13   1 
ATOM   4568 N N      . LEU   B 1 42  ? 10.92900  45.38100  -38.96600 1.000 30.49000  ? 8   LEU   B N      1 
ATOM   4569 C CA     . LEU   B 1 42  ? 12.29700  44.86600  -39.03300 1.000 32.12000  ? 8   LEU   B CA     1 
ATOM   4570 C C      . LEU   B 1 42  ? 13.17100  45.66900  -40.00300 1.000 35.35000  ? 8   LEU   B C      1 
ATOM   4571 O O      . LEU   B 1 42  ? 14.09300  45.12900  -40.61500 1.000 35.14000  ? 8   LEU   B O      1 
ATOM   4572 C CB     . LEU   B 1 42  ? 12.30600  43.38100  -39.42300 1.000 37.44000  ? 8   LEU   B CB     1 
ATOM   4573 C CG     . LEU   B 1 42  ? 11.43700  42.43900  -38.58200 1.000 39.74000  ? 8   LEU   B CG     1 
ATOM   4574 C CD1    . LEU   B 1 42  ? 11.36400  41.05700  -39.18600 1.000 39.59000  ? 8   LEU   B CD1    1 
ATOM   4575 C CD2    . LEU   B 1 42  ? 11.96500  42.35100  -37.16500 1.000 49.19000  ? 8   LEU   B CD2    1 
ATOM   4576 H H      . LEU   B 1 42  ? 10.68700  45.62300  -38.17700 1.000 30.49000  ? 8   LEU   B H      1 
ATOM   4577 H HA     . LEU   B 1 42  ? 12.69600  44.93900  -38.15200 1.000 32.12000  ? 8   LEU   B HA     1 
ATOM   4578 H HB2    . LEU   B 1 42  ? 11.99900  43.30900  -40.34000 1.000 37.44000  ? 8   LEU   B HB2    1 
ATOM   4579 H HB3    . LEU   B 1 42  ? 13.21900  43.05800  -39.36600 1.000 37.44000  ? 8   LEU   B HB3    1 
ATOM   4580 H HG     . LEU   B 1 42  ? 10.53500  42.79400  -38.54200 1.000 39.74000  ? 8   LEU   B HG     1 
ATOM   4581 H HD11   . LEU   B 1 42  ? 10.77100  40.50800  -38.64900 1.000 39.59000  ? 8   LEU   B HD11   1 
ATOM   4582 H HD12   . LEU   B 1 42  ? 11.02200  41.12600  -40.09100 1.000 39.59000  ? 8   LEU   B HD12   1 
ATOM   4583 H HD13   . LEU   B 1 42  ? 12.25400  40.67000  -39.19700 1.000 39.59000  ? 8   LEU   B HD13   1 
ATOM   4584 H HD21   . LEU   B 1 42  ? 11.91900  41.43000  -36.86400 1.000 49.19000  ? 8   LEU   B HD21   1 
ATOM   4585 H HD22   . LEU   B 1 42  ? 12.88400  42.65900  -37.15700 1.000 49.19000  ? 8   LEU   B HD22   1 
ATOM   4586 H HD23   . LEU   B 1 42  ? 11.42400  42.91700  -36.59200 1.000 49.19000  ? 8   LEU   B HD23   1 
ATOM   4587 N N      . GLY   B 1 43  ? 12.89500  46.96200  -40.15700 1.000 36.46000  ? 9   GLY   B N      1 
ATOM   4588 C CA     . GLY   B 1 43  ? 13.65300  47.77500  -41.09200 1.000 31.74000  ? 9   GLY   B CA     1 
ATOM   4589 C C      . GLY   B 1 43  ? 13.38200  47.50900  -42.55300 1.000 37.81000  ? 9   GLY   B C      1 
ATOM   4590 O O      . GLY   B 1 43  ? 14.11500  48.01600  -43.40100 1.000 35.81000  ? 9   GLY   B O      1 
ATOM   4591 H H      . GLY   B 1 43  ? 12.28300  47.38500  -39.72900 1.000 36.46000  ? 9   GLY   B H      1 
ATOM   4592 H HA2    . GLY   B 1 43  ? 13.46100  48.71000  -40.92000 1.000 31.74000  ? 9   GLY   B HA2    1 
ATOM   4593 H HA3    . GLY   B 1 43  ? 14.59900  47.63100  -40.93500 1.000 31.74000  ? 9   GLY   B HA3    1 
ATOM   4594 N N      . ASN   B 1 44  ? 12.33800  46.75200  -42.87900 1.000 32.54000  ? 10  ASN   B N      1 
ATOM   4595 C CA     . ASN   B 1 44  ? 11.97300  46.42100  -44.24800 1.000 29.31000  ? 10  ASN   B CA     1 
ATOM   4596 C C      . ASN   B 1 44  ? 10.54900  46.85400  -44.55400 1.000 29.35000  ? 10  ASN   B C      1 
ATOM   4597 O O      . ASN   B 1 44  ? 9.70200   46.96100  -43.67000 1.000 33.38000  ? 10  ASN   B O      1 
ATOM   4598 C CB     . ASN   B 1 44  ? 12.06300  44.90100  -44.49900 1.000 33.57000  ? 10  ASN   B CB     1 
ATOM   4599 C CG     . ASN   B 1 44  ? 13.48000  44.43300  -44.68300 1.000 41.19000  ? 10  ASN   B CG     1 
ATOM   4600 O OD1    . ASN   B 1 44  ? 14.03700  44.50900  -45.77700 1.000 39.60000  ? 10  ASN   B OD1    1 
ATOM   4601 N ND2    . ASN   B 1 44  ? 14.08300  43.97500  -43.60700 1.000 39.55000  ? 10  ASN   B ND2    1 
ATOM   4602 H H      . ASN   B 1 44  ? 11.80600  46.40600  -42.29800 1.000 32.54000  ? 10  ASN   B H      1 
ATOM   4603 H HA     . ASN   B 1 44  ? 12.57100  46.87100  -44.86500 1.000 29.31000  ? 10  ASN   B HA     1 
ATOM   4604 H HB2    . ASN   B 1 44  ? 11.68700  44.43100  -43.73800 1.000 33.57000  ? 10  ASN   B HB2    1 
ATOM   4605 H HB3    . ASN   B 1 44  ? 11.56700  44.68300  -45.30300 1.000 33.57000  ? 10  ASN   B HB3    1 
ATOM   4606 H HD21   . ASN   B 1 44  ? 14.89500  43.69700  -43.65500 1.000 39.55000  ? 10  ASN   B HD21   1 
ATOM   4607 H HD22   . ASN   B 1 44  ? 13.66100  43.94300  -42.85800 1.000 39.55000  ? 10  ASN   B HD22   1 
ATOM   4608 N N      . THR   B 1 45  ? 10.27200  47.04800  -45.83400 1.000 31.43000  ? 11  THR   B N      1 
ATOM   4609 C CA     . THR   B 1 45  ? 8.90100   47.20200  -46.29700 1.000 32.63000  ? 11  THR   B CA     1 
ATOM   4610 C C      . THR   B 1 45  ? 8.48400   45.90900  -46.99800 1.000 30.46000  ? 11  THR   B C      1 
ATOM   4611 O O      . THR   B 1 45  ? 9.15500   45.46600  -47.93900 1.000 40.64000  ? 11  THR   B O      1 
ATOM   4612 C CB     . THR   B 1 45  ? 8.75600   48.39000  -47.24100 1.000 41.66000  ? 11  THR   B CB     1 
ATOM   4613 O OG1    . THR   B 1 45  ? 9.24400   49.56500  -46.58700 1.000 48.06000  ? 11  THR   B OG1    1 
ATOM   4614 C CG2    . THR   B 1 45  ? 7.29000   48.58500  -47.56500 1.000 40.06000  ? 11  THR   B CG2    1 
ATOM   4615 H H      . THR   B 1 45  ? 10.86200  47.09500  -46.45800 1.000 31.43000  ? 11  THR   B H      1 
ATOM   4616 H HA     . THR   B 1 45  ? 8.31200   47.34200  -45.53900 1.000 32.63000  ? 11  THR   B HA     1 
ATOM   4617 H HB     . THR   B 1 45  ? 9.24800   48.23100  -48.06200 1.000 41.66000  ? 11  THR   B HB     1 
ATOM   4618 H HG1    . THR   B 1 45  ? 9.17000   50.22900  -47.09600 1.000 48.06000  ? 11  THR   B HG1    1 
ATOM   4619 H HG21   . THR   B 1 45  ? 7.16600   49.42200  -48.03900 1.000 40.06000  ? 11  THR   B HG21   1 
ATOM   4620 H HG22   . THR   B 1 45  ? 6.97100   47.85800  -48.12300 1.000 40.06000  ? 11  THR   B HG22   1 
ATOM   4621 H HG23   . THR   B 1 45  ? 6.77000   48.60800  -46.74700 1.000 40.06000  ? 11  THR   B HG23   1 
ATOM   4622 N N      . PHE   B 1 46  ? 7.40000   45.29300  -46.52500 1.000 32.83000  ? 12  PHE   B N      1 
ATOM   4623 C CA     . PHE   B 1 46  ? 6.81800   44.14100  -47.20500 1.000 29.96000  ? 12  PHE   B CA     1 
ATOM   4624 C C      . PHE   B 1 46  ? 5.55600   44.53800  -47.95700 1.000 33.73000  ? 12  PHE   B C      1 
ATOM   4625 O O      . PHE   B 1 46  ? 4.70500   45.26600  -47.42700 1.000 33.46000  ? 12  PHE   B O      1 
ATOM   4626 C CB     . PHE   B 1 46  ? 6.48700   43.01400  -46.22700 1.000 26.96000  ? 12  PHE   B CB     1 
ATOM   4627 C CG     . PHE   B 1 46  ? 7.67700   42.52700  -45.45000 1.000 29.13000  ? 12  PHE   B CG     1 
ATOM   4628 C CD1    . PHE   B 1 46  ? 8.17800   43.27300  -44.37400 1.000 31.55000  ? 12  PHE   B CD1    1 
ATOM   4629 C CD2    . PHE   B 1 46  ? 8.27900   41.31600  -45.75800 1.000 27.27000  ? 12  PHE   B CD2    1 
ATOM   4630 C CE1    . PHE   B 1 46  ? 9.26000   42.81800  -43.64700 1.000 29.08000  ? 12  PHE   B CE1    1 
ATOM   4631 C CE2    . PHE   B 1 46  ? 9.37600   40.86800  -45.03500 1.000 30.01000  ? 12  PHE   B CE2    1 
ATOM   4632 C CZ     . PHE   B 1 46  ? 9.86200   41.60800  -43.97800 1.000 33.49000  ? 12  PHE   B CZ     1 
ATOM   4633 H H      . PHE   B 1 46  ? 6.98300   45.52500  -45.81000 1.000 32.83000  ? 12  PHE   B H      1 
ATOM   4634 H HA     . PHE   B 1 46  ? 7.45400   43.79600  -47.85100 1.000 29.96000  ? 12  PHE   B HA     1 
ATOM   4635 H HB2    . PHE   B 1 46  ? 5.82700   43.33400  -45.59200 1.000 26.96000  ? 12  PHE   B HB2    1 
ATOM   4636 H HB3    . PHE   B 1 46  ? 6.12900   42.26200  -46.72400 1.000 26.96000  ? 12  PHE   B HB3    1 
ATOM   4637 H HD1    . PHE   B 1 46  ? 7.77800   44.08200  -44.14800 1.000 31.55000  ? 12  PHE   B HD1    1 
ATOM   4638 H HD2    . PHE   B 1 46  ? 7.95800   40.81000  -46.46900 1.000 27.27000  ? 12  PHE   B HD2    1 
ATOM   4639 H HE1    . PHE   B 1 46  ? 9.59000   43.32300  -42.93900 1.000 29.08000  ? 12  PHE   B HE1    1 
ATOM   4640 H HE2    . PHE   B 1 46  ? 9.77400   40.05600  -45.25300 1.000 30.01000  ? 12  PHE   B HE2    1 
ATOM   4641 H HZ     . PHE   B 1 46  ? 10.59400  41.30300  -43.49300 1.000 33.49000  ? 12  PHE   B HZ     1 
ATOM   4642 N N      . ALA   B 1 47  ? 5.43600   44.03600  -49.19500 1.000 30.21000  ? 13  ALA   B N      1 
ATOM   4643 C CA     . ALA   B 1 47  ? 4.30400   44.40900  -50.04000 1.000 31.05000  ? 13  ALA   B CA     1 
ATOM   4644 C C      . ALA   B 1 47  ? 3.00300   43.92900  -49.44400 1.000 30.83000  ? 13  ALA   B C      1 
ATOM   4645 O O      . ALA   B 1 47  ? 1.95300   44.54900  -49.64100 1.000 28.27000  ? 13  ALA   B O      1 
ATOM   4646 C CB     . ALA   B 1 47  ? 4.46400   43.83300  -51.45000 1.000 34.36000  ? 13  ALA   B CB     1 
ATOM   4647 H H      . ALA   B 1 47  ? 5.98900   43.48700  -49.55900 1.000 30.21000  ? 13  ALA   B H      1 
ATOM   4648 H HA     . ALA   B 1 47  ? 4.26500   45.37600  -50.11100 1.000 31.05000  ? 13  ALA   B HA     1 
ATOM   4649 H HB1    . ALA   B 1 47  ? 3.70000   44.09600  -51.98700 1.000 34.36000  ? 13  ALA   B HB1    1 
ATOM   4650 H HB2    . ALA   B 1 47  ? 5.28000   44.18100  -51.84200 1.000 34.36000  ? 13  ALA   B HB2    1 
ATOM   4651 H HB3    . ALA   B 1 47  ? 4.51100   42.86600  -51.39200 1.000 34.36000  ? 13  ALA   B HB3    1 
ATOM   4652 N N      . ASN   B 1 48  ? 3.04400   42.80500  -48.74400 1.000 28.31000  ? 14  ASN   B N      1 
ATOM   4653 C CA     . ASN   B 1 48  ? 1.87100   42.25800  -48.08800 1.000 27.78000  ? 14  ASN   B CA     1 
ATOM   4654 C C      . ASN   B 1 48  ? 2.35400   41.30200  -47.01400 1.000 26.17000  ? 14  ASN   B C      1 
ATOM   4655 O O      . ASN   B 1 48  ? 3.56400   41.03400  -46.92300 1.000 25.47000  ? 14  ASN   B O      1 
ATOM   4656 C CB     . ASN   B 1 48  ? 0.94100   41.54900  -49.09700 1.000 27.88000  ? 14  ASN   B CB     1 
ATOM   4657 C CG     . ASN   B 1 48  ? 1.61700   40.36900  -49.79700 1.000 28.79000  ? 14  ASN   B CG     1 
ATOM   4658 O OD1    . ASN   B 1 48  ? 1.87600   39.34200  -49.16400 1.000 26.85000  ? 14  ASN   B OD1    1 
ATOM   4659 N ND2    . ASN   B 1 48  ? 1.88700   40.50300  -51.10100 1.000 28.33000  ? 14  ASN   B ND2    1 
ATOM   4660 H H      . ASN   B 1 48  ? 3.75400   42.33200  -48.63300 1.000 28.31000  ? 14  ASN   B H      1 
ATOM   4661 H HA     . ASN   B 1 48  ? 1.37600   42.97300  -47.66900 1.000 27.78000  ? 14  ASN   B HA     1 
ATOM   4662 H HB2    . ASN   B 1 48  ? 0.13700   41.22500  -48.68300 1.000 27.88000  ? 14  ASN   B HB2    1 
ATOM   4663 H HB3    . ASN   B 1 48  ? 0.70500   42.19000  -49.78600 1.000 27.88000  ? 14  ASN   B HB3    1 
ATOM   4664 H HD21   . ASN   B 1 48  ? 2.26500   39.86100  -51.53000 1.000 28.33000  ? 14  ASN   B HD21   1 
ATOM   4665 H HD22   . ASN   B 1 48  ? 1.68800   41.23400  -51.50800 1.000 28.33000  ? 14  ASN   B HD22   1 
ATOM   4666 N N      . PRO   B 1 49  ? 1.46500   40.81800  -46.15300 1.000 25.45000  ? 15  PRO   B N      1 
ATOM   4667 C CA     . PRO   B 1 49  ? 1.90700   40.02400  -44.99700 1.000 24.61000  ? 15  PRO   B CA     1 
ATOM   4668 C C      . PRO   B 1 49  ? 2.24700   38.56700  -45.32100 1.000 26.06000  ? 15  PRO   B C      1 
ATOM   4669 O O      . PRO   B 1 49  ? 2.72200   37.84500  -44.43000 1.000 26.75000  ? 15  PRO   B O      1 
ATOM   4670 C CB     . PRO   B 1 49  ? 0.69900   40.11700  -44.04600 1.000 29.25000  ? 15  PRO   B CB     1 
ATOM   4671 C CG     . PRO   B 1 49  ? -0.49400  40.37200  -44.95600 1.000 30.92000  ? 15  PRO   B CG     1 
ATOM   4672 C CD     . PRO   B 1 49  ? 0.04500   41.22300  -46.06900 1.000 26.37000  ? 15  PRO   B CD     1 
ATOM   4673 H HA     . PRO   B 1 49  ? 2.67400   40.44400  -44.57800 1.000 24.61000  ? 15  PRO   B HA     1 
ATOM   4674 H HB2    . PRO   B 1 49  ? 0.59400   39.28000  -43.56700 1.000 29.25000  ? 15  PRO   B HB2    1 
ATOM   4675 H HB3    . PRO   B 1 49  ? 0.82400   40.85400  -43.42800 1.000 29.25000  ? 15  PRO   B HB3    1 
ATOM   4676 H HG2    . PRO   B 1 49  ? -0.83000  39.52900  -45.29900 1.000 30.92000  ? 15  PRO   B HG2    1 
ATOM   4677 H HG3    . PRO   B 1 49  ? -1.18500  40.84400  -44.46600 1.000 30.92000  ? 15  PRO   B HG3    1 
ATOM   4678 H HD2    . PRO   B 1 49  ? -0.44500  41.00600  -46.86900 1.000 26.37000  ? 15  PRO   B HD2    1 
ATOM   4679 H HD3    . PRO   B 1 49  ? -0.03000  42.16400  -45.84500 1.000 26.37000  ? 15  PRO   B HD3    1 
ATOM   4680 N N      . PHE   B 1 50  ? 2.02900   38.10700  -46.55000 1.000 24.93000  ? 16  PHE   B N      1 
ATOM   4681 C CA     . PHE   B 1 50  ? 2.05700   36.67100  -46.81400 1.000 25.95000  ? 16  PHE   B CA     1 
ATOM   4682 C C      . PHE   B 1 50  ? 3.45100   36.17100  -47.17500 1.000 23.61000  ? 16  PHE   B C      1 
ATOM   4683 O O      . PHE   B 1 50  ? 4.21100   36.84100  -47.87600 1.000 26.30000  ? 16  PHE   B O      1 
ATOM   4684 C CB     . PHE   B 1 50  ? 1.08800   36.31600  -47.94400 1.000 27.12000  ? 16  PHE   B CB     1 
ATOM   4685 C CG     . PHE   B 1 50  ? -0.34300  36.55800  -47.59300 1.000 26.46000  ? 16  PHE   B CG     1 
ATOM   4686 C CD1    . PHE   B 1 50  ? -1.01200  35.70900  -46.70200 1.000 24.85000  ? 16  PHE   B CD1    1 
ATOM   4687 C CD2    . PHE   B 1 50  ? -1.02100  37.64500  -48.13200 1.000 28.28000  ? 16  PHE   B CD2    1 
ATOM   4688 C CE1    . PHE   B 1 50  ? -2.33000  35.93800  -46.37200 1.000 29.62000  ? 16  PHE   B CE1    1 
ATOM   4689 C CE2    . PHE   B 1 50  ? -2.35100  37.88800  -47.81000 1.000 27.32000  ? 16  PHE   B CE2    1 
ATOM   4690 C CZ     . PHE   B 1 50  ? -3.01000  37.04500  -46.91500 1.000 27.79000  ? 16  PHE   B CZ     1 
ATOM   4691 H H      . PHE   B 1 50  ? 1.86500   38.59600  -47.23800 1.000 24.93000  ? 16  PHE   B H      1 
ATOM   4692 H HA     . PHE   B 1 50  ? 1.76800   36.20100  -46.01800 1.000 25.95000  ? 16  PHE   B HA     1 
ATOM   4693 H HB2    . PHE   B 1 50  ? 1.30000   36.85600  -48.72100 1.000 27.12000  ? 16  PHE   B HB2    1 
ATOM   4694 H HB3    . PHE   B 1 50  ? 1.18700   35.37500  -48.15800 1.000 27.12000  ? 16  PHE   B HB3    1 
ATOM   4695 H HD1    . PHE   B 1 50  ? -0.56400  34.98200  -46.33400 1.000 24.85000  ? 16  PHE   B HD1    1 
ATOM   4696 H HD2    . PHE   B 1 50  ? -0.58100  38.21400  -48.72200 1.000 28.28000  ? 16  PHE   B HD2    1 
ATOM   4697 H HE1    . PHE   B 1 50  ? -2.76600  35.36900  -45.77900 1.000 29.62000  ? 16  PHE   B HE1    1 
ATOM   4698 H HE2    . PHE   B 1 50  ? -2.79400  38.61900  -48.17600 1.000 27.32000  ? 16  PHE   B HE2    1 
ATOM   4699 H HZ     . PHE   B 1 50  ? -3.90200  37.19800  -46.69900 1.000 27.79000  ? 16  PHE   B HZ     1 
ATOM   4700 N N      . MET   B 1 51  ? 3.75400   34.95700  -46.72500 1.000 24.56000  ? 17  MET   B N      1 
ATOM   4701 C CA     . MET   B 1 51  ? 4.97000   34.24900  -47.11300 1.000 23.88000  ? 17  MET   B CA     1 
ATOM   4702 C C      . MET   B 1 51  ? 4.68900   32.76200  -46.99200 1.000 28.19000  ? 17  MET   B C      1 
ATOM   4703 O O      . MET   B 1 51  ? 3.64400   32.35900  -46.48500 1.000 25.27000  ? 17  MET   B O      1 
ATOM   4704 C CB     . MET   B 1 51  ? 6.15400   34.63500  -46.22900 1.000 27.38000  ? 17  MET   B CB     1 
ATOM   4705 C CG     . MET   B 1 51  ? 5.83900   34.47700  -44.73700 1.000 28.68000  ? 17  MET   B CG     1 
ATOM   4706 S SD     . MET   B 1 51  ? 7.10900   35.15300  -43.66000 1.000 30.66000  ? 17  MET   B SD     1 
ATOM   4707 C CE     . MET   B 1 51  ? 8.52500   34.09100  -44.08900 1.000 27.19000  ? 17  MET   B CE     1 
ATOM   4708 H H      . MET   B 1 51  ? 3.25900   34.51200  -46.18100 1.000 24.56000  ? 17  MET   B H      1 
ATOM   4709 H HA     . MET   B 1 51  ? 5.19000   34.46300  -48.03300 1.000 23.88000  ? 17  MET   B HA     1 
ATOM   4710 H HB2    . MET   B 1 51  ? 6.90800   34.06300  -46.44100 1.000 27.38000  ? 17  MET   B HB2    1 
ATOM   4711 H HB3    . MET   B 1 51  ? 6.38300   35.56300  -46.39200 1.000 27.38000  ? 17  MET   B HB3    1 
ATOM   4712 H HG2    . MET   B 1 51  ? 5.00800   34.93400  -44.53600 1.000 28.68000  ? 17  MET   B HG2    1 
ATOM   4713 H HG3    . MET   B 1 51  ? 5.75300   33.53200  -44.53800 1.000 28.68000  ? 17  MET   B HG3    1 
ATOM   4714 H HE1    . MET   B 1 51  ? 9.27300   34.31500  -43.51400 1.000 27.19000  ? 17  MET   B HE1    1 
ATOM   4715 H HE2    . MET   B 1 51  ? 8.27400   33.16300  -43.95900 1.000 27.19000  ? 17  MET   B HE2    1 
ATOM   4716 H HE3    . MET   B 1 51  ? 8.76300   34.24200  -45.01700 1.000 27.19000  ? 17  MET   B HE3    1 
ATOM   4717 N N      . ASN   B 1 52  ? 5.62800   31.94300  -47.45800 1.000 24.24000  ? 18  ASN   B N      1 
ATOM   4718 C CA     . ASN   B 1 52  ? 5.46400   30.51300  -47.20200 1.000 23.40000  ? 18  ASN   B CA     1 
ATOM   4719 C C      . ASN   B 1 52  ? 5.79700   30.21800  -45.74100 1.000 25.35000  ? 18  ASN   B C      1 
ATOM   4720 O O      . ASN   B 1 52  ? 6.47000   31.00200  -45.05500 1.000 25.88000  ? 18  ASN   B O      1 
ATOM   4721 C CB     . ASN   B 1 52  ? 6.36300   29.68000  -48.12800 1.000 23.54000  ? 18  ASN   B CB     1 
ATOM   4722 C CG     . ASN   B 1 52  ? 7.85000   29.97700  -47.91600 1.000 28.42000  ? 18  ASN   B CG     1 
ATOM   4723 O OD1    . ASN   B 1 52  ? 8.27900   31.12500  -48.03100 1.000 25.73000  ? 18  ASN   B OD1    1 
ATOM   4724 N ND2    . ASN   B 1 52  ? 8.63800   28.94300  -47.60200 1.000 26.10000  ? 18  ASN   B ND2    1 
ATOM   4725 H H      . ASN   B 1 52  ? 6.33000   32.17000  -47.90000 1.000 24.24000  ? 18  ASN   B H      1 
ATOM   4726 H HA     . ASN   B 1 52  ? 4.54200   30.25900  -47.36400 1.000 23.40000  ? 18  ASN   B HA     1 
ATOM   4727 H HB2    . ASN   B 1 52  ? 6.21500   28.73800  -47.95000 1.000 23.54000  ? 18  ASN   B HB2    1 
ATOM   4728 H HB3    . ASN   B 1 52  ? 6.14400   29.88400  -49.05100 1.000 23.54000  ? 18  ASN   B HB3    1 
ATOM   4729 H HD21   . ASN   B 1 52  ? 9.47900   29.06700  -47.47400 1.000 26.10000  ? 18  ASN   B HD21   1 
ATOM   4730 H HD22   . ASN   B 1 52  ? 8.30400   28.15400  -47.52900 1.000 26.10000  ? 18  ASN   B HD22   1 
ATOM   4731 N N      . ALA   B 1 53  ? 5.27600   29.09900  -45.25300 1.000 26.51000  ? 19  ALA   B N      1 
ATOM   4732 C CA     . ALA   B 1 53  ? 5.75300   28.54000  -43.99800 1.000 28.59000  ? 19  ALA   B CA     1 
ATOM   4733 C C      . ALA   B 1 53  ? 7.02400   27.75800  -44.26400 1.000 26.45000  ? 19  ALA   B C      1 
ATOM   4734 O O      . ALA   B 1 53  ? 7.18100   27.16600  -45.32600 1.000 27.98000  ? 19  ALA   B O      1 
ATOM   4735 C CB     . ALA   B 1 53  ? 4.69600   27.62500  -43.39100 1.000 27.90000  ? 19  ALA   B CB     1 
ATOM   4736 H H      . ALA   B 1 53  ? 4.64800   28.64700  -45.62800 1.000 26.51000  ? 19  ALA   B H      1 
ATOM   4737 H HA     . ALA   B 1 53  ? 5.94800   29.25300  -43.37100 1.000 28.59000  ? 19  ALA   B HA     1 
ATOM   4738 H HB1    . ALA   B 1 53  ? 5.01000   27.30800  -42.53100 1.000 27.90000  ? 19  ALA   B HB1    1 
ATOM   4739 H HB2    . ALA   B 1 53  ? 3.87400   28.12700  -43.27800 1.000 27.90000  ? 19  ALA   B HB2    1 
ATOM   4740 H HB3    . ALA   B 1 53  ? 4.54600   26.87600  -43.98800 1.000 27.90000  ? 19  ALA   B HB3    1 
ATOM   4741 N N      . ALA   B 1 54  ? 7.94100   27.77800  -43.30300 1.000 26.74000  ? 20  ALA   B N      1 
ATOM   4742 C CA     . ALA   B 1 54  ? 9.20800   27.07500  -43.49500 1.000 27.38000  ? 20  ALA   B CA     1 
ATOM   4743 C C      . ALA   B 1 54  ? 8.93200   25.61800  -43.82400 1.000 30.16000  ? 20  ALA   B C      1 
ATOM   4744 O O      . ALA   B 1 54  ? 8.02900   25.01300  -43.25200 1.000 29.48000  ? 20  ALA   B O      1 
ATOM   4745 C CB     . ALA   B 1 54  ? 10.08100  27.16300  -42.23400 1.000 29.45000  ? 20  ALA   B CB     1 
ATOM   4746 H H      . ALA   B 1 54  ? 7.86000   28.18000  -42.54700 1.000 26.74000  ? 20  ALA   B H      1 
ATOM   4747 H HA     . ALA   B 1 54  ? 9.69200   27.47200  -44.23500 1.000 27.38000  ? 20  ALA   B HA     1 
ATOM   4748 H HB1    . ALA   B 1 54  ? 10.90700  26.67900  -42.38800 1.000 29.45000  ? 20  ALA   B HB1    1 
ATOM   4749 H HB2    . ALA   B 1 54  ? 10.27300  28.09500  -42.04800 1.000 29.45000  ? 20  ALA   B HB2    1 
ATOM   4750 H HB3    . ALA   B 1 54  ? 9.60000   26.76900  -41.49000 1.000 29.45000  ? 20  ALA   B HB3    1 
ATOM   4751 N N      . GLY   B 1 55  ? 9.69300   25.06000  -44.77200 1.000 30.35000  ? 21  GLY   B N      1 
ATOM   4752 C CA     . GLY   B 1 55  ? 9.53600   23.66800  -45.15400 1.000 30.76000  ? 21  GLY   B CA     1 
ATOM   4753 C C      . GLY   B 1 55  ? 8.63000   23.42200  -46.33900 1.000 31.55000  ? 21  GLY   B C      1 
ATOM   4754 O O      . GLY   B 1 55  ? 8.70300   22.33900  -46.93900 1.000 32.79000  ? 21  GLY   B O      1 
ATOM   4755 H H      . GLY   B 1 55  ? 10.31000  25.47300  -45.20400 1.000 30.35000  ? 21  GLY   B H      1 
ATOM   4756 H HA2    . GLY   B 1 55  ? 10.40600  23.28800  -45.35100 1.000 30.76000  ? 21  GLY   B HA2    1 
ATOM   4757 H HA3    . GLY   B 1 55  ? 9.15800   23.19500  -44.41100 1.000 30.76000  ? 21  GLY   B HA3    1 
ATOM   4758 N N      . VAL   B 1 56  ? 7.79800   24.39100  -46.71300 1.000 29.46000  ? 22  VAL   B N      1 
ATOM   4759 C CA     . VAL   B 1 56  ? 6.87400   24.25700  -47.83400 1.000 30.35000  ? 22  VAL   B CA     1 
ATOM   4760 C C      . VAL   B 1 56  ? 7.38300   25.10400  -48.99300 1.000 34.42000  ? 22  VAL   B C      1 
ATOM   4761 O O      . VAL   B 1 56  ? 7.55100   26.32800  -48.86600 1.000 33.25000  ? 22  VAL   B O      1 
ATOM   4762 C CB     . VAL   B 1 56  ? 5.43500   24.64000  -47.45100 1.000 34.72000  ? 22  VAL   B CB     1 
ATOM   4763 C CG1    . VAL   B 1 56  ? 4.52600   24.59700  -48.69000 1.000 34.38000  ? 22  VAL   B CG1    1 
ATOM   4764 C CG2    . VAL   B 1 56  ? 4.92700   23.69100  -46.38400 1.000 32.28000  ? 22  VAL   B CG2    1 
ATOM   4765 H H      . VAL   B 1 56  ? 7.75000   25.15500  -46.32200 1.000 29.46000  ? 22  VAL   B H      1 
ATOM   4766 H HA     . VAL   B 1 56  ? 6.86400   23.33200  -48.12600 1.000 30.35000  ? 22  VAL   B HA     1 
ATOM   4767 H HB     . VAL   B 1 56  ? 5.42400   25.54100  -47.09200 1.000 34.72000  ? 22  VAL   B HB     1 
ATOM   4768 H HG11   . VAL   B 1 56  ? 3.60100   24.64500  -48.40200 1.000 34.38000  ? 22  VAL   B HG11   1 
ATOM   4769 H HG12   . VAL   B 1 56  ? 4.73100   25.35100  -49.26400 1.000 34.38000  ? 22  VAL   B HG12   1 
ATOM   4770 H HG13   . VAL   B 1 56  ? 4.68000   23.76500  -49.16500 1.000 34.38000  ? 22  VAL   B HG13   1 
ATOM   4771 H HG21   . VAL   B 1 56  ? 4.00900   23.92000  -46.16900 1.000 32.28000  ? 22  VAL   B HG21   1 
ATOM   4772 H HG22   . VAL   B 1 56  ? 4.97100   22.78300  -46.72300 1.000 32.28000  ? 22  VAL   B HG22   1 
ATOM   4773 H HG23   . VAL   B 1 56  ? 5.48300   23.77700  -45.59400 1.000 32.28000  ? 22  VAL   B HG23   1 
ATOM   4774 N N      A MET   B 1 57  ? 7.65100   24.43800  -50.11600 0.760 31.93000  ? 23  MET   B N      1 
ATOM   4775 N N      B MET   B 1 57  ? 7.62500   24.44700  -50.12500 0.240 32.15000  ? 23  MET   B N      1 
ATOM   4776 C CA     A MET   B 1 57  ? 8.04800   25.07600  -51.36700 0.760 34.69000  ? 23  MET   B CA     1 
ATOM   4777 C CA     B MET   B 1 57  ? 8.04500   25.10300  -51.36000 0.240 34.64000  ? 23  MET   B CA     1 
ATOM   4778 C C      A MET   B 1 57  ? 9.28400   25.95900  -51.19200 0.760 31.41000  ? 23  MET   B C      1 
ATOM   4779 C C      B MET   B 1 57  ? 9.26100   25.99600  -51.12500 0.240 31.60000  ? 23  MET   B C      1 
ATOM   4780 O O      A MET   B 1 57  ? 9.33300   27.09600  -51.66500 0.760 33.79000  ? 23  MET   B O      1 
ATOM   4781 O O      B MET   B 1 57  ? 9.27500   27.18000  -51.47200 0.240 34.01000  ? 23  MET   B O      1 
ATOM   4782 C CB     A MET   B 1 57  ? 6.88900   25.87800  -51.97700 0.760 37.68000  ? 23  MET   B CB     1 
ATOM   4783 C CB     B MET   B 1 57  ? 6.88900   25.90000  -51.97500 0.240 37.54000  ? 23  MET   B CB     1 
ATOM   4784 C CG     A MET   B 1 57  ? 7.23000   26.44600  -53.35500 0.760 42.84000  ? 23  MET   B CG     1 
ATOM   4785 C CG     B MET   B 1 57  ? 7.23900   26.57200  -53.29600 0.240 42.62000  ? 23  MET   B CG     1 
ATOM   4786 S SD     A MET   B 1 57  ? 5.84000   27.23000  -54.17800 0.760 47.09000  ? 23  MET   B SD     1 
ATOM   4787 S SD     B MET   B 1 57  ? 5.81100   27.30000  -54.12300 0.240 46.47000  ? 23  MET   B SD     1 
ATOM   4788 C CE     A MET   B 1 57  ? 4.83600   25.81500  -54.41000 0.760 32.97000  ? 23  MET   B CE     1 
ATOM   4789 C CE     B MET   B 1 57  ? 6.61800   28.15100  -55.47800 0.240 28.78000  ? 23  MET   B CE     1 
ATOM   4790 H H      A MET   B 1 57  ? 7.60700   23.58100  -50.17700 0.760 32.15000  ? 23  MET   B H      1 
ATOM   4791 H H      B MET   B 1 57  ? 7.55000   23.59400  -50.20400 0.240 32.15000  ? 23  MET   B H      1 
ATOM   4792 H HA     A MET   B 1 57  ? 8.27000   24.37600  -52.00000 0.760 34.64000  ? 23  MET   B HA     1 
ATOM   4793 H HA     B MET   B 1 57  ? 8.29200   24.41600  -51.99900 0.240 34.64000  ? 23  MET   B HA     1 
ATOM   4794 H HB2    A MET   B 1 57  ? 6.11800   25.29700  -52.06600 0.760 37.54000  ? 23  MET   B HB2    1 
ATOM   4795 H HB2    B MET   B 1 57  ? 6.14600   25.29800  -52.13600 0.240 37.54000  ? 23  MET   B HB2    1 
ATOM   4796 H HB3    A MET   B 1 57  ? 6.67700   26.62100  -51.39100 0.760 37.54000  ? 23  MET   B HB3    1 
ATOM   4797 H HB3    B MET   B 1 57  ? 6.62100   26.59300  -51.35200 0.240 37.54000  ? 23  MET   B HB3    1 
ATOM   4798 H HG2    A MET   B 1 57  ? 7.91500   27.12200  -53.28000 0.760 42.62000  ? 23  MET   B HG2    1 
ATOM   4799 H HG2    B MET   B 1 57  ? 7.87000   27.28900  -53.14800 0.240 42.62000  ? 23  MET   B HG2    1 
ATOM   4800 H HG3    A MET   B 1 57  ? 7.54200   25.72400  -53.92200 0.760 42.62000  ? 23  MET   B HG3    1 
ATOM   4801 H HG3    B MET   B 1 57  ? 7.62400   25.91100  -53.89200 0.240 42.62000  ? 23  MET   B HG3    1 
ATOM   4802 H HE1    A MET   B 1 57  ? 4.61300   25.73100  -55.35000 0.760 28.78000  ? 23  MET   B HE1    1 
ATOM   4803 H HE1    B MET   B 1 57  ? 5.95900   28.37200  -56.15300 0.240 28.78000  ? 23  MET   B HE1    1 
ATOM   4804 H HE2    A MET   B 1 57  ? 5.34000   25.04200  -54.11400 0.760 28.78000  ? 23  MET   B HE2    1 
ATOM   4805 H HE2    B MET   B 1 57  ? 7.03900   28.95800  -55.14300 0.240 28.78000  ? 23  MET   B HE2    1 
ATOM   4806 H HE3    A MET   B 1 57  ? 4.03400   25.95800  -53.88600 0.760 28.78000  ? 23  MET   B HE3    1 
ATOM   4807 H HE3    B MET   B 1 57  ? 7.28400   27.55600  -55.85400 0.240 28.78000  ? 23  MET   B HE3    1 
ATOM   4808 N N      . CYS   B 1 58  ? 10.30900  25.41600  -50.52800 1.000 30.68000  ? 24  CYS   B N      1 
ATOM   4809 C CA     . CYS   B 1 58  ? 11.47000  26.26300  -50.22900 1.000 30.18000  ? 24  CYS   B CA     1 
ATOM   4810 C C      . CYS   B 1 58  ? 12.76100  25.46900  -50.02700 1.000 30.08000  ? 24  CYS   B C      1 
ATOM   4811 O O      . CYS   B 1 58  ? 13.67000  25.98500  -49.38800 1.000 32.05000  ? 24  CYS   B O      1 
ATOM   4812 C CB     . CYS   B 1 58  ? 11.18900  27.10800  -48.98500 1.000 30.07000  ? 24  CYS   B CB     1 
ATOM   4813 S SG     . CYS   B 1 58  ? 10.74000  26.14600  -47.54800 1.000 35.07000  ? 24  CYS   B SG     1 
ATOM   4814 H H      A CYS   B 1 58  ? 10.35900  24.60300  -50.25200 0.760 30.68000  ? 24  CYS   B H      1 
ATOM   4815 H H      B CYS   B 1 58  ? 10.37300  24.59000  -50.29900 0.240 30.68000  ? 24  CYS   B H      1 
ATOM   4816 H HA     . CYS   B 1 58  ? 11.61700  26.86900  -50.97100 1.000 30.18000  ? 24  CYS   B HA     1 
ATOM   4817 H HB2    . CYS   B 1 58  ? 11.98400  27.61900  -48.76500 1.000 30.07000  ? 24  CYS   B HB2    1 
ATOM   4818 H HB3    . CYS   B 1 58  ? 10.45500  27.71100  -49.17800 1.000 30.07000  ? 24  CYS   B HB3    1 
ATOM   4819 H HG     . CYS   B 1 58  ? 10.52900  26.90900  -46.64600 1.000 35.07000  ? 24  CYS   B HG     1 
ATOM   4820 N N      . SER   B 1 59  ? 12.85500  24.25100  -50.57100 1.000 32.38000  ? 25  SER   B N      1 
ATOM   4821 C CA     . SER   B 1 59  ? 14.01500  23.39200  -50.37700 1.000 35.94000  ? 25  SER   B CA     1 
ATOM   4822 C C      . SER   B 1 59  ? 15.03900  23.48800  -51.50600 1.000 40.56000  ? 25  SER   B C      1 
ATOM   4823 O O      . SER   B 1 59  ? 16.24200  23.40400  -51.22800 1.000 37.05000  ? 25  SER   B O      1 
ATOM   4824 C CB     . SER   B 1 59  ? 13.54900  21.93800  -50.21300 1.000 36.09000  ? 25  SER   B CB     1 
ATOM   4825 O OG     . SER   B 1 59  ? 12.82800  21.79100  -48.98300 1.000 37.98000  ? 25  SER   B OG     1 
ATOM   4826 H H      . SER   B 1 59  ? 12.24500  23.89900  -51.06500 1.000 32.38000  ? 25  SER   B H      1 
ATOM   4827 H HA     . SER   B 1 59  ? 14.45800  23.65300  -49.55500 1.000 35.94000  ? 25  SER   B HA     1 
ATOM   4828 H HB2    . SER   B 1 59  ? 12.96700  21.70500  -50.95300 1.000 36.09000  ? 25  SER   B HB2    1 
ATOM   4829 H HB3    . SER   B 1 59  ? 14.32400  21.35500  -50.20000 1.000 36.09000  ? 25  SER   B HB3    1 
ATOM   4830 H HG     . SER   B 1 59  ? 12.15600  22.29500  -48.98200 1.000 37.98000  ? 25  SER   B HG     1 
ATOM   4831 N N      . THR   B 1 60  ? 14.60000  23.68700  -52.75900 1.000 37.95000  ? 26  THR   B N      1 
ATOM   4832 C CA     . THR   B 1 60  ? 15.48100  23.77000  -53.91600 1.000 38.96000  ? 26  THR   B CA     1 
ATOM   4833 C C      . THR   B 1 60  ? 15.52900  25.19100  -54.45800 1.000 36.53000  ? 26  THR   B C      1 
ATOM   4834 O O      . THR   B 1 60  ? 14.65900  26.01900  -54.18500 1.000 35.16000  ? 26  THR   B O      1 
ATOM   4835 C CB     . THR   B 1 60  ? 15.02700  22.85100  -55.06100 1.000 40.58000  ? 26  THR   B CB     1 
ATOM   4836 O OG1    . THR   B 1 60  ? 13.80000  23.34900  -55.61000 1.000 37.38000  ? 26  THR   B OG1    1 
ATOM   4837 C CG2    . THR   B 1 60  ? 14.85400  21.40700  -54.59900 1.000 41.28000  ? 26  THR   B CG2    1 
ATOM   4838 H H      . THR   B 1 60  ? 13.76900  23.77900  -52.96000 1.000 37.95000  ? 26  THR   B H      1 
ATOM   4839 H HA     . THR   B 1 60  ? 16.37900  23.51200  -53.65700 1.000 38.96000  ? 26  THR   B HA     1 
ATOM   4840 H HB     . THR   B 1 60  ? 15.70500  22.86000  -55.75500 1.000 40.58000  ? 26  THR   B HB     1 
ATOM   4841 H HG1    . THR   B 1 60  ? 13.55500  22.86500  -56.25100 1.000 37.38000  ? 26  THR   B HG1    1 
ATOM   4842 H HG21   . THR   B 1 60  ? 14.60300  20.84700  -55.35000 1.000 41.28000  ? 26  THR   B HG21   1 
ATOM   4843 H HG22   . THR   B 1 60  ? 15.68600  21.07700  -54.22400 1.000 41.28000  ? 26  THR   B HG22   1 
ATOM   4844 H HG23   . THR   B 1 60  ? 14.16100  21.35600  -53.92200 1.000 41.28000  ? 26  THR   B HG23   1 
ATOM   4845 N N      . GLU   B 1 61  ? 16.55400  25.45000  -55.26900 1.000 37.77000  ? 27  GLU   B N      1 
ATOM   4846 C CA     . GLU   B 1 61  ? 16.65500  26.73400  -55.94800 1.000 37.71000  ? 27  GLU   B CA     1 
ATOM   4847 C C      . GLU   B 1 61  ? 15.41300  27.01800  -56.79500 1.000 34.95000  ? 27  GLU   B C      1 
ATOM   4848 O O      . GLU   B 1 61  ? 14.90200  28.14300  -56.82000 1.000 34.27000  ? 27  GLU   B O      1 
ATOM   4849 C CB     . GLU   B 1 61  ? 17.91200  26.74200  -56.81600 1.000 39.76000  ? 27  GLU   B CB     1 
ATOM   4850 C CG     . GLU   B 1 61  ? 18.06500  27.97800  -57.64400 1.000 52.09000  ? 27  GLU   B CG     1 
ATOM   4851 C CD     . GLU   B 1 61  ? 18.73100  29.08900  -56.88200 1.000 68.24000  ? 27  GLU   B CD     1 
ATOM   4852 O OE1    . GLU   B 1 61  ? 19.54500  28.76900  -55.98100 1.000 67.13000  ? 27  GLU   B OE1    1 
ATOM   4853 O OE2    . GLU   B 1 61  ? 18.44000  30.27100  -57.17400 1.000 75.06000  ? 27  GLU   B OE2    1 
ATOM   4854 H H      . GLU   B 1 61  ? 17.19600  24.90400  -55.44000 1.000 37.77000  ? 27  GLU   B H      1 
ATOM   4855 H HA     . GLU   B 1 61  ? 16.73800  27.43900  -55.28700 1.000 37.71000  ? 27  GLU   B HA     1 
ATOM   4856 H HB2    . GLU   B 1 61  ? 18.69000  26.65400  -56.24400 1.000 39.76000  ? 27  GLU   B HB2    1 
ATOM   4857 H HB3    . GLU   B 1 61  ? 17.87000  25.98800  -57.42400 1.000 39.76000  ? 27  GLU   B HB3    1 
ATOM   4858 H HG2    . GLU   B 1 61  ? 18.62500  27.77100  -58.40800 1.000 52.09000  ? 27  GLU   B HG2    1 
ATOM   4859 H HG3    . GLU   B 1 61  ? 17.20500  28.30000  -57.95100 1.000 52.09000  ? 27  GLU   B HG3    1 
ATOM   4860 N N      . GLU   B 1 62  ? 14.90700  26.00900  -57.49700 1.000 33.94000  ? 28  GLU   B N      1 
ATOM   4861 C CA     . GLU   B 1 62  ? 13.71900  26.22600  -58.32000 1.000 35.26000  ? 28  GLU   B CA     1 
ATOM   4862 C C      . GLU   B 1 62  ? 12.52100  26.68200  -57.48100 1.000 33.48000  ? 28  GLU   B C      1 
ATOM   4863 O O      . GLU   B 1 62  ? 11.78000  27.58500  -57.88700 1.000 34.02000  ? 28  GLU   B O      1 
ATOM   4864 C CB     . GLU   B 1 62  ? 13.39800  24.93200  -59.07200 1.000 43.84000  ? 28  GLU   B CB     1 
ATOM   4865 C CG     . GLU   B 1 62  ? 12.39200  25.06900  -60.18700 1.000 53.08000  ? 28  GLU   B CG     1 
ATOM   4866 C CD     . GLU   B 1 62  ? 12.17100  23.74000  -60.90100 1.000 74.95000  ? 28  GLU   B CD     1 
ATOM   4867 O OE1    . GLU   B 1 62  ? 13.09700  23.27500  -61.60300 1.000 79.34000  ? 28  GLU   B OE1    1 
ATOM   4868 O OE2    . GLU   B 1 62  ? 11.08500  23.14800  -60.73100 1.000 80.77000  ? 28  GLU   B OE2    1 
ATOM   4869 H H      . GLU   B 1 62  ? 15.22200  25.20900  -57.51600 1.000 33.94000  ? 28  GLU   B H      1 
ATOM   4870 H HA     . GLU   B 1 62  ? 13.90800  26.91600  -58.97500 1.000 35.26000  ? 28  GLU   B HA     1 
ATOM   4871 H HB2    . GLU   B 1 62  ? 14.21900  24.59000  -59.46000 1.000 43.84000  ? 28  GLU   B HB2    1 
ATOM   4872 H HB3    . GLU   B 1 62  ? 13.04500  24.28700  -58.43900 1.000 43.84000  ? 28  GLU   B HB3    1 
ATOM   4873 H HG2    . GLU   B 1 62  ? 11.54400  25.36200  -59.81900 1.000 53.08000  ? 28  GLU   B HG2    1 
ATOM   4874 H HG3    . GLU   B 1 62  ? 12.71800  25.71300  -60.83500 1.000 53.08000  ? 28  GLU   B HG3    1 
ATOM   4875 N N      . GLU   B 1 63  ? 12.32000  26.07200  -56.30100 1.000 32.52000  ? 29  GLU   B N      1 
ATOM   4876 C CA     . GLU   B 1 63  ? 11.20500  26.46000  -55.43300 1.000 35.75000  ? 29  GLU   B CA     1 
ATOM   4877 C C      . GLU   B 1 63  ? 11.40000  27.86500  -54.87200 1.000 35.31000  ? 29  GLU   B C      1 
ATOM   4878 O O      . GLU   B 1 63  ? 10.45400  28.66700  -54.84200 1.000 32.13000  ? 29  GLU   B O      1 
ATOM   4879 C CB     . GLU   B 1 63  ? 11.05400  25.44900  -54.28800 1.000 33.30000  ? 29  GLU   B CB     1 
ATOM   4880 C CG     . GLU   B 1 63  ? 10.66000  24.07300  -54.77400 1.000 37.12000  ? 29  GLU   B CG     1 
ATOM   4881 C CD     . GLU   B 1 63  ? 10.61900  23.02400  -53.67000 1.000 43.05000  ? 29  GLU   B CD     1 
ATOM   4882 O OE1    . GLU   B 1 63  ? 11.57000  22.95900  -52.86400 1.000 39.29000  ? 29  GLU   B OE1    1 
ATOM   4883 O OE2    . GLU   B 1 63  ? 9.61200   22.28200  -53.60000 1.000 46.36000  ? 29  GLU   B OE2    1 
ATOM   4884 H H      . GLU   B 1 63  ? 12.81100  25.43900  -55.98700 1.000 32.52000  ? 29  GLU   B H      1 
ATOM   4885 H HA     . GLU   B 1 63  ? 10.38400  26.45400  -55.95000 1.000 35.75000  ? 29  GLU   B HA     1 
ATOM   4886 H HB2    . GLU   B 1 63  ? 11.90000  25.37200  -53.81900 1.000 33.30000  ? 29  GLU   B HB2    1 
ATOM   4887 H HB3    . GLU   B 1 63  ? 10.36500  25.76100  -53.68200 1.000 33.30000  ? 29  GLU   B HB3    1 
ATOM   4888 H HG2    . GLU   B 1 63  ? 9.77600   24.12200  -55.17000 1.000 37.12000  ? 29  GLU   B HG2    1 
ATOM   4889 H HG3    . GLU   B 1 63  ? 11.30200  23.77900  -55.43900 1.000 37.12000  ? 29  GLU   B HG3    1 
ATOM   4890 N N      . LEU   B 1 64  ? 12.62000  28.18000  -54.42900 1.000 30.16000  ? 30  LEU   B N      1 
ATOM   4891 C CA     . LEU   B 1 64  ? 12.88700  29.52100  -53.90500 1.000 31.04000  ? 30  LEU   B CA     1 
ATOM   4892 C C      . LEU   B 1 64  ? 12.70400  30.58100  -54.99200 1.000 31.20000  ? 30  LEU   B C      1 
ATOM   4893 O O      . LEU   B 1 64  ? 12.15600  31.66700  -54.73600 1.000 30.56000  ? 30  LEU   B O      1 
ATOM   4894 C CB     . LEU   B 1 64  ? 14.29400  29.56000  -53.29400 1.000 35.26000  ? 30  LEU   B CB     1 
ATOM   4895 C CG     . LEU   B 1 64  ? 14.46700  28.71300  -52.01000 1.000 32.23000  ? 30  LEU   B CG     1 
ATOM   4896 C CD1    . LEU   B 1 64  ? 15.94500  28.54000  -51.62100 1.000 28.78000  ? 30  LEU   B CD1    1 
ATOM   4897 C CD2    . LEU   B 1 64  ? 13.72100  29.36300  -50.84000 1.000 31.28000  ? 30  LEU   B CD2    1 
ATOM   4898 H H      . LEU   B 1 64  ? 13.29600  27.64800  -54.42100 1.000 30.16000  ? 30  LEU   B H      1 
ATOM   4899 H HA     . LEU   B 1 64  ? 12.25100  29.71200  -53.19900 1.000 31.04000  ? 30  LEU   B HA     1 
ATOM   4900 H HB2    . LEU   B 1 64  ? 14.92600  29.22900  -53.95100 1.000 35.26000  ? 30  LEU   B HB2    1 
ATOM   4901 H HB3    . LEU   B 1 64  ? 14.50800  30.47900  -53.07000 1.000 35.26000  ? 30  LEU   B HB3    1 
ATOM   4902 H HG     . LEU   B 1 64  ? 14.08900  27.83200  -52.15700 1.000 32.23000  ? 30  LEU   B HG     1 
ATOM   4903 H HD11   . LEU   B 1 64  ? 15.99800  28.00300  -50.81500 1.000 28.78000  ? 30  LEU   B HD11   1 
ATOM   4904 H HD12   . LEU   B 1 64  ? 16.41200  28.09700  -52.34600 1.000 28.78000  ? 30  LEU   B HD12   1 
ATOM   4905 H HD13   . LEU   B 1 64  ? 16.33400  29.41400  -51.46200 1.000 28.78000  ? 30  LEU   B HD13   1 
ATOM   4906 H HD21   . LEU   B 1 64  ? 13.91300  28.86700  -50.02900 1.000 31.28000  ? 30  LEU   B HD21   1 
ATOM   4907 H HD22   . LEU   B 1 64  ? 14.02200  30.28000  -50.74500 1.000 31.28000  ? 30  LEU   B HD22   1 
ATOM   4908 H HD23   . LEU   B 1 64  ? 12.76900  29.34400  -51.02200 1.000 31.28000  ? 30  LEU   B HD23   1 
ATOM   4909 N N      . ALA   B 1 65  ? 13.11300  30.26400  -56.22900 1.000 30.55000  ? 31  ALA   B N      1 
ATOM   4910 C CA     . ALA   B 1 65  ? 12.91000  31.20300  -57.33300 1.000 32.22000  ? 31  ALA   B CA     1 
ATOM   4911 C C      . ALA   B 1 65  ? 11.43200  31.40100  -57.60900 1.000 34.43000  ? 31  ALA   B C      1 
ATOM   4912 O O      . ALA   B 1 65  ? 10.98600  32.52800  -57.87200 1.000 34.54000  ? 31  ALA   B O      1 
ATOM   4913 C CB     . ALA   B 1 65  ? 13.62200  30.69900  -58.59200 1.000 40.39000  ? 31  ALA   B CB     1 
ATOM   4914 H H      . ALA   B 1 65  ? 13.50100  29.52900  -56.44800 1.000 30.55000  ? 31  ALA   B H      1 
ATOM   4915 H HA     . ALA   B 1 65  ? 13.29000  32.06300  -57.09400 1.000 32.22000  ? 31  ALA   B HA     1 
ATOM   4916 H HB1    . ALA   B 1 65  ? 13.47700  31.33300  -59.31200 1.000 40.39000  ? 31  ALA   B HB1    1 
ATOM   4917 H HB2    . ALA   B 1 65  ? 14.57100  30.62000  -58.40700 1.000 40.39000  ? 31  ALA   B HB2    1 
ATOM   4918 H HB3    . ALA   B 1 65  ? 13.25800  29.83300  -58.83500 1.000 40.39000  ? 31  ALA   B HB3    1 
ATOM   4919 N N      . ALA   B 1 66  ? 10.65900  30.31600  -57.54100 1.000 31.50000  ? 32  ALA   B N      1 
ATOM   4920 C CA     . ALA   B 1 66  ? 9.21200   30.40500  -57.71900 1.000 35.66000  ? 32  ALA   B CA     1 
ATOM   4921 C C      . ALA   B 1 66  ? 8.56900   31.25200  -56.62200 1.000 35.99000  ? 32  ALA   B C      1 
ATOM   4922 O O      . ALA   B 1 66  ? 7.65200   32.04500  -56.89400 1.000 30.99000  ? 32  ALA   B O      1 
ATOM   4923 C CB     . ALA   B 1 66  ? 8.60300   28.99700  -57.74300 1.000 36.21000  ? 32  ALA   B CB     1 
ATOM   4924 H H      . ALA   B 1 66  ? 10.94800  29.52000  -57.39300 1.000 31.50000  ? 32  ALA   B H      1 
ATOM   4925 H HA     . ALA   B 1 66  ? 9.02400   30.82700  -58.57200 1.000 35.66000  ? 32  ALA   B HA     1 
ATOM   4926 H HB1    . ALA   B 1 66  ? 7.63700   29.07200  -57.77900 1.000 36.21000  ? 32  ALA   B HB1    1 
ATOM   4927 H HB2    . ALA   B 1 66  ? 8.92800   28.52700  -58.52700 1.000 36.21000  ? 32  ALA   B HB2    1 
ATOM   4928 H HB3    . ALA   B 1 66  ? 8.87500   28.52800  -56.94000 1.000 36.21000  ? 32  ALA   B HB3    1 
ATOM   4929 N N      . MET   B 1 67  ? 9.02700   31.09200  -55.37200 1.000 33.03000  ? 33  MET   B N      1 
ATOM   4930 C CA     . MET   B 1 67  ? 8.50700   31.93800  -54.29500 1.000 29.74000  ? 33  MET   B CA     1 
ATOM   4931 C C      . MET   B 1 67  ? 8.87700   33.40200  -54.51500 1.000 30.05000  ? 33  MET   B C      1 
ATOM   4932 O O      . MET   B 1 67  ? 8.06900   34.30400  -54.24700 1.000 34.99000  ? 33  MET   B O      1 
ATOM   4933 C CB     . MET   B 1 67  ? 9.01600   31.44500  -52.93000 1.000 27.83000  ? 33  MET   B CB     1 
ATOM   4934 C CG     . MET   B 1 67  ? 8.27400   30.23800  -52.35900 1.000 29.76000  ? 33  MET   B CG     1 
ATOM   4935 S SD     . MET   B 1 67  ? 6.52600   30.58600  -51.97500 1.000 32.49000  ? 33  MET   B SD     1 
ATOM   4936 C CE     . MET   B 1 67  ? 6.60800   32.17500  -51.18000 1.000 27.23000  ? 33  MET   B CE     1 
ATOM   4937 H H      . MET   B 1 67  ? 9.62000   30.51800  -55.13000 1.000 33.03000  ? 33  MET   B H      1 
ATOM   4938 H HA     . MET   B 1 67  ? 7.54000   31.86600  -54.29000 1.000 29.74000  ? 33  MET   B HA     1 
ATOM   4939 H HB2    . MET   B 1 67  ? 9.94600   31.18700  -53.03100 1.000 27.83000  ? 33  MET   B HB2    1 
ATOM   4940 H HB3    . MET   B 1 67  ? 8.95500   32.17100  -52.29100 1.000 27.83000  ? 33  MET   B HB3    1 
ATOM   4941 H HG2    . MET   B 1 67  ? 8.29900   29.51900  -53.00900 1.000 29.76000  ? 33  MET   B HG2    1 
ATOM   4942 H HG3    . MET   B 1 67  ? 8.71000   29.95900  -51.53900 1.000 29.76000  ? 33  MET   B HG3    1 
ATOM   4943 H HE1    . MET   B 1 67  ? 5.74800   32.37100  -50.77600 1.000 27.23000  ? 33  MET   B HE1    1 
ATOM   4944 H HE2    . MET   B 1 67  ? 7.29600   32.15000  -50.49700 1.000 27.23000  ? 33  MET   B HE2    1 
ATOM   4945 H HE3    . MET   B 1 67  ? 6.82400   32.84900  -51.84300 1.000 27.23000  ? 33  MET   B HE3    1 
ATOM   4946 N N      . THR   B 1 68  ? 10.09800  33.65800  -55.01000 1.000 30.91000  ? 34  THR   B N      1 
ATOM   4947 C CA     . THR   B 1 68  ? 10.52100  35.03700  -55.25800 1.000 30.90000  ? 34  THR   B CA     1 
ATOM   4948 C C      . THR   B 1 68  ? 9.70300   35.67100  -56.38400 1.000 30.91000  ? 34  THR   B C      1 
ATOM   4949 O O      . THR   B 1 68  ? 9.31500   36.84600  -56.29800 1.000 31.93000  ? 34  THR   B O      1 
ATOM   4950 C CB     . THR   B 1 68  ? 12.03300  35.07500  -55.57100 1.000 34.07000  ? 34  THR   B CB     1 
ATOM   4951 O OG1    . THR   B 1 68  ? 12.76100  34.52300  -54.47500 1.000 35.11000  ? 34  THR   B OG1    1 
ATOM   4952 C CG2    . THR   B 1 68  ? 12.53700  36.51000  -55.77700 1.000 33.50000  ? 34  THR   B CG2    1 
ATOM   4953 H H      . THR   B 1 68  ? 10.68600  33.06100  -55.20600 1.000 30.91000  ? 34  THR   B H      1 
ATOM   4954 H HA     . THR   B 1 68  ? 10.37200  35.55900  -54.45400 1.000 30.90000  ? 34  THR   B HA     1 
ATOM   4955 H HB     . THR   B 1 68  ? 12.21400  34.56300  -56.37500 1.000 34.07000  ? 34  THR   B HB     1 
ATOM   4956 H HG1    . THR   B 1 68  ? 12.53000  33.72500  -54.34900 1.000 35.11000  ? 34  THR   B HG1    1 
ATOM   4957 H HG21   . THR   B 1 68  ? 13.50300  36.51100  -55.86300 1.000 33.50000  ? 34  THR   B HG21   1 
ATOM   4958 H HG22   . THR   B 1 68  ? 12.14900  36.88700  -56.58200 1.000 33.50000  ? 34  THR   B HG22   1 
ATOM   4959 H HG23   . THR   B 1 68  ? 12.28800  37.06100  -55.01800 1.000 33.50000  ? 34  THR   B HG23   1 
ATOM   4960 N N      . GLU   B 1 69  ? 9.42600   34.91000  -57.44300 0.910 31.04000  ? 35  GLU   B N      1 
ATOM   4961 C CA     . GLU   B 1 69  ? 8.63000   35.41800  -58.55700 0.910 30.41000  ? 35  GLU   B CA     1 
ATOM   4962 C C      . GLU   B 1 69  ? 7.15200   35.55900  -58.20600 0.910 32.68000  ? 35  GLU   B C      1 
ATOM   4963 O O      . GLU   B 1 69  ? 6.43700   36.27900  -58.90700 0.910 32.70000  ? 35  GLU   B O      1 
ATOM   4964 C CB     . GLU   B 1 69  ? 8.79800   34.48600  -59.77100 0.910 32.96000  ? 35  GLU   B CB     1 
ATOM   4965 C CG     . GLU   B 1 69  ? 10.24600  34.41000  -60.27300 0.910 41.28000  ? 35  GLU   B CG     1 
ATOM   4966 C CD     . GLU   B 1 69  ? 10.51800  33.18200  -61.15000 0.910 67.53000  ? 35  GLU   B CD     1 
ATOM   4967 O OE1    . GLU   B 1 69  ? 9.56600   32.42000  -61.43800 0.910 70.86000  ? 35  GLU   B OE1    1 
ATOM   4968 O OE2    . GLU   B 1 69  ? 11.69700  32.95900  -61.52000 0.910 66.46000  ? 35  GLU   B OE2    1 
ATOM   4969 H H      . GLU   B 1 69  ? 9.68800   34.09600  -57.54000 0.910 31.04000  ? 35  GLU   B H      1 
ATOM   4970 H HA     . GLU   B 1 69  ? 8.96200   36.29500  -58.80600 0.910 30.41000  ? 35  GLU   B HA     1 
ATOM   4971 H HB2    . GLU   B 1 69  ? 8.52000   33.59100  -59.52100 0.910 32.96000  ? 35  GLU   B HB2    1 
ATOM   4972 H HB3    . GLU   B 1 69  ? 8.24600   34.81300  -60.49800 0.910 32.96000  ? 35  GLU   B HB3    1 
ATOM   4973 H HG2    . GLU   B 1 69  ? 10.43600  35.20100  -60.80100 0.910 41.28000  ? 35  GLU   B HG2    1 
ATOM   4974 H HG3    . GLU   B 1 69  ? 10.84500  34.37100  -59.51100 0.910 41.28000  ? 35  GLU   B HG3    1 
ATOM   4975 N N      . SER   B 1 70  ? 6.67600   34.88100  -57.15700 1.000 32.28000  ? 36  SER   B N      1 
ATOM   4976 C CA     . SER   B 1 70  ? 5.27000   34.94000  -56.75500 1.000 30.61000  ? 36  SER   B CA     1 
ATOM   4977 C C      . SER   B 1 70  ? 4.94300   36.32100  -56.20100 1.000 30.12000  ? 36  SER   B C      1 
ATOM   4978 O O      . SER   B 1 70  ? 5.82100   37.17500  -56.04200 1.000 31.55000  ? 36  SER   B O      1 
ATOM   4979 C CB     . SER   B 1 70  ? 4.96700   33.87800  -55.69600 1.000 32.26000  ? 36  SER   B CB     1 
ATOM   4980 O OG     . SER   B 1 70  ? 5.30500   34.37100  -54.38800 1.000 28.75000  ? 36  SER   B OG     1 
ATOM   4981 H H      . SER   B 1 70  ? 7.15600   34.37300  -56.65600 1.000 32.28000  ? 36  SER   B H      1 
ATOM   4982 H HA     . SER   B 1 70  ? 4.70500   34.77600  -57.52600 1.000 30.61000  ? 36  SER   B HA     1 
ATOM   4983 H HB2    . SER   B 1 70  ? 4.02100   33.66500  -55.72100 1.000 32.26000  ? 36  SER   B HB2    1 
ATOM   4984 H HB3    . SER   B 1 70  ? 5.49300   33.08400  -55.88200 1.000 32.26000  ? 36  SER   B HB3    1 
ATOM   4985 H HG     . SER   B 1 70  ? 6.12200   34.56100  -54.35500 1.000 28.75000  ? 36  SER   B HG     1 
ATOM   4986 N N      . THR   B 1 71  ? 3.66600   36.54200  -55.87200 1.000 28.00000  ? 37  THR   B N      1 
ATOM   4987 C CA     . THR   B 1 71  ? 3.26300   37.82500  -55.29600 1.000 30.37000  ? 37  THR   B CA     1 
ATOM   4988 C C      . THR   B 1 71  ? 3.38000   37.86100  -53.76800 1.000 30.22000  ? 37  THR   B C      1 
ATOM   4989 O O      . THR   B 1 71  ? 2.98200   38.85300  -53.15900 1.000 31.75000  ? 37  THR   B O      1 
ATOM   4990 C CB     . THR   B 1 71  ? 1.83100   38.20500  -55.70900 1.000 32.38000  ? 37  THR   B CB     1 
ATOM   4991 O OG1    . THR   B 1 71  ? 0.90300   37.24000  -55.21400 1.000 34.67000  ? 37  THR   B OG1    1 
ATOM   4992 C CG2    . THR   B 1 71  ? 1.70300   38.31200  -57.22000 1.000 35.41000  ? 37  THR   B CG2    1 
ATOM   4993 H H      . THR   B 1 71  ? 3.02600   35.97600  -55.97100 1.000 28.00000  ? 37  THR   B H      1 
ATOM   4994 H HA     . THR   B 1 71  ? 3.85100   38.51300  -55.64400 1.000 30.37000  ? 37  THR   B HA     1 
ATOM   4995 H HB     . THR   B 1 71  ? 1.61500   39.07100  -55.33000 1.000 32.38000  ? 37  THR   B HB     1 
ATOM   4996 H HG1    . THR   B 1 71  ? 0.92100   37.22700  -54.37400 1.000 34.67000  ? 37  THR   B HG1    1 
ATOM   4997 H HG21   . THR   B 1 71  ? 0.80000   38.57600  -57.45800 1.000 35.41000  ? 37  THR   B HG21   1 
ATOM   4998 H HG22   . THR   B 1 71  ? 2.32500   38.97500  -57.55900 1.000 35.41000  ? 37  THR   B HG22   1 
ATOM   4999 H HG23   . THR   B 1 71  ? 1.90000   37.45600  -57.63100 1.000 35.41000  ? 37  THR   B HG23   1 
ATOM   5000 N N      . SER   B 1 72  ? 3.96100   36.84200  -53.14000 1.000 28.59000  ? 38  SER   B N      1 
ATOM   5001 C CA     . SER   B 1 72  ? 4.10200   36.86400  -51.68400 1.000 27.74000  ? 38  SER   B CA     1 
ATOM   5002 C C      . SER   B 1 72  ? 4.93600   38.06100  -51.22400 1.000 26.34000  ? 38  SER   B C      1 
ATOM   5003 O O      . SER   B 1 72  ? 5.83800   38.53700  -51.92400 1.000 28.39000  ? 38  SER   B O      1 
ATOM   5004 C CB     . SER   B 1 72  ? 4.76800   35.57400  -51.17300 1.000 28.49000  ? 38  SER   B CB     1 
ATOM   5005 O OG     . SER   B 1 72  ? 6.12300   35.54800  -51.57500 1.000 28.62000  ? 38  SER   B OG     1 
ATOM   5006 H H      . SER   B 1 72  ? 4.27700   36.13900  -53.52200 1.000 28.59000  ? 38  SER   B H      1 
ATOM   5007 H HA     . SER   B 1 72  ? 3.22300   36.93300  -51.27900 1.000 27.74000  ? 38  SER   B HA     1 
ATOM   5008 H HB2    . SER   B 1 72  ? 4.72100   35.55200  -50.20400 1.000 28.49000  ? 38  SER   B HB2    1 
ATOM   5009 H HB3    . SER   B 1 72  ? 4.30900   34.80700  -51.54800 1.000 28.49000  ? 38  SER   B HB3    1 
ATOM   5010 H HG     . SER   B 1 72  ? 6.50300   34.86900  -51.25900 1.000 28.62000  ? 38  SER   B HG     1 
ATOM   5011 N N      . GLY   B 1 73  ? 4.63600   38.53300  -50.01400 1.000 26.29000  ? 39  GLY   B N      1 
ATOM   5012 C CA     . GLY   B 1 73  ? 5.41100   39.63000  -49.44400 1.000 25.76000  ? 39  GLY   B CA     1 
ATOM   5013 C C      . GLY   B 1 73  ? 6.81500   39.21500  -49.04200 1.000 26.51000  ? 39  GLY   B C      1 
ATOM   5014 O O      . GLY   B 1 73  ? 7.72900   40.04600  -49.00600 1.000 27.27000  ? 39  GLY   B O      1 
ATOM   5015 H H      . GLY   B 1 73  ? 4.00100   38.24100  -49.51300 1.000 26.29000  ? 39  GLY   B H      1 
ATOM   5016 H HA2    . GLY   B 1 73  ? 5.47800   40.34800  -50.09300 1.000 25.76000  ? 39  GLY   B HA2    1 
ATOM   5017 H HA3    . GLY   B 1 73  ? 4.95600   39.97000  -48.65800 1.000 25.76000  ? 39  GLY   B HA3    1 
ATOM   5018 N N      . SER   B 1 74  ? 7.01800   37.93100  -48.75300 1.000 26.22000  ? 40  SER   B N      1 
ATOM   5019 C CA     . SER   B 1 74  ? 8.33500   37.44700  -48.37900 1.000 27.17000  ? 40  SER   B CA     1 
ATOM   5020 C C      . SER   B 1 74  ? 8.39300   35.94000  -48.62400 1.000 26.24000  ? 40  SER   B C      1 
ATOM   5021 O O      . SER   B 1 74  ? 7.46800   35.34500  -49.19400 1.000 25.59000  ? 40  SER   B O      1 
ATOM   5022 C CB     . SER   B 1 74  ? 8.64800   37.80100  -46.91500 1.000 26.59000  ? 40  SER   B CB     1 
ATOM   5023 O OG     . SER   B 1 74  ? 10.01600  37.56300  -46.62500 1.000 28.51000  ? 40  SER   B OG     1 
ATOM   5024 H H      . SER   B 1 74  ? 6.40900   37.32400  -48.76700 1.000 26.22000  ? 40  SER   B H      1 
ATOM   5025 H HA     . SER   B 1 74  ? 9.00200   37.87100  -48.94200 1.000 27.17000  ? 40  SER   B HA     1 
ATOM   5026 H HB2    . SER   B 1 74  ? 8.45200   38.73900  -46.76800 1.000 26.59000  ? 40  SER   B HB2    1 
ATOM   5027 H HB3    . SER   B 1 74  ? 8.10100   37.25100  -46.33200 1.000 26.59000  ? 40  SER   B HB3    1 
ATOM   5028 H HG     . SER   B 1 74  ? 10.50100  38.03300  -47.12400 1.000 28.51000  ? 40  SER   B HG     1 
ATOM   5029 N N      . LEU   B 1 75  ? 9.49600   35.33200  -48.19200 1.000 27.92000  ? 41  LEU   B N      1 
ATOM   5030 C CA     . LEU   B 1 75  ? 9.67200   33.88500  -48.28200 1.000 30.06000  ? 41  LEU   B CA     1 
ATOM   5031 C C      . LEU   B 1 75  ? 10.71800  33.46100  -47.26600 1.000 29.36000  ? 41  LEU   B C      1 
ATOM   5032 O O      . LEU   B 1 75  ? 11.52400  34.27100  -46.80600 1.000 27.94000  ? 41  LEU   B O      1 
ATOM   5033 C CB     . LEU   B 1 75  ? 10.08400  33.44400  -49.69500 1.000 29.93000  ? 41  LEU   B CB     1 
ATOM   5034 C CG     . LEU   B 1 75  ? 11.55500  33.66500  -50.05200 1.000 34.65000  ? 41  LEU   B CG     1 
ATOM   5035 C CD1    . LEU   B 1 75  ? 11.93500  32.95600  -51.34300 1.000 30.49000  ? 41  LEU   B CD1    1 
ATOM   5036 C CD2    . LEU   B 1 75  ? 11.86200  35.15300  -50.16900 1.000 31.88000  ? 41  LEU   B CD2    1 
ATOM   5037 H H      . LEU   B 1 75  ? 10.16400  35.74100  -47.83800 1.000 27.92000  ? 41  LEU   B H      1 
ATOM   5038 H HA     . LEU   B 1 75  ? 8.83500   33.45000  -48.05800 1.000 30.06000  ? 41  LEU   B HA     1 
ATOM   5039 H HB2    . LEU   B 1 75  ? 9.90200   32.49500  -49.78500 1.000 29.93000  ? 41  LEU   B HB2    1 
ATOM   5040 H HB3    . LEU   B 1 75  ? 9.55100   33.93800  -50.33800 1.000 29.93000  ? 41  LEU   B HB3    1 
ATOM   5041 H HG     . LEU   B 1 75  ? 12.12100  33.30000  -49.35600 1.000 34.65000  ? 41  LEU   B HG     1 
ATOM   5042 H HD11   . LEU   B 1 75  ? 12.87200  33.12200  -51.53000 1.000 30.49000  ? 41  LEU   B HD11   1 
ATOM   5043 H HD12   . LEU   B 1 75  ? 11.78200  32.00400  -51.23700 1.000 30.49000  ? 41  LEU   B HD12   1 
ATOM   5044 H HD13   . LEU   B 1 75  ? 11.38700  33.30100  -52.06500 1.000 30.49000  ? 41  LEU   B HD13   1 
ATOM   5045 H HD21   . LEU   B 1 75  ? 12.79000  35.25600  -50.42600 1.000 31.88000  ? 41  LEU   B HD21   1 
ATOM   5046 H HD22   . LEU   B 1 75  ? 11.28300  35.54500  -50.84100 1.000 31.88000  ? 41  LEU   B HD22   1 
ATOM   5047 H HD23   . LEU   B 1 75  ? 11.71300  35.57800  -49.31100 1.000 31.88000  ? 41  LEU   B HD23   1 
ATOM   5048 N N      . ILE   B 1 76  ? 10.71200  32.17300  -46.93000 1.000 26.23000  ? 42  ILE   B N      1 
ATOM   5049 C CA     . ILE   B 1 76  ? 11.64500  31.62700  -45.95300 1.000 24.43000  ? 42  ILE   B CA     1 
ATOM   5050 C C      . ILE   B 1 76  ? 12.18700  30.31400  -46.49900 1.000 28.19000  ? 42  ILE   B C      1 
ATOM   5051 O O      . ILE   B 1 76  ? 11.48800  29.57600  -47.20100 1.000 27.82000  ? 42  ILE   B O      1 
ATOM   5052 C CB     . ILE   B 1 76  ? 10.97700  31.43100  -44.56600 1.000 24.81000  ? 42  ILE   B CB     1 
ATOM   5053 C CG1    . ILE   B 1 76  ? 11.99900  30.98700  -43.49800 1.000 28.53000  ? 42  ILE   B CG1    1 
ATOM   5054 C CG2    . ILE   B 1 76  ? 9.81100   30.46800  -44.66100 1.000 25.31000  ? 42  ILE   B CG2    1 
ATOM   5055 C CD1    . ILE   B 1 76  ? 11.47200  31.16400  -42.05700 1.000 29.01000  ? 42  ILE   B CD1    1 
ATOM   5056 H H      . ILE   B 1 76  ? 10.17100  31.59100  -47.25800 1.000 26.23000  ? 42  ILE   B H      1 
ATOM   5057 H HA     . ILE   B 1 76  ? 12.38800  32.23900  -45.84600 1.000 24.43000  ? 42  ILE   B HA     1 
ATOM   5058 H HB     . ILE   B 1 76  ? 10.62300  32.29100  -44.29000 1.000 24.81000  ? 42  ILE   B HB     1 
ATOM   5059 H HG12   . ILE   B 1 76  ? 12.20500  30.04800  -43.62900 1.000 28.53000  ? 42  ILE   B HG12   1 
ATOM   5060 H HG13   . ILE   B 1 76  ? 12.80400  31.52000  -43.59000 1.000 28.53000  ? 42  ILE   B HG13   1 
ATOM   5061 H HG21   . ILE   B 1 76  ? 9.36000   30.43300  -43.80300 1.000 25.31000  ? 42  ILE   B HG21   1 
ATOM   5062 H HG22   . ILE   B 1 76  ? 9.19700   30.78100  -45.34300 1.000 25.31000  ? 42  ILE   B HG22   1 
ATOM   5063 H HG23   . ILE   B 1 76  ? 10.14400  29.58800  -44.89500 1.000 25.31000  ? 42  ILE   B HG23   1 
ATOM   5064 H HD11   . ILE   B 1 76  ? 12.17500  30.92700  -41.43300 1.000 29.01000  ? 42  ILE   B HD11   1 
ATOM   5065 H HD12   . ILE   B 1 76  ? 11.21300  32.09000  -41.92800 1.000 29.01000  ? 42  ILE   B HD12   1 
ATOM   5066 H HD13   . ILE   B 1 76  ? 10.70500  30.58500  -41.92800 1.000 29.01000  ? 42  ILE   B HD13   1 
ATOM   5067 N N      . THR   B 1 77  ? 13.45000  30.03600  -46.19600 1.000 26.20000  ? 43  THR   B N      1 
ATOM   5068 C CA     . THR   B 1 77  ? 14.03200  28.78100  -46.66300 1.000 29.50000  ? 43  THR   B CA     1 
ATOM   5069 C C      . THR   B 1 77  ? 13.57800  27.59500  -45.80000 1.000 35.72000  ? 43  THR   B C      1 
ATOM   5070 O O      . THR   B 1 77  ? 13.06100  27.73500  -44.68400 1.000 31.48000  ? 43  THR   B O      1 
ATOM   5071 C CB     . THR   B 1 77  ? 15.55800  28.84900  -46.64600 1.000 30.57000  ? 43  THR   B CB     1 
ATOM   5072 O OG1    . THR   B 1 77  ? 16.00600  29.01100  -45.29100 1.000 34.23000  ? 43  THR   B OG1    1 
ATOM   5073 C CG2    . THR   B 1 77  ? 16.08400  30.02400  -47.50000 1.000 35.11000  ? 43  THR   B CG2    1 
ATOM   5074 H H      . THR   B 1 77  ? 13.97700  30.53700  -45.73700 1.000 26.20000  ? 43  THR   B H      1 
ATOM   5075 H HA     . THR   B 1 77  ? 13.74700  28.61800  -47.57600 1.000 29.50000  ? 43  THR   B HA     1 
ATOM   5076 H HB     . THR   B 1 77  ? 15.92000  28.02400  -47.00700 1.000 30.57000  ? 43  THR   B HB     1 
ATOM   5077 H HG1    . THR   B 1 77  ? 16.82500  28.83500  -45.23900 1.000 34.23000  ? 43  THR   B HG1    1 
ATOM   5078 H HG21   . THR   B 1 77  ? 17.05400  30.02200  -47.50400 1.000 35.11000  ? 43  THR   B HG21   1 
ATOM   5079 H HG22   . THR   B 1 77  ? 15.76500  29.93900  -48.41200 1.000 35.11000  ? 43  THR   B HG22   1 
ATOM   5080 H HG23   . THR   B 1 77  ? 15.77200  30.86600  -47.13400 1.000 35.11000  ? 43  THR   B HG23   1 
ATOM   5081 N N      . LYS   B 1 78  ? 13.79600  26.39700  -46.33700 1.000 30.15000  ? 44  LYS   B N      1 
ATOM   5082 C CA     . LYS   B 1 78  ? 13.63600  25.17600  -45.56300 1.000 28.09000  ? 44  LYS   B CA     1 
ATOM   5083 C C      . LYS   B 1 78  ? 14.56100  25.20200  -44.34300 1.000 32.00000  ? 44  LYS   B C      1 
ATOM   5084 O O      . LYS   B 1 78  ? 15.71400  25.63200  -44.44200 1.000 34.12000  ? 44  LYS   B O      1 
ATOM   5085 C CB     . LYS   B 1 78  ? 13.94000  23.97300  -46.49300 1.000 29.14000  ? 44  LYS   B CB     1 
ATOM   5086 C CG     . LYS   B 1 78  ? 14.18700  22.63500  -45.80500 1.000 30.71000  ? 44  LYS   B CG     1 
ATOM   5087 C CD     . LYS   B 1 78  ? 12.89000  22.10900  -45.16600 1.000 35.92000  ? 44  LYS   B CD     1 
ATOM   5088 C CE     . LYS   B 1 78  ? 13.11000  20.83500  -44.29200 1.000 39.07000  ? 44  LYS   B CE     1 
ATOM   5089 N NZ     . LYS   B 1 78  ? 11.78100  20.27800  -43.75500 1.000 37.97000  ? 44  LYS   B NZ     1 
ATOM   5090 H H      . LYS   B 1 78  ? 14.03800  26.26700  -47.15200 1.000 30.15000  ? 44  LYS   B H      1 
ATOM   5091 H HA     . LYS   B 1 78  ? 12.71900  25.10400  -45.25400 1.000 28.09000  ? 44  LYS   B HA     1 
ATOM   5092 H HB2    . LYS   B 1 78  ? 13.18700  23.85400  -47.09300 1.000 29.14000  ? 44  LYS   B HB2    1 
ATOM   5093 H HB3    . LYS   B 1 78  ? 14.73300  24.18200  -47.01100 1.000 29.14000  ? 44  LYS   B HB3    1 
ATOM   5094 H HG2    . LYS   B 1 78  ? 14.48200  21.98800  -46.46500 1.000 30.71000  ? 44  LYS   B HG2    1 
ATOM   5095 H HG3    . LYS   B 1 78  ? 14.85700  22.73300  -45.11100 1.000 30.71000  ? 44  LYS   B HG3    1 
ATOM   5096 H HD2    . LYS   B 1 78  ? 12.51800  22.80000  -44.59600 1.000 35.92000  ? 44  LYS   B HD2    1 
ATOM   5097 H HD3    . LYS   B 1 78  ? 12.26100  21.88400  -45.86900 1.000 35.92000  ? 44  LYS   B HD3    1 
ATOM   5098 H HE2    . LYS   B 1 78  ? 13.52300  20.14800  -44.82900 1.000 39.07000  ? 44  LYS   B HE2    1 
ATOM   5099 H HE3    . LYS   B 1 78  ? 13.67700  21.06500  -43.54400 1.000 39.07000  ? 44  LYS   B HE3    1 
ATOM   5100 H HZ1    . LYS   B 1 78  ? 11.93300  19.55300  -43.26100 1.000 37.97000  ? 44  LYS   B HZ1    1 
ATOM   5101 H HZ2    . LYS   B 1 78  ? 11.37500  20.89100  -43.25300 1.000 37.97000  ? 44  LYS   B HZ2    1 
ATOM   5102 H HZ3    . LYS   B 1 78  ? 11.24700  20.05900  -44.43300 1.000 37.97000  ? 44  LYS   B HZ3    1 
ATOM   5103 N N      . SER   B 1 79  ? 14.06300  24.73700  -43.17900 1.000 28.91000  ? 45  SER   B N      1 
ATOM   5104 C CA     . SER   B 1 79  ? 14.92900  24.60100  -42.00000 1.000 30.76000  ? 45  SER   B CA     1 
ATOM   5105 C C      . SER   B 1 79  ? 16.13700  23.73000  -42.33600 1.000 32.34000  ? 45  SER   B C      1 
ATOM   5106 O O      . SER   B 1 79  ? 15.98400  22.62100  -42.85400 1.000 34.98000  ? 45  SER   B O      1 
ATOM   5107 C CB     . SER   B 1 79  ? 14.18000  23.96900  -40.82100 1.000 31.74000  ? 45  SER   B CB     1 
ATOM   5108 O OG     . SER   B 1 79  ? 13.20300  24.84800  -40.27300 1.000 35.10000  ? 45  SER   B OG     1 
ATOM   5109 H H      . SER   B 1 79  ? 13.24600  24.50000  -43.05300 1.000 28.91000  ? 45  SER   B H      1 
ATOM   5110 H HA     . SER   B 1 79  ? 15.24600  25.47600  -41.72900 1.000 30.76000  ? 45  SER   B HA     1 
ATOM   5111 H HB2    . SER   B 1 79  ? 13.73600  23.16400  -41.13000 1.000 31.74000  ? 45  SER   B HB2    1 
ATOM   5112 H HB3    . SER   B 1 79  ? 14.82100  23.74500  -40.12900 1.000 31.74000  ? 45  SER   B HB3    1 
ATOM   5113 H HG     . SER   B 1 79  ? 13.58100  25.45400  -39.83200 1.000 35.10000  ? 45  SER   B HG     1 
ATOM   5114 N N      . CYS   B 1 80  ? 17.33400  24.21800  -42.04100 1.000 32.75000  ? 46  CYS   B N      1 
ATOM   5115 C CA     . CYS   B 1 80  ? 18.52300  23.48700  -42.45300 1.000 34.90000  ? 46  CYS   B CA     1 
ATOM   5116 C C      . CYS   B 1 80  ? 19.36000  23.02900  -41.26100 1.000 42.40000  ? 46  CYS   B C      1 
ATOM   5117 O O      . CYS   B 1 80  ? 19.29600  23.56900  -40.15200 1.000 34.04000  ? 46  CYS   B O      1 
ATOM   5118 C CB     . CYS   B 1 80  ? 19.39400  24.32600  -43.39800 1.000 33.74000  ? 46  CYS   B CB     1 
ATOM   5119 S SG     . CYS   B 1 80  ? 19.98400  25.88600  -42.69300 1.000 40.11000  ? 46  CYS   B SG     1 
ATOM   5120 H H      . CYS   B 1 80  ? 17.48400  24.95000  -41.61500 1.000 32.75000  ? 46  CYS   B H      1 
ATOM   5121 H HA     . CYS   B 1 80  ? 18.25700  22.69300  -42.93900 1.000 34.90000  ? 46  CYS   B HA     1 
ATOM   5122 H HB2    . CYS   B 1 80  ? 20.17200  23.80400  -43.64900 1.000 33.74000  ? 46  CYS   B HB2    1 
ATOM   5123 H HB3    . CYS   B 1 80  ? 18.87500  24.53900  -44.18900 1.000 33.74000  ? 46  CYS   B HB3    1 
ATOM   5124 H HG     . CYS   B 1 80  ? 19.04600  26.56500  -42.38100 1.000 40.11000  ? 46  CYS   B HG     1 
ATOM   5125 N N      . THR   B 1 81  ? 20.15000  22.00400  -41.52300 1.000 35.62000  ? 47  THR   B N      1 
ATOM   5126 C CA     . THR   B 1 81  ? 21.14400  21.46000  -40.62000 1.000 37.91000  ? 47  THR   B CA     1 
ATOM   5127 C C      . THR   B 1 81  ? 22.53300  21.77400  -41.16300 1.000 42.30000  ? 47  THR   B C      1 
ATOM   5128 O O      . THR   B 1 81  ? 22.68400  22.20400  -42.31200 1.000 37.23000  ? 47  THR   B O      1 
ATOM   5129 C CB     . THR   B 1 81  ? 20.95000  19.94300  -40.46000 1.000 41.96000  ? 47  THR   B CB     1 
ATOM   5130 O OG1    . THR   B 1 81  ? 20.90200  19.31200  -41.74600 1.000 38.39000  ? 47  THR   B OG1    1 
ATOM   5131 C CG2    . THR   B 1 81  ? 19.64700  19.63800  -39.71100 1.000 41.17000  ? 47  THR   B CG2    1 
ATOM   5132 H H      . THR   B 1 81  ? 20.12400  21.58000  -42.27100 1.000 35.62000  ? 47  THR   B H      1 
ATOM   5133 H HA     . THR   B 1 81  ? 21.04800  21.87700  -39.75000 1.000 37.91000  ? 47  THR   B HA     1 
ATOM   5134 H HB     . THR   B 1 81  ? 21.68700  19.57300  -39.95000 1.000 41.96000  ? 47  THR   B HB     1 
ATOM   5135 H HG1    . THR   B 1 81  ? 21.62000  19.45000  -42.16100 1.000 38.39000  ? 47  THR   B HG1    1 
ATOM   5136 H HG21   . THR   B 1 81  ? 19.53700  18.67900  -39.61400 1.000 41.17000  ? 47  THR   B HG21   1 
ATOM   5137 H HG22   . THR   B 1 81  ? 19.66900  20.04300  -38.83000 1.000 41.17000  ? 47  THR   B HG22   1 
ATOM   5138 H HG23   . THR   B 1 81  ? 18.89100  19.99400  -40.20300 1.000 41.17000  ? 47  THR   B HG23   1 
ATOM   5139 N N      . PRO   B 1 82  ? 23.57700  21.61200  -40.34900 1.000 40.30000  ? 48  PRO   B N      1 
ATOM   5140 C CA     . PRO   B 1 82  ? 24.91900  21.97100  -40.83300 1.000 40.90000  ? 48  PRO   B CA     1 
ATOM   5141 C C      . PRO   B 1 82  ? 25.32400  21.19200  -42.07900 1.000 38.58000  ? 48  PRO   B C      1 
ATOM   5142 O O      . PRO   B 1 82  ? 25.97800  21.76700  -42.95900 1.000 48.01000  ? 48  PRO   B O      1 
ATOM   5143 C CB     . PRO   B 1 82  ? 25.82100  21.66800  -39.62700 1.000 40.00000  ? 48  PRO   B CB     1 
ATOM   5144 C CG     . PRO   B 1 82  ? 24.87700  21.73900  -38.42300 1.000 41.41000  ? 48  PRO   B CG     1 
ATOM   5145 C CD     . PRO   B 1 82  ? 23.56500  21.22800  -38.92600 1.000 39.27000  ? 48  PRO   B CD     1 
ATOM   5146 H HA     . PRO   B 1 82  ? 24.95900  22.92100  -41.02700 1.000 40.90000  ? 48  PRO   B HA     1 
ATOM   5147 H HB2    . PRO   B 1 82  ? 26.20200  20.78000  -39.71500 1.000 40.00000  ? 48  PRO   B HB2    1 
ATOM   5148 H HB3    . PRO   B 1 82  ? 26.51800  22.33900  -39.56000 1.000 40.00000  ? 48  PRO   B HB3    1 
ATOM   5149 H HG2    . PRO   B 1 82  ? 25.21400  21.17500  -37.70900 1.000 41.41000  ? 48  PRO   B HG2    1 
ATOM   5150 H HG3    . PRO   B 1 82  ? 24.79600  22.65900  -38.12500 1.000 41.41000  ? 48  PRO   B HG3    1 
ATOM   5151 H HD2    . PRO   B 1 82  ? 23.52200  20.26400  -38.83400 1.000 39.27000  ? 48  PRO   B HD2    1 
ATOM   5152 H HD3    . PRO   B 1 82  ? 22.83500  21.66400  -38.45900 1.000 39.27000  ? 48  PRO   B HD3    1 
ATOM   5153 N N      . ALA   B 1 83  ? 24.91900  19.92400  -42.19600 1.000 41.83000  ? 49  ALA   B N      1 
ATOM   5154 C CA     . ALA   B 1 83  ? 25.18800  19.08500  -43.35900 1.000 40.11000  ? 49  ALA   B CA     1 
ATOM   5155 C C      . ALA   B 1 83  ? 23.89100  18.69200  -44.05500 1.000 41.86000  ? 49  ALA   B C      1 
ATOM   5156 O O      . ALA   B 1 83  ? 22.81400  18.67400  -43.45400 1.000 36.95000  ? 49  ALA   B O      1 
ATOM   5157 C CB     . ALA   B 1 83  ? 25.94200  17.80300  -42.96800 1.000 44.31000  ? 49  ALA   B CB     1 
ATOM   5158 H H      . ALA   B 1 83  ? 24.46900  19.51600  -41.58700 1.000 41.83000  ? 49  ALA   B H      1 
ATOM   5159 H HA     . ALA   B 1 83  ? 25.73500  19.57700  -43.99100 1.000 40.11000  ? 49  ALA   B HA     1 
ATOM   5160 H HB1    . ALA   B 1 83  ? 26.10100  17.27500  -43.76600 1.000 44.31000  ? 49  ALA   B HB1    1 
ATOM   5161 H HB2    . ALA   B 1 83  ? 26.78700  18.04700  -42.55800 1.000 44.31000  ? 49  ALA   B HB2    1 
ATOM   5162 H HB3    . ALA   B 1 83  ? 25.40200  17.29900  -42.33900 1.000 44.31000  ? 49  ALA   B HB3    1 
ATOM   5163 N N      . LEU   B 1 84  ? 24.01800  18.34200  -45.33400 1.000 39.62000  ? 50  LEU   B N      1 
ATOM   5164 C CA     . LEU   B 1 84  ? 22.89300  17.82700  -46.10100 1.000 36.70000  ? 50  LEU   B CA     1 
ATOM   5165 C C      . LEU   B 1 84  ? 22.29400  16.59400  -45.42800 1.000 40.87000  ? 50  LEU   B C      1 
ATOM   5166 O O      . LEU   B 1 84  ? 23.00200  15.78700  -44.82400 1.000 40.55000  ? 50  LEU   B O      1 
ATOM   5167 C CB     . LEU   B 1 84  ? 23.35200  17.47500  -47.52100 1.000 43.76000  ? 50  LEU   B CB     1 
ATOM   5168 C CG     . LEU   B 1 84  ? 22.34400  16.85900  -48.49000 1.000 48.55000  ? 50  LEU   B CG     1 
ATOM   5169 C CD1    . LEU   B 1 84  ? 22.56800  17.38400  -49.90700 1.000 42.64000  ? 50  LEU   B CD1    1 
ATOM   5170 C CD2    . LEU   B 1 84  ? 22.45600  15.33700  -48.45600 1.000 46.23000  ? 50  LEU   B CD2    1 
ATOM   5171 H H      . LEU   B 1 84  ? 24.75100  18.39500  -45.78100 1.000 39.62000  ? 50  LEU   B H      1 
ATOM   5172 H HA     . LEU   B 1 84  ? 22.20500  18.50800  -46.16100 1.000 36.70000  ? 50  LEU   B HA     1 
ATOM   5173 H HB2    . LEU   B 1 84  ? 23.67500  18.29000  -47.93500 1.000 43.76000  ? 50  LEU   B HB2    1 
ATOM   5174 H HB3    . LEU   B 1 84  ? 24.08800  16.84800  -47.44600 1.000 43.76000  ? 50  LEU   B HB3    1 
ATOM   5175 H HG     . LEU   B 1 84  ? 21.44600  17.10300  -48.21500 1.000 48.55000  ? 50  LEU   B HG     1 
ATOM   5176 H HD11   . LEU   B 1 84  ? 22.17900  16.76200  -50.54100 1.000 42.64000  ? 50  LEU   B HD11   1 
ATOM   5177 H HD12   . LEU   B 1 84  ? 22.14600  18.25300  -49.99300 1.000 42.64000  ? 50  LEU   B HD12   1 
ATOM   5178 H HD13   . LEU   B 1 84  ? 23.52200  17.46100  -50.06100 1.000 42.64000  ? 50  LEU   B HD13   1 
ATOM   5179 H HD21   . LEU   B 1 84  ? 21.84000  14.96200  -49.10500 1.000 46.23000  ? 50  LEU   B HD21   1 
ATOM   5180 H HD22   . LEU   B 1 84  ? 23.36500  15.08200  -48.68000 1.000 46.23000  ? 50  LEU   B HD22   1 
ATOM   5181 H HD23   . LEU   B 1 84  ? 22.23200  15.01900  -47.56800 1.000 46.23000  ? 50  LEU   B HD23   1 
ATOM   5182 N N      . ARG   B 1 85  ? 20.97700  16.43600  -45.57400 1.000 37.35000  ? 51  ARG   B N      1 
ATOM   5183 C CA     . ARG   B 1 85  ? 20.24400  15.28300  -45.06000 1.000 39.47000  ? 51  ARG   B CA     1 
ATOM   5184 C C      . ARG   B 1 85  ? 19.17800  14.86500  -46.06000 1.000 45.82000  ? 51  ARG   B C      1 
ATOM   5185 O O      . ARG   B 1 85  ? 18.49900  15.71400  -46.64500 1.000 44.72000  ? 51  ARG   B O      1 
ATOM   5186 C CB     . ARG   B 1 85  ? 19.55700  15.58800  -43.71700 1.000 44.29000  ? 51  ARG   B CB     1 
ATOM   5187 C CG     . ARG   B 1 85  ? 20.49800  15.80200  -42.55900 1.000 46.68000  ? 51  ARG   B CG     1 
ATOM   5188 C CD     . ARG   B 1 85  ? 19.72700  16.34300  -41.36700 1.000 58.03000  ? 51  ARG   B CD     1 
ATOM   5189 N NE     . ARG   B 1 85  ? 18.59800  15.48900  -41.01400 1.000 60.48000  ? 51  ARG   B NE     1 
ATOM   5190 C CZ     . ARG   B 1 85  ? 18.71000  14.38200  -40.29300 1.000 66.46000  ? 51  ARG   B CZ     1 
ATOM   5191 N NH1    . ARG   B 1 85  ? 19.88500  13.96900  -39.83800 1.000 60.34000  ? 51  ARG   B NH1    1 
ATOM   5192 N NH2    . ARG   B 1 85  ? 17.61800  13.67400  -40.02000 1.000 64.30000  ? 51  ARG   B NH2    1 
ATOM   5193 H H      . ARG   B 1 85  ? 20.47400  17.00300  -45.98000 1.000 37.35000  ? 51  ARG   B H      1 
ATOM   5194 H HA     . ARG   B 1 85  ? 20.85500  14.54000  -44.93200 1.000 39.47000  ? 51  ARG   B HA     1 
ATOM   5195 H HB2    . ARG   B 1 85  ? 19.02700  16.39400  -43.81700 1.000 44.29000  ? 51  ARG   B HB2    1 
ATOM   5196 H HB3    . ARG   B 1 85  ? 18.97800  14.84300  -43.49200 1.000 44.29000  ? 51  ARG   B HB3    1 
ATOM   5197 H HG2    . ARG   B 1 85  ? 20.90400  14.95700  -42.30800 1.000 46.68000  ? 51  ARG   B HG2    1 
ATOM   5198 H HG3    . ARG   B 1 85  ? 21.17800  16.44800  -42.80700 1.000 46.68000  ? 51  ARG   B HG3    1 
ATOM   5199 H HD2    . ARG   B 1 85  ? 20.31900  16.40100  -40.60100 1.000 58.03000  ? 51  ARG   B HD2    1 
ATOM   5200 H HD3    . ARG   B 1 85  ? 19.38100  17.22200  -41.58700 1.000 58.03000  ? 51  ARG   B HD3    1 
ATOM   5201 H HE     . ARG   B 1 85  ? 17.83700  15.65700  -41.37800 1.000 60.48000  ? 51  ARG   B HE     1 
ATOM   5202 H HH11   . ARG   B 1 85  ? 20.59800  14.41800  -40.00800 1.000 60.34000  ? 51  ARG   B HH11   1 
ATOM   5203 H HH12   . ARG   B 1 85  ? 19.93400  13.24800  -39.37200 1.000 60.34000  ? 51  ARG   B HH12   1 
ATOM   5204 H HH21   . ARG   B 1 85  ? 16.85200  13.93500  -40.31100 1.000 64.30000  ? 51  ARG   B HH21   1 
ATOM   5205 H HH22   . ARG   B 1 85  ? 17.67800  12.95400  -39.55300 1.000 64.30000  ? 51  ARG   B HH22   1 
ATOM   5206 N N      . GLU   B 1 86  ? 19.00600  13.54700  -46.21500 1.000 55.19000  ? 52  GLU   B N      1 
ATOM   5207 C CA     . GLU   B 1 86  ? 17.97900  13.00700  -47.10000 1.000 55.89000  ? 52  GLU   B CA     1 
ATOM   5208 C C      . GLU   B 1 86  ? 16.59800  12.90500  -46.44600 1.000 66.97000  ? 52  GLU   B C      1 
ATOM   5209 O O      . GLU   B 1 86  ? 15.60400  12.76000  -47.16600 1.000 65.26000  ? 52  GLU   B O      1 
ATOM   5210 C CB     . GLU   B 1 86  ? 18.39800  11.62600  -47.60200 1.000 60.27000  ? 52  GLU   B CB     1 
ATOM   5211 C CG     . GLU   B 1 86  ? 19.88400  11.47300  -47.82500 1.000 56.31000  ? 52  GLU   B CG     1 
ATOM   5212 C CD     . GLU   B 1 86  ? 20.33900  11.94200  -49.19200 1.000 70.61000  ? 52  GLU   B CD     1 
ATOM   5213 O OE1    . GLU   B 1 86  ? 19.48900  12.40100  -49.98900 1.000 79.46000  ? 52  GLU   B OE1    1 
ATOM   5214 O OE2    . GLU   B 1 86  ? 21.55600  11.83800  -49.47000 1.000 75.46000  ? 52  GLU   B OE2    1 
ATOM   5215 H H      . GLU   B 1 86  ? 19.46300  12.95100  -45.79800 1.000 55.19000  ? 52  GLU   B H      1 
ATOM   5216 H HA     . GLU   B 1 86  ? 17.89700  13.58900  -47.87200 1.000 55.89000  ? 52  GLU   B HA     1 
ATOM   5217 H HB2    . GLU   B 1 86  ? 18.13100  10.96500  -46.94500 1.000 60.27000  ? 52  GLU   B HB2    1 
ATOM   5218 H HB3    . GLU   B 1 86  ? 17.94800  11.44900  -48.44300 1.000 60.27000  ? 52  GLU   B HB3    1 
ATOM   5219 H HG2    . GLU   B 1 86  ? 20.39900  11.95000  -47.16100 1.000 56.31000  ? 52  GLU   B HG2    1 
ATOM   5220 H HG3    . GLU   B 1 86  ? 20.09700  10.52800  -47.76700 1.000 56.31000  ? 52  GLU   B HG3    1 
ATOM   5221 N N      . GLY   B 1 87  ? 16.50500  12.95800  -45.11200 1.000 68.88000  ? 53  GLY   B N      1 
ATOM   5222 C CA     . GLY   B 1 87  ? 15.21300  12.90400  -44.42500 1.000 62.97000  ? 53  GLY   B CA     1 
ATOM   5223 C C      . GLY   B 1 87  ? 14.69900  11.50000  -44.14500 1.000 82.18000  ? 53  GLY   B C      1 
ATOM   5224 O O      . GLY   B 1 87  ? 15.36800  10.49200  -44.39800 1.000 74.48000  ? 53  GLY   B O      1 
ATOM   5225 H H      . GLY   B 1 87  ? 17.17900  13.02500  -44.58200 1.000 68.88000  ? 53  GLY   B H      1 
ATOM   5226 H HA2    . GLY   B 1 87  ? 15.28300  13.37400  -43.57900 1.000 62.97000  ? 53  GLY   B HA2    1 
ATOM   5227 H HA3    . GLY   B 1 87  ? 14.54100  13.34400  -44.95900 1.000 62.97000  ? 53  GLY   B HA3    1 
ATOM   5228 N N      . ASN   B 1 88  ? 13.46700  11.44600  -43.61300 1.000 73.81000  ? 54  ASN   B N      1 
ATOM   5229 C CA     . ASN   B 1 88  ? 12.83400  10.17700  -43.24700 1.000 73.68000  ? 54  ASN   B CA     1 
ATOM   5230 C C      . ASN   B 1 88  ? 12.41300  9.39400   -44.49500 1.000 74.98000  ? 54  ASN   B C      1 
ATOM   5231 O O      . ASN   B 1 88  ? 12.18500  9.97600   -45.55800 1.000 72.82000  ? 54  ASN   B O      1 
ATOM   5232 C CB     . ASN   B 1 88  ? 11.61200  10.41800  -42.35300 1.000 67.63000  ? 54  ASN   B CB     1 
ATOM   5233 C CG     . ASN   B 1 88  ? 11.98200  10.84600  -40.92700 1.000 70.38000  ? 54  ASN   B CG     1 
ATOM   5234 O OD1    . ASN   B 1 88  ? 13.10500  10.63100  -40.47100 1.000 78.37000  ? 54  ASN   B OD1    1 
ATOM   5235 N ND2    . ASN   B 1 88  ? 11.02400  11.44300  -40.21600 1.000 66.49000  ? 54  ASN   B ND2    1 
ATOM   5236 H H      . ASN   B 1 88  ? 12.97900  12.13600  -43.45500 1.000 73.81000  ? 54  ASN   B H      1 
ATOM   5237 H HA     . ASN   B 1 88  ? 13.47300  9.64400   -42.75000 1.000 73.68000  ? 54  ASN   B HA     1 
ATOM   5238 H HB2    . ASN   B 1 88  ? 11.06100  11.11300  -42.74600 1.000 67.63000  ? 54  ASN   B HB2    1 
ATOM   5239 H HB3    . ASN   B 1 88  ? 11.11900  9.59500   -42.29700 1.000 67.63000  ? 54  ASN   B HB3    1 
ATOM   5240 H HD21   . ASN   B 1 88  ? 11.18300  11.70000  -39.41100 1.000 66.49000  ? 54  ASN   B HD21   1 
ATOM   5241 H HD22   . ASN   B 1 88  ? 10.24900  11.57600  -40.56500 1.000 66.49000  ? 54  ASN   B HD22   1 
ATOM   5242 N N      . PRO   B 1 89  ? 12.29100  8.06900   -44.38700 1.000 77.07000  ? 55  PRO   B N      1 
ATOM   5243 C CA     . PRO   B 1 89  ? 11.84800  7.27500   -45.54300 1.000 73.82000  ? 55  PRO   B CA     1 
ATOM   5244 C C      . PRO   B 1 89  ? 10.40400  7.59000   -45.92200 1.000 73.52000  ? 55  PRO   B C      1 
ATOM   5245 O O      . PRO   B 1 89  ? 9.56200   7.87900   -45.06600 1.000 63.41000  ? 55  PRO   B O      1 
ATOM   5246 C CB     . PRO   B 1 89  ? 11.99700  5.82600   -45.05900 1.000 74.88000  ? 55  PRO   B CB     1 
ATOM   5247 C CG     . PRO   B 1 89  ? 11.89300  5.91100   -43.55900 1.000 69.19000  ? 55  PRO   B CG     1 
ATOM   5248 C CD     . PRO   B 1 89  ? 12.50700  7.24000   -43.18400 1.000 73.77000  ? 55  PRO   B CD     1 
ATOM   5249 H HA     . PRO   B 1 89  ? 12.42800  7.42600   -46.30600 1.000 73.82000  ? 55  PRO   B HA     1 
ATOM   5250 H HB2    . PRO   B 1 89  ? 11.28100  5.28300   -45.42400 1.000 74.88000  ? 55  PRO   B HB2    1 
ATOM   5251 H HB3    . PRO   B 1 89  ? 12.86300  5.47900   -45.32500 1.000 74.88000  ? 55  PRO   B HB3    1 
ATOM   5252 H HG2    . PRO   B 1 89  ? 10.96000  5.87900   -43.29500 1.000 69.19000  ? 55  PRO   B HG2    1 
ATOM   5253 H HG3    . PRO   B 1 89  ? 12.38800  5.18000   -43.15600 1.000 69.19000  ? 55  PRO   B HG3    1 
ATOM   5254 H HD2    . PRO   B 1 89  ? 12.04700  7.61800   -42.41900 1.000 73.77000  ? 55  PRO   B HD2    1 
ATOM   5255 H HD3    . PRO   B 1 89  ? 13.45600  7.13600   -43.01200 1.000 73.77000  ? 55  PRO   B HD3    1 
ATOM   5256 N N      . ALA   B 1 90  ? 10.12000  7.53600   -47.23300 1.000 57.81000  ? 56  ALA   B N      1 
ATOM   5257 C CA     . ALA   B 1 90  ? 8.79100   7.85600   -47.74100 1.000 61.22000  ? 56  ALA   B CA     1 
ATOM   5258 C C      . ALA   B 1 90  ? 7.83700   6.67700   -47.56100 1.000 65.81000  ? 56  ALA   B C      1 
ATOM   5259 O O      . ALA   B 1 90  ? 8.27100   5.54500   -47.33200 1.000 72.13000  ? 56  ALA   B O      1 
ATOM   5260 C CB     . ALA   B 1 90  ? 8.86200   8.24500   -49.21400 1.000 58.20000  ? 56  ALA   B CB     1 
ATOM   5261 H H      . ALA   B 1 90  ? 10.68500  7.31600   -47.84300 1.000 57.81000  ? 56  ALA   B H      1 
ATOM   5262 H HA     . ALA   B 1 90  ? 8.44800   8.61400   -47.24600 1.000 61.22000  ? 56  ALA   B HA     1 
ATOM   5263 H HB1    . ALA   B 1 90  ? 7.96700   8.39100   -49.55300 1.000 58.20000  ? 56  ALA   B HB1    1 
ATOM   5264 H HB2    . ALA   B 1 90  ? 9.38600   9.05700   -49.30000 1.000 58.20000  ? 56  ALA   B HB2    1 
ATOM   5265 H HB3    . ALA   B 1 90  ? 9.28400   7.52500   -49.70800 1.000 58.20000  ? 56  ALA   B HB3    1 
ATOM   5266 N N      . PRO   B 1 91  ? 6.51300   6.92700   -47.61500 1.000 59.65000  ? 57  PRO   B N      1 
ATOM   5267 C CA     . PRO   B 1 91  ? 5.85700   8.24500   -47.68100 1.000 55.91000  ? 57  PRO   B CA     1 
ATOM   5268 C C      . PRO   B 1 91  ? 6.00400   8.96900   -46.35300 1.000 48.39000  ? 57  PRO   B C      1 
ATOM   5269 O O      . PRO   B 1 91  ? 5.82000   8.36300   -45.30200 1.000 47.95000  ? 57  PRO   B O      1 
ATOM   5270 C CB     . PRO   B 1 91  ? 4.39100   7.89700   -47.99300 1.000 61.10000  ? 57  PRO   B CB     1 
ATOM   5271 C CG     . PRO   B 1 91  ? 4.19600   6.52300   -47.42800 1.000 59.19000  ? 57  PRO   B CG     1 
ATOM   5272 C CD     . PRO   B 1 91  ? 5.53200   5.82400   -47.58200 1.000 59.51000  ? 57  PRO   B CD     1 
ATOM   5273 H HA     . PRO   B 1 91  ? 6.22200   8.78700   -48.39500 1.000 55.91000  ? 57  PRO   B HA     1 
ATOM   5274 H HB2    . PRO   B 1 91  ? 3.80300   8.53400   -47.55800 1.000 61.10000  ? 57  PRO   B HB2    1 
ATOM   5275 H HB3    . PRO   B 1 91  ? 4.25100   7.89700   -48.95300 1.000 61.10000  ? 57  PRO   B HB3    1 
ATOM   5276 H HG2    . PRO   B 1 91  ? 3.95100   6.58800   -46.49200 1.000 59.19000  ? 57  PRO   B HG2    1 
ATOM   5277 H HG3    . PRO   B 1 91  ? 3.50800   6.05900   -47.93000 1.000 59.19000  ? 57  PRO   B HG3    1 
ATOM   5278 H HD2    . PRO   B 1 91  ? 5.70000   5.24800   -46.82000 1.000 59.51000  ? 57  PRO   B HD2    1 
ATOM   5279 H HD3    . PRO   B 1 91  ? 5.55700   5.32700   -48.41400 1.000 59.51000  ? 57  PRO   B HD3    1 
ATOM   5280 N N      . ARG   B 1 92  ? 6.34500   10.25900  -46.36700 1.000 48.00000  ? 58  ARG   B N      1 
ATOM   5281 C CA     . ARG   B 1 92  ? 6.48500   11.04100  -45.14500 1.000 41.77000  ? 58  ARG   B CA     1 
ATOM   5282 C C      . ARG   B 1 92  ? 5.58000   12.26700  -45.14300 1.000 44.60000  ? 58  ARG   B C      1 
ATOM   5283 O O      . ARG   B 1 92  ? 5.69300   13.10600  -44.24600 1.000 37.94000  ? 58  ARG   B O      1 
ATOM   5284 C CB     . ARG   B 1 92  ? 7.93900   11.45300  -44.95800 1.000 41.51000  ? 58  ARG   B CB     1 
ATOM   5285 C CG     . ARG   B 1 92  ? 8.48800   12.17200  -46.16600 1.000 49.70000  ? 58  ARG   B CG     1 
ATOM   5286 C CD     . ARG   B 1 92  ? 9.96100   11.88800  -46.35200 1.000 65.34000  ? 58  ARG   B CD     1 
ATOM   5287 N NE     . ARG   B 1 92  ? 10.53000  12.67600  -47.43800 1.000 64.27000  ? 58  ARG   B NE     1 
ATOM   5288 C CZ     . ARG   B 1 92  ? 11.82500  12.74200  -47.70900 1.000 73.31000  ? 58  ARG   B CZ     1 
ATOM   5289 N NH1    . ARG   B 1 92  ? 12.70800  12.03200  -47.02800 1.000 74.42000  ? 58  ARG   B NH1    1 
ATOM   5290 N NH2    . ARG   B 1 92  ? 12.24500  13.55000  -48.68000 1.000 79.25000  ? 58  ARG   B NH2    1 
ATOM   5291 H H      . ARG   B 1 92  ? 6.49000   10.70600  -47.08600 1.000 48.00000  ? 58  ARG   B H      1 
ATOM   5292 H HA     . ARG   B 1 92  ? 6.23500   10.49200  -44.38600 1.000 41.77000  ? 58  ARG   B HA     1 
ATOM   5293 H HB2    . ARG   B 1 92  ? 8.00500   12.05000  -44.19600 1.000 41.51000  ? 58  ARG   B HB2    1 
ATOM   5294 H HB3    . ARG   B 1 92  ? 8.47700   10.66000  -44.80800 1.000 41.51000  ? 58  ARG   B HB3    1 
ATOM   5295 H HG2    . ARG   B 1 92  ? 8.02700   11.89800  -46.97100 1.000 49.70000  ? 58  ARG   B HG2    1 
ATOM   5296 H HG3    . ARG   B 1 92  ? 8.37700   13.11200  -46.02900 1.000 49.70000  ? 58  ARG   B HG3    1 
ATOM   5297 H HD2    . ARG   B 1 92  ? 10.43500  12.11000  -45.53500 1.000 65.34000  ? 58  ARG   B HD2    1 
ATOM   5298 H HD3    . ARG   B 1 92  ? 10.08100  10.94900  -46.56400 1.000 65.34000  ? 58  ARG   B HD3    1 
ATOM   5299 H HE     . ARG   B 1 92  ? 9.98800   13.09300  -47.95900 1.000 64.27000  ? 58  ARG   B HE     1 
ATOM   5300 H HH11   . ARG   B 1 92  ? 12.44900  11.51000  -46.39600 1.000 74.42000  ? 58  ARG   B HH11   1 
ATOM   5301 H HH12   . ARG   B 1 92  ? 13.54400  12.09000  -47.22000 1.000 74.42000  ? 58  ARG   B HH12   1 
ATOM   5302 H HH21   . ARG   B 1 92  ? 11.67700  14.01500  -49.12800 1.000 79.25000  ? 58  ARG   B HH21   1 
ATOM   5303 H HH22   . ARG   B 1 92  ? 13.08300  13.59900  -48.86600 1.000 79.25000  ? 58  ARG   B HH22   1 
ATOM   5304 N N      . TYR   B 1 93  ? 4.69500   12.39400  -46.12900 1.000 36.83000  ? 59  TYR   B N      1 
ATOM   5305 C CA     . TYR   B 1 93  ? 3.69100   13.44900  -46.18500 1.000 35.97000  ? 59  TYR   B CA     1 
ATOM   5306 C C      . TYR   B 1 93  ? 2.39100   12.81300  -46.63400 1.000 38.78000  ? 59  TYR   B C      1 
ATOM   5307 O O      . TYR   B 1 93  ? 2.40600   11.88900  -47.44800 1.000 39.14000  ? 59  TYR   B O      1 
ATOM   5308 C CB     . TYR   B 1 93  ? 4.09500   14.56800  -47.15000 1.000 38.84000  ? 59  TYR   B CB     1 
ATOM   5309 C CG     . TYR   B 1 93  ? 3.07000   15.68700  -47.24600 1.000 35.02000  ? 59  TYR   B CG     1 
ATOM   5310 C CD1    . TYR   B 1 93  ? 3.10500   16.77100  -46.37200 1.000 40.15000  ? 59  TYR   B CD1    1 
ATOM   5311 C CD2    . TYR   B 1 93  ? 2.06100   15.65500  -48.21700 1.000 35.36000  ? 59  TYR   B CD2    1 
ATOM   5312 C CE1    . TYR   B 1 93  ? 2.16400   17.80000  -46.46200 1.000 35.97000  ? 59  TYR   B CE1    1 
ATOM   5313 C CE2    . TYR   B 1 93  ? 1.11900   16.67700  -48.31300 1.000 39.67000  ? 59  TYR   B CE2    1 
ATOM   5314 C CZ     . TYR   B 1 93  ? 1.18100   17.75100  -47.43500 1.000 37.62000  ? 59  TYR   B CZ     1 
ATOM   5315 O OH     . TYR   B 1 93  ? 0.24000   18.76700  -47.52600 1.000 36.66000  ? 59  TYR   B OH     1 
ATOM   5316 H H      . TYR   B 1 93  ? 4.65600   11.86000  -46.80200 1.000 36.83000  ? 59  TYR   B H      1 
ATOM   5317 H HA     . TYR   B 1 93  ? 3.56300   13.82900  -45.30200 1.000 35.97000  ? 59  TYR   B HA     1 
ATOM   5318 H HB2    . TYR   B 1 93  ? 4.93100   14.95600  -46.84700 1.000 38.84000  ? 59  TYR   B HB2    1 
ATOM   5319 H HB3    . TYR   B 1 93  ? 4.20800   14.19100  -48.03700 1.000 38.84000  ? 59  TYR   B HB3    1 
ATOM   5320 H HD1    . TYR   B 1 93  ? 3.76700   16.81200  -45.72000 1.000 40.15000  ? 59  TYR   B HD1    1 
ATOM   5321 H HD2    . TYR   B 1 93  ? 2.02100   14.94000  -48.81000 1.000 35.36000  ? 59  TYR   B HD2    1 
ATOM   5322 H HE1    . TYR   B 1 93  ? 2.20100   18.51900  -45.87300 1.000 35.97000  ? 59  TYR   B HE1    1 
ATOM   5323 H HE2    . TYR   B 1 93  ? 0.45600   16.64300  -48.96500 1.000 39.67000  ? 59  TYR   B HE2    1 
ATOM   5324 H HH     . TYR   B 1 93  ? 0.38300   19.34500  -46.93300 1.000 36.66000  ? 59  TYR   B HH     1 
ATOM   5325 N N      . TYR   B 1 94  ? 1.27100   13.28600  -46.10700 1.000 31.03000  ? 60  TYR   B N      1 
ATOM   5326 C CA     . TYR   B 1 94  ? 0.00400   12.72400  -46.54300 1.000 37.59000  ? 60  TYR   B CA     1 
ATOM   5327 C C      . TYR   B 1 94  ? -1.07400  13.78500  -46.43100 1.000 37.57000  ? 60  TYR   B C      1 
ATOM   5328 O O      . TYR   B 1 94  ? -1.15700  14.48700  -45.42500 1.000 32.99000  ? 60  TYR   B O      1 
ATOM   5329 C CB     . TYR   B 1 94  ? -0.36100  11.48800  -45.71900 1.000 32.06000  ? 60  TYR   B CB     1 
ATOM   5330 C CG     . TYR   B 1 94  ? -1.54200  10.68600  -46.23200 1.000 37.71000  ? 60  TYR   B CG     1 
ATOM   5331 C CD1    . TYR   B 1 94  ? -1.37300  9.70600   -47.20800 1.000 48.31000  ? 60  TYR   B CD1    1 
ATOM   5332 C CD2    . TYR   B 1 94  ? -2.81400  10.88100  -45.71300 1.000 41.70000  ? 60  TYR   B CD2    1 
ATOM   5333 C CE1    . TYR   B 1 94  ? -2.44900  8.94400   -47.66000 1.000 49.34000  ? 60  TYR   B CE1    1 
ATOM   5334 C CE2    . TYR   B 1 94  ? -3.89800  10.12200  -46.15700 1.000 48.67000  ? 60  TYR   B CE2    1 
ATOM   5335 C CZ     . TYR   B 1 94  ? -3.70500  9.15800   -47.13300 1.000 49.08000  ? 60  TYR   B CZ     1 
ATOM   5336 O OH     . TYR   B 1 94  ? -4.77900  8.40800   -47.57700 1.000 59.03000  ? 60  TYR   B OH     1 
ATOM   5337 H H      . TYR   B 1 94  ? 1.21600   13.90900  -45.51700 1.000 31.03000  ? 60  TYR   B H      1 
ATOM   5338 H HA     . TYR   B 1 94  ? 0.07100   12.46000  -47.47400 1.000 37.59000  ? 60  TYR   B HA     1 
ATOM   5339 H HB2    . TYR   B 1 94  ? 0.40600   10.89500  -45.69900 1.000 32.06000  ? 60  TYR   B HB2    1 
ATOM   5340 H HB3    . TYR   B 1 94  ? -0.57300  11.77300  -44.81600 1.000 32.06000  ? 60  TYR   B HB3    1 
ATOM   5341 H HD1    . TYR   B 1 94  ? -0.52600  9.55500   -47.56100 1.000 48.31000  ? 60  TYR   B HD1    1 
ATOM   5342 H HD2    . TYR   B 1 94  ? -2.94400  11.52300  -45.05400 1.000 41.70000  ? 60  TYR   B HD2    1 
ATOM   5343 H HE1    . TYR   B 1 94  ? -2.32100  8.29700   -48.31500 1.000 49.34000  ? 60  TYR   B HE1    1 
ATOM   5344 H HE2    . TYR   B 1 94  ? -4.74600  10.26700  -45.80400 1.000 48.67000  ? 60  TYR   B HE2    1 
ATOM   5345 H HH     . TYR   B 1 94  ? -5.47800  8.64100   -47.17400 1.000 59.03000  ? 60  TYR   B HH     1 
ATOM   5346 N N      . THR   B 1 95  ? -1.89200  13.89400  -47.47900 1.000 35.22000  ? 61  THR   B N      1 
ATOM   5347 C CA     . THR   B 1 95  ? -3.00700  14.83300  -47.49800 1.000 35.70000  ? 61  THR   B CA     1 
ATOM   5348 C C      . THR   B 1 95  ? -4.19700  14.25400  -46.75000 1.000 39.33000  ? 61  THR   B C      1 
ATOM   5349 O O      . THR   B 1 95  ? -4.61700  13.12200  -47.00700 1.000 37.66000  ? 61  THR   B O      1 
ATOM   5350 C CB     . THR   B 1 95  ? -3.40200  15.16000  -48.93900 1.000 39.98000  ? 61  THR   B CB     1 
ATOM   5351 O OG1    . THR   B 1 95  ? -2.31800  15.83600  -49.57700 1.000 39.95000  ? 61  THR   B OG1    1 
ATOM   5352 C CG2    . THR   B 1 95  ? -4.63700  16.04700  -48.96300 1.000 39.13000  ? 61  THR   B CG2    1 
ATOM   5353 H H      . THR   B 1 95  ? -1.81900  13.42800  -48.19800 1.000 35.22000  ? 61  THR   B H      1 
ATOM   5354 H HA     . THR   B 1 95  ? -2.74200  15.65600  -47.06000 1.000 35.70000  ? 61  THR   B HA     1 
ATOM   5355 H HB     . THR   B 1 95  ? -3.60100  14.33900  -49.41700 1.000 39.98000  ? 61  THR   B HB     1 
ATOM   5356 H HG1    . THR   B 1 95  ? -2.51200  15.99700  -50.37800 1.000 39.95000  ? 61  THR   B HG1    1 
ATOM   5357 H HG21   . THR   B 1 95  ? -4.72500  16.46500  -49.83400 1.000 39.13000  ? 61  THR   B HG21   1 
ATOM   5358 H HG22   . THR   B 1 95  ? -5.43200  15.52000  -48.78700 1.000 39.13000  ? 61  THR   B HG22   1 
ATOM   5359 H HG23   . THR   B 1 95  ? -4.56000  16.74000  -48.28900 1.000 39.13000  ? 61  THR   B HG23   1 
ATOM   5360 N N      . LEU   B 1 96  ? -4.71800  15.01700  -45.80600 1.000 38.25000  ? 62  LEU   B N      1 
ATOM   5361 C CA     . LEU   B 1 96  ? -5.82300  14.60800  -44.95600 1.000 38.25000  ? 62  LEU   B CA     1 
ATOM   5362 C C      . LEU   B 1 96  ? -7.09000  15.32700  -45.38400 1.000 40.70000  ? 62  LEU   B C      1 
ATOM   5363 O O      . LEU   B 1 96  ? -7.02900  16.32800  -46.10800 1.000 38.98000  ? 62  LEU   B O      1 
ATOM   5364 C CB     . LEU   B 1 96  ? -5.53700  14.92300  -43.47800 1.000 33.70000  ? 62  LEU   B CB     1 
ATOM   5365 C CG     . LEU   B 1 96  ? -4.30100  14.21000  -42.90100 1.000 34.99000  ? 62  LEU   B CG     1 
ATOM   5366 C CD1    . LEU   B 1 96  ? -4.06200  14.57900  -41.45100 1.000 37.23000  ? 62  LEU   B CD1    1 
ATOM   5367 C CD2    . LEU   B 1 96  ? -4.47800  12.71400  -43.05900 1.000 40.87000  ? 62  LEU   B CD2    1 
ATOM   5368 H H      . LEU   B 1 96  ? -4.43600  15.81000  -45.63100 1.000 38.25000  ? 62  LEU   B H      1 
ATOM   5369 H HA     . LEU   B 1 96  ? -5.96900  13.65500  -45.05300 1.000 38.25000  ? 62  LEU   B HA     1 
ATOM   5370 H HB2    . LEU   B 1 96  ? -5.39200  15.87800  -43.38900 1.000 33.70000  ? 62  LEU   B HB2    1 
ATOM   5371 H HB3    . LEU   B 1 96  ? -6.30100  14.65900  -42.94500 1.000 33.70000  ? 62  LEU   B HB3    1 
ATOM   5372 H HG     . LEU   B 1 96  ? -3.51900  14.47400  -43.41000 1.000 34.99000  ? 62  LEU   B HG     1 
ATOM   5373 H HD11   . LEU   B 1 96  ? -3.32000  14.05600  -41.11100 1.000 37.23000  ? 62  LEU   B HD11   1 
ATOM   5374 H HD12   . LEU   B 1 96  ? -3.85400  15.52500  -41.39600 1.000 37.23000  ? 62  LEU   B HD12   1 
ATOM   5375 H HD13   . LEU   B 1 96  ? -4.86400  14.38500  -40.94000 1.000 37.23000  ? 62  LEU   B HD13   1 
ATOM   5376 H HD21   . LEU   B 1 96  ? -3.75300  12.26300  -42.60100 1.000 40.87000  ? 62  LEU   B HD21   1 
ATOM   5377 H HD22   . LEU   B 1 96  ? -5.32800  12.45400  -42.67200 1.000 40.87000  ? 62  LEU   B HD22   1 
ATOM   5378 H HD23   . LEU   B 1 96  ? -4.45900  12.48700  -44.00100 1.000 40.87000  ? 62  LEU   B HD23   1 
ATOM   5379 N N      . PRO   B 1 97  ? -8.26300  14.85100  -44.95400 1.000 45.87000  ? 63  PRO   B N      1 
ATOM   5380 C CA     . PRO   B 1 97  ? -9.50000  15.56800  -45.30300 1.000 47.95000  ? 63  PRO   B CA     1 
ATOM   5381 C C      . PRO   B 1 97  ? -9.42700  17.05600  -44.98400 1.000 45.95000  ? 63  PRO   B C      1 
ATOM   5382 O O      . PRO   B 1 97  ? -9.85700  17.88000  -45.79500 1.000 47.03000  ? 63  PRO   B O      1 
ATOM   5383 C CB     . PRO   B 1 97  ? -10.56300 14.83800  -44.46900 1.000 42.26000  ? 63  PRO   B CB     1 
ATOM   5384 C CG     . PRO   B 1 97  ? -9.99400  13.41600  -44.31500 1.000 38.79000  ? 63  PRO   B CG     1 
ATOM   5385 C CD     . PRO   B 1 97  ? -8.51700  13.65800  -44.12500 1.000 48.84000  ? 63  PRO   B CD     1 
ATOM   5386 H HA     . PRO   B 1 97  ? -9.69900  15.45300  -46.24500 1.000 47.95000  ? 63  PRO   B HA     1 
ATOM   5387 H HB2    . PRO   B 1 97  ? -10.65900 15.26900  -43.60500 1.000 42.26000  ? 63  PRO   B HB2    1 
ATOM   5388 H HB3    . PRO   B 1 97  ? -11.40700 14.82400  -44.94700 1.000 42.26000  ? 63  PRO   B HB3    1 
ATOM   5389 H HG2    . PRO   B 1 97  ? -10.38000 12.98600  -43.53600 1.000 38.79000  ? 63  PRO   B HG2    1 
ATOM   5390 H HG3    . PRO   B 1 97  ? -10.16300 12.90100  -45.12000 1.000 38.79000  ? 63  PRO   B HG3    1 
ATOM   5391 H HD2    . PRO   B 1 97  ? -8.32600  13.84300  -43.19300 1.000 48.84000  ? 63  PRO   B HD2    1 
ATOM   5392 H HD3    . PRO   B 1 97  ? -8.00700  12.90100  -44.45100 1.000 48.84000  ? 63  PRO   B HD3    1 
ATOM   5393 N N      . LEU   B 1 98  ? -8.83900  17.42400  -43.84100 1.000 38.46000  ? 64  LEU   B N      1 
ATOM   5394 C CA     . LEU   B 1 98  ? -8.84500  18.80100  -43.35700 1.000 33.61000  ? 64  LEU   B CA     1 
ATOM   5395 C C      . LEU   B 1 98  ? -7.43500  19.36300  -43.19400 1.000 37.86000  ? 64  LEU   B C      1 
ATOM   5396 O O      . LEU   B 1 98  ? -7.23800  20.32900  -42.45400 1.000 38.31000  ? 64  LEU   B O      1 
ATOM   5397 C CB     . LEU   B 1 98  ? -9.60600  18.87800  -42.03400 1.000 37.72000  ? 64  LEU   B CB     1 
ATOM   5398 C CG     . LEU   B 1 98  ? -11.06200 18.41100  -42.12500 1.000 43.29000  ? 64  LEU   B CG     1 
ATOM   5399 C CD1    . LEU   B 1 98  ? -11.68900 18.26600  -40.74400 1.000 44.72000  ? 64  LEU   B CD1    1 
ATOM   5400 C CD2    . LEU   B 1 98  ? -11.85600 19.40200  -42.97600 1.000 40.19000  ? 64  LEU   B CD2    1 
ATOM   5401 H H      . LEU   B 1 98  ? -8.42300  16.88000  -43.32100 1.000 38.46000  ? 64  LEU   B H      1 
ATOM   5402 H HA     . LEU   B 1 98  ? -9.30800  19.36000  -44.00000 1.000 33.61000  ? 64  LEU   B HA     1 
ATOM   5403 H HB2    . LEU   B 1 98  ? -9.16100  18.32600  -41.37900 1.000 37.72000  ? 64  LEU   B HB2    1 
ATOM   5404 H HB3    . LEU   B 1 98  ? -9.61200  19.80000  -41.73300 1.000 37.72000  ? 64  LEU   B HB3    1 
ATOM   5405 H HG     . LEU   B 1 98  ? -11.09300 17.54600  -42.56200 1.000 43.29000  ? 64  LEU   B HG     1 
ATOM   5406 H HD11   . LEU   B 1 98  ? -12.63500 18.07900  -40.84500 1.000 44.72000  ? 64  LEU   B HD11   1 
ATOM   5407 H HD12   . LEU   B 1 98  ? -11.25600 17.53500  -40.27700 1.000 44.72000  ? 64  LEU   B HD12   1 
ATOM   5408 H HD13   . LEU   B 1 98  ? -11.56600 19.09200  -40.25200 1.000 44.72000  ? 64  LEU   B HD13   1 
ATOM   5409 H HD21   . LEU   B 1 98  ? -12.79900 19.18300  -42.91700 1.000 40.19000  ? 64  LEU   B HD21   1 
ATOM   5410 H HD22   . LEU   B 1 98  ? -11.70400 20.29900  -42.64000 1.000 40.19000  ? 64  LEU   B HD22   1 
ATOM   5411 H HD23   . LEU   B 1 98  ? -11.55900 19.33900  -43.89700 1.000 40.19000  ? 64  LEU   B HD23   1 
ATOM   5412 N N      . GLY   B 1 99  ? -6.44100  18.76700  -43.84700 1.000 35.00000  ? 65  GLY   B N      1 
ATOM   5413 C CA     . GLY   B 1 99  ? -5.09200  19.29400  -43.73400 1.000 30.00000  ? 65  GLY   B CA     1 
ATOM   5414 C C      . GLY   B 1 99  ? -4.01600  18.31000  -44.16300 1.000 28.75000  ? 65  GLY   B C      1 
ATOM   5415 O O      . GLY   B 1 99  ? -4.12300  17.67700  -45.22200 1.000 30.53000  ? 65  GLY   B O      1 
ATOM   5416 H H      . GLY   B 1 99  ? -6.52000  18.07400  -44.34900 1.000 35.00000  ? 65  GLY   B H      1 
ATOM   5417 H HA2    . GLY   B 1 99  ? -5.01300  20.08900  -44.28400 1.000 30.00000  ? 65  GLY   B HA2    1 
ATOM   5418 H HA3    . GLY   B 1 99  ? -4.92300  19.54400  -42.81200 1.000 30.00000  ? 65  GLY   B HA3    1 
ATOM   5419 N N      . SER   B 1 100 ? -2.98900  18.15500  -43.33000 1.000 26.76000  ? 66  SER   B N      1 
ATOM   5420 C CA     . SER   B 1 100 ? -1.82200  17.37300  -43.70600 1.000 28.62000  ? 66  SER   B CA     1 
ATOM   5421 C C      . SER   B 1 100 ? -1.21400  16.74100  -42.46300 1.000 28.00000  ? 66  SER   B C      1 
ATOM   5422 O O      . SER   B 1 100 ? -1.38400  17.22800  -41.33700 1.000 28.25000  ? 66  SER   B O      1 
ATOM   5423 C CB     . SER   B 1 100 ? -0.76100  18.24600  -44.39400 1.000 30.56000  ? 66  SER   B CB     1 
ATOM   5424 O OG     . SER   B 1 100 ? -0.26900  19.20200  -43.47100 1.000 29.48000  ? 66  SER   B OG     1 
ATOM   5425 H H      . SER   B 1 100 ? -2.94700  18.49400  -42.54100 1.000 26.76000  ? 66  SER   B H      1 
ATOM   5426 H HA     . SER   B 1 100 ? -2.08400  16.66600  -44.31600 1.000 28.62000  ? 66  SER   B HA     1 
ATOM   5427 H HB2    . SER   B 1 100 ? -0.03000  17.68400  -44.69300 1.000 30.56000  ? 66  SER   B HB2    1 
ATOM   5428 H HB3    . SER   B 1 100 ? -1.16300  18.70500  -45.14800 1.000 30.56000  ? 66  SER   B HB3    1 
ATOM   5429 H HG     . SER   B 1 100 ? 0.31200   19.68400  -43.83900 1.000 29.48000  ? 66  SER   B HG     1 
ATOM   5430 N N      . ILE   B 1 101 ? -0.47500  15.65800  -42.68400 1.000 29.23000  ? 67  ILE   B N      1 
ATOM   5431 C CA     . ILE   B 1 101 ? 0.39400   15.10700  -41.65700 1.000 29.78000  ? 67  ILE   B CA     1 
ATOM   5432 C C      . ILE   B 1 101 ? 1.75000   14.84500  -42.29700 1.000 28.71000  ? 67  ILE   B C      1 
ATOM   5433 O O      . ILE   B 1 101 ? 1.82100   14.44300  -43.46000 1.000 32.18000  ? 67  ILE   B O      1 
ATOM   5434 C CB     . ILE   B 1 101 ? -0.21400  13.82400  -41.04000 1.000 30.82000  ? 67  ILE   B CB     1 
ATOM   5435 C CG1    . ILE   B 1 101 ? 0.58300   13.40400  -39.81300 1.000 29.84000  ? 67  ILE   B CG1    1 
ATOM   5436 C CG2    . ILE   B 1 101 ? -0.39400  12.71100  -42.12100 1.000 28.02000  ? 67  ILE   B CG2    1 
ATOM   5437 C CD1    . ILE   B 1 101 ? 0.01200   12.16500  -39.08600 1.000 30.56000  ? 67  ILE   B CD1    1 
ATOM   5438 H H      . ILE   B 1 101 ? -0.46100  15.22300  -43.42600 1.000 29.23000  ? 67  ILE   B H      1 
ATOM   5439 H HA     . ILE   B 1 101 ? 0.50800   15.75900  -40.95100 1.000 29.78000  ? 67  ILE   B HA     1 
ATOM   5440 H HB     . ILE   B 1 101 ? -1.10200  14.05700  -40.72800 1.000 30.82000  ? 67  ILE   B HB     1 
ATOM   5441 H HG12   . ILE   B 1 101 ? 1.49000   13.19400  -40.08600 1.000 29.84000  ? 67  ILE   B HG12   1 
ATOM   5442 H HG13   . ILE   B 1 101 ? 0.59300   14.14000  -39.18100 1.000 29.84000  ? 67  ILE   B HG13   1 
ATOM   5443 H HG21   . ILE   B 1 101 ? -0.88100  11.96800  -41.73100 1.000 28.02000  ? 67  ILE   B HG21   1 
ATOM   5444 H HG22   . ILE   B 1 101 ? -0.89100  13.07600  -42.87000 1.000 28.02000  ? 67  ILE   B HG22   1 
ATOM   5445 H HG23   . ILE   B 1 101 ? 0.48000   12.41400  -42.41800 1.000 28.02000  ? 67  ILE   B HG23   1 
ATOM   5446 H HD11   . ILE   B 1 101 ? 0.53800   11.99800  -38.28800 1.000 30.56000  ? 67  ILE   B HD11   1 
ATOM   5447 H HD12   . ILE   B 1 101 ? -0.91100  12.33900  -38.84400 1.000 30.56000  ? 67  ILE   B HD12   1 
ATOM   5448 H HD13   . ILE   B 1 101 ? 0.05900   11.40000  -39.68000 1.000 30.56000  ? 67  ILE   B HD13   1 
ATOM   5449 N N      . ASN   B 1 102 ? 2.83200   15.10900  -41.56500 1.000 29.48000  ? 68  ASN   B N      1 
ATOM   5450 C CA     . ASN   B 1 102 ? 4.14400   14.89100  -42.15700 1.000 34.39000  ? 68  ASN   B CA     1 
ATOM   5451 C C      . ASN   B 1 102 ? 5.11000   14.41100  -41.08700 1.000 36.37000  ? 68  ASN   B C      1 
ATOM   5452 O O      . ASN   B 1 102 ? 5.00700   14.78400  -39.91600 1.000 31.58000  ? 68  ASN   B O      1 
ATOM   5453 C CB     . ASN   B 1 102 ? 4.71500   16.15600  -42.82000 1.000 36.20000  ? 68  ASN   B CB     1 
ATOM   5454 C CG     . ASN   B 1 102 ? 5.36900   17.10600  -41.81500 1.000 35.38000  ? 68  ASN   B CG     1 
ATOM   5455 O OD1    . ASN   B 1 102 ? 6.55300   16.95400  -41.46500 1.000 35.87000  ? 68  ASN   B OD1    1 
ATOM   5456 N ND2    . ASN   B 1 102 ? 4.60300   18.09700  -41.34100 1.000 31.41000  ? 68  ASN   B ND2    1 
ATOM   5457 H H      . ASN   B 1 102 ? 2.83400   15.40300  -40.75700 1.000 29.48000  ? 68  ASN   B H      1 
ATOM   5458 H HA     . ASN   B 1 102 ? 4.07900   14.19900  -42.83300 1.000 34.39000  ? 68  ASN   B HA     1 
ATOM   5459 H HB2    . ASN   B 1 102 ? 5.38700   15.89700  -43.46900 1.000 36.20000  ? 68  ASN   B HB2    1 
ATOM   5460 H HB3    . ASN   B 1 102 ? 3.99500   16.63400  -43.26100 1.000 36.20000  ? 68  ASN   B HB3    1 
ATOM   5461 H HD21   . ASN   B 1 102 ? 4.92600   18.65700  -40.77400 1.000 31.41000  ? 68  ASN   B HD21   1 
ATOM   5462 H HD22   . ASN   B 1 102 ? 3.78800   18.17400  -41.60400 1.000 31.41000  ? 68  ASN   B HD22   1 
ATOM   5463 N N      . SER   B 1 103 ? 6.05900   13.58700  -41.51200 1.000 35.94000  ? 69  SER   B N      1 
ATOM   5464 C CA     . SER   B 1 103 ? 7.25000   13.30000  -40.73100 1.000 37.88000  ? 69  SER   B CA     1 
ATOM   5465 C C      . SER   B 1 103 ? 8.47400   13.49000  -41.60900 1.000 41.00000  ? 69  SER   B C      1 
ATOM   5466 O O      . SER   B 1 103 ? 9.28900   12.58600  -41.79300 1.000 51.43000  ? 69  SER   B O      1 
ATOM   5467 C CB     . SER   B 1 103 ? 7.16600   11.90200  -40.14400 1.000 41.77000  ? 69  SER   B CB     1 
ATOM   5468 O OG     . SER   B 1 103 ? 7.02100   10.97200  -41.20100 1.000 58.52000  ? 69  SER   B OG     1 
ATOM   5469 H H      . SER   B 1 103 ? 6.03400   13.17400  -42.26600 1.000 35.94000  ? 69  SER   B H      1 
ATOM   5470 H HA     . SER   B 1 103 ? 7.30600   13.93000  -39.99800 1.000 37.88000  ? 69  SER   B HA     1 
ATOM   5471 H HB2    . SER   B 1 103 ? 7.98100   11.70900  -39.65400 1.000 41.77000  ? 69  SER   B HB2    1 
ATOM   5472 H HB3    . SER   B 1 103 ? 6.39600   11.84500  -39.55700 1.000 41.77000  ? 69  SER   B HB3    1 
ATOM   5473 H HG     . SER   B 1 103 ? 6.92100   10.20100  -40.88600 1.000 58.52000  ? 69  SER   B HG     1 
ATOM   5474 N N      . MET   B 1 104 ? 8.58900   14.68800  -42.20500 1.000 46.16000  ? 70  MET   B N      1 
ATOM   5475 C CA     . MET   B 1 104 ? 9.63400   14.92100  -43.20200 1.000 56.50000  ? 70  MET   B CA     1 
ATOM   5476 C C      . MET   B 1 104 ? 11.00900  14.53800  -42.66500 1.000 61.41000  ? 70  MET   B C      1 
ATOM   5477 O O      . MET   B 1 104 ? 11.83400  13.97600  -43.39600 1.000 55.65000  ? 70  MET   B O      1 
ATOM   5478 C CB     . MET   B 1 104 ? 9.62200   16.38500  -43.67000 1.000 52.06000  ? 70  MET   B CB     1 
ATOM   5479 C CG     . MET   B 1 104 ? 8.53200   16.74600  -44.70800 1.000 57.95000  ? 70  MET   B CG     1 
ATOM   5480 S SD     . MET   B 1 104 ? 8.42900   15.57000  -46.07800 1.000 71.87000  ? 70  MET   B SD     1 
ATOM   5481 C CE     . MET   B 1 104 ? 7.41300   16.37900  -47.32700 1.000 61.88000  ? 70  MET   B CE     1 
ATOM   5482 H H      . MET   B 1 104 ? 8.08300   15.36600  -42.05000 1.000 46.16000  ? 70  MET   B H      1 
ATOM   5483 H HA     . MET   B 1 104 ? 9.45100   14.35600  -43.96700 1.000 56.50000  ? 70  MET   B HA     1 
ATOM   5484 H HB2    . MET   B 1 104 ? 9.44700   16.93300  -42.89300 1.000 52.06000  ? 70  MET   B HB2    1 
ATOM   5485 H HB3    . MET   B 1 104 ? 10.48600  16.60700  -44.04900 1.000 52.06000  ? 70  MET   B HB3    1 
ATOM   5486 H HG2    . MET   B 1 104 ? 7.67000   16.76200  -44.26400 1.000 57.95000  ? 70  MET   B HG2    1 
ATOM   5487 H HG3    . MET   B 1 104 ? 8.72900   17.62000  -45.07900 1.000 57.95000  ? 70  MET   B HG3    1 
ATOM   5488 H HE1    . MET   B 1 104 ? 7.28400   15.77100  -48.07100 1.000 61.88000  ? 70  MET   B HE1    1 
ATOM   5489 H HE2    . MET   B 1 104 ? 6.55600   16.61000  -46.93500 1.000 61.88000  ? 70  MET   B HE2    1 
ATOM   5490 H HE3    . MET   B 1 104 ? 7.86500   17.18200  -47.63000 1.000 61.88000  ? 70  MET   B HE3    1 
ATOM   5491 N N      . GLY   B 1 105 ? 11.27000  14.81500  -41.38600 1.000 55.10000  ? 71  GLY   B N      1 
ATOM   5492 C CA     . GLY   B 1 105 ? 12.54400  14.44400  -40.79800 1.000 64.01000  ? 71  GLY   B CA     1 
ATOM   5493 C C      . GLY   B 1 105 ? 13.69100  15.37000  -41.13800 1.000 60.93000  ? 71  GLY   B C      1 
ATOM   5494 O O      . GLY   B 1 105 ? 14.85400  14.95000  -41.12300 1.000 57.93000  ? 71  GLY   B O      1 
ATOM   5495 H H      . GLY   B 1 105 ? 10.72900  15.21200  -40.84800 1.000 55.10000  ? 71  GLY   B H      1 
ATOM   5496 H HA2    . GLY   B 1 105 ? 12.45200  14.42400  -39.83300 1.000 64.01000  ? 71  GLY   B HA2    1 
ATOM   5497 H HA3    . GLY   B 1 105 ? 12.78100  13.55200  -41.09600 1.000 64.01000  ? 71  GLY   B HA3    1 
ATOM   5498 N N      . LEU   B 1 106 ? 13.40100  16.61200  -41.45900 1.000 50.33000  ? 72  LEU   B N      1 
ATOM   5499 C CA     . LEU   B 1 106 ? 14.46400  17.56400  -41.73900 1.000 64.55000  ? 72  LEU   B CA     1 
ATOM   5500 C C      . LEU   B 1 106 ? 15.29400  17.20400  -42.96700 1.000 58.25000  ? 72  LEU   B C      1 
ATOM   5501 O O      . LEU   B 1 106 ? 16.52900  17.31300  -42.92100 1.000 50.82000  ? 72  LEU   B O      1 
ATOM   5502 H H      . LEU   B 1 106 ? 12.60500  16.93200  -41.52300 1.000 50.33000  ? 72  LEU   B H      1 
ATOM   5503 N N      . PRO   B 1 107 ? 14.66500  16.78500  -44.07100 1.000 63.35000  ? 73  PRO   B N      1 
ATOM   5504 C CA     . PRO   B 1 107 ? 15.41400  16.62800  -45.32400 1.000 58.80000  ? 73  PRO   B CA     1 
ATOM   5505 C C      . PRO   B 1 107 ? 15.76800  18.00200  -45.85200 1.000 47.39000  ? 73  PRO   B C      1 
ATOM   5506 O O      . PRO   B 1 107 ? 14.89900  18.86800  -45.97900 1.000 50.44000  ? 73  PRO   B O      1 
ATOM   5507 C CB     . PRO   B 1 107 ? 14.42100  15.92400  -46.24700 1.000 55.61000  ? 73  PRO   B CB     1 
ATOM   5508 C CG     . PRO   B 1 107 ? 13.09700  16.54400  -45.83100 1.000 57.21000  ? 73  PRO   B CG     1 
ATOM   5509 C CD     . PRO   B 1 107 ? 13.20700  16.76100  -44.31600 1.000 64.86000  ? 73  PRO   B CD     1 
ATOM   5510 H HA     . PRO   B 1 107 ? 16.21100  16.08900  -45.20100 1.000 58.80000  ? 73  PRO   B HA     1 
ATOM   5511 H HB2    . PRO   B 1 107 ? 14.62500  16.13600  -47.17100 1.000 55.61000  ? 73  PRO   B HB2    1 
ATOM   5512 H HB3    . PRO   B 1 107 ? 14.42800  14.97100  -46.10300 1.000 55.61000  ? 73  PRO   B HB3    1 
ATOM   5513 H HG2    . PRO   B 1 107 ? 12.97200  17.38900  -46.29100 1.000 57.21000  ? 73  PRO   B HG2    1 
ATOM   5514 H HG3    . PRO   B 1 107 ? 12.37300  15.93300  -46.03700 1.000 57.21000  ? 73  PRO   B HG3    1 
ATOM   5515 H HD2    . PRO   B 1 107 ? 12.80700  17.60900  -44.06500 1.000 64.86000  ? 73  PRO   B HD2    1 
ATOM   5516 H HD3    . PRO   B 1 107 ? 12.80100  16.02400  -43.84300 1.000 64.86000  ? 73  PRO   B HD3    1 
ATOM   5517 N N      . ASN   B 1 108 ? 17.05000  18.22300  -46.12200 1.000 39.73000  ? 74  ASN   B N      1 
ATOM   5518 C CA     . ASN   B 1 108 ? 17.41400  19.57800  -46.50600 1.000 38.33000  ? 74  ASN   B CA     1 
ATOM   5519 C C      . ASN   B 1 108 ? 18.78100  19.54900  -47.16600 1.000 35.67000  ? 74  ASN   B C      1 
ATOM   5520 O O      . ASN   B 1 108 ? 19.57300  18.62800  -46.95000 1.000 39.91000  ? 74  ASN   B O      1 
ATOM   5521 C CB     . ASN   B 1 108 ? 17.36900  20.53400  -45.29800 1.000 36.92000  ? 74  ASN   B CB     1 
ATOM   5522 C CG     . ASN   B 1 108 ? 18.57400  20.40500  -44.38000 1.000 33.25000  ? 74  ASN   B CG     1 
ATOM   5523 O OD1    . ASN   B 1 108 ? 19.53400  21.16400  -44.50400 1.000 33.21000  ? 74  ASN   B OD1    1 
ATOM   5524 N ND2    . ASN   B 1 108 ? 18.51600  19.46200  -43.43300 1.000 37.96000  ? 74  ASN   B ND2    1 
ATOM   5525 H H      . ASN   B 1 108 ? 17.68900  17.64800  -46.09400 1.000 39.73000  ? 74  ASN   B H      1 
ATOM   5526 H HA     . ASN   B 1 108 ? 16.77700  19.90000  -47.16200 1.000 38.33000  ? 74  ASN   B HA     1 
ATOM   5527 H HB2    . ASN   B 1 108 ? 17.34100  21.44700  -45.62300 1.000 36.92000  ? 74  ASN   B HB2    1 
ATOM   5528 H HB3    . ASN   B 1 108 ? 16.57500  20.34700  -44.77400 1.000 36.92000  ? 74  ASN   B HB3    1 
ATOM   5529 H HD21   . ASN   B 1 108 ? 19.17500  19.35600  -42.89000 1.000 37.96000  ? 74  ASN   B HD21   1 
ATOM   5530 H HD22   . ASN   B 1 108 ? 17.82500  18.95400  -43.37400 1.000 37.96000  ? 74  ASN   B HD22   1 
ATOM   5531 N N      . LYS   B 1 109 ? 19.02700  20.55300  -48.01400 1.000 33.84000  ? 75  LYS   B N      1 
ATOM   5532 C CA     . LYS   B 1 109 ? 20.26400  20.61100  -48.79100 1.000 35.18000  ? 75  LYS   B CA     1 
ATOM   5533 C C      . LYS   B 1 109 ? 21.46300  21.01400  -47.95200 1.000 37.05000  ? 75  LYS   B C      1 
ATOM   5534 O O      . LYS   B 1 109 ? 22.57000  21.08700  -48.48700 1.000 37.20000  ? 75  LYS   B O      1 
ATOM   5535 C CB     . LYS   B 1 109 ? 20.12300  21.59300  -49.95900 1.000 35.57000  ? 75  LYS   B CB     1 
ATOM   5536 C CG     . LYS   B 1 109 ? 18.99600  21.28300  -50.93900 1.000 36.84000  ? 75  LYS   B CG     1 
ATOM   5537 C CD     . LYS   B 1 109 ? 19.19300  19.94800  -51.57800 1.000 41.42000  ? 75  LYS   B CD     1 
ATOM   5538 C CE     . LYS   B 1 109 ? 18.12500  19.65100  -52.62400 1.000 46.26000  ? 75  LYS   B CE     1 
ATOM   5539 N NZ     . LYS   B 1 109 ? 18.46800  18.36900  -53.29800 1.000 39.21000  ? 75  LYS   B NZ     1 
ATOM   5540 H H      . LYS   B 1 109 ? 18.49200  21.21100  -48.15600 1.000 33.84000  ? 75  LYS   B H      1 
ATOM   5541 H HA     . LYS   B 1 109 ? 20.44500  19.73200  -49.15700 1.000 35.18000  ? 75  LYS   B HA     1 
ATOM   5542 H HB2    . LYS   B 1 109 ? 19.96000  22.47800  -49.59800 1.000 35.57000  ? 75  LYS   B HB2    1 
ATOM   5543 H HB3    . LYS   B 1 109 ? 20.95300  21.59600  -50.46100 1.000 35.57000  ? 75  LYS   B HB3    1 
ATOM   5544 H HG2    . LYS   B 1 109 ? 18.15000  21.27200  -50.46400 1.000 36.84000  ? 75  LYS   B HG2    1 
ATOM   5545 H HG3    . LYS   B 1 109 ? 18.98200  21.95700  -51.63700 1.000 36.84000  ? 75  LYS   B HG3    1 
ATOM   5546 H HD2    . LYS   B 1 109 ? 20.05900  19.92800  -52.01500 1.000 41.42000  ? 75  LYS   B HD2    1 
ATOM   5547 H HD3    . LYS   B 1 109 ? 19.14400  19.25700  -50.89900 1.000 41.42000  ? 75  LYS   B HD3    1 
ATOM   5548 H HE2    . LYS   B 1 109 ? 17.26000  19.55800  -52.19500 1.000 46.26000  ? 75  LYS   B HE2    1 
ATOM   5549 H HE3    . LYS   B 1 109 ? 18.10700  20.35900  -53.28700 1.000 46.26000  ? 75  LYS   B HE3    1 
ATOM   5550 H HZ1    . LYS   B 1 109 ? 17.85600  18.17700  -53.91500 1.000 39.21000  ? 75  LYS   B HZ1    1 
ATOM   5551 H HZ2    . LYS   B 1 109 ? 19.26400  18.43600  -53.69100 1.000 39.21000  ? 75  LYS   B HZ2    1 
ATOM   5552 H HZ3    . LYS   B 1 109 ? 18.49400  17.70900  -52.70100 1.000 39.21000  ? 75  LYS   B HZ3    1 
ATOM   5553 N N      . GLY   B 1 110 ? 21.27900  21.28100  -46.67200 1.000 34.30000  ? 76  GLY   B N      1 
ATOM   5554 C CA     . GLY   B 1 110 ? 22.40600  21.68900  -45.84500 1.000 34.27000  ? 76  GLY   B CA     1 
ATOM   5555 C C      . GLY   B 1 110 ? 22.56700  23.19600  -45.79900 1.000 37.10000  ? 76  GLY   B C      1 
ATOM   5556 O O      . GLY   B 1 110 ? 22.21300  23.92300  -46.73000 1.000 33.08000  ? 76  GLY   B O      1 
ATOM   5557 H H      . GLY   B 1 110 ? 20.52700  21.23700  -46.25800 1.000 34.30000  ? 76  GLY   B H      1 
ATOM   5558 H HA2    . GLY   B 1 110 ? 22.27400  21.36700  -44.93900 1.000 34.27000  ? 76  GLY   B HA2    1 
ATOM   5559 H HA3    . GLY   B 1 110 ? 23.22500  21.30100  -46.19100 1.000 34.27000  ? 76  GLY   B HA3    1 
ATOM   5560 N N      . PHE   B 1 111 ? 23.16100  23.66400  -44.69200 1.000 36.68000  ? 77  PHE   B N      1 
ATOM   5561 C CA     . PHE   B 1 111 ? 23.28800  25.09800  -44.43200 1.000 33.83000  ? 77  PHE   B CA     1 
ATOM   5562 C C      . PHE   B 1 111 ? 24.06900  25.81000  -45.53400 1.000 38.31000  ? 77  PHE   B C      1 
ATOM   5563 O O      . PHE   B 1 111 ? 23.69300  26.91100  -45.95000 1.000 32.59000  ? 77  PHE   B O      1 
ATOM   5564 C CB     . PHE   B 1 111 ? 23.94400  25.30200  -43.05600 1.000 32.58000  ? 77  PHE   B CB     1 
ATOM   5565 C CG     . PHE   B 1 111 ? 24.31100  26.73600  -42.75100 1.000 34.87000  ? 77  PHE   B CG     1 
ATOM   5566 C CD1    . PHE   B 1 111 ? 23.33600  27.67000  -42.41700 1.000 36.07000  ? 77  PHE   B CD1    1 
ATOM   5567 C CD2    . PHE   B 1 111 ? 25.63500  27.14500  -42.77700 1.000 38.47000  ? 77  PHE   B CD2    1 
ATOM   5568 C CE1    . PHE   B 1 111 ? 23.67600  28.99400  -42.13800 1.000 39.00000  ? 77  PHE   B CE1    1 
ATOM   5569 C CE2    . PHE   B 1 111 ? 25.98500  28.45900  -42.49400 1.000 39.30000  ? 77  PHE   B CE2    1 
ATOM   5570 C CZ     . PHE   B 1 111 ? 25.00100  29.38800  -42.17600 1.000 38.64000  ? 77  PHE   B CZ     1 
ATOM   5571 H H      . PHE   B 1 111 ? 23.49800  23.16700  -44.07700 1.000 36.68000  ? 77  PHE   B H      1 
ATOM   5572 H HA     . PHE   B 1 111 ? 22.40100  25.48900  -44.39800 1.000 33.83000  ? 77  PHE   B HA     1 
ATOM   5573 H HB2    . PHE   B 1 111 ? 23.32700  25.00300  -42.37000 1.000 32.58000  ? 77  PHE   B HB2    1 
ATOM   5574 H HB3    . PHE   B 1 111 ? 24.75700  24.77500  -43.01800 1.000 32.58000  ? 77  PHE   B HB3    1 
ATOM   5575 H HD1    . PHE   B 1 111 ? 22.44300  27.41200  -42.39600 1.000 36.07000  ? 77  PHE   B HD1    1 
ATOM   5576 H HD2    . PHE   B 1 111 ? 26.29900  26.53100  -42.99400 1.000 38.47000  ? 77  PHE   B HD2    1 
ATOM   5577 H HE1    . PHE   B 1 111 ? 23.01300  29.60900  -41.92100 1.000 39.00000  ? 77  PHE   B HE1    1 
ATOM   5578 H HE2    . PHE   B 1 111 ? 26.87800  28.71900  -42.52200 1.000 39.30000  ? 77  PHE   B HE2    1 
ATOM   5579 H HZ     . PHE   B 1 111 ? 25.23300  30.26800  -41.98400 1.000 38.64000  ? 77  PHE   B HZ     1 
ATOM   5580 N N      . ASP   B 1 112 ? 25.16500  25.21100  -46.02500 1.000 33.62000  ? 78  ASP   B N      1 
ATOM   5581 C CA     . ASP   B 1 112 ? 25.97400  25.91700  -47.01700 1.000 31.78000  ? 78  ASP   B CA     1 
ATOM   5582 C C      . ASP   B 1 112 ? 25.15000  26.28700  -48.24900 1.000 30.57000  ? 78  ASP   B C      1 
ATOM   5583 O O      . ASP   B 1 112 ? 25.39200  27.32000  -48.88700 1.000 33.18000  ? 78  ASP   B O      1 
ATOM   5584 C CB     . ASP   B 1 112 ? 27.18200  25.05700  -47.42600 1.000 34.59000  ? 78  ASP   B CB     1 
ATOM   5585 C CG     . ASP   B 1 112 ? 28.19000  24.87500  -46.28600 1.000 46.14000  ? 78  ASP   B CG     1 
ATOM   5586 O OD1    . ASP   B 1 112 ? 27.88500  25.27200  -45.14700 1.000 51.63000  ? 78  ASP   B OD1    1 
ATOM   5587 O OD2    . ASP   B 1 112 ? 29.29000  24.33900  -46.53300 1.000 49.81000  ? 78  ASP   B OD2    1 
ATOM   5588 H H      . ASP   B 1 112 ? 25.44800  24.42900  -45.80800 1.000 33.62000  ? 78  ASP   B H      1 
ATOM   5589 H HA     . ASP   B 1 112 ? 26.31000  26.73800  -46.62400 1.000 31.78000  ? 78  ASP   B HA     1 
ATOM   5590 H HB2    . ASP   B 1 112 ? 26.86900  24.17900  -47.69300 1.000 34.59000  ? 78  ASP   B HB2    1 
ATOM   5591 H HB3    . ASP   B 1 112 ? 27.64000  25.48600  -48.16600 1.000 34.59000  ? 78  ASP   B HB3    1 
ATOM   5592 N N      . PHE   B 1 113 ? 24.19600  25.43500  -48.60600 1.000 31.88000  ? 79  PHE   B N      1 
ATOM   5593 C CA     . PHE   B 1 113 ? 23.34000  25.69900  -49.75700 1.000 32.12000  ? 79  PHE   B CA     1 
ATOM   5594 C C      . PHE   B 1 113 ? 22.44800  26.91800  -49.51400 1.000 29.39000  ? 79  PHE   B C      1 
ATOM   5595 O O      . PHE   B 1 113 ? 22.36200  27.81700  -50.35400 1.000 30.43000  ? 79  PHE   B O      1 
ATOM   5596 C CB     . PHE   B 1 113 ? 22.49400  24.45500  -50.03400 1.000 29.98000  ? 79  PHE   B CB     1 
ATOM   5597 C CG     . PHE   B 1 113 ? 21.52100  24.62900  -51.15200 1.000 33.91000  ? 79  PHE   B CG     1 
ATOM   5598 C CD1    . PHE   B 1 113 ? 21.91400  24.44100  -52.46200 1.000 33.18000  ? 79  PHE   B CD1    1 
ATOM   5599 C CD2    . PHE   B 1 113 ? 20.20800  24.99500  -50.89400 1.000 33.08000  ? 79  PHE   B CD2    1 
ATOM   5600 C CE1    . PHE   B 1 113 ? 21.01400  24.59800  -53.50300 1.000 44.43000  ? 79  PHE   B CE1    1 
ATOM   5601 C CE2    . PHE   B 1 113 ? 19.30200  25.15200  -51.92700 1.000 39.00000  ? 79  PHE   B CE2    1 
ATOM   5602 C CZ     . PHE   B 1 113 ? 19.70800  24.95700  -53.23500 1.000 43.66000  ? 79  PHE   B CZ     1 
ATOM   5603 H H      . PHE   B 1 113 ? 24.02300  24.69700  -48.19900 1.000 31.88000  ? 79  PHE   B H      1 
ATOM   5604 H HA     . PHE   B 1 113 ? 23.89200  25.87400  -50.53500 1.000 32.12000  ? 79  PHE   B HA     1 
ATOM   5605 H HB2    . PHE   B 1 113 ? 23.08400  23.72000  -50.26500 1.000 29.98000  ? 79  PHE   B HB2    1 
ATOM   5606 H HB3    . PHE   B 1 113 ? 21.99100  24.23400  -49.23500 1.000 29.98000  ? 79  PHE   B HB3    1 
ATOM   5607 H HD1    . PHE   B 1 113 ? 22.79200  24.19700  -52.64700 1.000 33.18000  ? 79  PHE   B HD1    1 
ATOM   5608 H HD2    . PHE   B 1 113 ? 19.93100  25.12400  -50.01600 1.000 33.08000  ? 79  PHE   B HD2    1 
ATOM   5609 H HE1    . PHE   B 1 113 ? 21.29000  24.46600  -54.38100 1.000 44.43000  ? 79  PHE   B HE1    1 
ATOM   5610 H HE2    . PHE   B 1 113 ? 18.42300  25.39600  -51.74300 1.000 39.00000  ? 79  PHE   B HE2    1 
ATOM   5611 H HZ     . PHE   B 1 113 ? 19.10200  25.06600  -53.93200 1.000 43.66000  ? 79  PHE   B HZ     1 
ATOM   5612 N N      . TYR   B 1 114 ? 21.76000  26.95700  -48.36500 1.000 30.27000  ? 80  TYR   B N      1 
ATOM   5613 C CA     . TYR   B 1 114 ? 20.85400  28.08200  -48.11000 1.000 27.34000  ? 80  TYR   B CA     1 
ATOM   5614 C C      . TYR   B 1 114 ? 21.61800  29.36600  -47.82600 1.000 28.26000  ? 80  TYR   B C      1 
ATOM   5615 O O      . TYR   B 1 114 ? 21.14700  30.45800  -48.18000 1.000 30.66000  ? 80  TYR   B O      1 
ATOM   5616 C CB     . TYR   B 1 114 ? 19.88600  27.71700  -46.98000 1.000 28.20000  ? 80  TYR   B CB     1 
ATOM   5617 C CG     . TYR   B 1 114 ? 19.07100  26.51100  -47.38600 1.000 32.42000  ? 80  TYR   B CG     1 
ATOM   5618 C CD1    . TYR   B 1 114 ? 18.06200  26.61600  -48.33900 1.000 30.59000  ? 80  TYR   B CD1    1 
ATOM   5619 C CD2    . TYR   B 1 114 ? 19.37300  25.24900  -46.87600 1.000 34.47000  ? 80  TYR   B CD2    1 
ATOM   5620 C CE1    . TYR   B 1 114 ? 17.34200  25.48100  -48.74800 1.000 31.57000  ? 80  TYR   B CE1    1 
ATOM   5621 C CE2    . TYR   B 1 114 ? 18.66300  24.12700  -47.26900 1.000 33.30000  ? 80  TYR   B CE2    1 
ATOM   5622 C CZ     . TYR   B 1 114 ? 17.65400  24.24800  -48.21000 1.000 33.16000  ? 80  TYR   B CZ     1 
ATOM   5623 O OH     . TYR   B 1 114 ? 16.97900  23.10300  -48.58900 1.000 34.83000  ? 80  TYR   B OH     1 
ATOM   5624 H H      . TYR   B 1 114 ? 21.79800  26.36800  -47.74000 1.000 30.27000  ? 80  TYR   B H      1 
ATOM   5625 H HA     . TYR   B 1 114 ? 20.32300  28.23300  -48.90800 1.000 27.34000  ? 80  TYR   B HA     1 
ATOM   5626 H HB2    . TYR   B 1 114 ? 20.38700  27.49800  -46.17900 1.000 28.20000  ? 80  TYR   B HB2    1 
ATOM   5627 H HB3    . TYR   B 1 114 ? 19.28300  28.45800  -46.81500 1.000 28.20000  ? 80  TYR   B HB3    1 
ATOM   5628 H HD1    . TYR   B 1 114 ? 17.85800  27.44700  -48.70400 1.000 30.59000  ? 80  TYR   B HD1    1 
ATOM   5629 H HD2    . TYR   B 1 114 ? 20.05400  25.16100  -46.24800 1.000 34.47000  ? 80  TYR   B HD2    1 
ATOM   5630 H HE1    . TYR   B 1 114 ? 16.66200  25.55900  -49.37800 1.000 31.57000  ? 80  TYR   B HE1    1 
ATOM   5631 H HE2    . TYR   B 1 114 ? 18.87200  23.29400  -46.91300 1.000 33.30000  ? 80  TYR   B HE2    1 
ATOM   5632 H HH     . TYR   B 1 114 ? 16.47400  23.27000  -49.23900 1.000 34.83000  ? 80  TYR   B HH     1 
ATOM   5633 N N      . LEU   B 1 115 ? 22.79800  29.25900  -47.21200 1.000 33.20000  ? 81  LEU   B N      1 
ATOM   5634 C CA     . LEU   B 1 115 ? 23.66000  30.42600  -47.03700 1.000 31.59000  ? 81  LEU   B CA     1 
ATOM   5635 C C      . LEU   B 1 115 ? 24.04300  31.02100  -48.38400 1.000 31.73000  ? 81  LEU   B C      1 
ATOM   5636 O O      . LEU   B 1 115 ? 23.97800  32.24400  -48.58500 1.000 33.95000  ? 81  LEU   B O      1 
ATOM   5637 C CB     . LEU   B 1 115 ? 24.91400  30.03100  -46.24500 1.000 28.62000  ? 81  LEU   B CB     1 
ATOM   5638 C CG     . LEU   B 1 115 ? 25.82100  31.21700  -45.88700 1.000 41.79000  ? 81  LEU   B CG     1 
ATOM   5639 C CD1    . LEU   B 1 115 ? 25.06200  32.20300  -44.99700 1.000 38.98000  ? 81  LEU   B CD1    1 
ATOM   5640 C CD2    . LEU   B 1 115 ? 27.12100  30.78000  -45.22600 1.000 41.65000  ? 81  LEU   B CD2    1 
ATOM   5641 H H      . LEU   B 1 115 ? 23.11900  28.52900  -46.89100 1.000 33.20000  ? 81  LEU   B H      1 
ATOM   5642 H HA     . LEU   B 1 115 ? 23.17700  31.10000  -46.53500 1.000 31.59000  ? 81  LEU   B HA     1 
ATOM   5643 H HB2    . LEU   B 1 115 ? 24.64000  29.60700  -45.41700 1.000 28.62000  ? 81  LEU   B HB2    1 
ATOM   5644 H HB3    . LEU   B 1 115 ? 25.43600  29.40900  -46.77600 1.000 28.62000  ? 81  LEU   B HB3    1 
ATOM   5645 H HG     . LEU   B 1 115 ? 26.05600  31.68400  -46.70400 1.000 41.79000  ? 81  LEU   B HG     1 
ATOM   5646 H HD11   . LEU   B 1 115 ? 25.69600  32.82500  -44.60600 1.000 38.98000  ? 81  LEU   B HD11   1 
ATOM   5647 H HD12   . LEU   B 1 115 ? 24.41600  32.68600  -45.53600 1.000 38.98000  ? 81  LEU   B HD12   1 
ATOM   5648 H HD13   . LEU   B 1 115 ? 24.60800  31.71000  -44.29600 1.000 38.98000  ? 81  LEU   B HD13   1 
ATOM   5649 H HD21   . LEU   B 1 115 ? 27.66500  31.56400  -45.05100 1.000 41.65000  ? 81  LEU   B HD21   1 
ATOM   5650 H HD22   . LEU   B 1 115 ? 26.91500  30.32800  -44.39300 1.000 41.65000  ? 81  LEU   B HD22   1 
ATOM   5651 H HD23   . LEU   B 1 115 ? 27.59100  30.17700  -45.82300 1.000 41.65000  ? 81  LEU   B HD23   1 
ATOM   5652 N N      . ALA   B 1 116 ? 24.44200  30.15800  -49.32500 1.000 32.76000  ? 82  ALA   B N      1 
ATOM   5653 C CA     . ALA   B 1 116 ? 24.77200  30.58500  -50.68400 1.000 30.95000  ? 82  ALA   B CA     1 
ATOM   5654 C C      . ALA   B 1 116 ? 23.57000  31.20900  -51.39300 1.000 34.07000  ? 82  ALA   B C      1 
ATOM   5655 O O      . ALA   B 1 116 ? 23.71200  32.21600  -52.09100 1.000 36.31000  ? 82  ALA   B O      1 
ATOM   5656 C CB     . ALA   B 1 116 ? 25.29300  29.37900  -51.48800 1.000 33.44000  ? 82  ALA   B CB     1 
ATOM   5657 H H      . ALA   B 1 116 ? 24.52900  29.31200  -49.19700 1.000 32.76000  ? 82  ALA   B H      1 
ATOM   5658 H HA     . ALA   B 1 116 ? 25.47800  31.25000  -50.64500 1.000 30.95000  ? 82  ALA   B HA     1 
ATOM   5659 H HB1    . ALA   B 1 116 ? 25.51600  29.67100  -52.38600 1.000 33.44000  ? 82  ALA   B HB1    1 
ATOM   5660 H HB2    . ALA   B 1 116 ? 26.08200  29.02500  -51.04900 1.000 33.44000  ? 82  ALA   B HB2    1 
ATOM   5661 H HB3    . ALA   B 1 116 ? 24.60100  28.70000  -51.52200 1.000 33.44000  ? 82  ALA   B HB3    1 
ATOM   5662 N N      . TYR   B 1 117 ? 22.38500  30.60700  -51.26100 1.000 31.97000  ? 83  TYR   B N      1 
ATOM   5663 C CA     . TYR   B 1 117 ? 21.20300  31.23300  -51.83600 1.000 30.18000  ? 83  TYR   B CA     1 
ATOM   5664 C C      . TYR   B 1 117 ? 21.02800  32.65300  -51.29400 1.000 30.72000  ? 83  TYR   B C      1 
ATOM   5665 O O      . TYR   B 1 117 ? 20.83900  33.61100  -52.06200 1.000 31.05000  ? 83  TYR   B O      1 
ATOM   5666 C CB     . TYR   B 1 117 ? 19.95000  30.37700  -51.56900 1.000 30.14000  ? 83  TYR   B CB     1 
ATOM   5667 C CG     . TYR   B 1 117 ? 18.72300  31.08600  -52.09100 1.000 32.86000  ? 83  TYR   B CG     1 
ATOM   5668 C CD1    . TYR   B 1 117 ? 18.36800  31.01100  -53.43900 1.000 33.26000  ? 83  TYR   B CD1    1 
ATOM   5669 C CD2    . TYR   B 1 117 ? 17.95300  31.89400  -51.24900 1.000 28.51000  ? 83  TYR   B CD2    1 
ATOM   5670 C CE1    . TYR   B 1 117 ? 17.27700  31.70600  -53.92000 1.000 38.08000  ? 83  TYR   B CE1    1 
ATOM   5671 C CE2    . TYR   B 1 117 ? 16.86300  32.58300  -51.72100 1.000 31.55000  ? 83  TYR   B CE2    1 
ATOM   5672 C CZ     . TYR   B 1 117 ? 16.52900  32.49200  -53.05200 1.000 34.75000  ? 83  TYR   B CZ     1 
ATOM   5673 O OH     . TYR   B 1 117 ? 15.44300  33.18600  -53.51900 1.000 31.89000  ? 83  TYR   B OH     1 
ATOM   5674 H H      . TYR   B 1 117 ? 22.24500  29.86100  -50.85700 1.000 31.97000  ? 83  TYR   B H      1 
ATOM   5675 H HA     . TYR   B 1 117 ? 21.32000  31.29500  -52.79700 1.000 30.18000  ? 83  TYR   B HA     1 
ATOM   5676 H HB2    . TYR   B 1 117 ? 20.03400  29.52600  -52.02700 1.000 30.14000  ? 83  TYR   B HB2    1 
ATOM   5677 H HB3    . TYR   B 1 117 ? 19.84600  30.24200  -50.61400 1.000 30.14000  ? 83  TYR   B HB3    1 
ATOM   5678 H HD1    . TYR   B 1 117 ? 18.87700  30.49300  -54.02100 1.000 33.26000  ? 83  TYR   B HD1    1 
ATOM   5679 H HD2    . TYR   B 1 117 ? 18.18400  31.96600  -50.35100 1.000 28.51000  ? 83  TYR   B HD2    1 
ATOM   5680 H HE1    . TYR   B 1 117 ? 17.04200  31.64600  -54.81800 1.000 38.08000  ? 83  TYR   B HE1    1 
ATOM   5681 H HE2    . TYR   B 1 117 ? 16.35800  33.11200  -51.14600 1.000 31.55000  ? 83  TYR   B HE2    1 
ATOM   5682 H HH     . TYR   B 1 117 ? 14.96700  33.44000  -52.87500 1.000 31.89000  ? 83  TYR   B HH     1 
ATOM   5683 N N      . SER   B 1 118 ? 21.10200  32.80300  -49.96400 1.000 28.59000  ? 84  SER   B N      1 
ATOM   5684 C CA     . SER   B 1 118 ? 20.93200  34.11600  -49.32700 1.000 29.84000  ? 84  SER   B CA     1 
ATOM   5685 C C      . SER   B 1 118 ? 22.00300  35.10200  -49.77200 1.000 39.96000  ? 84  SER   B C      1 
ATOM   5686 O O      . SER   B 1 118 ? 21.73600  36.29800  -49.95000 1.000 34.02000  ? 84  SER   B O      1 
ATOM   5687 C CB     . SER   B 1 118 ? 21.00100  33.95900  -47.80600 1.000 32.02000  ? 84  SER   B CB     1 
ATOM   5688 O OG     . SER   B 1 118 ? 20.04800  33.00200  -47.34200 1.000 37.39000  ? 84  SER   B OG     1 
ATOM   5689 H H      . SER   B 1 118 ? 21.24900  32.16100  -49.41100 1.000 28.59000  ? 84  SER   B H      1 
ATOM   5690 H HA     . SER   B 1 118 ? 20.06300  34.47900  -49.56000 1.000 29.84000  ? 84  SER   B HA     1 
ATOM   5691 H HB2    . SER   B 1 118 ? 21.89100  33.66100  -47.56000 1.000 32.02000  ? 84  SER   B HB2    1 
ATOM   5692 H HB3    . SER   B 1 118 ? 20.81300  34.81600  -47.39200 1.000 32.02000  ? 84  SER   B HB3    1 
ATOM   5693 H HG     . SER   B 1 118 ? 20.20600  32.25000  -47.68200 1.000 37.39000  ? 84  SER   B HG     1 
ATOM   5694 N N      . ALA   B 1 119 ? 23.23300  34.62400  -49.90900 1.000 36.05000  ? 85  ALA   B N      1 
ATOM   5695 C CA     . ALA   B 1 119 ? 24.36700  35.50600  -50.16300 1.000 33.62000  ? 85  ALA   B CA     1 
ATOM   5696 C C      . ALA   B 1 119 ? 24.43500  35.93500  -51.62500 1.000 35.76000  ? 85  ALA   B C      1 
ATOM   5697 O O      . ALA   B 1 119 ? 24.80400  37.07800  -51.92700 1.000 42.18000  ? 85  ALA   B O      1 
ATOM   5698 C CB     . ALA   B 1 119 ? 25.66100  34.79600  -49.74800 1.000 35.61000  ? 85  ALA   B CB     1 
ATOM   5699 H H      . ALA   B 1 119 ? 23.44000  33.79100  -49.85900 1.000 36.05000  ? 85  ALA   B H      1 
ATOM   5700 H HA     . ALA   B 1 119 ? 24.27500  36.30400  -49.62000 1.000 33.62000  ? 85  ALA   B HA     1 
ATOM   5701 H HB1    . ALA   B 1 119 ? 26.41200  35.38500  -49.91800 1.000 35.61000  ? 85  ALA   B HB1    1 
ATOM   5702 H HB2    . ALA   B 1 119 ? 25.61500  34.58300  -48.80300 1.000 35.61000  ? 85  ALA   B HB2    1 
ATOM   5703 H HB3    . ALA   B 1 119 ? 25.75400  33.98200  -50.26700 1.000 35.61000  ? 85  ALA   B HB3    1 
ATOM   5704 N N      . ARG   B 1 120 ? 24.07900  35.03800  -52.54800 1.000 38.81000  ? 86  ARG   B N      1 
ATOM   5705 C CA     . ARG   B 1 120 ? 24.42200  35.21300  -53.95800 1.000 35.45000  ? 86  ARG   B CA     1 
ATOM   5706 C C      . ARG   B 1 120 ? 23.25500  35.09200  -54.92800 1.000 46.73000  ? 86  ARG   B C      1 
ATOM   5707 O O      . ARG   B 1 120 ? 23.34400  35.64200  -56.03100 1.000 50.06000  ? 86  ARG   B O      1 
ATOM   5708 C CB     . ARG   B 1 120 ? 25.49100  34.17800  -54.37700 1.000 40.49000  ? 86  ARG   B CB     1 
ATOM   5709 C CG     . ARG   B 1 120 ? 26.76100  34.15300  -53.52400 1.000 47.85000  ? 86  ARG   B CG     1 
ATOM   5710 C CD     . ARG   B 1 120 ? 27.75300  35.26700  -53.88100 1.000 55.72000  ? 86  ARG   B CD     1 
ATOM   5711 N NE     . ARG   B 1 120 ? 28.88000  35.32700  -52.94900 1.000 75.64000  ? 86  ARG   B NE     1 
ATOM   5712 C CZ     . ARG   B 1 120 ? 30.09400  34.83800  -53.17700 1.000 70.01000  ? 86  ARG   B CZ     1 
ATOM   5713 N NH1    . ARG   B 1 120 ? 30.40900  34.27300  -54.32400 1.000 71.71000  ? 86  ARG   B NH1    1 
ATOM   5714 N NH2    . ARG   B 1 120 ? 31.01800  34.91600  -52.22500 1.000 75.48000  ? 86  ARG   B NH2    1 
ATOM   5715 H H      . ARG   B 1 120 ? 23.63800  34.31900  -52.38100 1.000 38.81000  ? 86  ARG   B H      1 
ATOM   5716 H HA     . ARG   B 1 120 ? 24.80800  36.09400  -54.07800 1.000 35.45000  ? 86  ARG   B HA     1 
ATOM   5717 H HB2    . ARG   B 1 120 ? 25.09500  33.29400  -54.33300 1.000 40.49000  ? 86  ARG   B HB2    1 
ATOM   5718 H HB3    . ARG   B 1 120 ? 25.75800  34.36700  -55.29000 1.000 40.49000  ? 86  ARG   B HB3    1 
ATOM   5719 H HG2    . ARG   B 1 120 ? 26.51900  34.25700  -52.59100 1.000 47.85000  ? 86  ARG   B HG2    1 
ATOM   5720 H HG3    . ARG   B 1 120 ? 27.20900  33.30300  -53.65500 1.000 47.85000  ? 86  ARG   B HG3    1 
ATOM   5721 H HD2    . ARG   B 1 120 ? 28.08900  35.11900  -54.77700 1.000 55.72000  ? 86  ARG   B HD2    1 
ATOM   5722 H HD3    . ARG   B 1 120 ? 27.29100  36.11900  -53.84100 1.000 55.72000  ? 86  ARG   B HD3    1 
ATOM   5723 H HE     . ARG   B 1 120 ? 28.74500  35.71100  -52.19100 1.000 75.64000  ? 86  ARG   B HE     1 
ATOM   5724 H HH11   . ARG   B 1 120 ? 29.82200  34.21400  -54.94700 1.000 71.71000  ? 86  ARG   B HH11   1 
ATOM   5725 H HH12   . ARG   B 1 120 ? 31.20200  33.96400  -54.44800 1.000 71.71000  ? 86  ARG   B HH12   1 
ATOM   5726 H HH21   . ARG   B 1 120 ? 30.82800  35.28300  -51.47100 1.000 75.48000  ? 86  ARG   B HH21   1 
ATOM   5727 H HH22   . ARG   B 1 120 ? 31.80700  34.60400  -52.36500 1.000 75.48000  ? 86  ARG   B HH22   1 
ATOM   5728 N N      . HIS   B 1 121 ? 22.18500  34.37800  -54.58700 1.000 37.70000  ? 87  HIS   B N      1 
ATOM   5729 C CA     . HIS   B 1 121 ? 21.12600  34.10700  -55.55300 1.000 31.88000  ? 87  HIS   B CA     1 
ATOM   5730 C C      . HIS   B 1 121 ? 19.86200  34.91600  -55.32900 1.000 37.08000  ? 87  HIS   B C      1 
ATOM   5731 O O      . HIS   B 1 121 ? 19.18000  35.24300  -56.30300 1.000 42.14000  ? 87  HIS   B O      1 
ATOM   5732 C CB     . HIS   B 1 121 ? 20.75900  32.61600  -55.53800 1.000 37.54000  ? 87  HIS   B CB     1 
ATOM   5733 C CG     . HIS   B 1 121 ? 21.89200  31.70900  -55.90700 1.000 47.45000  ? 87  HIS   B CG     1 
ATOM   5734 N ND1    . HIS   B 1 121 ? 21.95600  30.39300  -55.49500 1.000 51.71000  ? 87  HIS   B ND1    1 
ATOM   5735 C CD2    . HIS   B 1 121 ? 23.00000  31.92500  -56.65400 1.000 57.96000  ? 87  HIS   B CD2    1 
ATOM   5736 C CE1    . HIS   B 1 121 ? 23.06000  29.83900  -55.96700 1.000 58.23000  ? 87  HIS   B CE1    1 
ATOM   5737 N NE2    . HIS   B 1 121 ? 23.71000  30.74600  -56.67600 1.000 52.50000  ? 87  HIS   B NE2    1 
ATOM   5738 H H      . HIS   B 1 121 ? 22.04900  34.04100  -53.80700 1.000 37.70000  ? 87  HIS   B H      1 
ATOM   5739 H HA     . HIS   B 1 121 ? 21.45100  34.31600  -56.44200 1.000 31.88000  ? 87  HIS   B HA     1 
ATOM   5740 H HB2    . HIS   B 1 121 ? 20.46800  32.37700  -54.64500 1.000 37.54000  ? 87  HIS   B HB2    1 
ATOM   5741 H HB3    . HIS   B 1 121 ? 20.03900  32.46500  -56.17000 1.000 37.54000  ? 87  HIS   B HB3    1 
ATOM   5742 H HD1    . HIS   B 1 121 ? 21.37200  29.99700  -55.00300 1.000 51.71000  ? 87  HIS   B HD1    1 
ATOM   5743 H HD2    . HIS   B 1 121 ? 23.23800  32.72100  -57.07200 1.000 57.96000  ? 87  HIS   B HD2    1 
ATOM   5744 H HE1    . HIS   B 1 121 ? 23.33000  28.96000  -55.82800 1.000 58.23000  ? 87  HIS   B HE1    1 
ATOM   5745 N N      . HIS   B 1 122 ? 19.52400  35.24600  -54.08500 1.000 36.49000  ? 88  HIS   B N      1 
ATOM   5746 C CA     . HIS   B 1 122 ? 18.23300  35.87700  -53.82900 1.000 33.49000  ? 88  HIS   B CA     1 
ATOM   5747 C C      . HIS   B 1 122 ? 18.19400  37.31700  -54.31700 1.000 35.48000  ? 88  HIS   B C      1 
ATOM   5748 O O      . HIS   B 1 122 ? 19.12400  38.09800  -54.08600 1.000 34.94000  ? 88  HIS   B O      1 
ATOM   5749 C CB     . HIS   B 1 122 ? 17.86900  35.86300  -52.33900 1.000 31.04000  ? 88  HIS   B CB     1 
ATOM   5750 C CG     . HIS   B 1 122 ? 16.50200  36.42200  -52.09500 1.000 32.45000  ? 88  HIS   B CG     1 
ATOM   5751 N ND1    . HIS   B 1 122 ? 15.36400  35.76900  -52.51900 1.000 29.41000  ? 88  HIS   B ND1    1 
ATOM   5752 C CD2    . HIS   B 1 122 ? 16.08700  37.60800  -51.58300 1.000 30.63000  ? 88  HIS   B CD2    1 
ATOM   5753 C CE1    . HIS   B 1 122 ? 14.30100  36.50100  -52.22800 1.000 35.87000  ? 88  HIS   B CE1    1 
ATOM   5754 N NE2    . HIS   B 1 122 ? 14.71000  37.62000  -51.65200 1.000 33.42000  ? 88  HIS   B NE2    1 
ATOM   5755 H H      . HIS   B 1 122 ? 20.01100  35.11900  -53.38800 1.000 36.49000  ? 88  HIS   B H      1 
ATOM   5756 H HA     . HIS   B 1 122 ? 17.54700  35.38500  -54.30600 1.000 33.49000  ? 88  HIS   B HA     1 
ATOM   5757 H HB2    . HIS   B 1 122 ? 17.89700  34.95500  -52.00900 1.000 31.04000  ? 88  HIS   B HB2    1 
ATOM   5758 H HB3    . HIS   B 1 122 ? 18.50600  36.41100  -51.85400 1.000 31.04000  ? 88  HIS   B HB3    1 
ATOM   5759 H HD2    . HIS   B 1 122 ? 16.62700  38.27100  -51.21900 1.000 30.63000  ? 88  HIS   B HD2    1 
ATOM   5760 H HE1    . HIS   B 1 122 ? 13.41700  36.26600  -52.39400 1.000 35.87000  ? 88  HIS   B HE1    1 
ATOM   5761 H HE2    . HIS   B 1 122 ? 14.20100  38.25500  -51.37500 1.000 33.42000  ? 88  HIS   B HE2    1 
ATOM   5762 N N      . ASP   B 1 123 ? 17.08400  37.67900  -54.96100 1.000 33.69000  ? 89  ASP   B N      1 
ATOM   5763 C CA     . ASP   B 1 123 ? 16.85200  39.04700  -55.44200 1.000 34.94000  ? 89  ASP   B CA     1 
ATOM   5764 C C      . ASP   B 1 123 ? 16.16300  39.84800  -54.34300 1.000 34.96000  ? 89  ASP   B C      1 
ATOM   5765 O O      . ASP   B 1 123 ? 14.93600  39.81100  -54.21000 1.000 36.68000  ? 89  ASP   B O      1 
ATOM   5766 C CB     . ASP   B 1 123 ? 16.01500  39.01800  -56.71900 1.000 39.38000  ? 89  ASP   B CB     1 
ATOM   5767 C CG     . ASP   B 1 123 ? 15.86400  40.39200  -57.37100 1.000 50.02000  ? 89  ASP   B CG     1 
ATOM   5768 O OD1    . ASP   B 1 123 ? 16.25100  41.41300  -56.76500 1.000 44.09000  ? 89  ASP   B OD1    1 
ATOM   5769 O OD2    . ASP   B 1 123 ? 15.33900  40.43900  -58.50400 1.000 48.78000  ? 89  ASP   B OD2    1 
ATOM   5770 H H      . ASP   B 1 123 ? 16.43600  37.14100  -55.13600 1.000 33.69000  ? 89  ASP   B H      1 
ATOM   5771 H HA     . ASP   B 1 123 ? 17.70200  39.46800  -55.64200 1.000 34.94000  ? 89  ASP   B HA     1 
ATOM   5772 H HB2    . ASP   B 1 123 ? 16.44100  38.42800  -57.36100 1.000 39.38000  ? 89  ASP   B HB2    1 
ATOM   5773 H HB3    . ASP   B 1 123 ? 15.12800  38.68900  -56.50600 1.000 39.38000  ? 89  ASP   B HB3    1 
ATOM   5774 N N      . TYR   B 1 124 ? 16.94800  40.60300  -53.56400 1.000 34.34000  ? 90  TYR   B N      1 
ATOM   5775 C CA     . TYR   B 1 124 ? 16.38700  41.38300  -52.46300 1.000 34.64000  ? 90  TYR   B CA     1 
ATOM   5776 C C      . TYR   B 1 124 ? 15.58200  42.58200  -52.94400 1.000 36.95000  ? 90  TYR   B C      1 
ATOM   5777 O O      . TYR   B 1 124 ? 14.78000  43.11500  -52.17300 1.000 37.40000  ? 90  TYR   B O      1 
ATOM   5778 C CB     . TYR   B 1 124 ? 17.49500  41.85600  -51.50000 1.000 34.33000  ? 90  TYR   B CB     1 
ATOM   5779 C CG     . TYR   B 1 124 ? 18.10800  40.71400  -50.70000 1.000 35.04000  ? 90  TYR   B CG     1 
ATOM   5780 C CD1    . TYR   B 1 124 ? 19.20000  40.01700  -51.18500 1.000 34.35000  ? 90  TYR   B CD1    1 
ATOM   5781 C CD2    . TYR   B 1 124 ? 17.57900  40.33300  -49.46700 1.000 31.36000  ? 90  TYR   B CD2    1 
ATOM   5782 C CE1    . TYR   B 1 124 ? 19.75400  38.95500  -50.48000 1.000 32.85000  ? 90  TYR   B CE1    1 
ATOM   5783 C CE2    . TYR   B 1 124 ? 18.12700  39.27800  -48.73900 1.000 29.87000  ? 90  TYR   B CE2    1 
ATOM   5784 C CZ     . TYR   B 1 124 ? 19.22200  38.58700  -49.25500 1.000 33.24000  ? 90  TYR   B CZ     1 
ATOM   5785 O OH     . TYR   B 1 124 ? 19.77200  37.53800  -48.53500 1.000 32.76000  ? 90  TYR   B OH     1 
ATOM   5786 H H      . TYR   B 1 124 ? 17.80000  40.67800  -53.65400 1.000 34.34000  ? 90  TYR   B H      1 
ATOM   5787 H HA     . TYR   B 1 124 ? 15.78600  40.81300  -51.95800 1.000 34.64000  ? 90  TYR   B HA     1 
ATOM   5788 H HB2    . TYR   B 1 124 ? 18.20200  42.27600  -52.01400 1.000 34.33000  ? 90  TYR   B HB2    1 
ATOM   5789 H HB3    . TYR   B 1 124 ? 17.11800  42.49300  -50.87300 1.000 34.33000  ? 90  TYR   B HB3    1 
ATOM   5790 H HD1    . TYR   B 1 124 ? 19.55900  40.25200  -52.01000 1.000 34.35000  ? 90  TYR   B HD1    1 
ATOM   5791 H HD2    . TYR   B 1 124 ? 16.84400  40.78900  -49.12500 1.000 31.36000  ? 90  TYR   B HD2    1 
ATOM   5792 H HE1    . TYR   B 1 124 ? 20.48900  38.50100  -50.82400 1.000 32.85000  ? 90  TYR   B HE1    1 
ATOM   5793 H HE2    . TYR   B 1 124 ? 17.76300  39.03500  -47.91900 1.000 29.87000  ? 90  TYR   B HE2    1 
ATOM   5794 H HH     . TYR   B 1 124 ? 20.42300  37.21200  -48.95400 1.000 32.76000  ? 90  TYR   B HH     1 
ATOM   5795 N N      . SER   B 1 125 ? 15.77800  43.02800  -54.18400 1.000 39.48000  ? 91  SER   B N      1 
ATOM   5796 C CA     . SER   B 1 125 ? 14.90600  44.08200  -54.70300 1.000 41.00000  ? 91  SER   B CA     1 
ATOM   5797 C C      . SER   B 1 125 ? 13.48900  43.57800  -54.95300 1.000 43.22000  ? 91  SER   B C      1 
ATOM   5798 O O      . SER   B 1 125 ? 12.57000  44.39200  -55.07600 1.000 40.57000  ? 91  SER   B O      1 
ATOM   5799 C CB     . SER   B 1 125 ? 15.48700  44.66700  -55.99100 1.000 41.90000  ? 91  SER   B CB     1 
ATOM   5800 O OG     . SER   B 1 125 ? 15.21900  43.80700  -57.08200 1.000 46.97000  ? 91  SER   B OG     1 
ATOM   5801 H H      . SER   B 1 125 ? 16.38400  42.75000  -54.72700 1.000 39.48000  ? 91  SER   B H      1 
ATOM   5802 H HA     . SER   B 1 125 ? 14.85600  44.79700  -54.04900 1.000 41.00000  ? 91  SER   B HA     1 
ATOM   5803 H HB2    . SER   B 1 125 ? 15.08000  45.53100  -56.16000 1.000 41.90000  ? 91  SER   B HB2    1 
ATOM   5804 H HB3    . SER   B 1 125 ? 16.44700  44.76400  -55.89100 1.000 41.90000  ? 91  SER   B HB3    1 
ATOM   5805 H HG     . SER   B 1 125 ? 15.56500  43.05400  -56.94600 1.000 46.97000  ? 91  SER   B HG     1 
ATOM   5806 N N      . ARG   B 1 126 ? 13.29600  42.25300  -55.03600 1.000 38.87000  ? 92  ARG   B N      1 
ATOM   5807 C CA     . ARG   B 1 126 ? 11.96000  41.67600  -55.16900 1.000 32.97000  ? 92  ARG   B CA     1 
ATOM   5808 C C      . ARG   B 1 126 ? 11.23400  41.62900  -53.82600 1.000 39.88000  ? 92  ARG   B C      1 
ATOM   5809 O O      . ARG   B 1 126 ? 10.05800  42.00000  -53.74100 1.000 37.22000  ? 92  ARG   B O      1 
ATOM   5810 C CB     . ARG   B 1 126 ? 12.05200  40.26400  -55.76200 1.000 36.90000  ? 92  ARG   B CB     1 
ATOM   5811 C CG     . ARG   B 1 126 ? 12.28600  40.17200  -57.27000 1.000 50.88000  ? 92  ARG   B CG     1 
ATOM   5812 C CD     . ARG   B 1 126 ? 11.01900  40.47400  -58.05900 1.000 53.21000  ? 92  ARG   B CD     1 
ATOM   5813 N NE     . ARG   B 1 126 ? 9.91700   39.60100  -57.67300 1.000 50.00000  ? 92  ARG   B NE     1 
ATOM   5814 C CZ     . ARG   B 1 126 ? 8.65500   39.99600  -57.59000 1.000 52.90000  ? 92  ARG   B CZ     1 
ATOM   5815 N NH1    . ARG   B 1 126 ? 8.30000   41.24000  -57.87400 1.000 52.25000  ? 92  ARG   B NH1    1 
ATOM   5816 N NH2    . ARG   B 1 126 ? 7.72700   39.12500  -57.20700 1.000 42.48000  ? 92  ARG   B NH2    1 
ATOM   5817 H H      . ARG   B 1 126 ? 13.92700  41.66900  -55.01800 1.000 38.87000  ? 92  ARG   B H      1 
ATOM   5818 H HA     . ARG   B 1 126 ? 11.43700  42.22400  -55.77500 1.000 32.97000  ? 92  ARG   B HA     1 
ATOM   5819 H HB2    . ARG   B 1 126 ? 12.78800  39.80400  -55.33100 1.000 36.90000  ? 92  ARG   B HB2    1 
ATOM   5820 H HB3    . ARG   B 1 126 ? 11.22600  39.79700  -55.56200 1.000 36.90000  ? 92  ARG   B HB3    1 
ATOM   5821 H HG2    . ARG   B 1 126 ? 12.96400  40.81600  -57.52800 1.000 50.88000  ? 92  ARG   B HG2    1 
ATOM   5822 H HG3    . ARG   B 1 126 ? 12.57500  39.27400  -57.49400 1.000 50.88000  ? 92  ARG   B HG3    1 
ATOM   5823 H HD2    . ARG   B 1 126 ? 10.76900  41.39500  -57.89100 1.000 53.21000  ? 92  ARG   B HD2    1 
ATOM   5824 H HD3    . ARG   B 1 126 ? 11.19300  40.34200  -59.00400 1.000 53.21000  ? 92  ARG   B HD3    1 
ATOM   5825 H HE     . ARG   B 1 126 ? 10.08400  38.76400  -57.56800 1.000 50.00000  ? 92  ARG   B HE     1 
ATOM   5826 H HH11   . ARG   B 1 126 ? 8.88500   41.81700  -58.12300 1.000 52.25000  ? 92  ARG   B HH11   1 
ATOM   5827 H HH12   . ARG   B 1 126 ? 7.47400   41.47100  -57.81200 1.000 52.25000  ? 92  ARG   B HH12   1 
ATOM   5828 H HH21   . ARG   B 1 126 ? 7.94800   38.31500  -57.02000 1.000 42.48000  ? 92  ARG   B HH21   1 
ATOM   5829 H HH22   . ARG   B 1 126 ? 6.90500   39.37000  -57.15000 1.000 42.48000  ? 92  ARG   B HH22   1 
ATOM   5830 N N      . LYS   B 1 127 ? 11.92000  41.15500  -52.76000 1.000 31.58000  ? 93  LYS   B N      1 
ATOM   5831 C CA     . LYS   B 1 127 ? 11.30900  41.02400  -51.44000 1.000 28.32000  ? 93  LYS   B CA     1 
ATOM   5832 C C      . LYS   B 1 127 ? 12.33400  40.57000  -50.40700 1.000 29.33000  ? 93  LYS   B C      1 
ATOM   5833 O O      . LYS   B 1 127 ? 13.35200  39.95000  -50.76600 1.000 32.04000  ? 93  LYS   B O      1 
ATOM   5834 C CB     . LYS   B 1 127 ? 10.14500  40.02200  -51.48900 1.000 27.33000  ? 93  LYS   B CB     1 
ATOM   5835 C CG     . LYS   B 1 127 ? 10.58500  38.59800  -51.82700 1.000 27.40000  ? 93  LYS   B CG     1 
ATOM   5836 C CD     . LYS   B 1 127 ? 9.39200   37.61900  -52.09500 1.000 25.94000  ? 93  LYS   B CD     1 
ATOM   5837 C CE     . LYS   B 1 127 ? 8.69700   37.96100  -53.42600 1.000 29.38000  ? 93  LYS   B CE     1 
ATOM   5838 N NZ     . LYS   B 1 127 ? 7.56200   37.05100  -53.74700 1.000 30.07000  ? 93  LYS   B NZ     1 
ATOM   5839 H H      . LYS   B 1 127 ? 12.74200  40.90500  -52.78800 1.000 31.58000  ? 93  LYS   B H      1 
ATOM   5840 H HA     . LYS   B 1 127 ? 10.95600  41.88700  -51.17700 1.000 28.32000  ? 93  LYS   B HA     1 
ATOM   5841 H HB2    . LYS   B 1 127 ? 9.71700   40.00000  -50.61900 1.000 27.33000  ? 93  LYS   B HB2    1 
ATOM   5842 H HB3    . LYS   B 1 127 ? 9.50700   40.30800  -52.16000 1.000 27.33000  ? 93  LYS   B HB3    1 
ATOM   5843 H HG2    . LYS   B 1 127 ? 11.13500  38.62100  -52.62500 1.000 27.40000  ? 93  LYS   B HG2    1 
ATOM   5844 H HG3    . LYS   B 1 127 ? 11.09700  38.24200  -51.08400 1.000 27.40000  ? 93  LYS   B HG3    1 
ATOM   5845 H HD2    . LYS   B 1 127 ? 9.72600   36.71000  -52.14800 1.000 25.94000  ? 93  LYS   B HD2    1 
ATOM   5846 H HD3    . LYS   B 1 127 ? 8.74200   37.69900  -51.38000 1.000 25.94000  ? 93  LYS   B HD3    1 
ATOM   5847 H HE2    . LYS   B 1 127 ? 8.34600   38.86400  -53.37700 1.000 29.38000  ? 93  LYS   B HE2    1 
ATOM   5848 H HE3    . LYS   B 1 127 ? 9.34600   37.89800  -54.14300 1.000 29.38000  ? 93  LYS   B HE3    1 
ATOM   5849 H HZ1    . LYS   B 1 127 ? 7.19300   37.28700  -54.52200 1.000 30.07000  ? 93  LYS   B HZ1    1 
ATOM   5850 H HZ2    . LYS   B 1 127 ? 7.85300   36.21200  -53.80800 1.000 30.07000  ? 93  LYS   B HZ2    1 
ATOM   5851 H HZ3    . LYS   B 1 127 ? 6.94500   37.09700  -53.10700 1.000 30.07000  ? 93  LYS   B HZ3    1 
ATOM   5852 N N      . PRO   B 1 128 ? 12.09400  40.82800  -49.12000 1.000 30.56000  ? 94  PRO   B N      1 
ATOM   5853 C CA     . PRO   B 1 128 ? 12.99600  40.31700  -48.08000 1.000 31.93000  ? 94  PRO   B CA     1 
ATOM   5854 C C      . PRO   B 1 128 ? 12.96500  38.80000  -47.98400 1.000 31.53000  ? 94  PRO   B C      1 
ATOM   5855 O O      . PRO   B 1 128 ? 12.02100  38.13300  -48.42100 1.000 31.81000  ? 94  PRO   B O      1 
ATOM   5856 C CB     . PRO   B 1 128 ? 12.45900  40.95800  -46.78600 1.000 29.78000  ? 94  PRO   B CB     1 
ATOM   5857 C CG     . PRO   B 1 128 ? 11.66000  42.12700  -47.24400 1.000 32.28000  ? 94  PRO   B CG     1 
ATOM   5858 C CD     . PRO   B 1 128 ? 11.06000  41.70500  -48.55100 1.000 32.51000  ? 94  PRO   B CD     1 
ATOM   5859 H HA     . PRO   B 1 128 ? 13.90500  40.61600  -48.23900 1.000 31.93000  ? 94  PRO   B HA     1 
ATOM   5860 H HB2    . PRO   B 1 128 ? 11.89900  40.32200  -46.31300 1.000 29.78000  ? 94  PRO   B HB2    1 
ATOM   5861 H HB3    . PRO   B 1 128 ? 13.20000  41.24500  -46.23000 1.000 29.78000  ? 94  PRO   B HB3    1 
ATOM   5862 H HG2    . PRO   B 1 128 ? 10.96900  42.33300  -46.59700 1.000 32.28000  ? 94  PRO   B HG2    1 
ATOM   5863 H HG3    . PRO   B 1 128 ? 12.24600  42.89000  -47.37000 1.000 32.28000  ? 94  PRO   B HG3    1 
ATOM   5864 H HD2    . PRO   B 1 128 ? 10.23800  41.21100  -48.40400 1.000 32.51000  ? 94  PRO   B HD2    1 
ATOM   5865 H HD3    . PRO   B 1 128 ? 10.91600  42.48100  -49.11400 1.000 32.51000  ? 94  PRO   B HD3    1 
ATOM   5866 N N      . LEU   B 1 129 ? 14.02600  38.26400  -47.37300 1.000 27.97000  ? 95  LEU   B N      1 
ATOM   5867 C CA     . LEU   B 1 129 ? 14.25400  36.82600  -47.24500 1.000 29.90000  ? 95  LEU   B CA     1 
ATOM   5868 C C      . LEU   B 1 129 ? 14.50500  36.44700  -45.79900 1.000 27.81000  ? 95  LEU   B C      1 
ATOM   5869 O O      . LEU   B 1 129 ? 15.25800  37.13100  -45.09600 1.000 28.90000  ? 95  LEU   B O      1 
ATOM   5870 C CB     . LEU   B 1 129 ? 15.47800  36.38700  -48.08400 1.000 29.66000  ? 95  LEU   B CB     1 
ATOM   5871 C CG     . LEU   B 1 129 ? 15.91700  34.93000  -47.92300 1.000 30.73000  ? 95  LEU   B CG     1 
ATOM   5872 C CD1    . LEU   B 1 129 ? 14.92200  33.94600  -48.54800 1.000 30.80000  ? 95  LEU   B CD1    1 
ATOM   5873 C CD2    . LEU   B 1 129 ? 17.29400  34.83500  -48.57800 1.000 27.64000  ? 95  LEU   B CD2    1 
ATOM   5874 H H      . LEU   B 1 129 ? 14.64900  38.73500  -47.01200 1.000 27.97000  ? 95  LEU   B H      1 
ATOM   5875 H HA     . LEU   B 1 129 ? 13.47400  36.34300  -47.56000 1.000 29.90000  ? 95  LEU   B HA     1 
ATOM   5876 H HB2    . LEU   B 1 129 ? 15.26900  36.52400  -49.02100 1.000 29.66000  ? 95  LEU   B HB2    1 
ATOM   5877 H HB3    . LEU   B 1 129 ? 16.23200  36.94500  -47.83700 1.000 29.66000  ? 95  LEU   B HB3    1 
ATOM   5878 H HG     . LEU   B 1 129 ? 16.01700  34.71100  -46.98400 1.000 30.73000  ? 95  LEU   B HG     1 
ATOM   5879 H HD11   . LEU   B 1 129 ? 15.24800  33.04200  -48.41800 1.000 30.80000  ? 95  LEU   B HD11   1 
ATOM   5880 H HD12   . LEU   B 1 129 ? 14.06000  34.05200  -48.11600 1.000 30.80000  ? 95  LEU   B HD12   1 
ATOM   5881 H HD13   . LEU   B 1 129 ? 14.84400  34.13600  -49.49600 1.000 30.80000  ? 95  LEU   B HD13   1 
ATOM   5882 H HD21   . LEU   B 1 129 ? 17.59400  33.91300  -48.55000 1.000 27.64000  ? 95  LEU   B HD21   1 
ATOM   5883 H HD22   . LEU   B 1 129 ? 17.22600  35.13300  -49.49900 1.000 27.64000  ? 95  LEU   B HD22   1 
ATOM   5884 H HD23   . LEU   B 1 129 ? 17.91500  35.40000  -48.09200 1.000 27.64000  ? 95  LEU   B HD23   1 
ATOM   5885 N N      . PHE   B 1 130 ? 13.89200  35.34500  -45.36100 1.000 25.49000  ? 96  PHE   B N      1 
ATOM   5886 C CA     . PHE   B 1 130 ? 14.19800  34.74300  -44.07900 1.000 25.94000  ? 96  PHE   B CA     1 
ATOM   5887 C C      . PHE   B 1 130 ? 14.90000  33.41400  -44.31000 1.000 31.10000  ? 96  PHE   B C      1 
ATOM   5888 O O      . PHE   B 1 130 ? 14.61800  32.71900  -45.29300 1.000 28.51000  ? 96  PHE   B O      1 
ATOM   5889 C CB     . PHE   B 1 130 ? 12.93400  34.49300  -43.25600 1.000 28.51000  ? 96  PHE   B CB     1 
ATOM   5890 C CG     . PHE   B 1 130 ? 12.17900  35.74300  -42.89000 1.000 27.06000  ? 96  PHE   B CG     1 
ATOM   5891 C CD1    . PHE   B 1 130 ? 11.27800  36.31400  -43.77500 1.000 29.01000  ? 96  PHE   B CD1    1 
ATOM   5892 C CD2    . PHE   B 1 130 ? 12.32900  36.30300  -41.62200 1.000 29.33000  ? 96  PHE   B CD2    1 
ATOM   5893 C CE1    . PHE   B 1 130 ? 10.55600  37.45000  -43.40500 1.000 30.79000  ? 96  PHE   B CE1    1 
ATOM   5894 C CE2    . PHE   B 1 130 ? 11.62100  37.44000  -41.24500 1.000 28.18000  ? 96  PHE   B CE2    1 
ATOM   5895 C CZ     . PHE   B 1 130 ? 10.74100  38.01900  -42.14100 1.000 29.38000  ? 96  PHE   B CZ     1 
ATOM   5896 H H      . PHE   B 1 130 ? 13.28500  34.92600  -45.80300 1.000 25.49000  ? 96  PHE   B H      1 
ATOM   5897 H HA     . PHE   B 1 130 ? 14.78700  35.32700  -43.57900 1.000 25.94000  ? 96  PHE   B HA     1 
ATOM   5898 H HB2    . PHE   B 1 130 ? 12.33600  33.92600  -43.76800 1.000 28.51000  ? 96  PHE   B HB2    1 
ATOM   5899 H HB3    . PHE   B 1 130 ? 13.18300  34.04600  -42.43200 1.000 28.51000  ? 96  PHE   B HB3    1 
ATOM   5900 H HD1    . PHE   B 1 130 ? 11.15700  35.94200  -44.61900 1.000 29.01000  ? 96  PHE   B HD1    1 
ATOM   5901 H HD2    . PHE   B 1 130 ? 12.92500  35.91800  -41.02100 1.000 29.33000  ? 96  PHE   B HD2    1 
ATOM   5902 H HE1    . PHE   B 1 130 ? 9.96500   37.84100  -44.00800 1.000 30.79000  ? 96  PHE   B HE1    1 
ATOM   5903 H HE2    . PHE   B 1 130 ? 11.74400  37.81100  -40.40100 1.000 28.18000  ? 96  PHE   B HE2    1 
ATOM   5904 H HZ     . PHE   B 1 130 ? 10.26100  38.77800  -41.89800 1.000 29.38000  ? 96  PHE   B HZ     1 
ATOM   5905 N N      . ILE   B 1 131 ? 15.80500  33.05800  -43.39900 1.000 27.46000  ? 97  ILE   B N      1 
ATOM   5906 C CA     . ILE   B 1 131 ? 16.47400  31.75600  -43.42500 1.000 26.16000  ? 97  ILE   B CA     1 
ATOM   5907 C C      . ILE   B 1 131 ? 16.14200  31.04600  -42.12200 1.000 28.18000  ? 97  ILE   B C      1 
ATOM   5908 O O      . ILE   B 1 131 ? 16.25800  31.64100  -41.05000 1.000 30.26000  ? 97  ILE   B O      1 
ATOM   5909 C CB     . ILE   B 1 131 ? 18.00600  31.90200  -43.62100 1.000 31.84000  ? 97  ILE   B CB     1 
ATOM   5910 C CG1    . ILE   B 1 131 ? 18.68600  30.53000  -43.68000 1.000 29.65000  ? 97  ILE   B CG1    1 
ATOM   5911 C CG2    . ILE   B 1 131 ? 18.68300  32.68200  -42.47400 1.000 30.43000  ? 97  ILE   B CG2    1 
ATOM   5912 C CD1    . ILE   B 1 131 ? 20.18300  30.64300  -44.07000 1.000 35.01000  ? 97  ILE   B CD1    1 
ATOM   5913 H H      . ILE   B 1 131 ? 16.05200  33.56000  -42.74600 1.000 27.46000  ? 97  ILE   B H      1 
ATOM   5914 H HA     . ILE   B 1 131 ? 16.12300  31.22600  -44.15800 1.000 26.16000  ? 97  ILE   B HA     1 
ATOM   5915 H HB     . ILE   B 1 131 ? 18.17100  32.36800  -44.45500 1.000 31.84000  ? 97  ILE   B HB     1 
ATOM   5916 H HG12   . ILE   B 1 131 ? 18.63200  30.10600  -42.80900 1.000 29.65000  ? 97  ILE   B HG12   1 
ATOM   5917 H HG13   . ILE   B 1 131 ? 18.24300  29.98400  -44.34600 1.000 29.65000  ? 97  ILE   B HG13   1 
ATOM   5918 H HG21   . ILE   B 1 131 ? 19.57900  32.93500  -42.74600 1.000 30.43000  ? 97  ILE   B HG21   1 
ATOM   5919 H HG22   . ILE   B 1 131 ? 18.16100  33.47700  -42.28300 1.000 30.43000  ? 97  ILE   B HG22   1 
ATOM   5920 H HG23   . ILE   B 1 131 ? 18.72100  32.11700  -41.68700 1.000 30.43000  ? 97  ILE   B HG23   1 
ATOM   5921 H HD11   . ILE   B 1 131 ? 20.51900  29.76000  -44.28900 1.000 35.01000  ? 97  ILE   B HD11   1 
ATOM   5922 H HD12   . ILE   B 1 131 ? 20.26400  31.22800  -44.84000 1.000 35.01000  ? 97  ILE   B HD12   1 
ATOM   5923 H HD13   . ILE   B 1 131 ? 20.68000  31.01000  -43.32200 1.000 35.01000  ? 97  ILE   B HD13   1 
ATOM   5924 N N      . SER   B 1 132 ? 15.68300  29.79500  -42.21200 1.000 29.22000  ? 98  SER   B N      1 
ATOM   5925 C CA     . SER   B 1 132 ? 15.33100  28.99700  -41.04700 1.000 27.30000  ? 98  SER   B CA     1 
ATOM   5926 C C      . SER   B 1 132 ? 16.46000  28.01500  -40.76300 1.000 35.58000  ? 98  SER   B C      1 
ATOM   5927 O O      . SER   B 1 132 ? 16.91900  27.32100  -41.66700 1.000 28.09000  ? 98  SER   B O      1 
ATOM   5928 C CB     . SER   B 1 132 ? 14.01800  28.24000  -41.28000 1.000 29.70000  ? 98  SER   B CB     1 
ATOM   5929 O OG     . SER   B 1 132 ? 13.69100  27.39100  -40.16800 1.000 32.43000  ? 98  SER   B OG     1 
ATOM   5930 H H      . SER   B 1 132 ? 15.56600  29.38200  -42.95700 1.000 29.22000  ? 98  SER   B H      1 
ATOM   5931 H HA     . SER   B 1 132 ? 15.22000  29.57600  -40.28000 1.000 27.30000  ? 98  SER   B HA     1 
ATOM   5932 H HB2    . SER   B 1 132 ? 13.30300  28.88400  -41.40300 1.000 29.70000  ? 98  SER   B HB2    1 
ATOM   5933 H HB3    . SER   B 1 132 ? 14.10900  27.69300  -42.07600 1.000 29.70000  ? 98  SER   B HB3    1 
ATOM   5934 H HG     . SER   B 1 132 ? 12.88700  27.15300  -40.21800 1.000 32.43000  ? 98  SER   B HG     1 
ATOM   5935 N N      . ILE   B 1 133 ? 16.91400  27.96500  -39.52300 1.000 31.08000  ? 99  ILE   B N      1 
ATOM   5936 C CA     . ILE   B 1 133 ? 17.94200  26.99800  -39.15400 1.000 32.89000  ? 99  ILE   B CA     1 
ATOM   5937 C C      . ILE   B 1 133 ? 17.40000  26.09300  -38.05700 1.000 36.74000  ? 99  ILE   B C      1 
ATOM   5938 O O      . ILE   B 1 133 ? 16.62600  26.51200  -37.18700 1.000 34.07000  ? 99  ILE   B O      1 
ATOM   5939 C CB     . ILE   B 1 133 ? 19.26000  27.66100  -38.68700 1.000 32.36000  ? 99  ILE   B CB     1 
ATOM   5940 C CG1    . ILE   B 1 133 ? 19.08300  28.26800  -37.30200 1.000 40.12000  ? 99  ILE   B CG1    1 
ATOM   5941 C CG2    . ILE   B 1 133 ? 19.77500  28.69700  -39.71400 1.000 31.80000  ? 99  ILE   B CG2    1 
ATOM   5942 C CD1    . ILE   B 1 133 ? 20.35400  28.90000  -36.78600 1.000 42.93000  ? 99  ILE   B CD1    1 
ATOM   5943 H H      . ILE   B 1 133 ? 16.65000  28.47200  -38.88000 1.000 31.08000  ? 99  ILE   B H      1 
ATOM   5944 H HA     . ILE   B 1 133 ? 18.14900  26.44000  -39.91900 1.000 32.89000  ? 99  ILE   B HA     1 
ATOM   5945 H HB     . ILE   B 1 133 ? 19.92900  26.96300  -38.61600 1.000 32.36000  ? 99  ILE   B HB     1 
ATOM   5946 H HG12   . ILE   B 1 133 ? 18.39500  28.95100  -37.33700 1.000 40.12000  ? 99  ILE   B HG12   1 
ATOM   5947 H HG13   . ILE   B 1 133 ? 18.83800  27.58100  -36.66500 1.000 40.12000  ? 99  ILE   B HG13   1 
ATOM   5948 H HG21   . ILE   B 1 133 ? 20.68500  28.94400  -39.48800 1.000 31.80000  ? 99  ILE   B HG21   1 
ATOM   5949 H HG22   . ILE   B 1 133 ? 19.75100  28.30000  -40.59900 1.000 31.80000  ? 99  ILE   B HG22   1 
ATOM   5950 H HG23   . ILE   B 1 133 ? 19.20200  29.47900  -39.68800 1.000 31.80000  ? 99  ILE   B HG23   1 
ATOM   5951 H HD11   . ILE   B 1 133 ? 20.23800  29.12000  -35.84800 1.000 42.93000  ? 99  ILE   B HD11   1 
ATOM   5952 H HD12   . ILE   B 1 133 ? 21.08400  28.27000  -36.89000 1.000 42.93000  ? 99  ILE   B HD12   1 
ATOM   5953 H HD13   . ILE   B 1 133 ? 20.53700  29.70600  -37.29400 1.000 42.93000  ? 99  ILE   B HD13   1 
ATOM   5954 N N      . SER   B 1 134 ? 17.82700  24.83700  -38.08800 1.000 32.27000  ? 100 SER   B N      1 
ATOM   5955 C CA     . SER   B 1 134 ? 17.31600  23.88300  -37.12500 1.000 32.24000  ? 100 SER   B CA     1 
ATOM   5956 C C      . SER   B 1 134 ? 18.36800  22.81600  -36.84400 1.000 36.14000  ? 100 SER   B C      1 
ATOM   5957 O O      . SER   B 1 134 ? 18.17500  21.62400  -37.07500 1.000 39.81000  ? 100 SER   B O      1 
ATOM   5958 C CB     . SER   B 1 134 ? 15.99800  23.27000  -37.63200 1.000 33.88000  ? 100 SER   B CB     1 
ATOM   5959 O OG     . SER   B 1 134 ? 15.39700  22.48100  -36.61900 1.000 44.02000  ? 100 SER   B OG     1 
ATOM   5960 H H      . SER   B 1 134 ? 18.40000  24.52000  -38.64500 1.000 32.27000  ? 100 SER   B H      1 
ATOM   5961 H HA     . SER   B 1 134 ? 17.13000  24.34200  -36.29100 1.000 32.24000  ? 100 SER   B HA     1 
ATOM   5962 H HB2    . SER   B 1 134 ? 15.39300  23.98200  -37.88800 1.000 33.88000  ? 100 SER   B HB2    1 
ATOM   5963 H HB3    . SER   B 1 134 ? 16.18800  22.70600  -38.39800 1.000 33.88000  ? 100 SER   B HB3    1 
ATOM   5964 H HG     . SER   B 1 134 ? 14.67900  22.14900  -36.90100 1.000 44.02000  ? 100 SER   B HG     1 
ATOM   5965 N N      . GLY   B 1 135 ? 19.51700  23.25200  -36.32000 1.000 36.36000  ? 101 GLY   B N      1 
ATOM   5966 C CA     . GLY   B 1 135 ? 20.52600  22.30700  -35.87300 1.000 44.64000  ? 101 GLY   B CA     1 
ATOM   5967 C C      . GLY   B 1 135 ? 20.03800  21.44200  -34.72200 1.000 45.66000  ? 101 GLY   B C      1 
ATOM   5968 O O      . GLY   B 1 135 ? 19.05800  21.73900  -34.04100 1.000 40.02000  ? 101 GLY   B O      1 
ATOM   5969 H H      . GLY   B 1 135 ? 19.72900  24.07900  -36.21600 1.000 36.36000  ? 101 GLY   B H      1 
ATOM   5970 H HA2    . GLY   B 1 135 ? 20.77500  21.72700  -36.61000 1.000 44.64000  ? 101 GLY   B HA2    1 
ATOM   5971 H HA3    . GLY   B 1 135 ? 21.31500  22.79000  -35.58200 1.000 44.64000  ? 101 GLY   B HA3    1 
ATOM   5972 N N      . PHE   B 1 136 ? 20.74800  20.34000  -34.49900 1.000 42.10000  ? 102 PHE   B N      1 
ATOM   5973 C CA     . PHE   B 1 136 ? 20.34800  19.34900  -33.50600 1.000 41.24000  ? 102 PHE   B CA     1 
ATOM   5974 C C      . PHE   B 1 136 ? 20.87800  19.64000  -32.10600 1.000 46.61000  ? 102 PHE   B C      1 
ATOM   5975 O O      . PHE   B 1 136 ? 20.58600  18.88200  -31.17900 1.000 47.44000  ? 102 PHE   B O      1 
ATOM   5976 C CB     . PHE   B 1 136 ? 20.78100  17.95600  -33.97700 1.000 45.65000  ? 102 PHE   B CB     1 
ATOM   5977 C CG     . PHE   B 1 136 ? 19.95600  17.45000  -35.12900 1.000 53.83000  ? 102 PHE   B CG     1 
ATOM   5978 C CD1    . PHE   B 1 136 ? 18.64100  17.87300  -35.27200 1.000 70.11000  ? 102 PHE   B CD1    1 
ATOM   5979 C CD2    . PHE   B 1 136 ? 20.48200  16.59700  -36.08200 1.000 71.03000  ? 102 PHE   B CD2    1 
ATOM   5980 C CE1    . PHE   B 1 136 ? 17.85400  17.44100  -36.32800 1.000 63.76000  ? 102 PHE   B CE1    1 
ATOM   5981 C CE2    . PHE   B 1 136 ? 19.69400  16.15500  -37.14500 1.000 70.94000  ? 102 PHE   B CE2    1 
ATOM   5982 C CZ     . PHE   B 1 136 ? 18.37700  16.58000  -37.26200 1.000 61.06000  ? 102 PHE   B CZ     1 
ATOM   5983 H H      . PHE   B 1 136 ? 21.47400  20.14100  -34.91500 1.000 42.10000  ? 102 PHE   B H      1 
ATOM   5984 H HA     . PHE   B 1 136 ? 19.38600  19.37600  -33.41400 1.000 41.24000  ? 102 PHE   B HA     1 
ATOM   5985 H HB2    . PHE   B 1 136 ? 21.70700  17.99300  -34.26400 1.000 45.65000  ? 102 PHE   B HB2    1 
ATOM   5986 H HB3    . PHE   B 1 136 ? 20.68600  17.33000  -33.24200 1.000 45.65000  ? 102 PHE   B HB3    1 
ATOM   5987 H HD1    . PHE   B 1 136 ? 18.26800  18.45000  -34.64800 1.000 70.11000  ? 102 PHE   B HD1    1 
ATOM   5988 H HD2    . PHE   B 1 136 ? 21.36200  16.30600  -36.00600 1.000 71.03000  ? 102 PHE   B HD2    1 
ATOM   5989 H HE1    . PHE   B 1 136 ? 16.97200  17.72800  -36.40100 1.000 63.76000  ? 102 PHE   B HE1    1 
ATOM   5990 H HE2    . PHE   B 1 136 ? 20.05200  15.57500  -37.77800 1.000 70.94000  ? 102 PHE   B HE2    1 
ATOM   5991 H HZ     . PHE   B 1 136 ? 17.85300  16.28800  -37.97300 1.000 61.06000  ? 102 PHE   B HZ     1 
ATOM   5992 N N      . SER   B 1 137 ? 21.61600  20.72700  -31.92300 1.000 43.56000  ? 103 SER   B N      1 
ATOM   5993 C CA     . SER   B 1 137 ? 22.08400  21.12300  -30.60800 1.000 45.52000  ? 103 SER   B CA     1 
ATOM   5994 C C      . SER   B 1 137 ? 22.26300  22.63200  -30.61300 1.000 44.12000  ? 103 SER   B C      1 
ATOM   5995 O O      . SER   B 1 137 ? 22.28600  23.26400  -31.67200 1.000 45.63000  ? 103 SER   B O      1 
ATOM   5996 C CB     . SER   B 1 137 ? 23.40000  20.43200  -30.25000 1.000 39.86000  ? 103 SER   B CB     1 
ATOM   5997 O OG     . SER   B 1 137 ? 24.44500  20.98700  -31.01300 1.000 44.48000  ? 103 SER   B OG     1 
ATOM   5998 H H      . SER   B 1 137 ? 21.86200  21.25800  -32.55400 1.000 43.56000  ? 103 SER   B H      1 
ATOM   5999 H HA     . SER   B 1 137 ? 21.41700  20.88900  -29.94500 1.000 45.52000  ? 103 SER   B HA     1 
ATOM   6000 H HB2    . SER   B 1 137 ? 23.58600  20.56600  -29.30700 1.000 39.86000  ? 103 SER   B HB2    1 
ATOM   6001 H HB3    . SER   B 1 137 ? 23.32800  19.48500  -30.44700 1.000 39.86000  ? 103 SER   B HB3    1 
ATOM   6002 H HG     . SER   B 1 137 ? 25.17200  20.61200  -30.82100 1.000 44.48000  ? 103 SER   B HG     1 
ATOM   6003 N N      . ALA   B 1 138 ? 22.38400  23.20800  -29.41400 1.000 40.48000  ? 104 ALA   B N      1 
ATOM   6004 C CA     . ALA   B 1 138 ? 22.63800  24.64000  -29.31500 1.000 42.84000  ? 104 ALA   B CA     1 
ATOM   6005 C C      . ALA   B 1 138 ? 23.93500  25.00300  -30.02200 1.000 44.75000  ? 104 ALA   B C      1 
ATOM   6006 O O      . ALA   B 1 138 ? 24.00600  26.01900  -30.71900 1.000 44.19000  ? 104 ALA   B O      1 
ATOM   6007 C CB     . ALA   B 1 138 ? 22.67500  25.07300  -27.84300 1.000 43.73000  ? 104 ALA   B CB     1 
ATOM   6008 H H      . ALA   B 1 138 ? 22.35400  22.83700  -28.67800 1.000 40.48000  ? 104 ALA   B H      1 
ATOM   6009 H HA     . ALA   B 1 138 ? 21.91600  25.11900  -29.75000 1.000 42.84000  ? 104 ALA   B HA     1 
ATOM   6010 H HB1    . ALA   B 1 138 ? 22.84500  26.02700  -27.79900 1.000 43.73000  ? 104 ALA   B HB1    1 
ATOM   6011 H HB2    . ALA   B 1 138 ? 21.82000  24.87000  -27.43300 1.000 43.73000  ? 104 ALA   B HB2    1 
ATOM   6012 H HB3    . ALA   B 1 138 ? 23.38300  24.58900  -27.39000 1.000 43.73000  ? 104 ALA   B HB3    1 
ATOM   6013 N N      . GLU   B 1 139 ? 24.96600  24.16200  -29.87500 1.000 43.10000  ? 105 GLU   B N      1 
ATOM   6014 C CA     . GLU   B 1 139 ? 26.25700  24.42500  -30.51100 1.000 45.38000  ? 105 GLU   B CA     1 
ATOM   6015 C C      . GLU   B 1 139 ? 26.16800  24.36700  -32.03700 1.000 37.94000  ? 105 GLU   B C      1 
ATOM   6016 O O      . GLU   B 1 139 ? 26.78300  25.18800  -32.72800 1.000 44.23000  ? 105 GLU   B O      1 
ATOM   6017 C CB     . GLU   B 1 139 ? 27.30200  23.42800  -29.98800 1.000 49.68000  ? 105 GLU   B CB     1 
ATOM   6018 C CG     . GLU   B 1 139 ? 28.54800  23.27000  -30.86200 1.000 58.25000  ? 105 GLU   B CG     1 
ATOM   6019 C CD     . GLU   B 1 139 ? 29.46600  24.48200  -30.84300 1.000 60.62000  ? 105 GLU   B CD     1 
ATOM   6020 H H      . GLU   B 1 139 ? 24.94100  23.43700  -29.41400 1.000 43.10000  ? 105 GLU   B H      1 
ATOM   6021 H HA     . GLU   B 1 139 ? 26.55000  25.31700  -30.26600 1.000 45.38000  ? 105 GLU   B HA     1 
ATOM   6022 H HB2    . GLU   B 1 139 ? 27.59600  23.72100  -29.11100 1.000 49.68000  ? 105 GLU   B HB2    1 
ATOM   6023 H HB3    . GLU   B 1 139 ? 26.88500  22.55500  -29.91600 1.000 49.68000  ? 105 GLU   B HB3    1 
ATOM   6024 H HG2    . GLU   B 1 139 ? 29.06000  22.52100  -30.51900 1.000 58.25000  ? 105 GLU   B HG2    1 
ATOM   6025 H HG3    . GLU   B 1 139 ? 28.30000  23.08900  -31.78100 1.000 58.25000  ? 105 GLU   B HG3    1 
ATOM   6026 N N      . GLU   B 1 140 ? 25.42800  23.40500  -32.59500 1.000 40.50000  ? 106 GLU   B N      1 
ATOM   6027 C CA     . GLU   B 1 140 ? 25.28100  23.37800  -34.05400 1.000 45.07000  ? 106 GLU   B CA     1 
ATOM   6028 C C      . GLU   B 1 140 ? 24.64200  24.66800  -34.56000 1.000 40.79000  ? 106 GLU   B C      1 
ATOM   6029 O O      . GLU   B 1 140 ? 25.09200  25.25100  -35.55200 1.000 36.80000  ? 106 GLU   B O      1 
ATOM   6030 C CB     . GLU   B 1 140 ? 24.45400  22.17600  -34.49700 1.000 38.90000  ? 106 GLU   B CB     1 
ATOM   6031 C CG     . GLU   B 1 140 ? 25.19700  20.86500  -34.45700 1.000 44.14000  ? 106 GLU   B CG     1 
ATOM   6032 C CD     . GLU   B 1 140 ? 24.43200  19.74000  -35.12900 1.000 55.72000  ? 106 GLU   B CD     1 
ATOM   6033 O OE1    . GLU   B 1 140 ? 23.36700  19.99700  -35.74100 1.000 45.68000  ? 106 GLU   B OE1    1 
ATOM   6034 O OE2    . GLU   B 1 140 ? 24.89600  18.58900  -35.03900 1.000 64.22000  ? 106 GLU   B OE2    1 
ATOM   6035 H H      . GLU   B 1 140 ? 25.01600  22.78000  -32.17200 1.000 40.50000  ? 106 GLU   B H      1 
ATOM   6036 H HA     . GLU   B 1 140 ? 26.16000  23.30100  -34.45800 1.000 45.07000  ? 106 GLU   B HA     1 
ATOM   6037 H HB2    . GLU   B 1 140 ? 23.68300  22.09600  -33.91300 1.000 38.90000  ? 106 GLU   B HB2    1 
ATOM   6038 H HB3    . GLU   B 1 140 ? 24.16000  22.32100  -35.41000 1.000 38.90000  ? 106 GLU   B HB3    1 
ATOM   6039 H HG2    . GLU   B 1 140 ? 26.04500  20.96800  -34.91600 1.000 44.14000  ? 106 GLU   B HG2    1 
ATOM   6040 H HG3    . GLU   B 1 140 ? 25.34800  20.61500  -33.53200 1.000 44.14000  ? 106 GLU   B HG3    1 
ATOM   6041 N N      . ASN   B 1 141 ? 23.57900  25.11800  -33.88500 1.000 39.28000  ? 107 ASN   B N      1 
ATOM   6042 C CA     . ASN   B 1 141 ? 22.91900  26.36400  -34.25800 1.000 39.57000  ? 107 ASN   B CA     1 
ATOM   6043 C C      . ASN   B 1 141 ? 23.85900  27.55400  -34.14400 1.000 39.46000  ? 107 ASN   B C      1 
ATOM   6044 O O      . ASN   B 1 141 ? 23.90300  28.41000  -35.03700 1.000 39.56000  ? 107 ASN   B O      1 
ATOM   6045 C CB     . ASN   B 1 141 ? 21.67500  26.56500  -33.39100 1.000 35.75000  ? 107 ASN   B CB     1 
ATOM   6046 C CG     . ASN   B 1 141 ? 20.53200  25.71800  -33.84100 1.000 40.88000  ? 107 ASN   B CG     1 
ATOM   6047 O OD1    . ASN   B 1 141 ? 20.25300  25.64300  -35.03200 1.000 43.46000  ? 107 ASN   B OD1    1 
ATOM   6048 N ND2    . ASN   B 1 141 ? 19.87000  25.05600  -32.90800 1.000 44.16000  ? 107 ASN   B ND2    1 
ATOM   6049 H H      . ASN   B 1 141 ? 23.22500  24.71900  -33.21000 1.000 39.28000  ? 107 ASN   B H      1 
ATOM   6050 H HA     . ASN   B 1 141 ? 22.63100  26.30100  -35.18200 1.000 39.57000  ? 107 ASN   B HA     1 
ATOM   6051 H HB2    . ASN   B 1 141 ? 21.87600  26.36200  -32.46400 1.000 35.75000  ? 107 ASN   B HB2    1 
ATOM   6052 H HB3    . ASN   B 1 141 ? 21.38500  27.48000  -33.49200 1.000 35.75000  ? 107 ASN   B HB3    1 
ATOM   6053 H HD21   . ASN   B 1 141 ? 19.20600  24.55500  -33.12600 1.000 44.16000  ? 107 ASN   B HD21   1 
ATOM   6054 H HD22   . ASN   B 1 141 ? 20.09900  25.13200  -32.08200 1.000 44.16000  ? 107 ASN   B HD22   1 
ATOM   6055 N N      . ALA   B 1 142 ? 24.62900  27.62600  -33.05800 1.000 40.87000  ? 108 ALA   B N      1 
ATOM   6056 C CA     . ALA   B 1 142 ? 25.49900  28.78200  -32.87400 1.000 35.39000  ? 108 ALA   B CA     1 
ATOM   6057 C C      . ALA   B 1 142 ? 26.59700  28.83400  -33.92600 1.000 36.17000  ? 108 ALA   B C      1 
ATOM   6058 O O      . ALA   B 1 142 ? 26.97100  29.91900  -34.37700 1.000 36.70000  ? 108 ALA   B O      1 
ATOM   6059 C CB     . ALA   B 1 142 ? 26.09800  28.76600  -31.46300 1.000 44.86000  ? 108 ALA   B CB     1 
ATOM   6060 H H      . ALA   B 1 142 ? 24.66500  27.03700  -32.43200 1.000 40.87000  ? 108 ALA   B H      1 
ATOM   6061 H HA     . ALA   B 1 142 ? 24.96800  29.58900  -32.96100 1.000 35.39000  ? 108 ALA   B HA     1 
ATOM   6062 H HB1    . ALA   B 1 142 ? 26.67400  29.53900  -31.35600 1.000 44.86000  ? 108 ALA   B HB1    1 
ATOM   6063 H HB2    . ALA   B 1 142 ? 25.37800  28.79800  -30.81400 1.000 44.86000  ? 108 ALA   B HB2    1 
ATOM   6064 H HB3    . ALA   B 1 142 ? 26.61200  27.95100  -31.34800 1.000 44.86000  ? 108 ALA   B HB3    1 
ATOM   6065 N N      . GLU   B 1 143 ? 27.10500  27.68000  -34.35000 0.880 35.52000  ? 109 GLU   B N      1 
ATOM   6066 C CA     . GLU   B 1 143 ? 28.13300  27.67900  -35.38000 0.880 35.42000  ? 109 GLU   B CA     1 
ATOM   6067 C C      . GLU   B 1 143 ? 27.57200  28.16200  -36.71800 0.880 37.12000  ? 109 GLU   B C      1 
ATOM   6068 O O      . GLU   B 1 143 ? 28.21900  28.94700  -37.41800 0.880 38.79000  ? 109 GLU   B O      1 
ATOM   6069 C CB     . GLU   B 1 143 ? 28.74700  26.28100  -35.47800 0.880 42.81000  ? 109 GLU   B CB     1 
ATOM   6070 C CG     . GLU   B 1 143 ? 30.07100  26.24400  -36.20600 0.880 55.87000  ? 109 GLU   B CG     1 
ATOM   6071 C CD     . GLU   B 1 143 ? 29.90200  26.20800  -37.71400 0.880 69.26000  ? 109 GLU   B CD     1 
ATOM   6072 O OE1    . GLU   B 1 143 ? 28.84100  25.71900  -38.18700 0.880 67.68000  ? 109 GLU   B OE1    1 
ATOM   6073 O OE2    . GLU   B 1 143 ? 30.82700  26.65600  -38.42600 0.880 67.95000  ? 109 GLU   B OE2    1 
ATOM   6074 H H      . GLU   B 1 143 ? 26.87700  26.90200  -34.06400 0.880 35.52000  ? 109 GLU   B H      1 
ATOM   6075 H HA     . GLU   B 1 143 ? 28.83700  28.29300  -35.11700 0.880 35.42000  ? 109 GLU   B HA     1 
ATOM   6076 H HB2    . GLU   B 1 143 ? 28.89700  25.94600  -34.58000 0.880 42.81000  ? 109 GLU   B HB2    1 
ATOM   6077 H HB3    . GLU   B 1 143 ? 28.12800  25.69800  -35.94400 0.880 42.81000  ? 109 GLU   B HB3    1 
ATOM   6078 H HG2    . GLU   B 1 143 ? 30.58100  27.03700  -35.97900 0.880 55.87000  ? 109 GLU   B HG2    1 
ATOM   6079 H HG3    . GLU   B 1 143 ? 30.55700  25.44800  -35.93900 0.880 55.87000  ? 109 GLU   B HG3    1 
ATOM   6080 N N      . MET   B 1 144 ? 26.34800  27.74400  -37.06900 1.000 41.42000  ? 110 MET   B N      1 
ATOM   6081 C CA     . MET   B 1 144 ? 25.71400  28.25600  -38.28600 1.000 38.22000  ? 110 MET   B CA     1 
ATOM   6082 C C      . MET   B 1 144 ? 25.48200  29.76200  -38.20500 1.000 38.84000  ? 110 MET   B C      1 
ATOM   6083 O O      . MET   B 1 144 ? 25.67000  30.48000  -39.19200 1.000 34.80000  ? 110 MET   B O      1 
ATOM   6084 C CB     . MET   B 1 144 ? 24.38900  27.52000  -38.54600 1.000 34.71000  ? 110 MET   B CB     1 
ATOM   6085 C CG     . MET   B 1 144 ? 24.55800  26.05700  -39.04600 1.000 35.47000  ? 110 MET   B CG     1 
ATOM   6086 S SD     . MET   B 1 144 ? 22.99200  25.21200  -39.48300 1.000 40.31000  ? 110 MET   B SD     1 
ATOM   6087 C CE     . MET   B 1 144 ? 22.28100  24.88400  -37.87400 1.000 34.39000  ? 110 MET   B CE     1 
ATOM   6088 H H      . MET   B 1 144 ? 25.87500  27.17700  -36.62800 1.000 41.42000  ? 110 MET   B H      1 
ATOM   6089 H HA     . MET   B 1 144 ? 26.30000  28.07500  -39.03700 1.000 38.22000  ? 110 MET   B HA     1 
ATOM   6090 H HB2    . MET   B 1 144 ? 23.88100  27.49300  -37.72000 1.000 34.71000  ? 110 MET   B HB2    1 
ATOM   6091 H HB3    . MET   B 1 144 ? 23.89000  28.00700  -39.22100 1.000 34.71000  ? 110 MET   B HB3    1 
ATOM   6092 H HG2    . MET   B 1 144 ? 25.11900  26.06300  -39.83700 1.000 35.47000  ? 110 MET   B HG2    1 
ATOM   6093 H HG3    . MET   B 1 144 ? 24.98600  25.53800  -38.34700 1.000 35.47000  ? 110 MET   B HG3    1 
ATOM   6094 H HE1    . MET   B 1 144 ? 21.43600  24.42100  -37.99100 1.000 34.39000  ? 110 MET   B HE1    1 
ATOM   6095 H HE2    . MET   B 1 144 ? 22.89400  24.33100  -37.36500 1.000 34.39000  ? 110 MET   B HE2    1 
ATOM   6096 H HE3    . MET   B 1 144 ? 22.13700  25.72700  -37.41600 1.000 34.39000  ? 110 MET   B HE3    1 
ATOM   6097 N N      . CYS   B 1 145 ? 25.05700  30.26000  -37.04000 1.000 39.61000  ? 111 CYS   B N      1 
ATOM   6098 C CA     . CYS   B 1 145 ? 24.84000  31.70000  -36.90000 1.000 39.09000  ? 111 CYS   B CA     1 
ATOM   6099 C C      . CYS   B 1 145 ? 26.12400  32.48400  -37.08300 1.000 41.36000  ? 111 CYS   B C      1 
ATOM   6100 O O      . CYS   B 1 145 ? 26.09200  33.59500  -37.61000 1.000 35.55000  ? 111 CYS   B O      1 
ATOM   6101 C CB     . CYS   B 1 145 ? 24.23600  32.01800  -35.53100 1.000 37.89000  ? 111 CYS   B CB     1 
ATOM   6102 S SG     . CYS   B 1 145 ? 22.56000  31.39400  -35.33500 1.000 45.71000  ? 111 CYS   B SG     1 
ATOM   6103 H H      . CYS   B 1 145 ? 24.89100  29.79800  -36.33400 1.000 39.61000  ? 111 CYS   B H      1 
ATOM   6104 H HA     . CYS   B 1 145 ? 24.21200  31.99100  -37.57900 1.000 39.09000  ? 111 CYS   B HA     1 
ATOM   6105 H HB2    . CYS   B 1 145 ? 24.78800  31.61500  -34.84200 1.000 37.89000  ? 111 CYS   B HB2    1 
ATOM   6106 H HB3    . CYS   B 1 145 ? 24.21300  32.98000  -35.41700 1.000 37.89000  ? 111 CYS   B HB3    1 
ATOM   6107 H HG     . CYS   B 1 145 ? 22.52500  30.22200  -35.58200 1.000 45.71000  ? 111 CYS   B HG     1 
ATOM   6108 N N      . LYS   B 1 146 ? 27.26200  31.93800  -36.64800 1.000 41.21000  ? 112 LYS   B N      1 
ATOM   6109 C CA     . LYS   B 1 146 ? 28.51800  32.65800  -36.83000 1.000 39.70000  ? 112 LYS   B CA     1 
ATOM   6110 C C      . LYS   B 1 146 ? 28.82100  32.86600  -38.30700 1.000 39.60000  ? 112 LYS   B C      1 
ATOM   6111 O O      . LYS   B 1 146 ? 29.31600  33.92700  -38.70100 1.000 39.32000  ? 112 LYS   B O      1 
ATOM   6112 C CB     . LYS   B 1 146 ? 29.66200  31.91600  -36.13000 1.000 44.33000  ? 112 LYS   B CB     1 
ATOM   6113 C CG     . LYS   B 1 146 ? 29.56300  31.97400  -34.61200 1.000 56.16000  ? 112 LYS   B CG     1 
ATOM   6114 C CD     . LYS   B 1 146 ? 30.72000  31.26900  -33.91900 1.000 51.02000  ? 112 LYS   B CD     1 
ATOM   6115 H H      . LYS   B 1 146 ? 27.33100  31.17500  -36.25600 1.000 41.21000  ? 112 LYS   B H      1 
ATOM   6116 H HA     . LYS   B 1 146 ? 28.43800  33.53300  -36.41900 1.000 39.70000  ? 112 LYS   B HA     1 
ATOM   6117 H HB2    . LYS   B 1 146 ? 29.64300  30.98300  -36.39600 1.000 44.33000  ? 112 LYS   B HB2    1 
ATOM   6118 H HB3    . LYS   B 1 146 ? 30.50500  32.31800  -36.39100 1.000 44.33000  ? 112 LYS   B HB3    1 
ATOM   6119 H HG2    . LYS   B 1 146 ? 29.56700  32.90200  -34.33100 1.000 56.16000  ? 112 LYS   B HG2    1 
ATOM   6120 H HG3    . LYS   B 1 146 ? 28.73900  31.54700  -34.33100 1.000 56.16000  ? 112 LYS   B HG3    1 
ATOM   6121 N N      . ARG   B 1 147 ? 28.49800  31.88300  -39.15100 1.000 38.01000  ? 113 ARG   B N      1 
ATOM   6122 C CA     . ARG   B 1 147 ? 28.73900  32.05600  -40.58100 1.000 33.63000  ? 113 ARG   B CA     1 
ATOM   6123 C C      . ARG   B 1 147 ? 27.65700  32.88900  -41.25100 1.000 39.32000  ? 113 ARG   B C      1 
ATOM   6124 O O      . ARG   B 1 147 ? 27.92300  33.56800  -42.25200 1.000 39.42000  ? 113 ARG   B O      1 
ATOM   6125 C CB     . ARG   B 1 147 ? 28.85000  30.69000  -41.25500 1.000 40.77000  ? 113 ARG   B CB     1 
ATOM   6126 C CG     . ARG   B 1 147 ? 29.85100  29.80000  -40.56500 1.000 49.03000  ? 113 ARG   B CG     1 
ATOM   6127 C CD     . ARG   B 1 147 ? 30.59800  28.94700  -41.55900 1.000 64.58000  ? 113 ARG   B CD     1 
ATOM   6128 N NE     . ARG   B 1 147 ? 29.86700  27.73300  -41.89400 1.000 65.41000  ? 113 ARG   B NE     1 
ATOM   6129 C CZ     . ARG   B 1 147 ? 29.61100  27.32500  -43.13100 1.000 51.39000  ? 113 ARG   B CZ     1 
ATOM   6130 N NH1    . ARG   B 1 147 ? 29.99900  28.02600  -44.18500 1.000 63.72000  ? 113 ARG   B NH1    1 
ATOM   6131 N NH2    . ARG   B 1 147 ? 28.95000  26.18600  -43.31300 1.000 58.08000  ? 113 ARG   B NH2    1 
ATOM   6132 H H      . ARG   B 1 147 ? 28.14900  31.12900  -38.92800 1.000 38.01000  ? 113 ARG   B H      1 
ATOM   6133 H HA     . ARG   B 1 147 ? 29.58500  32.51500  -40.70300 1.000 33.63000  ? 113 ARG   B HA     1 
ATOM   6134 H HB2    . ARG   B 1 147 ? 27.98600  30.25100  -41.22400 1.000 40.77000  ? 113 ARG   B HB2    1 
ATOM   6135 H HB3    . ARG   B 1 147 ? 29.12600  30.81600  -42.17600 1.000 40.77000  ? 113 ARG   B HB3    1 
ATOM   6136 H HG2    . ARG   B 1 147 ? 30.49500  30.34800  -40.09000 1.000 49.03000  ? 113 ARG   B HG2    1 
ATOM   6137 H HG3    . ARG   B 1 147 ? 29.38700  29.21300  -39.94700 1.000 49.03000  ? 113 ARG   B HG3    1 
ATOM   6138 H HD2    . ARG   B 1 147 ? 30.76500  29.46400  -42.35900 1.000 64.58000  ? 113 ARG   B HD2    1 
ATOM   6139 H HD3    . ARG   B 1 147 ? 31.44200  28.68000  -41.16300 1.000 64.58000  ? 113 ARG   B HD3    1 
ATOM   6140 H HE     . ARG   B 1 147 ? 29.58100  27.24600  -41.24500 1.000 65.41000  ? 113 ARG   B HE     1 
ATOM   6141 H HH11   . ARG   B 1 147 ? 30.42700  28.76300  -44.09100 1.000 63.72000  ? 113 ARG   B HH11   1 
ATOM   6142 H HH12   . ARG   B 1 147 ? 29.82000  27.73800  -44.97500 1.000 63.72000  ? 113 ARG   B HH12   1 
ATOM   6143 H HH21   . ARG   B 1 147 ? 28.69300  25.72300  -42.63500 1.000 58.08000  ? 113 ARG   B HH21   1 
ATOM   6144 H HH22   . ARG   B 1 147 ? 28.78200  25.91500  -44.10700 1.000 58.08000  ? 113 ARG   B HH22   1 
ATOM   6145 N N      . LEU   B 1 148 ? 26.43600  32.84800  -40.72200 1.000 38.54000  ? 114 LEU   B N      1 
ATOM   6146 C CA     . LEU   B 1 148 ? 25.36300  33.64200  -41.31200 1.000 31.88000  ? 114 LEU   B CA     1 
ATOM   6147 C C      . LEU   B 1 148 ? 25.55500  35.12700  -41.04200 1.000 36.35000  ? 114 LEU   B C      1 
ATOM   6148 O O      . LEU   B 1 148 ? 25.19800  35.95900  -41.88300 1.000 34.83000  ? 114 LEU   B O      1 
ATOM   6149 C CB     . LEU   B 1 148 ? 24.01400  33.15600  -40.77100 1.000 33.40000  ? 114 LEU   B CB     1 
ATOM   6150 C CG     . LEU   B 1 148 ? 22.78400  33.98900  -41.14400 1.000 37.43000  ? 114 LEU   B CG     1 
ATOM   6151 C CD1    . LEU   B 1 148 ? 22.51600  33.95800  -42.64100 1.000 36.57000  ? 114 LEU   B CD1    1 
ATOM   6152 C CD2    . LEU   B 1 148 ? 21.55000  33.53900  -40.32600 1.000 34.18000  ? 114 LEU   B CD2    1 
ATOM   6153 H H      . LEU   B 1 148 ? 26.20700  32.38000  -40.03800 1.000 38.54000  ? 114 LEU   B H      1 
ATOM   6154 H HA     . LEU   B 1 148 ? 25.36500  33.51000  -42.27300 1.000 31.88000  ? 114 LEU   B HA     1 
ATOM   6155 H HB2    . LEU   B 1 148 ? 23.86200  32.25600  -41.10100 1.000 33.40000  ? 114 LEU   B HB2    1 
ATOM   6156 H HB3    . LEU   B 1 148 ? 24.06500  33.13800  -39.80300 1.000 33.40000  ? 114 LEU   B HB3    1 
ATOM   6157 H HG     . LEU   B 1 148 ? 22.95300  34.91300  -40.90500 1.000 37.43000  ? 114 LEU   B HG     1 
ATOM   6158 H HD11   . LEU   B 1 148 ? 21.72400  34.48600  -42.83000 1.000 36.57000  ? 114 LEU   B HD11   1 
ATOM   6159 H HD12   . LEU   B 1 148 ? 23.28100  34.33000  -43.10600 1.000 36.57000  ? 114 LEU   B HD12   1 
ATOM   6160 H HD13   . LEU   B 1 148 ? 22.37500  33.03900  -42.91700 1.000 36.57000  ? 114 LEU   B HD13   1 
ATOM   6161 H HD21   . LEU   B 1 148 ? 20.78700  34.08100  -40.58100 1.000 34.18000  ? 114 LEU   B HD21   1 
ATOM   6162 H HD22   . LEU   B 1 148 ? 21.37000  32.60500  -40.51500 1.000 34.18000  ? 114 LEU   B HD22   1 
ATOM   6163 H HD23   . LEU   B 1 148 ? 21.73800  33.65600  -39.38200 1.000 34.18000  ? 114 LEU   B HD23   1 
ATOM   6164 N N      . ALA   B 1 149 ? 26.12700  35.47300  -39.88300 1.000 37.88000  ? 115 ALA   B N      1 
ATOM   6165 C CA     . ALA   B 1 149 ? 26.19600  36.86900  -39.45000 1.000 33.79000  ? 115 ALA   B CA     1 
ATOM   6166 C C      . ALA   B 1 149 ? 26.71400  37.81700  -40.51400 1.000 33.72000  ? 115 ALA   B C      1 
ATOM   6167 O O      . ALA   B 1 149 ? 26.06000  38.84700  -40.76100 1.000 38.77000  ? 115 ALA   B O      1 
ATOM   6168 C CB     . ALA   B 1 149 ? 27.04900  36.97000  -38.17400 1.000 34.19000  ? 115 ALA   B CB     1 
ATOM   6169 H H      . ALA   B 1 149 ? 26.48200  34.91700  -39.33100 1.000 37.88000  ? 115 ALA   B H      1 
ATOM   6170 H HA     . ALA   B 1 149 ? 25.29900  37.15900  -39.22000 1.000 33.79000  ? 115 ALA   B HA     1 
ATOM   6171 H HB1    . ALA   B 1 149 ? 27.11700  37.90200  -37.91400 1.000 34.19000  ? 115 ALA   B HB1    1 
ATOM   6172 H HB2    . ALA   B 1 149 ? 26.62100  36.46000  -37.46800 1.000 34.19000  ? 115 ALA   B HB2    1 
ATOM   6173 H HB3    . ALA   B 1 149 ? 27.93200  36.61100  -38.35200 1.000 34.19000  ? 115 ALA   B HB3    1 
ATOM   6174 N N      . PRO   B 1 150 ? 27.85000  37.56600  -41.17200 1.000 40.48000  ? 116 PRO   B N      1 
ATOM   6175 C CA     . PRO   B 1 150 ? 28.32000  38.53900  -42.17300 1.000 38.39000  ? 116 PRO   B CA     1 
ATOM   6176 C C      . PRO   B 1 150 ? 27.38200  38.65700  -43.36800 1.000 43.64000  ? 116 PRO   B C      1 
ATOM   6177 O O      . PRO   B 1 150 ? 27.26800  39.74600  -43.94900 1.000 40.91000  ? 116 PRO   B O      1 
ATOM   6178 C CB     . PRO   B 1 150 ? 29.70600  38.00800  -42.57000 1.000 42.25000  ? 116 PRO   B CB     1 
ATOM   6179 C CG     . PRO   B 1 150 ? 29.71800  36.57100  -42.14200 1.000 38.34000  ? 116 PRO   B CG     1 
ATOM   6180 C CD     . PRO   B 1 150 ? 28.81700  36.47200  -40.94400 1.000 38.05000  ? 116 PRO   B CD     1 
ATOM   6181 H HA     . PRO   B 1 150 ? 28.42200  39.41300  -41.76400 1.000 38.39000  ? 116 PRO   B HA     1 
ATOM   6182 H HB2    . PRO   B 1 150 ? 29.82000  38.08000  -43.53100 1.000 42.25000  ? 116 PRO   B HB2    1 
ATOM   6183 H HB3    . PRO   B 1 150 ? 30.39300  38.51000  -42.10400 1.000 42.25000  ? 116 PRO   B HB3    1 
ATOM   6184 H HG2    . PRO   B 1 150 ? 29.38300  36.01700  -42.86400 1.000 38.34000  ? 116 PRO   B HG2    1 
ATOM   6185 H HG3    . PRO   B 1 150 ? 30.62300  36.31200  -41.90700 1.000 38.34000  ? 116 PRO   B HG3    1 
ATOM   6186 H HD2    . PRO   B 1 150 ? 28.37000  35.61200  -40.93200 1.000 38.05000  ? 116 PRO   B HD2    1 
ATOM   6187 H HD3    . PRO   B 1 150 ? 29.32000  36.62600  -40.12900 1.000 38.05000  ? 116 PRO   B HD3    1 
ATOM   6188 N N      . VAL   B 1 151 ? 26.69300  37.56900  -43.73700 1.000 37.43000  ? 117 VAL   B N      1 
ATOM   6189 C CA     . VAL   B 1 151 ? 25.73400  37.61500  -44.84200 1.000 34.52000  ? 117 VAL   B CA     1 
ATOM   6190 C C      . VAL   B 1 151 ? 24.47800  38.37900  -44.43800 1.000 35.32000  ? 117 VAL   B C      1 
ATOM   6191 O O      . VAL   B 1 151 ? 23.92300  39.14700  -45.23300 1.000 35.51000  ? 117 VAL   B O      1 
ATOM   6192 C CB     . VAL   B 1 151 ? 25.39800  36.18400  -45.31500 1.000 35.36000  ? 117 VAL   B CB     1 
ATOM   6193 C CG1    . VAL   B 1 151 ? 24.29200  36.22800  -46.37700 1.000 37.59000  ? 117 VAL   B CG1    1 
ATOM   6194 C CG2    . VAL   B 1 151 ? 26.65500  35.49500  -45.86200 1.000 39.19000  ? 117 VAL   B CG2    1 
ATOM   6195 H H      . VAL   B 1 151 ? 26.76400  36.79700  -43.36400 1.000 37.43000  ? 117 VAL   B H      1 
ATOM   6196 H HA     . VAL   B 1 151 ? 26.13900  38.08500  -45.58700 1.000 34.52000  ? 117 VAL   B HA     1 
ATOM   6197 H HB     . VAL   B 1 151 ? 25.07300  35.66700  -44.56100 1.000 35.36000  ? 117 VAL   B HB     1 
ATOM   6198 H HG11   . VAL   B 1 151 ? 24.26700  35.37600  -46.83900 1.000 37.59000  ? 117 VAL   B HG11   1 
ATOM   6199 H HG12   . VAL   B 1 151 ? 23.44000  36.39200  -45.94400 1.000 37.59000  ? 117 VAL   B HG12   1 
ATOM   6200 H HG13   . VAL   B 1 151 ? 24.48800  36.93900  -47.00700 1.000 37.59000  ? 117 VAL   B HG13   1 
ATOM   6201 H HG21   . VAL   B 1 151 ? 26.41700  34.61000  -46.17900 1.000 39.19000  ? 117 VAL   B HG21   1 
ATOM   6202 H HG22   . VAL   B 1 151 ? 27.01100  36.02400  -46.59300 1.000 39.19000  ? 117 VAL   B HG22   1 
ATOM   6203 H HG23   . VAL   B 1 151 ? 27.31200  35.42600  -45.15200 1.000 39.19000  ? 117 VAL   B HG23   1 
ATOM   6204 N N      . ALA   B 1 152 ? 24.00300  38.17700  -43.20400 1.000 38.20000  ? 118 ALA   B N      1 
ATOM   6205 C CA     . ALA   B 1 152 ? 22.90800  39.00000  -42.70700 1.000 34.72000  ? 118 ALA   B CA     1 
ATOM   6206 C C      . ALA   B 1 152 ? 23.28600  40.48300  -42.71500 1.000 38.56000  ? 118 ALA   B C      1 
ATOM   6207 O O      . ALA   B 1 152 ? 22.47900  41.33800  -43.10100 1.000 41.36000  ? 118 ALA   B O      1 
ATOM   6208 C CB     . ALA   B 1 152 ? 22.50900  38.54000  -41.30400 1.000 33.90000  ? 118 ALA   B CB     1 
ATOM   6209 H H      . ALA   B 1 152 ? 24.29200  37.58500  -42.65100 1.000 38.20000  ? 118 ALA   B H      1 
ATOM   6210 H HA     . ALA   B 1 152 ? 22.14000  38.88500  -43.28800 1.000 34.72000  ? 118 ALA   B HA     1 
ATOM   6211 H HB1    . ALA   B 1 152 ? 21.78200  39.09700  -40.98500 1.000 33.90000  ? 118 ALA   B HB1    1 
ATOM   6212 H HB2    . ALA   B 1 152 ? 22.22400  37.61400  -41.34500 1.000 33.90000  ? 118 ALA   B HB2    1 
ATOM   6213 H HB3    . ALA   B 1 152 ? 23.27500  38.62500  -40.71500 1.000 33.90000  ? 118 ALA   B HB3    1 
ATOM   6214 N N      . ALA   B 1 153 ? 24.51400  40.81100  -42.31200 1.000 37.21000  ? 119 ALA   B N      1 
ATOM   6215 C CA     . ALA   B 1 153 ? 24.89700  42.22100  -42.23700 1.000 41.35000  ? 119 ALA   B CA     1 
ATOM   6216 C C      . ALA   B 1 153 ? 24.95900  42.85100  -43.62000 1.000 37.14000  ? 119 ALA   B C      1 
ATOM   6217 O O      . ALA   B 1 153 ? 24.54600  44.00000  -43.80600 1.000 41.23000  ? 119 ALA   B O      1 
ATOM   6218 C CB     . ALA   B 1 153 ? 26.24200  42.37000  -41.52300 1.000 41.39000  ? 119 ALA   B CB     1 
ATOM   6219 H H      . ALA   B 1 153 ? 25.12800  40.25400  -42.08300 1.000 37.21000  ? 119 ALA   B H      1 
ATOM   6220 H HA     . ALA   B 1 153 ? 24.23000  42.70000  -41.72100 1.000 41.35000  ? 119 ALA   B HA     1 
ATOM   6221 H HB1    . ALA   B 1 153 ? 26.47600  43.31100  -41.48500 1.000 41.39000  ? 119 ALA   B HB1    1 
ATOM   6222 H HB2    . ALA   B 1 153 ? 26.16400  42.01100  -40.62500 1.000 41.39000  ? 119 ALA   B HB2    1 
ATOM   6223 H HB3    . ALA   B 1 153 ? 26.91800  41.88000  -42.01800 1.000 41.39000  ? 119 ALA   B HB3    1 
ATOM   6224 N N      . GLU   B 1 154 ? 25.44300  42.09800  -44.60600 1.000 39.93000  ? 120 GLU   B N      1 
ATOM   6225 C CA     . GLU   B 1 154 ? 25.70000  42.63100  -45.93700 1.000 40.98000  ? 120 GLU   B CA     1 
ATOM   6226 C C      . GLU   B 1 154 ? 24.45100  42.62200  -46.81800 1.000 39.74000  ? 120 GLU   B C      1 
ATOM   6227 O O      . GLU   B 1 154 ? 24.21600  43.57100  -47.57500 1.000 39.19000  ? 120 GLU   B O      1 
ATOM   6228 C CB     . GLU   B 1 154 ? 26.81200  41.81500  -46.60300 1.000 42.02000  ? 120 GLU   B CB     1 
ATOM   6229 C CG     . GLU   B 1 154 ? 27.02900  42.21000  -48.04300 1.000 61.00000  ? 120 GLU   B CG     1 
ATOM   6230 C CD     . GLU   B 1 154 ? 28.23300  41.53600  -48.65400 1.000 79.53000  ? 120 GLU   B CD     1 
ATOM   6231 O OE1    . GLU   B 1 154 ? 29.10300  41.05200  -47.89100 1.000 80.59000  ? 120 GLU   B OE1    1 
ATOM   6232 O OE2    . GLU   B 1 154 ? 28.30500  41.49200  -49.90100 1.000 87.47000  ? 120 GLU   B OE2    1 
ATOM   6233 H H      . GLU   B 1 154 ? 25.63300  41.26300  -44.52500 1.000 39.93000  ? 120 GLU   B H      1 
ATOM   6234 H HA     . GLU   B 1 154 ? 26.00600  43.54800  -45.85800 1.000 40.98000  ? 120 GLU   B HA     1 
ATOM   6235 H HB2    . GLU   B 1 154 ? 27.64200  41.95900  -46.12200 1.000 42.02000  ? 120 GLU   B HB2    1 
ATOM   6236 H HB3    . GLU   B 1 154 ? 26.57300  40.87500  -46.58100 1.000 42.02000  ? 120 GLU   B HB3    1 
ATOM   6237 H HG2    . GLU   B 1 154 ? 26.25600  41.95300  -48.56900 1.000 61.00000  ? 120 GLU   B HG2    1 
ATOM   6238 H HG3    . GLU   B 1 154 ? 27.16300  43.16900  -48.09300 1.000 61.00000  ? 120 GLU   B HG3    1 
ATOM   6239 N N      . LYS   B 1 155 ? 23.66000  41.54400  -46.75900 1.000 36.89000  ? 121 LYS   B N      1 
ATOM   6240 C CA     . LYS   B 1 155 ? 22.52000  41.32900  -47.64700 1.000 34.38000  ? 121 LYS   B CA     1 
ATOM   6241 C C      . LYS   B 1 155 ? 21.17200  41.57600  -46.97400 1.000 37.42000  ? 121 LYS   B C      1 
ATOM   6242 O O      . LYS   B 1 155 ? 20.20200  41.91800  -47.66200 1.000 35.57000  ? 121 LYS   B O      1 
ATOM   6243 C CB     . LYS   B 1 155 ? 22.54200  39.89100  -48.19400 1.000 37.06000  ? 121 LYS   B CB     1 
ATOM   6244 C CG     . LYS   B 1 155 ? 23.68300  39.61500  -49.17600 1.000 39.35000  ? 121 LYS   B CG     1 
ATOM   6245 C CD     . LYS   B 1 155 ? 23.63000  40.65700  -50.31800 1.000 43.88000  ? 121 LYS   B CD     1 
ATOM   6246 C CE     . LYS   B 1 155 ? 24.25100  40.17900  -51.62400 1.000 59.98000  ? 121 LYS   B CE     1 
ATOM   6247 N NZ     . LYS   B 1 155 ? 23.20100  39.78900  -52.62400 1.000 68.48000  ? 121 LYS   B NZ     1 
ATOM   6248 H H      . LYS   B 1 155 ? 23.77100  40.90600  -46.19300 1.000 36.89000  ? 121 LYS   B H      1 
ATOM   6249 H HA     . LYS   B 1 155 ? 22.58300  41.94700  -48.39000 1.000 34.38000  ? 121 LYS   B HA     1 
ATOM   6250 H HB2    . LYS   B 1 155 ? 22.63600  39.27600  -47.45000 1.000 37.06000  ? 121 LYS   B HB2    1 
ATOM   6251 H HB3    . LYS   B 1 155 ? 21.70700  39.72200  -48.65600 1.000 37.06000  ? 121 LYS   B HB3    1 
ATOM   6252 H HG2    . LYS   B 1 155 ? 24.53500  39.69600  -48.72000 1.000 39.35000  ? 121 LYS   B HG2    1 
ATOM   6253 H HG3    . LYS   B 1 155 ? 23.58000  38.72900  -49.55700 1.000 39.35000  ? 121 LYS   B HG3    1 
ATOM   6254 H HD2    . LYS   B 1 155 ? 22.70200  40.87900  -50.49500 1.000 43.88000  ? 121 LYS   B HD2    1 
ATOM   6255 H HD3    . LYS   B 1 155 ? 24.11000  41.45200  -50.03700 1.000 43.88000  ? 121 LYS   B HD3    1 
ATOM   6256 H HE2    . LYS   B 1 155 ? 24.78100  40.89600  -52.00600 1.000 59.98000  ? 121 LYS   B HE2    1 
ATOM   6257 H HE3    . LYS   B 1 155 ? 24.81000  39.40700  -51.44800 1.000 59.98000  ? 121 LYS   B HE3    1 
ATOM   6258 H HZ1    . LYS   B 1 155 ? 23.58700  39.49600  -53.37000 1.000 68.48000  ? 121 LYS   B HZ1    1 
ATOM   6259 H HZ2    . LYS   B 1 155 ? 22.68900  39.14200  -52.29000 1.000 68.48000  ? 121 LYS   B HZ2    1 
ATOM   6260 H HZ3    . LYS   B 1 155 ? 22.69000  40.49200  -52.81800 1.000 68.48000  ? 121 LYS   B HZ3    1 
ATOM   6261 N N      . GLY   B 1 156 ? 21.07500  41.38100  -45.66000 1.000 36.93000  ? 122 GLY   B N      1 
ATOM   6262 C CA     . GLY   B 1 156 ? 19.83500  41.65800  -44.96700 1.000 35.10000  ? 122 GLY   B CA     1 
ATOM   6263 C C      . GLY   B 1 156 ? 18.91300  40.47300  -44.76400 1.000 36.39000  ? 122 GLY   B C      1 
ATOM   6264 O O      . GLY   B 1 156 ? 17.78900  40.67300  -44.28800 1.000 32.83000  ? 122 GLY   B O      1 
ATOM   6265 H H      . GLY   B 1 156 ? 21.71000  41.09200  -45.15700 1.000 36.93000  ? 122 GLY   B H      1 
ATOM   6266 H HA2    . GLY   B 1 156 ? 20.04400  42.02100  -44.09200 1.000 35.10000  ? 122 GLY   B HA2    1 
ATOM   6267 H HA3    . GLY   B 1 156 ? 19.34400  42.33500  -45.45800 1.000 35.10000  ? 122 GLY   B HA3    1 
ATOM   6268 N N      . VAL   B 1 157 ? 19.35100  39.24900  -45.09500 1.000 29.49000  ? 123 VAL   B N      1 
ATOM   6269 C CA     . VAL   B 1 157 ? 18.56900  38.07100  -44.74800 1.000 29.59000  ? 123 VAL   B CA     1 
ATOM   6270 C C      . VAL   B 1 157 ? 18.34200  38.02600  -43.23600 1.000 31.34000  ? 123 VAL   B C      1 
ATOM   6271 O O      . VAL   B 1 157 ? 19.20800  38.41900  -42.44000 1.000 31.75000  ? 123 VAL   B O      1 
ATOM   6272 C CB     . VAL   B 1 157 ? 19.25600  36.79600  -45.28700 1.000 31.16000  ? 123 VAL   B CB     1 
ATOM   6273 C CG1    . VAL   B 1 157 ? 20.65100  36.60500  -44.70100 1.000 32.51000  ? 123 VAL   B CG1    1 
ATOM   6274 C CG2    . VAL   B 1 157 ? 18.38900  35.54700  -45.01000 1.000 27.34000  ? 123 VAL   B CG2    1 
ATOM   6275 H H      . VAL   B 1 157 ? 20.08400  39.08400  -45.51300 1.000 29.49000  ? 123 VAL   B H      1 
ATOM   6276 H HA     . VAL   B 1 157 ? 17.70000  38.13900  -45.17400 1.000 29.59000  ? 123 VAL   B HA     1 
ATOM   6277 H HB     . VAL   B 1 157 ? 19.35100  36.87900  -46.24800 1.000 31.16000  ? 123 VAL   B HB     1 
ATOM   6278 H HG11   . VAL   B 1 157 ? 21.04300  35.80300  -45.07900 1.000 32.51000  ? 123 VAL   B HG11   1 
ATOM   6279 H HG12   . VAL   B 1 157 ? 21.19600  37.37600  -44.92300 1.000 32.51000  ? 123 VAL   B HG12   1 
ATOM   6280 H HG13   . VAL   B 1 157 ? 20.58100  36.51600  -43.73800 1.000 32.51000  ? 123 VAL   B HG13   1 
ATOM   6281 H HG21   . VAL   B 1 157 ? 18.79700  34.77900  -45.44100 1.000 27.34000  ? 123 VAL   B HG21   1 
ATOM   6282 H HG22   . VAL   B 1 157 ? 18.34000  35.40100  -44.05200 1.000 27.34000  ? 123 VAL   B HG22   1 
ATOM   6283 H HG23   . VAL   B 1 157 ? 17.50000  35.69400  -45.36900 1.000 27.34000  ? 123 VAL   B HG23   1 
ATOM   6284 N N      . ILE   B 1 158 ? 17.17000  37.52600  -42.83700 1.000 26.52000  ? 124 ILE   B N      1 
ATOM   6285 C CA     . ILE   B 1 158 ? 16.70400  37.54200  -41.45100 1.000 29.22000  ? 124 ILE   B CA     1 
ATOM   6286 C C      . ILE   B 1 158 ? 16.58200  36.11200  -40.94100 1.000 31.40000  ? 124 ILE   B C      1 
ATOM   6287 O O      . ILE   B 1 158 ? 15.91900  35.28700  -41.57100 1.000 28.27000  ? 124 ILE   B O      1 
ATOM   6288 C CB     . ILE   B 1 158 ? 15.34000  38.24900  -41.33100 1.000 30.89000  ? 124 ILE   B CB     1 
ATOM   6289 C CG1    . ILE   B 1 158 ? 15.38800  39.63900  -41.99100 1.000 32.26000  ? 124 ILE   B CG1    1 
ATOM   6290 C CG2    . ILE   B 1 158 ? 14.88800  38.28900  -39.87900 1.000 29.82000  ? 124 ILE   B CG2    1 
ATOM   6291 C CD1    . ILE   B 1 158 ? 13.99900  40.18700  -42.36800 1.000 33.09000  ? 124 ILE   B CD1    1 
ATOM   6292 H H      . ILE   B 1 158 ? 16.60800  37.15900  -43.37400 1.000 26.52000  ? 124 ILE   B H      1 
ATOM   6293 H HA     . ILE   B 1 158 ? 17.34500  38.01400  -40.89700 1.000 29.22000  ? 124 ILE   B HA     1 
ATOM   6294 H HB     . ILE   B 1 158 ? 14.69500  37.71800  -41.82200 1.000 30.89000  ? 124 ILE   B HB     1 
ATOM   6295 H HG12   . ILE   B 1 158 ? 15.79400  40.26500  -41.37100 1.000 32.26000  ? 124 ILE   B HG12   1 
ATOM   6296 H HG13   . ILE   B 1 158 ? 15.91300  39.59700  -42.80400 1.000 32.26000  ? 124 ILE   B HG13   1 
ATOM   6297 H HG21   . ILE   B 1 158 ? 14.14300  38.90500  -39.79900 1.000 29.82000  ? 124 ILE   B HG21   1 
ATOM   6298 H HG22   . ILE   B 1 158 ? 14.61100  37.40000  -39.60700 1.000 29.82000  ? 124 ILE   B HG22   1 
ATOM   6299 H HG23   . ILE   B 1 158 ? 15.62600  38.59100  -39.32700 1.000 29.82000  ? 124 ILE   B HG23   1 
ATOM   6300 H HD11   . ILE   B 1 158 ? 14.10600  41.05400  -42.78900 1.000 33.09000  ? 124 ILE   B HD11   1 
ATOM   6301 H HD12   . ILE   B 1 158 ? 13.57300  39.57000  -42.98400 1.000 33.09000  ? 124 ILE   B HD12   1 
ATOM   6302 H HD13   . ILE   B 1 158 ? 13.46400  40.27300  -41.56300 1.000 33.09000  ? 124 ILE   B HD13   1 
ATOM   6303 N N      . LEU   B 1 159 ? 17.13700  35.84800  -39.76100 1.000 29.90000  ? 125 LEU   B N      1 
ATOM   6304 C CA     . LEU   B 1 159 ? 17.15400  34.50300  -39.18600 1.000 31.50000  ? 125 LEU   B CA     1 
ATOM   6305 C C      . LEU   B 1 159 ? 15.87000  34.16300  -38.42800 1.000 34.57000  ? 125 LEU   B C      1 
ATOM   6306 O O      . LEU   B 1 159 ? 15.40300  34.95900  -37.60700 1.000 30.82000  ? 125 LEU   B O      1 
ATOM   6307 C CB     . LEU   B 1 159 ? 18.34300  34.39000  -38.24000 1.000 34.53000  ? 125 LEU   B CB     1 
ATOM   6308 C CG     . LEU   B 1 159 ? 18.38500  33.14200  -37.37200 1.000 32.92000  ? 125 LEU   B CG     1 
ATOM   6309 C CD1    . LEU   B 1 159 ? 18.60600  31.92700  -38.28200 1.000 32.79000  ? 125 LEU   B CD1    1 
ATOM   6310 C CD2    . LEU   B 1 159 ? 19.51900  33.30500  -36.36100 1.000 29.57000  ? 125 LEU   B CD2    1 
ATOM   6311 H H      . LEU   B 1 159 ? 17.51600  36.44000  -39.26600 1.000 29.90000  ? 125 LEU   B H      1 
ATOM   6312 H HA     . LEU   B 1 159 ? 17.26800  33.85300  -39.89700 1.000 31.50000  ? 125 LEU   B HA     1 
ATOM   6313 H HB2    . LEU   B 1 159 ? 19.15600  34.40300  -38.76900 1.000 34.53000  ? 125 LEU   B HB2    1 
ATOM   6314 H HB3    . LEU   B 1 159 ? 18.33300  35.15600  -37.64500 1.000 34.53000  ? 125 LEU   B HB3    1 
ATOM   6315 H HG     . LEU   B 1 159 ? 17.55500  33.02800  -36.88500 1.000 32.92000  ? 125 LEU   B HG     1 
ATOM   6316 H HD11   . LEU   B 1 159 ? 18.72500  31.13900  -37.72900 1.000 32.79000  ? 125 LEU   B HD11   1 
ATOM   6317 H HD12   . LEU   B 1 159 ? 17.83200  31.81600  -38.85600 1.000 32.79000  ? 125 LEU   B HD12   1 
ATOM   6318 H HD13   . LEU   B 1 159 ? 19.39900  32.07600  -38.82000 1.000 32.79000  ? 125 LEU   B HD13   1 
ATOM   6319 H HD21   . LEU   B 1 159 ? 19.56400  32.51000  -35.80700 1.000 29.57000  ? 125 LEU   B HD21   1 
ATOM   6320 H HD22   . LEU   B 1 159 ? 20.35400  33.42300  -36.84000 1.000 29.57000  ? 125 LEU   B HD22   1 
ATOM   6321 H HD23   . LEU   B 1 159 ? 19.34100  34.08300  -35.81000 1.000 29.57000  ? 125 LEU   B HD23   1 
ATOM   6322 N N      . GLU   B 1 160 ? 15.31700  32.96600  -38.68700 1.000 30.35000  ? 126 GLU   B N      1 
ATOM   6323 C CA     . GLU   B 1 160 ? 14.27600  32.33400  -37.86800 1.000 30.04000  ? 126 GLU   B CA     1 
ATOM   6324 C C      . GLU   B 1 160 ? 14.85500  31.04400  -37.30000 1.000 35.30000  ? 126 GLU   B C      1 
ATOM   6325 O O      . GLU   B 1 160 ? 15.27100  30.16900  -38.06200 1.000 31.29000  ? 126 GLU   B O      1 
ATOM   6326 C CB     . GLU   B 1 160 ? 12.99800  32.04100  -38.68900 1.000 29.09000  ? 126 GLU   B CB     1 
ATOM   6327 C CG     . GLU   B 1 160 ? 11.73500  31.53600  -37.84500 1.000 31.37000  ? 126 GLU   B CG     1 
ATOM   6328 C CD     . GLU   B 1 160 ? 10.44300  31.24300  -38.69400 1.000 38.05000  ? 126 GLU   B CD     1 
ATOM   6329 O OE1    . GLU   B 1 160 ? 10.22500  30.07500  -39.12300 1.000 34.30000  ? 126 GLU   B OE1    1 
ATOM   6330 O OE2    . GLU   B 1 160 ? 9.60400   32.15100  -38.88500 1.000 35.64000  ? 126 GLU   B OE2    1 
ATOM   6331 H H      . GLU   B 1 160 ? 15.54300  32.48400  -39.36300 1.000 30.35000  ? 126 GLU   B H      1 
ATOM   6332 H HA     . GLU   B 1 160 ? 14.04200  32.91900  -37.13000 1.000 30.04000  ? 126 GLU   B HA     1 
ATOM   6333 H HB2    . GLU   B 1 160 ? 12.73500  32.85400  -39.14700 1.000 29.09000  ? 126 GLU   B HB2    1 
ATOM   6334 H HB3    . GLU   B 1 160 ? 13.20400  31.35400  -39.34200 1.000 29.09000  ? 126 GLU   B HB3    1 
ATOM   6335 H HG2    . GLU   B 1 160 ? 11.97700  30.71500  -37.38800 1.000 31.37000  ? 126 GLU   B HG2    1 
ATOM   6336 H HG3    . GLU   B 1 160 ? 11.50800  32.21700  -37.19200 1.000 31.37000  ? 126 GLU   B HG3    1 
ATOM   6337 N N      . LEU   B 1 161 ? 14.90200  30.93500  -35.97100 1.000 30.53000  ? 127 LEU   B N      1 
ATOM   6338 C CA     . LEU   B 1 161 ? 15.41400  29.74800  -35.29000 1.000 31.19000  ? 127 LEU   B CA     1 
ATOM   6339 C C      . LEU   B 1 161 ? 14.28300  28.76400  -35.02600 1.000 32.70000  ? 127 LEU   B C      1 
ATOM   6340 O O      . LEU   B 1 161 ? 13.32000  29.08500  -34.32500 1.000 33.29000  ? 127 LEU   B O      1 
ATOM   6341 C CB     . LEU   B 1 161 ? 16.07500  30.14600  -33.97000 1.000 34.90000  ? 127 LEU   B CB     1 
ATOM   6342 C CG     . LEU   B 1 161 ? 16.64700  29.07800  -33.03400 1.000 40.56000  ? 127 LEU   B CG     1 
ATOM   6343 C CD1    . LEU   B 1 161 ? 17.88100  28.43800  -33.63800 1.000 41.70000  ? 127 LEU   B CD1    1 
ATOM   6344 C CD2    . LEU   B 1 161 ? 16.98300  29.77000  -31.71600 1.000 40.34000  ? 127 LEU   B CD2    1 
ATOM   6345 H H      . LEU   B 1 161 ? 14.63700  31.55000  -35.43200 1.000 30.53000  ? 127 LEU   B H      1 
ATOM   6346 H HA     . LEU   B 1 161 ? 16.07700  29.31300  -35.84800 1.000 31.19000  ? 127 LEU   B HA     1 
ATOM   6347 H HB2    . LEU   B 1 161 ? 16.80900  30.74300  -34.18300 1.000 34.90000  ? 127 LEU   B HB2    1 
ATOM   6348 H HB3    . LEU   B 1 161 ? 15.41600  30.63700  -33.45400 1.000 34.90000  ? 127 LEU   B HB3    1 
ATOM   6349 H HG     . LEU   B 1 161 ? 15.98300  28.39100  -32.86800 1.000 40.56000  ? 127 LEU   B HG     1 
ATOM   6350 H HD11   . LEU   B 1 161 ? 18.22000  27.76700  -33.02500 1.000 41.70000  ? 127 LEU   B HD11   1 
ATOM   6351 H HD12   . LEU   B 1 161 ? 17.64100  28.02400  -34.48200 1.000 41.70000  ? 127 LEU   B HD12   1 
ATOM   6352 H HD13   . LEU   B 1 161 ? 18.55200  29.12300  -33.78400 1.000 41.70000  ? 127 LEU   B HD13   1 
ATOM   6353 H HD21   . LEU   B 1 161 ? 17.38900  29.12500  -31.11600 1.000 40.34000  ? 127 LEU   B HD21   1 
ATOM   6354 H HD22   . LEU   B 1 161 ? 17.60200  30.49600  -31.89000 1.000 40.34000  ? 127 LEU   B HD22   1 
ATOM   6355 H HD23   . LEU   B 1 161 ? 16.16600  30.11800  -31.32500 1.000 40.34000  ? 127 LEU   B HD23   1 
ATOM   6356 N N      . ASN   B 1 162 ? 14.40600  27.54900  -35.53500 1.000 31.86000  ? 128 ASN   B N      1 
ATOM   6357 C CA     . ASN   B 1 162 ? 13.35700  26.55400  -35.33600 1.000 33.34000  ? 128 ASN   B CA     1 
ATOM   6358 C C      . ASN   B 1 162 ? 13.56200  25.85100  -33.99200 1.000 41.28000  ? 128 ASN   B C      1 
ATOM   6359 O O      . ASN   B 1 162 ? 14.53100  25.11300  -33.81100 1.000 39.83000  ? 128 ASN   B O      1 
ATOM   6360 C CB     . ASN   B 1 162 ? 13.33900  25.56000  -36.48800 1.000 33.87000  ? 128 ASN   B CB     1 
ATOM   6361 C CG     . ASN   B 1 162 ? 12.14900  24.61300  -36.42000 1.000 37.63000  ? 128 ASN   B CG     1 
ATOM   6362 O OD1    . ASN   B 1 162 ? 11.40100  24.59200  -35.43300 1.000 39.41000  ? 128 ASN   B OD1    1 
ATOM   6363 N ND2    . ASN   B 1 162 ? 11.97000  23.82700  -37.47200 1.000 38.32000  ? 128 ASN   B ND2    1 
ATOM   6364 H H      . ASN   B 1 162 ? 15.07800  27.27400  -35.99500 1.000 31.86000  ? 128 ASN   B H      1 
ATOM   6365 H HA     . ASN   B 1 162 ? 12.49700  26.99900  -35.31200 1.000 33.34000  ? 128 ASN   B HA     1 
ATOM   6366 H HB2    . ASN   B 1 162 ? 13.29400  26.04400  -37.32700 1.000 33.87000  ? 128 ASN   B HB2    1 
ATOM   6367 H HB3    . ASN   B 1 162 ? 14.14700  25.02800  -36.45200 1.000 33.87000  ? 128 ASN   B HB3    1 
ATOM   6368 H HD21   . ASN   B 1 162 ? 11.31300  23.27200  -37.48700 1.000 38.32000  ? 128 ASN   B HD21   1 
ATOM   6369 H HD22   . ASN   B 1 162 ? 12.51100  23.87100  -38.13900 1.000 38.32000  ? 128 ASN   B HD22   1 
ATOM   6370 N N      . LEU   B 1 163 ? 12.65600  26.09000  -33.04300 1.000 35.13000  ? 129 LEU   B N      1 
ATOM   6371 C CA     . LEU   B 1 163 ? 12.68800  25.42700  -31.74000 1.000 33.66000  ? 129 LEU   B CA     1 
ATOM   6372 C C      . LEU   B 1 163 ? 11.53900  24.45200  -31.57700 1.000 38.60000  ? 129 LEU   B C      1 
ATOM   6373 O O      . LEU   B 1 163 ? 11.09000  24.21100  -30.45400 1.000 41.08000  ? 129 LEU   B O      1 
ATOM   6374 C CB     . LEU   B 1 163 ? 12.63700  26.44400  -30.60800 1.000 34.42000  ? 129 LEU   B CB     1 
ATOM   6375 C CG     . LEU   B 1 163 ? 13.69400  27.53600  -30.54900 1.000 40.80000  ? 129 LEU   B CG     1 
ATOM   6376 C CD1    . LEU   B 1 163 ? 13.34400  28.48400  -29.42500 1.000 47.96000  ? 129 LEU   B CD1    1 
ATOM   6377 C CD2    . LEU   B 1 163 ? 15.07400  26.93800  -30.35000 1.000 39.99000  ? 129 LEU   B CD2    1 
ATOM   6378 H H      . LEU   B 1 163 ? 12.00200  26.64200  -33.13200 1.000 35.13000  ? 129 LEU   B H      1 
ATOM   6379 H HA     . LEU   B 1 163 ? 13.51600  24.92900  -31.65600 1.000 33.66000  ? 129 LEU   B HA     1 
ATOM   6380 H HB2    . LEU   B 1 163 ? 11.77700  26.89100  -30.65200 1.000 34.42000  ? 129 LEU   B HB2    1 
ATOM   6381 H HB3    . LEU   B 1 163 ? 12.69500  25.95700  -29.77100 1.000 34.42000  ? 129 LEU   B HB3    1 
ATOM   6382 H HG     . LEU   B 1 163 ? 13.69200  28.03300  -31.38200 1.000 40.80000  ? 129 LEU   B HG     1 
ATOM   6383 H HD11   . LEU   B 1 163 ? 14.02100  29.17700  -29.37500 1.000 47.96000  ? 129 LEU   B HD11   1 
ATOM   6384 H HD12   . LEU   B 1 163 ? 12.47700  28.88100  -29.60500 1.000 47.96000  ? 129 LEU   B HD12   1 
ATOM   6385 H HD13   . LEU   B 1 163 ? 13.31500  27.98800  -28.59200 1.000 47.96000  ? 129 LEU   B HD13   1 
ATOM   6386 H HD21   . LEU   B 1 163 ? 15.72200  27.65600  -30.28000 1.000 39.99000  ? 129 LEU   B HD21   1 
ATOM   6387 H HD22   . LEU   B 1 163 ? 15.07500  26.41100  -29.53600 1.000 39.99000  ? 129 LEU   B HD22   1 
ATOM   6388 H HD23   . LEU   B 1 163 ? 15.28600  26.37300  -31.11000 1.000 39.99000  ? 129 LEU   B HD23   1 
ATOM   6389 N N      . SER   B 1 164 ? 10.98200  23.92600  -32.67600 1.000 32.96000  ? 130 SER   B N      1 
ATOM   6390 C CA     . SER   B 1 164 ? 9.70300   23.16700  -32.61400 1.000 33.03000  ? 130 SER   B CA     1 
ATOM   6391 C C      . SER   B 1 164 ? 9.57600   21.97700  -33.57300 1.000 39.03000  ? 130 SER   B C      1 
ATOM   6392 O O      . SER   B 1 164 ? 8.45500   21.45700  -33.69900 1.000 43.85000  ? 130 SER   B O      1 
ATOM   6393 C CB     . SER   B 1 164 ? 8.58200   24.13100  -32.85800 1.000 37.20000  ? 130 SER   B CB     1 
ATOM   6394 O OG     . SER   B 1 164 ? 9.01700   25.26800  -33.56800 1.000 34.49000  ? 130 SER   B OG     1 
ATOM   6395 H H      . SER   B 1 164 ? 11.35100  24.01300  -33.49400 1.000 32.96000  ? 130 SER   B H      1 
ATOM   6396 H HA     . SER   B 1 164 ? 9.59900   22.81000  -31.70000 1.000 33.03000  ? 130 SER   B HA     1 
ATOM   6397 H HB2    . SER   B 1 164 ? 7.86600   23.70400  -33.35200 1.000 37.20000  ? 130 SER   B HB2    1 
ATOM   6398 H HB3    . SER   B 1 164 ? 8.22600   24.40000  -32.00800 1.000 37.20000  ? 130 SER   B HB3    1 
ATOM   6399 H HG     . SER   B 1 164 ? 9.18000   25.85200  -32.99300 1.000 34.49000  ? 130 SER   B HG     1 
ATOM   6400 N N      . CYS   B 1 165 ? 10.75900  21.50100  -34.18700 0.870 41.09000  ? 131 CYS   B N      1 
ATOM   6401 C CA     . CYS   B 1 165 ? 10.56000  20.27100  -34.99200 0.870 44.56000  ? 131 CYS   B CA     1 
ATOM   6402 C C      . CYS   B 1 165 ? 9.96100   19.29900  -34.25500 0.870 39.30000  ? 131 CYS   B C      1 
ATOM   6403 O O      . CYS   B 1 165 ? 10.45600  18.99300  -33.23200 0.870 45.39000  ? 131 CYS   B O      1 
ATOM   6404 C CB     . CYS   B 1 165 ? 11.83600  19.77000  -35.67000 0.870 53.81000  ? 131 CYS   B CB     1 
ATOM   6405 S SG     . CYS   B 1 165 ? 11.46300  18.63700  -37.03700 0.870 45.44000  ? 131 CYS   B SG     1 
ATOM   6406 H H      . CYS   B 1 165 ? 11.32500  22.02600  -34.82400 0.870 49.31000  ? 131 CYS   B H      1 
ATOM   6407 H HA     . CYS   B 1 165 ? 9.97100   20.87600  -35.47000 0.870 53.48000  ? 131 CYS   B HA     1 
ATOM   6408 H HB2    . CYS   B 1 165 ? 12.33700  20.52900  -36.00600 0.870 64.57000  ? 131 CYS   B HB2    1 
ATOM   6409 H HB3    . CYS   B 1 165 ? 12.37800  19.31400  -35.01500 0.870 64.57000  ? 131 CYS   B HB3    1 
ATOM   6410 N N      . PRO   B 1 166 ? 8.83600   18.68900  -34.69700 0.930 44.78000  ? 132 PRO   B N      1 
ATOM   6411 C CA     . PRO   B 1 166 ? 8.24500   17.56200  -33.99500 0.930 40.34000  ? 132 PRO   B CA     1 
ATOM   6412 C C      . PRO   B 1 166 ? 8.68200   16.20500  -34.53700 0.930 44.56000  ? 132 PRO   B C      1 
ATOM   6413 O O      . PRO   B 1 166 ? 8.13700   15.21300  -34.02900 0.930 49.13000  ? 132 PRO   B O      1 
ATOM   6414 C CB     . PRO   B 1 166 ? 6.78300   17.84200  -34.29200 0.930 41.33000  ? 132 PRO   B CB     1 
ATOM   6415 C CG     . PRO   B 1 166 ? 6.79400   18.24600  -35.74100 0.930 37.22000  ? 132 PRO   B CG     1 
ATOM   6416 C CD     . PRO   B 1 166 ? 8.08200   19.03500  -35.89000 0.930 39.79000  ? 132 PRO   B CD     1 
ATOM   6417 H HA     . PRO   B 1 166 ? 8.40800   17.62000  -33.02300 0.930 40.34000  ? 132 PRO   B HA     1 
ATOM   6418 H HB2    . PRO   B 1 166 ? 6.23000   17.04800  -34.14700 0.930 41.33000  ? 132 PRO   B HB2    1 
ATOM   6419 H HB3    . PRO   B 1 166 ? 6.44400   18.57500  -33.72700 0.930 41.33000  ? 132 PRO   B HB3    1 
ATOM   6420 H HG2    . PRO   B 1 166 ? 6.79500   17.46000  -36.32500 0.930 37.22000  ? 132 PRO   B HG2    1 
ATOM   6421 H HG3    . PRO   B 1 166 ? 6.01600   18.80200  -35.95700 0.930 37.22000  ? 132 PRO   B HG3    1 
ATOM   6422 H HD2    . PRO   B 1 166 ? 8.56500   18.76500  -36.70000 0.930 39.79000  ? 132 PRO   B HD2    1 
ATOM   6423 H HD3    . PRO   B 1 166 ? 7.90100   20.00000  -35.93100 0.930 39.79000  ? 132 PRO   B HD3    1 
ATOM   6424 N N      . ASN   B 1 167 ? 9.63600   16.14300  -35.47900 1.000 47.84000  ? 133 ASN   B N      1 
ATOM   6425 C CA     . ASN   B 1 167 ? 10.01500  14.89900  -36.14400 1.000 58.08000  ? 133 ASN   B CA     1 
ATOM   6426 C C      . ASN   B 1 167 ? 11.50500  14.56600  -35.98100 1.000 63.32000  ? 133 ASN   B C      1 
ATOM   6427 O O      . ASN   B 1 167 ? 12.05600  13.81300  -36.79100 1.000 56.90000  ? 133 ASN   B O      1 
ATOM   6428 C CB     . ASN   B 1 167 ? 9.60000   14.96700  -37.62100 1.000 45.82000  ? 133 ASN   B CB     1 
ATOM   6429 C CG     . ASN   B 1 167 ? 8.07900   15.19700  -37.80400 1.000 53.72000  ? 133 ASN   B CG     1 
ATOM   6430 O OD1    . ASN   B 1 167 ? 7.65600   16.00200  -38.64200 1.000 51.73000  ? 133 ASN   B OD1    1 
ATOM   6431 N ND2    . ASN   B 1 167 ? 7.26000   14.48700  -37.01300 1.000 38.81000  ? 133 ASN   B ND2    1 
ATOM   6432 H H      . ASN   B 1 167 ? 10.06100  16.84100  -35.74700 1.000 47.84000  ? 133 ASN   B H      1 
ATOM   6433 H HA     . ASN   B 1 167 ? 9.52200   14.16800  -35.74200 1.000 58.08000  ? 133 ASN   B HA     1 
ATOM   6434 H HB2    . ASN   B 1 167 ? 10.06800  15.70200  -38.04800 1.000 45.82000  ? 133 ASN   B HB2    1 
ATOM   6435 H HB3    . ASN   B 1 167 ? 9.83100   14.13000  -38.05300 1.000 45.82000  ? 133 ASN   B HB3    1 
ATOM   6436 H HD21   . ASN   B 1 167 ? 6.40800   14.58300  -37.08100 1.000 38.81000  ? 133 ASN   B HD21   1 
ATOM   6437 H HD22   . ASN   B 1 167 ? 7.58500   13.93500  -36.44000 1.000 38.81000  ? 133 ASN   B HD22   1 
ATOM   6438 N N      . VAL   B 1 168 ? 12.14600  15.07700  -34.93300 1.000 61.13000  ? 134 VAL   B N      1 
ATOM   6439 C CA     . VAL   B 1 168 ? 13.56500  14.82900  -34.67200 1.000 71.05000  ? 134 VAL   B CA     1 
ATOM   6440 C C      . VAL   B 1 168 ? 13.67700  13.55900  -33.83700 1.000 65.00000  ? 134 VAL   B C      1 
ATOM   6441 O O      . VAL   B 1 168 ? 13.16500  13.52700  -32.70500 1.000 68.71000  ? 134 VAL   B O      1 
ATOM   6442 C CB     . VAL   B 1 168 ? 14.20500  16.01800  -33.93900 1.000 71.85000  ? 134 VAL   B CB     1 
ATOM   6443 C CG1    . VAL   B 1 168 ? 15.61300  15.66400  -33.44700 1.000 65.97000  ? 134 VAL   B CG1    1 
ATOM   6444 C CG2    . VAL   B 1 168 ? 14.20600  17.28700  -34.81400 1.000 57.01000  ? 134 VAL   B CG2    1 
ATOM   6445 H H      . VAL   B 1 168 ? 11.77400  15.58200  -34.34500 1.000 61.13000  ? 134 VAL   B H      1 
ATOM   6446 H HA     . VAL   B 1 168 ? 14.02800  14.71900  -35.51400 1.000 71.05000  ? 134 VAL   B HA     1 
ATOM   6447 H HB     . VAL   B 1 168 ? 13.66900  16.21300  -33.15400 1.000 71.85000  ? 134 VAL   B HB     1 
ATOM   6448 H HG11   . VAL   B 1 168 ? 16.08100  16.48300  -33.22200 1.000 65.97000  ? 134 VAL   B HG11   1 
ATOM   6449 H HG12   . VAL   B 1 168 ? 15.54400  15.09800  -32.66200 1.000 65.97000  ? 134 VAL   B HG12   1 
ATOM   6450 H HG13   . VAL   B 1 168 ? 16.08600  15.19800  -34.15400 1.000 65.97000  ? 134 VAL   B HG13   1 
ATOM   6451 H HG21   . VAL   B 1 168 ? 14.20600  18.06700  -34.23800 1.000 57.01000  ? 134 VAL   B HG21   1 
ATOM   6452 H HG22   . VAL   B 1 168 ? 15.00100  17.28600  -35.37000 1.000 57.01000  ? 134 VAL   B HG22   1 
ATOM   6453 H HG23   . VAL   B 1 168 ? 13.41400  17.28100  -35.37000 1.000 57.01000  ? 134 VAL   B HG23   1 
ATOM   6454 N N      . PRO   B 1 169 ? 14.34200  12.50500  -34.32700 1.000 79.60000  ? 135 PRO   B N      1 
ATOM   6455 C CA     . PRO   B 1 169 ? 14.38400  11.23300  -33.57500 1.000 75.22000  ? 135 PRO   B CA     1 
ATOM   6456 C C      . PRO   B 1 169 ? 15.03500  11.38900  -32.20700 1.000 74.36000  ? 135 PRO   B C      1 
ATOM   6457 O O      . PRO   B 1 169 ? 16.19000  11.81100  -32.09000 1.000 75.46000  ? 135 PRO   B O      1 
ATOM   6458 C CB     . PRO   B 1 169 ? 15.20300  10.31000  -34.48800 1.000 68.20000  ? 135 PRO   B CB     1 
ATOM   6459 C CG     . PRO   B 1 169 ? 15.05700  10.89000  -35.85300 1.000 83.38000  ? 135 PRO   B CG     1 
ATOM   6460 C CD     . PRO   B 1 169 ? 14.98200  12.38300  -35.64900 1.000 88.68000  ? 135 PRO   B CD     1 
ATOM   6461 H HA     . PRO   B 1 169 ? 13.49000  10.87200  -33.46900 1.000 75.22000  ? 135 PRO   B HA     1 
ATOM   6462 H HB2    . PRO   B 1 169 ? 16.13200  10.31500  -34.21000 1.000 68.20000  ? 135 PRO   B HB2    1 
ATOM   6463 H HB3    . PRO   B 1 169 ? 14.83900  9.41100   -34.45600 1.000 68.20000  ? 135 PRO   B HB3    1 
ATOM   6464 H HG2    . PRO   B 1 169 ? 15.83000  10.65700  -36.39100 1.000 83.38000  ? 135 PRO   B HG2    1 
ATOM   6465 H HG3    . PRO   B 1 169 ? 14.24200  10.55900  -36.26200 1.000 83.38000  ? 135 PRO   B HG3    1 
ATOM   6466 H HD2    . PRO   B 1 169 ? 15.87100  12.77000  -35.63400 1.000 88.68000  ? 135 PRO   B HD2    1 
ATOM   6467 H HD3    . PRO   B 1 169 ? 14.42900  12.78200  -36.33800 1.000 88.68000  ? 135 PRO   B HD3    1 
ATOM   6468 N N      . GLY   B 1 170 ? 14.27700  11.03900  -31.16000 1.000 72.38000  ? 136 GLY   B N      1 
ATOM   6469 C CA     . GLY   B 1 170 ? 14.76600  11.05400  -29.79400 1.000 67.90000  ? 136 GLY   B CA     1 
ATOM   6470 C C      . GLY   B 1 170 ? 14.79200  12.40300  -29.10000 1.000 72.11000  ? 136 GLY   B C      1 
ATOM   6471 O O      . GLY   B 1 170 ? 14.91900  12.44400  -27.86900 1.000 75.57000  ? 136 GLY   B O      1 
ATOM   6472 H H      . GLY   B 1 170 ? 13.45800  10.78500  -31.22700 1.000 72.38000  ? 136 GLY   B H      1 
ATOM   6473 H HA2    . GLY   B 1 170 ? 14.21300  10.46100  -29.26100 1.000 67.90000  ? 136 GLY   B HA2    1 
ATOM   6474 H HA3    . GLY   B 1 170 ? 15.67000  10.70200  -29.78600 1.000 67.90000  ? 136 GLY   B HA3    1 
ATOM   6475 N N      . LYS   B 1 171 ? 14.68400  13.51200  -29.83600 1.000 76.58000  ? 137 LYS   B N      1 
ATOM   6476 C CA     . LYS   B 1 171 ? 14.76600  14.85000  -29.24600 1.000 69.91000  ? 137 LYS   B CA     1 
ATOM   6477 C C      . LYS   B 1 171 ? 13.41900  15.55800  -29.34500 1.000 71.38000  ? 137 LYS   B C      1 
ATOM   6478 O O      . LYS   B 1 171 ? 13.02500  15.97000  -30.44800 1.000 65.31000  ? 137 LYS   B O      1 
ATOM   6479 C CB     . LYS   B 1 171 ? 15.85400  15.67900  -29.93800 1.000 65.78000  ? 137 LYS   B CB     1 
ATOM   6480 H H      . LYS   B 1 171 ? 14.56200  13.51600  -30.68700 1.000 76.58000  ? 137 LYS   B H      1 
ATOM   6481 H HA     . LYS   B 1 171 ? 15.02100  14.77200  -28.31600 1.000 69.91000  ? 137 LYS   B HA     1 
ATOM   6482 N N      . PRO   B 1 172 ? 12.68500  15.72700  -28.24200 1.000 66.72000  ? 138 PRO   B N      1 
ATOM   6483 C CA     . PRO   B 1 172 ? 11.38800  16.41400  -28.31100 1.000 60.88000  ? 138 PRO   B CA     1 
ATOM   6484 C C      . PRO   B 1 172 ? 11.54300  17.88200  -28.69700 1.000 50.17000  ? 138 PRO   B C      1 
ATOM   6485 O O      . PRO   B 1 172 ? 12.63000  18.45500  -28.64600 1.000 48.91000  ? 138 PRO   B O      1 
ATOM   6486 C CB     . PRO   B 1 172 ? 10.83000  16.27800  -26.88500 1.000 57.82000  ? 138 PRO   B CB     1 
ATOM   6487 C CG     . PRO   B 1 172 ? 11.65700  15.19600  -26.22500 1.000 64.39000  ? 138 PRO   B CG     1 
ATOM   6488 C CD     . PRO   B 1 172 ? 13.00100  15.26000  -26.87900 1.000 59.74000  ? 138 PRO   B CD     1 
ATOM   6489 H HA     . PRO   B 1 172 ? 10.78900  15.99900  -28.94000 1.000 60.88000  ? 138 PRO   B HA     1 
ATOM   6490 H HB2    . PRO   B 1 172 ? 10.93100  17.12000  -26.41400 1.000 57.82000  ? 138 PRO   B HB2    1 
ATOM   6491 H HB3    . PRO   B 1 172 ? 9.89600   16.01800  -26.92400 1.000 57.82000  ? 138 PRO   B HB3    1 
ATOM   6492 H HG2    . PRO   B 1 172 ? 11.74100  15.39900  -25.28000 1.000 64.39000  ? 138 PRO   B HG2    1 
ATOM   6493 H HG3    . PRO   B 1 172 ? 11.24100  14.34100  -26.33800 1.000 64.39000  ? 138 PRO   B HG3    1 
ATOM   6494 H HD2    . PRO   B 1 172 ? 13.57100  15.89900  -26.42400 1.000 59.74000  ? 138 PRO   B HD2    1 
ATOM   6495 H HD3    . PRO   B 1 172 ? 13.40100  14.37700  -26.90300 1.000 59.74000  ? 138 PRO   B HD3    1 
ATOM   6496 N N      A GLN   B 1 173 ? 10.42700  18.47500  -29.11300 0.620 42.74000  ? 139 GLN   B N      1 
ATOM   6497 N N      B GLN   B 1 173 ? 10.42600  18.48300  -29.09900 0.380 42.83000  ? 139 GLN   B N      1 
ATOM   6498 C CA     A GLN   B 1 173 ? 10.35800  19.90700  -29.35400 0.620 41.81000  ? 139 GLN   B CA     1 
ATOM   6499 C CA     B GLN   B 1 173 ? 10.39600  19.91100  -29.38200 0.380 41.90000  ? 139 GLN   B CA     1 
ATOM   6500 C C      A GLN   B 1 173 ? 11.17100  20.65500  -28.30000 0.620 46.38000  ? 139 GLN   B C      1 
ATOM   6501 C C      B GLN   B 1 173 ? 11.16900  20.66700  -28.31500 0.380 46.27000  ? 139 GLN   B C      1 
ATOM   6502 O O      A GLN   B 1 173 ? 10.90200  20.54000  -27.10000 0.620 40.22000  ? 139 GLN   B O      1 
ATOM   6503 O O      B GLN   B 1 173 ? 10.85400  20.58400  -27.12300 0.380 40.32000  ? 139 GLN   B O      1 
ATOM   6504 C CB     A GLN   B 1 173 ? 8.89100   20.35600  -29.33400 0.620 45.16000  ? 139 GLN   B CB     1 
ATOM   6505 C CB     B GLN   B 1 173 ? 8.95700   20.41100  -29.43700 0.380 45.04000  ? 139 GLN   B CB     1 
ATOM   6506 C CG     A GLN   B 1 173 ? 7.99400   19.69800  -30.41800 0.620 41.00000  ? 139 GLN   B CG     1 
ATOM   6507 C CG     B GLN   B 1 173 ? 7.93600   19.31000  -29.31300 0.380 41.73000  ? 139 GLN   B CG     1 
ATOM   6508 C CD     A GLN   B 1 173 ? 7.36300   18.34300  -30.00700 0.620 41.74000  ? 139 GLN   B CD     1 
ATOM   6509 C CD     B GLN   B 1 173 ? 7.12500   19.14800  -30.56800 0.380 47.99000  ? 139 GLN   B CD     1 
ATOM   6510 O OE1    A GLN   B 1 173 ? 7.81100   17.67900  -29.08200 0.620 49.32000  ? 139 GLN   B OE1    1 
ATOM   6511 O OE1    B GLN   B 1 173 ? 7.47200   19.70500  -31.61100 0.380 45.19000  ? 139 GLN   B OE1    1 
ATOM   6512 N NE2    A GLN   B 1 173 ? 6.30700   17.95200  -30.70900 0.620 43.38000  ? 139 GLN   B NE2    1 
ATOM   6513 N NE2    B GLN   B 1 173 ? 6.02800   18.38900  -30.47900 0.380 35.10000  ? 139 GLN   B NE2    1 
ATOM   6514 H H      A GLN   B 1 173 ? 9.69100   18.05900  -29.26300 0.620 42.83000  ? 139 GLN   B H      1 
ATOM   6515 H H      B GLN   B 1 173 ? 9.73700   18.03200  -29.28800 0.380 42.83000  ? 139 GLN   B H      1 
ATOM   6516 H HA     A GLN   B 1 173 ? 10.72900  20.10700  -30.22800 0.620 41.90000  ? 139 GLN   B HA     1 
ATOM   6517 H HA     B GLN   B 1 173 ? 10.81300  20.07900  -30.24100 0.380 41.90000  ? 139 GLN   B HA     1 
ATOM   6518 H HB2    A GLN   B 1 173 ? 8.51500   20.13700  -28.46800 0.620 45.04000  ? 139 GLN   B HB2    1 
ATOM   6519 H HB2    B GLN   B 1 173 ? 8.81600   21.02200  -28.69700 0.380 45.04000  ? 139 GLN   B HB2    1 
ATOM   6520 H HB3    A GLN   B 1 173 ? 8.85900   21.31600  -29.47000 0.620 45.04000  ? 139 GLN   B HB3    1 
ATOM   6521 H HB3    B GLN   B 1 173 ? 8.82000   20.88100  -30.27300 0.380 45.04000  ? 139 GLN   B HB3    1 
ATOM   6522 H HG2    A GLN   B 1 173 ? 7.26900   20.30600  -30.63000 0.620 41.73000  ? 139 GLN   B HG2    1 
ATOM   6523 H HG2    B GLN   B 1 173 ? 8.17200   18.47100  -28.90800 0.380 41.73000  ? 139 GLN   B HG2    1 
ATOM   6524 H HG3    A GLN   B 1 173 ? 8.53100   19.54300  -31.21100 0.620 41.73000  ? 139 GLN   B HG3    1 
ATOM   6525 H HG3    B GLN   B 1 173 ? 7.30600   19.72300  -28.77900 0.380 41.73000  ? 139 GLN   B HG3    1 
ATOM   6526 H HE21   A GLN   B 1 173 ? 6.01400   18.44100  -31.35300 0.620 35.10000  ? 139 GLN   B HE21   1 
ATOM   6527 H HE21   B GLN   B 1 173 ? 5.82100   18.01900  -29.73100 0.380 35.10000  ? 139 GLN   B HE21   1 
ATOM   6528 H HE22   A GLN   B 1 173 ? 5.91800   17.20800  -30.52200 0.620 35.10000  ? 139 GLN   B HE22   1 
ATOM   6529 H HE22   B GLN   B 1 173 ? 5.53200   18.26800  -31.17100 0.380 35.10000  ? 139 GLN   B HE22   1 
ATOM   6530 N N      . VAL   B 1 174 ? 12.21300  21.37500  -28.74500 1.000 37.48000  ? 140 VAL   B N      1 
ATOM   6531 C CA     . VAL   B 1 174 ? 13.08000  22.09100  -27.80900 1.000 40.77000  ? 140 VAL   B CA     1 
ATOM   6532 C C      . VAL   B 1 174 ? 12.26800  23.04700  -26.94500 1.000 46.55000  ? 140 VAL   B C      1 
ATOM   6533 O O      . VAL   B 1 174 ? 12.46400  23.13200  -25.72700 1.000 39.23000  ? 140 VAL   B O      1 
ATOM   6534 C CB     . VAL   B 1 174 ? 14.19200  22.84000  -28.57100 1.000 41.10000  ? 140 VAL   B CB     1 
ATOM   6535 C CG1    . VAL   B 1 174 ? 14.82500  23.90600  -27.68400 1.000 38.99000  ? 140 VAL   B CG1    1 
ATOM   6536 C CG2    . VAL   B 1 174 ? 15.25800  21.86500  -29.06000 1.000 50.87000  ? 140 VAL   B CG2    1 
ATOM   6537 H H      A VAL   B 1 174 ? 12.43300  21.46100  -29.57200 0.620 37.48000  ? 140 VAL   B H      1 
ATOM   6538 H H      B VAL   B 1 174 ? 12.44000  21.45700  -29.57000 0.380 37.48000  ? 140 VAL   B H      1 
ATOM   6539 H HA     . VAL   B 1 174 ? 13.50500  21.44700  -27.22100 1.000 40.77000  ? 140 VAL   B HA     1 
ATOM   6540 H HB     . VAL   B 1 174 ? 13.80700  23.28000  -29.34500 1.000 41.10000  ? 140 VAL   B HB     1 
ATOM   6541 H HG11   . VAL   B 1 174 ? 15.68300  24.15600  -28.06100 1.000 38.99000  ? 140 VAL   B HG11   1 
ATOM   6542 H HG12   . VAL   B 1 174 ? 14.24400  24.68200  -27.65000 1.000 38.99000  ? 140 VAL   B HG12   1 
ATOM   6543 H HG13   . VAL   B 1 174 ? 14.95200  23.54300  -26.79300 1.000 38.99000  ? 140 VAL   B HG13   1 
ATOM   6544 H HG21   . VAL   B 1 174 ? 15.93600  22.35800  -29.54800 1.000 50.87000  ? 140 VAL   B HG21   1 
ATOM   6545 H HG22   . VAL   B 1 174 ? 15.65700  21.42300  -28.29400 1.000 50.87000  ? 140 VAL   B HG22   1 
ATOM   6546 H HG23   . VAL   B 1 174 ? 14.84200  21.20900  -29.64100 1.000 50.87000  ? 140 VAL   B HG23   1 
ATOM   6547 N N      . ALA   B 1 175 ? 11.34300  23.78000  -27.55300 1.000 35.69000  ? 141 ALA   B N      1 
ATOM   6548 C CA     . ALA   B 1 175 ? 10.58400  24.72600  -26.75200 1.000 40.88000  ? 141 ALA   B CA     1 
ATOM   6549 C C      . ALA   B 1 175 ? 9.58500   24.04600  -25.81300 1.000 37.03000  ? 141 ALA   B C      1 
ATOM   6550 O O      . ALA   B 1 175 ? 8.89100   24.75200  -25.07900 1.000 39.13000  ? 141 ALA   B O      1 
ATOM   6551 C CB     . ALA   B 1 175 ? 9.87500   25.73500  -27.66300 1.000 40.79000  ? 141 ALA   B CB     1 
ATOM   6552 H H      . ALA   B 1 175 ? 11.14300  23.75200  -28.38900 1.000 35.69000  ? 141 ALA   B H      1 
ATOM   6553 H HA     . ALA   B 1 175 ? 11.20600  25.22500  -26.19900 1.000 40.88000  ? 141 ALA   B HA     1 
ATOM   6554 H HB1    . ALA   B 1 175 ? 9.27100   26.27600  -27.13100 1.000 40.79000  ? 141 ALA   B HB1    1 
ATOM   6555 H HB2    . ALA   B 1 175 ? 10.53800  26.29700  -28.09300 1.000 40.79000  ? 141 ALA   B HB2    1 
ATOM   6556 H HB3    . ALA   B 1 175 ? 9.38200   25.23700  -28.32500 1.000 40.79000  ? 141 ALA   B HB3    1 
ATOM   6557 N N      . TYR   B 1 176 ? 9.47800   22.71300  -25.80100 1.000 40.48000  ? 142 TYR   B N      1 
ATOM   6558 C CA     . TYR   B 1 176 ? 8.71000   22.05800  -24.74800 1.000 39.77000  ? 142 TYR   B CA     1 
ATOM   6559 C C      . TYR   B 1 176 ? 9.54900   21.76600  -23.50800 1.000 46.26000  ? 142 TYR   B C      1 
ATOM   6560 O O      . TYR   B 1 176 ? 9.06800   21.09800  -22.59200 1.000 44.89000  ? 142 TYR   B O      1 
ATOM   6561 C CB     . TYR   B 1 176 ? 8.07100   20.76500  -25.26300 1.000 42.47000  ? 142 TYR   B CB     1 
ATOM   6562 C CG     . TYR   B 1 176 ? 6.84000   20.98300  -26.12700 1.000 37.92000  ? 142 TYR   B CG     1 
ATOM   6563 C CD1    . TYR   B 1 176 ? 6.21700   22.22900  -26.20100 1.000 32.46000  ? 142 TYR   B CD1    1 
ATOM   6564 C CD2    . TYR   B 1 176 ? 6.29900   19.94200  -26.86300 1.000 39.54000  ? 142 TYR   B CD2    1 
ATOM   6565 C CE1    . TYR   B 1 176 ? 5.09300   22.42300  -27.00100 1.000 34.20000  ? 142 TYR   B CE1    1 
ATOM   6566 C CE2    . TYR   B 1 176 ? 5.17800   20.12500  -27.66600 1.000 43.18000  ? 142 TYR   B CE2    1 
ATOM   6567 C CZ     . TYR   B 1 176 ? 4.57900   21.36700  -27.73200 1.000 36.70000  ? 142 TYR   B CZ     1 
ATOM   6568 O OH     . TYR   B 1 176 ? 3.44500   21.51500  -28.53100 1.000 30.30000  ? 142 TYR   B OH     1 
ATOM   6569 H H      . TYR   B 1 176 ? 9.83100   22.18100  -26.37700 1.000 40.48000  ? 142 TYR   B H      1 
ATOM   6570 H HA     . TYR   B 1 176 ? 8.01000   22.65500  -24.44900 1.000 39.77000  ? 142 TYR   B HA     1 
ATOM   6571 H HB2    . TYR   B 1 176 ? 8.72400   20.28500  -25.79500 1.000 42.47000  ? 142 TYR   B HB2    1 
ATOM   6572 H HB3    . TYR   B 1 176 ? 7.80600   20.22300  -24.50400 1.000 42.47000  ? 142 TYR   B HB3    1 
ATOM   6573 H HD1    . TYR   B 1 176 ? 6.55600   22.94800  -25.72100 1.000 32.46000  ? 142 TYR   B HD1    1 
ATOM   6574 H HD2    . TYR   B 1 176 ? 6.70100   19.10400  -26.82800 1.000 39.54000  ? 142 TYR   B HD2    1 
ATOM   6575 H HE1    . TYR   B 1 176 ? 4.68800   23.25900  -27.04100 1.000 34.20000  ? 142 TYR   B HE1    1 
ATOM   6576 H HE2    . TYR   B 1 176 ? 4.83000   19.41200  -28.15200 1.000 43.18000  ? 142 TYR   B HE2    1 
ATOM   6577 H HH     . TYR   B 1 176 ? 3.17100   22.30800  -28.49600 1.000 30.30000  ? 142 TYR   B HH     1 
ATOM   6578 N N      . ASP   B 1 177 ? 10.78300  22.25300  -23.46100 1.000 40.37000  ? 143 ASP   B N      1 
ATOM   6579 C CA     . ASP   B 1 177 ? 11.69800  22.06500  -22.33500 1.000 41.81000  ? 143 ASP   B CA     1 
ATOM   6580 C C      . ASP   B 1 177 ? 12.29600  23.43900  -22.04500 1.000 36.40000  ? 143 ASP   B C      1 
ATOM   6581 O O      . ASP   B 1 177 ? 13.22500  23.86600  -22.73500 1.000 39.30000  ? 143 ASP   B O      1 
ATOM   6582 C CB     . ASP   B 1 177 ? 12.76700  21.03100  -22.69100 1.000 43.67000  ? 143 ASP   B CB     1 
ATOM   6583 C CG     . ASP   B 1 177 ? 13.85000  20.88400  -21.62000 1.000 53.52000  ? 143 ASP   B CG     1 
ATOM   6584 O OD1    . ASP   B 1 177 ? 13.90000  21.68700  -20.67000 1.000 47.34000  ? 143 ASP   B OD1    1 
ATOM   6585 O OD2    . ASP   B 1 177 ? 14.65900  19.94000  -21.74100 1.000 58.48000  ? 143 ASP   B OD2    1 
ATOM   6586 H H      . ASP   B 1 177 ? 11.13100  22.71700  -24.09600 1.000 40.37000  ? 143 ASP   B H      1 
ATOM   6587 H HA     . ASP   B 1 177 ? 11.21000  21.76100  -21.55400 1.000 41.81000  ? 143 ASP   B HA     1 
ATOM   6588 H HB2    . ASP   B 1 177 ? 12.34200  20.16700  -22.80500 1.000 43.67000  ? 143 ASP   B HB2    1 
ATOM   6589 H HB3    . ASP   B 1 177 ? 13.19900  21.29800  -23.51700 1.000 43.67000  ? 143 ASP   B HB3    1 
ATOM   6590 N N      . PHE   B 1 178 ? 11.74800  24.15800  -21.05500 1.000 39.99000  ? 144 PHE   B N      1 
ATOM   6591 C CA     . PHE   B 1 178 ? 12.08600  25.57700  -20.93400 1.000 40.86000  ? 144 PHE   B CA     1 
ATOM   6592 C C      . PHE   B 1 178 ? 13.54400  25.79300  -20.57000 1.000 43.54000  ? 144 PHE   B C      1 
ATOM   6593 O O      . PHE   B 1 178 ? 14.11300  26.81900  -20.94600 1.000 37.64000  ? 144 PHE   B O      1 
ATOM   6594 C CB     . PHE   B 1 178 ? 11.15200  26.27000  -19.94300 1.000 44.85000  ? 144 PHE   B CB     1 
ATOM   6595 C CG     . PHE   B 1 178 ? 9.76600   26.40700  -20.46700 1.000 41.57000  ? 144 PHE   B CG     1 
ATOM   6596 C CD1    . PHE   B 1 178 ? 9.55200   26.91200  -21.74000 1.000 43.11000  ? 144 PHE   B CD1    1 
ATOM   6597 C CD2    . PHE   B 1 178 ? 8.68100   25.96300  -19.73400 1.000 43.45000  ? 144 PHE   B CD2    1 
ATOM   6598 C CE1    . PHE   B 1 178 ? 8.27500   27.01000  -22.25000 1.000 46.76000  ? 144 PHE   B CE1    1 
ATOM   6599 C CE2    . PHE   B 1 178 ? 7.40000   26.05300  -20.24200 1.000 49.19000  ? 144 PHE   B CE2    1 
ATOM   6600 C CZ     . PHE   B 1 178 ? 7.19500   26.57700  -21.50500 1.000 41.60000  ? 144 PHE   B CZ     1 
ATOM   6601 H H      . PHE   B 1 178 ? 11.19900  23.85900  -20.46400 1.000 39.99000  ? 144 PHE   B H      1 
ATOM   6602 H HA     . PHE   B 1 178 ? 11.96300  25.98800  -21.80200 1.000 40.86000  ? 144 PHE   B HA     1 
ATOM   6603 H HB2    . PHE   B 1 178 ? 11.11300  25.74600  -19.12800 1.000 44.85000  ? 144 PHE   B HB2    1 
ATOM   6604 H HB3    . PHE   B 1 178 ? 11.49400  27.15400  -19.75000 1.000 44.85000  ? 144 PHE   B HB3    1 
ATOM   6605 H HD1    . PHE   B 1 178 ? 10.27400  27.20300  -22.24800 1.000 43.11000  ? 144 PHE   B HD1    1 
ATOM   6606 H HD2    . PHE   B 1 178 ? 8.81500   25.60700  -18.88500 1.000 43.45000  ? 144 PHE   B HD2    1 
ATOM   6607 H HE1    . PHE   B 1 178 ? 8.14100   27.36300  -23.10000 1.000 46.76000  ? 144 PHE   B HE1    1 
ATOM   6608 H HE2    . PHE   B 1 178 ? 6.67600   25.76500  -19.73400 1.000 49.19000  ? 144 PHE   B HE2    1 
ATOM   6609 H HZ     . PHE   B 1 178 ? 6.33300   26.64800  -21.84700 1.000 41.60000  ? 144 PHE   B HZ     1 
ATOM   6610 N N      . ASP   B 1 179 ? 14.17900  24.83200  -19.89000 1.000 48.27000  ? 145 ASP   B N      1 
ATOM   6611 C CA     . ASP   B 1 179 ? 15.61300  24.95300  -19.63500 1.000 42.42000  ? 145 ASP   B CA     1 
ATOM   6612 C C      . ASP   B 1 179 ? 16.42000  24.88900  -20.92900 1.000 44.85000  ? 145 ASP   B C      1 
ATOM   6613 O O      . ASP   B 1 179 ? 17.38200  25.64800  -21.10600 1.000 43.13000  ? 145 ASP   B O      1 
ATOM   6614 C CB     . ASP   B 1 179 ? 16.08600  23.85500  -18.67300 1.000 47.40000  ? 145 ASP   B CB     1 
ATOM   6615 C CG     . ASP   B 1 179 ? 15.42900  23.93900  -17.30000 1.000 67.78000  ? 145 ASP   B CG     1 
ATOM   6616 O OD1    . ASP   B 1 179 ? 14.97300  25.03600  -16.90100 1.000 66.41000  ? 145 ASP   B OD1    1 
ATOM   6617 O OD2    . ASP   B 1 179 ? 15.35900  22.89200  -16.62100 1.000 75.22000  ? 145 ASP   B OD2    1 
ATOM   6618 H H      . ASP   B 1 179 ? 13.81200  24.12100  -19.57500 1.000 48.27000  ? 145 ASP   B H      1 
ATOM   6619 H HA     . ASP   B 1 179 ? 15.78700  25.81100  -19.21700 1.000 42.42000  ? 145 ASP   B HA     1 
ATOM   6620 H HB2    . ASP   B 1 179 ? 15.87200  22.98900  -19.05400 1.000 47.40000  ? 145 ASP   B HB2    1 
ATOM   6621 H HB3    . ASP   B 1 179 ? 17.04500  23.93500  -18.55100 1.000 47.40000  ? 145 ASP   B HB3    1 
ATOM   6622 N N      . ALA   B 1 180 ? 16.08500  23.95500  -21.82800 1.000 41.64000  ? 146 ALA   B N      1 
ATOM   6623 C CA     . ALA   B 1 180 ? 16.78800  23.90600  -23.10800 1.000 41.79000  ? 146 ALA   B CA     1 
ATOM   6624 C C      . ALA   B 1 180 ? 16.46900  25.14100  -23.94800 1.000 42.82000  ? 146 ALA   B C      1 
ATOM   6625 O O      . ALA   B 1 180 ? 17.35700  25.70600  -24.59800 1.000 44.12000  ? 146 ALA   B O      1 
ATOM   6626 C CB     . ALA   B 1 180 ? 16.42300  22.63300  -23.87100 1.000 45.83000  ? 146 ALA   B CB     1 
ATOM   6627 H H      . ALA   B 1 180 ? 15.47400  23.35900  -21.72300 1.000 41.64000  ? 146 ALA   B H      1 
ATOM   6628 H HA     . ALA   B 1 180 ? 17.74400  23.89400  -22.94300 1.000 41.79000  ? 146 ALA   B HA     1 
ATOM   6629 H HB1    . ALA   B 1 180 ? 16.90100  22.62300  -24.71500 1.000 45.83000  ? 146 ALA   B HB1    1 
ATOM   6630 H HB2    . ALA   B 1 180 ? 16.67600  21.86300  -23.33800 1.000 45.83000  ? 146 ALA   B HB2    1 
ATOM   6631 H HB3    . ALA   B 1 180 ? 15.46600  22.62500  -24.03200 1.000 45.83000  ? 146 ALA   B HB3    1 
ATOM   6632 N N      . MET   B 1 181 ? 15.20700  25.57600  -23.95000 1.000 39.42000  ? 147 MET   B N      1 
ATOM   6633 C CA     . MET   B 1 181 ? 14.87100  26.77000  -24.71900 1.000 36.11000  ? 147 MET   B CA     1 
ATOM   6634 C C      . MET   B 1 181 ? 15.75400  27.93600  -24.30000 1.000 35.62000  ? 147 MET   B C      1 
ATOM   6635 O O      . MET   B 1 181 ? 16.37800  28.59100  -25.14100 1.000 39.88000  ? 147 MET   B O      1 
ATOM   6636 C CB     . MET   B 1 181 ? 13.39500  27.11600  -24.55200 1.000 38.17000  ? 147 MET   B CB     1 
ATOM   6637 C CG     . MET   B 1 181 ? 12.97400  28.36700  -25.32200 1.000 40.72000  ? 147 MET   B CG     1 
ATOM   6638 S SD     . MET   B 1 181 ? 11.27600  28.72500  -24.87600 1.000 48.71000  ? 147 MET   B SD     1 
ATOM   6639 C CE     . MET   B 1 181 ? 11.07700  30.36300  -25.62300 1.000 46.22000  ? 147 MET   B CE     1 
ATOM   6640 H H      . MET   B 1 181 ? 14.55100  25.21200  -23.53000 1.000 39.42000  ? 147 MET   B H      1 
ATOM   6641 H HA     . MET   B 1 181 ? 15.02500  26.58700  -25.65900 1.000 36.11000  ? 147 MET   B HA     1 
ATOM   6642 H HB2    . MET   B 1 181 ? 12.86000  26.37400  -24.87400 1.000 38.17000  ? 147 MET   B HB2    1 
ATOM   6643 H HB3    . MET   B 1 181 ? 13.21300  27.27000  -23.61200 1.000 38.17000  ? 147 MET   B HB3    1 
ATOM   6644 H HG2    . MET   B 1 181 ? 13.52700  29.12300  -25.07100 1.000 40.72000  ? 147 MET   B HG2    1 
ATOM   6645 H HG3    . MET   B 1 181 ? 13.02200  28.20200  -26.27700 1.000 40.72000  ? 147 MET   B HG3    1 
ATOM   6646 H HE1    . MET   B 1 181 ? 10.17000  30.67100  -25.46900 1.000 46.22000  ? 147 MET   B HE1    1 
ATOM   6647 H HE2    . MET   B 1 181 ? 11.70900  30.97500  -25.21500 1.000 46.22000  ? 147 MET   B HE2    1 
ATOM   6648 H HE3    . MET   B 1 181 ? 11.24700  30.29800  -26.57600 1.000 46.22000  ? 147 MET   B HE3    1 
ATOM   6649 N N      . ARG   B 1 182 ? 15.83500  28.20000  -22.99300 1.000 38.08000  ? 148 ARG   B N      1 
ATOM   6650 C CA     . ARG   B 1 182 ? 16.70000  29.27700  -22.51400 1.000 42.30000  ? 148 ARG   B CA     1 
ATOM   6651 C C      . ARG   B 1 182 ? 18.14800  29.06200  -22.93000 1.000 44.13000  ? 148 ARG   B C      1 
ATOM   6652 O O      . ARG   B 1 182 ? 18.85400  30.01900  -23.27200 1.000 39.98000  ? 148 ARG   B O      1 
ATOM   6653 C CB     . ARG   B 1 182 ? 16.61100  29.39800  -20.99000 1.000 43.47000  ? 148 ARG   B CB     1 
ATOM   6654 C CG     . ARG   B 1 182 ? 17.51600  30.49900  -20.44600 1.000 49.54000  ? 148 ARG   B CG     1 
ATOM   6655 C CD     . ARG   B 1 182 ? 17.52700  30.54400  -18.93200 1.000 52.16000  ? 148 ARG   B CD     1 
ATOM   6656 N NE     . ARG   B 1 182 ? 16.19900  30.81900  -18.39900 1.000 64.14000  ? 148 ARG   B NE     1 
ATOM   6657 C CZ     . ARG   B 1 182 ? 15.65600  32.03000  -18.34000 1.000 72.07000  ? 148 ARG   B CZ     1 
ATOM   6658 N NH1    . ARG   B 1 182 ? 16.29200  33.09900  -18.80000 1.000 67.86000  ? 148 ARG   B NH1    1 
ATOM   6659 N NH2    . ARG   B 1 182 ? 14.44500  32.17400  -17.81100 1.000 66.14000  ? 148 ARG   B NH2    1 
ATOM   6660 H H      . ARG   B 1 182 ? 15.40800  27.77900  -22.37600 1.000 38.08000  ? 148 ARG   B H      1 
ATOM   6661 H HA     . ARG   B 1 182 ? 16.40000  30.11600  -22.89800 1.000 42.30000  ? 148 ARG   B HA     1 
ATOM   6662 H HB2    . ARG   B 1 182 ? 15.69700  29.60700  -20.74100 1.000 43.47000  ? 148 ARG   B HB2    1 
ATOM   6663 H HB3    . ARG   B 1 182 ? 16.88200  28.55800  -20.58800 1.000 43.47000  ? 148 ARG   B HB3    1 
ATOM   6664 H HG2    . ARG   B 1 182 ? 18.42800  30.34900  -20.73600 1.000 49.54000  ? 148 ARG   B HG2    1 
ATOM   6665 H HG3    . ARG   B 1 182 ? 17.20100  31.35700  -20.77000 1.000 49.54000  ? 148 ARG   B HG3    1 
ATOM   6666 H HD2    . ARG   B 1 182 ? 17.81900  29.68500  -18.58900 1.000 52.16000  ? 148 ARG   B HD2    1 
ATOM   6667 H HD3    . ARG   B 1 182 ? 18.12800  31.24500  -18.63500 1.000 52.16000  ? 148 ARG   B HD3    1 
ATOM   6668 H HE     . ARG   B 1 182 ? 15.75700  30.16300  -18.06200 1.000 64.14000  ? 148 ARG   B HE     1 
ATOM   6669 H HH11   . ARG   B 1 182 ? 17.07600  33.02200  -19.14500 1.000 67.86000  ? 148 ARG   B HH11   1 
ATOM   6670 H HH12   . ARG   B 1 182 ? 15.92000  33.87300  -18.75200 1.000 67.86000  ? 148 ARG   B HH12   1 
ATOM   6671 H HH21   . ARG   B 1 182 ? 14.02300  31.48800  -17.51100 1.000 66.14000  ? 148 ARG   B HH21   1 
ATOM   6672 H HH22   . ARG   B 1 182 ? 14.08400  32.95300  -17.77000 1.000 66.14000  ? 148 ARG   B HH22   1 
ATOM   6673 N N      . ARG   B 1 183 ? 18.62700  27.81800  -22.86400 1.000 40.63000  ? 149 ARG   B N      1 
ATOM   6674 C CA     . ARG   B 1 183 ? 20.01200  27.54900  -23.23800 1.000 43.47000  ? 149 ARG   B CA     1 
ATOM   6675 C C      . ARG   B 1 183 ? 20.26700  27.85400  -24.71100 1.000 45.93000  ? 149 ARG   B C      1 
ATOM   6676 O O      . ARG   B 1 183 ? 21.28900  28.46100  -25.05600 1.000 41.40000  ? 149 ARG   B O      1 
ATOM   6677 C CB     . ARG   B 1 183 ? 20.35300  26.09500  -22.91400 1.000 47.67000  ? 149 ARG   B CB     1 
ATOM   6678 C CG     . ARG   B 1 183 ? 21.79800  25.73500  -23.11400 1.000 60.95000  ? 149 ARG   B CG     1 
ATOM   6679 C CD     . ARG   B 1 183 ? 22.18700  24.56700  -22.18900 1.000 60.87000  ? 149 ARG   B CD     1 
ATOM   6680 N NE     . ARG   B 1 183 ? 21.20300  23.48900  -22.20800 1.000 60.48000  ? 149 ARG   B NE     1 
ATOM   6681 C CZ     . ARG   B 1 183 ? 21.01900  22.68000  -23.24200 1.000 66.41000  ? 149 ARG   B CZ     1 
ATOM   6682 N NH1    . ARG   B 1 183 ? 21.72100  22.82100  -24.35300 1.000 59.21000  ? 149 ARG   B NH1    1 
ATOM   6683 N NH2    . ARG   B 1 183 ? 20.10600  21.71400  -23.16000 1.000 56.02000  ? 149 ARG   B NH2    1 
ATOM   6684 H H      . ARG   B 1 183 ? 18.18000  27.12800  -22.61100 1.000 40.63000  ? 149 ARG   B H      1 
ATOM   6685 H HA     . ARG   B 1 183 ? 20.59600  28.11700  -22.71100 1.000 43.47000  ? 149 ARG   B HA     1 
ATOM   6686 H HB2    . ARG   B 1 183 ? 20.13300  25.92500  -21.98500 1.000 47.67000  ? 149 ARG   B HB2    1 
ATOM   6687 H HB3    . ARG   B 1 183 ? 19.82400  25.51700  -23.48600 1.000 47.67000  ? 149 ARG   B HB3    1 
ATOM   6688 H HG2    . ARG   B 1 183 ? 21.94800  25.47200  -24.03500 1.000 60.95000  ? 149 ARG   B HG2    1 
ATOM   6689 H HG3    . ARG   B 1 183 ? 22.34900  26.49400  -22.87900 1.000 60.95000  ? 149 ARG   B HG3    1 
ATOM   6690 H HD2    . ARG   B 1 183 ? 23.03800  24.20300  -22.47900 1.000 60.87000  ? 149 ARG   B HD2    1 
ATOM   6691 H HD3    . ARG   B 1 183 ? 22.25700  24.89400  -21.27800 1.000 60.87000  ? 149 ARG   B HD3    1 
ATOM   6692 H HE     . ARG   B 1 183 ? 20.79700  23.30200  -21.47300 1.000 60.48000  ? 149 ARG   B HE     1 
ATOM   6693 H HH11   . ARG   B 1 183 ? 22.32000  23.43200  -24.43600 1.000 59.21000  ? 149 ARG   B HH11   1 
ATOM   6694 H HH12   . ARG   B 1 183 ? 21.56500  22.27600  -24.96800 1.000 59.21000  ? 149 ARG   B HH12   1 
ATOM   6695 H HH21   . ARG   B 1 183 ? 19.64900  21.62300  -22.43700 1.000 56.02000  ? 149 ARG   B HH21   1 
ATOM   6696 H HH22   . ARG   B 1 183 ? 19.97300  21.18000  -23.81100 1.000 56.02000  ? 149 ARG   B HH22   1 
ATOM   6697 N N      . TYR   B 1 184 ? 19.35000  27.44100  -25.59600 1.000 40.48000  ? 150 TYR   B N      1 
ATOM   6698 C CA     . TYR   B 1 184 ? 19.49500  27.75900  -27.01700 1.000 38.26000  ? 150 TYR   B CA     1 
ATOM   6699 C C      . TYR   B 1 184 ? 19.53100  29.26300  -27.25300 1.000 40.64000  ? 150 TYR   B C      1 
ATOM   6700 O O      . TYR   B 1 184 ? 20.37800  29.76300  -27.99600 1.000 37.61000  ? 150 TYR   B O      1 
ATOM   6701 C CB     . TYR   B 1 184 ? 18.35200  27.14600  -27.81600 1.000 37.46000  ? 150 TYR   B CB     1 
ATOM   6702 C CG     . TYR   B 1 184 ? 18.55700  25.71500  -28.22600 1.000 41.41000  ? 150 TYR   B CG     1 
ATOM   6703 C CD1    . TYR   B 1 184 ? 18.82800  24.73300  -27.28200 1.000 42.29000  ? 150 TYR   B CD1    1 
ATOM   6704 C CD2    . TYR   B 1 184 ? 18.44700  25.33700  -29.55900 1.000 47.40000  ? 150 TYR   B CD2    1 
ATOM   6705 C CE1    . TYR   B 1 184 ? 18.99600  23.40200  -27.66000 1.000 47.49000  ? 150 TYR   B CE1    1 
ATOM   6706 C CE2    . TYR   B 1 184 ? 18.61400  24.01600  -29.94700 1.000 41.71000  ? 150 TYR   B CE2    1 
ATOM   6707 C CZ     . TYR   B 1 184 ? 18.88300  23.05200  -28.99600 1.000 49.63000  ? 150 TYR   B CZ     1 
ATOM   6708 O OH     . TYR   B 1 184 ? 19.04800  21.73600  -29.39600 1.000 52.14000  ? 150 TYR   B OH     1 
ATOM   6709 H H      . TYR   B 1 184 ? 18.64800  26.98400  -25.40100 1.000 40.48000  ? 150 TYR   B H      1 
ATOM   6710 H HA     . TYR   B 1 184 ? 20.32700  27.38200  -27.34300 1.000 38.26000  ? 150 TYR   B HA     1 
ATOM   6711 H HB2    . TYR   B 1 184 ? 17.54500  27.18300  -27.27900 1.000 37.46000  ? 150 TYR   B HB2    1 
ATOM   6712 H HB3    . TYR   B 1 184 ? 18.22800  27.66700  -28.62500 1.000 37.46000  ? 150 TYR   B HB3    1 
ATOM   6713 H HD1    . TYR   B 1 184 ? 18.89800  24.96700  -26.38500 1.000 42.29000  ? 150 TYR   B HD1    1 
ATOM   6714 H HD2    . TYR   B 1 184 ? 18.26000  25.98200  -30.20300 1.000 47.40000  ? 150 TYR   B HD2    1 
ATOM   6715 H HE1    . TYR   B 1 184 ? 19.18000  22.75300  -27.02000 1.000 47.49000  ? 150 TYR   B HE1    1 
ATOM   6716 H HE2    . TYR   B 1 184 ? 18.53900  23.78000  -30.84300 1.000 41.71000  ? 150 TYR   B HE2    1 
ATOM   6717 H HH     . TYR   B 1 184 ? 19.21300  21.25200  -28.73000 1.000 52.14000  ? 150 TYR   B HH     1 
ATOM   6718 N N      . LEU   B 1 185 ? 18.59700  29.99900  -26.64800 1.000 37.59000  ? 151 LEU   B N      1 
ATOM   6719 C CA     . LEU   B 1 185 ? 18.52800  31.43600  -26.90800 1.000 36.83000  ? 151 LEU   B CA     1 
ATOM   6720 C C      . LEU   B 1 185 ? 19.77600  32.14800  -26.40200 1.000 36.22000  ? 151 LEU   B C      1 
ATOM   6721 O O      . LEU   B 1 185 ? 20.27300  33.08500  -27.04100 1.000 35.23000  ? 151 LEU   B O      1 
ATOM   6722 C CB     . LEU   B 1 185 ? 17.26900  32.02500  -26.26900 1.000 33.43000  ? 151 LEU   B CB     1 
ATOM   6723 C CG     . LEU   B 1 185 ? 15.96200  31.47400  -26.86700 1.000 36.02000  ? 151 LEU   B CG     1 
ATOM   6724 C CD1    . LEU   B 1 185 ? 14.75800  31.98300  -26.08300 1.000 34.62000  ? 151 LEU   B CD1    1 
ATOM   6725 C CD2    . LEU   B 1 185 ? 15.86400  31.85700  -28.34700 1.000 36.31000  ? 151 LEU   B CD2    1 
ATOM   6726 H H      . LEU   B 1 185 ? 18.00700  29.70000  -26.09800 1.000 37.59000  ? 151 LEU   B H      1 
ATOM   6727 H HA     . LEU   B 1 185 ? 18.47900  31.57900  -27.86500 1.000 36.83000  ? 151 LEU   B HA     1 
ATOM   6728 H HB2    . LEU   B 1 185 ? 17.27300  31.81900  -25.32100 1.000 33.43000  ? 151 LEU   B HB2    1 
ATOM   6729 H HB3    . LEU   B 1 185 ? 17.27300  32.98600  -26.39700 1.000 33.43000  ? 151 LEU   B HB3    1 
ATOM   6730 H HG     . LEU   B 1 185 ? 15.97100  30.50600  -26.80800 1.000 36.02000  ? 151 LEU   B HG     1 
ATOM   6731 H HD11   . LEU   B 1 185 ? 13.94900  31.62200  -26.47800 1.000 34.62000  ? 151 LEU   B HD11   1 
ATOM   6732 H HD12   . LEU   B 1 185 ? 14.83600  31.69100  -25.16100 1.000 34.62000  ? 151 LEU   B HD12   1 
ATOM   6733 H HD13   . LEU   B 1 185 ? 14.74200  32.95200  -26.12300 1.000 34.62000  ? 151 LEU   B HD13   1 
ATOM   6734 H HD21   . LEU   B 1 185 ? 14.96100  31.68600  -28.65600 1.000 36.31000  ? 151 LEU   B HD21   1 
ATOM   6735 H HD22   . LEU   B 1 185 ? 16.07500  32.79900  -28.44400 1.000 36.31000  ? 151 LEU   B HD22   1 
ATOM   6736 H HD23   . LEU   B 1 185 ? 16.49400  31.32300  -28.85600 1.000 36.31000  ? 151 LEU   B HD23   1 
ATOM   6737 N N      . ALA   B 1 186 ? 20.27700  31.73200  -25.23200 1.000 39.61000  ? 152 ALA   B N      1 
ATOM   6738 C CA     . ALA   B 1 186 ? 21.53100  32.26900  -24.71800 1.000 43.18000  ? 152 ALA   B CA     1 
ATOM   6739 C C      . ALA   B 1 186 ? 22.68500  31.99600  -25.67400 1.000 42.29000  ? 152 ALA   B C      1 
ATOM   6740 O O      . ALA   B 1 186 ? 23.50600  32.88100  -25.93300 1.000 38.63000  ? 152 ALA   B O      1 
ATOM   6741 C CB     . ALA   B 1 186 ? 21.82600  31.66200  -23.34300 1.000 39.61000  ? 152 ALA   B CB     1 
ATOM   6742 H H      . ALA   B 1 186 ? 19.90900  31.14400  -24.72400 1.000 39.61000  ? 152 ALA   B H      1 
ATOM   6743 H HA     . ALA   B 1 186 ? 21.44700  33.23000  -24.61300 1.000 43.18000  ? 152 ALA   B HA     1 
ATOM   6744 H HB1    . ALA   B 1 186 ? 22.66200  32.02600  -23.01000 1.000 39.61000  ? 152 ALA   B HB1    1 
ATOM   6745 H HB2    . ALA   B 1 186 ? 21.10300  31.88700  -22.73700 1.000 39.61000  ? 152 ALA   B HB2    1 
ATOM   6746 H HB3    . ALA   B 1 186 ? 21.89600  30.69900  -23.43200 1.000 39.61000  ? 152 ALA   B HB3    1 
ATOM   6747 N N      . ALA   B 1 187 ? 22.76600  30.76800  -26.20500 1.000 40.98000  ? 153 ALA   B N      1 
ATOM   6748 C CA     . ALA   B 1 187 ? 23.86900  30.40900  -27.09200 1.000 42.23000  ? 153 ALA   B CA     1 
ATOM   6749 C C      . ALA   B 1 187 ? 23.79100  31.17700  -28.40900 1.000 38.86000  ? 153 ALA   B C      1 
ATOM   6750 O O      . ALA   B 1 187 ? 24.79700  31.72300  -28.88500 1.000 36.47000  ? 153 ALA   B O      1 
ATOM   6751 C CB     . ALA   B 1 187 ? 23.87400  28.89500  -27.32900 1.000 41.47000  ? 153 ALA   B CB     1 
ATOM   6752 H H      . ALA   B 1 187 ? 22.20000  30.13600  -26.06600 1.000 40.98000  ? 153 ALA   B H      1 
ATOM   6753 H HA     . ALA   B 1 187 ? 24.70600  30.64400  -26.66100 1.000 42.23000  ? 153 ALA   B HA     1 
ATOM   6754 H HB1    . ALA   B 1 187 ? 24.61100  28.67100  -27.91900 1.000 41.47000  ? 153 ALA   B HB1    1 
ATOM   6755 H HB2    . ALA   B 1 187 ? 23.98200  28.44300  -26.47800 1.000 41.47000  ? 153 ALA   B HB2    1 
ATOM   6756 H HB3    . ALA   B 1 187 ? 23.03300  28.63700  -27.73700 1.000 41.47000  ? 153 ALA   B HB3    1 
ATOM   6757 N N      . ILE   B 1 188 ? 22.59800  31.25200  -29.00500 1.000 38.45000  ? 154 ILE   B N      1 
ATOM   6758 C CA     . ILE   B 1 188 ? 22.44900  32.03100  -30.23400 1.000 38.99000  ? 154 ILE   B CA     1 
ATOM   6759 C C      . ILE   B 1 188 ? 22.75500  33.50200  -29.97100 1.000 37.34000  ? 154 ILE   B C      1 
ATOM   6760 O O      . ILE   B 1 188 ? 23.48700  34.15300  -30.73300 1.000 36.87000  ? 154 ILE   B O      1 
ATOM   6761 C CB     . ILE   B 1 188 ? 21.04200  31.84300  -30.83300 1.000 35.62000  ? 154 ILE   B CB     1 
ATOM   6762 C CG1    . ILE   B 1 188 ? 20.81300  30.38400  -31.22900 1.000 42.98000  ? 154 ILE   B CG1    1 
ATOM   6763 C CG2    . ILE   B 1 188 ? 20.86900  32.71900  -32.04400 1.000 35.75000  ? 154 ILE   B CG2    1 
ATOM   6764 C CD1    . ILE   B 1 188 ? 22.02800  29.72700  -31.84200 1.000 44.03000  ? 154 ILE   B CD1    1 
ATOM   6765 H H      . ILE   B 1 188 ? 21.87900  30.87200  -28.72600 1.000 38.45000  ? 154 ILE   B H      1 
ATOM   6766 H HA     . ILE   B 1 188 ? 23.11000  31.73900  -30.87800 1.000 38.99000  ? 154 ILE   B HA     1 
ATOM   6767 H HB     . ILE   B 1 188 ? 20.38200  32.09400  -30.16800 1.000 35.62000  ? 154 ILE   B HB     1 
ATOM   6768 H HG12   . ILE   B 1 188 ? 20.57300  29.87900  -30.43700 1.000 42.98000  ? 154 ILE   B HG12   1 
ATOM   6769 H HG13   . ILE   B 1 188 ? 20.09200  30.34000  -31.87700 1.000 42.98000  ? 154 ILE   B HG13   1 
ATOM   6770 H HG21   . ILE   B 1 188 ? 20.06500  32.45200  -32.51700 1.000 35.75000  ? 154 ILE   B HG21   1 
ATOM   6771 H HG22   . ILE   B 1 188 ? 20.78900  33.64300  -31.76100 1.000 35.75000  ? 154 ILE   B HG22   1 
ATOM   6772 H HG23   . ILE   B 1 188 ? 21.64100  32.61400  -32.62200 1.000 35.75000  ? 154 ILE   B HG23   1 
ATOM   6773 H HD11   . ILE   B 1 188 ? 21.77400  28.84700  -32.12900 1.000 44.03000  ? 154 ILE   B HD11   1 
ATOM   6774 H HD12   . ILE   B 1 188 ? 22.33300  30.25400  -32.59700 1.000 44.03000  ? 154 ILE   B HD12   1 
ATOM   6775 H HD13   . ILE   B 1 188 ? 22.73000  29.64800  -31.17800 1.000 44.03000  ? 154 ILE   B HD13   1 
ATOM   6776 N N      . SER   B 1 189 ? 22.19900  34.05700  -28.88600 1.000 37.84000  ? 155 SER   B N      1 
ATOM   6777 C CA     . SER   B 1 189 ? 22.40900  35.48400  -28.65100 1.000 38.63000  ? 155 SER   B CA     1 
ATOM   6778 C C      . SER   B 1 189 ? 23.87900  35.80600  -28.45800 1.000 41.69000  ? 155 SER   B C      1 
ATOM   6779 O O      . SER   B 1 189 ? 24.32200  36.89600  -28.82900 1.000 39.68000  ? 155 SER   B O      1 
ATOM   6780 C CB     . SER   B 1 189 ? 21.62400  35.97000  -27.43600 1.000 36.98000  ? 155 SER   B CB     1 
ATOM   6781 O OG     . SER   B 1 189 ? 20.23400  35.74900  -27.60100 1.000 39.70000  ? 155 SER   B OG     1 
ATOM   6782 H H      . SER   B 1 189 ? 21.72000  33.65000  -28.30000 1.000 37.84000  ? 155 SER   B H      1 
ATOM   6783 H HA     . SER   B 1 189 ? 22.09500  35.97800  -29.42500 1.000 38.63000  ? 155 SER   B HA     1 
ATOM   6784 H HB2    . SER   B 1 189 ? 21.92800  35.48700  -26.65100 1.000 36.98000  ? 155 SER   B HB2    1 
ATOM   6785 H HB3    . SER   B 1 189 ? 21.78000  36.92000  -27.32100 1.000 36.98000  ? 155 SER   B HB3    1 
ATOM   6786 H HG     . SER   B 1 189 ? 20.08300  34.92900  -27.70100 1.000 39.70000  ? 155 SER   B HG     1 
ATOM   6787 N N      . GLU   B 1 190 ? 24.64900  34.87900  -27.88200 1.000 41.71000  ? 156 GLU   B N      1 
ATOM   6788 C CA     . GLU   B 1 190 ? 26.08300  35.12000  -27.74800 1.000 41.56000  ? 156 GLU   B CA     1 
ATOM   6789 C C      . GLU   B 1 190 ? 26.78200  35.05000  -29.10000 1.000 50.53000  ? 156 GLU   B C      1 
ATOM   6790 O O      . GLU   B 1 190 ? 27.65800  35.87000  -29.39100 1.000 51.47000  ? 156 GLU   B O      1 
ATOM   6791 C CB     . GLU   B 1 190 ? 26.69500  34.12200  -26.76000 1.000 43.05000  ? 156 GLU   B CB     1 
ATOM   6792 H H      . GLU   B 1 190 ? 24.37400  34.12600  -27.57000 1.000 41.71000  ? 156 GLU   B H      1 
ATOM   6793 H HA     . GLU   B 1 190 ? 26.21800  36.01200  -27.39000 1.000 41.56000  ? 156 GLU   B HA     1 
ATOM   6794 N N      . ALA   B 1 191 ? 26.39100  34.09400  -29.95100 1.000 40.45000  ? 157 ALA   B N      1 
ATOM   6795 C CA     . ALA   B 1 191 ? 27.06500  33.87300  -31.22500 1.000 39.37000  ? 157 ALA   B CA     1 
ATOM   6796 C C      . ALA   B 1 191 ? 26.62500  34.81400  -32.34300 1.000 47.59000  ? 157 ALA   B C      1 
ATOM   6797 O O      . ALA   B 1 191 ? 27.37800  35.00800  -33.29900 1.000 49.69000  ? 157 ALA   B O      1 
ATOM   6798 C CB     . ALA   B 1 191 ? 26.82800  32.43400  -31.68700 1.000 44.44000  ? 157 ALA   B CB     1 
ATOM   6799 H H      . ALA   B 1 191 ? 25.73300  33.55900  -29.80800 1.000 40.45000  ? 157 ALA   B H      1 
ATOM   6800 H HA     . ALA   B 1 191 ? 28.01900  33.99100  -31.09700 1.000 39.37000  ? 157 ALA   B HA     1 
ATOM   6801 H HB1    . ALA   B 1 191 ? 27.27900  32.29700  -32.53500 1.000 44.44000  ? 157 ALA   B HB1    1 
ATOM   6802 H HB2    . ALA   B 1 191 ? 27.18400  31.82600  -31.02000 1.000 44.44000  ? 157 ALA   B HB2    1 
ATOM   6803 H HB3    . ALA   B 1 191 ? 25.87500  32.29000  -31.79200 1.000 44.44000  ? 157 ALA   B HB3    1 
ATOM   6804 N N      . TYR   B 1 192 ? 25.42400  35.37900  -32.27400 1.000 44.73000  ? 158 TYR   B N      1 
ATOM   6805 C CA     . TYR   B 1 192 ? 24.83100  36.08200  -33.41300 1.000 34.27000  ? 158 TYR   B CA     1 
ATOM   6806 C C      . TYR   B 1 192 ? 24.56500  37.53300  -33.04200 1.000 38.31000  ? 158 TYR   B C      1 
ATOM   6807 O O      . TYR   B 1 192 ? 23.84500  37.78600  -32.06100 1.000 39.75000  ? 158 TYR   B O      1 
ATOM   6808 C CB     . TYR   B 1 192 ? 23.53300  35.38100  -33.80900 1.000 35.66000  ? 158 TYR   B CB     1 
ATOM   6809 C CG     . TYR   B 1 192 ? 22.92600  35.79400  -35.12000 1.000 40.78000  ? 158 TYR   B CG     1 
ATOM   6810 C CD1    . TYR   B 1 192 ? 23.57100  35.52800  -36.31200 1.000 37.77000  ? 158 TYR   B CD1    1 
ATOM   6811 C CD2    . TYR   B 1 192 ? 21.66600  36.39000  -35.16200 1.000 38.97000  ? 158 TYR   B CD2    1 
ATOM   6812 C CE1    . TYR   B 1 192 ? 23.01100  35.88200  -37.51800 1.000 35.53000  ? 158 TYR   B CE1    1 
ATOM   6813 C CE2    . TYR   B 1 192 ? 21.09200  36.74600  -36.34700 1.000 32.01000  ? 158 TYR   B CE2    1 
ATOM   6814 C CZ     . TYR   B 1 192 ? 21.76700  36.47800  -37.53500 1.000 33.58000  ? 158 TYR   B CZ     1 
ATOM   6815 O OH     . TYR   B 1 192 ? 21.20600  36.81700  -38.72900 1.000 39.11000  ? 158 TYR   B OH     1 
ATOM   6816 H H      . TYR   B 1 192 ? 24.92600  35.37000  -31.57300 1.000 44.73000  ? 158 TYR   B H      1 
ATOM   6817 H HA     . TYR   B 1 192 ? 25.43500  36.03300  -34.16700 1.000 34.27000  ? 158 TYR   B HA     1 
ATOM   6818 H HB2    . TYR   B 1 192 ? 23.70200  34.42800  -33.85300 1.000 35.66000  ? 158 TYR   B HB2    1 
ATOM   6819 H HB3    . TYR   B 1 192 ? 22.87300  35.55700  -33.12000 1.000 35.66000  ? 158 TYR   B HB3    1 
ATOM   6820 H HD1    . TYR   B 1 192 ? 24.40800  35.12200  -36.29800 1.000 37.77000  ? 158 TYR   B HD1    1 
ATOM   6821 H HD2    . TYR   B 1 192 ? 21.21600  36.56300  -34.36700 1.000 38.97000  ? 158 TYR   B HD2    1 
ATOM   6822 H HE1    . TYR   B 1 192 ? 23.45800  35.70400  -38.31400 1.000 35.53000  ? 158 TYR   B HE1    1 
ATOM   6823 H HE2    . TYR   B 1 192 ? 20.25400  37.14900  -36.36200 1.000 32.01000  ? 158 TYR   B HE2    1 
ATOM   6824 H HH     . TYR   B 1 192 ? 21.72100  36.60800  -39.35800 1.000 39.11000  ? 158 TYR   B HH     1 
ATOM   6825 N N      . PRO   B 1 193 ? 25.09800  38.50600  -33.78700 1.000 36.41000  ? 159 PRO   B N      1 
ATOM   6826 C CA     . PRO   B 1 193 ? 24.95800  39.92000  -33.39300 1.000 41.41000  ? 159 PRO   B CA     1 
ATOM   6827 C C      . PRO   B 1 193 ? 23.63000  40.55700  -33.76300 1.000 43.71000  ? 159 PRO   B C      1 
ATOM   6828 O O      . PRO   B 1 193 ? 23.31500  41.63000  -33.23700 1.000 42.94000  ? 159 PRO   B O      1 
ATOM   6829 C CB     . PRO   B 1 193 ? 26.10400  40.60700  -34.15100 1.000 44.40000  ? 159 PRO   B CB     1 
ATOM   6830 C CG     . PRO   B 1 193 ? 26.35400  39.72400  -35.32400 1.000 41.74000  ? 159 PRO   B CG     1 
ATOM   6831 C CD     . PRO   B 1 193 ? 26.06900  38.32000  -34.87700 1.000 40.46000  ? 159 PRO   B CD     1 
ATOM   6832 H HA     . PRO   B 1 193 ? 25.10400  40.01800  -32.43900 1.000 41.41000  ? 159 PRO   B HA     1 
ATOM   6833 H HB2    . PRO   B 1 193 ? 25.82600  41.49100  -34.43700 1.000 44.40000  ? 159 PRO   B HB2    1 
ATOM   6834 H HB3    . PRO   B 1 193 ? 26.88900  40.65800  -33.58400 1.000 44.40000  ? 159 PRO   B HB3    1 
ATOM   6835 H HG2    . PRO   B 1 193 ? 25.76000  39.97500  -36.04900 1.000 41.74000  ? 159 PRO   B HG2    1 
ATOM   6836 H HG3    . PRO   B 1 193 ? 27.28000  39.81000  -35.60000 1.000 41.74000  ? 159 PRO   B HG3    1 
ATOM   6837 H HD2    . PRO   B 1 193 ? 25.67300  37.80900  -35.60000 1.000 40.46000  ? 159 PRO   B HD2    1 
ATOM   6838 H HD3    . PRO   B 1 193 ? 26.87700  37.90000  -34.54300 1.000 40.46000  ? 159 PRO   B HD3    1 
ATOM   6839 N N      . HIS   B 1 194 ? 22.84700  39.94200  -34.62700 1.000 40.57000  ? 160 HIS   B N      1 
ATOM   6840 C CA     . HIS   B 1 194 ? 21.66300  40.60500  -35.13800 1.000 34.68000  ? 160 HIS   B CA     1 
ATOM   6841 C C      . HIS   B 1 194 ? 20.40700  40.11000  -34.44900 1.000 34.48000  ? 160 HIS   B C      1 
ATOM   6842 O O      . HIS   B 1 194 ? 20.40000  39.05700  -33.80100 1.000 37.02000  ? 160 HIS   B O      1 
ATOM   6843 C CB     . HIS   B 1 194 ? 21.53300  40.36100  -36.63700 1.000 39.07000  ? 160 HIS   B CB     1 
ATOM   6844 C CG     . HIS   B 1 194 ? 22.81200  40.55800  -37.37900 1.000 42.06000  ? 160 HIS   B CG     1 
ATOM   6845 N ND1    . HIS   B 1 194 ? 23.42500  41.78600  -37.47900 1.000 42.40000  ? 160 HIS   B ND1    1 
ATOM   6846 C CD2    . HIS   B 1 194 ? 23.60100  39.68600  -38.04900 1.000 42.43000  ? 160 HIS   B CD2    1 
ATOM   6847 C CE1    . HIS   B 1 194 ? 24.53600  41.66500  -38.18400 1.000 49.36000  ? 160 HIS   B CE1    1 
ATOM   6848 N NE2    . HIS   B 1 194 ? 24.66300  40.40200  -38.54700 1.000 47.67000  ? 160 HIS   B NE2    1 
ATOM   6849 H H      . HIS   B 1 194 ? 22.97500  39.14800  -34.93200 1.000 40.57000  ? 160 HIS   B H      1 
ATOM   6850 H HA     . HIS   B 1 194 ? 21.75600  41.55700  -34.99100 1.000 34.68000  ? 160 HIS   B HA     1 
ATOM   6851 H HB2    . HIS   B 1 194 ? 21.24000  39.44900  -36.78400 1.000 39.07000  ? 160 HIS   B HB2    1 
ATOM   6852 H HB3    . HIS   B 1 194 ? 20.88200  40.97900  -37.00300 1.000 39.07000  ? 160 HIS   B HB3    1 
ATOM   6853 H HD2    . HIS   B 1 194 ? 23.44800  38.77500  -38.16000 1.000 42.43000  ? 160 HIS   B HD2    1 
ATOM   6854 H HE1    . HIS   B 1 194 ? 25.12500  42.35300  -38.39400 1.000 49.36000  ? 160 HIS   B HE1    1 
ATOM   6855 H HE2    . HIS   B 1 194 ? 25.31000  40.07800  -39.01200 1.000 47.67000  ? 160 HIS   B HE2    1 
ATOM   6856 N N      . PRO   B 1 195 ? 19.32000  40.85200  -34.58600 1.000 35.33000  ? 161 PRO   B N      1 
ATOM   6857 C CA     . PRO   B 1 195 ? 18.02800  40.35800  -34.09700 1.000 30.76000  ? 161 PRO   B CA     1 
ATOM   6858 C C      . PRO   B 1 195 ? 17.59100  39.15200  -34.91700 1.000 37.03000  ? 161 PRO   B C      1 
ATOM   6859 O O      . PRO   B 1 195 ? 17.96600  38.99700  -36.08000 1.000 38.00000  ? 161 PRO   B O      1 
ATOM   6860 C CB     . PRO   B 1 195 ? 17.08800  41.55600  -34.31100 1.000 36.85000  ? 161 PRO   B CB     1 
ATOM   6861 C CG     . PRO   B 1 195 ? 18.03400  42.77400  -34.56800 1.000 39.53000  ? 161 PRO   B CG     1 
ATOM   6862 C CD     . PRO   B 1 195 ? 19.23300  42.18200  -35.21300 1.000 37.51000  ? 161 PRO   B CD     1 
ATOM   6863 H HA     . PRO   B 1 195 ? 18.07300  40.12900  -33.15600 1.000 30.76000  ? 161 PRO   B HA     1 
ATOM   6864 H HB2    . PRO   B 1 195 ? 16.61400  41.38500  -35.12100 1.000 36.85000  ? 161 PRO   B HB2    1 
ATOM   6865 H HB3    . PRO   B 1 195 ? 16.50000  41.69100  -33.55200 1.000 36.85000  ? 161 PRO   B HB3    1 
ATOM   6866 H HG2    . PRO   B 1 195 ? 17.60100  43.40800  -35.16100 1.000 39.53000  ? 161 PRO   B HG2    1 
ATOM   6867 H HG3    . PRO   B 1 195 ? 18.26700  43.19300  -33.72500 1.000 39.53000  ? 161 PRO   B HG3    1 
ATOM   6868 H HD2    . PRO   B 1 195 ? 19.09600  42.10000  -36.17000 1.000 37.51000  ? 161 PRO   B HD2    1 
ATOM   6869 H HD3    . PRO   B 1 195 ? 20.01100  42.72100  -35.00700 1.000 37.51000  ? 161 PRO   B HD3    1 
ATOM   6870 N N      . PHE   B 1 196 ? 16.80500  38.27800  -34.29600 1.000 31.65000  ? 162 PHE   B N      1 
ATOM   6871 C CA     . PHE   B 1 196 ? 16.35400  37.07300  -34.98300 1.000 32.47000  ? 162 PHE   B CA     1 
ATOM   6872 C C      . PHE   B 1 196 ? 14.98700  36.71300  -34.43700 1.000 32.21000  ? 162 PHE   B C      1 
ATOM   6873 O O      . PHE   B 1 196 ? 14.51600  37.29900  -33.46100 1.000 34.03000  ? 162 PHE   B O      1 
ATOM   6874 C CB     . PHE   B 1 196 ? 17.35400  35.91700  -34.81900 1.000 27.98000  ? 162 PHE   B CB     1 
ATOM   6875 C CG     . PHE   B 1 196 ? 17.54400  35.46100  -33.39200 1.000 29.03000  ? 162 PHE   B CG     1 
ATOM   6876 C CD1    . PHE   B 1 196 ? 18.43900  36.12000  -32.55200 1.000 33.12000  ? 162 PHE   B CD1    1 
ATOM   6877 C CD2    . PHE   B 1 196 ? 16.84500  34.37100  -32.88800 1.000 31.94000  ? 162 PHE   B CD2    1 
ATOM   6878 C CE1    . PHE   B 1 196 ? 18.61700  35.70600  -31.24600 1.000 31.75000  ? 162 PHE   B CE1    1 
ATOM   6879 C CE2    . PHE   B 1 196 ? 17.03100  33.94700  -31.57600 1.000 30.65000  ? 162 PHE   B CE2    1 
ATOM   6880 C CZ     . PHE   B 1 196 ? 17.91600  34.62300  -30.75600 1.000 35.07000  ? 162 PHE   B CZ     1 
ATOM   6881 H H      . PHE   B 1 196 ? 16.52200  38.35700  -33.48800 1.000 31.65000  ? 162 PHE   B H      1 
ATOM   6882 H HA     . PHE   B 1 196 ? 16.26100  37.26000  -35.93000 1.000 32.47000  ? 162 PHE   B HA     1 
ATOM   6883 H HB2    . PHE   B 1 196 ? 17.03800  35.15700  -35.33200 1.000 27.98000  ? 162 PHE   B HB2    1 
ATOM   6884 H HB3    . PHE   B 1 196 ? 18.21800  36.20300  -35.15500 1.000 27.98000  ? 162 PHE   B HB3    1 
ATOM   6885 H HD1    . PHE   B 1 196 ? 18.91500  36.85300  -32.87100 1.000 33.12000  ? 162 PHE   B HD1    1 
ATOM   6886 H HD2    . PHE   B 1 196 ? 16.24800  33.91600  -33.43700 1.000 31.94000  ? 162 PHE   B HD2    1 
ATOM   6887 H HE1    . PHE   B 1 196 ? 19.21600  36.15700  -30.69500 1.000 31.75000  ? 162 PHE   B HE1    1 
ATOM   6888 H HE2    . PHE   B 1 196 ? 16.55400  33.21900  -31.24800 1.000 30.65000  ? 162 PHE   B HE2    1 
ATOM   6889 H HZ     . PHE   B 1 196 ? 18.04200  34.34600  -29.87700 1.000 35.07000  ? 162 PHE   B HZ     1 
ATOM   6890 N N      . GLY   B 1 197 ? 14.33200  35.74600  -35.08300 1.000 29.76000  ? 163 GLY   B N      1 
ATOM   6891 C CA     . GLY   B 1 197 ? 13.04300  35.27400  -34.64300 1.000 26.67000  ? 163 GLY   B CA     1 
ATOM   6892 C C      . GLY   B 1 197 ? 13.12100  33.81200  -34.24100 1.000 28.99000  ? 163 GLY   B C      1 
ATOM   6893 O O      . GLY   B 1 197 ? 14.12900  33.12700  -34.47000 1.000 32.04000  ? 163 GLY   B O      1 
ATOM   6894 H H      . GLY   B 1 197 ? 14.62700  35.34900  -35.78700 1.000 29.76000  ? 163 GLY   B H      1 
ATOM   6895 H HA2    . GLY   B 1 197 ? 12.74900  35.78900  -33.87600 1.000 26.67000  ? 163 GLY   B HA2    1 
ATOM   6896 H HA3    . GLY   B 1 197 ? 12.38800  35.36600  -35.34500 1.000 26.67000  ? 163 GLY   B HA3    1 
ATOM   6897 N N      . VAL   B 1 198 ? 12.04200  33.34300  -33.62700 1.000 27.94000  ? 164 VAL   B N      1 
ATOM   6898 C CA     . VAL   B 1 198 ? 11.96000  31.96400  -33.15900 1.000 28.25000  ? 164 VAL   B CA     1 
ATOM   6899 C C      . VAL   B 1 198 ? 10.65100  31.36700  -33.64000 1.000 32.80000  ? 164 VAL   B C      1 
ATOM   6900 O O      . VAL   B 1 198 ? 9.59200   31.98400  -33.49200 1.000 33.62000  ? 164 VAL   B O      1 
ATOM   6901 C CB     . VAL   B 1 198 ? 12.06900  31.86900  -31.62200 1.000 33.51000  ? 164 VAL   B CB     1 
ATOM   6902 C CG1    . VAL   B 1 198 ? 13.37800  32.48200  -31.15300 1.000 30.73000  ? 164 VAL   B CG1    1 
ATOM   6903 C CG2    . VAL   B 1 198 ? 10.89000  32.57200  -30.97400 1.000 38.16000  ? 164 VAL   B CG2    1 
ATOM   6904 H H      . VAL   B 1 198 ? 11.33600  33.80800  -33.46800 1.000 27.94000  ? 164 VAL   B H      1 
ATOM   6905 H HA     . VAL   B 1 198 ? 12.68500  31.44900  -33.54500 1.000 28.25000  ? 164 VAL   B HA     1 
ATOM   6906 H HB     . VAL   B 1 198 ? 12.05400  30.93700  -31.35500 1.000 33.51000  ? 164 VAL   B HB     1 
ATOM   6907 H HG11   . VAL   B 1 198 ? 13.43500  32.40100  -30.18800 1.000 30.73000  ? 164 VAL   B HG11   1 
ATOM   6908 H HG12   . VAL   B 1 198 ? 14.11500  32.00900  -31.57000 1.000 30.73000  ? 164 VAL   B HG12   1 
ATOM   6909 H HG13   . VAL   B 1 198 ? 13.39900  33.41800  -31.40700 1.000 30.73000  ? 164 VAL   B HG13   1 
ATOM   6910 H HG21   . VAL   B 1 198 ? 11.08200  32.70300  -30.03200 1.000 38.16000  ? 164 VAL   B HG21   1 
ATOM   6911 H HG22   . VAL   B 1 198 ? 10.75500  33.43000  -31.40500 1.000 38.16000  ? 164 VAL   B HG22   1 
ATOM   6912 H HG23   . VAL   B 1 198 ? 10.09700  32.02300  -31.07500 1.000 38.16000  ? 164 VAL   B HG23   1 
ATOM   6913 N N      . LYS   B 1 199 ? 10.72200  30.15300  -34.17700 1.000 27.22000  ? 165 LYS   B N      1 
ATOM   6914 C CA     . LYS   B 1 199 ? 9.53900   29.39500  -34.56000 1.000 26.13000  ? 165 LYS   B CA     1 
ATOM   6915 C C      . LYS   B 1 199 ? 9.13900   28.49300  -33.39200 1.000 32.86000  ? 165 LYS   B C      1 
ATOM   6916 O O      . LYS   B 1 199 ? 9.90300   27.60200  -32.99800 1.000 30.70000  ? 165 LYS   B O      1 
ATOM   6917 C CB     . LYS   B 1 199 ? 9.83500   28.57100  -35.81300 1.000 26.09000  ? 165 LYS   B CB     1 
ATOM   6918 C CG     . LYS   B 1 199 ? 8.70700   27.62400  -36.29200 1.000 28.26000  ? 165 LYS   B CG     1 
ATOM   6919 C CD     . LYS   B 1 199 ? 7.62300   28.40600  -37.03400 1.000 28.34000  ? 165 LYS   B CD     1 
ATOM   6920 C CE     . LYS   B 1 199 ? 6.70200   27.48000  -37.88900 1.000 28.08000  ? 165 LYS   B CE     1 
ATOM   6921 N NZ     . LYS   B 1 199 ? 7.34600   26.90800  -39.14900 1.000 29.45000  ? 165 LYS   B NZ     1 
ATOM   6922 H H      . LYS   B 1 199 ? 11.46000  29.74000  -34.33200 1.000 27.22000  ? 165 LYS   B H      1 
ATOM   6923 H HA     . LYS   B 1 199 ? 8.80700   30.00100  -34.75000 1.000 26.13000  ? 165 LYS   B HA     1 
ATOM   6924 H HB2    . LYS   B 1 199 ? 10.03000  29.18200  -36.54100 1.000 26.09000  ? 165 LYS   B HB2    1 
ATOM   6925 H HB3    . LYS   B 1 199 ? 10.61400  28.02300  -35.63800 1.000 26.09000  ? 165 LYS   B HB3    1 
ATOM   6926 H HG2    . LYS   B 1 199 ? 9.07800   26.96700  -36.90100 1.000 28.26000  ? 165 LYS   B HG2    1 
ATOM   6927 H HG3    . LYS   B 1 199 ? 8.30000   27.18300  -35.53100 1.000 28.26000  ? 165 LYS   B HG3    1 
ATOM   6928 H HD2    . LYS   B 1 199 ? 7.06800   28.86900  -36.38800 1.000 28.34000  ? 165 LYS   B HD2    1 
ATOM   6929 H HD3    . LYS   B 1 199 ? 8.04300   29.04500  -37.63100 1.000 28.34000  ? 165 LYS   B HD3    1 
ATOM   6930 H HE2    . LYS   B 1 199 ? 6.42500   26.73200  -37.33800 1.000 28.08000  ? 165 LYS   B HE2    1 
ATOM   6931 H HE3    . LYS   B 1 199 ? 5.92300   27.98800  -38.16400 1.000 28.08000  ? 165 LYS   B HE3    1 
ATOM   6932 H HZ1    . LYS   B 1 199 ? 6.91600   26.17100  -39.40100 1.000 29.45000  ? 165 LYS   B HZ1    1 
ATOM   6933 H HZ2    . LYS   B 1 199 ? 7.31100   27.50500  -39.80800 1.000 29.45000  ? 165 LYS   B HZ2    1 
ATOM   6934 H HZ3    . LYS   B 1 199 ? 8.19700   26.70200  -38.98800 1.000 29.45000  ? 165 LYS   B HZ3    1 
ATOM   6935 N N      . MET   B 1 200 ? 7.91700   28.70400  -32.85600 1.000 28.58000  ? 166 MET   B N      1 
ATOM   6936 C CA     . MET   B 1 200 ? 7.45300   28.05500  -31.63000 1.000 29.10000  ? 166 MET   B CA     1 
ATOM   6937 C C      . MET   B 1 200 ? 6.47300   26.91200  -31.89700 1.000 29.75000  ? 166 MET   B C      1 
ATOM   6938 O O      . MET   B 1 200 ? 5.65600   26.96700  -32.82900 1.000 29.58000  ? 166 MET   B O      1 
ATOM   6939 C CB     . MET   B 1 200 ? 6.76400   29.08600  -30.72400 1.000 30.41000  ? 166 MET   B CB     1 
ATOM   6940 C CG     . MET   B 1 200 ? 7.66100   30.24300  -30.31600 1.000 33.09000  ? 166 MET   B CG     1 
ATOM   6941 S SD     . MET   B 1 200 ? 8.99300   29.71700  -29.23800 1.000 39.18000  ? 166 MET   B SD     1 
ATOM   6942 C CE     . MET   B 1 200 ? 8.04400   29.21000  -27.74500 1.000 36.06000  ? 166 MET   B CE     1 
ATOM   6943 H H      . MET   B 1 200 ? 7.33300   29.23300  -33.20000 1.000 28.58000  ? 166 MET   B H      1 
ATOM   6944 H HA     . MET   B 1 200 ? 8.23500   27.72600  -31.16500 1.000 29.10000  ? 166 MET   B HA     1 
ATOM   6945 H HB2    . MET   B 1 200 ? 6.00300   29.45600  -31.19800 1.000 30.41000  ? 166 MET   B HB2    1 
ATOM   6946 H HB3    . MET   B 1 200 ? 6.46200   28.64100  -29.91700 1.000 30.41000  ? 166 MET   B HB3    1 
ATOM   6947 H HG2    . MET   B 1 200 ? 8.05200   30.64100  -31.10900 1.000 33.09000  ? 166 MET   B HG2    1 
ATOM   6948 H HG3    . MET   B 1 200 ? 7.13100   30.90000  -29.83900 1.000 33.09000  ? 166 MET   B HG3    1 
ATOM   6949 H HE1    . MET   B 1 200 ? 8.66600   29.02900  -27.02300 1.000 36.06000  ? 166 MET   B HE1    1 
ATOM   6950 H HE2    . MET   B 1 200 ? 7.44500   29.93000  -27.49300 1.000 36.06000  ? 166 MET   B HE2    1 
ATOM   6951 H HE3    . MET   B 1 200 ? 7.53400   28.41100  -27.95000 1.000 36.06000  ? 166 MET   B HE3    1 
ATOM   6952 N N      . PRO   B 1 201 ? 6.52500   25.88600  -31.04600 1.000 29.87000  ? 167 PRO   B N      1 
ATOM   6953 C CA     . PRO   B 1 201 ? 5.47900   24.84900  -31.04100 1.000 26.80000  ? 167 PRO   B CA     1 
ATOM   6954 C C      . PRO   B 1 201 ? 4.20500   25.39100  -30.41200 1.000 30.97000  ? 167 PRO   B C      1 
ATOM   6955 O O      . PRO   B 1 201 ? 4.25800   26.40400  -29.69800 1.000 30.58000  ? 167 PRO   B O      1 
ATOM   6956 C CB     . PRO   B 1 201 ? 6.10300   23.74600  -30.16900 1.000 30.68000  ? 167 PRO   B CB     1 
ATOM   6957 C CG     . PRO   B 1 201 ? 6.86400   24.55000  -29.11600 1.000 32.72000  ? 167 PRO   B CG     1 
ATOM   6958 C CD     . PRO   B 1 201 ? 7.45500   25.74900  -29.90900 1.000 33.50000  ? 167 PRO   B CD     1 
ATOM   6959 H HA     . PRO   B 1 201 ? 5.30700   24.51800  -31.93600 1.000 26.80000  ? 167 PRO   B HA     1 
ATOM   6960 H HB2    . PRO   B 1 201 ? 5.40600   23.20700  -29.76300 1.000 30.68000  ? 167 PRO   B HB2    1 
ATOM   6961 H HB3    . PRO   B 1 201 ? 6.70700   23.20200  -30.69900 1.000 30.68000  ? 167 PRO   B HB3    1 
ATOM   6962 H HG2    . PRO   B 1 201 ? 6.25100   24.85700  -28.43000 1.000 32.72000  ? 167 PRO   B HG2    1 
ATOM   6963 H HG3    . PRO   B 1 201 ? 7.56800   24.00400  -28.73300 1.000 32.72000  ? 167 PRO   B HG3    1 
ATOM   6964 H HD2    . PRO   B 1 201 ? 7.42200   26.54700  -29.35900 1.000 33.50000  ? 167 PRO   B HD2    1 
ATOM   6965 H HD3    . PRO   B 1 201 ? 8.35900   25.56800  -30.19700 1.000 33.50000  ? 167 PRO   B HD3    1 
ATOM   6966 N N      . PRO   B 1 202 ? 3.04300   24.76800  -30.65000 1.000 27.89000  ? 168 PRO   B N      1 
ATOM   6967 C CA     . PRO   B 1 202 ? 1.82700   25.20800  -29.95400 1.000 28.62000  ? 168 PRO   B CA     1 
ATOM   6968 C C      . PRO   B 1 202 ? 1.87300   24.84000  -28.48200 1.000 31.24000  ? 168 PRO   B C      1 
ATOM   6969 O O      . PRO   B 1 202 ? 2.34900   23.75900  -28.11000 1.000 31.27000  ? 168 PRO   B O      1 
ATOM   6970 C CB     . PRO   B 1 202 ? 0.69900   24.46000  -30.67900 1.000 29.08000  ? 168 PRO   B CB     1 
ATOM   6971 C CG     . PRO   B 1 202 ? 1.36600   23.20500  -31.22100 1.000 30.76000  ? 168 PRO   B CG     1 
ATOM   6972 C CD     . PRO   B 1 202 ? 2.78400   23.63000  -31.56000 1.000 32.13000  ? 168 PRO   B CD     1 
ATOM   6973 H HA     . PRO   B 1 202 ? 1.70200   26.16500  -30.05100 1.000 28.62000  ? 168 PRO   B HA     1 
ATOM   6974 H HB2    . PRO   B 1 202 ? -0.00300  24.23300  -30.04900 1.000 29.08000  ? 168 PRO   B HB2    1 
ATOM   6975 H HB3    . PRO   B 1 202 ? 0.35300   25.00700  -31.40200 1.000 29.08000  ? 168 PRO   B HB3    1 
ATOM   6976 H HG2    . PRO   B 1 202 ? 1.36700   22.51400  -30.54000 1.000 30.76000  ? 168 PRO   B HG2    1 
ATOM   6977 H HG3    . PRO   B 1 202 ? 0.90000   22.90400  -32.01600 1.000 30.76000  ? 168 PRO   B HG3    1 
ATOM   6978 H HD2    . PRO   B 1 202 ? 3.40400   22.90700  -31.37900 1.000 32.13000  ? 168 PRO   B HD2    1 
ATOM   6979 H HD3    . PRO   B 1 202 ? 2.83700   23.91900  -32.48400 1.000 32.13000  ? 168 PRO   B HD3    1 
ATOM   6980 N N      . TYR   B 1 203 ? 1.35400   25.74500  -27.65400 1.000 30.10000  ? 169 TYR   B N      1 
ATOM   6981 C CA     . TYR   B 1 203 ? 1.06900   25.47100  -26.25700 1.000 32.91000  ? 169 TYR   B CA     1 
ATOM   6982 C C      . TYR   B 1 203 ? -0.43200  25.44800  -26.04200 1.000 33.83000  ? 169 TYR   B C      1 
ATOM   6983 O O      . TYR   B 1 203 ? -1.21000  25.97500  -26.84100 1.000 32.80000  ? 169 TYR   B O      1 
ATOM   6984 C CB     . TYR   B 1 203 ? 1.69900   26.51000  -25.32900 1.000 28.93000  ? 169 TYR   B CB     1 
ATOM   6985 C CG     . TYR   B 1 203 ? 3.18200   26.58000  -25.43000 1.000 32.31000  ? 169 TYR   B CG     1 
ATOM   6986 C CD1    . TYR   B 1 203 ? 3.98700   25.58000  -24.90300 1.000 32.75000  ? 169 TYR   B CD1    1 
ATOM   6987 C CD2    . TYR   B 1 203 ? 3.79200   27.64300  -26.07700 1.000 32.48000  ? 169 TYR   B CD2    1 
ATOM   6988 C CE1    . TYR   B 1 203 ? 5.37700   25.65700  -25.01400 1.000 28.92000  ? 169 TYR   B CE1    1 
ATOM   6989 C CE2    . TYR   B 1 203 ? 5.15800   27.72700  -26.18300 1.000 35.99000  ? 169 TYR   B CE2    1 
ATOM   6990 C CZ     . TYR   B 1 203 ? 5.94400   26.73900  -25.65700 1.000 35.64000  ? 169 TYR   B CZ     1 
ATOM   6991 O OH     . TYR   B 1 203 ? 7.30200   26.84200  -25.78400 1.000 34.97000  ? 169 TYR   B OH     1 
ATOM   6992 H H      . TYR   B 1 203 ? 1.15400   26.54700  -27.89100 1.000 30.10000  ? 169 TYR   B H      1 
ATOM   6993 H HA     . TYR   B 1 203 ? 1.42300   24.59900  -26.02100 1.000 32.91000  ? 169 TYR   B HA     1 
ATOM   6994 H HB2    . TYR   B 1 203 ? 1.34700   27.38200  -25.55300 1.000 28.93000  ? 169 TYR   B HB2    1 
ATOM   6995 H HB3    . TYR   B 1 203 ? 1.47300   26.28900  -24.41200 1.000 28.93000  ? 169 TYR   B HB3    1 
ATOM   6996 H HD1    . TYR   B 1 203 ? 3.59800   24.85500  -24.46900 1.000 32.75000  ? 169 TYR   B HD1    1 
ATOM   6997 H HD2    . TYR   B 1 203 ? 3.26500   28.32000  -26.43500 1.000 32.48000  ? 169 TYR   B HD2    1 
ATOM   6998 H HE1    . TYR   B 1 203 ? 5.91500   24.98800  -24.65600 1.000 28.92000  ? 169 TYR   B HE1    1 
ATOM   6999 H HE2    . TYR   B 1 203 ? 5.54800   28.45000  -26.61900 1.000 35.99000  ? 169 TYR   B HE2    1 
ATOM   7000 H HH     . TYR   B 1 203 ? 7.67500   26.18000  -25.42700 1.000 34.97000  ? 169 TYR   B HH     1 
ATOM   7001 N N      . PHE   B 1 204 ? -0.82700  24.83900  -24.92800 1.000 29.83000  ? 170 PHE   B N      1 
ATOM   7002 C CA     . PHE   B 1 204 ? -2.23600  24.53300  -24.71300 1.000 33.23000  ? 170 PHE   B CA     1 
ATOM   7003 C C      . PHE   B 1 204 ? -2.71200  24.89600  -23.31300 1.000 40.37000  ? 170 PHE   B C      1 
ATOM   7004 O O      . PHE   B 1 204 ? -3.80600  24.46900  -22.91500 1.000 40.51000  ? 170 PHE   B O      1 
ATOM   7005 C CB     . PHE   B 1 204 ? -2.48800  23.04800  -24.98000 1.000 35.47000  ? 170 PHE   B CB     1 
ATOM   7006 C CG     . PHE   B 1 204 ? -2.10300  22.62700  -26.35900 1.000 33.63000  ? 170 PHE   B CG     1 
ATOM   7007 C CD1    . PHE   B 1 204 ? -3.00500  22.75900  -27.40300 1.000 30.17000  ? 170 PHE   B CD1    1 
ATOM   7008 C CD2    . PHE   B 1 204 ? -0.83600  22.14700  -26.62200 1.000 30.74000  ? 170 PHE   B CD2    1 
ATOM   7009 C CE1    . PHE   B 1 204 ? -2.65500  22.39300  -28.69800 1.000 30.10000  ? 170 PHE   B CE1    1 
ATOM   7010 C CE2    . PHE   B 1 204 ? -0.48200  21.77400  -27.89100 1.000 27.85000  ? 170 PHE   B CE2    1 
ATOM   7011 C CZ     . PHE   B 1 204 ? -1.37800  21.91300  -28.94000 1.000 30.33000  ? 170 PHE   B CZ     1 
ATOM   7012 H H      . PHE   B 1 204 ? -0.30600  24.59500  -24.28900 1.000 29.83000  ? 170 PHE   B H      1 
ATOM   7013 H HA     . PHE   B 1 204 ? -2.77000  25.04000  -25.34300 1.000 33.23000  ? 170 PHE   B HA     1 
ATOM   7014 H HB2    . PHE   B 1 204 ? -1.96900  22.52300  -24.35100 1.000 35.47000  ? 170 PHE   B HB2    1 
ATOM   7015 H HB3    . PHE   B 1 204 ? -3.43300  22.86300  -24.86400 1.000 35.47000  ? 170 PHE   B HB3    1 
ATOM   7016 H HD1    . PHE   B 1 204 ? -3.85700  23.09300  -27.23500 1.000 30.17000  ? 170 PHE   B HD1    1 
ATOM   7017 H HD2    . PHE   B 1 204 ? -0.22300  22.05900  -25.92800 1.000 30.74000  ? 170 PHE   B HD2    1 
ATOM   7018 H HE1    . PHE   B 1 204 ? -3.26600  22.48000  -29.39400 1.000 30.10000  ? 170 PHE   B HE1    1 
ATOM   7019 H HE2    . PHE   B 1 204 ? 0.37400   21.45000  -28.05500 1.000 27.85000  ? 170 PHE   B HE2    1 
ATOM   7020 H HZ     . PHE   B 1 204 ? -1.13300  21.65300  -29.79900 1.000 30.33000  ? 170 PHE   B HZ     1 
ATOM   7021 N N      . ASP   B 1 205 ? -1.93400  25.65100  -22.54900 1.000 37.33000  ? 171 ASP   B N      1 
ATOM   7022 C CA     . ASP   B 1 205 ? -2.41700  26.14800  -21.27000 1.000 41.95000  ? 171 ASP   B CA     1 
ATOM   7023 C C      . ASP   B 1 205 ? -1.64000  27.40600  -20.92600 1.000 38.96000  ? 171 ASP   B C      1 
ATOM   7024 O O      . ASP   B 1 205 ? -0.50200  27.58800  -21.36500 1.000 38.63000  ? 171 ASP   B O      1 
ATOM   7025 C CB     . ASP   B 1 205 ? -2.28100  25.10900  -20.14500 1.000 44.39000  ? 171 ASP   B CB     1 
ATOM   7026 C CG     . ASP   B 1 205 ? -0.84000  24.83700  -19.77600 1.000 50.76000  ? 171 ASP   B CG     1 
ATOM   7027 O OD1    . ASP   B 1 205 ? -0.23200  25.68700  -19.08800 1.000 57.69000  ? 171 ASP   B OD1    1 
ATOM   7028 O OD2    . ASP   B 1 205 ? -0.30700  23.78800  -20.18700 1.000 60.06000  ? 171 ASP   B OD2    1 
ATOM   7029 H H      . ASP   B 1 205 ? -1.13100  25.88800  -22.74500 1.000 37.33000  ? 171 ASP   B H      1 
ATOM   7030 H HA     . ASP   B 1 205 ? -3.35400  26.38400  -21.35200 1.000 41.95000  ? 171 ASP   B HA     1 
ATOM   7031 H HB2    . ASP   B 1 205 ? -2.73700  25.43700  -19.35400 1.000 44.39000  ? 171 ASP   B HB2    1 
ATOM   7032 H HB3    . ASP   B 1 205 ? -2.67900  24.27400  -20.43600 1.000 44.39000  ? 171 ASP   B HB3    1 
ATOM   7033 N N      . PHE   B 1 206 ? -2.26700  28.26800  -20.12200 1.000 41.30000  ? 172 PHE   B N      1 
ATOM   7034 C CA     . PHE   B 1 206 ? -1.69800  29.58700  -19.86400 1.000 38.51000  ? 172 PHE   B CA     1 
ATOM   7035 C C      . PHE   B 1 206 ? -0.42900  29.51100  -19.03200 1.000 40.39000  ? 172 PHE   B C      1 
ATOM   7036 O O      . PHE   B 1 206 ? 0.42900   30.39300  -19.13700 1.000 39.38000  ? 172 PHE   B O      1 
ATOM   7037 C CB     . PHE   B 1 206 ? -2.74200  30.48400  -19.18700 1.000 47.20000  ? 172 PHE   B CB     1 
ATOM   7038 C CG     . PHE   B 1 206 ? -3.80600  30.99500  -20.13300 1.000 55.28000  ? 172 PHE   B CG     1 
ATOM   7039 C CD1    . PHE   B 1 206 ? -4.50500  30.12000  -20.94700 1.000 56.20000  ? 172 PHE   B CD1    1 
ATOM   7040 C CD2    . PHE   B 1 206 ? -4.09800  32.35200  -20.21700 1.000 69.67000  ? 172 PHE   B CD2    1 
ATOM   7041 C CE1    . PHE   B 1 206 ? -5.48100  30.57500  -21.82100 1.000 57.98000  ? 172 PHE   B CE1    1 
ATOM   7042 C CE2    . PHE   B 1 206 ? -5.07300  32.82100  -21.09300 1.000 70.37000  ? 172 PHE   B CE2    1 
ATOM   7043 C CZ     . PHE   B 1 206 ? -5.76600  31.92100  -21.89800 1.000 56.53000  ? 172 PHE   B CZ     1 
ATOM   7044 H H      . PHE   B 1 206 ? -3.01200  28.11400  -19.72000 1.000 41.30000  ? 172 PHE   B H      1 
ATOM   7045 H HA     . PHE   B 1 206 ? -1.46700  29.99500  -20.71300 1.000 38.51000  ? 172 PHE   B HA     1 
ATOM   7046 H HB2    . PHE   B 1 206 ? -3.18400  29.97700  -18.48800 1.000 47.20000  ? 172 PHE   B HB2    1 
ATOM   7047 H HB3    . PHE   B 1 206 ? -2.29200  31.25300  -18.80200 1.000 47.20000  ? 172 PHE   B HB3    1 
ATOM   7048 H HD1    . PHE   B 1 206 ? -4.32200  29.21000  -20.90400 1.000 56.20000  ? 172 PHE   B HD1    1 
ATOM   7049 H HD2    . PHE   B 1 206 ? -3.63600  32.95400  -19.68000 1.000 69.67000  ? 172 PHE   B HD2    1 
ATOM   7050 H HE1    . PHE   B 1 206 ? -5.94100  29.97100  -22.35800 1.000 57.98000  ? 172 PHE   B HE1    1 
ATOM   7051 H HE2    . PHE   B 1 206 ? -5.26200  33.73000  -21.13900 1.000 70.37000  ? 172 PHE   B HE2    1 
ATOM   7052 H HZ     . PHE   B 1 206 ? -6.42000  32.22700  -22.48400 1.000 56.53000  ? 172 PHE   B HZ     1 
ATOM   7053 N N      . ALA   B 1 207 ? -0.26900  28.47700  -18.20500 1.000 41.16000  ? 173 ALA   B N      1 
ATOM   7054 C CA     . ALA   B 1 207 ? 0.98600   28.35900  -17.47100 1.000 40.11000  ? 173 ALA   B CA     1 
ATOM   7055 C C      . ALA   B 1 207 ? 2.16800   28.25300  -18.43200 1.000 44.63000  ? 173 ALA   B C      1 
ATOM   7056 O O      . ALA   B 1 207 ? 3.21300   28.87500  -18.21600 1.000 39.22000  ? 173 ALA   B O      1 
ATOM   7057 C CB     . ALA   B 1 207 ? 0.93900   27.15500  -16.51900 1.000 43.09000  ? 173 ALA   B CB     1 
ATOM   7058 H H      . ALA   B 1 207 ? -0.84600  27.85600  -18.05700 1.000 41.16000  ? 173 ALA   B H      1 
ATOM   7059 H HA     . ALA   B 1 207 ? 1.11100   29.15700  -16.93400 1.000 40.11000  ? 173 ALA   B HA     1 
ATOM   7060 H HB1    . ALA   B 1 207 ? 1.77000   27.11500  -16.02100 1.000 43.09000  ? 173 ALA   B HB1    1 
ATOM   7061 H HB2    . ALA   B 1 207 ? 0.19300   27.26500  -15.90900 1.000 43.09000  ? 173 ALA   B HB2    1 
ATOM   7062 H HB3    . ALA   B 1 207 ? 0.82500   26.34400  -17.03800 1.000 43.09000  ? 173 ALA   B HB3    1 
ATOM   7063 N N      . HIS   B 1 208 ? 2.02400   27.46900  -19.50500 1.000 40.87000  ? 174 HIS   B N      1 
ATOM   7064 C CA     . HIS   B 1 208 ? 3.11400   27.35900  -20.47400 1.000 39.15000  ? 174 HIS   B CA     1 
ATOM   7065 C C      . HIS   B 1 208 ? 3.28900   28.64900  -21.27700 1.000 35.85000  ? 174 HIS   B C      1 
ATOM   7066 O O      . HIS   B 1 208 ? 4.42400   29.06000  -21.55000 1.000 39.50000  ? 174 HIS   B O      1 
ATOM   7067 C CB     . HIS   B 1 208 ? 2.88000   26.16500  -21.40300 1.000 35.36000  ? 174 HIS   B CB     1 
ATOM   7068 C CG     . HIS   B 1 208 ? 3.17400   24.84400  -20.76000 1.000 49.45000  ? 174 HIS   B CG     1 
ATOM   7069 N ND1    . HIS   B 1 208 ? 2.20100   24.07300  -20.16200 1.000 62.78000  ? 174 HIS   B ND1    1 
ATOM   7070 C CD2    . HIS   B 1 208 ? 4.33500   24.16200  -20.61700 1.000 52.36000  ? 174 HIS   B CD2    1 
ATOM   7071 C CE1    . HIS   B 1 208 ? 2.75000   22.97300  -19.67600 1.000 56.48000  ? 174 HIS   B CE1    1 
ATOM   7072 N NE2    . HIS   B 1 208 ? 4.04400   23.00300  -19.94000 1.000 58.04000  ? 174 HIS   B NE2    1 
ATOM   7073 H H      . HIS   B 1 208 ? 1.32500   27.00300  -19.69000 1.000 40.87000  ? 174 HIS   B H      1 
ATOM   7074 H HA     . HIS   B 1 208 ? 3.94100   27.19900  -19.99300 1.000 39.15000  ? 174 HIS   B HA     1 
ATOM   7075 H HB2    . HIS   B 1 208 ? 1.95100   26.16100  -21.68100 1.000 35.36000  ? 174 HIS   B HB2    1 
ATOM   7076 H HB3    . HIS   B 1 208 ? 3.45600   26.25300  -22.17800 1.000 35.36000  ? 174 HIS   B HB3    1 
ATOM   7077 H HD1    . HIS   B 1 208 ? 1.37400   24.27600  -20.11100 1.000 62.78000  ? 174 HIS   B HD1    1 
ATOM   7078 H HD2    . HIS   B 1 208 ? 5.17300   24.43000  -20.91800 1.000 52.36000  ? 174 HIS   B HD2    1 
ATOM   7079 H HE1    . HIS   B 1 208 ? 2.30100   22.29200  -19.22900 1.000 56.48000  ? 174 HIS   B HE1    1 
ATOM   7080 N N      . PHE   B 1 209 ? 2.18400   29.29900  -21.67200 1.000 36.91000  ? 175 PHE   B N      1 
ATOM   7081 C CA     . PHE   B 1 209 ? 2.29700   30.60500  -22.33000 1.000 34.53000  ? 175 PHE   B CA     1 
ATOM   7082 C C      . PHE   B 1 209 ? 3.10000   31.57700  -21.47400 1.000 36.40000  ? 175 PHE   B C      1 
ATOM   7083 O O      . PHE   B 1 209 ? 4.01300   32.25300  -21.96100 1.000 35.08000  ? 175 PHE   B O      1 
ATOM   7084 C CB     . PHE   B 1 209 ? 0.91500   31.19400  -22.62000 1.000 31.29000  ? 175 PHE   B CB     1 
ATOM   7085 C CG     . PHE   B 1 209 ? 0.18700   30.53200  -23.77200 1.000 39.27000  ? 175 PHE   B CG     1 
ATOM   7086 C CD1    . PHE   B 1 209 ? 0.83700   30.29100  -24.97300 1.000 38.60000  ? 175 PHE   B CD1    1 
ATOM   7087 C CD2    . PHE   B 1 209 ? -1.15100  30.17000  -23.65000 1.000 45.77000  ? 175 PHE   B CD2    1 
ATOM   7088 C CE1    . PHE   B 1 209 ? 0.16700   29.69100  -26.03000 1.000 36.24000  ? 175 PHE   B CE1    1 
ATOM   7089 C CE2    . PHE   B 1 209 ? -1.82300  29.56300  -24.69700 1.000 52.71000  ? 175 PHE   B CE2    1 
ATOM   7090 C CZ     . PHE   B 1 209 ? -1.16200  29.31600  -25.88400 1.000 36.46000  ? 175 PHE   B CZ     1 
ATOM   7091 H H      . PHE   B 1 209 ? 1.37900   29.01300  -21.57300 1.000 36.91000  ? 175 PHE   B H      1 
ATOM   7092 H HA     . PHE   B 1 209 ? 2.77000   30.49500  -23.16900 1.000 34.53000  ? 175 PHE   B HA     1 
ATOM   7093 H HB2    . PHE   B 1 209 ? 0.36300   31.09800  -21.82800 1.000 31.29000  ? 175 PHE   B HB2    1 
ATOM   7094 H HB3    . PHE   B 1 209 ? 1.01700   32.13400  -22.83600 1.000 31.29000  ? 175 PHE   B HB3    1 
ATOM   7095 H HD1    . PHE   B 1 209 ? 1.73000   30.53200  -25.07100 1.000 38.60000  ? 175 PHE   B HD1    1 
ATOM   7096 H HD2    . PHE   B 1 209 ? -1.59600  30.32500  -22.84900 1.000 45.77000  ? 175 PHE   B HD2    1 
ATOM   7097 H HE1    . PHE   B 1 209 ? 0.61200   29.52600  -26.82900 1.000 36.24000  ? 175 PHE   B HE1    1 
ATOM   7098 H HE2    . PHE   B 1 209 ? -2.71600  29.32000  -24.60000 1.000 52.71000  ? 175 PHE   B HE2    1 
ATOM   7099 H HZ     . PHE   B 1 209 ? -1.61300  28.91800  -26.59300 1.000 36.46000  ? 175 PHE   B HZ     1 
ATOM   7100 N N      . ASP   B 1 210 ? 2.76000   31.66900  -20.18600 1.000 38.47000  ? 176 ASP   B N      1 
ATOM   7101 C CA     . ASP   B 1 210 ? 3.48100   32.58700  -19.30200 1.000 32.77000  ? 176 ASP   B CA     1 
ATOM   7102 C C      . ASP   B 1 210 ? 4.95300   32.21100  -19.18200 1.000 33.86000  ? 176 ASP   B C      1 
ATOM   7103 O O      . ASP   B 1 210 ? 5.82800   33.08700  -19.22000 1.000 37.03000  ? 176 ASP   B O      1 
ATOM   7104 C CB     . ASP   B 1 210 ? 2.84200   32.60800  -17.90900 1.000 40.84000  ? 176 ASP   B CB     1 
ATOM   7105 C CG     . ASP   B 1 210 ? 1.46200   33.22900  -17.90300 1.000 50.25000  ? 176 ASP   B CG     1 
ATOM   7106 O OD1    . ASP   B 1 210 ? 1.16000   34.03800  -18.80400 1.000 45.09000  ? 176 ASP   B OD1    1 
ATOM   7107 O OD2    . ASP   B 1 210 ? 0.68000   32.90600  -16.97700 1.000 47.55000  ? 176 ASP   B OD2    1 
ATOM   7108 H H      . ASP   B 1 210 ? 2.13100   31.22200  -19.80700 1.000 38.47000  ? 176 ASP   B H      1 
ATOM   7109 H HA     . ASP   B 1 210 ? 3.43000   33.48300  -19.66900 1.000 32.77000  ? 176 ASP   B HA     1 
ATOM   7110 H HB2    . ASP   B 1 210 ? 2.76200   31.69700  -17.58500 1.000 40.84000  ? 176 ASP   B HB2    1 
ATOM   7111 H HB3    . ASP   B 1 210 ? 3.40500   33.12400  -17.31100 1.000 40.84000  ? 176 ASP   B HB3    1 
ATOM   7112 N N      . ALA   B 1 211 ? 5.25200   30.91400  -19.02000 1.000 36.32000  ? 177 ALA   B N      1 
ATOM   7113 C CA     . ALA   B 1 211 ? 6.65000   30.51500  -18.88200 1.000 36.92000  ? 177 ALA   B CA     1 
ATOM   7114 C C      . ALA   B 1 211 ? 7.44300   30.79000  -20.16200 1.000 40.35000  ? 177 ALA   B C      1 
ATOM   7115 O O      . ALA   B 1 211 ? 8.58300   31.26100  -20.10100 1.000 32.59000  ? 177 ALA   B O      1 
ATOM   7116 C CB     . ALA   B 1 211 ? 6.75200   29.04300  -18.49300 1.000 39.06000  ? 177 ALA   B CB     1 
ATOM   7117 H H      . ALA   B 1 211 ? 4.68300   30.27000  -18.98800 1.000 36.32000  ? 177 ALA   B H      1 
ATOM   7118 H HA     . ALA   B 1 211 ? 7.05200   31.03600  -18.16900 1.000 36.92000  ? 177 ALA   B HA     1 
ATOM   7119 H HB1    . ALA   B 1 211 ? 7.68800   28.80300  -18.41100 1.000 39.06000  ? 177 ALA   B HB1    1 
ATOM   7120 H HB2    . ALA   B 1 211 ? 6.30000   28.90900  -17.64500 1.000 39.06000  ? 177 ALA   B HB2    1 
ATOM   7121 H HB3    . ALA   B 1 211 ? 6.33100   28.50500  -19.18200 1.000 39.06000  ? 177 ALA   B HB3    1 
ATOM   7122 N N      . ALA   B 1 212 ? 6.87100   30.49000  -21.33000 1.000 38.05000  ? 178 ALA   B N      1 
ATOM   7123 C CA     . ALA   B 1 212 ? 7.58700   30.75800  -22.57700 1.000 35.38000  ? 178 ALA   B CA     1 
ATOM   7124 C C      . ALA   B 1 212 ? 7.79000   32.25200  -22.78300 1.000 33.39000  ? 178 ALA   B C      1 
ATOM   7125 O O      . ALA   B 1 212 ? 8.87300   32.69200  -23.18400 1.000 34.96000  ? 178 ALA   B O      1 
ATOM   7126 C CB     . ALA   B 1 212 ? 6.83300   30.15200  -23.76300 1.000 31.67000  ? 178 ALA   B CB     1 
ATOM   7127 H H      . ALA   B 1 212 ? 6.09100   30.14000  -21.42600 1.000 38.05000  ? 178 ALA   B H      1 
ATOM   7128 H HA     . ALA   B 1 212 ? 8.46200   30.34100  -22.53400 1.000 35.38000  ? 178 ALA   B HA     1 
ATOM   7129 H HB1    . ALA   B 1 212 ? 7.32400   30.34100  -24.57800 1.000 31.67000  ? 178 ALA   B HB1    1 
ATOM   7130 H HB2    . ALA   B 1 212 ? 6.76100   29.19300  -23.63400 1.000 31.67000  ? 178 ALA   B HB2    1 
ATOM   7131 H HB3    . ALA   B 1 212 ? 5.94800   30.54700  -23.81000 1.000 31.67000  ? 178 ALA   B HB3    1 
ATOM   7132 N N      . ALA   B 1 213 ? 6.76000   33.05200  -22.50700 1.000 35.46000  ? 179 ALA   B N      1 
ATOM   7133 C CA     . ALA   B 1 213 ? 6.88300   34.48800  -22.73900 1.000 35.22000  ? 179 ALA   B CA     1 
ATOM   7134 C C      . ALA   B 1 213 ? 7.88700   35.11000  -21.78100 1.000 35.70000  ? 179 ALA   B C      1 
ATOM   7135 O O      . ALA   B 1 213 ? 8.67000   35.98500  -22.17400 1.000 36.58000  ? 179 ALA   B O      1 
ATOM   7136 C CB     . ALA   B 1 213 ? 5.51500   35.16300  -22.60600 1.000 34.54000  ? 179 ALA   B CB     1 
ATOM   7137 H H      . ALA   B 1 213 ? 6.00100   32.79700  -22.19400 1.000 35.46000  ? 179 ALA   B H      1 
ATOM   7138 H HA     . ALA   B 1 213 ? 7.20200   34.63500  -23.64300 1.000 35.22000  ? 179 ALA   B HA     1 
ATOM   7139 H HB1    . ALA   B 1 213 ? 5.61600   36.11500  -22.76300 1.000 34.54000  ? 179 ALA   B HB1    1 
ATOM   7140 H HB2    . ALA   B 1 213 ? 4.91000   34.78200  -23.26100 1.000 34.54000  ? 179 ALA   B HB2    1 
ATOM   7141 H HB3    . ALA   B 1 213 ? 5.17300   35.01000  -21.71100 1.000 34.54000  ? 179 ALA   B HB3    1 
ATOM   7142 N N      . GLU   B 1 214 ? 7.89300   34.65800  -20.52400 1.000 36.36000  ? 180 GLU   B N      1 
ATOM   7143 C CA     . GLU   B 1 214 ? 8.86400   35.17500  -19.56700 1.000 38.69000  ? 180 GLU   B CA     1 
ATOM   7144 C C      . GLU   B 1 214 ? 10.28400  34.94800  -20.06400 1.000 40.54000  ? 180 GLU   B C      1 
ATOM   7145 O O      . GLU   B 1 214 ? 11.14200  35.82200  -19.93000 1.000 40.86000  ? 180 GLU   B O      1 
ATOM   7146 C CB     . GLU   B 1 214 ? 8.65700   34.51400  -18.19900 1.000 40.02000  ? 180 GLU   B CB     1 
ATOM   7147 C CG     . GLU   B 1 214 ? 9.66500   34.94800  -17.13800 1.000 56.93000  ? 180 GLU   B CG     1 
ATOM   7148 H H      . GLU   B 1 214 ? 7.35600   34.06500  -20.20900 1.000 36.36000  ? 180 GLU   B H      1 
ATOM   7149 H HA     . GLU   B 1 214 ? 8.73000   36.13000  -19.46400 1.000 38.69000  ? 180 GLU   B HA     1 
ATOM   7150 H HB2    . GLU   B 1 214 ? 7.77100   34.74000  -17.87500 1.000 40.02000  ? 180 GLU   B HB2    1 
ATOM   7151 H HB3    . GLU   B 1 214 ? 8.73300   33.55300  -18.30300 1.000 40.02000  ? 180 GLU   B HB3    1 
ATOM   7152 N N      . ILE   B 1 215 ? 10.55200  33.78500  -20.65600 1.000 37.39000  ? 181 ILE   B N      1 
ATOM   7153 C CA     . ILE   B 1 215 ? 11.88600  33.52500  -21.19100 1.000 39.29000  ? 181 ILE   B CA     1 
ATOM   7154 C C      . ILE   B 1 215 ? 12.15300  34.40200  -22.40600 1.000 36.40000  ? 181 ILE   B C      1 
ATOM   7155 O O      . ILE   B 1 215 ? 13.19300  35.06500  -22.49900 1.000 36.57000  ? 181 ILE   B O      1 
ATOM   7156 C CB     . ILE   B 1 215 ? 12.05700  32.03400  -21.53900 1.000 38.45000  ? 181 ILE   B CB     1 
ATOM   7157 C CG1    . ILE   B 1 215 ? 12.09000  31.17800  -20.27000 1.000 45.42000  ? 181 ILE   B CG1    1 
ATOM   7158 C CG2    . ILE   B 1 215 ? 13.32200  31.84100  -22.34900 1.000 38.31000  ? 181 ILE   B CG2    1 
ATOM   7159 C CD1    . ILE   B 1 215 ? 11.93000  29.72900  -20.56800 1.000 40.59000  ? 181 ILE   B CD1    1 
ATOM   7160 H H      . ILE   B 1 215 ? 9.99100   33.14200  -20.75900 1.000 37.39000  ? 181 ILE   B H      1 
ATOM   7161 H HA     . ILE   B 1 215 ? 12.54300  33.74900  -20.51400 1.000 39.29000  ? 181 ILE   B HA     1 
ATOM   7162 H HB     . ILE   B 1 215 ? 11.30100  31.75600  -22.07900 1.000 38.45000  ? 181 ILE   B HB     1 
ATOM   7163 H HG12   . ILE   B 1 215 ? 12.94300  31.30200  -19.82500 1.000 45.42000  ? 181 ILE   B HG12   1 
ATOM   7164 H HG13   . ILE   B 1 215 ? 11.36500  31.44800  -19.68500 1.000 45.42000  ? 181 ILE   B HG13   1 
ATOM   7165 H HG21   . ILE   B 1 215 ? 13.58800  30.91000  -22.31200 1.000 38.31000  ? 181 ILE   B HG21   1 
ATOM   7166 H HG22   . ILE   B 1 215 ? 13.15200  32.09400  -23.27000 1.000 38.31000  ? 181 ILE   B HG22   1 
ATOM   7167 H HG23   . ILE   B 1 215 ? 14.02400  32.39600  -21.97500 1.000 38.31000  ? 181 ILE   B HG23   1 
ATOM   7168 H HD11   . ILE   B 1 215 ? 11.71100  29.27200  -19.74200 1.000 40.59000  ? 181 ILE   B HD11   1 
ATOM   7169 H HD12   . ILE   B 1 215 ? 11.21300  29.61500  -21.21200 1.000 40.59000  ? 181 ILE   B HD12   1 
ATOM   7170 H HD13   . ILE   B 1 215 ? 12.76000  29.38300  -20.93000 1.000 40.59000  ? 181 ILE   B HD13   1 
ATOM   7171 N N      . LEU   B 1 216 ? 11.21900  34.42500  -23.36100 1.000 33.42000  ? 182 LEU   B N      1 
ATOM   7172 C CA     . LEU   B 1 216 ? 11.45400  35.20700  -24.57300 1.000 31.73000  ? 182 LEU   B CA     1 
ATOM   7173 C C      . LEU   B 1 216 ? 11.70100  36.67700  -24.25800 1.000 32.36000  ? 182 LEU   B C      1 
ATOM   7174 O O      . LEU   B 1 216 ? 12.53800  37.32700  -24.89800 1.000 35.01000  ? 182 LEU   B O      1 
ATOM   7175 C CB     . LEU   B 1 216 ? 10.27000  35.06200  -25.53400 1.000 33.89000  ? 182 LEU   B CB     1 
ATOM   7176 C CG     . LEU   B 1 216 ? 10.17600  33.64400  -26.12700 1.000 35.88000  ? 182 LEU   B CG     1 
ATOM   7177 C CD1    . LEU   B 1 216 ? 8.83200   33.45600  -26.79800 1.000 39.14000  ? 182 LEU   B CD1    1 
ATOM   7178 C CD2    . LEU   B 1 216 ? 11.34100  33.39600  -27.11200 1.000 34.74000  ? 182 LEU   B CD2    1 
ATOM   7179 H H      . LEU   B 1 216 ? 10.46600  34.01100  -23.33300 1.000 33.42000  ? 182 LEU   B H      1 
ATOM   7180 H HA     . LEU   B 1 216 ? 12.24600  34.86500  -25.01600 1.000 31.73000  ? 182 LEU   B HA     1 
ATOM   7181 H HB2    . LEU   B 1 216 ? 9.44700   35.24400  -25.05400 1.000 33.89000  ? 182 LEU   B HB2    1 
ATOM   7182 H HB3    . LEU   B 1 216 ? 10.37600  35.69000  -26.26600 1.000 33.89000  ? 182 LEU   B HB3    1 
ATOM   7183 H HG     . LEU   B 1 216 ? 10.24600  32.99600  -25.40900 1.000 35.88000  ? 182 LEU   B HG     1 
ATOM   7184 H HD11   . LEU   B 1 216 ? 8.78400   32.55800  -27.16100 1.000 39.14000  ? 182 LEU   B HD11   1 
ATOM   7185 H HD12   . LEU   B 1 216 ? 8.13000   33.58500  -26.14100 1.000 39.14000  ? 182 LEU   B HD12   1 
ATOM   7186 H HD13   . LEU   B 1 216 ? 8.74200   34.10700  -27.51100 1.000 39.14000  ? 182 LEU   B HD13   1 
ATOM   7187 H HD21   . LEU   B 1 216 ? 11.16500  32.58100  -27.60800 1.000 34.74000  ? 182 LEU   B HD21   1 
ATOM   7188 H HD22   . LEU   B 1 216 ? 11.40300  34.14800  -27.72200 1.000 34.74000  ? 182 LEU   B HD22   1 
ATOM   7189 H HD23   . LEU   B 1 216 ? 12.16700  33.30700  -26.61100 1.000 34.74000  ? 182 LEU   B HD23   1 
ATOM   7190 N N      . ASN   B 1 217 ? 10.98000  37.22300  -23.28000 1.000 30.57000  ? 183 ASN   B N      1 
ATOM   7191 C CA     . ASN   B 1 217 ? 11.11900  38.64700  -22.97700 1.000 34.23000  ? 183 ASN   B CA     1 
ATOM   7192 C C      . ASN   B 1 217 ? 12.47000  38.99800  -22.37000 1.000 39.19000  ? 183 ASN   B C      1 
ATOM   7193 O O      . ASN   B 1 217 ? 12.80200  40.18600  -22.26800 1.000 34.88000  ? 183 ASN   B O      1 
ATOM   7194 C CB     . ASN   B 1 217 ? 9.97800   39.08200  -22.05200 1.000 34.29000  ? 183 ASN   B CB     1 
ATOM   7195 C CG     . ASN   B 1 217 ? 8.67000   39.24900  -22.80400 1.000 33.76000  ? 183 ASN   B CG     1 
ATOM   7196 O OD1    . ASN   B 1 217 ? 8.67600   39.54100  -23.99600 1.000 37.11000  ? 183 ASN   B OD1    1 
ATOM   7197 N ND2    . ASN   B 1 217 ? 7.54900   39.05800  -22.11900 1.000 34.66000  ? 183 ASN   B ND2    1 
ATOM   7198 H H      . ASN   B 1 217 ? 10.41500  36.80200  -22.78700 1.000 30.57000  ? 183 ASN   B H      1 
ATOM   7199 H HA     . ASN   B 1 217 ? 11.03600  39.14700  -23.80400 1.000 34.23000  ? 183 ASN   B HA     1 
ATOM   7200 H HB2    . ASN   B 1 217 ? 9.84900   38.40800  -21.36600 1.000 34.29000  ? 183 ASN   B HB2    1 
ATOM   7201 H HB3    . ASN   B 1 217 ? 10.20400  39.93300  -21.64600 1.000 34.29000  ? 183 ASN   B HB3    1 
ATOM   7202 H HD21   . ASN   B 1 217 ? 6.78700   39.14200  -22.50900 1.000 34.66000  ? 183 ASN   B HD21   1 
ATOM   7203 H HD22   . ASN   B 1 217 ? 7.58500   38.85300  -21.28500 1.000 34.66000  ? 183 ASN   B HD22   1 
ATOM   7204 N N      . GLN   B 1 218 ? 13.26600  38.00600  -21.99000 1.000 35.93000  ? 184 GLN   B N      1 
ATOM   7205 C CA     . GLN   B 1 218 ? 14.59300  38.24600  -21.44100 1.000 32.81000  ? 184 GLN   B CA     1 
ATOM   7206 C C      . GLN   B 1 218 ? 15.67800  38.27900  -22.49900 1.000 37.62000  ? 184 GLN   B C      1 
ATOM   7207 O O      . GLN   B 1 218 ? 16.83900  38.52200  -22.16300 1.000 38.57000  ? 184 GLN   B O      1 
ATOM   7208 C CB     . GLN   B 1 218 ? 14.91000  37.18100  -20.38800 1.000 40.81000  ? 184 GLN   B CB     1 
ATOM   7209 C CG     . GLN   B 1 218 ? 13.96400  37.25500  -19.20600 1.000 43.36000  ? 184 GLN   B CG     1 
ATOM   7210 C CD     . GLN   B 1 218 ? 14.45700  36.47300  -18.00800 1.000 63.30000  ? 184 GLN   B CD     1 
ATOM   7211 O OE1    . GLN   B 1 218 ? 14.99000  35.37200  -18.14500 1.000 57.67000  ? 184 GLN   B OE1    1 
ATOM   7212 N NE2    . GLN   B 1 218 ? 14.28400  37.04600  -16.81900 1.000 63.07000  ? 184 GLN   B NE2    1 
ATOM   7213 H H      . GLN   B 1 218 ? 13.05800  37.17300  -22.04000 1.000 35.93000  ? 184 GLN   B H      1 
ATOM   7214 H HA     . GLN   B 1 218 ? 14.59300  39.10700  -20.99500 1.000 32.81000  ? 184 GLN   B HA     1 
ATOM   7215 H HB2    . GLN   B 1 218 ? 14.82600  36.30200  -20.78900 1.000 40.81000  ? 184 GLN   B HB2    1 
ATOM   7216 H HB3    . GLN   B 1 218 ? 15.81400  37.31500  -20.06100 1.000 40.81000  ? 184 GLN   B HB3    1 
ATOM   7217 H HG2    . GLN   B 1 218 ? 13.86600  38.18200  -18.93800 1.000 43.36000  ? 184 GLN   B HG2    1 
ATOM   7218 H HG3    . GLN   B 1 218 ? 13.10500  36.89500  -19.46700 1.000 43.36000  ? 184 GLN   B HG3    1 
ATOM   7219 H HE21   . GLN   B 1 218 ? 13.90800  37.81700  -16.76400 1.000 63.07000  ? 184 GLN   B HE21   1 
ATOM   7220 H HE22   . GLN   B 1 218 ? 14.54700  36.64400  -16.10600 1.000 63.07000  ? 184 GLN   B HE22   1 
ATOM   7221 N N      . PHE   B 1 219 ? 15.33400  38.06200  -23.76600 1.000 33.25000  ? 185 PHE   B N      1 
ATOM   7222 C CA     . PHE   B 1 219 ? 16.31700  38.06600  -24.85000 1.000 31.63000  ? 185 PHE   B CA     1 
ATOM   7223 C C      . PHE   B 1 219 ? 15.98200  39.16900  -25.83400 1.000 39.17000  ? 185 PHE   B C      1 
ATOM   7224 O O      . PHE   B 1 219 ? 15.09100  39.00400  -26.68800 1.000 33.85000  ? 185 PHE   B O      1 
ATOM   7225 C CB     . PHE   B 1 219 ? 16.36700  36.69900  -25.52800 1.000 33.61000  ? 185 PHE   B CB     1 
ATOM   7226 C CG     . PHE   B 1 219 ? 16.92800  35.63300  -24.63700 1.000 33.57000  ? 185 PHE   B CG     1 
ATOM   7227 C CD1    . PHE   B 1 219 ? 18.30700  35.46700  -24.52300 1.000 36.31000  ? 185 PHE   B CD1    1 
ATOM   7228 C CD2    . PHE   B 1 219 ? 16.08700  34.83100  -23.86900 1.000 33.94000  ? 185 PHE   B CD2    1 
ATOM   7229 C CE1    . PHE   B 1 219 ? 18.83100  34.49800  -23.67300 1.000 38.61000  ? 185 PHE   B CE1    1 
ATOM   7230 C CE2    . PHE   B 1 219 ? 16.60900  33.85900  -23.02400 1.000 38.48000  ? 185 PHE   B CE2    1 
ATOM   7231 C CZ     . PHE   B 1 219 ? 17.97200  33.68600  -22.92800 1.000 38.33000  ? 185 PHE   B CZ     1 
ATOM   7232 H H      . PHE   B 1 219 ? 14.53000  37.90800  -24.02900 1.000 33.25000  ? 185 PHE   B H      1 
ATOM   7233 H HA     . PHE   B 1 219 ? 17.19600  38.21700  -24.47800 1.000 31.63000  ? 185 PHE   B HA     1 
ATOM   7234 H HB2    . PHE   B 1 219 ? 15.46700  36.43700  -25.77900 1.000 33.61000  ? 185 PHE   B HB2    1 
ATOM   7235 H HB3    . PHE   B 1 219 ? 16.92900  36.75700  -26.31700 1.000 33.61000  ? 185 PHE   B HB3    1 
ATOM   7236 H HD1    . PHE   B 1 219 ? 18.88000  36.00400  -25.02100 1.000 36.31000  ? 185 PHE   B HD1    1 
ATOM   7237 H HD2    . PHE   B 1 219 ? 15.16500  34.93900  -23.93200 1.000 33.94000  ? 185 PHE   B HD2    1 
ATOM   7238 H HE1    . PHE   B 1 219 ? 19.75200  34.38200  -23.61100 1.000 38.61000  ? 185 PHE   B HE1    1 
ATOM   7239 H HE2    . PHE   B 1 219 ? 16.03700  33.32100  -22.52600 1.000 38.48000  ? 185 PHE   B HE2    1 
ATOM   7240 H HZ     . PHE   B 1 219 ? 18.32000  33.03600  -22.36100 1.000 38.33000  ? 185 PHE   B HZ     1 
ATOM   7241 N N      . PRO   B 1 220 ? 16.64800  40.31700  -25.73100 1.000 34.97000  ? 186 PRO   B N      1 
ATOM   7242 C CA     . PRO   B 1 220 ? 16.28600  41.46200  -26.58000 1.000 34.19000  ? 186 PRO   B CA     1 
ATOM   7243 C C      . PRO   B 1 220 ? 16.51100  41.21100  -28.05200 1.000 37.03000  ? 186 PRO   B C      1 
ATOM   7244 O O      . PRO   B 1 220 ? 15.87500  41.87100  -28.87000 1.000 34.29000  ? 186 PRO   B O      1 
ATOM   7245 C CB     . PRO   B 1 220 ? 17.18200  42.60200  -26.06200 1.000 35.11000  ? 186 PRO   B CB     1 
ATOM   7246 C CG     . PRO   B 1 220 ? 18.16300  42.00100  -25.13400 1.000 33.61000  ? 186 PRO   B CG     1 
ATOM   7247 C CD     . PRO   B 1 220 ? 17.71700  40.61400  -24.75700 1.000 36.96000  ? 186 PRO   B CD     1 
ATOM   7248 H HA     . PRO   B 1 220 ? 15.35700  41.70100  -26.43800 1.000 34.19000  ? 186 PRO   B HA     1 
ATOM   7249 H HB2    . PRO   B 1 220 ? 17.63800  43.01700  -26.81100 1.000 35.11000  ? 186 PRO   B HB2    1 
ATOM   7250 H HB3    . PRO   B 1 220 ? 16.63500  43.25400  -25.59700 1.000 35.11000  ? 186 PRO   B HB3    1 
ATOM   7251 H HG2    . PRO   B 1 220 ? 19.02600  41.96000  -25.57400 1.000 33.61000  ? 186 PRO   B HG2    1 
ATOM   7252 H HG3    . PRO   B 1 220 ? 18.22400  42.55500  -24.34000 1.000 33.61000  ? 186 PRO   B HG3    1 
ATOM   7253 H HD2    . PRO   B 1 220 ? 18.45200  39.98900  -24.85800 1.000 36.96000  ? 186 PRO   B HD2    1 
ATOM   7254 H HD3    . PRO   B 1 220 ? 17.36400  40.60600  -23.85400 1.000 36.96000  ? 186 PRO   B HD3    1 
ATOM   7255 N N      . LYS   B 1 221 ? 17.38500  40.28000  -28.43100 1.000 32.91000  ? 187 LYS   B N      1 
ATOM   7256 C CA     . LYS   B 1 221 ? 17.58000  40.01600  -29.85300 1.000 32.55000  ? 187 LYS   B CA     1 
ATOM   7257 C C      . LYS   B 1 221 ? 16.44000  39.22000  -30.46600 1.000 32.81000  ? 187 LYS   B C      1 
ATOM   7258 O O      . LYS   B 1 221 ? 16.32600  39.17900  -31.69300 1.000 35.33000  ? 187 LYS   B O      1 
ATOM   7259 C CB     . LYS   B 1 221 ? 18.89000  39.27800  -30.08600 1.000 34.42000  ? 187 LYS   B CB     1 
ATOM   7260 C CG     . LYS   B 1 221 ? 20.10000  40.17500  -29.91600 1.000 34.69000  ? 187 LYS   B CG     1 
ATOM   7261 C CD     . LYS   B 1 221 ? 21.35100  39.34000  -29.76900 1.000 36.15000  ? 187 LYS   B CD     1 
ATOM   7262 C CE     . LYS   B 1 221 ? 22.58900  40.19600  -29.98600 1.000 36.35000  ? 187 LYS   B CE     1 
ATOM   7263 N NZ     . LYS   B 1 221 ? 23.78700  39.33100  -29.86400 1.000 40.13000  ? 187 LYS   B NZ     1 
ATOM   7264 H H      . LYS   B 1 221 ? 17.86400  39.80100  -27.90100 1.000 32.91000  ? 187 LYS   B H      1 
ATOM   7265 H HA     . LYS   B 1 221 ? 17.63200  40.86400  -30.32200 1.000 32.55000  ? 187 LYS   B HA     1 
ATOM   7266 H HB2    . LYS   B 1 221 ? 18.96200  38.55100  -29.44700 1.000 34.42000  ? 187 LYS   B HB2    1 
ATOM   7267 H HB3    . LYS   B 1 221 ? 18.90000  38.92800  -30.99100 1.000 34.42000  ? 187 LYS   B HB3    1 
ATOM   7268 H HG2    . LYS   B 1 221 ? 20.19700  40.74100  -30.69800 1.000 34.69000  ? 187 LYS   B HG2    1 
ATOM   7269 H HG3    . LYS   B 1 221 ? 19.99400  40.71500  -29.11700 1.000 34.69000  ? 187 LYS   B HG3    1 
ATOM   7270 H HD2    . LYS   B 1 221 ? 21.38800  38.96700  -28.87400 1.000 36.15000  ? 187 LYS   B HD2    1 
ATOM   7271 H HD3    . LYS   B 1 221 ? 21.34700  38.63200  -30.43200 1.000 36.15000  ? 187 LYS   B HD3    1 
ATOM   7272 H HE2    . LYS   B 1 221 ? 22.57100  40.58200  -30.87600 1.000 36.35000  ? 187 LYS   B HE2    1 
ATOM   7273 H HE3    . LYS   B 1 221 ? 22.63300  40.88900  -29.30900 1.000 36.35000  ? 187 LYS   B HE3    1 
ATOM   7274 H HZ1    . LYS   B 1 221 ? 24.52400  39.81400  -29.98800 1.000 40.13000  ? 187 LYS   B HZ1    1 
ATOM   7275 H HZ2    . LYS   B 1 221 ? 23.81500  38.96300  -29.05400 1.000 40.13000  ? 187 LYS   B HZ2    1 
ATOM   7276 H HZ3    . LYS   B 1 221 ? 23.75800  38.68400  -30.47500 1.000 40.13000  ? 187 LYS   B HZ3    1 
ATOM   7277 N N      . VAL   B 1 222 ? 15.60600  38.57500  -29.65800 1.000 30.98000  ? 188 VAL   B N      1 
ATOM   7278 C CA     . VAL   B 1 222 ? 14.43300  37.92300  -30.22400 1.000 29.96000  ? 188 VAL   B CA     1 
ATOM   7279 C C      . VAL   B 1 222 ? 13.44300  39.01600  -30.59800 1.000 36.98000  ? 188 VAL   B C      1 
ATOM   7280 O O      . VAL   B 1 222 ? 12.81500  39.62500  -29.72700 1.000 36.01000  ? 188 VAL   B O      1 
ATOM   7281 C CB     . VAL   B 1 222 ? 13.81100  36.90800  -29.26600 1.000 33.54000  ? 188 VAL   B CB     1 
ATOM   7282 C CG1    . VAL   B 1 222 ? 12.55300  36.32700  -29.89700 1.000 33.29000  ? 188 VAL   B CG1    1 
ATOM   7283 C CG2    . VAL   B 1 222 ? 14.80000  35.79800  -28.97200 1.000 34.78000  ? 188 VAL   B CG2    1 
ATOM   7284 H H      . VAL   B 1 222 ? 15.69200  38.50100  -28.80600 1.000 30.98000  ? 188 VAL   B H      1 
ATOM   7285 H HA     . VAL   B 1 222 ? 14.68800  37.45400  -31.03400 1.000 29.96000  ? 188 VAL   B HA     1 
ATOM   7286 H HB     . VAL   B 1 222 ? 13.57200  37.34400  -28.43300 1.000 33.54000  ? 188 VAL   B HB     1 
ATOM   7287 H HG11   . VAL   B 1 222 ? 12.27500  35.55200  -29.38500 1.000 33.29000  ? 188 VAL   B HG11   1 
ATOM   7288 H HG12   . VAL   B 1 222 ? 11.85100  36.99600  -29.88900 1.000 33.29000  ? 188 VAL   B HG12   1 
ATOM   7289 H HG13   . VAL   B 1 222 ? 12.75100  36.06400  -30.80900 1.000 33.29000  ? 188 VAL   B HG13   1 
ATOM   7290 H HG21   . VAL   B 1 222 ? 14.38100  35.15000  -28.38300 1.000 34.78000  ? 188 VAL   B HG21   1 
ATOM   7291 H HG22   . VAL   B 1 222 ? 15.05300  35.37200  -29.80600 1.000 34.78000  ? 188 VAL   B HG22   1 
ATOM   7292 H HG23   . VAL   B 1 222 ? 15.58300  36.17800  -28.54300 1.000 34.78000  ? 188 VAL   B HG23   1 
ATOM   7293 N N      A GLN   B 1 223 ? 13.30900  39.27700  -31.89700 0.550 30.75000  ? 189 GLN   B N      1 
ATOM   7294 N N      B GLN   B 1 223 ? 13.31000  39.26400  -31.90100 0.450 30.80000  ? 189 GLN   B N      1 
ATOM   7295 C CA     A GLN   B 1 223 ? 12.42900  40.34000  -32.35900 0.550 30.94000  ? 189 GLN   B CA     1 
ATOM   7296 C CA     B GLN   B 1 223 ? 12.46500  40.32900  -32.42300 0.450 30.96000  ? 189 GLN   B CA     1 
ATOM   7297 C C      A GLN   B 1 223 ? 11.09300  39.84400  -32.91000 0.550 33.15000  ? 189 GLN   B C      1 
ATOM   7298 C C      B GLN   B 1 223 ? 11.11400  39.84800  -32.94500 0.450 33.19000  ? 189 GLN   B C      1 
ATOM   7299 O O      A GLN   B 1 223 ? 10.17100  40.65300  -33.05800 0.550 33.98000  ? 189 GLN   B O      1 
ATOM   7300 O O      B GLN   B 1 223 ? 10.21200  40.67300  -33.12200 0.450 33.96000  ? 189 GLN   B O      1 
ATOM   7301 C CB     A GLN   B 1 223 ? 13.14700  41.19000  -33.41400 0.550 35.40000  ? 189 GLN   B CB     1 
ATOM   7302 C CB     B GLN   B 1 223 ? 13.20200  41.06600  -33.54500 0.450 35.53000  ? 189 GLN   B CB     1 
ATOM   7303 C CG     A GLN   B 1 223 ? 12.34200  42.37300  -33.90700 0.550 43.10000  ? 189 GLN   B CG     1 
ATOM   7304 C CG     B GLN   B 1 223 ? 13.74000  40.12600  -34.62500 0.450 34.48000  ? 189 GLN   B CG     1 
ATOM   7305 C CD     A GLN   B 1 223 ? 11.73000  43.16600  -32.76800 0.550 52.85000  ? 189 GLN   B CD     1 
ATOM   7306 C CD     B GLN   B 1 223 ? 14.42500  40.86200  -35.75600 0.450 41.22000  ? 189 GLN   B CD     1 
ATOM   7307 O OE1    A GLN   B 1 223 ? 10.51600  43.38900  -32.73700 0.550 35.63000  ? 189 GLN   B OE1    1 
ATOM   7308 O OE1    B GLN   B 1 223 ? 14.62700  42.07500  -35.68800 0.450 45.21000  ? 189 GLN   B OE1    1 
ATOM   7309 N NE2    A GLN   B 1 223 ? 12.56700  43.59300  -31.82000 0.550 50.16000  ? 189 GLN   B NE2    1 
ATOM   7310 N NE2    B GLN   B 1 223 ? 14.78400  40.13000  -36.81100 0.450 27.70000  ? 189 GLN   B NE2    1 
ATOM   7311 H H      A GLN   B 1 223 ? 13.71500  38.85400  -32.52600 0.550 30.80000  ? 189 GLN   B H      1 
ATOM   7312 H H      B GLN   B 1 223 ? 13.70600  38.80700  -32.51000 0.450 30.80000  ? 189 GLN   B H      1 
ATOM   7313 H HA     A GLN   B 1 223 ? 12.23200  40.91400  -31.60300 0.550 30.96000  ? 189 GLN   B HA     1 
ATOM   7314 H HA     B GLN   B 1 223 ? 12.29500  40.96800  -31.71300 0.450 30.96000  ? 189 GLN   B HA     1 
ATOM   7315 H HB2    A GLN   B 1 223 ? 13.97000  41.53200  -33.03100 0.550 35.53000  ? 189 GLN   B HB2    1 
ATOM   7316 H HB2    B GLN   B 1 223 ? 12.59000  41.68900  -33.96800 0.450 35.53000  ? 189 GLN   B HB2    1 
ATOM   7317 H HB3    A GLN   B 1 223 ? 13.34900  40.63000  -34.18000 0.550 35.53000  ? 189 GLN   B HB3    1 
ATOM   7318 H HB3    B GLN   B 1 223 ? 13.95400  41.54700  -33.16500 0.450 35.53000  ? 189 GLN   B HB3    1 
ATOM   7319 H HG2    A GLN   B 1 223 ? 12.92300  42.96600  -34.40900 0.550 34.48000  ? 189 GLN   B HG2    1 
ATOM   7320 H HG2    B GLN   B 1 223 ? 14.39600  39.53200  -34.23200 0.450 34.48000  ? 189 GLN   B HG2    1 
ATOM   7321 H HG3    A GLN   B 1 223 ? 11.62200  42.05400  -34.47200 0.550 34.48000  ? 189 GLN   B HG3    1 
ATOM   7322 H HG3    B GLN   B 1 223 ? 13.00600  39.61400  -34.99600 0.450 34.48000  ? 189 GLN   B HG3    1 
ATOM   7323 H HE21   A GLN   B 1 223 ? 13.40700  43.41700  -31.87700 0.550 27.70000  ? 189 GLN   B HE21   1 
ATOM   7324 H HE21   B GLN   B 1 223 ? 14.62500  39.28500  -36.82200 0.450 27.70000  ? 189 GLN   B HE21   1 
ATOM   7325 H HE22   A GLN   B 1 223 ? 12.26700  44.04600  -31.15400 0.550 27.70000  ? 189 GLN   B HE22   1 
ATOM   7326 H HE22   B GLN   B 1 223 ? 15.17600  40.50300  -37.48000 0.450 27.70000  ? 189 GLN   B HE22   1 
ATOM   7327 N N      . PHE   B 1 224 ? 10.95200  38.55700  -33.22200 1.000 31.43000  ? 190 PHE   B N      1 
ATOM   7328 C CA     . PHE   B 1 224 ? 9.65500   38.05500  -33.65200 1.000 24.52000  ? 190 PHE   B CA     1 
ATOM   7329 C C      . PHE   B 1 224 ? 9.51800   36.60500  -33.23400 1.000 30.69000  ? 190 PHE   B C      1 
ATOM   7330 O O      . PHE   B 1 224 ? 10.50400  35.89900  -33.02600 1.000 29.28000  ? 190 PHE   B O      1 
ATOM   7331 C CB     . PHE   B 1 224 ? 9.38800   38.22800  -35.18000 1.000 31.95000  ? 190 PHE   B CB     1 
ATOM   7332 C CG     . PHE   B 1 224 ? 10.25300  37.36400  -36.10000 1.000 28.73000  ? 190 PHE   B CG     1 
ATOM   7333 C CD1    . PHE   B 1 224 ? 11.47400  37.83300  -36.59100 1.000 30.25000  ? 190 PHE   B CD1    1 
ATOM   7334 C CD2    . PHE   B 1 224 ? 9.82300   36.10200  -36.50400 1.000 28.35000  ? 190 PHE   B CD2    1 
ATOM   7335 C CE1    . PHE   B 1 224 ? 12.27000  37.05800  -37.45300 1.000 32.46000  ? 190 PHE   B CE1    1 
ATOM   7336 C CE2    . PHE   B 1 224 ? 10.61200  35.32200  -37.37500 1.000 30.53000  ? 190 PHE   B CE2    1 
ATOM   7337 C CZ     . PHE   B 1 224 ? 11.83300  35.80600  -37.85000 1.000 31.33000  ? 190 PHE   B CZ     1 
ATOM   7338 H H      A PHE   B 1 224 ? 11.57800  37.96800  -33.19400 0.550 31.43000  ? 190 PHE   B H      1 
ATOM   7339 H H      B PHE   B 1 224 ? 11.56900  37.96000  -33.16900 0.450 31.43000  ? 190 PHE   B H      1 
ATOM   7340 H HA     . PHE   B 1 224 ? 8.97600   38.55600  -33.18100 1.000 24.52000  ? 190 PHE   B HA     1 
ATOM   7341 H HB2    . PHE   B 1 224 ? 8.46100   38.00400  -35.35700 1.000 31.95000  ? 190 PHE   B HB2    1 
ATOM   7342 H HB3    . PHE   B 1 224 ? 9.54800   39.15500  -35.41700 1.000 31.95000  ? 190 PHE   B HB3    1 
ATOM   7343 H HD1    . PHE   B 1 224 ? 11.77100  38.67600  -36.33500 1.000 30.25000  ? 190 PHE   B HD1    1 
ATOM   7344 H HD2    . PHE   B 1 224 ? 9.00800   35.77200  -36.19900 1.000 28.35000  ? 190 PHE   B HD2    1 
ATOM   7345 H HE1    . PHE   B 1 224 ? 13.08100  37.39000  -37.76400 1.000 32.46000  ? 190 PHE   B HE1    1 
ATOM   7346 H HE2    . PHE   B 1 224 ? 10.31800  34.47800  -37.63300 1.000 30.53000  ? 190 PHE   B HE2    1 
ATOM   7347 H HZ     . PHE   B 1 224 ? 12.35600  35.28500  -38.41600 1.000 31.33000  ? 190 PHE   B HZ     1 
ATOM   7348 N N      . ILE   B 1 225 ? 8.26600   36.20400  -33.06000 1.000 26.41000  ? 191 ILE   B N      1 
ATOM   7349 C CA     . ILE   B 1 225 ? 7.88500   34.87500  -32.60600 1.000 27.99000  ? 191 ILE   B CA     1 
ATOM   7350 C C      . ILE   B 1 225 ? 6.90900   34.34400  -33.64100 1.000 29.62000  ? 191 ILE   B C      1 
ATOM   7351 O O      . ILE   B 1 225 ? 5.87600   34.97800  -33.89600 1.000 28.45000  ? 191 ILE   B O      1 
ATOM   7352 C CB     . ILE   B 1 225 ? 7.21500   34.91900  -31.21300 1.000 29.63000  ? 191 ILE   B CB     1 
ATOM   7353 C CG1    . ILE   B 1 225 ? 8.07100   35.70200  -30.19800 1.000 33.91000  ? 191 ILE   B CG1    1 
ATOM   7354 C CG2    . ILE   B 1 225 ? 6.87500   33.50300  -30.70200 1.000 29.89000  ? 191 ILE   B CG2    1 
ATOM   7355 C CD1    . ILE   B 1 225 ? 7.31100   36.11000  -28.89400 1.000 35.90000  ? 191 ILE   B CD1    1 
ATOM   7356 H H      . ILE   B 1 225 ? 7.58700   36.71100  -33.20700 1.000 26.41000  ? 191 ILE   B H      1 
ATOM   7357 H HA     . ILE   B 1 225 ? 8.66100   34.29500  -32.57000 1.000 27.99000  ? 191 ILE   B HA     1 
ATOM   7358 H HB     . ILE   B 1 225 ? 6.37700   35.39800  -31.31200 1.000 29.63000  ? 191 ILE   B HB     1 
ATOM   7359 H HG12   . ILE   B 1 225 ? 8.82600   35.15100  -29.93800 1.000 33.91000  ? 191 ILE   B HG12   1 
ATOM   7360 H HG13   . ILE   B 1 225 ? 8.39000   36.51800  -30.61300 1.000 33.91000  ? 191 ILE   B HG13   1 
ATOM   7361 H HG21   . ILE   B 1 225 ? 6.45000   33.57300  -29.83300 1.000 29.89000  ? 191 ILE   B HG21   1 
ATOM   7362 H HG22   . ILE   B 1 225 ? 6.27300   33.07400  -31.33000 1.000 29.89000  ? 191 ILE   B HG22   1 
ATOM   7363 H HG23   . ILE   B 1 225 ? 7.69600   32.99200  -30.62900 1.000 29.89000  ? 191 ILE   B HG23   1 
ATOM   7364 H HD11   . ILE   B 1 225 ? 7.94700   36.47900  -28.26300 1.000 35.90000  ? 191 ILE   B HD11   1 
ATOM   7365 H HD12   . ILE   B 1 225 ? 6.63900   36.77400  -29.11500 1.000 35.90000  ? 191 ILE   B HD12   1 
ATOM   7366 H HD13   . ILE   B 1 225 ? 6.88900   35.32400  -28.51300 1.000 35.90000  ? 191 ILE   B HD13   1 
ATOM   7367 N N      . THR   B 1 226 ? 7.20300   33.18300  -34.22900 1.000 30.31000  ? 192 THR   B N      1 
ATOM   7368 C CA     . THR   B 1 226 ? 6.28000   32.58200  -35.18400 1.000 26.86000  ? 192 THR   B CA     1 
ATOM   7369 C C      . THR   B 1 226 ? 5.46100   31.48900  -34.50700 1.000 29.43000  ? 192 THR   B C      1 
ATOM   7370 O O      . THR   B 1 226 ? 6.01900   30.48600  -34.05200 1.000 29.29000  ? 192 THR   B O      1 
ATOM   7371 C CB     . THR   B 1 226 ? 7.01100   32.00400  -36.39500 1.000 29.89000  ? 192 THR   B CB     1 
ATOM   7372 O OG1    . THR   B 1 226 ? 7.74900   33.05400  -37.02800 1.000 29.10000  ? 192 THR   B OG1    1 
ATOM   7373 C CG2    . THR   B 1 226 ? 5.99600   31.44100  -37.38800 1.000 29.39000  ? 192 THR   B CG2    1 
ATOM   7374 H H      . THR   B 1 226 ? 7.92200   32.73100  -34.09300 1.000 30.31000  ? 192 THR   B H      1 
ATOM   7375 H HA     . THR   B 1 226 ? 5.66600   33.26000  -35.50500 1.000 26.86000  ? 192 THR   B HA     1 
ATOM   7376 H HB     . THR   B 1 226 ? 7.61100   31.29500  -36.11800 1.000 29.89000  ? 192 THR   B HB     1 
ATOM   7377 H HG1    . THR   B 1 226 ? 8.15800   32.75400  -37.69700 1.000 29.10000  ? 192 THR   B HG1    1 
ATOM   7378 H HG21   . THR   B 1 226 ? 6.42800   31.27200  -38.24000 1.000 29.39000  ? 192 THR   B HG21   1 
ATOM   7379 H HG22   . THR   B 1 226 ? 5.62600   30.60900  -37.05400 1.000 29.39000  ? 192 THR   B HG22   1 
ATOM   7380 H HG23   . THR   B 1 226 ? 5.27600   32.07700  -37.52200 1.000 29.39000  ? 192 THR   B HG23   1 
ATOM   7381 N N      . CYS   B 1 227 ? 4.14100   31.67200  -34.48300 1.000 24.95000  ? 193 CYS   B N      1 
ATOM   7382 C CA     . CYS   B 1 227 ? 3.19400   30.71900  -33.91100 1.000 27.34000  ? 193 CYS   B CA     1 
ATOM   7383 C C      . CYS   B 1 227 ? 2.27000   30.29400  -35.04000 1.000 28.71000  ? 193 CYS   B C      1 
ATOM   7384 O O      . CYS   B 1 227 ? 1.51800   31.13200  -35.55100 1.000 27.93000  ? 193 CYS   B O      1 
ATOM   7385 C CB     . CYS   B 1 227 ? 2.38200   31.37600  -32.78500 1.000 29.80000  ? 193 CYS   B CB     1 
ATOM   7386 S SG     . CYS   B 1 227 ? 3.36900   32.11900  -31.47900 1.000 32.02000  ? 193 CYS   B SG     1 
ATOM   7387 H H      . CYS   B 1 227 ? 3.75700   32.37100  -34.80600 1.000 24.95000  ? 193 CYS   B H      1 
ATOM   7388 H HA     . CYS   B 1 227 ? 3.67800   29.97600  -33.53500 1.000 27.34000  ? 193 CYS   B HA     1 
ATOM   7389 H HB2    . CYS   B 1 227 ? 1.83000   32.07500  -33.16900 1.000 29.80000  ? 193 CYS   B HB2    1 
ATOM   7390 H HB3    . CYS   B 1 227 ? 1.81700   30.70100  -32.37900 1.000 29.80000  ? 193 CYS   B HB3    1 
ATOM   7391 H HG     . CYS   B 1 227 ? 2.62900   32.64300  -30.69400 1.000 32.02000  ? 193 CYS   B HG     1 
ATOM   7392 N N      . ILE   B 1 228 ? 2.29600   29.01300  -35.44200 1.000 24.90000  ? 194 ILE   B N      1 
ATOM   7393 C CA     . ILE   B 1 228 ? 2.89100   27.86400  -34.75100 1.000 23.71000  ? 194 ILE   B CA     1 
ATOM   7394 C C      . ILE   B 1 228 ? 3.51500   26.90700  -35.76900 1.000 28.00000  ? 194 ILE   B C      1 
ATOM   7395 O O      . ILE   B 1 228 ? 3.14700   26.90300  -36.94800 1.000 26.59000  ? 194 ILE   B O      1 
ATOM   7396 C CB     . ILE   B 1 228 ? 1.83600   27.09000  -33.94800 1.000 25.41000  ? 194 ILE   B CB     1 
ATOM   7397 C CG1    . ILE   B 1 228 ? 0.66000   26.72300  -34.87800 1.000 27.04000  ? 194 ILE   B CG1    1 
ATOM   7398 C CG2    . ILE   B 1 228 ? 1.38300   27.89400  -32.73700 1.000 29.45000  ? 194 ILE   B CG2    1 
ATOM   7399 C CD1    . ILE   B 1 228 ? -0.28600  25.60500  -34.34200 1.000 30.83000  ? 194 ILE   B CD1    1 
ATOM   7400 H H      . ILE   B 1 228 ? 1.93800   28.77200  -36.18600 1.000 24.90000  ? 194 ILE   B H      1 
ATOM   7401 H HA     . ILE   B 1 228 ? 3.59600   28.12800  -34.14800 1.000 23.71000  ? 194 ILE   B HA     1 
ATOM   7402 H HB     . ILE   B 1 228 ? 2.24000   26.26700  -33.63100 1.000 25.41000  ? 194 ILE   B HB     1 
ATOM   7403 H HG12   . ILE   B 1 228 ? 0.12000   27.51700  -35.01500 1.000 27.04000  ? 194 ILE   B HG12   1 
ATOM   7404 H HG13   . ILE   B 1 228 ? 1.00500   26.41800  -35.73100 1.000 27.04000  ? 194 ILE   B HG13   1 
ATOM   7405 H HG21   . ILE   B 1 228 ? 0.77800   27.35200  -32.20700 1.000 29.45000  ? 194 ILE   B HG21   1 
ATOM   7406 H HG22   . ILE   B 1 228 ? 2.16100   28.13500  -32.20900 1.000 29.45000  ? 194 ILE   B HG22   1 
ATOM   7407 H HG23   . ILE   B 1 228 ? 0.92900   28.69500  -33.04300 1.000 29.45000  ? 194 ILE   B HG23   1 
ATOM   7408 H HD11   . ILE   B 1 228 ? -0.98800  25.44700  -34.99300 1.000 30.83000  ? 194 ILE   B HD11   1 
ATOM   7409 H HD12   . ILE   B 1 228 ? 0.22900   24.79400  -34.20700 1.000 30.83000  ? 194 ILE   B HD12   1 
ATOM   7410 H HD13   . ILE   B 1 228 ? -0.67300  25.89600  -33.50100 1.000 30.83000  ? 194 ILE   B HD13   1 
ATOM   7411 N N      . ASN   B 1 229 ? 4.44800   26.08700  -35.29800 1.000 29.93000  ? 195 ASN   B N      1 
ATOM   7412 C CA     . ASN   B 1 229 ? 4.80900   24.86000  -35.99400 1.000 25.28000  ? 195 ASN   B CA     1 
ATOM   7413 C C      . ASN   B 1 229 ? 3.63500   23.87500  -35.93700 1.000 30.00000  ? 195 ASN   B C      1 
ATOM   7414 O O      . ASN   B 1 229 ? 2.59500   24.13600  -35.32600 1.000 29.31000  ? 195 ASN   B O      1 
ATOM   7415 C CB     . ASN   B 1 229 ? 6.06700   24.26700  -35.36900 1.000 25.89000  ? 195 ASN   B CB     1 
ATOM   7416 C CG     . ASN   B 1 229 ? 6.96700   23.60700  -36.39700 1.000 34.80000  ? 195 ASN   B CG     1 
ATOM   7417 O OD1    . ASN   B 1 229 ? 6.49900   22.90600  -37.29900 1.000 32.23000  ? 195 ASN   B OD1    1 
ATOM   7418 N ND2    . ASN   B 1 229 ? 8.27000   23.84900  -36.27700 1.000 33.75000  ? 195 ASN   B ND2    1 
ATOM   7419 H H      . ASN   B 1 229 ? 4.88900   26.22100  -34.57200 1.000 29.93000  ? 195 ASN   B H      1 
ATOM   7420 H HA     . ASN   B 1 229 ? 4.99900   25.05800  -36.92300 1.000 25.28000  ? 195 ASN   B HA     1 
ATOM   7421 H HB2    . ASN   B 1 229 ? 6.57200   24.97400  -34.93800 1.000 25.89000  ? 195 ASN   B HB2    1 
ATOM   7422 H HB3    . ASN   B 1 229 ? 5.81100   23.59600  -34.71700 1.000 25.89000  ? 195 ASN   B HB3    1 
ATOM   7423 H HD21   . ASN   B 1 229 ? 8.82500   23.50100  -36.83400 1.000 33.75000  ? 195 ASN   B HD21   1 
ATOM   7424 H HD22   . ASN   B 1 229 ? 8.55800   24.34600  -35.63700 1.000 33.75000  ? 195 ASN   B HD22   1 
ATOM   7425 N N      A SER   B 1 230 ? 3.79600   22.72900  -36.59600 0.690 30.73000  ? 196 SER   B N      1 
ATOM   7426 N N      B SER   B 1 230 ? 3.81600   22.71800  -36.57100 0.310 30.73000  ? 196 SER   B N      1 
ATOM   7427 C CA     A SER   B 1 230 ? 2.72600   21.74100  -36.62600 0.690 29.30000  ? 196 SER   B CA     1 
ATOM   7428 C CA     B SER   B 1 230 ? 2.77100   21.70300  -36.59900 0.310 29.46000  ? 196 SER   B CA     1 
ATOM   7429 C C      A SER   B 1 230 ? 2.37300   21.27200  -35.21300 0.690 32.24000  ? 196 SER   B C      1 
ATOM   7430 C C      B SER   B 1 230 ? 2.37300   21.28200  -35.18800 0.310 32.11000  ? 196 SER   B C      1 
ATOM   7431 O O      A SER   B 1 230 ? 3.18300   21.34800  -34.28400 0.690 31.82000  ? 196 SER   B O      1 
ATOM   7432 O O      B SER   B 1 230 ? 3.15800   21.37700  -34.24000 0.310 31.80000  ? 196 SER   B O      1 
ATOM   7433 C CB     A SER   B 1 230 ? 3.13200   20.55100  -37.50000 0.690 33.43000  ? 196 SER   B CB     1 
ATOM   7434 C CB     B SER   B 1 230 ? 3.24400   20.47900  -37.38100 0.310 33.11000  ? 196 SER   B CB     1 
ATOM   7435 O OG     A SER   B 1 230 ? 4.45200   20.13800  -37.22500 0.690 32.00000  ? 196 SER   B OG     1 
ATOM   7436 O OG     B SER   B 1 230 ? 3.58200   20.82300  -38.70800 0.310 29.70000  ? 196 SER   B OG     1 
ATOM   7437 H H      A SER   B 1 230 ? 4.50500   22.50400  -37.02700 0.690 30.73000  ? 196 SER   B H      1 
ATOM   7438 H H      B SER   B 1 230 ? 4.53400   22.49900  -36.99100 0.310 30.73000  ? 196 SER   B H      1 
ATOM   7439 H HA     A SER   B 1 230 ? 1.93400   22.14400  -37.01500 0.690 29.46000  ? 196 SER   B HA     1 
ATOM   7440 H HA     B SER   B 1 230 ? 1.98700   22.06300  -37.04200 0.310 29.46000  ? 196 SER   B HA     1 
ATOM   7441 H HB2    A SER   B 1 230 ? 2.52700   19.81200  -37.33100 0.690 33.11000  ? 196 SER   B HB2    1 
ATOM   7442 H HB2    B SER   B 1 230 ? 4.02600   20.10800  -36.94300 0.310 33.11000  ? 196 SER   B HB2    1 
ATOM   7443 H HB3    A SER   B 1 230 ? 3.08000   20.81700  -38.42800 0.690 33.11000  ? 196 SER   B HB3    1 
ATOM   7444 H HB3    B SER   B 1 230 ? 2.53100   19.82100  -37.39800 0.310 33.11000  ? 196 SER   B HB3    1 
ATOM   7445 H HG     A SER   B 1 230 ? 4.65600   19.48600  -37.71300 0.690 29.70000  ? 196 SER   B HG     1 
ATOM   7446 H HG     B SER   B 1 230 ? 3.84000   20.14100  -39.12500 0.310 29.70000  ? 196 SER   B HG     1 
ATOM   7447 N N      . ILE   B 1 231 ? 1.13400   20.81500  -35.05300 1.000 26.96000  ? 197 ILE   B N      1 
ATOM   7448 C CA     . ILE   B 1 231 ? 0.70700   20.15300  -33.82300 1.000 28.34000  ? 197 ILE   B CA     1 
ATOM   7449 C C      . ILE   B 1 231 ? 1.31900   18.75700  -33.85200 1.000 27.01000  ? 197 ILE   B C      1 
ATOM   7450 O O      . ILE   B 1 231 ? 0.99200   17.94300  -34.72600 1.000 30.06000  ? 197 ILE   B O      1 
ATOM   7451 C CB     . ILE   B 1 231 ? -0.82400  20.09300  -33.71600 1.000 27.50000  ? 197 ILE   B CB     1 
ATOM   7452 C CG1    . ILE   B 1 231 ? -1.40500  21.51100  -33.55100 1.000 28.11000  ? 197 ILE   B CG1    1 
ATOM   7453 C CG2    . ILE   B 1 231 ? -1.26800  19.21600  -32.51900 1.000 27.18000  ? 197 ILE   B CG2    1 
ATOM   7454 C CD1    . ILE   B 1 231 ? -2.89700  21.51300  -33.29900 1.000 31.69000  ? 197 ILE   B CD1    1 
ATOM   7455 H H      A ILE   B 1 231 ? 0.51600   20.87700  -35.64800 0.690 26.96000  ? 197 ILE   B H      1 
ATOM   7456 H H      B ILE   B 1 231 ? 0.52400   20.86900  -35.65600 0.310 26.96000  ? 197 ILE   B H      1 
ATOM   7457 H HA     . ILE   B 1 231 ? 1.05500   20.63100  -33.05400 1.000 28.34000  ? 197 ILE   B HA     1 
ATOM   7458 H HB     . ILE   B 1 231 ? -1.17700  19.70600  -34.53200 1.000 27.50000  ? 197 ILE   B HB     1 
ATOM   7459 H HG12   . ILE   B 1 231 ? -0.97500  21.94200  -32.79600 1.000 28.11000  ? 197 ILE   B HG12   1 
ATOM   7460 H HG13   . ILE   B 1 231 ? -1.23700  22.01700  -34.36100 1.000 28.11000  ? 197 ILE   B HG13   1 
ATOM   7461 H HG21   . ILE   B 1 231 ? -2.23400  19.13400  -32.52000 1.000 27.18000  ? 197 ILE   B HG21   1 
ATOM   7462 H HG22   . ILE   B 1 231 ? -0.87500  18.33400  -32.59800 1.000 27.18000  ? 197 ILE   B HG22   1 
ATOM   7463 H HG23   . ILE   B 1 231 ? -0.97200  19.63500  -31.69600 1.000 27.18000  ? 197 ILE   B HG23   1 
ATOM   7464 H HD11   . ILE   B 1 231 ? -3.24500  22.40200  -33.47400 1.000 31.69000  ? 197 ILE   B HD11   1 
ATOM   7465 H HD12   . ILE   B 1 231 ? -3.31700  20.87100  -33.89200 1.000 31.69000  ? 197 ILE   B HD12   1 
ATOM   7466 H HD13   . ILE   B 1 231 ? -3.06400  21.26800  -32.37500 1.000 31.69000  ? 197 ILE   B HD13   1 
ATOM   7467 N N      . GLY   B 1 232 ? 2.20300   18.48300  -32.90900 1.000 27.49000  ? 198 GLY   B N      1 
ATOM   7468 C CA     . GLY   B 1 232 ? 3.08600   17.32700  -33.03900 1.000 29.21000  ? 198 GLY   B CA     1 
ATOM   7469 C C      . GLY   B 1 232 ? 2.39300   16.00700  -32.76600 1.000 32.66000  ? 198 GLY   B C      1 
ATOM   7470 O O      . GLY   B 1 232 ? 1.45300   15.92000  -31.98100 1.000 30.65000  ? 198 GLY   B O      1 
ATOM   7471 H H      . GLY   B 1 232 ? 2.31500   18.94100  -32.19000 1.000 27.49000  ? 198 GLY   B H      1 
ATOM   7472 H HA2    . GLY   B 1 232 ? 3.44700   17.30000  -33.93900 1.000 29.21000  ? 198 GLY   B HA2    1 
ATOM   7473 H HA3    . GLY   B 1 232 ? 3.82500   17.41700  -32.41700 1.000 29.21000  ? 198 GLY   B HA3    1 
ATOM   7474 N N      . ASN   B 1 233 ? 2.84500   14.98600  -33.49700 1.000 30.44000  ? 199 ASN   B N      1 
ATOM   7475 C CA     . ASN   B 1 233 ? 2.56000   13.58000  -33.19000 1.000 29.85000  ? 199 ASN   B CA     1 
ATOM   7476 C C      . ASN   B 1 233 ? 1.06400   13.24900  -33.17100 1.000 35.32000  ? 199 ASN   B C      1 
ATOM   7477 O O      . ASN   B 1 233 ? 0.56900   12.56500  -32.27200 1.000 28.95000  ? 199 ASN   B O      1 
ATOM   7478 C CB     . ASN   B 1 233 ? 3.24600   13.19100  -31.87400 1.000 32.49000  ? 199 ASN   B CB     1 
ATOM   7479 C CG     . ASN   B 1 233 ? 4.77400   13.19200  -32.01000 1.000 39.95000  ? 199 ASN   B CG     1 
ATOM   7480 O OD1    . ASN   B 1 233 ? 5.32900   12.40900  -32.78000 1.000 34.78000  ? 199 ASN   B OD1    1 
ATOM   7481 N ND2    . ASN   B 1 233 ? 5.44300   14.11400  -31.32000 1.000 34.46000  ? 199 ASN   B ND2    1 
ATOM   7482 H H      . ASN   B 1 233 ? 3.33400   15.08600  -34.19700 1.000 30.44000  ? 199 ASN   B H      1 
ATOM   7483 H HA     . ASN   B 1 233 ? 2.95900   13.03700  -33.88800 1.000 29.85000  ? 199 ASN   B HA     1 
ATOM   7484 H HB2    . ASN   B 1 233 ? 3.00200   13.82800  -31.18400 1.000 32.49000  ? 199 ASN   B HB2    1 
ATOM   7485 H HB3    . ASN   B 1 233 ? 2.96600   12.29800  -31.62000 1.000 32.49000  ? 199 ASN   B HB3    1 
ATOM   7486 H HD21   . ASN   B 1 233 ? 6.30000   14.15300  -31.37300 1.000 34.46000  ? 199 ASN   B HD21   1 
ATOM   7487 H HD22   . ASN   B 1 233 ? 5.02000   14.65300  -30.80100 1.000 34.46000  ? 199 ASN   B HD22   1 
ATOM   7488 N N      . GLY   B 1 234 ? 0.34400   13.71400  -34.19200 1.000 29.41000  ? 200 GLY   B N      1 
ATOM   7489 C CA     . GLY   B 1 234 ? -0.96100  13.15600  -34.50100 1.000 28.59000  ? 200 GLY   B CA     1 
ATOM   7490 C C      . GLY   B 1 234 ? -0.78900  11.80500  -35.18900 1.000 30.44000  ? 200 GLY   B C      1 
ATOM   7491 O O      . GLY   B 1 234 ? 0.32000   11.35600  -35.48100 1.000 32.55000  ? 200 GLY   B O      1 
ATOM   7492 H H      . GLY   B 1 234 ? 0.59200   14.34900  -34.71600 1.000 29.41000  ? 200 GLY   B H      1 
ATOM   7493 H HA2    . GLY   B 1 234 ? -1.47200  13.03300  -33.68600 1.000 28.59000  ? 200 GLY   B HA2    1 
ATOM   7494 H HA3    . GLY   B 1 234 ? -1.44600  13.75300  -35.09200 1.000 28.59000  ? 200 GLY   B HA3    1 
ATOM   7495 N N      . LEU   B 1 235 ? -1.91100  11.14300  -35.45500 1.000 29.53000  ? 201 LEU   B N      1 
ATOM   7496 C CA     . LEU   B 1 235 ? -1.85400  9.82000   -36.07600 1.000 28.33000  ? 201 LEU   B CA     1 
ATOM   7497 C C      . LEU   B 1 235 ? -3.05100  9.66500   -36.99800 1.000 28.48000  ? 201 LEU   B C      1 
ATOM   7498 O O      . LEU   B 1 235 ? -4.17400  10.01500  -36.62700 1.000 31.77000  ? 201 LEU   B O      1 
ATOM   7499 C CB     . LEU   B 1 235 ? -1.83200  8.71100   -35.01500 1.000 29.04000  ? 201 LEU   B CB     1 
ATOM   7500 C CG     . LEU   B 1 235 ? -1.79100  7.24800   -35.50000 1.000 30.85000  ? 201 LEU   B CG     1 
ATOM   7501 C CD1    . LEU   B 1 235 ? -0.44000  6.91600   -36.12200 1.000 31.52000  ? 201 LEU   B CD1    1 
ATOM   7502 C CD2    . LEU   B 1 235 ? -2.12600  6.29400   -34.33500 1.000 31.69000  ? 201 LEU   B CD2    1 
ATOM   7503 H H      . LEU   B 1 235 ? -2.70500  11.43000  -35.29000 1.000 29.53000  ? 201 LEU   B H      1 
ATOM   7504 H HA     . LEU   B 1 235 ? -1.04800  9.74700   -36.61100 1.000 28.33000  ? 201 LEU   B HA     1 
ATOM   7505 H HB2    . LEU   B 1 235 ? -1.04900  8.84600   -34.45900 1.000 29.04000  ? 201 LEU   B HB2    1 
ATOM   7506 H HB3    . LEU   B 1 235 ? -2.62800  8.80500   -34.46900 1.000 29.04000  ? 201 LEU   B HB3    1 
ATOM   7507 H HG     . LEU   B 1 235 ? -2.46800  7.12600   -36.18400 1.000 30.85000  ? 201 LEU   B HG     1 
ATOM   7508 H HD11   . LEU   B 1 235 ? -0.44600  5.99100   -36.41300 1.000 31.52000  ? 201 LEU   B HD11   1 
ATOM   7509 H HD12   . LEU   B 1 235 ? -0.29000  7.50100   -36.88100 1.000 31.52000  ? 201 LEU   B HD12   1 
ATOM   7510 H HD13   . LEU   B 1 235 ? 0.25400   7.05000   -35.45800 1.000 31.52000  ? 201 LEU   B HD13   1 
ATOM   7511 H HD21   . LEU   B 1 235 ? -2.09300  5.38000   -34.65700 1.000 31.69000  ? 201 LEU   B HD21   1 
ATOM   7512 H HD22   . LEU   B 1 235 ? -1.47500  6.42000   -33.62700 1.000 31.69000  ? 201 LEU   B HD22   1 
ATOM   7513 H HD23   . LEU   B 1 235 ? -3.01600  6.49700   -34.00700 1.000 31.69000  ? 201 LEU   B HD23   1 
ATOM   7514 N N      . VAL   B 1 236 ? -2.79500  9.19100   -38.20900 1.000 31.52000  ? 202 VAL   B N      1 
ATOM   7515 C CA     . VAL   B 1 236 ? -3.83100  8.91700   -39.19800 1.000 29.87000  ? 202 VAL   B CA     1 
ATOM   7516 C C      . VAL   B 1 236 ? -3.71500  7.46000   -39.61200 1.000 33.20000  ? 202 VAL   B C      1 
ATOM   7517 O O      . VAL   B 1 236 ? -2.60700  6.95700   -39.83300 1.000 34.68000  ? 202 VAL   B O      1 
ATOM   7518 C CB     . VAL   B 1 236 ? -3.68800  9.83500   -40.42700 1.000 33.25000  ? 202 VAL   B CB     1 
ATOM   7519 C CG1    . VAL   B 1 236 ? -4.71900  9.47900   -41.48700 1.000 39.35000  ? 202 VAL   B CG1    1 
ATOM   7520 C CG2    . VAL   B 1 236 ? -3.80500  11.29900  -39.99500 1.000 38.54000  ? 202 VAL   B CG2    1 
ATOM   7521 H H      . VAL   B 1 236 ? -2.00200  9.01400   -38.49100 1.000 31.52000  ? 202 VAL   B H      1 
ATOM   7522 H HA     . VAL   B 1 236 ? -4.70600  9.05900   -38.80500 1.000 29.87000  ? 202 VAL   B HA     1 
ATOM   7523 H HB     . VAL   B 1 236 ? -2.80700  9.70800   -40.81300 1.000 33.25000  ? 202 VAL   B HB     1 
ATOM   7524 H HG11   . VAL   B 1 236 ? -4.74100  10.18300  -42.15300 1.000 39.35000  ? 202 VAL   B HG11   1 
ATOM   7525 H HG12   . VAL   B 1 236 ? -4.47100  8.64000   -41.90500 1.000 39.35000  ? 202 VAL   B HG12   1 
ATOM   7526 H HG13   . VAL   B 1 236 ? -5.58900  9.39700   -41.06600 1.000 39.35000  ? 202 VAL   B HG13   1 
ATOM   7527 H HG21   . VAL   B 1 236 ? -3.18200  11.82900  -40.51500 1.000 38.54000  ? 202 VAL   B HG21   1 
ATOM   7528 H HG22   . VAL   B 1 236 ? -4.71200  11.60300  -40.15500 1.000 38.54000  ? 202 VAL   B HG22   1 
ATOM   7529 H HG23   . VAL   B 1 236 ? -3.59100  11.37900  -39.05300 1.000 38.54000  ? 202 VAL   B HG23   1 
ATOM   7530 N N      . ILE   B 1 237 ? -4.86700  6.80100   -39.73700 1.000 36.72000  ? 203 ILE   B N      1 
ATOM   7531 C CA     . ILE   B 1 237 ? -4.96200  5.39300   -40.11700 1.000 36.98000  ? 203 ILE   B CA     1 
ATOM   7532 C C      . ILE   B 1 237 ? -5.92800  5.29400   -41.29400 1.000 36.11000  ? 203 ILE   B C      1 
ATOM   7533 O O      . ILE   B 1 237 ? -7.00600  5.89800   -41.26000 1.000 36.45000  ? 203 ILE   B O      1 
ATOM   7534 C CB     . ILE   B 1 237 ? -5.44500  4.53000   -38.93200 1.000 39.04000  ? 203 ILE   B CB     1 
ATOM   7535 C CG1    . ILE   B 1 237 ? -4.50000  4.68200   -37.72800 1.000 33.96000  ? 203 ILE   B CG1    1 
ATOM   7536 C CG2    . ILE   B 1 237 ? -5.62700  3.05600   -39.34500 1.000 38.07000  ? 203 ILE   B CG2    1 
ATOM   7537 C CD1    . ILE   B 1 237 ? -5.11100  4.21300   -36.40600 1.000 37.02000  ? 203 ILE   B CD1    1 
ATOM   7538 H H      . ILE   B 1 237 ? -5.63500  7.16400   -39.60100 1.000 36.72000  ? 203 ILE   B H      1 
ATOM   7539 H HA     . ILE   B 1 237 ? -4.09300  5.07100   -40.40100 1.000 36.98000  ? 203 ILE   B HA     1 
ATOM   7540 H HB     . ILE   B 1 237 ? -6.31400  4.86700   -38.66300 1.000 39.04000  ? 203 ILE   B HB     1 
ATOM   7541 H HG12   . ILE   B 1 237 ? -3.70200  4.15600   -37.89000 1.000 33.96000  ? 203 ILE   B HG12   1 
ATOM   7542 H HG13   . ILE   B 1 237 ? -4.26200  5.61600   -37.62400 1.000 33.96000  ? 203 ILE   B HG13   1 
ATOM   7543 H HG21   . ILE   B 1 237 ? -5.79200  2.52400   -38.55100 1.000 38.07000  ? 203 ILE   B HG21   1 
ATOM   7544 H HG22   . ILE   B 1 237 ? -6.38200  2.98600   -39.95000 1.000 38.07000  ? 203 ILE   B HG22   1 
ATOM   7545 H HG23   . ILE   B 1 237 ? -4.81900  2.75000   -39.78500 1.000 38.07000  ? 203 ILE   B HG23   1 
ATOM   7546 H HD11   . ILE   B 1 237 ? -4.48700  4.39800   -35.68700 1.000 37.02000  ? 203 ILE   B HD11   1 
ATOM   7547 H HD12   . ILE   B 1 237 ? -5.94100  4.69200   -36.25500 1.000 37.02000  ? 203 ILE   B HD12   1 
ATOM   7548 H HD13   . ILE   B 1 237 ? -5.28300  3.26000   -36.45700 1.000 37.02000  ? 203 ILE   B HD13   1 
ATOM   7549 N N      . ASP   B 1 238 ? -5.55300  4.52500   -42.32400 1.000 36.39000  ? 204 ASP   B N      1 
ATOM   7550 C CA     . ASP   B 1 238 ? -6.43900  4.31800   -43.46700 1.000 42.69000  ? 204 ASP   B CA     1 
ATOM   7551 C C      . ASP   B 1 238 ? -7.43300  3.20400   -43.15300 1.000 42.90000  ? 204 ASP   B C      1 
ATOM   7552 O O      . ASP   B 1 238 ? -7.03700  2.11500   -42.72500 1.000 39.10000  ? 204 ASP   B O      1 
ATOM   7553 C CB     . ASP   B 1 238 ? -5.63100  3.97600   -44.72100 1.000 37.95000  ? 204 ASP   B CB     1 
ATOM   7554 C CG     . ASP   B 1 238 ? -6.51000  3.77800   -45.94900 1.000 50.58000  ? 204 ASP   B CG     1 
ATOM   7555 O OD1    . ASP   B 1 238 ? -7.14400  4.75400   -46.39100 1.000 52.70000  ? 204 ASP   B OD1    1 
ATOM   7556 O OD2    . ASP   B 1 238 ? -6.57600  2.64100   -46.46400 1.000 50.53000  ? 204 ASP   B OD2    1 
ATOM   7557 H H      . ASP   B 1 238 ? -4.79800  4.11800   -42.38100 1.000 36.39000  ? 204 ASP   B H      1 
ATOM   7558 H HA     . ASP   B 1 238 ? -6.93800  5.13200   -43.63900 1.000 42.69000  ? 204 ASP   B HA     1 
ATOM   7559 H HB2    . ASP   B 1 238 ? -5.01400  4.70100   -44.90700 1.000 37.95000  ? 204 ASP   B HB2    1 
ATOM   7560 H HB3    . ASP   B 1 238 ? -5.14100  3.15400   -44.56700 1.000 37.95000  ? 204 ASP   B HB3    1 
ATOM   7561 N N      . VAL   B 1 239 ? -8.72700  3.48100   -43.34600 1.000 40.29000  ? 205 VAL   B N      1 
ATOM   7562 C CA     . VAL   B 1 239 ? -9.73600  2.46600   -43.05300 1.000 44.68000  ? 205 VAL   B CA     1 
ATOM   7563 C C      . VAL   B 1 239 ? -9.51700  1.22900   -43.91600 1.000 43.18000  ? 205 VAL   B C      1 
ATOM   7564 O O      . VAL   B 1 239 ? -9.60100  0.09600   -43.43100 1.000 41.16000  ? 205 VAL   B O      1 
ATOM   7565 C CB     . VAL   B 1 239 ? -11.15500 3.02400   -43.24500 1.000 39.84000  ? 205 VAL   B CB     1 
ATOM   7566 C CG1    . VAL   B 1 239 ? -12.17600 1.90200   -43.06500 1.000 48.20000  ? 205 VAL   B CG1    1 
ATOM   7567 C CG2    . VAL   B 1 239 ? -11.43300 4.16000   -42.26500 1.000 49.73000  ? 205 VAL   B CG2    1 
ATOM   7568 H H      . VAL   B 1 239 ? -9.03700  4.22800   -43.63800 1.000 40.29000  ? 205 VAL   B H      1 
ATOM   7569 H HA     . VAL   B 1 239 ? -9.64700  2.19800   -42.12500 1.000 44.68000  ? 205 VAL   B HA     1 
ATOM   7570 H HB     . VAL   B 1 239 ? -11.24200 3.37200   -44.14600 1.000 39.84000  ? 205 VAL   B HB     1 
ATOM   7571 H HG11   . VAL   B 1 239 ? -13.04700 2.29500   -42.90000 1.000 48.20000  ? 205 VAL   B HG11   1 
ATOM   7572 H HG12   . VAL   B 1 239 ? -12.20500 1.36500   -43.87200 1.000 48.20000  ? 205 VAL   B HG12   1 
ATOM   7573 H HG13   . VAL   B 1 239 ? -11.91300 1.35400   -42.30900 1.000 48.20000  ? 205 VAL   B HG13   1 
ATOM   7574 H HG21   . VAL   B 1 239 ? -12.33600 4.48400   -42.40600 1.000 49.73000  ? 205 VAL   B HG21   1 
ATOM   7575 H HG22   . VAL   B 1 239 ? -11.33900 3.82500   -41.35900 1.000 49.73000  ? 205 VAL   B HG22   1 
ATOM   7576 H HG23   . VAL   B 1 239 ? -10.79700 4.87500   -42.42200 1.000 49.73000  ? 205 VAL   B HG23   1 
ATOM   7577 N N      . GLU   B 1 240 ? -9.23000  1.42100   -45.20300 1.000 42.47000  ? 206 GLU   B N      1 
ATOM   7578 C CA     . GLU   B 1 240 ? -9.22800  0.29100   -46.12600 1.000 48.66000  ? 206 GLU   B CA     1 
ATOM   7579 C C      . GLU   B 1 240 ? -8.07500  -0.65400  -45.83900 1.000 47.86000  ? 206 GLU   B C      1 
ATOM   7580 O O      . GLU   B 1 240 ? -8.25700  -1.87700  -45.80300 1.000 50.41000  ? 206 GLU   B O      1 
ATOM   7581 C CB     . GLU   B 1 240 ? -9.16900  0.78500   -47.57300 1.000 51.72000  ? 206 GLU   B CB     1 
ATOM   7582 C CG     . GLU   B 1 240 ? -8.70900  -0.26500  -48.57700 1.000 65.20000  ? 206 GLU   B CG     1 
ATOM   7583 C CD     . GLU   B 1 240 ? -9.81600  -1.21100  -49.01800 1.000 77.38000  ? 206 GLU   B CD     1 
ATOM   7584 O OE1    . GLU   B 1 240 ? -10.99900 -0.87600  -48.81600 1.000 79.61000  ? 206 GLU   B OE1    1 
ATOM   7585 O OE2    . GLU   B 1 240 ? -9.49900  -2.29400  -49.57200 1.000 79.56000  ? 206 GLU   B OE2    1 
ATOM   7586 H H      . GLU   B 1 240 ? -9.03700  2.17900   -45.56000 1.000 42.47000  ? 206 GLU   B H      1 
ATOM   7587 H HA     . GLU   B 1 240 ? -10.05400 -0.20600  -46.01500 1.000 48.66000  ? 206 GLU   B HA     1 
ATOM   7588 H HB2    . GLU   B 1 240 ? -10.05300 1.08500   -47.83700 1.000 51.72000  ? 206 GLU   B HB2    1 
ATOM   7589 H HB3    . GLU   B 1 240 ? -8.54700  1.52700   -47.62000 1.000 51.72000  ? 206 GLU   B HB3    1 
ATOM   7590 H HG2    . GLU   B 1 240 ? -8.41300  0.20300   -49.37300 1.000 65.20000  ? 206 GLU   B HG2    1 
ATOM   7591 H HG3    . GLU   B 1 240 ? -7.97300  -0.79400  -48.24000 1.000 65.20000  ? 206 GLU   B HG3    1 
ATOM   7592 N N      . THR   B 1 241 ? -6.88100  -0.10900  -45.63100 1.000 41.30000  ? 207 THR   B N      1 
ATOM   7593 C CA     . THR   B 1 241 ? -5.70300  -0.92900  -45.38300 1.000 40.64000  ? 207 THR   B CA     1 
ATOM   7594 C C      . THR   B 1 241 ? -5.45400  -1.17600  -43.90100 1.000 39.10000  ? 207 THR   B C      1 
ATOM   7595 O O      . THR   B 1 241 ? -4.55600  -1.96100  -43.55800 1.000 44.61000  ? 207 THR   B O      1 
ATOM   7596 C CB     . THR   B 1 241 ? -4.47600  -0.26400  -45.99400 1.000 50.95000  ? 207 THR   B CB     1 
ATOM   7597 O OG1    . THR   B 1 241 ? -4.22700  0.96000   -45.29500 1.000 50.33000  ? 207 THR   B OG1    1 
ATOM   7598 C CG2    . THR   B 1 241 ? -4.71600  0.02200   -47.48000 1.000 48.26000  ? 207 THR   B CG2    1 
ATOM   7599 H H      . THR   B 1 241 ? -6.72700  0.73700   -45.62900 1.000 41.30000  ? 207 THR   B H      1 
ATOM   7600 H HA     . THR   B 1 241 ? -5.82100  -1.79000  -45.81400 1.000 40.64000  ? 207 THR   B HA     1 
ATOM   7601 H HB     . THR   B 1 241 ? -3.70900  -0.85100  -45.91000 1.000 50.95000  ? 207 THR   B HB     1 
ATOM   7602 H HG1    . THR   B 1 241 ? -3.55300  1.34300   -45.61800 1.000 50.33000  ? 207 THR   B HG1    1 
ATOM   7603 H HG21   . THR   B 1 241 ? -3.89500  0.33200   -47.89400 1.000 48.26000  ? 207 THR   B HG21   1 
ATOM   7604 H HG22   . THR   B 1 241 ? -5.01000  -0.78600  -47.92900 1.000 48.26000  ? 207 THR   B HG22   1 
ATOM   7605 H HG23   . THR   B 1 241 ? -5.39700  0.70500   -47.58200 1.000 48.26000  ? 207 THR   B HG23   1 
ATOM   7606 N N      . GLU   B 1 242 ? -6.21800  -0.52000  -43.02800 1.000 37.22000  ? 208 GLU   B N      1 
ATOM   7607 C CA     . GLU   B 1 242 ? -6.03800  -0.61600  -41.57900 1.000 35.85000  ? 208 GLU   B CA     1 
ATOM   7608 C C      . GLU   B 1 242 ? -4.60300  -0.30000  -41.16400 1.000 40.66000  ? 208 GLU   B C      1 
ATOM   7609 O O      . GLU   B 1 242 ? -4.11400  -0.79100  -40.14000 1.000 40.96000  ? 208 GLU   B O      1 
ATOM   7610 C CB     . GLU   B 1 242 ? -6.46700  -1.99400  -41.07500 1.000 40.31000  ? 208 GLU   B CB     1 
ATOM   7611 C CG     . GLU   B 1 242 ? -7.87100  -2.30500  -41.53100 1.000 38.10000  ? 208 GLU   B CG     1 
ATOM   7612 C CD     . GLU   B 1 242 ? -8.36900  -3.66900  -41.10700 1.000 45.43000  ? 208 GLU   B CD     1 
ATOM   7613 O OE1    . GLU   B 1 242 ? -7.81300  -4.27400  -40.16100 1.000 43.04000  ? 208 GLU   B OE1    1 
ATOM   7614 O OE2    . GLU   B 1 242 ? -9.33300  -4.13600  -41.73900 1.000 49.98000  ? 208 GLU   B OE2    1 
ATOM   7615 H H      . GLU   B 1 242 ? -6.86400  0.00000   -43.25500 1.000 37.22000  ? 208 GLU   B H      1 
ATOM   7616 H HA     . GLU   B 1 242 ? -6.61300  0.04300   -41.16100 1.000 35.85000  ? 208 GLU   B HA     1 
ATOM   7617 H HB2    . GLU   B 1 242 ? -5.87100  -2.66900  -41.43500 1.000 40.31000  ? 208 GLU   B HB2    1 
ATOM   7618 H HB3    . GLU   B 1 242 ? -6.44700  -2.00700  -40.10600 1.000 40.31000  ? 208 GLU   B HB3    1 
ATOM   7619 H HG2    . GLU   B 1 242 ? -8.47400  -1.64100  -41.16000 1.000 38.10000  ? 208 GLU   B HG2    1 
ATOM   7620 H HG3    . GLU   B 1 242 ? -7.90400  -2.27300  -42.50000 1.000 38.10000  ? 208 GLU   B HG3    1 
ATOM   7621 N N      . SER   B 1 243 ? -3.91500  0.55200   -41.92400 1.000 37.37000  ? 209 SER   B N      1 
ATOM   7622 C CA     . SER   B 1 243 ? -2.52700  0.83800   -41.59500 1.000 39.69000  ? 209 SER   B CA     1 
ATOM   7623 C C      . SER   B 1 243 ? -2.28600  2.34700   -41.56300 1.000 40.68000  ? 209 SER   B C      1 
ATOM   7624 O O      . SER   B 1 243 ? -3.05900  3.13200   -42.11900 1.000 36.14000  ? 209 SER   B O      1 
ATOM   7625 C CB     . SER   B 1 243 ? -1.57700  0.12200   -42.56800 1.000 54.53000  ? 209 SER   B CB     1 
ATOM   7626 O OG     . SER   B 1 243 ? -1.10400  0.97400   -43.58500 1.000 64.21000  ? 209 SER   B OG     1 
ATOM   7627 H H      . SER   B 1 243 ? -4.22000  0.96500   -42.61400 1.000 37.37000  ? 209 SER   B H      1 
ATOM   7628 H HA     . SER   B 1 243 ? -2.33300  0.50300   -40.70700 1.000 39.69000  ? 209 SER   B HA     1 
ATOM   7629 H HB2    . SER   B 1 243 ? -0.81400  -0.20700  -42.06900 1.000 54.53000  ? 209 SER   B HB2    1 
ATOM   7630 H HB3    . SER   B 1 243 ? -2.04900  -0.62100  -42.97600 1.000 54.53000  ? 209 SER   B HB3    1 
ATOM   7631 H HG     . SER   B 1 243 ? -0.58900  0.55200   -44.09700 1.000 64.21000  ? 209 SER   B HG     1 
ATOM   7632 N N      . VAL   B 1 244 ? -1.21900  2.74000   -40.85700 1.000 34.38000  ? 210 VAL   B N      1 
ATOM   7633 C CA     . VAL   B 1 244 ? -0.84000  4.15100   -40.79500 1.000 37.83000  ? 210 VAL   B CA     1 
ATOM   7634 C C      . VAL   B 1 244 ? -0.45800  4.62800   -42.19600 1.000 42.37000  ? 210 VAL   B C      1 
ATOM   7635 O O      . VAL   B 1 244 ? -0.09300  3.82700   -43.07200 1.000 41.55000  ? 210 VAL   B O      1 
ATOM   7636 C CB     . VAL   B 1 244 ? 0.30400   4.37500   -39.78600 1.000 40.22000  ? 210 VAL   B CB     1 
ATOM   7637 C CG1    . VAL   B 1 244 ? -0.11000  3.90800   -38.40500 1.000 36.26000  ? 210 VAL   B CG1    1 
ATOM   7638 C CG2    . VAL   B 1 244 ? 1.59200   3.66600   -40.24100 1.000 37.94000  ? 210 VAL   B CG2    1 
ATOM   7639 H H      . VAL   B 1 244 ? -0.70600  2.21300   -40.41100 1.000 34.38000  ? 210 VAL   B H      1 
ATOM   7640 H HA     . VAL   B 1 244 ? -1.60400  4.67000   -40.50000 1.000 37.83000  ? 210 VAL   B HA     1 
ATOM   7641 H HB     . VAL   B 1 244 ? 0.49100   5.32500   -39.73400 1.000 40.22000  ? 210 VAL   B HB     1 
ATOM   7642 H HG11   . VAL   B 1 244 ? 0.59600   4.12100   -37.77500 1.000 36.26000  ? 210 VAL   B HG11   1 
ATOM   7643 H HG12   . VAL   B 1 244 ? -0.92800  4.36300   -38.15100 1.000 36.26000  ? 210 VAL   B HG12   1 
ATOM   7644 H HG13   . VAL   B 1 244 ? -0.25700  2.94900   -38.42600 1.000 36.26000  ? 210 VAL   B HG13   1 
ATOM   7645 H HG21   . VAL   B 1 244 ? 2.24400   3.70900   -39.52500 1.000 37.94000  ? 210 VAL   B HG21   1 
ATOM   7646 H HG22   . VAL   B 1 244 ? 1.38800   2.74000   -40.44600 1.000 37.94000  ? 210 VAL   B HG22   1 
ATOM   7647 H HG23   . VAL   B 1 244 ? 1.93800   4.11100   -41.03000 1.000 37.94000  ? 210 VAL   B HG23   1 
ATOM   7648 N N      . VAL   B 1 245 ? -0.57100  5.94300   -42.42700 1.000 41.57000  ? 211 VAL   B N      1 
ATOM   7649 C CA     . VAL   B 1 245 ? -0.42200  6.48600   -43.77800 1.000 42.90000  ? 211 VAL   B CA     1 
ATOM   7650 C C      . VAL   B 1 245 ? 0.95900   7.07700   -44.04700 1.000 43.92000  ? 211 VAL   B C      1 
ATOM   7651 O O      . VAL   B 1 245 ? 1.27100   7.37000   -45.20900 1.000 42.31000  ? 211 VAL   B O      1 
ATOM   7652 C CB     . VAL   B 1 245 ? -1.51300  7.53600   -44.08600 1.000 42.97000  ? 211 VAL   B CB     1 
ATOM   7653 C CG1    . VAL   B 1 245 ? -2.91000  6.92800   -43.93100 1.000 42.50000  ? 211 VAL   B CG1    1 
ATOM   7654 C CG2    . VAL   B 1 245 ? -1.33200  8.78000   -43.20200 1.000 34.58000  ? 211 VAL   B CG2    1 
ATOM   7655 H H      . VAL   B 1 245 ? -0.73100  6.53300   -41.82200 1.000 41.57000  ? 211 VAL   B H      1 
ATOM   7656 H HA     . VAL   B 1 245 ? -0.54600  5.76000   -44.40900 1.000 42.90000  ? 211 VAL   B HA     1 
ATOM   7657 H HB     . VAL   B 1 245 ? -1.41800  7.81700   -45.00900 1.000 42.97000  ? 211 VAL   B HB     1 
ATOM   7658 H HG11   . VAL   B 1 245 ? -3.57200  7.59400   -44.17400 1.000 42.50000  ? 211 VAL   B HG11   1 
ATOM   7659 H HG12   . VAL   B 1 245 ? -2.98500  6.15800   -44.51600 1.000 42.50000  ? 211 VAL   B HG12   1 
ATOM   7660 H HG13   . VAL   B 1 245 ? -3.03600  6.65700   -43.00800 1.000 42.50000  ? 211 VAL   B HG13   1 
ATOM   7661 H HG21   . VAL   B 1 245 ? -2.10300  9.35800   -43.31300 1.000 34.58000  ? 211 VAL   B HG21   1 
ATOM   7662 H HG22   . VAL   B 1 245 ? -1.25900  8.50300   -42.27600 1.000 34.58000  ? 211 VAL   B HG22   1 
ATOM   7663 H HG23   . VAL   B 1 245 ? -0.52700  9.24800   -43.47200 1.000 34.58000  ? 211 VAL   B HG23   1 
ATOM   7664 N N      . ILE   B 1 246 ? 1.79500   7.25800   -43.02700 1.000 37.81000  ? 212 ILE   B N      1 
ATOM   7665 C CA     . ILE   B 1 246 ? 3.18900   7.63200   -43.23300 1.000 40.90000  ? 212 ILE   B CA     1 
ATOM   7666 C C      . ILE   B 1 246 ? 4.07400   6.63100   -42.49000 1.000 42.65000  ? 212 ILE   B C      1 
ATOM   7667 O O      . ILE   B 1 246 ? 3.66500   6.01100   -41.50500 1.000 44.15000  ? 212 ILE   B O      1 
ATOM   7668 C CB     . ILE   B 1 246 ? 3.50300   9.07200   -42.78400 1.000 40.72000  ? 212 ILE   B CB     1 
ATOM   7669 C CG1    . ILE   B 1 246 ? 3.23600   9.22600   -41.29700 1.000 39.83000  ? 212 ILE   B CG1    1 
ATOM   7670 C CG2    . ILE   B 1 246 ? 2.70500   10.09600  -43.63300 1.000 37.85000  ? 212 ILE   B CG2    1 
ATOM   7671 C CD1    . ILE   B 1 246 ? 3.33100   10.68300  -40.79700 1.000 37.04000  ? 212 ILE   B CD1    1 
ATOM   7672 H H      . ILE   B 1 246 ? 1.57600   7.16900   -42.20000 1.000 37.81000  ? 212 ILE   B H      1 
ATOM   7673 H HA     . ILE   B 1 246 ? 3.39900   7.56500   -44.17700 1.000 40.90000  ? 212 ILE   B HA     1 
ATOM   7674 H HB     . ILE   B 1 246 ? 4.44800   9.23200   -42.93500 1.000 40.72000  ? 212 ILE   B HB     1 
ATOM   7675 H HG12   . ILE   B 1 246 ? 2.34200   8.90400   -41.10300 1.000 39.83000  ? 212 ILE   B HG12   1 
ATOM   7676 H HG13   . ILE   B 1 246 ? 3.88800   8.70500   -40.80300 1.000 39.83000  ? 212 ILE   B HG13   1 
ATOM   7677 H HG21   . ILE   B 1 246 ? 3.06300   10.98400  -43.48000 1.000 37.85000  ? 212 ILE   B HG21   1 
ATOM   7678 H HG22   . ILE   B 1 246 ? 2.79200   9.86200   -44.57000 1.000 37.85000  ? 212 ILE   B HG22   1 
ATOM   7679 H HG23   . ILE   B 1 246 ? 1.77200   10.06400  -43.37100 1.000 37.85000  ? 212 ILE   B HG23   1 
ATOM   7680 H HD11   . ILE   B 1 246 ? 3.31700   10.68500  -39.82700 1.000 37.04000  ? 212 ILE   B HD11   1 
ATOM   7681 H HD12   . ILE   B 1 246 ? 4.16000   11.07200  -41.11600 1.000 37.04000  ? 212 ILE   B HD12   1 
ATOM   7682 H HD13   . ILE   B 1 246 ? 2.57600   11.18600  -41.14000 1.000 37.04000  ? 212 ILE   B HD13   1 
ATOM   7683 N N      . LYS   B 1 247 ? 5.30200   6.49200   -42.96600 0.980 38.92000  ? 213 LYS   B N      1 
ATOM   7684 C CA     . LYS   B 1 247 ? 6.13700   5.35600   -42.56700 0.980 47.09000  ? 213 LYS   B CA     1 
ATOM   7685 C C      . LYS   B 1 247 ? 6.90200   5.58100   -41.25900 0.980 51.03000  ? 213 LYS   B C      1 
ATOM   7686 O O      . LYS   B 1 247 ? 6.86100   4.72300   -40.36300 0.980 47.25000  ? 213 LYS   B O      1 
ATOM   7687 C CB     . LYS   B 1 247 ? 7.09600   5.02700   -43.71600 0.980 50.97000  ? 213 LYS   B CB     1 
ATOM   7688 C CG     . LYS   B 1 247 ? 7.84900   3.71300   -43.58400 0.980 65.65000  ? 213 LYS   B CG     1 
ATOM   7689 C CD     . LYS   B 1 247 ? 8.62100   3.39100   -44.87000 0.980 71.35000  ? 213 LYS   B CD     1 
ATOM   7690 C CE     . LYS   B 1 247 ? 9.90300   2.61000   -44.57000 0.980 82.23000  ? 213 LYS   B CE     1 
ATOM   7691 N NZ     . LYS   B 1 247 ? 10.65900  2.19000   -45.79400 0.980 83.11000  ? 213 LYS   B NZ     1 
ATOM   7692 H H      . LYS   B 1 247 ? 5.67800   7.03400   -43.51800 0.980 38.92000  ? 213 LYS   B H      1 
ATOM   7693 H HA     . LYS   B 1 247 ? 5.56300   4.58500   -42.43700 0.980 47.09000  ? 213 LYS   B HA     1 
ATOM   7694 H HB2    . LYS   B 1 247 ? 6.58200   4.98300   -44.53800 0.980 50.97000  ? 213 LYS   B HB2    1 
ATOM   7695 H HB3    . LYS   B 1 247 ? 7.76100   5.72500   -43.79100 0.980 50.97000  ? 213 LYS   B HB3    1 
ATOM   7696 H HG2    . LYS   B 1 247 ? 8.48500   3.77800   -42.85400 0.980 65.65000  ? 213 LYS   B HG2    1 
ATOM   7697 H HG3    . LYS   B 1 247 ? 7.21800   2.99500   -43.41900 0.980 65.65000  ? 213 LYS   B HG3    1 
ATOM   7698 H HD2    . LYS   B 1 247 ? 8.06400   2.85100   -45.45200 0.980 71.35000  ? 213 LYS   B HD2    1 
ATOM   7699 H HD3    . LYS   B 1 247 ? 8.86600   4.21900   -45.31200 0.980 71.35000  ? 213 LYS   B HD3    1 
ATOM   7700 H HE2    . LYS   B 1 247 ? 10.49000  3.16700   -44.03600 0.980 82.23000  ? 213 LYS   B HE2    1 
ATOM   7701 H HE3    . LYS   B 1 247 ? 9.67200   1.80800   -44.07500 0.980 82.23000  ? 213 LYS   B HE3    1 
ATOM   7702 H HZ1    . LYS   B 1 247 ? 11.39200  1.74200   -45.56000 0.980 83.11000  ? 213 LYS   B HZ1    1 
ATOM   7703 H HZ2    . LYS   B 1 247 ? 10.14900  1.66600   -46.30100 0.980 83.11000  ? 213 LYS   B HZ2    1 
ATOM   7704 H HZ3    . LYS   B 1 247 ? 10.89600  2.90700   -46.26500 0.980 83.11000  ? 213 LYS   B HZ3    1 
ATOM   7705 N N      . PRO   B 1 248 ? 7.59200   6.70900   -41.08900 1.000 46.45000  ? 214 PRO   B N      1 
ATOM   7706 C CA     . PRO   B 1 248 ? 8.44700   6.87700   -39.90400 1.000 49.84000  ? 214 PRO   B CA     1 
ATOM   7707 C C      . PRO   B 1 248 ? 7.65600   6.85000   -38.59900 1.000 48.77000  ? 214 PRO   B C      1 
ATOM   7708 O O      . PRO   B 1 248 ? 6.44700   7.08500   -38.56100 1.000 45.08000  ? 214 PRO   B O      1 
ATOM   7709 C CB     . PRO   B 1 248 ? 9.09700   8.25100   -40.12500 1.000 48.61000  ? 214 PRO   B CB     1 
ATOM   7710 C CG     . PRO   B 1 248 ? 8.93800   8.53600   -41.58900 1.000 46.18000  ? 214 PRO   B CG     1 
ATOM   7711 C CD     . PRO   B 1 248 ? 7.67200   7.86100   -42.00700 1.000 48.29000  ? 214 PRO   B CD     1 
ATOM   7712 H HA     . PRO   B 1 248 ? 9.13500   6.19300   -39.88100 1.000 49.84000  ? 214 PRO   B HA     1 
ATOM   7713 H HB2    . PRO   B 1 248 ? 8.63600   8.91900   -39.59400 1.000 48.61000  ? 214 PRO   B HB2    1 
ATOM   7714 H HB3    . PRO   B 1 248 ? 10.03600  8.21000   -39.88400 1.000 48.61000  ? 214 PRO   B HB3    1 
ATOM   7715 H HG2    . PRO   B 1 248 ? 8.89000   9.49300   -41.73900 1.000 46.18000  ? 214 PRO   B HG2    1 
ATOM   7716 H HG3    . PRO   B 1 248 ? 9.68200   8.14500   -42.07100 1.000 46.18000  ? 214 PRO   B HG3    1 
ATOM   7717 H HD2    . PRO   B 1 248 ? 6.91300   8.44900   -41.87300 1.000 48.29000  ? 214 PRO   B HD2    1 
ATOM   7718 H HD3    . PRO   B 1 248 ? 7.73800   7.57900   -42.92900 1.000 48.29000  ? 214 PRO   B HD3    1 
ATOM   7719 N N      . LYS   B 1 249 ? 8.36500   6.55200   -37.51000 1.000 48.95000  ? 215 LYS   B N      1 
ATOM   7720 C CA     . LYS   B 1 249 ? 7.85300   6.76900   -36.15100 1.000 49.55000  ? 215 LYS   B CA     1 
ATOM   7721 C C      . LYS   B 1 249 ? 6.45700   6.16700   -35.93500 1.000 52.25000  ? 215 LYS   B C      1 
ATOM   7722 O O      . LYS   B 1 249 ? 5.58900   6.78700   -35.31600 1.000 43.43000  ? 215 LYS   B O      1 
ATOM   7723 C CB     . LYS   B 1 249 ? 7.84800   8.26500   -35.81700 1.000 51.92000  ? 215 LYS   B CB     1 
ATOM   7724 H H      . LYS   B 1 249 ? 9.15700   6.21800   -37.53000 1.000 48.95000  ? 215 LYS   B H      1 
ATOM   7725 H HA     . LYS   B 1 249 ? 8.45400   6.33500   -35.52600 1.000 49.55000  ? 215 LYS   B HA     1 
ATOM   7726 N N      . GLN   B 1 250 ? 6.23900   4.93400   -36.42200 1.000 45.12000  ? 216 GLN   B N      1 
ATOM   7727 C CA     . GLN   B 1 250 ? 4.95500   4.22100   -36.24700 1.000 39.67000  ? 216 GLN   B CA     1 
ATOM   7728 C C      . GLN   B 1 250 ? 3.75800   5.01100   -36.78900 1.000 42.63000  ? 216 GLN   B C      1 
ATOM   7729 O O      . GLN   B 1 250 ? 2.62900   4.84300   -36.32900 1.000 35.46000  ? 216 GLN   B O      1 
ATOM   7730 C CB     . GLN   B 1 250 ? 4.68800   3.86400   -34.77700 1.000 40.20000  ? 216 GLN   B CB     1 
ATOM   7731 C CG     . GLN   B 1 250 ? 5.63100   2.84800   -34.14700 1.000 54.00000  ? 216 GLN   B CG     1 
ATOM   7732 C CD     . GLN   B 1 250 ? 6.99900   3.43800   -33.88800 1.000 67.79000  ? 216 GLN   B CD     1 
ATOM   7733 O OE1    . GLN   B 1 250 ? 7.97000   3.09700   -34.56900 1.000 76.92000  ? 216 GLN   B OE1    1 
ATOM   7734 N NE2    . GLN   B 1 250 ? 7.08300   4.35100   -32.91800 1.000 65.25000  ? 216 GLN   B NE2    1 
ATOM   7735 H H      . GLN   B 1 250 ? 6.82400   4.48300   -36.86200 1.000 45.12000  ? 216 GLN   B H      1 
ATOM   7736 H HA     . GLN   B 1 250 ? 5.00000   3.38900   -36.74300 1.000 39.67000  ? 216 GLN   B HA     1 
ATOM   7737 H HB2    . GLN   B 1 250 ? 4.74600   4.67600   -34.25000 1.000 40.20000  ? 216 GLN   B HB2    1 
ATOM   7738 H HB3    . GLN   B 1 250 ? 3.79100   3.50000   -34.70900 1.000 40.20000  ? 216 GLN   B HB3    1 
ATOM   7739 H HG2    . GLN   B 1 250 ? 5.26300   2.55300   -33.30000 1.000 54.00000  ? 216 GLN   B HG2    1 
ATOM   7740 H HG3    . GLN   B 1 250 ? 5.73500   2.09400   -34.74800 1.000 54.00000  ? 216 GLN   B HG3    1 
ATOM   7741 H HE21   . GLN   B 1 250 ? 6.38200   4.56600   -32.46800 1.000 65.25000  ? 216 GLN   B HE21   1 
ATOM   7742 H HE22   . GLN   B 1 250 ? 7.84000   4.71600   -32.73600 1.000 65.25000  ? 216 GLN   B HE22   1 
ATOM   7743 N N      . GLY   B 1 251 ? 3.97200   5.88000   -37.77200 1.000 37.46000  ? 217 GLY   B N      1 
ATOM   7744 C CA     . GLY   B 1 251 ? 2.86900   6.65300   -38.32700 1.000 33.98000  ? 217 GLY   B CA     1 
ATOM   7745 C C      . GLY   B 1 251 ? 2.58500   7.99400   -37.66700 1.000 33.88000  ? 217 GLY   B C      1 
ATOM   7746 O O      . GLY   B 1 251 ? 1.69300   8.71000   -38.13900 1.000 32.71000  ? 217 GLY   B O      1 
ATOM   7747 H H      . GLY   B 1 251 ? 4.73700   6.03900   -38.13100 1.000 37.46000  ? 217 GLY   B H      1 
ATOM   7748 H HA2    . GLY   B 1 251 ? 3.05200   6.82200   -39.26400 1.000 33.98000  ? 217 GLY   B HA2    1 
ATOM   7749 H HA3    . GLY   B 1 251 ? 2.05900   6.12300   -38.27600 1.000 33.98000  ? 217 GLY   B HA3    1 
ATOM   7750 N N      . PHE   B 1 252 ? 3.29000   8.34700   -36.59000 1.000 30.59000  ? 218 PHE   B N      1 
ATOM   7751 C CA     . PHE   B 1 252 ? 3.05200   9.61200   -35.88300 1.000 29.28000  ? 218 PHE   B CA     1 
ATOM   7752 C C      . PHE   B 1 252 ? 3.73700   10.76100  -36.62600 1.000 32.30000  ? 218 PHE   B C      1 
ATOM   7753 O O      . PHE   B 1 252 ? 4.85000   10.60200  -37.14000 1.000 35.19000  ? 218 PHE   B O      1 
ATOM   7754 C CB     . PHE   B 1 252 ? 3.58600   9.52700   -34.44600 1.000 29.19000  ? 218 PHE   B CB     1 
ATOM   7755 C CG     . PHE   B 1 252 ? 2.78700   8.59800   -33.54500 1.000 33.20000  ? 218 PHE   B CG     1 
ATOM   7756 C CD1    . PHE   B 1 252 ? 3.01100   7.23000   -33.57000 1.000 38.77000  ? 218 PHE   B CD1    1 
ATOM   7757 C CD2    . PHE   B 1 252 ? 1.81600   9.09400   -32.67900 1.000 31.68000  ? 218 PHE   B CD2    1 
ATOM   7758 C CE1    . PHE   B 1 252 ? 2.28400   6.36600   -32.75400 1.000 35.32000  ? 218 PHE   B CE1    1 
ATOM   7759 C CE2    . PHE   B 1 252 ? 1.07800   8.22600   -31.84700 1.000 33.38000  ? 218 PHE   B CE2    1 
ATOM   7760 C CZ     . PHE   B 1 252 ? 1.31300   6.86700   -31.89100 1.000 35.44000  ? 218 PHE   B CZ     1 
ATOM   7761 H H      . PHE   B 1 252 ? 3.91600   7.86900   -36.24500 1.000 30.59000  ? 218 PHE   B H      1 
ATOM   7762 H HA     . PHE   B 1 252 ? 2.10000   9.78900   -35.84900 1.000 29.28000  ? 218 PHE   B HA     1 
ATOM   7763 H HB2    . PHE   B 1 252 ? 4.49900   9.20200   -34.47100 1.000 29.19000  ? 218 PHE   B HB2    1 
ATOM   7764 H HB3    . PHE   B 1 252 ? 3.56400   10.41300  -34.05200 1.000 29.19000  ? 218 PHE   B HB3    1 
ATOM   7765 H HD1    . PHE   B 1 252 ? 3.65400   6.88200   -34.14400 1.000 38.77000  ? 218 PHE   B HD1    1 
ATOM   7766 H HD2    . PHE   B 1 252 ? 1.65200   10.00900  -32.64800 1.000 31.68000  ? 218 PHE   B HD2    1 
ATOM   7767 H HE1    . PHE   B 1 252 ? 2.44800   5.45100   -32.78500 1.000 35.32000  ? 218 PHE   B HE1    1 
ATOM   7768 H HE2    . PHE   B 1 252 ? 0.43100   8.56900   -31.27300 1.000 33.38000  ? 218 PHE   B HE2    1 
ATOM   7769 H HZ     . PHE   B 1 252 ? 0.83000   6.29000   -31.34400 1.000 35.44000  ? 218 PHE   B HZ     1 
ATOM   7770 N N      . GLY   B 1 253 ? 3.07700   11.91900  -36.68500 1.000 29.96000  ? 219 GLY   B N      1 
ATOM   7771 C CA     . GLY   B 1 253 ? 3.68300   13.03700  -37.40400 1.000 30.23000  ? 219 GLY   B CA     1 
ATOM   7772 C C      . GLY   B 1 253 ? 2.95000   14.33600  -37.11600 1.000 30.19000  ? 219 GLY   B C      1 
ATOM   7773 O O      . GLY   B 1 253 ? 1.92300   14.36300  -36.43300 1.000 29.30000  ? 219 GLY   B O      1 
ATOM   7774 H H      . GLY   B 1 253 ? 2.30900   12.07900  -36.33300 1.000 29.96000  ? 219 GLY   B H      1 
ATOM   7775 H HA2    . GLY   B 1 253 ? 4.61000   13.13600  -37.13400 1.000 30.23000  ? 219 GLY   B HA2    1 
ATOM   7776 H HA3    . GLY   B 1 253 ? 3.65300   12.86700  -38.35900 1.000 30.23000  ? 219 GLY   B HA3    1 
ATOM   7777 N N      . GLY   B 1 254 ? 3.48100   15.43600  -37.64800 1.000 29.79000  ? 220 GLY   B N      1 
ATOM   7778 C CA     . GLY   B 1 254 ? 2.95100   16.76400  -37.33300 1.000 27.65000  ? 220 GLY   B CA     1 
ATOM   7779 C C      . GLY   B 1 254 ? 1.75300   17.11900  -38.20200 1.000 29.04000  ? 220 GLY   B C      1 
ATOM   7780 O O      . GLY   B 1 254 ? 1.76900   16.90800  -39.40700 1.000 29.45000  ? 220 GLY   B O      1 
ATOM   7781 H H      . GLY   B 1 254 ? 4.14700   15.44200  -38.19300 1.000 29.79000  ? 220 GLY   B H      1 
ATOM   7782 H HA2    . GLY   B 1 254 ? 2.67700   16.79200  -36.40300 1.000 27.65000  ? 220 GLY   B HA2    1 
ATOM   7783 H HA3    . GLY   B 1 254 ? 3.64200   17.43100  -37.47200 1.000 27.65000  ? 220 GLY   B HA3    1 
ATOM   7784 N N      . LEU   B 1 255 ? 0.72800   17.69600  -37.57100 1.000 28.00000  ? 221 LEU   B N      1 
ATOM   7785 C CA     . LEU   B 1 255 ? -0.50200  18.06500  -38.26600 1.000 26.41000  ? 221 LEU   B CA     1 
ATOM   7786 C C      . LEU   B 1 255 ? -0.41700  19.50700  -38.73200 1.000 27.01000  ? 221 LEU   B C      1 
ATOM   7787 O O      . LEU   B 1 255 ? 0.02700   20.37400  -37.98100 1.000 29.24000  ? 221 LEU   B O      1 
ATOM   7788 C CB     . LEU   B 1 255 ? -1.72400  17.94000  -37.35700 1.000 27.36000  ? 221 LEU   B CB     1 
ATOM   7789 C CG     . LEU   B 1 255 ? -1.86000  16.53800  -36.75300 1.000 28.58000  ? 221 LEU   B CG     1 
ATOM   7790 C CD1    . LEU   B 1 255 ? -2.86200  16.61000  -35.61900 1.000 30.01000  ? 221 LEU   B CD1    1 
ATOM   7791 C CD2    . LEU   B 1 255 ? -2.33600  15.58200  -37.84500 1.000 28.73000  ? 221 LEU   B CD2    1 
ATOM   7792 H H      . LEU   B 1 255 ? 0.72300   17.88500  -36.73200 1.000 28.00000  ? 221 LEU   B H      1 
ATOM   7793 H HA     . LEU   B 1 255 ? -0.62700  17.49400  -39.03900 1.000 26.41000  ? 221 LEU   B HA     1 
ATOM   7794 H HB2    . LEU   B 1 255 ? -1.64300  18.57500  -36.62900 1.000 27.36000  ? 221 LEU   B HB2    1 
ATOM   7795 H HB3    . LEU   B 1 255 ? -2.52400  18.12500  -37.87300 1.000 27.36000  ? 221 LEU   B HB3    1 
ATOM   7796 H HG     . LEU   B 1 255 ? -1.00700  16.23200  -36.40700 1.000 28.58000  ? 221 LEU   B HG     1 
ATOM   7797 H HD11   . LEU   B 1 255 ? -2.97200  15.72400  -35.23900 1.000 30.01000  ? 221 LEU   B HD11   1 
ATOM   7798 H HD12   . LEU   B 1 255 ? -2.53000  17.22200  -34.94300 1.000 30.01000  ? 221 LEU   B HD12   1 
ATOM   7799 H HD13   . LEU   B 1 255 ? -3.71000  16.92800  -35.96700 1.000 30.01000  ? 221 LEU   B HD13   1 
ATOM   7800 H HD21   . LEU   B 1 255 ? -2.48900  14.70800  -37.45300 1.000 28.73000  ? 221 LEU   B HD21   1 
ATOM   7801 H HD22   . LEU   B 1 255 ? -3.16100  15.92300  -38.22500 1.000 28.73000  ? 221 LEU   B HD22   1 
ATOM   7802 H HD23   . LEU   B 1 255 ? -1.65500  15.52200  -38.53300 1.000 28.73000  ? 221 LEU   B HD23   1 
ATOM   7803 N N      . GLY   B 1 256 ? -0.85600  19.75300  -39.96600 1.000 28.92000  ? 222 GLY   B N      1 
ATOM   7804 C CA     . GLY   B 1 256 ? -1.00000  21.10300  -40.46500 1.000 27.91000  ? 222 GLY   B CA     1 
ATOM   7805 C C      . GLY   B 1 256 ? -2.37900  21.28200  -41.08600 1.000 31.28000  ? 222 GLY   B C      1 
ATOM   7806 O O      . GLY   B 1 256 ? -3.12800  20.32600  -41.26300 1.000 29.51000  ? 222 GLY   B O      1 
ATOM   7807 H H      . GLY   B 1 256 ? -1.07700  19.14500  -40.53200 1.000 28.92000  ? 222 GLY   B H      1 
ATOM   7808 H HA2    . GLY   B 1 256 ? -0.89700  21.74000  -39.74100 1.000 27.91000  ? 222 GLY   B HA2    1 
ATOM   7809 H HA3    . GLY   B 1 256 ? -0.32500  21.28000  -41.13900 1.000 27.91000  ? 222 GLY   B HA3    1 
ATOM   7810 N N      . GLY   B 1 257 ? -2.70200  22.52400  -41.40700 1.000 28.57000  ? 223 GLY   B N      1 
ATOM   7811 C CA     . GLY   B 1 257 ? -3.95500  22.73000  -42.10500 1.000 28.05000  ? 223 GLY   B CA     1 
ATOM   7812 C C      . GLY   B 1 257 ? -5.10200  23.16400  -41.21800 1.000 27.20000  ? 223 GLY   B C      1 
ATOM   7813 O O      . GLY   B 1 257 ? -4.91300  23.76600  -40.15400 1.000 30.24000  ? 223 GLY   B O      1 
ATOM   7814 H H      . GLY   B 1 257 ? -2.24000  23.23000  -41.24200 1.000 28.57000  ? 223 GLY   B H      1 
ATOM   7815 H HA2    . GLY   B 1 257 ? -3.82700  23.41500  -42.77900 1.000 28.05000  ? 223 GLY   B HA2    1 
ATOM   7816 H HA3    . GLY   B 1 257 ? -4.21500  21.91300  -42.55800 1.000 28.05000  ? 223 GLY   B HA3    1 
ATOM   7817 N N      . ARG   B 1 258 ? -6.31400  22.81200  -41.64200 1.000 28.28000  ? 224 ARG   B N      1 
ATOM   7818 C CA     . ARG   B 1 258 ? -7.49600  23.29100  -40.94200 1.000 33.55000  ? 224 ARG   B CA     1 
ATOM   7819 C C      . ARG   B 1 258 ? -7.56000  22.75800  -39.51200 1.000 33.30000  ? 224 ARG   B C      1 
ATOM   7820 O O      . ARG   B 1 258 ? -8.10600  23.42600  -38.62700 1.000 32.81000  ? 224 ARG   B O      1 
ATOM   7821 C CB     . ARG   B 1 258 ? -8.75400  22.93500  -41.75000 1.000 36.94000  ? 224 ARG   B CB     1 
ATOM   7822 C CG     . ARG   B 1 258 ? -8.80200  23.70200  -43.11600 1.000 44.55000  ? 224 ARG   B CG     1 
ATOM   7823 C CD     . ARG   B 1 258 ? -10.05400 23.41400  -43.98400 1.000 52.94000  ? 224 ARG   B CD     1 
ATOM   7824 N NE     . ARG   B 1 258 ? -10.45500 24.57800  -44.77700 1.000 71.38000  ? 224 ARG   B NE     1 
ATOM   7825 C CZ     . ARG   B 1 258 ? -10.29100 24.71700  -46.09200 1.000 65.07000  ? 224 ARG   B CZ     1 
ATOM   7826 N NH1    . ARG   B 1 258 ? -9.76800  23.75200  -46.83700 1.000 52.99000  ? 224 ARG   B NH1    1 
ATOM   7827 N NH2    . ARG   B 1 258 ? -10.66300 25.85900  -46.67700 1.000 59.33000  ? 224 ARG   B NH2    1 
ATOM   7828 H H      . ARG   B 1 258 ? -6.47500  22.30700  -42.31900 1.000 28.28000  ? 224 ARG   B H      1 
ATOM   7829 H HA     . ARG   B 1 258 ? -7.44900  24.25800  -40.88900 1.000 33.55000  ? 224 ARG   B HA     1 
ATOM   7830 H HB2    . ARG   B 1 258 ? -8.76600  21.98400  -41.93200 1.000 36.94000  ? 224 ARG   B HB2    1 
ATOM   7831 H HB3    . ARG   B 1 258 ? -9.53900  23.18500  -41.23800 1.000 36.94000  ? 224 ARG   B HB3    1 
ATOM   7832 H HG2    . ARG   B 1 258 ? -8.77300  24.65600  -42.94200 1.000 44.55000  ? 224 ARG   B HG2    1 
ATOM   7833 H HG3    . ARG   B 1 258 ? -8.02900  23.43800  -43.63500 1.000 44.55000  ? 224 ARG   B HG3    1 
ATOM   7834 H HD2    . ARG   B 1 258 ? -9.86600  22.67300  -44.57800 1.000 52.94000  ? 224 ARG   B HD2    1 
ATOM   7835 H HD3    . ARG   B 1 258 ? -10.79300 23.18600  -43.39900 1.000 52.94000  ? 224 ARG   B HD3    1 
ATOM   7836 H HE     . ARG   B 1 258 ? -10.82900 25.22900  -44.35700 1.000 71.38000  ? 224 ARG   B HE     1 
ATOM   7837 H HH11   . ARG   B 1 258 ? -9.52000  23.01100  -46.48000 1.000 52.99000  ? 224 ARG   B HH11   1 
ATOM   7838 H HH12   . ARG   B 1 258 ? -9.67500  23.87000  -47.68400 1.000 52.99000  ? 224 ARG   B HH12   1 
ATOM   7839 H HH21   . ARG   B 1 258 ? -11.00500 26.49200  -46.20600 1.000 59.33000  ? 224 ARG   B HH21   1 
ATOM   7840 H HH22   . ARG   B 1 258 ? -10.56500 25.95900  -47.52500 1.000 59.33000  ? 224 ARG   B HH22   1 
ATOM   7841 N N      . TYR   B 1 259 ? -6.97100  21.58000  -39.25100 1.000 31.44000  ? 225 TYR   B N      1 
ATOM   7842 C CA     . TYR   B 1 259 ? -6.94900  21.05000  -37.89000 1.000 29.68000  ? 225 TYR   B CA     1 
ATOM   7843 C C      . TYR   B 1 259 ? -6.38200  22.03800  -36.90100 1.000 31.09000  ? 225 TYR   B C      1 
ATOM   7844 O O      . TYR   B 1 259 ? -6.78800  22.04300  -35.73800 1.000 32.24000  ? 225 TYR   B O      1 
ATOM   7845 C CB     . TYR   B 1 259 ? -6.10000  19.77400  -37.78300 1.000 31.18000  ? 225 TYR   B CB     1 
ATOM   7846 C CG     . TYR   B 1 259 ? -6.59800  18.67100  -38.65000 1.000 31.01000  ? 225 TYR   B CG     1 
ATOM   7847 C CD1    . TYR   B 1 259 ? -7.70600  17.91500  -38.28100 1.000 31.69000  ? 225 TYR   B CD1    1 
ATOM   7848 C CD2    . TYR   B 1 259 ? -5.98100  18.40500  -39.85600 1.000 29.14000  ? 225 TYR   B CD2    1 
ATOM   7849 C CE1    . TYR   B 1 259 ? -8.18100  16.87600  -39.10200 1.000 32.97000  ? 225 TYR   B CE1    1 
ATOM   7850 C CE2    . TYR   B 1 259 ? -6.42600  17.36600  -40.67900 1.000 33.95000  ? 225 TYR   B CE2    1 
ATOM   7851 C CZ     . TYR   B 1 259 ? -7.53900  16.63000  -40.31300 1.000 38.44000  ? 225 TYR   B CZ     1 
ATOM   7852 O OH     . TYR   B 1 259 ? -7.96700  15.64000  -41.17600 1.000 37.96000  ? 225 TYR   B OH     1 
ATOM   7853 H H      . TYR   B 1 259 ? -6.58600  21.08200  -39.83600 1.000 31.44000  ? 225 TYR   B H      1 
ATOM   7854 H HA     . TYR   B 1 259 ? -7.85500  20.83500  -37.61800 1.000 29.68000  ? 225 TYR   B HA     1 
ATOM   7855 H HB2    . TYR   B 1 259 ? -5.19000  19.97700  -38.05000 1.000 31.18000  ? 225 TYR   B HB2    1 
ATOM   7856 H HB3    . TYR   B 1 259 ? -6.11400  19.46200  -36.86500 1.000 31.18000  ? 225 TYR   B HB3    1 
ATOM   7857 H HD1    . TYR   B 1 259 ? -8.13300  18.09200  -37.47400 1.000 31.69000  ? 225 TYR   B HD1    1 
ATOM   7858 H HD2    . TYR   B 1 259 ? -5.23800  18.90300  -40.10900 1.000 29.14000  ? 225 TYR   B HD2    1 
ATOM   7859 H HE1    . TYR   B 1 259 ? -8.92600  16.37800  -38.85200 1.000 32.97000  ? 225 TYR   B HE1    1 
ATOM   7860 H HE2    . TYR   B 1 259 ? -6.00700  17.20400  -41.49300 1.000 33.95000  ? 225 TYR   B HE2    1 
ATOM   7861 H HH     . TYR   B 1 259 ? -8.69100  15.31600  -40.90200 1.000 37.96000  ? 225 TYR   B HH     1 
ATOM   7862 N N      . VAL   B 1 260 ? -5.39600  22.83500  -37.31600 1.000 27.19000  ? 226 VAL   B N      1 
ATOM   7863 C CA     . VAL   B 1 260 ? -4.60800  23.58200  -36.34600 1.000 25.53000  ? 226 VAL   B CA     1 
ATOM   7864 C C      . VAL   B 1 260 ? -5.04000  25.03400  -36.21900 1.000 30.56000  ? 226 VAL   B C      1 
ATOM   7865 O O      . VAL   B 1 260 ? -4.44100  25.76900  -35.43400 1.000 27.86000  ? 226 VAL   B O      1 
ATOM   7866 C CB     . VAL   B 1 260 ? -3.09200  23.50100  -36.65400 1.000 24.59000  ? 226 VAL   B CB     1 
ATOM   7867 C CG1    . VAL   B 1 260 ? -2.67300  22.07100  -37.05900 1.000 28.25000  ? 226 VAL   B CG1    1 
ATOM   7868 C CG2    . VAL   B 1 260 ? -2.64400  24.51500  -37.73600 1.000 25.87000  ? 226 VAL   B CG2    1 
ATOM   7869 H H      . VAL   B 1 260 ? -5.16900  22.95700  -38.13700 1.000 27.19000  ? 226 VAL   B H      1 
ATOM   7870 H HA     . VAL   B 1 260 ? -4.73600  23.17400  -35.47500 1.000 25.53000  ? 226 VAL   B HA     1 
ATOM   7871 H HB     . VAL   B 1 260 ? -2.60900  23.72000  -35.84200 1.000 24.59000  ? 226 VAL   B HB     1 
ATOM   7872 H HG11   . VAL   B 1 260 ? -1.70600  22.03300  -37.12400 1.000 28.25000  ? 226 VAL   B HG11   1 
ATOM   7873 H HG12   . VAL   B 1 260 ? -2.98400  21.44800  -36.38300 1.000 28.25000  ? 226 VAL   B HG12   1 
ATOM   7874 H HG13   . VAL   B 1 260 ? -3.07100  21.85500  -37.91700 1.000 28.25000  ? 226 VAL   B HG13   1 
ATOM   7875 H HG21   . VAL   B 1 260 ? -1.76800  24.25800  -38.06500 1.000 25.87000  ? 226 VAL   B HG21   1 
ATOM   7876 H HG22   . VAL   B 1 260 ? -3.28600  24.50500  -38.46200 1.000 25.87000  ? 226 VAL   B HG22   1 
ATOM   7877 H HG23   . VAL   B 1 260 ? -2.60300  25.40100  -37.34300 1.000 25.87000  ? 226 VAL   B HG23   1 
ATOM   7878 N N      . PHE   B 1 261 ? -6.08800  25.46200  -36.91800 1.000 29.09000  ? 227 PHE   B N      1 
ATOM   7879 C CA     . PHE   B 1 261 ? -6.35600  26.90200  -36.99500 1.000 30.11000  ? 227 PHE   B CA     1 
ATOM   7880 C C      . PHE   B 1 261 ? -6.74100  27.51800  -35.65100 1.000 31.39000  ? 227 PHE   B C      1 
ATOM   7881 O O      . PHE   B 1 261 ? -6.13200  28.53000  -35.26700 1.000 30.46000  ? 227 PHE   B O      1 
ATOM   7882 C CB     . PHE   B 1 261 ? -7.40700  27.17000  -38.07800 1.000 27.02000  ? 227 PHE   B CB     1 
ATOM   7883 C CG     . PHE   B 1 261 ? -7.68300  28.63100  -38.31800 1.000 26.43000  ? 227 PHE   B CG     1 
ATOM   7884 C CD1    . PHE   B 1 261 ? -6.68900  29.47800  -38.78000 1.000 29.44000  ? 227 PHE   B CD1    1 
ATOM   7885 C CD2    . PHE   B 1 261 ? -8.95800  29.13000  -38.14200 1.000 34.48000  ? 227 PHE   B CD2    1 
ATOM   7886 C CE1    . PHE   B 1 261 ? -6.96800  30.83200  -39.04600 1.000 28.48000  ? 227 PHE   B CE1    1 
ATOM   7887 C CE2    . PHE   B 1 261 ? -9.24400  30.48000  -38.40600 1.000 38.15000  ? 227 PHE   B CE2    1 
ATOM   7888 C CZ     . PHE   B 1 261 ? -8.25000  31.32100  -38.85000 1.000 32.33000  ? 227 PHE   B CZ     1 
ATOM   7889 H H      . PHE   B 1 261 ? -6.64400  24.96200  -37.34400 1.000 29.09000  ? 227 PHE   B H      1 
ATOM   7890 H HA     . PHE   B 1 261 ? -5.53900  27.34100  -37.28000 1.000 30.11000  ? 227 PHE   B HA     1 
ATOM   7891 H HB2    . PHE   B 1 261 ? -7.08400  26.79700  -38.91300 1.000 27.02000  ? 227 PHE   B HB2    1 
ATOM   7892 H HB3    . PHE   B 1 261 ? -8.24300  26.74700  -37.84300 1.000 27.02000  ? 227 PHE   B HB3    1 
ATOM   7893 H HD1    . PHE   B 1 261 ? -5.83000  29.14900  -38.91600 1.000 29.44000  ? 227 PHE   B HD1    1 
ATOM   7894 H HD2    . PHE   B 1 261 ? -9.63600  28.56600  -37.84600 1.000 34.48000  ? 227 PHE   B HD2    1 
ATOM   7895 H HE1    . PHE   B 1 261 ? -6.29300  31.39800  -39.34300 1.000 28.48000  ? 227 PHE   B HE1    1 
ATOM   7896 H HE2    . PHE   B 1 261 ? -10.10400 30.80800  -38.27100 1.000 38.15000  ? 227 PHE   B HE2    1 
ATOM   7897 H HZ     . PHE   B 1 261 ? -8.43700  32.21700  -39.01500 1.000 32.33000  ? 227 PHE   B HZ     1 
ATOM   7898 N N      . PRO   B 1 262 ? -7.72100  27.00200  -34.90000 1.000 31.33000  ? 228 PRO   B N      1 
ATOM   7899 C CA     . PRO   B 1 262 ? -8.00800  27.62200  -33.58800 1.000 32.31000  ? 228 PRO   B CA     1 
ATOM   7900 C C      . PRO   B 1 262 ? -6.82900  27.56700  -32.62800 1.000 32.84000  ? 228 PRO   B C      1 
ATOM   7901 O O      . PRO   B 1 262 ? -6.63100  28.50800  -31.84500 1.000 29.44000  ? 228 PRO   B O      1 
ATOM   7902 C CB     . PRO   B 1 262 ? -9.21600  26.82600  -33.06100 1.000 35.50000  ? 228 PRO   B CB     1 
ATOM   7903 C CG     . PRO   B 1 262 ? -9.79600  26.11900  -34.24300 1.000 32.84000  ? 228 PRO   B CG     1 
ATOM   7904 C CD     . PRO   B 1 262 ? -8.64900  25.90300  -35.22500 1.000 32.72000  ? 228 PRO   B CD     1 
ATOM   7905 H HA     . PRO   B 1 262 ? -8.27100  28.54800  -33.71000 1.000 32.31000  ? 228 PRO   B HA     1 
ATOM   7906 H HB2    . PRO   B 1 262 ? -8.91700  26.18700  -32.39600 1.000 35.50000  ? 228 PRO   B HB2    1 
ATOM   7907 H HB3    . PRO   B 1 262 ? -9.86500  27.43700  -32.67900 1.000 35.50000  ? 228 PRO   B HB3    1 
ATOM   7908 H HG2    . PRO   B 1 262 ? -10.16500 25.26800  -33.96100 1.000 32.84000  ? 228 PRO   B HG2    1 
ATOM   7909 H HG3    . PRO   B 1 262 ? -10.48500 26.67200  -34.64300 1.000 32.84000  ? 228 PRO   B HG3    1 
ATOM   7910 H HD2    . PRO   B 1 262 ? -8.22900  25.04400  -35.07200 1.000 32.72000  ? 228 PRO   B HD2    1 
ATOM   7911 H HD3    . PRO   B 1 262 ? -8.98200  25.97700  -36.12800 1.000 32.72000  ? 228 PRO   B HD3    1 
ATOM   7912 N N      . THR   B 1 263 ? -6.03300  26.48900  -32.65200 1.000 25.25000  ? 229 THR   B N      1 
ATOM   7913 C CA     . THR   B 1 263 ? -4.81700  26.46900  -31.84400 1.000 27.19000  ? 229 THR   B CA     1 
ATOM   7914 C C      . THR   B 1 263 ? -3.82900  27.54300  -32.27800 1.000 28.95000  ? 229 THR   B C      1 
ATOM   7915 O O      . THR   B 1 263 ? -3.21400  28.20200  -31.43300 1.000 27.32000  ? 229 THR   B O      1 
ATOM   7916 C CB     . THR   B 1 263 ? -4.16000  25.08500  -31.93700 1.000 29.33000  ? 229 THR   B CB     1 
ATOM   7917 O OG1    . THR   B 1 263 ? -5.06200  24.12000  -31.40400 1.000 30.43000  ? 229 THR   B OG1    1 
ATOM   7918 C CG2    . THR   B 1 263 ? -2.87300  25.04800  -31.15000 1.000 27.10000  ? 229 THR   B CG2    1 
ATOM   7919 H H      . THR   B 1 263 ? -6.17300  25.77800  -33.11500 1.000 25.25000  ? 229 THR   B H      1 
ATOM   7920 H HA     . THR   B 1 263 ? -5.05000  26.63100  -30.91600 1.000 27.19000  ? 229 THR   B HA     1 
ATOM   7921 H HB     . THR   B 1 263 ? -3.96500  24.87500  -32.86400 1.000 29.33000  ? 229 THR   B HB     1 
ATOM   7922 H HG1    . THR   B 1 263 ? -5.23300  24.29900  -30.60100 1.000 30.43000  ? 229 THR   B HG1    1 
ATOM   7923 H HG21   . THR   B 1 263 ? -2.60000  24.12800  -31.00900 1.000 27.10000  ? 229 THR   B HG21   1 
ATOM   7924 H HG22   . THR   B 1 263 ? -2.17200  25.51300  -31.63300 1.000 27.10000  ? 229 THR   B HG22   1 
ATOM   7925 H HG23   . THR   B 1 263 ? -3.00000  25.47300  -30.28700 1.000 27.10000  ? 229 THR   B HG23   1 
ATOM   7926 N N      . ALA   B 1 264 ? -3.64000  27.71500  -33.58700 1.000 29.53000  ? 230 ALA   B N      1 
ATOM   7927 C CA     . ALA   B 1 264 ? -2.70400  28.73700  -34.06700 1.000 27.10000  ? 230 ALA   B CA     1 
ATOM   7928 C C      . ALA   B 1 264 ? -3.14500  30.14500  -33.65800 1.000 27.38000  ? 230 ALA   B C      1 
ATOM   7929 O O      . ALA   B 1 264 ? -2.32500  30.94800  -33.19000 1.000 28.37000  ? 230 ALA   B O      1 
ATOM   7930 C CB     . ALA   B 1 264 ? -2.56100  28.63400  -35.59300 1.000 25.79000  ? 230 ALA   B CB     1 
ATOM   7931 H H      . ALA   B 1 264 ? -4.03100  27.26500  -34.20600 1.000 29.53000  ? 230 ALA   B H      1 
ATOM   7932 H HA     . ALA   B 1 264 ? -1.83200  28.57300  -33.67500 1.000 27.10000  ? 230 ALA   B HA     1 
ATOM   7933 H HB1    . ALA   B 1 264 ? -1.94000  29.31400  -35.89800 1.000 25.79000  ? 230 ALA   B HB1    1 
ATOM   7934 H HB2    . ALA   B 1 264 ? -2.22500  27.75300  -35.81900 1.000 25.79000  ? 230 ALA   B HB2    1 
ATOM   7935 H HB3    . ALA   B 1 264 ? -3.43000  28.77200  -36.00100 1.000 25.79000  ? 230 ALA   B HB3    1 
ATOM   7936 N N      . LEU   B 1 265 ? -4.42800  30.47100  -33.83900 1.000 27.79000  ? 231 LEU   B N      1 
ATOM   7937 C CA     . LEU   B 1 265 ? -4.89600  31.80300  -33.43600 1.000 28.69000  ? 231 LEU   B CA     1 
ATOM   7938 C C      . LEU   B 1 265 ? -4.69900  32.01700  -31.94700 1.000 31.22000  ? 231 LEU   B C      1 
ATOM   7939 O O      . LEU   B 1 265 ? -4.35500  33.12400  -31.50200 1.000 29.33000  ? 231 LEU   B O      1 
ATOM   7940 C CB     . LEU   B 1 265 ? -6.37300  31.99100  -33.76400 1.000 27.06000  ? 231 LEU   B CB     1 
ATOM   7941 C CG     . LEU   B 1 265 ? -6.85100  32.06500  -35.19200 1.000 34.83000  ? 231 LEU   B CG     1 
ATOM   7942 C CD1    . LEU   B 1 265 ? -8.35700  32.24600  -35.14200 1.000 37.47000  ? 231 LEU   B CD1    1 
ATOM   7943 C CD2    . LEU   B 1 265 ? -6.17700  33.22100  -35.94100 1.000 29.87000  ? 231 LEU   B CD2    1 
ATOM   7944 H H      . LEU   B 1 265 ? -5.02900  29.96000  -34.18100 1.000 27.79000  ? 231 LEU   B H      1 
ATOM   7945 H HA     . LEU   B 1 265 ? -4.38800  32.47900  -33.91100 1.000 28.69000  ? 231 LEU   B HA     1 
ATOM   7946 H HB2    . LEU   B 1 265 ? -6.85300  31.25400  -33.35600 1.000 27.06000  ? 231 LEU   B HB2    1 
ATOM   7947 H HB3    . LEU   B 1 265 ? -6.65700  32.81600  -33.34000 1.000 27.06000  ? 231 LEU   B HB3    1 
ATOM   7948 H HG     . LEU   B 1 265 ? -6.65000  31.23400  -35.65000 1.000 34.83000  ? 231 LEU   B HG     1 
ATOM   7949 H HD11   . LEU   B 1 265 ? -8.69800  32.29900  -36.04800 1.000 37.47000  ? 231 LEU   B HD11   1 
ATOM   7950 H HD12   . LEU   B 1 265 ? -8.75100  31.48700  -34.68400 1.000 37.47000  ? 231 LEU   B HD12   1 
ATOM   7951 H HD13   . LEU   B 1 265 ? -8.56100  33.06400  -34.66300 1.000 37.47000  ? 231 LEU   B HD13   1 
ATOM   7952 H HD21   . LEU   B 1 265 ? -6.54600  33.27400  -36.83700 1.000 29.87000  ? 231 LEU   B HD21   1 
ATOM   7953 H HD22   . LEU   B 1 265 ? -6.34800  34.04800  -35.46400 1.000 29.87000  ? 231 LEU   B HD22   1 
ATOM   7954 H HD23   . LEU   B 1 265 ? -5.22200  33.05500  -35.98500 1.000 29.87000  ? 231 LEU   B HD23   1 
ATOM   7955 N N      . ALA   B 1 266 ? -4.97500  30.98300  -31.14800 1.000 29.59000  ? 232 ALA   B N      1 
ATOM   7956 C CA     . ALA   B 1 266 ? -4.80700  31.13100  -29.70800 1.000 27.43000  ? 232 ALA   B CA     1 
ATOM   7957 C C      . ALA   B 1 266 ? -3.35900  31.41000  -29.35800 1.000 29.49000  ? 232 ALA   B C      1 
ATOM   7958 O O      . ALA   B 1 266 ? -3.06900  32.22400  -28.47300 1.000 29.21000  ? 232 ALA   B O      1 
ATOM   7959 C CB     . ALA   B 1 266 ? -5.30000  29.88200  -28.97500 1.000 26.14000  ? 232 ALA   B CB     1 
ATOM   7960 H H      . ALA   B 1 266 ? -5.25200  30.21100  -31.40700 1.000 29.59000  ? 232 ALA   B H      1 
ATOM   7961 H HA     . ALA   B 1 266 ? -5.33800  31.88400  -29.40500 1.000 27.43000  ? 232 ALA   B HA     1 
ATOM   7962 H HB1    . ALA   B 1 266 ? -5.17200  30.00300  -28.02100 1.000 26.14000  ? 232 ALA   B HB1    1 
ATOM   7963 H HB2    . ALA   B 1 266 ? -6.24000  29.75200  -29.17000 1.000 26.14000  ? 232 ALA   B HB2    1 
ATOM   7964 H HB3    . ALA   B 1 266 ? -4.79000  29.11600  -29.28200 1.000 26.14000  ? 232 ALA   B HB3    1 
ATOM   7965 N N      . ASN   B 1 267 ? -2.42500  30.74700  -30.04400 1.000 27.92000  ? 233 ASN   B N      1 
ATOM   7966 C CA     . ASN   B 1 267 ? -1.01900  30.97500  -29.72800 1.000 27.60000  ? 233 ASN   B CA     1 
ATOM   7967 C C      . ASN   B 1 267 ? -0.58100  32.35800  -30.19700 1.000 31.15000  ? 233 ASN   B C      1 
ATOM   7968 O O      . ASN   B 1 267 ? 0.12700   33.07200  -29.47300 1.000 27.44000  ? 233 ASN   B O      1 
ATOM   7969 C CB     . ASN   B 1 267 ? -0.15700  29.86100  -30.34700 1.000 26.11000  ? 233 ASN   B CB     1 
ATOM   7970 C CG     . ASN   B 1 267 ? -0.04200  28.63800  -29.43600 1.000 25.33000  ? 233 ASN   B CG     1 
ATOM   7971 O OD1    . ASN   B 1 267 ? 0.98800   28.42600  -28.79800 1.000 29.84000  ? 233 ASN   B OD1    1 
ATOM   7972 N ND2    . ASN   B 1 267 ? -1.10900  27.85000  -29.36500 1.000 28.76000  ? 233 ASN   B ND2    1 
ATOM   7973 H H      . ASN   B 1 267 ? -2.57400  30.18100  -30.67400 1.000 27.92000  ? 233 ASN   B H      1 
ATOM   7974 H HA     . ASN   B 1 267 ? -0.90400  30.93800  -28.76500 1.000 27.60000  ? 233 ASN   B HA     1 
ATOM   7975 H HB2    . ASN   B 1 267 ? -0.55500  29.57800  -31.18500 1.000 26.11000  ? 233 ASN   B HB2    1 
ATOM   7976 H HB3    . ASN   B 1 267 ? 0.73700   30.20300  -30.50100 1.000 26.11000  ? 233 ASN   B HB3    1 
ATOM   7977 H HD21   . ASN   B 1 267 ? -1.09400  27.15000  -28.86500 1.000 28.76000  ? 233 ASN   B HD21   1 
ATOM   7978 H HD22   . ASN   B 1 267 ? -1.81200  28.03500  -29.82500 1.000 28.76000  ? 233 ASN   B HD22   1 
ATOM   7979 N N      . VAL   B 1 268 ? -1.00600  32.76500  -31.39200 1.000 28.49000  ? 234 VAL   B N      1 
ATOM   7980 C CA     . VAL   B 1 268 ? -0.71000  34.12000  -31.85700 1.000 26.58000  ? 234 VAL   B CA     1 
ATOM   7981 C C      . VAL   B 1 268 ? -1.19400  35.14500  -30.83700 1.000 28.01000  ? 234 VAL   B C      1 
ATOM   7982 O O      . VAL   B 1 268 ? -0.45100  36.04600  -30.42800 1.000 28.34000  ? 234 VAL   B O      1 
ATOM   7983 C CB     . VAL   B 1 268 ? -1.33400  34.36900  -33.24300 1.000 24.00000  ? 234 VAL   B CB     1 
ATOM   7984 C CG1    . VAL   B 1 268 ? -1.31200  35.90300  -33.60200 1.000 26.07000  ? 234 VAL   B CG1    1 
ATOM   7985 C CG2    . VAL   B 1 268 ? -0.60000  33.57200  -34.35700 1.000 23.30000  ? 234 VAL   B CG2    1 
ATOM   7986 H H      . VAL   B 1 268 ? -1.45900  32.28600  -31.94400 1.000 28.49000  ? 234 VAL   B H      1 
ATOM   7987 H HA     . VAL   B 1 268 ? 0.25100   34.21800  -31.94300 1.000 26.58000  ? 234 VAL   B HA     1 
ATOM   7988 H HB     . VAL   B 1 268 ? -2.25900  34.07900  -33.22800 1.000 24.00000  ? 234 VAL   B HB     1 
ATOM   7989 H HG11   . VAL   B 1 268 ? -1.46300  36.00400  -34.55500 1.000 26.07000  ? 234 VAL   B HG11   1 
ATOM   7990 H HG12   . VAL   B 1 268 ? -2.01300  36.35600  -33.10800 1.000 26.07000  ? 234 VAL   B HG12   1 
ATOM   7991 H HG13   . VAL   B 1 268 ? -0.44600  36.27000  -33.36500 1.000 26.07000  ? 234 VAL   B HG13   1 
ATOM   7992 H HG21   . VAL   B 1 268 ? -1.02800  33.75300  -35.20800 1.000 23.30000  ? 234 VAL   B HG21   1 
ATOM   7993 H HG22   . VAL   B 1 268 ? 0.32800   33.85300  -34.38700 1.000 23.30000  ? 234 VAL   B HG22   1 
ATOM   7994 H HG23   . VAL   B 1 268 ? -0.65300  32.62500  -34.15400 1.000 23.30000  ? 234 VAL   B HG23   1 
ATOM   7995 N N      . ASN   B 1 269 ? -2.44200  35.01400  -30.39100 1.000 29.14000  ? 235 ASN   B N      1 
ATOM   7996 C CA     . ASN   B 1 269 ? -2.97000  36.04000  -29.48600 1.000 29.24000  ? 235 ASN   B CA     1 
ATOM   7997 C C      . ASN   B 1 269 ? -2.32700  35.96300  -28.09800 1.000 31.59000  ? 235 ASN   B C      1 
ATOM   7998 O O      . ASN   B 1 269 ? -2.07900  36.99100  -27.46800 1.000 31.16000  ? 235 ASN   B O      1 
ATOM   7999 C CB     . ASN   B 1 269 ? -4.49200  35.93200  -29.39400 1.000 29.91000  ? 235 ASN   B CB     1 
ATOM   8000 C CG     . ASN   B 1 269 ? -5.10200  37.10300  -28.62100 1.000 37.30000  ? 235 ASN   B CG     1 
ATOM   8001 O OD1    . ASN   B 1 269 ? -5.68800  36.92400  -27.56300 1.000 36.04000  ? 235 ASN   B OD1    1 
ATOM   8002 N ND2    . ASN   B 1 269 ? -4.90500  38.31000  -29.13300 1.000 30.40000  ? 235 ASN   B ND2    1 
ATOM   8003 H H      . ASN   B 1 269 ? -2.98300  34.37400  -30.58400 1.000 29.14000  ? 235 ASN   B H      1 
ATOM   8004 H HA     . ASN   B 1 269 ? -2.76100  36.91200  -29.85500 1.000 29.24000  ? 235 ASN   B HA     1 
ATOM   8005 H HB2    . ASN   B 1 269 ? -4.86600  35.93200  -30.28900 1.000 29.91000  ? 235 ASN   B HB2    1 
ATOM   8006 H HB3    . ASN   B 1 269 ? -4.72600  35.11100  -28.93400 1.000 29.91000  ? 235 ASN   B HB3    1 
ATOM   8007 H HD21   . ASN   B 1 269 ? -5.22300  39.00300  -28.73500 1.000 30.40000  ? 235 ASN   B HD21   1 
ATOM   8008 H HD22   . ASN   B 1 269 ? -4.47900  38.39800  -29.87500 1.000 30.40000  ? 235 ASN   B HD22   1 
ATOM   8009 N N      . ALA   B 1 270 ? -2.05800  34.75700  -27.58900 1.000 29.46000  ? 236 ALA   B N      1 
ATOM   8010 C CA     . ALA   B 1 270 ? -1.43300  34.64500  -26.26700 1.000 35.17000  ? 236 ALA   B CA     1 
ATOM   8011 C C      . ALA   B 1 270 ? -0.07100  35.33100  -26.23000 1.000 34.07000  ? 236 ALA   B C      1 
ATOM   8012 O O      . ALA   B 1 270 ? 0.24700   36.06000  -25.27400 1.000 31.92000  ? 236 ALA   B O      1 
ATOM   8013 C CB     . ALA   B 1 270 ? -1.29900  33.16700  -25.87700 1.000 30.38000  ? 236 ALA   B CB     1 
ATOM   8014 H H      . ALA   B 1 270 ? -2.22200  34.00700  -27.97700 1.000 29.46000  ? 236 ALA   B H      1 
ATOM   8015 H HA     . ALA   B 1 270 ? -2.00300  35.07700  -25.61200 1.000 35.17000  ? 236 ALA   B HA     1 
ATOM   8016 H HB1    . ALA   B 1 270 ? -0.88500  33.10800  -25.00200 1.000 30.38000  ? 236 ALA   B HB1    1 
ATOM   8017 H HB2    . ALA   B 1 270 ? -2.18200  32.76600  -25.85300 1.000 30.38000  ? 236 ALA   B HB2    1 
ATOM   8018 H HB3    . ALA   B 1 270 ? -0.74800  32.71600  -26.53500 1.000 30.38000  ? 236 ALA   B HB3    1 
ATOM   8019 N N      . PHE   B 1 271 ? 0.76000   35.10200  -27.24700 1.000 28.43000  ? 237 PHE   B N      1 
ATOM   8020 C CA     . PHE   B 1 271 ? 2.06000   35.75700  -27.27600 1.000 27.44000  ? 237 PHE   B CA     1 
ATOM   8021 C C      . PHE   B 1 271 ? 1.96100   37.22200  -27.67900 1.000 30.86000  ? 237 PHE   B C      1 
ATOM   8022 O O      . PHE   B 1 271 ? 2.76400   38.03200  -27.21300 1.000 30.98000  ? 237 PHE   B O      1 
ATOM   8023 C CB     . PHE   B 1 271 ? 3.01600   35.00700  -28.20200 1.000 29.55000  ? 237 PHE   B CB     1 
ATOM   8024 C CG     . PHE   B 1 271 ? 3.55500   33.75000  -27.58000 1.000 29.88000  ? 237 PHE   B CG     1 
ATOM   8025 C CD1    . PHE   B 1 271 ? 4.52500   33.82400  -26.58400 1.000 33.30000  ? 237 PHE   B CD1    1 
ATOM   8026 C CD2    . PHE   B 1 271 ? 3.04600   32.50900  -27.93100 1.000 33.84000  ? 237 PHE   B CD2    1 
ATOM   8027 C CE1    . PHE   B 1 271 ? 5.00700   32.67800  -25.98200 1.000 38.25000  ? 237 PHE   B CE1    1 
ATOM   8028 C CE2    . PHE   B 1 271 ? 3.52600   31.35300  -27.34100 1.000 35.30000  ? 237 PHE   B CE2    1 
ATOM   8029 C CZ     . PHE   B 1 271 ? 4.51300   31.44200  -26.36000 1.000 37.08000  ? 237 PHE   B CZ     1 
ATOM   8030 H H      . PHE   B 1 271 ? 0.59800   34.58500  -27.91500 1.000 28.43000  ? 237 PHE   B H      1 
ATOM   8031 H HA     . PHE   B 1 271 ? 2.43800   35.72700  -26.38300 1.000 27.44000  ? 237 PHE   B HA     1 
ATOM   8032 H HB2    . PHE   B 1 271 ? 2.54400   34.76200  -29.01300 1.000 29.55000  ? 237 PHE   B HB2    1 
ATOM   8033 H HB3    . PHE   B 1 271 ? 3.76700   35.58300  -28.41500 1.000 29.55000  ? 237 PHE   B HB3    1 
ATOM   8034 H HD1    . PHE   B 1 271 ? 4.86300   34.65300  -26.33100 1.000 33.30000  ? 237 PHE   B HD1    1 
ATOM   8035 H HD2    . PHE   B 1 271 ? 2.39100   32.45100  -28.58900 1.000 33.84000  ? 237 PHE   B HD2    1 
ATOM   8036 H HE1    . PHE   B 1 271 ? 5.66700   32.73700  -25.32900 1.000 38.25000  ? 237 PHE   B HE1    1 
ATOM   8037 H HE2    . PHE   B 1 271 ? 3.18900   30.52400  -27.59300 1.000 35.30000  ? 237 PHE   B HE2    1 
ATOM   8038 H HZ     . PHE   B 1 271 ? 4.83700   30.66900  -25.95700 1.000 37.08000  ? 237 PHE   B HZ     1 
ATOM   8039 N N      . TYR   B 1 272 ? 1.00400   37.59100  -28.52600 1.000 28.08000  ? 238 TYR   B N      1 
ATOM   8040 C CA     . TYR   B 1 272 ? 0.80800   39.02000  -28.78600 1.000 30.02000  ? 238 TYR   B CA     1 
ATOM   8041 C C      . TYR   B 1 272 ? 0.55500   39.77900  -27.48400 1.000 30.42000  ? 238 TYR   B C      1 
ATOM   8042 O O      . TYR   B 1 272 ? 1.11200   40.85800  -27.26500 1.000 33.73000  ? 238 TYR   B O      1 
ATOM   8043 C CB     . TYR   B 1 272 ? -0.36600  39.22000  -29.73900 1.000 27.92000  ? 238 TYR   B CB     1 
ATOM   8044 C CG     . TYR   B 1 272 ? -0.60400  40.65900  -30.13500 1.000 30.07000  ? 238 TYR   B CG     1 
ATOM   8045 C CD1    . TYR   B 1 272 ? 0.22000   41.27900  -31.05900 1.000 26.34000  ? 238 TYR   B CD1    1 
ATOM   8046 C CD2    . TYR   B 1 272 ? -1.65000  41.40000  -29.57800 1.000 34.21000  ? 238 TYR   B CD2    1 
ATOM   8047 C CE1    . TYR   B 1 272 ? 0.00000   42.60800  -31.44400 1.000 29.63000  ? 238 TYR   B CE1    1 
ATOM   8048 C CE2    . TYR   B 1 272 ? -1.87000  42.72300  -29.95000 1.000 32.37000  ? 238 TYR   B CE2    1 
ATOM   8049 C CZ     . TYR   B 1 272 ? -1.03900  43.31800  -30.88300 1.000 36.88000  ? 238 TYR   B CZ     1 
ATOM   8050 O OH     . TYR   B 1 272 ? -1.22400  44.62000  -31.28500 1.000 34.76000  ? 238 TYR   B OH     1 
ATOM   8051 H H      . TYR   B 1 272 ? 0.47400   37.06100  -28.94800 1.000 28.08000  ? 238 TYR   B H      1 
ATOM   8052 H HA     . TYR   B 1 272 ? 1.60500   39.38400  -29.20200 1.000 30.02000  ? 238 TYR   B HA     1 
ATOM   8053 H HB2    . TYR   B 1 272 ? -0.19800  38.71500  -30.55000 1.000 27.92000  ? 238 TYR   B HB2    1 
ATOM   8054 H HB3    . TYR   B 1 272 ? -1.17300  38.89400  -29.31100 1.000 27.92000  ? 238 TYR   B HB3    1 
ATOM   8055 H HD1    . TYR   B 1 272 ? 0.91900   40.80000  -31.44300 1.000 26.34000  ? 238 TYR   B HD1    1 
ATOM   8056 H HD2    . TYR   B 1 272 ? -2.21200  41.00000  -28.95400 1.000 34.21000  ? 238 TYR   B HD2    1 
ATOM   8057 H HE1    . TYR   B 1 272 ? 0.55800   43.01200  -32.06900 1.000 29.63000  ? 238 TYR   B HE1    1 
ATOM   8058 H HE2    . TYR   B 1 272 ? -2.57300  43.20300  -29.57600 1.000 32.37000  ? 238 TYR   B HE2    1 
ATOM   8059 H HH     . TYR   B 1 272 ? -1.88100  44.95500  -30.88200 1.000 34.76000  ? 238 TYR   B HH     1 
ATOM   8060 N N      . ARG   B 1 273 ? -0.28900  39.22300  -26.61200 1.000 30.17000  ? 239 ARG   B N      1 
ATOM   8061 C CA     . ARG   B 1 273 ? -0.59300  39.87200  -25.33600 1.000 33.77000  ? 239 ARG   B CA     1 
ATOM   8062 C C      . ARG   B 1 273 ? 0.61100   39.87700  -24.40800 1.000 36.05000  ? 239 ARG   B C      1 
ATOM   8063 O O      . ARG   B 1 273 ? 0.83700   40.85500  -23.69200 1.000 35.99000  ? 239 ARG   B O      1 
ATOM   8064 C CB     . ARG   B 1 273 ? -1.77800  39.18600  -24.64400 1.000 31.42000  ? 239 ARG   B CB     1 
ATOM   8065 C CG     . ARG   B 1 273 ? -3.15600  39.44800  -25.25300 1.000 33.88000  ? 239 ARG   B CG     1 
ATOM   8066 C CD     . ARG   B 1 273 ? -4.16300  38.46600  -24.68100 1.000 37.93000  ? 239 ARG   B CD     1 
ATOM   8067 N NE     . ARG   B 1 273 ? -5.47100  38.53700  -25.32200 1.000 44.21000  ? 239 ARG   B NE     1 
ATOM   8068 C CZ     . ARG   B 1 273 ? -6.40500  39.42500  -25.00800 1.000 55.28000  ? 239 ARG   B CZ     1 
ATOM   8069 N NH1    . ARG   B 1 273 ? -6.19500  40.34100  -24.07800 1.000 53.50000  ? 239 ARG   B NH1    1 
ATOM   8070 N NH2    . ARG   B 1 273 ? -7.57900  39.39200  -25.64200 1.000 46.74000  ? 239 ARG   B NH2    1 
ATOM   8071 H H      . ARG   B 1 273 ? -0.69600  38.47500  -26.73500 1.000 30.17000  ? 239 ARG   B H      1 
ATOM   8072 H HA     . ARG   B 1 273 ? -0.84100  40.79400  -25.50600 1.000 33.77000  ? 239 ARG   B HA     1 
ATOM   8073 H HB2    . ARG   B 1 273 ? -1.62900  38.22800  -24.66500 1.000 31.42000  ? 239 ARG   B HB2    1 
ATOM   8074 H HB3    . ARG   B 1 273 ? -1.80800  39.48600  -23.72200 1.000 31.42000  ? 239 ARG   B HB3    1 
ATOM   8075 H HG2    . ARG   B 1 273 ? -3.44300  40.34800  -25.03500 1.000 33.88000  ? 239 ARG   B HG2    1 
ATOM   8076 H HG3    . ARG   B 1 273 ? -3.11600  39.32600  -26.21400 1.000 33.88000  ? 239 ARG   B HG3    1 
ATOM   8077 H HD2    . ARG   B 1 273 ? -3.82400  37.56500  -24.80300 1.000 37.93000  ? 239 ARG   B HD2    1 
ATOM   8078 H HD3    . ARG   B 1 273 ? -4.27900  38.64700  -23.73500 1.000 37.93000  ? 239 ARG   B HD3    1 
ATOM   8079 H HE     . ARG   B 1 273 ? -5.62600  38.00600  -25.98000 1.000 44.21000  ? 239 ARG   B HE     1 
ATOM   8080 H HH11   . ARG   B 1 273 ? -5.44400  40.37300  -23.66200 1.000 53.50000  ? 239 ARG   B HH11   1 
ATOM   8081 H HH12   . ARG   B 1 273 ? -6.81300  40.90800  -23.88900 1.000 53.50000  ? 239 ARG   B HH12   1 
ATOM   8082 H HH21   . ARG   B 1 273 ? -7.72400  38.80000  -26.24800 1.000 46.74000  ? 239 ARG   B HH21   1 
ATOM   8083 H HH22   . ARG   B 1 273 ? -8.19000  39.96400  -25.44600 1.000 46.74000  ? 239 ARG   B HH22   1 
ATOM   8084 N N      . ARG   B 1 274 ? 1.39000   38.79700  -24.39300 1.000 32.61000  ? 240 ARG   B N      1 
ATOM   8085 C CA     . ARG   B 1 274 ? 2.42900   38.64100  -23.38200 1.000 33.81000  ? 240 ARG   B CA     1 
ATOM   8086 C C      . ARG   B 1 274 ? 3.79300   39.18100  -23.80100 1.000 36.99000  ? 240 ARG   B C      1 
ATOM   8087 O O      . ARG   B 1 274 ? 4.65600   39.37300  -22.93100 1.000 35.73000  ? 240 ARG   B O      1 
ATOM   8088 C CB     . ARG   B 1 274 ? 2.55100   37.16000  -22.99300 1.000 31.33000  ? 240 ARG   B CB     1 
ATOM   8089 C CG     . ARG   B 1 274 ? 1.36800   36.64000  -22.17000 1.000 36.80000  ? 240 ARG   B CG     1 
ATOM   8090 C CD     . ARG   B 1 274 ? 1.35200   35.10300  -22.09000 1.000 41.69000  ? 240 ARG   B CD     1 
ATOM   8091 N NE     . ARG   B 1 274 ? 0.22700   34.59900  -21.31200 1.000 38.52000  ? 240 ARG   B NE     1 
ATOM   8092 C CZ     . ARG   B 1 274 ? -1.03800  34.65400  -21.70600 1.000 44.91000  ? 240 ARG   B CZ     1 
ATOM   8093 N NH1    . ARG   B 1 274 ? -1.36900  35.08100  -22.91700 1.000 36.25000  ? 240 ARG   B NH1    1 
ATOM   8094 N NH2    . ARG   B 1 274 ? -1.99700  34.29600  -20.85900 1.000 48.55000  ? 240 ARG   B NH2    1 
ATOM   8095 H H      . ARG   B 1 274 ? 1.33700   38.14600  -24.95300 1.000 32.61000  ? 240 ARG   B H      1 
ATOM   8096 H HA     . ARG   B 1 274 ? 2.15800   39.12700  -22.58700 1.000 33.81000  ? 240 ARG   B HA     1 
ATOM   8097 H HB2    . ARG   B 1 274 ? 2.60700   36.62800  -23.80200 1.000 31.33000  ? 240 ARG   B HB2    1 
ATOM   8098 H HB3    . ARG   B 1 274 ? 3.35600   37.04100  -22.46400 1.000 31.33000  ? 240 ARG   B HB3    1 
ATOM   8099 H HG2    . ARG   B 1 274 ? 1.43000   36.98900  -21.26700 1.000 36.80000  ? 240 ARG   B HG2    1 
ATOM   8100 H HG3    . ARG   B 1 274 ? 0.54000   36.93000  -22.58400 1.000 36.80000  ? 240 ARG   B HG3    1 
ATOM   8101 H HD2    . ARG   B 1 274 ? 1.28600   34.73900  -22.98700 1.000 41.69000  ? 240 ARG   B HD2    1 
ATOM   8102 H HD3    . ARG   B 1 274 ? 2.17000   34.79900  -21.66700 1.000 41.69000  ? 240 ARG   B HD3    1 
ATOM   8103 H HE     . ARG   B 1 274 ? 0.39500   34.24300  -20.54700 1.000 38.52000  ? 240 ARG   B HE     1 
ATOM   8104 H HH11   . ARG   B 1 274 ? -0.75900  35.32300  -23.47200 1.000 36.25000  ? 240 ARG   B HH11   1 
ATOM   8105 H HH12   . ARG   B 1 274 ? -2.19600  35.10900  -23.15000 1.000 36.25000  ? 240 ARG   B HH12   1 
ATOM   8106 H HH21   . ARG   B 1 274 ? -1.79500  34.01700  -20.07100 1.000 48.55000  ? 240 ARG   B HH21   1 
ATOM   8107 H HH22   . ARG   B 1 274 ? -2.81900  34.32700  -21.10900 1.000 48.55000  ? 240 ARG   B HH22   1 
ATOM   8108 N N      . CYS   B 1 275 ? 4.02600   39.42900  -25.09500 1.000 32.26000  ? 241 CYS   B N      1 
ATOM   8109 C CA     . CYS   B 1 275 ? 5.32000   39.90500  -25.58400 1.000 28.24000  ? 241 CYS   B CA     1 
ATOM   8110 C C      . CYS   B 1 275 ? 5.08800   41.14800  -26.43300 1.000 34.27000  ? 241 CYS   B C      1 
ATOM   8111 O O      . CYS   B 1 275 ? 5.32000   41.14000  -27.64600 1.000 32.66000  ? 241 CYS   B O      1 
ATOM   8112 C CB     . CYS   B 1 275 ? 6.05800   38.81900  -26.38100 1.000 31.39000  ? 241 CYS   B CB     1 
ATOM   8113 S SG     . CYS   B 1 275 ? 6.33300   37.27800  -25.48000 1.000 36.14000  ? 241 CYS   B SG     1 
ATOM   8114 H H      . CYS   B 1 275 ? 3.44000   39.32700  -25.71600 1.000 32.26000  ? 241 CYS   B H      1 
ATOM   8115 H HA     . CYS   B 1 275 ? 5.87800   40.15400  -24.83100 1.000 28.24000  ? 241 CYS   B HA     1 
ATOM   8116 H HB2    . CYS   B 1 275 ? 5.53700   38.60800  -27.17200 1.000 31.39000  ? 241 CYS   B HB2    1 
ATOM   8117 H HB3    . CYS   B 1 275 ? 6.92600   39.16400  -26.64400 1.000 31.39000  ? 241 CYS   B HB3    1 
ATOM   8118 H HG     . CYS   B 1 275 ? 6.92100   36.50500  -26.18400 1.000 36.14000  ? 241 CYS   B HG     1 
ATOM   8119 N N      . PRO   B 1 276 ? 4.61600   42.23900  -25.82000 1.000 35.90000  ? 242 PRO   B N      1 
ATOM   8120 C CA     . PRO   B 1 276 ? 4.33500   43.45400  -26.60600 1.000 35.20000  ? 242 PRO   B CA     1 
ATOM   8121 C C      . PRO   B 1 276 ? 5.55000   44.02400  -27.30400 1.000 38.41000  ? 242 PRO   B C      1 
ATOM   8122 O O      . PRO   B 1 276 ? 5.38600   44.73400  -28.30100 1.000 36.33000  ? 242 PRO   B O      1 
ATOM   8123 C CB     . PRO   B 1 276 ? 3.77400   44.43600  -25.56000 1.000 36.13000  ? 242 PRO   B CB     1 
ATOM   8124 C CG     . PRO   B 1 276 ? 4.30500   43.94900  -24.26200 1.000 35.31000  ? 242 PRO   B CG     1 
ATOM   8125 C CD     . PRO   B 1 276 ? 4.33600   42.43600  -24.38400 1.000 35.83000  ? 242 PRO   B CD     1 
ATOM   8126 H HA     . PRO   B 1 276 ? 3.64900   43.27000  -27.26600 1.000 35.20000  ? 242 PRO   B HA     1 
ATOM   8127 H HB2    . PRO   B 1 276 ? 4.09300   45.33300  -25.74800 1.000 36.13000  ? 242 PRO   B HB2    1 
ATOM   8128 H HB3    . PRO   B 1 276 ? 2.80500   44.40600  -25.56800 1.000 36.13000  ? 242 PRO   B HB3    1 
ATOM   8129 H HG2    . PRO   B 1 276 ? 5.19900   44.30000  -24.12300 1.000 35.31000  ? 242 PRO   B HG2    1 
ATOM   8130 H HG3    . PRO   B 1 276 ? 3.71300   44.22300  -23.54400 1.000 35.31000  ? 242 PRO   B HG3    1 
ATOM   8131 H HD2    . PRO   B 1 276 ? 5.05100   42.06600  -23.84200 1.000 35.83000  ? 242 PRO   B HD2    1 
ATOM   8132 H HD3    . PRO   B 1 276 ? 3.47400   42.05700  -24.15000 1.000 35.83000  ? 242 PRO   B HD3    1 
ATOM   8133 N N      . GLY   B 1 277 ? 6.76000   43.73500  -26.83500 1.000 33.25000  ? 243 GLY   B N      1 
ATOM   8134 C CA     . GLY   B 1 277 ? 7.94300   44.25400  -27.49100 1.000 34.89000  ? 243 GLY   B CA     1 
ATOM   8135 C C      . GLY   B 1 277 ? 8.45600   43.41800  -28.64600 1.000 39.27000  ? 243 GLY   B C      1 
ATOM   8136 O O      . GLY   B 1 277 ? 9.51000   43.73800  -29.19900 1.000 42.59000  ? 243 GLY   B O      1 
ATOM   8137 H H      . GLY   B 1 277 ? 6.91700   43.24600  -26.14600 1.000 33.25000  ? 243 GLY   B H      1 
ATOM   8138 H HA2    . GLY   B 1 277 ? 7.75300   45.14400  -27.82700 1.000 34.89000  ? 243 GLY   B HA2    1 
ATOM   8139 H HA3    . GLY   B 1 277 ? 8.65600   44.32800  -26.83800 1.000 34.89000  ? 243 GLY   B HA3    1 
ATOM   8140 N N      . LYS   B 1 278 ? 7.75400   42.34800  -29.02100 1.000 33.26000  ? 244 LYS   B N      1 
ATOM   8141 C CA     . LYS   B 1 278 ? 8.15400   41.48600  -30.12200 1.000 30.86000  ? 244 LYS   B CA     1 
ATOM   8142 C C      . LYS   B 1 278 ? 7.05300   41.48800  -31.17200 1.000 37.57000  ? 244 LYS   B C      1 
ATOM   8143 O O      . LYS   B 1 278 ? 5.89200   41.79200  -30.87900 1.000 35.96000  ? 244 LYS   B O      1 
ATOM   8144 C CB     . LYS   B 1 278 ? 8.44200   40.06200  -29.61300 1.000 37.38000  ? 244 LYS   B CB     1 
ATOM   8145 C CG     . LYS   B 1 278 ? 9.50000   40.07200  -28.48500 1.000 42.80000  ? 244 LYS   B CG     1 
ATOM   8146 C CD     . LYS   B 1 278 ? 9.97700   38.72400  -28.00300 1.000 53.73000  ? 244 LYS   B CD     1 
ATOM   8147 C CE     . LYS   B 1 278 ? 10.92200  38.89600  -26.79000 1.000 38.21000  ? 244 LYS   B CE     1 
ATOM   8148 N NZ     . LYS   B 1 278 ? 12.19800  39.66800  -27.08600 1.000 37.67000  ? 244 LYS   B NZ     1 
ATOM   8149 H H      . LYS   B 1 278 ? 7.02400   42.09800  -28.64000 1.000 33.26000  ? 244 LYS   B H      1 
ATOM   8150 H HA     . LYS   B 1 278 ? 8.96300   41.83200  -30.53000 1.000 30.86000  ? 244 LYS   B HA     1 
ATOM   8151 H HB2    . LYS   B 1 278 ? 7.62500   39.67600  -29.26100 1.000 37.38000  ? 244 LYS   B HB2    1 
ATOM   8152 H HB3    . LYS   B 1 278 ? 8.78100   39.52200  -30.34400 1.000 37.38000  ? 244 LYS   B HB3    1 
ATOM   8153 H HG2    . LYS   B 1 278 ? 10.27800  40.55600  -28.80200 1.000 42.80000  ? 244 LYS   B HG2    1 
ATOM   8154 H HG3    . LYS   B 1 278 ? 9.12400   40.53400  -27.71900 1.000 42.80000  ? 244 LYS   B HG3    1 
ATOM   8155 H HD2    . LYS   B 1 278 ? 9.21600   38.19300  -27.72400 1.000 53.73000  ? 244 LYS   B HD2    1 
ATOM   8156 H HD3    . LYS   B 1 278 ? 10.46200  38.27800  -28.71400 1.000 53.73000  ? 244 LYS   B HD3    1 
ATOM   8157 H HE2    . LYS   B 1 278 ? 10.44700  39.36000  -26.08200 1.000 38.21000  ? 244 LYS   B HE2    1 
ATOM   8158 H HE3    . LYS   B 1 278 ? 11.17200  38.01100  -26.49600 1.000 38.21000  ? 244 LYS   B HE3    1 
ATOM   8159 H HZ1    . LYS   B 1 278 ? 12.69400  39.72900  -26.35000 1.000 37.67000  ? 244 LYS   B HZ1    1 
ATOM   8160 H HZ2    . LYS   B 1 278 ? 12.66700  39.25000  -27.71700 1.000 37.67000  ? 244 LYS   B HZ2    1 
ATOM   8161 H HZ3    . LYS   B 1 278 ? 11.99800  40.48800  -27.36900 1.000 37.67000  ? 244 LYS   B HZ3    1 
ATOM   8162 N N      . LEU   B 1 279 ? 7.42300   41.17000  -32.40700 1.000 31.84000  ? 245 LEU   B N      1 
ATOM   8163 C CA     . LEU   B 1 279 ? 6.40800   40.91600  -33.42600 1.000 30.53000  ? 245 LEU   B CA     1 
ATOM   8164 C C      . LEU   B 1 279 ? 5.96200   39.46300  -33.34000 1.000 29.70000  ? 245 LEU   B C      1 
ATOM   8165 O O      . LEU   B 1 279 ? 6.74300   38.59300  -32.96800 1.000 30.51000  ? 245 LEU   B O      1 
ATOM   8166 C CB     . LEU   B 1 279 ? 6.97300   41.18900  -34.81500 1.000 30.88000  ? 245 LEU   B CB     1 
ATOM   8167 C CG     . LEU   B 1 279 ? 7.55000   42.59400  -35.00000 1.000 35.36000  ? 245 LEU   B CG     1 
ATOM   8168 C CD1    . LEU   B 1 279 ? 8.35700   42.62900  -36.26600 1.000 36.12000  ? 245 LEU   B CD1    1 
ATOM   8169 C CD2    . LEU   B 1 279 ? 6.37200   43.53600  -35.08800 1.000 34.19000  ? 245 LEU   B CD2    1 
ATOM   8170 H H      . LEU   B 1 279 ? 8.23600   41.09600  -32.67800 1.000 31.84000  ? 245 LEU   B H      1 
ATOM   8171 H HA     . LEU   B 1 279 ? 5.63900   41.48900  -33.28000 1.000 30.53000  ? 245 LEU   B HA     1 
ATOM   8172 H HB2    . LEU   B 1 279 ? 7.68500   40.55400  -34.98900 1.000 30.88000  ? 245 LEU   B HB2    1 
ATOM   8173 H HB3    . LEU   B 1 279 ? 6.26500   41.07100  -35.46700 1.000 30.88000  ? 245 LEU   B HB3    1 
ATOM   8174 H HG     . LEU   B 1 279 ? 8.11000   42.83900  -34.24800 1.000 35.36000  ? 245 LEU   B HG     1 
ATOM   8175 H HD11   . LEU   B 1 279 ? 8.73300   43.51600  -36.37500 1.000 36.12000  ? 245 LEU   B HD11   1 
ATOM   8176 H HD12   . LEU   B 1 279 ? 9.06900   41.97300  -36.20500 1.000 36.12000  ? 245 LEU   B HD12   1 
ATOM   8177 H HD13   . LEU   B 1 279 ? 7.77700   42.42000  -37.01500 1.000 36.12000  ? 245 LEU   B HD13   1 
ATOM   8178 H HD21   . LEU   B 1 279 ? 6.70000   44.43300  -35.25600 1.000 34.19000  ? 245 LEU   B HD21   1 
ATOM   8179 H HD22   . LEU   B 1 279 ? 5.79400   43.25400  -35.81400 1.000 34.19000  ? 245 LEU   B HD22   1 
ATOM   8180 H HD23   . LEU   B 1 279 ? 5.88500   43.51500  -34.25000 1.000 34.19000  ? 245 LEU   B HD23   1 
ATOM   8181 N N      . ILE   B 1 280 ? 4.70300   39.20200  -33.68400 1.000 27.31000  ? 246 ILE   B N      1 
ATOM   8182 C CA     . ILE   B 1 280 ? 4.18800   37.83200  -33.80700 1.000 28.63000  ? 246 ILE   B CA     1 
ATOM   8183 C C      . ILE   B 1 280 ? 3.93500   37.55400  -35.28100 1.000 30.47000  ? 246 ILE   B C      1 
ATOM   8184 O O      . ILE   B 1 280 ? 3.27700   38.35100  -35.96400 1.000 28.78000  ? 246 ILE   B O      1 
ATOM   8185 C CB     . ILE   B 1 280 ? 2.88700   37.62100  -33.01200 1.000 30.46000  ? 246 ILE   B CB     1 
ATOM   8186 C CG1    . ILE   B 1 280 ? 2.95800   38.20800  -31.59700 1.000 32.19000  ? 246 ILE   B CG1    1 
ATOM   8187 C CG2    . ILE   B 1 280 ? 2.53400   36.10800  -32.98000 1.000 31.75000  ? 246 ILE   B CG2    1 
ATOM   8188 C CD1    . ILE   B 1 280 ? 4.16600   37.74300  -30.77000 1.000 34.51000  ? 246 ILE   B CD1    1 
ATOM   8189 H H      . ILE   B 1 280 ? 4.11600   39.80700  -33.85400 1.000 27.31000  ? 246 ILE   B H      1 
ATOM   8190 H HA     . ILE   B 1 280 ? 4.85100   37.20200  -33.48400 1.000 28.63000  ? 246 ILE   B HA     1 
ATOM   8191 H HB     . ILE   B 1 280 ? 2.17500   38.08000  -33.48500 1.000 30.46000  ? 246 ILE   B HB     1 
ATOM   8192 H HG12   . ILE   B 1 280 ? 3.00200   39.17500  -31.66400 1.000 32.19000  ? 246 ILE   B HG12   1 
ATOM   8193 H HG13   . ILE   B 1 280 ? 2.15600   37.95100  -31.11500 1.000 32.19000  ? 246 ILE   B HG13   1 
ATOM   8194 H HG21   . ILE   B 1 280 ? 1.75900   35.97800  -32.41100 1.000 31.75000  ? 246 ILE   B HG21   1 
ATOM   8195 H HG22   . ILE   B 1 280 ? 2.33600   35.80900  -33.88100 1.000 31.75000  ? 246 ILE   B HG22   1 
ATOM   8196 H HG23   . ILE   B 1 280 ? 3.29100   35.61500  -32.62600 1.000 31.75000  ? 246 ILE   B HG23   1 
ATOM   8197 H HD11   . ILE   B 1 280 ? 4.08400   38.09300  -29.86900 1.000 34.51000  ? 246 ILE   B HD11   1 
ATOM   8198 H HD12   . ILE   B 1 280 ? 4.17900   36.77300  -30.74900 1.000 34.51000  ? 246 ILE   B HD12   1 
ATOM   8199 H HD13   . ILE   B 1 280 ? 4.97900   38.07500  -31.18100 1.000 34.51000  ? 246 ILE   B HD13   1 
ATOM   8200 N N      . PHE   B 1 281 ? 4.43300   36.42000  -35.77500 1.000 28.19000  ? 247 PHE   B N      1 
ATOM   8201 C CA     . PHE   B 1 281 ? 4.08600   35.95200  -37.11200 1.000 23.77000  ? 247 PHE   B CA     1 
ATOM   8202 C C      . PHE   B 1 281 ? 3.11500   34.79200  -36.94100 1.000 25.74000  ? 247 PHE   B C      1 
ATOM   8203 O O      . PHE   B 1 281 ? 3.36100   33.90500  -36.12700 1.000 32.42000  ? 247 PHE   B O      1 
ATOM   8204 C CB     . PHE   B 1 281 ? 5.29000   35.45900  -37.91400 1.000 26.29000  ? 247 PHE   B CB     1 
ATOM   8205 C CG     . PHE   B 1 281 ? 6.28100   36.51600  -38.31900 1.000 29.21000  ? 247 PHE   B CG     1 
ATOM   8206 C CD1    . PHE   B 1 281 ? 6.13100   37.84700  -37.96600 1.000 27.91000  ? 247 PHE   B CD1    1 
ATOM   8207 C CD2    . PHE   B 1 281 ? 7.38700   36.14600  -39.08200 1.000 29.21000  ? 247 PHE   B CD2    1 
ATOM   8208 C CE1    . PHE   B 1 281 ? 7.07600   38.79600  -38.34500 1.000 28.35000  ? 247 PHE   B CE1    1 
ATOM   8209 C CE2    . PHE   B 1 281 ? 8.33200   37.08100  -39.47300 1.000 31.42000  ? 247 PHE   B CE2    1 
ATOM   8210 C CZ     . PHE   B 1 281 ? 8.18300   38.42200  -39.10700 1.000 31.60000  ? 247 PHE   B CZ     1 
ATOM   8211 H H      . PHE   B 1 281 ? 4.97600   35.90300  -35.35300 1.000 28.19000  ? 247 PHE   B H      1 
ATOM   8212 H HA     . PHE   B 1 281 ? 3.64400   36.65700  -37.61000 1.000 23.77000  ? 247 PHE   B HA     1 
ATOM   8213 H HB2    . PHE   B 1 281 ? 5.76600   34.80400  -37.38000 1.000 26.29000  ? 247 PHE   B HB2    1 
ATOM   8214 H HB3    . PHE   B 1 281 ? 4.96600   35.03900  -38.72600 1.000 26.29000  ? 247 PHE   B HB3    1 
ATOM   8215 H HD1    . PHE   B 1 281 ? 5.40100   38.10800  -37.45300 1.000 27.91000  ? 247 PHE   B HD1    1 
ATOM   8216 H HD2    . PHE   B 1 281 ? 7.49700   35.25500  -39.32600 1.000 29.21000  ? 247 PHE   B HD2    1 
ATOM   8217 H HE1    . PHE   B 1 281 ? 6.96200   39.68600  -38.10000 1.000 28.35000  ? 247 PHE   B HE1    1 
ATOM   8218 H HE2    . PHE   B 1 281 ? 9.06500   36.81600  -39.98000 1.000 31.42000  ? 247 PHE   B HE2    1 
ATOM   8219 H HZ     . PHE   B 1 281 ? 8.81100   39.05500  -39.36900 1.000 31.60000  ? 247 PHE   B HZ     1 
ATOM   8220 N N      . GLY   B 1 282 ? 2.02500   34.80000  -37.69800 1.000 26.30000  ? 248 GLY   B N      1 
ATOM   8221 C CA     . GLY   B 1 282 ? 1.00600   33.77100  -37.59800 1.000 25.68000  ? 248 GLY   B CA     1 
ATOM   8222 C C      . GLY   B 1 282 ? 1.26500   32.69400  -38.64200 1.000 28.36000  ? 248 GLY   B C      1 
ATOM   8223 O O      . GLY   B 1 282 ? 1.63200   32.99100  -39.77700 1.000 27.12000  ? 248 GLY   B O      1 
ATOM   8224 H H      . GLY   B 1 282 ? 1.85200   35.40300  -38.28700 1.000 26.30000  ? 248 GLY   B H      1 
ATOM   8225 H HA2    . GLY   B 1 282 ? 1.02400   33.36800  -36.71600 1.000 25.68000  ? 248 GLY   B HA2    1 
ATOM   8226 H HA3    . GLY   B 1 282 ? 0.12900   34.15600  -37.75200 1.000 25.68000  ? 248 GLY   B HA3    1 
ATOM   8227 N N      . CYS   B 1 283 ? 1.09800   31.44900  -38.22200 1.000 26.84000  ? 249 CYS   B N      1 
ATOM   8228 C CA     . CYS   B 1 283 ? 1.26800   30.32100  -39.12700 1.000 25.40000  ? 249 CYS   B CA     1 
ATOM   8229 C C      . CYS   B 1 283 ? 0.31000   29.24600  -38.64700 1.000 27.47000  ? 249 CYS   B C      1 
ATOM   8230 O O      . CYS   B 1 283 ? 0.32000   28.90500  -37.46200 1.000 28.64000  ? 249 CYS   B O      1 
ATOM   8231 C CB     . CYS   B 1 283 ? 2.71300   29.82200  -39.10300 1.000 27.28000  ? 249 CYS   B CB     1 
ATOM   8232 S SG     . CYS   B 1 283 ? 2.99700   28.50700  -40.32600 1.000 28.86000  ? 249 CYS   B SG     1 
ATOM   8233 H H      . CYS   B 1 283 ? 0.88600   31.22900  -37.41800 1.000 26.84000  ? 249 CYS   B H      1 
ATOM   8234 H HA     . CYS   B 1 283 ? 1.03300   30.57800  -40.03200 1.000 25.40000  ? 249 CYS   B HA     1 
ATOM   8235 H HB2    . CYS   B 1 283 ? 3.30800   30.56000  -39.30800 1.000 27.28000  ? 249 CYS   B HB2    1 
ATOM   8236 H HB3    . CYS   B 1 283 ? 2.91300   29.46500  -38.22300 1.000 27.28000  ? 249 CYS   B HB3    1 
ATOM   8237 H HG     . CYS   B 1 283 ? 4.14300   28.15600  -40.26300 1.000 28.86000  ? 249 CYS   B HG     1 
ATOM   8238 N N      . GLY   B 1 284 ? -0.54500  28.76000  -39.53600 1.000 28.02000  ? 250 GLY   B N      1 
ATOM   8239 C CA     . GLY   B 1 284 ? -1.41200  27.65400  -39.19300 1.000 28.87000  ? 250 GLY   B CA     1 
ATOM   8240 C C      . GLY   B 1 284 ? -2.81200  27.82100  -39.74300 1.000 27.72000  ? 250 GLY   B C      1 
ATOM   8241 O O      . GLY   B 1 284 ? -3.50900  28.77200  -39.38900 1.000 29.69000  ? 250 GLY   B O      1 
ATOM   8242 H H      . GLY   B 1 284 ? -0.64000  29.05300  -40.33900 1.000 28.02000  ? 250 GLY   B H      1 
ATOM   8243 H HA2    . GLY   B 1 284 ? -1.04000  26.83100  -39.54800 1.000 28.87000  ? 250 GLY   B HA2    1 
ATOM   8244 H HA3    . GLY   B 1 284 ? -1.47300  27.57200  -38.22900 1.000 28.87000  ? 250 GLY   B HA3    1 
ATOM   8245 N N      . GLY   B 1 285 ? -3.23100  26.90100  -40.61700 1.000 25.38000  ? 251 GLY   B N      1 
ATOM   8246 C CA     . GLY   B 1 285 ? -4.60900  26.82100  -41.07000 1.000 28.89000  ? 251 GLY   B CA     1 
ATOM   8247 C C      . GLY   B 1 285 ? -5.06700  27.86800  -42.06300 1.000 29.82000  ? 251 GLY   B C      1 
ATOM   8248 O O      . GLY   B 1 285 ? -6.27400  27.98900  -42.28200 1.000 28.72000  ? 251 GLY   B O      1 
ATOM   8249 H H      . GLY   B 1 285 ? -2.72000  26.30300  -40.96500 1.000 25.38000  ? 251 GLY   B H      1 
ATOM   8250 H HA2    . GLY   B 1 285 ? -4.74800  25.95200  -41.47800 1.000 28.89000  ? 251 GLY   B HA2    1 
ATOM   8251 H HA3    . GLY   B 1 285 ? -5.19100  26.87900  -40.29600 1.000 28.89000  ? 251 GLY   B HA3    1 
ATOM   8252 N N      . VAL   B 1 286 ? -4.16100  28.60900  -42.69300 1.000 26.55000  ? 252 VAL   B N      1 
ATOM   8253 C CA     . VAL   B 1 286 ? -4.56200  29.68400  -43.60400 1.000 27.90000  ? 252 VAL   B CA     1 
ATOM   8254 C C      . VAL   B 1 286 ? -4.88300  29.09700  -44.97400 1.000 29.86000  ? 252 VAL   B C      1 
ATOM   8255 O O      . VAL   B 1 286 ? -3.99200  28.60400  -45.67200 1.000 28.66000  ? 252 VAL   B O      1 
ATOM   8256 C CB     . VAL   B 1 286 ? -3.48200  30.76000  -43.71600 1.000 28.59000  ? 252 VAL   B CB     1 
ATOM   8257 C CG1    . VAL   B 1 286 ? -3.87200  31.79100  -44.81400 1.000 27.40000  ? 252 VAL   B CG1    1 
ATOM   8258 C CG2    . VAL   B 1 286 ? -3.29200  31.42500  -42.36100 1.000 25.16000  ? 252 VAL   B CG2    1 
ATOM   8259 H H      . VAL   B 1 286 ? -3.31000  28.51300  -42.61300 1.000 26.55000  ? 252 VAL   B H      1 
ATOM   8260 H HA     . VAL   B 1 286 ? -5.36700  30.10400  -43.26200 1.000 27.90000  ? 252 VAL   B HA     1 
ATOM   8261 H HB     . VAL   B 1 286 ? -2.64300  30.34600  -43.97200 1.000 28.59000  ? 252 VAL   B HB     1 
ATOM   8262 H HG11   . VAL   B 1 286 ? -3.34200  32.59400  -44.69200 1.000 27.40000  ? 252 VAL   B HG11   1 
ATOM   8263 H HG12   . VAL   B 1 286 ? -3.69500  31.40900  -45.68800 1.000 27.40000  ? 252 VAL   B HG12   1 
ATOM   8264 H HG13   . VAL   B 1 286 ? -4.81500  32.00300  -44.72700 1.000 27.40000  ? 252 VAL   B HG13   1 
ATOM   8265 H HG21   . VAL   B 1 286 ? -2.60100  32.10000  -42.43600 1.000 25.16000  ? 252 VAL   B HG21   1 
ATOM   8266 H HG22   . VAL   B 1 286 ? -4.12800  31.83600  -42.09100 1.000 25.16000  ? 252 VAL   B HG22   1 
ATOM   8267 H HG23   . VAL   B 1 286 ? -3.02800  30.75300  -41.71300 1.000 25.16000  ? 252 VAL   B HG23   1 
ATOM   8268 N N      . TYR   B 1 287 ? -6.15900  29.14300  -45.35400 1.000 25.38000  ? 253 TYR   B N      1 
ATOM   8269 C CA     . TYR   B 1 287 ? -6.58700  28.80700  -46.71100 1.000 27.18000  ? 253 TYR   B CA     1 
ATOM   8270 C C      . TYR   B 1 287 ? -7.28100  29.94100  -47.43800 1.000 25.79000  ? 253 TYR   B C      1 
ATOM   8271 O O      . TYR   B 1 287 ? -7.46300  29.82700  -48.65600 1.000 33.69000  ? 253 TYR   B O      1 
ATOM   8272 C CB     . TYR   B 1 287 ? -7.56400  27.62600  -46.72800 1.000 27.35000  ? 253 TYR   B CB     1 
ATOM   8273 C CG     . TYR   B 1 287 ? -6.93800  26.29900  -46.43800 1.000 33.32000  ? 253 TYR   B CG     1 
ATOM   8274 C CD1    . TYR   B 1 287 ? -6.63100  25.95400  -45.12900 1.000 38.14000  ? 253 TYR   B CD1    1 
ATOM   8275 C CD2    . TYR   B 1 287 ? -6.67000  25.36900  -47.45800 1.000 32.15000  ? 253 TYR   B CD2    1 
ATOM   8276 C CE1    . TYR   B 1 287 ? -6.06500  24.74200  -44.82500 1.000 37.19000  ? 253 TYR   B CE1    1 
ATOM   8277 C CE2    . TYR   B 1 287 ? -6.08900  24.11500  -47.14600 1.000 36.96000  ? 253 TYR   B CE2    1 
ATOM   8278 C CZ     . TYR   B 1 287 ? -5.80300  23.82200  -45.81600 1.000 42.28000  ? 253 TYR   B CZ     1 
ATOM   8279 O OH     . TYR   B 1 287 ? -5.23800  22.62100  -45.43400 1.000 44.91000  ? 253 TYR   B OH     1 
ATOM   8280 H H      . TYR   B 1 287 ? -6.80600  29.37000  -44.83500 1.000 25.38000  ? 253 TYR   B H      1 
ATOM   8281 H HA     . TYR   B 1 287 ? -5.80900  28.55500  -47.23300 1.000 27.18000  ? 253 TYR   B HA     1 
ATOM   8282 H HB2    . TYR   B 1 287 ? -8.24900  27.78100  -46.05900 1.000 27.35000  ? 253 TYR   B HB2    1 
ATOM   8283 H HB3    . TYR   B 1 287 ? -7.97200  27.57300  -47.60700 1.000 27.35000  ? 253 TYR   B HB3    1 
ATOM   8284 H HD1    . TYR   B 1 287 ? -6.80700  26.55900  -44.44500 1.000 38.14000  ? 253 TYR   B HD1    1 
ATOM   8285 H HD2    . TYR   B 1 287 ? -6.87300  25.57900  -48.34100 1.000 32.15000  ? 253 TYR   B HD2    1 
ATOM   8286 H HE1    . TYR   B 1 287 ? -5.87000  24.53400  -43.94000 1.000 37.19000  ? 253 TYR   B HE1    1 
ATOM   8287 H HE2    . TYR   B 1 287 ? -5.91000  23.49600  -47.81700 1.000 36.96000  ? 253 TYR   B HE2    1 
ATOM   8288 H HH     . TYR   B 1 287 ? -5.11900  22.13300  -46.10700 1.000 44.91000  ? 253 TYR   B HH     1 
ATOM   8289 N N      . THR   B 1 288 ? -7.71900  31.00000  -46.73800 1.000 30.12000  ? 254 THR   B N      1 
ATOM   8290 C CA     . THR   B 1 288 ? -8.47500  32.09100  -47.36000 1.000 28.78000  ? 254 THR   B CA     1 
ATOM   8291 C C      . THR   B 1 288 ? -7.99600  33.42100  -46.80800 1.000 29.76000  ? 254 THR   B C      1 
ATOM   8292 O O      . THR   B 1 288 ? -7.33100  33.48100  -45.77300 1.000 28.12000  ? 254 THR   B O      1 
ATOM   8293 C CB     . THR   B 1 288 ? -9.97800  32.01200  -47.08200 1.000 34.64000  ? 254 THR   B CB     1 
ATOM   8294 O OG1    . THR   B 1 288 ? -10.19600 32.14000  -45.67500 1.000 35.60000  ? 254 THR   B OG1    1 
ATOM   8295 C CG2    . THR   B 1 288 ? -10.59700 30.68600  -47.59800 1.000 34.47000  ? 254 THR   B CG2    1 
ATOM   8296 H H      . THR   B 1 288 ? -7.58800  31.10700  -45.89500 1.000 30.12000  ? 254 THR   B H      1 
ATOM   8297 H HA     . THR   B 1 288 ? -8.33400  32.08300  -48.32000 1.000 28.78000  ? 254 THR   B HA     1 
ATOM   8298 H HB     . THR   B 1 288 ? -10.42100 32.74500  -47.53700 1.000 34.64000  ? 254 THR   B HB     1 
ATOM   8299 H HG1    . THR   B 1 288 ? -11.01800 32.09800  -45.50700 1.000 35.60000  ? 254 THR   B HG1    1 
ATOM   8300 H HG21   . THR   B 1 288 ? -11.54800 30.66900  -47.40900 1.000 34.47000  ? 254 THR   B HG21   1 
ATOM   8301 H HG22   . THR   B 1 288 ? -10.46400 30.60900  -48.55600 1.000 34.47000  ? 254 THR   B HG22   1 
ATOM   8302 H HG23   . THR   B 1 288 ? -10.17500 29.93100  -47.15900 1.000 34.47000  ? 254 THR   B HG23   1 
ATOM   8303 N N      . GLY   B 1 289 ? -8.40500  34.50500  -47.47900 1.000 28.89000  ? 255 GLY   B N      1 
ATOM   8304 C CA     . GLY   B 1 289 ? -8.13100  35.83100  -46.94300 1.000 29.06000  ? 255 GLY   B CA     1 
ATOM   8305 C C      . GLY   B 1 289 ? -8.79600  36.08800  -45.60200 1.000 29.35000  ? 255 GLY   B C      1 
ATOM   8306 O O      . GLY   B 1 289 ? -8.27700  36.86400  -44.78600 1.000 30.00000  ? 255 GLY   B O      1 
ATOM   8307 H H      . GLY   B 1 289 ? -8.83100  34.49600  -48.22600 1.000 28.89000  ? 255 GLY   B H      1 
ATOM   8308 H HA2    . GLY   B 1 289 ? -7.17300  35.94000  -46.83300 1.000 29.06000  ? 255 GLY   B HA2    1 
ATOM   8309 H HA3    . GLY   B 1 289 ? -8.44400  36.50100  -47.57000 1.000 29.06000  ? 255 GLY   B HA3    1 
ATOM   8310 N N      . GLU   B 1 290 ? -9.95900  35.47000  -45.36500 1.000 30.86000  ? 256 GLU   B N      1 
ATOM   8311 C CA     . GLU   B 1 290 ? -10.60900 35.59300  -44.06300 1.000 31.37000  ? 256 GLU   B CA     1 
ATOM   8312 C C      . GLU   B 1 290 ? -9.78200  34.94600  -42.96500 1.000 27.16000  ? 256 GLU   B C      1 
ATOM   8313 O O      . GLU   B 1 290 ? -9.69200  35.48800  -41.85800 1.000 29.97000  ? 256 GLU   B O      1 
ATOM   8314 C CB     . GLU   B 1 290 ? -12.00700 34.97100  -44.09700 1.000 34.91000  ? 256 GLU   B CB     1 
ATOM   8315 C CG     . GLU   B 1 290 ? -13.00600 35.83000  -44.83100 1.000 44.25000  ? 256 GLU   B CG     1 
ATOM   8316 C CD     . GLU   B 1 290 ? -14.45000 35.43300  -44.56200 1.000 63.93000  ? 256 GLU   B CD     1 
ATOM   8317 O OE1    . GLU   B 1 290 ? -14.69700 34.32900  -44.02100 1.000 58.07000  ? 256 GLU   B OE1    1 
ATOM   8318 O OE2    . GLU   B 1 290 ? -15.34100 36.24400  -44.89400 1.000 59.58000  ? 256 GLU   B OE2    1 
ATOM   8319 H H      . GLU   B 1 290 ? -10.38300 34.98300  -45.93300 1.000 30.86000  ? 256 GLU   B H      1 
ATOM   8320 H HA     . GLU   B 1 290 ? -10.70500 36.53400  -43.84800 1.000 31.37000  ? 256 GLU   B HA     1 
ATOM   8321 H HB2    . GLU   B 1 290 ? -11.96100 34.11300  -44.54700 1.000 34.91000  ? 256 GLU   B HB2    1 
ATOM   8322 H HB3    . GLU   B 1 290 ? -12.32300 34.85300  -43.18800 1.000 34.91000  ? 256 GLU   B HB3    1 
ATOM   8323 H HG2    . GLU   B 1 290 ? -12.89400 36.75200  -44.55100 1.000 44.25000  ? 256 GLU   B HG2    1 
ATOM   8324 H HG3    . GLU   B 1 290 ? -12.84800 35.75300  -45.78400 1.000 44.25000  ? 256 GLU   B HG3    1 
ATOM   8325 N N      . ASP   B 1 291 ? -9.20800  33.76000  -43.23000 1.000 28.94000  ? 257 ASP   B N      1 
ATOM   8326 C CA     . ASP   B 1 291 ? -8.31200  33.15600  -42.24400 1.000 26.97000  ? 257 ASP   B CA     1 
ATOM   8327 C C      . ASP   B 1 291 ? -7.15500  34.09400  -41.91600 1.000 25.46000  ? 257 ASP   B C      1 
ATOM   8328 O O      . ASP   B 1 291 ? -6.74500  34.20000  -40.76100 1.000 26.84000  ? 257 ASP   B O      1 
ATOM   8329 C CB     . ASP   B 1 291 ? -7.73500  31.81400  -42.74400 1.000 25.55000  ? 257 ASP   B CB     1 
ATOM   8330 C CG     . ASP   B 1 291 ? -8.79800  30.78600  -43.08500 1.000 32.98000  ? 257 ASP   B CG     1 
ATOM   8331 O OD1    . ASP   B 1 291 ? -9.87900  30.82300  -42.46900 1.000 35.46000  ? 257 ASP   B OD1    1 
ATOM   8332 O OD2    . ASP   B 1 291 ? -8.54100  29.90100  -43.95400 1.000 32.90000  ? 257 ASP   B OD2    1 
ATOM   8333 H H      . ASP   B 1 291 ? -9.31900  33.30300  -43.95000 1.000 28.94000  ? 257 ASP   B H      1 
ATOM   8334 H HA     . ASP   B 1 291 ? -8.80600  32.98700  -41.42600 1.000 26.97000  ? 257 ASP   B HA     1 
ATOM   8335 H HB2    . ASP   B 1 291 ? -7.21100  31.97700  -43.54400 1.000 25.55000  ? 257 ASP   B HB2    1 
ATOM   8336 H HB3    . ASP   B 1 291 ? -7.17000  31.43800  -42.05100 1.000 25.55000  ? 257 ASP   B HB3    1 
ATOM   8337 N N      . ALA   B 1 292 ? -6.56800  34.71700  -42.93900 1.000 26.40000  ? 258 ALA   B N      1 
ATOM   8338 C CA     . ALA   B 1 292 ? -5.45600  35.63100  -42.72300 1.000 25.14000  ? 258 ALA   B CA     1 
ATOM   8339 C C      . ALA   B 1 292 ? -5.90200  36.85100  -41.93300 1.000 30.65000  ? 258 ALA   B C      1 
ATOM   8340 O O      . ALA   B 1 292 ? -5.15600  37.36400  -41.08900 1.000 27.98000  ? 258 ALA   B O      1 
ATOM   8341 C CB     . ALA   B 1 292 ? -4.87600  36.05500  -44.07700 1.000 28.92000  ? 258 ALA   B CB     1 
ATOM   8342 H H      . ALA   B 1 292 ? -6.79700  34.62600  -43.76300 1.000 26.40000  ? 258 ALA   B H      1 
ATOM   8343 H HA     . ALA   B 1 292 ? -4.76100  35.17900  -42.22000 1.000 25.14000  ? 258 ALA   B HA     1 
ATOM   8344 H HB1    . ALA   B 1 292 ? -4.13400  36.66100  -43.92600 1.000 28.92000  ? 258 ALA   B HB1    1 
ATOM   8345 H HB2    . ALA   B 1 292 ? -4.56800  35.26600  -44.54900 1.000 28.92000  ? 258 ALA   B HB2    1 
ATOM   8346 H HB3    . ALA   B 1 292 ? -5.56800  36.49900  -44.59100 1.000 28.92000  ? 258 ALA   B HB3    1 
ATOM   8347 N N      . PHE   B 1 293 ? -7.11000  37.34100  -42.21900 1.000 26.60000  ? 259 PHE   B N      1 
ATOM   8348 C CA     . PHE   B 1 293 ? -7.66900  38.48400  -41.49600 1.000 28.95000  ? 259 PHE   B CA     1 
ATOM   8349 C C      . PHE   B 1 293 ? -7.75000  38.19300  -40.00100 1.000 29.38000  ? 259 PHE   B C      1 
ATOM   8350 O O      . PHE   B 1 293 ? -7.41600  39.04700  -39.16900 1.000 29.10000  ? 259 PHE   B O      1 
ATOM   8351 C CB     . PHE   B 1 293 ? -9.05600  38.80100  -42.07200 1.000 29.33000  ? 259 PHE   B CB     1 
ATOM   8352 C CG     . PHE   B 1 293 ? -9.81000  39.87300  -41.30700 1.000 29.11000  ? 259 PHE   B CG     1 
ATOM   8353 C CD1    . PHE   B 1 293 ? -9.58900  41.21500  -41.56800 1.000 31.33000  ? 259 PHE   B CD1    1 
ATOM   8354 C CD2    . PHE   B 1 293 ? -10.72700 39.52800  -40.32900 1.000 32.25000  ? 259 PHE   B CD2    1 
ATOM   8355 C CE1    . PHE   B 1 293 ? -10.27400 42.19700  -40.86300 1.000 38.03000  ? 259 PHE   B CE1    1 
ATOM   8356 C CE2    . PHE   B 1 293 ? -11.40500 40.49000  -39.62600 1.000 38.06000  ? 259 PHE   B CE2    1 
ATOM   8357 C CZ     . PHE   B 1 293 ? -11.17500 41.83600  -39.89600 1.000 37.06000  ? 259 PHE   B CZ     1 
ATOM   8358 H H      . PHE   B 1 293 ? -7.62700  37.02700  -42.83000 1.000 26.60000  ? 259 PHE   B H      1 
ATOM   8359 H HA     . PHE   B 1 293 ? -7.09900  39.25800  -41.62700 1.000 28.95000  ? 259 PHE   B HA     1 
ATOM   8360 H HB2    . PHE   B 1 293 ? -8.95200  39.10800  -42.98600 1.000 29.33000  ? 259 PHE   B HB2    1 
ATOM   8361 H HB3    . PHE   B 1 293 ? -9.59300  37.99300  -42.05600 1.000 29.33000  ? 259 PHE   B HB3    1 
ATOM   8362 H HD1    . PHE   B 1 293 ? -8.97500  41.46200  -42.22200 1.000 31.33000  ? 259 PHE   B HD1    1 
ATOM   8363 H HD2    . PHE   B 1 293 ? -10.88100 38.63000  -40.14200 1.000 32.25000  ? 259 PHE   B HD2    1 
ATOM   8364 H HE1    . PHE   B 1 293 ? -10.11900 43.09600  -41.04500 1.000 38.03000  ? 259 PHE   B HE1    1 
ATOM   8365 H HE2    . PHE   B 1 293 ? -12.01900 40.24400  -38.97200 1.000 38.06000  ? 259 PHE   B HE2    1 
ATOM   8366 H HZ     . PHE   B 1 293 ? -11.63800 42.49000  -39.42400 1.000 37.06000  ? 259 PHE   B HZ     1 
ATOM   8367 N N      . LEU   B 1 294 ? -8.19600  36.98300  -39.64800 1.000 27.81000  ? 260 LEU   B N      1 
ATOM   8368 C CA     . LEU   B 1 294 ? -8.28100  36.58400  -38.24700 1.000 28.70000  ? 260 LEU   B CA     1 
ATOM   8369 C C      . LEU   B 1 294 ? -6.90600  36.48700  -37.59800 1.000 31.39000  ? 260 LEU   B C      1 
ATOM   8370 O O      . LEU   B 1 294 ? -6.74300  36.88300  -36.43600 1.000 27.58000  ? 260 LEU   B O      1 
ATOM   8371 C CB     . LEU   B 1 294 ? -9.04000  35.24800  -38.12600 1.000 26.16000  ? 260 LEU   B CB     1 
ATOM   8372 C CG     . LEU   B 1 294 ? -10.53100 35.32600  -38.48500 1.000 30.94000  ? 260 LEU   B CG     1 
ATOM   8373 C CD1    . LEU   B 1 294 ? -11.24400 33.95400  -38.30500 1.000 30.19000  ? 260 LEU   B CD1    1 
ATOM   8374 C CD2    . LEU   B 1 294 ? -11.24200 36.43200  -37.67200 1.000 29.12000  ? 260 LEU   B CD2    1 
ATOM   8375 H H      . LEU   B 1 294 ? -8.45400  36.37900  -40.20300 1.000 27.81000  ? 260 LEU   B H      1 
ATOM   8376 H HA     . LEU   B 1 294 ? -8.77700  37.26100  -37.76200 1.000 28.70000  ? 260 LEU   B HA     1 
ATOM   8377 H HB2    . LEU   B 1 294 ? -8.62800  34.60200  -38.72100 1.000 26.16000  ? 260 LEU   B HB2    1 
ATOM   8378 H HB3    . LEU   B 1 294 ? -8.97400  34.93600  -37.21000 1.000 26.16000  ? 260 LEU   B HB3    1 
ATOM   8379 H HG     . LEU   B 1 294 ? -10.60500 35.56700  -39.42200 1.000 30.94000  ? 260 LEU   B HG     1 
ATOM   8380 H HD11   . LEU   B 1 294 ? -12.17900 34.05000  -38.54600 1.000 30.19000  ? 260 LEU   B HD11   1 
ATOM   8381 H HD12   . LEU   B 1 294 ? -10.81900 33.30000  -38.88200 1.000 30.19000  ? 260 LEU   B HD12   1 
ATOM   8382 H HD13   . LEU   B 1 294 ? -11.16700 33.67800  -37.37800 1.000 30.19000  ? 260 LEU   B HD13   1 
ATOM   8383 H HD21   . LEU   B 1 294 ? -12.19900 36.27500  -37.69400 1.000 29.12000  ? 260 LEU   B HD21   1 
ATOM   8384 H HD22   . LEU   B 1 294 ? -10.92200 36.40500  -36.75700 1.000 29.12000  ? 260 LEU   B HD22   1 
ATOM   8385 H HD23   . LEU   B 1 294 ? -11.03800 37.29400  -38.06700 1.000 29.12000  ? 260 LEU   B HD23   1 
ATOM   8386 N N      . HIS   B 1 295 ? -5.91400  35.92800  -38.30300 1.000 27.82000  ? 261 HIS   B N      1 
ATOM   8387 C CA     . HIS   B 1 295 ? -4.55500  35.94000  -37.76100 1.000 27.05000  ? 261 HIS   B CA     1 
ATOM   8388 C C      . HIS   B 1 295 ? -4.11400  37.35600  -37.43500 1.000 25.83000  ? 261 HIS   B C      1 
ATOM   8389 O O      . HIS   B 1 295 ? -3.55600  37.61500  -36.36300 1.000 28.43000  ? 261 HIS   B O      1 
ATOM   8390 C CB     . HIS   B 1 295 ? -3.56600  35.31600  -38.74500 1.000 25.44000  ? 261 HIS   B CB     1 
ATOM   8391 C CG     . HIS   B 1 295 ? -3.35300  33.85100  -38.52200 1.000 28.78000  ? 261 HIS   B CG     1 
ATOM   8392 N ND1    . HIS   B 1 295 ? -2.64300  33.35300  -37.44600 1.000 29.67000  ? 261 HIS   B ND1    1 
ATOM   8393 C CD2    . HIS   B 1 295 ? -3.77200  32.77500  -39.22600 1.000 29.03000  ? 261 HIS   B CD2    1 
ATOM   8394 C CE1    . HIS   B 1 295 ? -2.60800  32.03300  -37.51500 1.000 30.54000  ? 261 HIS   B CE1    1 
ATOM   8395 N NE2    . HIS   B 1 295 ? -3.29200  31.65800  -38.58200 1.000 27.80000  ? 261 HIS   B NE2    1 
ATOM   8396 H H      . HIS   B 1 295 ? -5.99900  35.54900  -39.07000 1.000 27.82000  ? 261 HIS   B H      1 
ATOM   8397 H HA     . HIS   B 1 295 ? -4.53500  35.42100  -36.94200 1.000 27.05000  ? 261 HIS   B HA     1 
ATOM   8398 H HB2    . HIS   B 1 295 ? -3.90300  35.43400  -39.64700 1.000 25.44000  ? 261 HIS   B HB2    1 
ATOM   8399 H HB3    . HIS   B 1 295 ? -2.70800  35.75900  -38.65200 1.000 25.44000  ? 261 HIS   B HB3    1 
ATOM   8400 H HD2    . HIS   B 1 295 ? -4.27600  32.78800  -40.00800 1.000 29.03000  ? 261 HIS   B HD2    1 
ATOM   8401 H HE1    . HIS   B 1 295 ? -2.19200  31.46600  -36.90600 1.000 30.54000  ? 261 HIS   B HE1    1 
ATOM   8402 H HE2    . HIS   B 1 295 ? -3.41900  30.84500  -38.83200 1.000 27.80000  ? 261 HIS   B HE2    1 
ATOM   8403 N N      . VAL   B 1 296 ? -4.32800  38.28700  -38.36800 1.000 27.51000  ? 262 VAL   B N      1 
ATOM   8404 C CA     . VAL   B 1 296 ? -3.90800  39.66900  -38.11100 1.000 23.90000  ? 262 VAL   B CA     1 
ATOM   8405 C C      . VAL   B 1 296 ? -4.69300  40.26800  -36.94200 1.000 28.16000  ? 262 VAL   B C      1 
ATOM   8406 O O      . VAL   B 1 296 ? -4.12300  40.95100  -36.07800 1.000 27.52000  ? 262 VAL   B O      1 
ATOM   8407 C CB     . VAL   B 1 296 ? -4.04100  40.52500  -39.38400 1.000 24.50000  ? 262 VAL   B CB     1 
ATOM   8408 C CG1    . VAL   B 1 296 ? -3.68700  41.99100  -39.06700 1.000 27.87000  ? 262 VAL   B CG1    1 
ATOM   8409 C CG2    . VAL   B 1 296 ? -3.10400  40.00000  -40.47500 1.000 26.45000  ? 262 VAL   B CG2    1 
ATOM   8410 H H      . VAL   B 1 296 ? -4.70100  38.15300  -39.13100 1.000 27.51000  ? 262 VAL   B H      1 
ATOM   8411 H HA     . VAL   B 1 296 ? -2.97100  39.66400  -37.86000 1.000 23.90000  ? 262 VAL   B HA     1 
ATOM   8412 H HB     . VAL   B 1 296 ? -4.95300  40.48800  -39.71100 1.000 24.50000  ? 262 VAL   B HB     1 
ATOM   8413 H HG11   . VAL   B 1 296 ? -3.53700  42.46500  -39.90000 1.000 27.87000  ? 262 VAL   B HG11   1 
ATOM   8414 H HG12   . VAL   B 1 296 ? -4.42300  42.39900  -38.58400 1.000 27.87000  ? 262 VAL   B HG12   1 
ATOM   8415 H HG13   . VAL   B 1 296 ? -2.88200  42.01100  -38.52700 1.000 27.87000  ? 262 VAL   B HG13   1 
ATOM   8416 H HG21   . VAL   B 1 296 ? -3.19100  40.56000  -41.26200 1.000 26.45000  ? 262 VAL   B HG21   1 
ATOM   8417 H HG22   . VAL   B 1 296 ? -2.19100  40.02900  -40.14700 1.000 26.45000  ? 262 VAL   B HG22   1 
ATOM   8418 H HG23   . VAL   B 1 296 ? -3.35000  39.08700  -40.69000 1.000 26.45000  ? 262 VAL   B HG23   1 
ATOM   8419 N N      . LEU   B 1 297 ? -6.00700  40.02900  -36.89800 1.000 31.40000  ? 263 LEU   B N      1 
ATOM   8420 C CA     . LEU   B 1 297 ? -6.81800  40.51400  -35.77600 1.000 31.75000  ? 263 LEU   B CA     1 
ATOM   8421 C C      . LEU   B 1 297 ? -6.30100  39.97600  -34.44200 1.000 29.97000  ? 263 LEU   B C      1 
ATOM   8422 O O      . LEU   B 1 297 ? -6.36500  40.65700  -33.41400 1.000 32.43000  ? 263 LEU   B O      1 
ATOM   8423 C CB     . LEU   B 1 297 ? -8.27300  40.10200  -35.99100 1.000 32.53000  ? 263 LEU   B CB     1 
ATOM   8424 C CG     . LEU   B 1 297 ? -9.46300  40.74000  -35.29500 1.000 42.80000  ? 263 LEU   B CG     1 
ATOM   8425 C CD1    . LEU   B 1 297 ? -9.54900  42.24900  -35.58900 1.000 33.90000  ? 263 LEU   B CD1    1 
ATOM   8426 C CD2    . LEU   B 1 297 ? -10.72500 39.99000  -35.75000 1.000 35.77000  ? 263 LEU   B CD2    1 
ATOM   8427 H H      . LEU   B 1 297 ? -6.44700  39.59500  -37.49600 1.000 31.40000  ? 263 LEU   B H      1 
ATOM   8428 H HA     . LEU   B 1 297 ? -6.77800  41.48300  -35.74800 1.000 31.75000  ? 263 LEU   B HA     1 
ATOM   8429 H HB2    . LEU   B 1 297 ? -8.44800  40.20000  -36.94000 1.000 32.53000  ? 263 LEU   B HB2    1 
ATOM   8430 H HB3    . LEU   B 1 297 ? -8.32100  39.15800  -35.77300 1.000 32.53000  ? 263 LEU   B HB3    1 
ATOM   8431 H HG     . LEU   B 1 297 ? -9.37100  40.62300  -34.33600 1.000 42.80000  ? 263 LEU   B HG     1 
ATOM   8432 H HD11   . LEU   B 1 297 ? -10.32600 42.61400  -35.13800 1.000 33.90000  ? 263 LEU   B HD11   1 
ATOM   8433 H HD12   . LEU   B 1 297 ? -8.74400  42.68000  -35.26300 1.000 33.90000  ? 263 LEU   B HD12   1 
ATOM   8434 H HD13   . LEU   B 1 297 ? -9.63000  42.38000  -36.54700 1.000 33.90000  ? 263 LEU   B HD13   1 
ATOM   8435 H HD21   . LEU   B 1 297 ? -11.44700 40.19400  -35.13600 1.000 35.77000  ? 263 LEU   B HD21   1 
ATOM   8436 H HD22   . LEU   B 1 297 ? -10.95900 40.28000  -36.64600 1.000 35.77000  ? 263 LEU   B HD22   1 
ATOM   8437 H HD23   . LEU   B 1 297 ? -10.54800 39.03700  -35.74600 1.000 35.77000  ? 263 LEU   B HD23   1 
ATOM   8438 N N      . ALA   B 1 298 ? -5.81100  38.74100  -34.43400 1.000 29.10000  ? 264 ALA   B N      1 
ATOM   8439 C CA     . ALA   B 1 298 ? -5.24700  38.14800  -33.23200 1.000 30.09000  ? 264 ALA   B CA     1 
ATOM   8440 C C      . ALA   B 1 298 ? -3.87800  38.71800  -32.89600 1.000 27.03000  ? 264 ALA   B C      1 
ATOM   8441 O O      . ALA   B 1 298 ? -3.39500  38.53100  -31.76600 1.000 29.63000  ? 264 ALA   B O      1 
ATOM   8442 C CB     . ALA   B 1 298 ? -5.16200  36.61500  -33.40100 1.000 27.78000  ? 264 ALA   B CB     1 
ATOM   8443 H H      . ALA   B 1 298 ? -5.79400  38.22200  -35.12000 1.000 29.10000  ? 264 ALA   B H      1 
ATOM   8444 H HA     . ALA   B 1 298 ? -5.83700  38.33300  -32.48500 1.000 30.09000  ? 264 ALA   B HA     1 
ATOM   8445 H HB1    . ALA   B 1 298 ? -4.78000  36.23000  -32.59700 1.000 27.78000  ? 264 ALA   B HB1    1 
ATOM   8446 H HB2    . ALA   B 1 298 ? -6.05500  36.26400  -33.54500 1.000 27.78000  ? 264 ALA   B HB2    1 
ATOM   8447 H HB3    . ALA   B 1 298 ? -4.59900  36.41300  -34.16400 1.000 27.78000  ? 264 ALA   B HB3    1 
ATOM   8448 N N      . GLY   B 1 299 ? -3.24500  39.41400  -33.84400 1.000 28.16000  ? 265 GLY   B N      1 
ATOM   8449 C CA     . GLY   B 1 299 ? -1.99000  40.06800  -33.55600 1.000 26.23000  ? 265 GLY   B CA     1 
ATOM   8450 C C      . GLY   B 1 299 ? -0.87100  39.79400  -34.54500 1.000 28.07000  ? 265 GLY   B C      1 
ATOM   8451 O O      . GLY   B 1 299 ? 0.23000   40.31300  -34.36500 1.000 29.18000  ? 265 GLY   B O      1 
ATOM   8452 H H      . GLY   B 1 299 ? -3.52500  39.51600  -34.65100 1.000 28.16000  ? 265 GLY   B H      1 
ATOM   8453 H HA2    . GLY   B 1 299 ? -2.13700  41.02700  -33.53400 1.000 26.23000  ? 265 GLY   B HA2    1 
ATOM   8454 H HA3    . GLY   B 1 299 ? -1.67900  39.79600  -32.67900 1.000 26.23000  ? 265 GLY   B HA3    1 
ATOM   8455 N N      . ALA   B 1 300 ? -1.11300  38.99400  -35.58400 1.000 27.40000  ? 266 ALA   B N      1 
ATOM   8456 C CA     . ALA   B 1 300 ? -0.03200  38.64400  -36.50700 1.000 24.83000  ? 266 ALA   B CA     1 
ATOM   8457 C C      . ALA   B 1 300 ? 0.41400   39.83100  -37.36000 1.000 26.33000  ? 266 ALA   B C      1 
ATOM   8458 O O      . ALA   B 1 300 ? -0.42700  40.53400  -37.93200 1.000 25.47000  ? 266 ALA   B O      1 
ATOM   8459 C CB     . ALA   B 1 300 ? -0.46300  37.50800  -37.44200 1.000 22.37000  ? 266 ALA   B CB     1 
ATOM   8460 H H      . ALA   B 1 300 ? -1.87700  38.64700  -35.77400 1.000 27.40000  ? 266 ALA   B H      1 
ATOM   8461 H HA     . ALA   B 1 300 ? 0.73300   38.33800  -35.99500 1.000 24.83000  ? 266 ALA   B HA     1 
ATOM   8462 H HB1    . ALA   B 1 300 ? 0.27000   37.29700  -38.04100 1.000 22.37000  ? 266 ALA   B HB1    1 
ATOM   8463 H HB2    . ALA   B 1 300 ? -0.69000  36.73000  -36.90900 1.000 22.37000  ? 266 ALA   B HB2    1 
ATOM   8464 H HB3    . ALA   B 1 300 ? -1.23600  37.79600  -37.95300 1.000 22.37000  ? 266 ALA   B HB3    1 
ATOM   8465 N N      . SER   B 1 301 ? 1.75100   40.01400  -37.47100 1.000 27.21000  ? 267 SER   B N      1 
ATOM   8466 C CA     . SER   B 1 301 ? 2.34000   40.98100  -38.40100 1.000 25.92000  ? 267 SER   B CA     1 
ATOM   8467 C C      . SER   B 1 301 ? 2.51000   40.38500  -39.79600 1.000 30.38000  ? 267 SER   B C      1 
ATOM   8468 O O      . SER   B 1 301 ? 2.12500   41.00400  -40.79200 1.000 30.07000  ? 267 SER   B O      1 
ATOM   8469 C CB     . SER   B 1 301 ? 3.69900   41.49400  -37.88500 1.000 27.33000  ? 267 SER   B CB     1 
ATOM   8470 O OG     . SER   B 1 301 ? 3.49400   42.33000  -36.76100 1.000 40.03000  ? 267 SER   B OG     1 
ATOM   8471 H H      . SER   B 1 301 ? 2.33400   39.58100  -37.01000 1.000 27.21000  ? 267 SER   B H      1 
ATOM   8472 H HA     . SER   B 1 301 ? 1.74600   41.74300  -38.47700 1.000 25.92000  ? 267 SER   B HA     1 
ATOM   8473 H HB2    . SER   B 1 301 ? 4.24900   40.73800  -37.62500 1.000 27.33000  ? 267 SER   B HB2    1 
ATOM   8474 H HB3    . SER   B 1 301 ? 4.13600   42.00200  -38.58600 1.000 27.33000  ? 267 SER   B HB3    1 
ATOM   8475 H HG     . SER   B 1 301 ? 3.11100   41.90000  -36.14900 1.000 40.03000  ? 267 SER   B HG     1 
ATOM   8476 N N      . MET   B 1 302 ? 3.12100   39.20100  -39.89500 1.000 29.25000  ? 268 MET   B N      1 
ATOM   8477 C CA     . MET   B 1 302 ? 3.16700   38.43100  -41.13700 1.000 25.21000  ? 268 MET   B CA     1 
ATOM   8478 C C      . MET   B 1 302 ? 2.32300   37.17600  -40.95600 1.000 27.10000  ? 268 MET   B C      1 
ATOM   8479 O O      . MET   B 1 302 ? 2.08300   36.73400  -39.83000 1.000 25.93000  ? 268 MET   B O      1 
ATOM   8480 C CB     . MET   B 1 302 ? 4.60500   38.03000  -41.53100 1.000 25.89000  ? 268 MET   B CB     1 
ATOM   8481 C CG     . MET   B 1 302 ? 5.60800   39.22600  -41.69200 1.000 26.47000  ? 268 MET   B CG     1 
ATOM   8482 S SD     . MET   B 1 302 ? 5.25300   40.28500  -43.10200 1.000 30.68000  ? 268 MET   B SD     1 
ATOM   8483 C CE     . MET   B 1 302 ? 5.90800   39.22200  -44.44100 1.000 30.77000  ? 268 MET   B CE     1 
ATOM   8484 H H      . MET   B 1 302 ? 3.52400   38.81600  -39.24000 1.000 29.25000  ? 268 MET   B H      1 
ATOM   8485 H HA     . MET   B 1 302 ? 2.79500   38.96200  -41.85800 1.000 25.21000  ? 268 MET   B HA     1 
ATOM   8486 H HB2    . MET   B 1 302 ? 4.95900   37.44100  -40.84600 1.000 25.89000  ? 268 MET   B HB2    1 
ATOM   8487 H HB3    . MET   B 1 302 ? 4.57300   37.56000  -42.37900 1.000 25.89000  ? 268 MET   B HB3    1 
ATOM   8488 H HG2    . MET   B 1 302 ? 5.57200   39.77400  -40.89300 1.000 26.47000  ? 268 MET   B HG2    1 
ATOM   8489 H HG3    . MET   B 1 302 ? 6.50300   38.87000  -41.80600 1.000 26.47000  ? 268 MET   B HG3    1 
ATOM   8490 H HE1    . MET   B 1 302 ? 5.78700   39.67400  -45.29000 1.000 30.77000  ? 268 MET   B HE1    1 
ATOM   8491 H HE2    . MET   B 1 302 ? 6.85100   39.06100  -44.28300 1.000 30.77000  ? 268 MET   B HE2    1 
ATOM   8492 H HE3    . MET   B 1 302 ? 5.42400   38.38100  -44.44100 1.000 30.77000  ? 268 MET   B HE3    1 
ATOM   8493 N N      . VAL   B 1 303 ? 1.87400   36.61500  -42.07600 1.000 25.72000  ? 269 VAL   B N      1 
ATOM   8494 C CA     . VAL   B 1 303 ? 1.02000   35.42600  -42.10300 1.000 24.10000  ? 269 VAL   B CA     1 
ATOM   8495 C C      . VAL   B 1 303 ? 1.67500   34.40200  -43.02400 1.000 27.13000  ? 269 VAL   B C      1 
ATOM   8496 O O      . VAL   B 1 303 ? 1.86700   34.67400  -44.21200 1.000 27.61000  ? 269 VAL   B O      1 
ATOM   8497 C CB     . VAL   B 1 303 ? -0.40400  35.76200  -42.58600 1.000 27.42000  ? 269 VAL   B CB     1 
ATOM   8498 C CG1    . VAL   B 1 303 ? -1.31100  34.49900  -42.63100 1.000 26.50000  ? 269 VAL   B CG1    1 
ATOM   8499 C CG2    . VAL   B 1 303 ? -1.02200  36.85600  -41.71900 1.000 29.06000  ? 269 VAL   B CG2    1 
ATOM   8500 H H      . VAL   B 1 303 ? 2.05700   36.91500  -42.86100 1.000 25.72000  ? 269 VAL   B H      1 
ATOM   8501 H HA     . VAL   B 1 303 ? 0.96100   35.04600  -41.21200 1.000 24.10000  ? 269 VAL   B HA     1 
ATOM   8502 H HB     . VAL   B 1 303 ? -0.34600  36.10800  -43.49000 1.000 27.42000  ? 269 VAL   B HB     1 
ATOM   8503 H HG11   . VAL   B 1 303 ? -2.22200  34.77300  -42.82000 1.000 26.50000  ? 269 VAL   B HG11   1 
ATOM   8504 H HG12   . VAL   B 1 303 ? -0.99400  33.90400  -43.32900 1.000 26.50000  ? 269 VAL   B HG12   1 
ATOM   8505 H HG13   . VAL   B 1 303 ? -1.27200  34.05200  -41.77100 1.000 26.50000  ? 269 VAL   B HG13   1 
ATOM   8506 H HG21   . VAL   B 1 303 ? -1.93700  37.00400  -42.00300 1.000 29.06000  ? 269 VAL   B HG21   1 
ATOM   8507 H HG22   . VAL   B 1 303 ? -1.00500  36.57000  -40.79200 1.000 29.06000  ? 269 VAL   B HG22   1 
ATOM   8508 H HG23   . VAL   B 1 303 ? -0.50700  37.67100  -41.82300 1.000 29.06000  ? 269 VAL   B HG23   1 
ATOM   8509 N N      . GLN   B 1 304 ? 2.01600   33.23400  -42.47900 1.000 26.50000  ? 270 GLN   B N      1 
ATOM   8510 C CA     . GLN   B 1 304 ? 2.70600   32.18900  -43.22700 1.000 24.57000  ? 270 GLN   B CA     1 
ATOM   8511 C C      . GLN   B 1 304 ? 1.70700   31.12600  -43.66300 1.000 24.69000  ? 270 GLN   B C      1 
ATOM   8512 O O      . GLN   B 1 304 ? 0.72900   30.84600  -42.96400 1.000 27.71000  ? 270 GLN   B O      1 
ATOM   8513 C CB     . GLN   B 1 304 ? 3.81800   31.54900  -42.38200 1.000 22.80000  ? 270 GLN   B CB     1 
ATOM   8514 C CG     . GLN   B 1 304 ? 4.77800   32.54300  -41.77900 1.000 26.96000  ? 270 GLN   B CG     1 
ATOM   8515 C CD     . GLN   B 1 304 ? 5.97600   31.86200  -41.12200 1.000 29.20000  ? 270 GLN   B CD     1 
ATOM   8516 O OE1    . GLN   B 1 304 ? 5.91600   30.67900  -40.72400 1.000 30.25000  ? 270 GLN   B OE1    1 
ATOM   8517 N NE2    . GLN   B 1 304 ? 7.07500   32.60300  -41.00700 1.000 31.41000  ? 270 GLN   B NE2    1 
ATOM   8518 H H      . GLN   B 1 304 ? 1.85400   33.02200  -41.66200 1.000 26.50000  ? 270 GLN   B H      1 
ATOM   8519 H HA     . GLN   B 1 304 ? 3.11000   32.57300  -44.02100 1.000 24.57000  ? 270 GLN   B HA     1 
ATOM   8520 H HB2    . GLN   B 1 304 ? 3.41100   31.05300  -41.65500 1.000 22.80000  ? 270 GLN   B HB2    1 
ATOM   8521 H HB3    . GLN   B 1 304 ? 4.33000   30.94700  -42.94400 1.000 22.80000  ? 270 GLN   B HB3    1 
ATOM   8522 H HG2    . GLN   B 1 304 ? 5.10800   33.13100  -42.47400 1.000 26.96000  ? 270 GLN   B HG2    1 
ATOM   8523 H HG3    . GLN   B 1 304 ? 4.31500   33.05800  -41.09900 1.000 26.96000  ? 270 GLN   B HG3    1 
ATOM   8524 H HE21   . GLN   B 1 304 ? 7.07900   33.41400  -41.29300 1.000 31.41000  ? 270 GLN   B HE21   1 
ATOM   8525 H HE22   . GLN   B 1 304 ? 7.78100   32.27200  -40.64500 1.000 31.41000  ? 270 GLN   B HE22   1 
ATOM   8526 N N      . VAL   B 1 305 ? 1.97000   30.52000  -44.82000 1.000 24.17000  ? 271 VAL   B N      1 
ATOM   8527 C CA     . VAL   B 1 305 ? 1.02800   29.60100  -45.46000 1.000 25.92000  ? 271 VAL   B CA     1 
ATOM   8528 C C      . VAL   B 1 305 ? 1.78500   28.30800  -45.76900 1.000 27.65000  ? 271 VAL   B C      1 
ATOM   8529 O O      . VAL   B 1 305 ? 2.75800   28.32900  -46.53900 1.000 26.12000  ? 271 VAL   B O      1 
ATOM   8530 C CB     . VAL   B 1 305 ? 0.41900   30.21600  -46.74000 1.000 25.24000  ? 271 VAL   B CB     1 
ATOM   8531 C CG1    . VAL   B 1 305 ? -0.71300  29.34300  -47.24200 1.000 28.05000  ? 271 VAL   B CG1    1 
ATOM   8532 C CG2    . VAL   B 1 305 ? -0.10300  31.66200  -46.49000 1.000 24.93000  ? 271 VAL   B CG2    1 
ATOM   8533 H H      . VAL   B 1 305 ? 2.70000   30.62700  -45.26200 1.000 24.17000  ? 271 VAL   B H      1 
ATOM   8534 H HA     . VAL   B 1 305 ? 0.30600   29.39400  -44.84600 1.000 25.92000  ? 271 VAL   B HA     1 
ATOM   8535 H HB     . VAL   B 1 305 ? 1.10000   30.25500  -47.43000 1.000 25.24000  ? 271 VAL   B HB     1 
ATOM   8536 H HG11   . VAL   B 1 305 ? -1.12500  29.77200  -48.00900 1.000 28.05000  ? 271 VAL   B HG11   1 
ATOM   8537 H HG12   . VAL   B 1 305 ? -0.35600  28.47800  -47.49900 1.000 28.05000  ? 271 VAL   B HG12   1 
ATOM   8538 H HG13   . VAL   B 1 305 ? -1.36600  29.23500  -46.53300 1.000 28.05000  ? 271 VAL   B HG13   1 
ATOM   8539 H HG21   . VAL   B 1 305 ? -0.54500  31.98100  -47.29200 1.000 24.93000  ? 271 VAL   B HG21   1 
ATOM   8540 H HG22   . VAL   B 1 305 ? -0.73000  31.64700  -45.75000 1.000 24.93000  ? 271 VAL   B HG22   1 
ATOM   8541 H HG23   . VAL   B 1 305 ? 0.64800   32.23700  -46.27600 1.000 24.93000  ? 271 VAL   B HG23   1 
ATOM   8542 N N      . GLY   B 1 306 ? 1.37400   27.19600  -45.13200 1.000 28.01000  ? 272 GLY   B N      1 
ATOM   8543 C CA     . GLY   B 1 306 ? 2.06600   25.93000  -45.31600 1.000 25.49000  ? 272 GLY   B CA     1 
ATOM   8544 C C      . GLY   B 1 306 ? 1.26400   24.95300  -46.15000 1.000 30.05000  ? 272 GLY   B C      1 
ATOM   8545 O O      . GLY   B 1 306 ? 1.39200   24.94000  -47.36600 1.000 27.43000  ? 272 GLY   B O      1 
ATOM   8546 H H      . GLY   B 1 306 ? 0.70300   27.15900  -44.59500 1.000 28.01000  ? 272 GLY   B H      1 
ATOM   8547 H HA2    . GLY   B 1 306 ? 2.91800   26.08200  -45.75400 1.000 25.49000  ? 272 GLY   B HA2    1 
ATOM   8548 H HA3    . GLY   B 1 306 ? 2.23500   25.52700  -44.45000 1.000 25.49000  ? 272 GLY   B HA3    1 
ATOM   8549 N N      . THR   B 1 307 ? 0.40000   24.16500  -45.51000 1.000 25.63000  ? 273 THR   B N      1 
ATOM   8550 C CA     . THR   B 1 307 ? -0.31800  23.09900  -46.21300 1.000 25.99000  ? 273 THR   B CA     1 
ATOM   8551 C C      . THR   B 1 307 ? -1.04800  23.61900  -47.45200 1.000 27.85000  ? 273 THR   B C      1 
ATOM   8552 O O      . THR   B 1 307 ? -1.00300  22.99100  -48.51500 1.000 27.45000  ? 273 THR   B O      1 
ATOM   8553 C CB     . THR   B 1 307 ? -1.31000  22.42800  -45.25800 1.000 26.14000  ? 273 THR   B CB     1 
ATOM   8554 O OG1    . THR   B 1 307 ? -0.61400  21.82400  -44.15600 1.000 28.58000  ? 273 THR   B OG1    1 
ATOM   8555 C CG2    . THR   B 1 307 ? -2.13100  21.35800  -45.98800 1.000 26.51000  ? 273 THR   B CG2    1 
ATOM   8556 H H      . THR   B 1 307 ? 0.21200   24.22600  -44.67300 1.000 25.63000  ? 273 THR   B H      1 
ATOM   8557 H HA     . THR   B 1 307 ? 0.32000   22.42800  -46.50200 1.000 25.99000  ? 273 THR   B HA     1 
ATOM   8558 H HB     . THR   B 1 307 ? -1.92400  23.09700  -44.91700 1.000 26.14000  ? 273 THR   B HB     1 
ATOM   8559 H HG1    . THR   B 1 307 ? -0.18500  22.40900  -43.73200 1.000 28.58000  ? 273 THR   B HG1    1 
ATOM   8560 H HG21   . THR   B 1 307 ? -2.57000  20.78200  -45.34200 1.000 26.51000  ? 273 THR   B HG21   1 
ATOM   8561 H HG22   . THR   B 1 307 ? -2.80600  21.77600  -46.54500 1.000 26.51000  ? 273 THR   B HG22   1 
ATOM   8562 H HG23   . THR   B 1 307 ? -1.55000  20.81800  -46.54600 1.000 26.51000  ? 273 THR   B HG23   1 
ATOM   8563 N N      . ALA   B 1 308 ? -1.77100  24.74500  -47.32000 1.000 28.01000  ? 274 ALA   B N      1 
ATOM   8564 C CA     . ALA   B 1 308 ? -2.53900  25.26200  -48.45600 1.000 27.35000  ? 274 ALA   B CA     1 
ATOM   8565 C C      . ALA   B 1 308 ? -1.64000  25.58500  -49.63800 1.000 30.75000  ? 274 ALA   B C      1 
ATOM   8566 O O      . ALA   B 1 308 ? -2.03000  25.41100  -50.80000 1.000 28.25000  ? 274 ALA   B O      1 
ATOM   8567 C CB     . ALA   B 1 308 ? -3.32600  26.51900  -48.03800 1.000 26.24000  ? 274 ALA   B CB     1 
ATOM   8568 H H      . ALA   B 1 308 ? -1.83000  25.21400  -46.60100 1.000 28.01000  ? 274 ALA   B H      1 
ATOM   8569 H HA     . ALA   B 1 308 ? -3.17700  24.58800  -48.73900 1.000 27.35000  ? 274 ALA   B HA     1 
ATOM   8570 H HB1    . ALA   B 1 308 ? -3.82900  26.84400  -48.80100 1.000 26.24000  ? 274 ALA   B HB1    1 
ATOM   8571 H HB2    . ALA   B 1 308 ? -3.93100  26.28700  -47.31600 1.000 26.24000  ? 274 ALA   B HB2    1 
ATOM   8572 H HB3    . ALA   B 1 308 ? -2.70100  27.19800  -47.74000 1.000 26.24000  ? 274 ALA   B HB3    1 
ATOM   8573 N N      . LEU   B 1 309 ? -0.43900  26.09100  -49.36300 1.000 25.46000  ? 275 LEU   B N      1 
ATOM   8574 C CA     . LEU   B 1 309 ? 0.49500   26.40400  -50.43700 1.000 29.28000  ? 275 LEU   B CA     1 
ATOM   8575 C C      . LEU   B 1 309 ? 1.07400   25.13000  -51.04100 1.000 27.00000  ? 275 LEU   B C      1 
ATOM   8576 O O      . LEU   B 1 309 ? 1.31500   25.05200  -52.25800 1.000 29.10000  ? 275 LEU   B O      1 
ATOM   8577 C CB     . LEU   B 1 309 ? 1.61000   27.30300  -49.89200 1.000 29.64000  ? 275 LEU   B CB     1 
ATOM   8578 C CG     . LEU   B 1 309 ? 2.87000   27.42500  -50.73800 1.000 28.65000  ? 275 LEU   B CG     1 
ATOM   8579 C CD1    . LEU   B 1 309 ? 2.56100   28.25500  -52.00400 1.000 23.59000  ? 275 LEU   B CD1    1 
ATOM   8580 C CD2    . LEU   B 1 309 ? 4.00500   28.04800  -49.89500 1.000 25.54000  ? 275 LEU   B CD2    1 
ATOM   8581 H H      . LEU   B 1 309 ? -0.14500  26.26000  -48.57200 1.000 25.46000  ? 275 LEU   B H      1 
ATOM   8582 H HA     . LEU   B 1 309 ? 0.02900   26.88800  -51.13700 1.000 29.28000  ? 275 LEU   B HA     1 
ATOM   8583 H HB2    . LEU   B 1 309 ? 1.25100   28.19700  -49.78300 1.000 29.64000  ? 275 LEU   B HB2    1 
ATOM   8584 H HB3    . LEU   B 1 309 ? 1.87900   26.95900  -49.02600 1.000 29.64000  ? 275 LEU   B HB3    1 
ATOM   8585 H HG     . LEU   B 1 309 ? 3.17000   26.54800  -51.01900 1.000 28.65000  ? 275 LEU   B HG     1 
ATOM   8586 H HD11   . LEU   B 1 309 ? 3.36800   28.32800  -52.53800 1.000 23.59000  ? 275 LEU   B HD11   1 
ATOM   8587 H HD12   . LEU   B 1 309 ? 1.86700   27.80800  -52.51300 1.000 23.59000  ? 275 LEU   B HD12   1 
ATOM   8588 H HD13   . LEU   B 1 309 ? 2.25900   29.13700  -51.73700 1.000 23.59000  ? 275 LEU   B HD13   1 
ATOM   8589 H HD21   . LEU   B 1 309 ? 4.82500   28.03800  -50.41400 1.000 25.54000  ? 275 LEU   B HD21   1 
ATOM   8590 H HD22   . LEU   B 1 309 ? 3.76600   28.96100  -49.67100 1.000 25.54000  ? 275 LEU   B HD22   1 
ATOM   8591 H HD23   . LEU   B 1 309 ? 4.12000   27.52800  -49.08500 1.000 25.54000  ? 275 LEU   B HD23   1 
ATOM   8592 N N      . HIS   B 1 310 ? 1.31400   24.12400  -50.20600 1.000 26.96000  ? 276 HIS   B N      1 
ATOM   8593 C CA     . HIS   B 1 310 ? 1.74300   22.82500  -50.71700 1.000 34.39000  ? 276 HIS   B CA     1 
ATOM   8594 C C      . HIS   B 1 310 ? 0.75700   22.31200  -51.76700 1.000 33.83000  ? 276 HIS   B C      1 
ATOM   8595 O O      . HIS   B 1 310 ? 1.15600   21.77700  -52.80900 1.000 34.88000  ? 276 HIS   B O      1 
ATOM   8596 C CB     . HIS   B 1 310 ? 1.85700   21.85100  -49.54200 1.000 31.41000  ? 276 HIS   B CB     1 
ATOM   8597 C CG     . HIS   B 1 310 ? 2.53600   20.56300  -49.87700 1.000 41.55000  ? 276 HIS   B CG     1 
ATOM   8598 N ND1    . HIS   B 1 310 ? 1.92200   19.56900  -50.61100 1.000 41.16000  ? 276 HIS   B ND1    1 
ATOM   8599 C CD2    . HIS   B 1 310 ? 3.76800   20.09800  -49.56300 1.000 47.62000  ? 276 HIS   B CD2    1 
ATOM   8600 C CE1    . HIS   B 1 310 ? 2.75700   18.55500  -50.75300 1.000 48.84000  ? 276 HIS   B CE1    1 
ATOM   8601 N NE2    . HIS   B 1 310 ? 3.87900   18.84600  -50.11700 1.000 52.39000  ? 276 HIS   B NE2    1 
ATOM   8602 H H      . HIS   B 1 310 ? 1.23800   24.16500  -49.35000 1.000 26.96000  ? 276 HIS   B H      1 
ATOM   8603 H HA     . HIS   B 1 310 ? 2.61600   22.91200  -51.13100 1.000 34.39000  ? 276 HIS   B HA     1 
ATOM   8604 H HB2    . HIS   B 1 310 ? 2.36400   22.27700  -48.83300 1.000 31.41000  ? 276 HIS   B HB2    1 
ATOM   8605 H HB3    . HIS   B 1 310 ? 0.96500   21.64000  -49.22500 1.000 31.41000  ? 276 HIS   B HB3    1 
ATOM   8606 H HD2    . HIS   B 1 310 ? 4.41700   20.54300  -49.06800 1.000 47.62000  ? 276 HIS   B HD2    1 
ATOM   8607 H HE1    . HIS   B 1 310 ? 2.57900   17.76300  -51.20700 1.000 48.84000  ? 276 HIS   B HE1    1 
ATOM   8608 H HE2    . HIS   B 1 310 ? 4.57100   18.33700  -50.06700 1.000 52.39000  ? 276 HIS   B HE2    1 
ATOM   8609 N N      . GLU   B 1 311 ? -0.53600  22.53500  -51.54000 1.000 27.87000  ? 277 GLU   B N      1 
ATOM   8610 C CA     . GLU   B 1 311 ? -1.56000  21.97700  -52.41900 1.000 31.20000  ? 277 GLU   B CA     1 
ATOM   8611 C C      . GLU   B 1 311 ? -1.81100  22.84700  -53.64100 1.000 38.56000  ? 277 GLU   B C      1 
ATOM   8612 O O      . GLU   B 1 311 ? -2.02500  22.33300  -54.74100 1.000 31.93000  ? 277 GLU   B O      1 
ATOM   8613 C CB     . GLU   B 1 311 ? -2.83800  21.77100  -51.61700 1.000 30.79000  ? 277 GLU   B CB     1 
ATOM   8614 C CG     . GLU   B 1 311 ? -2.58000  20.81200  -50.48500 1.000 31.56000  ? 277 GLU   B CG     1 
ATOM   8615 C CD     . GLU   B 1 311 ? -3.72200  20.69000  -49.49400 1.000 45.39000  ? 277 GLU   B CD     1 
ATOM   8616 O OE1    . GLU   B 1 311 ? -4.54100  21.63200  -49.38100 1.000 41.87000  ? 277 GLU   B OE1    1 
ATOM   8617 O OE2    . GLU   B 1 311 ? -3.77800  19.64500  -48.81000 1.000 46.81000  ? 277 GLU   B OE2    1 
ATOM   8618 H H      . GLU   B 1 311 ? -0.84500  23.00300  -50.88800 1.000 27.87000  ? 277 GLU   B H      1 
ATOM   8619 H HA     . GLU   B 1 311 ? -1.26300  21.10800  -52.73100 1.000 31.20000  ? 277 GLU   B HA     1 
ATOM   8620 H HB2    . GLU   B 1 311 ? -3.12900  22.61800  -51.24500 1.000 30.79000  ? 277 GLU   B HB2    1 
ATOM   8621 H HB3    . GLU   B 1 311 ? -3.52500  21.39600  -52.19000 1.000 30.79000  ? 277 GLU   B HB3    1 
ATOM   8622 H HG2    . GLU   B 1 311 ? -2.42000  19.93100  -50.85700 1.000 31.56000  ? 277 GLU   B HG2    1 
ATOM   8623 H HG3    . GLU   B 1 311 ? -1.79900  21.10400  -49.99000 1.000 31.56000  ? 277 GLU   B HG3    1 
ATOM   8624 N N      . GLU   B 1 312 ? -1.81200  24.16800  -53.48000 1.000 29.61000  ? 278 GLU   B N      1 
ATOM   8625 C CA     . GLU   B 1 312 ? -2.25300  25.04800  -54.55500 1.000 30.48000  ? 278 GLU   B CA     1 
ATOM   8626 C C      . GLU   B 1 312 ? -1.11100  25.64200  -55.36000 1.000 33.13000  ? 278 GLU   B C      1 
ATOM   8627 O O      . GLU   B 1 312 ? -1.33300  26.05300  -56.50200 1.000 34.95000  ? 278 GLU   B O      1 
ATOM   8628 C CB     . GLU   B 1 312 ? -3.11500  26.17600  -53.95800 1.000 29.44000  ? 278 GLU   B CB     1 
ATOM   8629 C CG     . GLU   B 1 312 ? -3.78000  27.15400  -54.92500 1.000 34.80000  ? 278 GLU   B CG     1 
ATOM   8630 C CD     . GLU   B 1 312 ? -4.84100  28.00600  -54.21000 1.000 36.82000  ? 278 GLU   B CD     1 
ATOM   8631 O OE1    . GLU   B 1 312 ? -5.32600  27.55700  -53.14000 1.000 35.08000  ? 278 GLU   B OE1    1 
ATOM   8632 O OE2    . GLU   B 1 312 ? -5.17300  29.11800  -54.70000 1.000 34.21000  ? 278 GLU   B OE2    1 
ATOM   8633 H H      . GLU   B 1 312 ? -1.56400  24.57600  -52.76400 1.000 29.61000  ? 278 GLU   B H      1 
ATOM   8634 H HA     . GLU   B 1 312 ? -2.81200  24.54400  -55.16600 1.000 30.48000  ? 278 GLU   B HA     1 
ATOM   8635 H HB2    . GLU   B 1 312 ? -3.82200  25.76100  -53.44000 1.000 29.44000  ? 278 GLU   B HB2    1 
ATOM   8636 H HB3    . GLU   B 1 312 ? -2.55300  26.70100  -53.36600 1.000 29.44000  ? 278 GLU   B HB3    1 
ATOM   8637 H HG2    . GLU   B 1 312 ? -3.10800  27.74900  -55.29300 1.000 34.80000  ? 278 GLU   B HG2    1 
ATOM   8638 H HG3    . GLU   B 1 312 ? -4.21500  26.65700  -55.63500 1.000 34.80000  ? 278 GLU   B HG3    1 
ATOM   8639 N N      . GLY   B 1 313 ? 0.10100   25.69100  -54.80500 1.000 32.61000  ? 279 GLY   B N      1 
ATOM   8640 C CA     . GLY   B 1 313 ? 1.21100   26.35100  -55.46800 1.000 26.79000  ? 279 GLY   B CA     1 
ATOM   8641 C C      . GLY   B 1 313 ? 1.15600   27.86000  -55.28400 1.000 29.78000  ? 279 GLY   B C      1 
ATOM   8642 O O      . GLY   B 1 313 ? 0.26500   28.41800  -54.65200 1.000 27.84000  ? 279 GLY   B O      1 
ATOM   8643 H H      . GLY   B 1 313 ? 0.30100   25.34700  -54.04300 1.000 32.61000  ? 279 GLY   B H      1 
ATOM   8644 H HA2    . GLY   B 1 313 ? 2.04900   26.02500  -55.10400 1.000 26.79000  ? 279 GLY   B HA2    1 
ATOM   8645 H HA3    . GLY   B 1 313 ? 1.18800   26.15300  -56.41700 1.000 26.79000  ? 279 GLY   B HA3    1 
ATOM   8646 N N      . ALA   B 1 314 ? 2.14100   28.53100  -55.87300 1.000 27.71000  ? 280 ALA   B N      1 
ATOM   8647 C CA     . ALA   B 1 314 ? 2.42900   29.92000  -55.50600 1.000 31.54000  ? 280 ALA   B CA     1 
ATOM   8648 C C      . ALA   B 1 314 ? 1.38000   30.90600  -56.00200 1.000 34.35000  ? 280 ALA   B C      1 
ATOM   8649 O O      . ALA   B 1 314 ? 1.36500   32.04300  -55.52800 1.000 29.05000  ? 280 ALA   B O      1 
ATOM   8650 C CB     . ALA   B 1 314 ? 3.80200   30.34300  -56.03400 1.000 40.18000  ? 280 ALA   B CB     1 
ATOM   8651 H H      . ALA   B 1 314 ? 2.65500   28.21100  -56.48400 1.000 27.71000  ? 280 ALA   B H      1 
ATOM   8652 H HA     . ALA   B 1 314 ? 2.45500   29.98300  -54.53800 1.000 31.54000  ? 280 ALA   B HA     1 
ATOM   8653 H HB1    . ALA   B 1 314 ? 3.91300   31.29500  -55.88800 1.000 40.18000  ? 280 ALA   B HB1    1 
ATOM   8654 H HB2    . ALA   B 1 314 ? 4.48600   29.85500  -55.55300 1.000 40.18000  ? 280 ALA   B HB2    1 
ATOM   8655 H HB3    . ALA   B 1 314 ? 3.85100   30.14700  -56.98300 1.000 40.18000  ? 280 ALA   B HB3    1 
ATOM   8656 N N      . ALA   B 1 315 ? 0.51900   30.52300  -56.95000 1.000 30.27000  ? 281 ALA   B N      1 
ATOM   8657 C CA     . ALA   B 1 315 ? -0.59200  31.40600  -57.29600 1.000 34.46000  ? 281 ALA   B CA     1 
ATOM   8658 C C      . ALA   B 1 315 ? -1.51800  31.66100  -56.11400 1.000 32.58000  ? 281 ALA   B C      1 
ATOM   8659 O O      . ALA   B 1 315 ? -2.32900  32.59700  -56.16400 1.000 34.02000  ? 281 ALA   B O      1 
ATOM   8660 C CB     . ALA   B 1 315 ? -1.40000  30.82400  -58.45900 1.000 39.51000  ? 281 ALA   B CB     1 
ATOM   8661 H H      . ALA   B 1 315 ? 0.55400   29.78600  -57.39100 1.000 30.27000  ? 281 ALA   B H      1 
ATOM   8662 H HA     . ALA   B 1 315 ? -0.23400  32.26100  -57.58200 1.000 34.46000  ? 281 ALA   B HA     1 
ATOM   8663 H HB1    . ALA   B 1 315 ? -2.13000  31.42700  -58.66900 1.000 39.51000  ? 281 ALA   B HB1    1 
ATOM   8664 H HB2    . ALA   B 1 315 ? -0.81900  30.72700  -59.22900 1.000 39.51000  ? 281 ALA   B HB2    1 
ATOM   8665 H HB3    . ALA   B 1 315 ? -1.75100  29.95800  -58.19700 1.000 39.51000  ? 281 ALA   B HB3    1 
ATOM   8666 N N      . ILE   B 1 316 ? -1.42300  30.86000  -55.04800 1.000 28.58000  ? 282 ILE   B N      1 
ATOM   8667 C CA     . ILE   B 1 316 ? -2.29900  31.08900  -53.90600 1.000 28.74000  ? 282 ILE   B CA     1 
ATOM   8668 C C      . ILE   B 1 316 ? -2.15400  32.51800  -53.39400 1.000 26.10000  ? 282 ILE   B C      1 
ATOM   8669 O O      . ILE   B 1 316 ? -3.10900  33.08700  -52.84600 1.000 28.98000  ? 282 ILE   B O      1 
ATOM   8670 C CB     . ILE   B 1 316 ? -2.02600  30.06000  -52.78500 1.000 27.47000  ? 282 ILE   B CB     1 
ATOM   8671 C CG1    . ILE   B 1 316 ? -3.11400  30.14300  -51.71500 1.000 26.01000  ? 282 ILE   B CG1    1 
ATOM   8672 C CG2    . ILE   B 1 316 ? -0.62500  30.26500  -52.15400 1.000 26.47000  ? 282 ILE   B CG2    1 
ATOM   8673 C CD1    . ILE   B 1 316 ? -3.07300  28.99000  -50.67100 1.000 27.87000  ? 282 ILE   B CD1    1 
ATOM   8674 H H      . ILE   B 1 316 ? -0.88000  30.19900  -54.96500 1.000 28.58000  ? 282 ILE   B H      1 
ATOM   8675 H HA     . ILE   B 1 316 ? -3.21800  30.97300  -54.19300 1.000 28.74000  ? 282 ILE   B HA     1 
ATOM   8676 H HB     . ILE   B 1 316 ? -2.05400  29.17300  -53.17600 1.000 27.47000  ? 282 ILE   B HB     1 
ATOM   8677 H HG12   . ILE   B 1 316 ? -3.01400  30.97900  -51.23400 1.000 26.01000  ? 282 ILE   B HG12   1 
ATOM   8678 H HG13   . ILE   B 1 316 ? -3.98100  30.11700  -52.14900 1.000 26.01000  ? 282 ILE   B HG13   1 
ATOM   8679 H HG21   . ILE   B 1 316 ? -0.42500  29.51100  -51.57800 1.000 26.47000  ? 282 ILE   B HG21   1 
ATOM   8680 H HG22   . ILE   B 1 316 ? 0.03400   30.32300  -52.86300 1.000 26.47000  ? 282 ILE   B HG22   1 
ATOM   8681 H HG23   . ILE   B 1 316 ? -0.62700  31.08500  -51.63700 1.000 26.47000  ? 282 ILE   B HG23   1 
ATOM   8682 H HD11   . ILE   B 1 316 ? -3.81500  29.09600  -50.05500 1.000 27.87000  ? 282 ILE   B HD11   1 
ATOM   8683 H HD12   . ILE   B 1 316 ? -3.14700  28.14200  -51.13500 1.000 27.87000  ? 282 ILE   B HD12   1 
ATOM   8684 H HD13   . ILE   B 1 316 ? -2.23300  29.03100  -50.18800 1.000 27.87000  ? 282 ILE   B HD13   1 
ATOM   8685 N N      . PHE   B 1 317 ? -0.96500  33.12500  -53.54400 1.000 27.40000  ? 283 PHE   B N      1 
ATOM   8686 C CA     . PHE   B 1 317 ? -0.76400  34.44300  -52.93800 1.000 28.74000  ? 283 PHE   B CA     1 
ATOM   8687 C C      . PHE   B 1 317 ? -1.56300  35.52300  -53.65300 1.000 32.53000  ? 283 PHE   B C      1 
ATOM   8688 O O      . PHE   B 1 317 ? -1.98900  36.49400  -53.01500 1.000 30.14000  ? 283 PHE   B O      1 
ATOM   8689 C CB     . PHE   B 1 317 ? 0.73900   34.78700  -52.87800 1.000 27.52000  ? 283 PHE   B CB     1 
ATOM   8690 C CG     . PHE   B 1 317 ? 1.49800   33.87100  -51.95700 1.000 28.29000  ? 283 PHE   B CG     1 
ATOM   8691 C CD1    . PHE   B 1 317 ? 1.26100   33.89200  -50.58800 1.000 29.16000  ? 283 PHE   B CD1    1 
ATOM   8692 C CD2    . PHE   B 1 317 ? 2.40100   32.94300  -52.46300 1.000 27.34000  ? 283 PHE   B CD2    1 
ATOM   8693 C CE1    . PHE   B 1 317 ? 1.92800   33.00100  -49.71600 1.000 28.82000  ? 283 PHE   B CE1    1 
ATOM   8694 C CE2    . PHE   B 1 317 ? 3.07200   32.06000  -51.61900 1.000 24.81000  ? 283 PHE   B CE2    1 
ATOM   8695 C CZ     . PHE   B 1 317 ? 2.83700   32.07900  -50.24500 1.000 28.10000  ? 283 PHE   B CZ     1 
ATOM   8696 H H      . PHE   B 1 317 ? -0.29000  32.80900  -53.97200 1.000 27.40000  ? 283 PHE   B H      1 
ATOM   8697 H HA     . PHE   B 1 317 ? -1.08800  34.40800  -52.02400 1.000 28.74000  ? 283 PHE   B HA     1 
ATOM   8698 H HB2    . PHE   B 1 317 ? 1.11900   34.70400  -53.76600 1.000 27.52000  ? 283 PHE   B HB2    1 
ATOM   8699 H HB3    . PHE   B 1 317 ? 0.84400   35.69500  -52.55400 1.000 27.52000  ? 283 PHE   B HB3    1 
ATOM   8700 H HD1    . PHE   B 1 317 ? 0.64600   34.49700  -50.24000 1.000 29.16000  ? 283 PHE   B HD1    1 
ATOM   8701 H HD2    . PHE   B 1 317 ? 2.55900   32.91000  -53.37900 1.000 27.34000  ? 283 PHE   B HD2    1 
ATOM   8702 H HE1    . PHE   B 1 317 ? 1.76800   33.03100  -48.80000 1.000 28.82000  ? 283 PHE   B HE1    1 
ATOM   8703 H HE2    . PHE   B 1 317 ? 3.67900   31.45200  -51.97500 1.000 24.81000  ? 283 PHE   B HE2    1 
ATOM   8704 H HZ     . PHE   B 1 317 ? 3.29700   31.49800  -49.68300 1.000 28.10000  ? 283 PHE   B HZ     1 
ATOM   8705 N N      . GLU   B 1 318 ? -1.81800  35.35200  -54.95300 1.000 31.02000  ? 284 GLU   B N      1 
ATOM   8706 C CA     . GLU   B 1 318 ? -2.70600  36.27500  -55.65500 1.000 29.05000  ? 284 GLU   B CA     1 
ATOM   8707 C C      . GLU   B 1 318 ? -4.10800  36.19300  -55.09300 1.000 29.25000  ? 284 GLU   B C      1 
ATOM   8708 O O      . GLU   B 1 318 ? -4.78900  37.21300  -54.93100 1.000 31.02000  ? 284 GLU   B O      1 
ATOM   8709 C CB     . GLU   B 1 318 ? -2.71100  35.96000  -57.15000 1.000 33.91000  ? 284 GLU   B CB     1 
ATOM   8710 C CG     . GLU   B 1 318 ? -1.30600  36.06800  -57.73400 1.000 54.78000  ? 284 GLU   B CG     1 
ATOM   8711 C CD     . GLU   B 1 318 ? -1.16000  35.39500  -59.08700 1.000 75.04000  ? 284 GLU   B CD     1 
ATOM   8712 O OE1    . GLU   B 1 318 ? -2.15400  35.33100  -59.83800 1.000 63.48000  ? 284 GLU   B OE1    1 
ATOM   8713 O OE2    . GLU   B 1 318 ? -0.02500  34.93200  -59.39000 1.000 74.15000  ? 284 GLU   B OE2    1 
ATOM   8714 H H      . GLU   B 1 318 ? -1.49700  34.72000  -55.44000 1.000 31.02000  ? 284 GLU   B H      1 
ATOM   8715 H HA     . GLU   B 1 318 ? -2.38300  37.18200  -55.53600 1.000 29.05000  ? 284 GLU   B HA     1 
ATOM   8716 H HB2    . GLU   B 1 318 ? -3.03000  35.05400  -57.28700 1.000 33.91000  ? 284 GLU   B HB2    1 
ATOM   8717 H HB3    . GLU   B 1 318 ? -3.28300  36.59300  -57.61100 1.000 33.91000  ? 284 GLU   B HB3    1 
ATOM   8718 H HG2    . GLU   B 1 318 ? -1.08500  37.00600  -57.84500 1.000 54.78000  ? 284 GLU   B HG2    1 
ATOM   8719 H HG3    . GLU   B 1 318 ? -0.67300  35.65100  -57.13000 1.000 54.78000  ? 284 GLU   B HG3    1 
ATOM   8720 N N      . ARG   B 1 319 ? -4.54300  34.98600  -54.75500 1.000 29.62000  ? 285 ARG   B N      1 
ATOM   8721 C CA     . ARG   B 1 319 ? -5.89200  34.80700  -54.24500 1.000 29.47000  ? 285 ARG   B CA     1 
ATOM   8722 C C      . ARG   B 1 319 ? -6.01200  35.32000  -52.81200 1.000 32.05000  ? 285 ARG   B C      1 
ATOM   8723 O O      . ARG   B 1 319 ? -7.00000  35.96900  -52.46200 1.000 29.62000  ? 285 ARG   B O      1 
ATOM   8724 C CB     . ARG   B 1 319 ? -6.26800  33.32500  -54.33800 1.000 26.62000  ? 285 ARG   B CB     1 
ATOM   8725 C CG     . ARG   B 1 319 ? -7.63400  32.99100  -53.79300 1.000 33.88000  ? 285 ARG   B CG     1 
ATOM   8726 C CD     . ARG   B 1 319 ? -7.96100  31.50600  -53.99700 1.000 33.64000  ? 285 ARG   B CD     1 
ATOM   8727 N NE     . ARG   B 1 319 ? -7.15500  30.58200  -53.19700 1.000 31.03000  ? 285 ARG   B NE     1 
ATOM   8728 C CZ     . ARG   B 1 319 ? -7.36200  30.30100  -51.91500 1.000 32.15000  ? 285 ARG   B CZ     1 
ATOM   8729 N NH1    . ARG   B 1 319 ? -8.27200  30.95300  -51.19200 1.000 30.52000  ? 285 ARG   B NH1    1 
ATOM   8730 N NH2    . ARG   B 1 319 ? -6.64300  29.33800  -51.34000 1.000 30.75000  ? 285 ARG   B NH2    1 
ATOM   8731 H H      . ARG   B 1 319 ? -4.08200  34.26200  -54.81100 1.000 29.62000  ? 285 ARG   B H      1 
ATOM   8732 H HA     . ARG   B 1 319 ? -6.50900  35.31400  -54.79200 1.000 29.47000  ? 285 ARG   B HA     1 
ATOM   8733 H HB2    . ARG   B 1 319 ? -6.25000  33.05800  -55.27000 1.000 26.62000  ? 285 ARG   B HB2    1 
ATOM   8734 H HB3    . ARG   B 1 319 ? -5.61700  32.80800  -53.83800 1.000 26.62000  ? 285 ARG   B HB3    1 
ATOM   8735 H HG2    . ARG   B 1 319 ? -7.65800  33.17800  -52.84200 1.000 33.88000  ? 285 ARG   B HG2    1 
ATOM   8736 H HG3    . ARG   B 1 319 ? -8.30300  33.51800  -54.25700 1.000 33.88000  ? 285 ARG   B HG3    1 
ATOM   8737 H HD2    . ARG   B 1 319 ? -8.89100  31.36000  -53.76500 1.000 33.64000  ? 285 ARG   B HD2    1 
ATOM   8738 H HD3    . ARG   B 1 319 ? -7.82000  31.28400  -54.93100 1.000 33.64000  ? 285 ARG   B HD3    1 
ATOM   8739 H HE     . ARG   B 1 319 ? -6.49600  30.19100  -53.58700 1.000 31.03000  ? 285 ARG   B HE     1 
ATOM   8740 H HH11   . ARG   B 1 319 ? -8.74600  31.57300  -51.55300 1.000 30.52000  ? 285 ARG   B HH11   1 
ATOM   8741 H HH12   . ARG   B 1 319 ? -8.38500  30.75300  -50.36300 1.000 30.52000  ? 285 ARG   B HH12   1 
ATOM   8742 H HH21   . ARG   B 1 319 ? -6.05000  28.91300  -51.79600 1.000 30.75000  ? 285 ARG   B HH21   1 
ATOM   8743 H HH22   . ARG   B 1 319 ? -6.76100  29.15100  -50.50900 1.000 30.75000  ? 285 ARG   B HH22   1 
ATOM   8744 N N      . LEU   B 1 320 ? -5.01300  35.04500  -51.97300 1.000 30.53000  ? 286 LEU   B N      1 
ATOM   8745 C CA     . LEU   B 1 320 ? -5.06000  35.47500  -50.57800 1.000 32.51000  ? 286 LEU   B CA     1 
ATOM   8746 C C      . LEU   B 1 320 ? -5.02700  36.98900  -50.44900 1.000 26.78000  ? 286 LEU   B C      1 
ATOM   8747 O O      . LEU   B 1 320 ? -5.73500  37.55000  -49.60200 1.000 29.10000  ? 286 LEU   B O      1 
ATOM   8748 C CB     . LEU   B 1 320 ? -3.90200  34.86000  -49.79800 1.000 27.86000  ? 286 LEU   B CB     1 
ATOM   8749 C CG     . LEU   B 1 320 ? -3.99900  33.33000  -49.66400 1.000 28.35000  ? 286 LEU   B CG     1 
ATOM   8750 C CD1    . LEU   B 1 320 ? -2.78000  32.83500  -48.95000 1.000 27.86000  ? 286 LEU   B CD1    1 
ATOM   8751 C CD2    . LEU   B 1 320 ? -5.25400  32.97800  -48.86700 1.000 31.86000  ? 286 LEU   B CD2    1 
ATOM   8752 H H      . LEU   B 1 320 ? -4.30100  34.61300  -52.18600 1.000 30.53000  ? 286 LEU   B H      1 
ATOM   8753 H HA     . LEU   B 1 320 ? -5.89100  35.16900  -50.18500 1.000 32.51000  ? 286 LEU   B HA     1 
ATOM   8754 H HB2    . LEU   B 1 320 ? -3.07100  35.06700  -50.25400 1.000 27.86000  ? 286 LEU   B HB2    1 
ATOM   8755 H HB3    . LEU   B 1 320 ? -3.89000  35.23700  -48.90500 1.000 27.86000  ? 286 LEU   B HB3    1 
ATOM   8756 H HG     . LEU   B 1 320 ? -4.04900  32.91700  -50.54000 1.000 28.35000  ? 286 LEU   B HG     1 
ATOM   8757 H HD11   . LEU   B 1 320 ? -2.83400  31.87000  -48.86500 1.000 27.86000  ? 286 LEU   B HD11   1 
ATOM   8758 H HD12   . LEU   B 1 320 ? -1.99300  33.07900  -49.46300 1.000 27.86000  ? 286 LEU   B HD12   1 
ATOM   8759 H HD13   . LEU   B 1 320 ? -2.74200  33.24300  -48.07100 1.000 27.86000  ? 286 LEU   B HD13   1 
ATOM   8760 H HD21   . LEU   B 1 320 ? -5.18200  32.06200  -48.55500 1.000 31.86000  ? 286 LEU   B HD21   1 
ATOM   8761 H HD22   . LEU   B 1 320 ? -5.32600  33.58000  -48.11000 1.000 31.86000  ? 286 LEU   B HD22   1 
ATOM   8762 H HD23   . LEU   B 1 320 ? -6.03100  33.07200  -49.44000 1.000 31.86000  ? 286 LEU   B HD23   1 
ATOM   8763 N N      . THR   B 1 321 ? -4.19300  37.67200  -51.24300 1.000 27.13000  ? 287 THR   B N      1 
ATOM   8764 C CA     . THR   B 1 321 ? -4.20000  39.13400  -51.14000 1.000 31.71000  ? 287 THR   B CA     1 
ATOM   8765 C C      . THR   B 1 321 ? -5.53000  39.70300  -51.60800 1.000 32.58000  ? 287 THR   B C      1 
ATOM   8766 O O      . THR   B 1 321 ? -6.08000  40.60800  -50.96400 1.000 30.51000  ? 287 THR   B O      1 
ATOM   8767 C CB     . THR   B 1 321 ? -3.04900  39.77700  -51.92700 1.000 31.47000  ? 287 THR   B CB     1 
ATOM   8768 O OG1    . THR   B 1 321 ? -3.10000  39.38900  -53.30400 1.000 37.50000  ? 287 THR   B OG1    1 
ATOM   8769 C CG2    . THR   B 1 321 ? -1.70500  39.39500  -51.33900 1.000 28.84000  ? 287 THR   B CG2    1 
ATOM   8770 H H      . THR   B 1 321 ? -3.64600  37.33700  -51.81500 1.000 27.13000  ? 287 THR   B H      1 
ATOM   8771 H HA     . THR   B 1 321 ? -4.08900  39.37800  -50.20800 1.000 31.71000  ? 287 THR   B HA     1 
ATOM   8772 H HB     . THR   B 1 321 ? -3.13300  40.74200  -51.87100 1.000 31.47000  ? 287 THR   B HB     1 
ATOM   8773 H HG1    . THR   B 1 321 ? -3.03500  38.55400  -53.37000 1.000 37.50000  ? 287 THR   B HG1    1 
ATOM   8774 H HG21   . THR   B 1 321 ? -0.99100  39.81100  -51.84700 1.000 28.84000  ? 287 THR   B HG21   1 
ATOM   8775 H HG22   . THR   B 1 321 ? -1.65000  39.69200  -50.41700 1.000 28.84000  ? 287 THR   B HG22   1 
ATOM   8776 H HG23   . THR   B 1 321 ? -1.59300  38.43200  -51.36700 1.000 28.84000  ? 287 THR   B HG23   1 
ATOM   8777 N N      . ALA   B 1 322 ? -6.07300  39.17400  -52.71500 1.000 30.10000  ? 288 ALA   B N      1 
ATOM   8778 C CA     . ALA   B 1 322 ? -7.36400  39.65800  -53.19100 1.000 33.58000  ? 288 ALA   B CA     1 
ATOM   8779 C C      . ALA   B 1 322 ? -8.45000  39.42700  -52.15200 1.000 35.51000  ? 288 ALA   B C      1 
ATOM   8780 O O      . ALA   B 1 322 ? -9.28900  40.30300  -51.90900 1.000 33.94000  ? 288 ALA   B O      1 
ATOM   8781 C CB     . ALA   B 1 322 ? -7.73200  38.97500  -54.51400 1.000 31.48000  ? 288 ALA   B CB     1 
ATOM   8782 H H      . ALA   B 1 322 ? -5.72000  38.55100  -53.19200 1.000 30.10000  ? 288 ALA   B H      1 
ATOM   8783 H HA     . ALA   B 1 322 ? -7.30300  40.61200  -53.35300 1.000 33.58000  ? 288 ALA   B HA     1 
ATOM   8784 H HB1    . ALA   B 1 322 ? -8.59200  39.31000  -54.81300 1.000 31.48000  ? 288 ALA   B HB1    1 
ATOM   8785 H HB2    . ALA   B 1 322 ? -7.05000  39.17700  -55.17400 1.000 31.48000  ? 288 ALA   B HB2    1 
ATOM   8786 H HB3    . ALA   B 1 322 ? -7.78100  38.01700  -54.37100 1.000 31.48000  ? 288 ALA   B HB3    1 
ATOM   8787 N N      . GLU   B 1 323 ? -8.45000  38.24900  -51.52800 1.000 29.42000  ? 289 GLU   B N      1 
ATOM   8788 C CA     . GLU   B 1 323 ? -9.47600  37.93500  -50.54100 1.000 30.76000  ? 289 GLU   B CA     1 
ATOM   8789 C C      . GLU   B 1 323 ? -9.34100  38.79400  -49.28600 1.000 34.51000  ? 289 GLU   B C      1 
ATOM   8790 O O      . GLU   B 1 323 ? -10.34700 39.24400  -48.71800 1.000 33.80000  ? 289 GLU   B O      1 
ATOM   8791 C CB     . GLU   B 1 323 ? -9.40800  36.44000  -50.18400 1.000 31.84000  ? 289 GLU   B CB     1 
ATOM   8792 C CG     . GLU   B 1 323 ? -9.86100  35.54800  -51.34500 1.000 33.22000  ? 289 GLU   B CG     1 
ATOM   8793 C CD     . GLU   B 1 323 ? -9.82100  34.05700  -51.03300 1.000 40.09000  ? 289 GLU   B CD     1 
ATOM   8794 O OE1    . GLU   B 1 323 ? -9.33400  33.68400  -49.93800 1.000 36.29000  ? 289 GLU   B OE1    1 
ATOM   8795 O OE2    . GLU   B 1 323 ? -10.28000 33.25800  -51.88900 1.000 35.40000  ? 289 GLU   B OE2    1 
ATOM   8796 H H      . GLU   B 1 323 ? -7.87400  37.62400  -51.65700 1.000 29.42000  ? 289 GLU   B H      1 
ATOM   8797 H HA     . GLU   B 1 323 ? -10.34800 38.10900  -50.92900 1.000 30.76000  ? 289 GLU   B HA     1 
ATOM   8798 H HB2    . GLU   B 1 323 ? -8.49300  36.20700  -49.96400 1.000 31.84000  ? 289 GLU   B HB2    1 
ATOM   8799 H HB3    . GLU   B 1 323 ? -9.98800  36.26700  -49.42600 1.000 31.84000  ? 289 GLU   B HB3    1 
ATOM   8800 H HG2    . GLU   B 1 323 ? -10.77700 35.77500  -51.57000 1.000 33.22000  ? 289 GLU   B HG2    1 
ATOM   8801 H HG3    . GLU   B 1 323 ? -9.29000  35.70900  -52.11100 1.000 33.22000  ? 289 GLU   B HG3    1 
ATOM   8802 N N      . LEU   B 1 324 ? -8.11500  39.01000  -48.81300 1.000 28.42000  ? 290 LEU   B N      1 
ATOM   8803 C CA     . LEU   B 1 324 ? -7.94600  39.85200  -47.62300 1.000 28.01000  ? 290 LEU   B CA     1 
ATOM   8804 C C      . LEU   B 1 324 ? -8.35000  41.29700  -47.90900 1.000 34.33000  ? 290 LEU   B C      1 
ATOM   8805 O O      . LEU   B 1 324 ? -8.96000  41.96700  -47.05700 1.000 30.71000  ? 290 LEU   B O      1 
ATOM   8806 C CB     . LEU   B 1 324 ? -6.49600  39.78300  -47.14900 1.000 28.15000  ? 290 LEU   B CB     1 
ATOM   8807 C CG     . LEU   B 1 324 ? -6.10800  40.65600  -45.97100 1.000 34.08000  ? 290 LEU   B CG     1 
ATOM   8808 C CD1    . LEU   B 1 324 ? -7.05000  40.40000  -44.80000 1.000 30.66000  ? 290 LEU   B CD1    1 
ATOM   8809 C CD2    . LEU   B 1 324 ? -4.69800  40.31100  -45.61200 1.000 29.88000  ? 290 LEU   B CD2    1 
ATOM   8810 H H      . LEU   B 1 324 ? -7.38700  38.69500  -49.14600 1.000 28.42000  ? 290 LEU   B H      1 
ATOM   8811 H HA     . LEU   B 1 324 ? -8.51500  39.51400  -46.91400 1.000 28.01000  ? 290 LEU   B HA     1 
ATOM   8812 H HB2    . LEU   B 1 324 ? -6.30500  38.86500  -46.89900 1.000 28.15000  ? 290 LEU   B HB2    1 
ATOM   8813 H HB3    . LEU   B 1 324 ? -5.92500  40.03600  -47.89100 1.000 28.15000  ? 290 LEU   B HB3    1 
ATOM   8814 H HG     . LEU   B 1 324 ? -6.15300  41.59300  -46.21900 1.000 34.08000  ? 290 LEU   B HG     1 
ATOM   8815 H HD11   . LEU   B 1 324 ? -6.70700  40.85500  -44.01500 1.000 30.66000  ? 290 LEU   B HD11   1 
ATOM   8816 H HD12   . LEU   B 1 324 ? -7.93100  40.74100  -45.02100 1.000 30.66000  ? 290 LEU   B HD12   1 
ATOM   8817 H HD13   . LEU   B 1 324 ? -7.09500  39.44500  -44.63500 1.000 30.66000  ? 290 LEU   B HD13   1 
ATOM   8818 H HD21   . LEU   B 1 324 ? -4.41300  40.87600  -44.87700 1.000 29.88000  ? 290 LEU   B HD21   1 
ATOM   8819 H HD22   . LEU   B 1 324 ? -4.65800  39.37900  -45.34700 1.000 29.88000  ? 290 LEU   B HD22   1 
ATOM   8820 H HD23   . LEU   B 1 324 ? -4.13000  40.46100  -46.38400 1.000 29.88000  ? 290 LEU   B HD23   1 
ATOM   8821 N N      . LEU   B 1 325 ? -8.02400  41.79100  -49.10600 1.000 32.35000  ? 291 LEU   B N      1 
ATOM   8822 C CA     . LEU   B 1 325 ? -8.42800  43.14800  -49.47600 1.000 31.70000  ? 291 LEU   B CA     1 
ATOM   8823 C C      . LEU   B 1 325 ? -9.94700  43.27400  -49.53200 1.000 32.83000  ? 291 LEU   B C      1 
ATOM   8824 O O      . LEU   B 1 325 ? -10.50800 44.31600  -49.15500 1.000 35.36000  ? 291 LEU   B O      1 
ATOM   8825 C CB     . LEU   B 1 325 ? -7.79000  43.53900  -50.80900 1.000 32.72000  ? 291 LEU   B CB     1 
ATOM   8826 C CG     . LEU   B 1 325 ? -6.34600  43.97800  -50.63100 1.000 32.00000  ? 291 LEU   B CG     1 
ATOM   8827 C CD1    . LEU   B 1 325 ? -5.61000  44.00100  -51.94300 1.000 35.90000  ? 291 LEU   B CD1    1 
ATOM   8828 C CD2    . LEU   B 1 325 ? -6.32100  45.37000  -49.95500 1.000 35.88000  ? 291 LEU   B CD2    1 
ATOM   8829 H H      . LEU   B 1 325 ? -7.57900  41.37000  -49.71000 1.000 32.35000  ? 291 LEU   B H      1 
ATOM   8830 H HA     . LEU   B 1 325 ? -8.11100  43.76000  -48.79500 1.000 31.70000  ? 291 LEU   B HA     1 
ATOM   8831 H HB2    . LEU   B 1 325 ? -7.80300  42.77400  -51.40500 1.000 32.72000  ? 291 LEU   B HB2    1 
ATOM   8832 H HB3    . LEU   B 1 325 ? -8.28700  44.27500  -51.19800 1.000 32.72000  ? 291 LEU   B HB3    1 
ATOM   8833 H HG     . LEU   B 1 325 ? -5.89500  43.35100  -50.04400 1.000 32.00000  ? 291 LEU   B HG     1 
ATOM   8834 H HD11   . LEU   B 1 325 ? -4.69600  44.28500  -51.78700 1.000 35.90000  ? 291 LEU   B HD11   1 
ATOM   8835 H HD12   . LEU   B 1 325 ? -5.61900  43.11000  -52.32500 1.000 35.90000  ? 291 LEU   B HD12   1 
ATOM   8836 H HD13   . LEU   B 1 325 ? -6.05200  44.62300  -52.54200 1.000 35.90000  ? 291 LEU   B HD13   1 
ATOM   8837 H HD21   . LEU   B 1 325 ? -5.43000  45.74400  -50.04000 1.000 35.88000  ? 291 LEU   B HD21   1 
ATOM   8838 H HD22   . LEU   B 1 325 ? -6.96300  45.94600  -50.39600 1.000 35.88000  ? 291 LEU   B HD22   1 
ATOM   8839 H HD23   . LEU   B 1 325 ? -6.55100  45.27500  -49.01800 1.000 35.88000  ? 291 LEU   B HD23   1 
ATOM   8840 N N      . ASP   B 1 326 ? -10.63100 42.22200  -49.98500 1.000 33.88000  ? 292 ASP   B N      1 
ATOM   8841 C CA     . ASP   B 1 326 ? -12.09500 42.20600  -49.97500 1.000 37.25000  ? 292 ASP   B CA     1 
ATOM   8842 C C      . ASP   B 1 326 ? -12.65500 42.33000  -48.56800 1.000 43.51000  ? 292 ASP   B C      1 
ATOM   8843 O O      . ASP   B 1 326 ? -13.60000 43.09100  -48.33300 1.000 39.68000  ? 292 ASP   B O      1 
ATOM   8844 C CB     . ASP   B 1 326 ? -12.62600 40.92300  -50.60800 1.000 38.97000  ? 292 ASP   B CB     1 
ATOM   8845 C CG     . ASP   B 1 326 ? -12.76700 41.03100  -52.10100 1.000 59.91000  ? 292 ASP   B CG     1 
ATOM   8846 O OD1    . ASP   B 1 326 ? -12.83200 42.17400  -52.59900 1.000 71.54000  ? 292 ASP   B OD1    1 
ATOM   8847 O OD2    . ASP   B 1 326 ? -12.81100 39.97600  -52.77300 1.000 71.14000  ? 292 ASP   B OD2    1 
ATOM   8848 H H      . ASP   B 1 326 ? -10.27200 41.50800  -50.30200 1.000 33.88000  ? 292 ASP   B H      1 
ATOM   8849 H HA     . ASP   B 1 326 ? -12.42100 42.96200  -50.48600 1.000 37.25000  ? 292 ASP   B HA     1 
ATOM   8850 H HB2    . ASP   B 1 326 ? -12.01200 40.19700  -50.41600 1.000 38.97000  ? 292 ASP   B HB2    1 
ATOM   8851 H HB3    . ASP   B 1 326 ? -13.50000 40.72600  -50.23700 1.000 38.97000  ? 292 ASP   B HB3    1 
ATOM   8852 N N      . VAL   B 1 327 ? -12.13700 41.53300  -47.63200 1.000 35.18000  ? 293 VAL   B N      1 
ATOM   8853 C CA     . VAL   B 1 327 ? -12.58300 41.64500  -46.24600 1.000 35.54000  ? 293 VAL   B CA     1 
ATOM   8854 C C      . VAL   B 1 327 ? -12.37800 43.07500  -45.75000 1.000 36.11000  ? 293 VAL   B C      1 
ATOM   8855 O O      . VAL   B 1 327 ? -13.26600 43.67000  -45.13100 1.000 39.39000  ? 293 VAL   B O      1 
ATOM   8856 C CB     . VAL   B 1 327 ? -11.85100 40.62600  -45.34400 1.000 39.93000  ? 293 VAL   B CB     1 
ATOM   8857 C CG1    . VAL   B 1 327 ? -12.32200 40.77700  -43.89500 1.000 45.14000  ? 293 VAL   B CG1    1 
ATOM   8858 C CG2    . VAL   B 1 327 ? -12.06300 39.19000  -45.81900 1.000 38.52000  ? 293 VAL   B CG2    1 
ATOM   8859 H H      . VAL   B 1 327 ? -11.53700 40.93300  -47.77100 1.000 35.18000  ? 293 VAL   B H      1 
ATOM   8860 H HA     . VAL   B 1 327 ? -13.53200 41.44900  -46.20500 1.000 35.54000  ? 293 VAL   B HA     1 
ATOM   8861 H HB     . VAL   B 1 327 ? -10.89900 40.81100  -45.36900 1.000 39.93000  ? 293 VAL   B HB     1 
ATOM   8862 H HG11   . VAL   B 1 327 ? -12.01300 40.01300  -43.38300 1.000 45.14000  ? 293 VAL   B HG11   1 
ATOM   8863 H HG12   . VAL   B 1 327 ? -11.95300 41.59300  -43.52300 1.000 45.14000  ? 293 VAL   B HG12   1 
ATOM   8864 H HG13   . VAL   B 1 327 ? -13.29100 40.81300  -43.88100 1.000 45.14000  ? 293 VAL   B HG13   1 
ATOM   8865 H HG21   . VAL   B 1 327 ? -11.58800 38.58900  -45.22500 1.000 38.52000  ? 293 VAL   B HG21   1 
ATOM   8866 H HG22   . VAL   B 1 327 ? -13.01200 38.99000  -45.80300 1.000 38.52000  ? 293 VAL   B HG22   1 
ATOM   8867 H HG23   . VAL   B 1 327 ? -11.72200 39.10000  -46.72200 1.000 38.52000  ? 293 VAL   B HG23   1 
ATOM   8868 N N      . MET   B 1 328 ? -11.20000 43.64300  -46.01600 1.000 32.59000  ? 294 MET   B N      1 
ATOM   8869 C CA     . MET   B 1 328 ? -10.89800 44.99000  -45.54300 1.000 39.50000  ? 294 MET   B CA     1 
ATOM   8870 C C      . MET   B 1 328 ? -11.83400 46.01900  -46.16500 1.000 43.61000  ? 294 MET   B C      1 
ATOM   8871 O O      . MET   B 1 328 ? -12.28200 46.94500  -45.48300 1.000 39.43000  ? 294 MET   B O      1 
ATOM   8872 C CB     . MET   B 1 328 ? -9.44300  45.32900  -45.83900 1.000 35.32000  ? 294 MET   B CB     1 
ATOM   8873 C CG     . MET   B 1 328 ? -8.46700  44.52000  -44.98000 1.000 30.74000  ? 294 MET   B CG     1 
ATOM   8874 S SD     . MET   B 1 328 ? -6.76700  44.80300  -45.44100 1.000 34.86000  ? 294 MET   B SD     1 
ATOM   8875 C CE     . MET   B 1 328 ? -6.50400  46.58300  -45.01900 1.000 31.72000  ? 294 MET   B CE     1 
ATOM   8876 H H      . MET   B 1 328 ? -10.56600 43.27200  -46.46400 1.000 32.59000  ? 294 MET   B H      1 
ATOM   8877 H HA     . MET   B 1 328 ? -11.01300 45.01100  -44.58000 1.000 39.50000  ? 294 MET   B HA     1 
ATOM   8878 H HB2    . MET   B 1 328 ? -9.25600  45.13500  -46.77100 1.000 35.32000  ? 294 MET   B HB2    1 
ATOM   8879 H HB3    . MET   B 1 328 ? -9.29400  46.27000  -45.65800 1.000 35.32000  ? 294 MET   B HB3    1 
ATOM   8880 H HG2    . MET   B 1 328 ? -8.57400  44.77600  -44.05100 1.000 30.74000  ? 294 MET   B HG2    1 
ATOM   8881 H HG3    . MET   B 1 328 ? -8.65600  43.57500  -45.08900 1.000 30.74000  ? 294 MET   B HG3    1 
ATOM   8882 H HE1    . MET   B 1 328 ? -5.58700  46.82300  -45.22400 1.000 31.72000  ? 294 MET   B HE1    1 
ATOM   8883 H HE2    . MET   B 1 328 ? -7.11400  47.12500  -45.54400 1.000 31.72000  ? 294 MET   B HE2    1 
ATOM   8884 H HE3    . MET   B 1 328 ? -6.67700  46.71200  -44.07300 1.000 31.72000  ? 294 MET   B HE3    1 
ATOM   8885 N N      . ALA   B 1 329 ? -12.14700 45.86200  -47.45500 1.000 41.39000  ? 295 ALA   B N      1 
ATOM   8886 C CA     . ALA   B 1 329 ? -12.99900 46.82800  -48.14800 1.000 46.24000  ? 295 ALA   B CA     1 
ATOM   8887 C C      . ALA   B 1 329 ? -14.41400 46.81200  -47.59200 1.000 45.58000  ? 295 ALA   B C      1 
ATOM   8888 O O      . ALA   B 1 329 ? -15.03800 47.87000  -47.43500 1.000 44.18000  ? 295 ALA   B O      1 
ATOM   8889 C CB     . ALA   B 1 329 ? -13.01600 46.53600  -49.65100 1.000 40.46000  ? 295 ALA   B CB     1 
ATOM   8890 H H      . ALA   B 1 329 ? -11.88000 45.20900  -47.94700 1.000 41.39000  ? 295 ALA   B H      1 
ATOM   8891 H HA     . ALA   B 1 329 ? -12.63600 47.71800  -48.01900 1.000 46.24000  ? 295 ALA   B HA     1 
ATOM   8892 H HB1    . ALA   B 1 329 ? -13.58500 47.18600  -50.09200 1.000 40.46000  ? 295 ALA   B HB1    1 
ATOM   8893 H HB2    . ALA   B 1 329 ? -12.11100 46.60000  -49.99500 1.000 40.46000  ? 295 ALA   B HB2    1 
ATOM   8894 H HB3    . ALA   B 1 329 ? -13.36200 45.64100  -49.79400 1.000 40.46000  ? 295 ALA   B HB3    1 
ATOM   8895 N N      . LYS   B 1 330 ? -14.94200 45.62400  -47.29100 1.000 41.02000  ? 296 LYS   B N      1 
ATOM   8896 C CA     . LYS   B 1 330 ? -16.26900 45.55100  -46.70300 1.000 43.25000  ? 296 LYS   B CA     1 
ATOM   8897 C C      . LYS   B 1 330 ? -16.31600 46.20200  -45.33600 1.000 47.82000  ? 296 LYS   B C      1 
ATOM   8898 O O      . LYS   B 1 330 ? -17.38400 46.64600  -44.91400 1.000 52.47000  ? 296 LYS   B O      1 
ATOM   8899 C CB     . LYS   B 1 330 ? -16.73600 44.10000  -46.61300 1.000 51.05000  ? 296 LYS   B CB     1 
ATOM   8900 C CG     . LYS   B 1 330 ? -16.67100 43.38300  -47.94900 1.000 60.77000  ? 296 LYS   B CG     1 
ATOM   8901 C CD     . LYS   B 1 330 ? -17.75200 42.31900  -48.09500 1.000 70.28000  ? 296 LYS   B CD     1 
ATOM   8902 C CE     . LYS   B 1 330 ? -17.92700 41.91400  -49.56000 1.000 77.42000  ? 296 LYS   B CE     1 
ATOM   8903 N NZ     . LYS   B 1 330 ? -19.27600 41.32700  -49.82200 1.000 89.59000  ? 296 LYS   B NZ     1 
ATOM   8904 H H      . LYS   B 1 330 ? -14.55800 44.86500  -47.41600 1.000 41.02000  ? 296 LYS   B H      1 
ATOM   8905 H HA     . LYS   B 1 330 ? -16.89000 46.02600  -47.27700 1.000 43.25000  ? 296 LYS   B HA     1 
ATOM   8906 H HB2    . LYS   B 1 330 ? -16.16700 43.62300  -45.98900 1.000 51.05000  ? 296 LYS   B HB2    1 
ATOM   8907 H HB3    . LYS   B 1 330 ? -17.65500 44.08300  -46.30400 1.000 51.05000  ? 296 LYS   B HB3    1 
ATOM   8908 H HG2    . LYS   B 1 330 ? -16.77900 44.03000  -48.66300 1.000 60.77000  ? 296 LYS   B HG2    1 
ATOM   8909 H HG3    . LYS   B 1 330 ? -15.81700 42.93800  -48.02700 1.000 60.77000  ? 296 LYS   B HG3    1 
ATOM   8910 H HD2    . LYS   B 1 330 ? -17.49900 41.53200  -47.58800 1.000 70.28000  ? 296 LYS   B HD2    1 
ATOM   8911 H HD3    . LYS   B 1 330 ? -18.59700 42.67000  -47.77400 1.000 70.28000  ? 296 LYS   B HD3    1 
ATOM   8912 H HE2    . LYS   B 1 330 ? -17.82500 42.69700  -50.12400 1.000 77.42000  ? 296 LYS   B HE2    1 
ATOM   8913 H HE3    . LYS   B 1 330 ? -17.25900 41.24900  -49.78800 1.000 77.42000  ? 296 LYS   B HE3    1 
ATOM   8914 H HZ1    . LYS   B 1 330 ? -19.34800 41.10200  -50.68000 1.000 89.59000  ? 296 LYS   B HZ1    1 
ATOM   8915 H HZ2    . LYS   B 1 330 ? -19.39400 40.60100  -49.32100 1.000 89.59000  ? 296 LYS   B HZ2    1 
ATOM   8916 H HZ3    . LYS   B 1 330 ? -19.90900 41.92000  -49.62500 1.000 89.59000  ? 296 LYS   B HZ3    1 
ATOM   8917 N N      . LYS   B 1 331 ? -15.18900 46.29500  -44.64000 1.000 39.70000  ? 297 LYS   B N      1 
ATOM   8918 C CA     . LYS   B 1 331 ? -15.17400 46.87900  -43.30800 1.000 40.28000  ? 297 LYS   B CA     1 
ATOM   8919 C C      . LYS   B 1 331 ? -14.65600 48.31400  -43.27700 1.000 41.96000  ? 297 LYS   B C      1 
ATOM   8920 O O      . LYS   B 1 331 ? -14.61700 48.91500  -42.20400 1.000 43.61000  ? 297 LYS   B O      1 
ATOM   8921 C CB     . LYS   B 1 331 ? -14.33800 46.00800  -42.37300 1.000 36.99000  ? 297 LYS   B CB     1 
ATOM   8922 C CG     . LYS   B 1 331 ? -14.95200 44.63400  -42.14200 1.000 38.74000  ? 297 LYS   B CG     1 
ATOM   8923 C CD     . LYS   B 1 331 ? -13.97400 43.68200  -41.48300 1.000 43.83000  ? 297 LYS   B CD     1 
ATOM   8924 C CE     . LYS   B 1 331 ? -14.64000 42.37700  -41.10600 1.000 37.54000  ? 297 LYS   B CE     1 
ATOM   8925 N NZ     . LYS   B 1 331 ? -15.49200 42.55500  -39.90100 1.000 38.00000  ? 297 LYS   B NZ     1 
ATOM   8926 H H      . LYS   B 1 331 ? -14.42000 46.02700  -44.91700 1.000 39.70000  ? 297 LYS   B H      1 
ATOM   8927 H HA     . LYS   B 1 331 ? -16.07900 46.88900  -42.96100 1.000 40.28000  ? 297 LYS   B HA     1 
ATOM   8928 H HB2    . LYS   B 1 331 ? -13.45800 45.88200  -42.76100 1.000 36.99000  ? 297 LYS   B HB2    1 
ATOM   8929 H HB3    . LYS   B 1 331 ? -14.26100 46.45100  -41.51300 1.000 36.99000  ? 297 LYS   B HB3    1 
ATOM   8930 H HG2    . LYS   B 1 331 ? -15.72500 44.72400  -41.56200 1.000 38.74000  ? 297 LYS   B HG2    1 
ATOM   8931 H HG3    . LYS   B 1 331 ? -15.21600 44.25400  -42.99500 1.000 38.74000  ? 297 LYS   B HG3    1 
ATOM   8932 H HD2    . LYS   B 1 331 ? -13.25300 43.48600  -42.10200 1.000 43.83000  ? 297 LYS   B HD2    1 
ATOM   8933 H HD3    . LYS   B 1 331 ? -13.62200 44.09100  -40.67800 1.000 43.83000  ? 297 LYS   B HD3    1 
ATOM   8934 H HE2    . LYS   B 1 331 ? -15.20200 42.07800  -41.83800 1.000 37.54000  ? 297 LYS   B HE2    1 
ATOM   8935 H HE3    . LYS   B 1 331 ? -13.96100 41.71300  -40.90700 1.000 37.54000  ? 297 LYS   B HE3    1 
ATOM   8936 H HZ1    . LYS   B 1 331 ? -15.87700 41.78300  -39.68400 1.000 38.00000  ? 297 LYS   B HZ1    1 
ATOM   8937 H HZ2    . LYS   B 1 331 ? -14.99600 42.83300  -39.21600 1.000 38.00000  ? 297 LYS   B HZ2    1 
ATOM   8938 H HZ3    . LYS   B 1 331 ? -16.12500 43.15900  -40.06300 1.000 38.00000  ? 297 LYS   B HZ3    1 
ATOM   8939 N N      . GLY   B 1 332 ? -14.25600 48.87500  -44.41200 1.000 40.51000  ? 298 GLY   B N      1 
ATOM   8940 C CA     . GLY   B 1 332 ? -13.69900 50.21400  -44.43900 1.000 37.54000  ? 298 GLY   B CA     1 
ATOM   8941 C C      . GLY   B 1 332 ? -12.27700 50.34100  -43.94400 1.000 48.97000  ? 298 GLY   B C      1 
ATOM   8942 O O      . GLY   B 1 332 ? -11.83000 51.46100  -43.68700 1.000 42.82000  ? 298 GLY   B O      1 
ATOM   8943 H H      . GLY   B 1 332 ? -14.29800 48.49700  -45.18300 1.000 40.51000  ? 298 GLY   B H      1 
ATOM   8944 H HA2    . GLY   B 1 332 ? -13.72600 50.54500  -45.35100 1.000 37.54000  ? 298 GLY   B HA2    1 
ATOM   8945 H HA3    . GLY   B 1 332 ? -14.25500 50.79400  -43.89500 1.000 37.54000  ? 298 GLY   B HA3    1 
ATOM   8946 N N      . TYR   B 1 333 ? -11.53500 49.24100  -43.80800 1.000 36.53000  ? 299 TYR   B N      1 
ATOM   8947 C CA     . TYR   B 1 333 ? -10.14900 49.33900  -43.36900 1.000 36.94000  ? 299 TYR   B CA     1 
ATOM   8948 C C      . TYR   B 1 333 ? -9.24300  49.69500  -44.54000 1.000 34.52000  ? 299 TYR   B C      1 
ATOM   8949 O O      . TYR   B 1 333 ? -9.36400  49.14100  -45.63800 1.000 42.08000  ? 299 TYR   B O      1 
ATOM   8950 C CB     . TYR   B 1 333 ? -9.68000  48.02200  -42.74000 1.000 35.83000  ? 299 TYR   B CB     1 
ATOM   8951 C CG     . TYR   B 1 333 ? -10.29800 47.69500  -41.39800 1.000 39.65000  ? 299 TYR   B CG     1 
ATOM   8952 C CD1    . TYR   B 1 333 ? -10.37000 48.64800  -40.38400 1.000 43.63000  ? 299 TYR   B CD1    1 
ATOM   8953 C CD2    . TYR   B 1 333 ? -10.80100 46.41100  -41.13700 1.000 32.43000  ? 299 TYR   B CD2    1 
ATOM   8954 C CE1    . TYR   B 1 333 ? -10.93300 48.34300  -39.14600 1.000 38.20000  ? 299 TYR   B CE1    1 
ATOM   8955 C CE2    . TYR   B 1 333 ? -11.37700 46.10800  -39.90100 1.000 34.65000  ? 299 TYR   B CE2    1 
ATOM   8956 C CZ     . TYR   B 1 333 ? -11.43300 47.08400  -38.91300 1.000 40.95000  ? 299 TYR   B CZ     1 
ATOM   8957 O OH     . TYR   B 1 333 ? -11.97600 46.81200  -37.68400 1.000 43.68000  ? 299 TYR   B OH     1 
ATOM   8958 H H      . TYR   B 1 333 ? -11.80800 48.44000  -43.96200 1.000 36.53000  ? 299 TYR   B H      1 
ATOM   8959 H HA     . TYR   B 1 333 ? -10.07200 50.04100  -42.70500 1.000 36.94000  ? 299 TYR   B HA     1 
ATOM   8960 H HB2    . TYR   B 1 333 ? -9.89700  47.29700  -43.34600 1.000 35.83000  ? 299 TYR   B HB2    1 
ATOM   8961 H HB3    . TYR   B 1 333 ? -8.71900  48.06500  -42.61600 1.000 35.83000  ? 299 TYR   B HB3    1 
ATOM   8962 H HD1    . TYR   B 1 333 ? -10.03700 49.50300  -40.53600 1.000 43.63000  ? 299 TYR   B HD1    1 
ATOM   8963 H HD2    . TYR   B 1 333 ? -10.76600 45.76000  -41.80000 1.000 32.43000  ? 299 TYR   B HD2    1 
ATOM   8964 H HE1    . TYR   B 1 333 ? -10.97600 48.99200  -38.48100 1.000 38.20000  ? 299 TYR   B HE1    1 
ATOM   8965 H HE2    . TYR   B 1 333 ? -11.70900 45.25500  -39.73600 1.000 34.65000  ? 299 TYR   B HE2    1 
ATOM   8966 H HH     . TYR   B 1 333 ? -12.20400 46.00600  -37.64400 1.000 43.68000  ? 299 TYR   B HH     1 
ATOM   8967 N N      . LYS   B 1 334 ? -8.30200  50.59900  -44.28800 1.000 35.56000  ? 300 LYS   B N      1 
ATOM   8968 C CA     . LYS   B 1 334 ? -7.34500  51.03000  -45.29400 1.000 43.17000  ? 300 LYS   B CA     1 
ATOM   8969 C C      . LYS   B 1 334 ? -5.94500  50.50500  -45.05600 1.000 41.59000  ? 300 LYS   B C      1 
ATOM   8970 O O      . LYS   B 1 334 ? -5.11900  50.57500  -45.96400 1.000 38.97000  ? 300 LYS   B O      1 
ATOM   8971 C CB     . LYS   B 1 334 ? -7.26700  52.56500  -45.33900 1.000 41.34000  ? 300 LYS   B CB     1 
ATOM   8972 C CG     . LYS   B 1 334 ? -8.60500  53.25500  -45.44500 1.000 51.30000  ? 300 LYS   B CG     1 
ATOM   8973 C CD     . LYS   B 1 334 ? -9.11500  53.27000  -46.86700 1.000 59.06000  ? 300 LYS   B CD     1 
ATOM   8974 C CE     . LYS   B 1 334 ? -10.32100 54.19100  -46.98000 1.000 73.40000  ? 300 LYS   B CE     1 
ATOM   8975 N NZ     . LYS   B 1 334 ? -11.27900 53.71500  -48.01300 1.000 76.51000  ? 300 LYS   B NZ     1 
ATOM   8976 H H      . LYS   B 1 334 ? -8.19800  50.98300  -43.52600 1.000 35.56000  ? 300 LYS   B H      1 
ATOM   8977 H HA     . LYS   B 1 334 ? -7.63700  50.72000  -46.16500 1.000 43.17000  ? 300 LYS   B HA     1 
ATOM   8978 H HB2    . LYS   B 1 334 ? -6.83900  52.87700  -44.52700 1.000 41.34000  ? 300 LYS   B HB2    1 
ATOM   8979 H HB3    . LYS   B 1 334 ? -6.73800  52.82700  -46.10800 1.000 41.34000  ? 300 LYS   B HB3    1 
ATOM   8980 H HG2    . LYS   B 1 334 ? -9.25700  52.79600  -44.89400 1.000 51.30000  ? 300 LYS   B HG2    1 
ATOM   8981 H HG3    . LYS   B 1 334 ? -8.51000  54.17400  -45.15100 1.000 51.30000  ? 300 LYS   B HG3    1 
ATOM   8982 H HD2    . LYS   B 1 334 ? -8.42000  53.59900  -47.45900 1.000 59.06000  ? 300 LYS   B HD2    1 
ATOM   8983 H HD3    . LYS   B 1 334 ? -9.38500  52.37500  -47.12400 1.000 59.06000  ? 300 LYS   B HD3    1 
ATOM   8984 H HE2    . LYS   B 1 334 ? -10.78300 54.21900  -46.12700 1.000 73.40000  ? 300 LYS   B HE2    1 
ATOM   8985 H HE3    . LYS   B 1 334 ? -10.02200 55.08000  -47.22900 1.000 73.40000  ? 300 LYS   B HE3    1 
ATOM   8986 H HZ1    . LYS   B 1 334 ? -11.97400 54.26800  -48.06100 1.000 76.51000  ? 300 LYS   B HZ1    1 
ATOM   8987 H HZ2    . LYS   B 1 334 ? -10.87900 53.68400  -48.80700 1.000 76.51000  ? 300 LYS   B HZ2    1 
ATOM   8988 H HZ3    . LYS   B 1 334 ? -11.57100 52.90100  -47.80400 1.000 76.51000  ? 300 LYS   B HZ3    1 
ATOM   8989 N N      . ALA   B 1 335 ? -5.64700  50.02800  -43.85600 1.000 33.72000  ? 301 ALA   B N      1 
ATOM   8990 C CA     . ALA   B 1 335 ? -4.31300  49.54800  -43.54400 1.000 31.90000  ? 301 ALA   B CA     1 
ATOM   8991 C C      . ALA   B 1 335 ? -4.45400  48.46900  -42.48700 1.000 36.16000  ? 301 ALA   B C      1 
ATOM   8992 O O      . ALA   B 1 335 ? -5.42900  48.45400  -41.72900 1.000 35.38000  ? 301 ALA   B O      1 
ATOM   8993 C CB     . ALA   B 1 335 ? -3.38700  50.66500  -43.04900 1.000 32.40000  ? 301 ALA   B CB     1 
ATOM   8994 H H      . ALA   B 1 335 ? -6.20300  49.97200  -43.20200 1.000 33.72000  ? 301 ALA   B H      1 
ATOM   8995 H HA     . ALA   B 1 335 ? -3.91800  49.15100  -44.33600 1.000 31.90000  ? 301 ALA   B HA     1 
ATOM   8996 H HB1    . ALA   B 1 335 ? -2.51400  50.28900  -42.85700 1.000 32.40000  ? 301 ALA   B HB1    1 
ATOM   8997 H HB2    . ALA   B 1 335 ? -3.31200  51.34100  -43.74000 1.000 32.40000  ? 301 ALA   B HB2    1 
ATOM   8998 H HB3    . ALA   B 1 335 ? -3.76400  51.05400  -42.24400 1.000 32.40000  ? 301 ALA   B HB3    1 
ATOM   8999 N N      . LEU   B 1 336 ? -3.49000  47.54700  -42.46500 1.000 31.04000  ? 302 LEU   B N      1 
ATOM   9000 C CA     . LEU   B 1 336 ? -3.56700  46.44800  -41.50800 1.000 28.09000  ? 302 LEU   B CA     1 
ATOM   9001 C C      . LEU   B 1 336 ? -3.44800  46.94300  -40.07200 1.000 32.84000  ? 302 LEU   B C      1 
ATOM   9002 O O      . LEU   B 1 336 ? -4.06600  46.36400  -39.17500 1.000 30.59000  ? 302 LEU   B O      1 
ATOM   9003 C CB     . LEU   B 1 336 ? -2.47700  45.42300  -41.82000 1.000 29.77000  ? 302 LEU   B CB     1 
ATOM   9004 C CG     . LEU   B 1 336 ? -2.61000  44.75900  -43.20400 1.000 30.52000  ? 302 LEU   B CG     1 
ATOM   9005 C CD1    . LEU   B 1 336 ? -1.32800  44.01300  -43.55800 1.000 30.98000  ? 302 LEU   B CD1    1 
ATOM   9006 C CD2    . LEU   B 1 336 ? -3.79900  43.82700  -43.21600 1.000 31.76000  ? 302 LEU   B CD2    1 
ATOM   9007 H H      . LEU   B 1 336 ? -2.80000  47.53500  -42.97900 1.000 31.04000  ? 302 LEU   B H      1 
ATOM   9008 H HA     . LEU   B 1 336 ? -4.42700  46.01000  -41.60000 1.000 28.09000  ? 302 LEU   B HA     1 
ATOM   9009 H HB2    . LEU   B 1 336 ? -1.61500  45.86600  -41.78700 1.000 29.77000  ? 302 LEU   B HB2    1 
ATOM   9010 H HB3    . LEU   B 1 336 ? -2.51000  44.72100  -41.15100 1.000 29.77000  ? 302 LEU   B HB3    1 
ATOM   9011 H HG     . LEU   B 1 336 ? -2.75600  45.44400  -43.87500 1.000 30.52000  ? 302 LEU   B HG     1 
ATOM   9012 H HD11   . LEU   B 1 336 ? -1.43300  43.60200  -44.43000 1.000 30.98000  ? 302 LEU   B HD11   1 
ATOM   9013 H HD12   . LEU   B 1 336 ? -0.59100  44.64300  -43.57500 1.000 30.98000  ? 302 LEU   B HD12   1 
ATOM   9014 H HD13   . LEU   B 1 336 ? -1.16500  43.33100  -42.88800 1.000 30.98000  ? 302 LEU   B HD13   1 
ATOM   9015 H HD21   . LEU   B 1 336 ? -3.81000  43.34100  -44.05500 1.000 31.76000  ? 302 LEU   B HD21   1 
ATOM   9016 H HD22   . LEU   B 1 336 ? -3.72000  43.20600  -42.47500 1.000 31.76000  ? 302 LEU   B HD22   1 
ATOM   9017 H HD23   . LEU   B 1 336 ? -4.61200  44.34900  -43.12600 1.000 31.76000  ? 302 LEU   B HD23   1 
ATOM   9018 N N      . ASP   B 1 337 ? -2.69100  48.02100  -39.83000 1.000 31.05000  ? 303 ASP   B N      1 
ATOM   9019 C CA     . ASP   B 1 337 ? -2.59200  48.54600  -38.46700 1.000 34.82000  ? 303 ASP   B CA     1 
ATOM   9020 C C      . ASP   B 1 337 ? -3.93200  49.05500  -37.94000 1.000 40.42000  ? 303 ASP   B C      1 
ATOM   9021 O O      . ASP   B 1 337 ? -4.07000  49.24800  -36.72700 1.000 41.83000  ? 303 ASP   B O      1 
ATOM   9022 C CB     . ASP   B 1 337 ? -1.52400  49.66100  -38.38100 1.000 39.82000  ? 303 ASP   B CB     1 
ATOM   9023 C CG     . ASP   B 1 337 ? -0.08400  49.11100  -38.26900 1.000 49.82000  ? 303 ASP   B CG     1 
ATOM   9024 O OD1    . ASP   B 1 337 ? 0.12500   47.89600  -38.44700 1.000 59.45000  ? 303 ASP   B OD1    1 
ATOM   9025 O OD2    . ASP   B 1 337 ? 0.84600   49.89200  -37.99200 1.000 60.32000  ? 303 ASP   B OD2    1 
ATOM   9026 H H      . ASP   B 1 337 ? -2.23900  48.45300  -40.42000 1.000 31.05000  ? 303 ASP   B H      1 
ATOM   9027 H HA     . ASP   B 1 337 ? -2.30700  47.82600  -37.88300 1.000 34.82000  ? 303 ASP   B HA     1 
ATOM   9028 H HB2    . ASP   B 1 337 ? -1.57400  50.20800  -39.18100 1.000 39.82000  ? 303 ASP   B HB2    1 
ATOM   9029 H HB3    . ASP   B 1 337 ? -1.69800  50.20500  -37.59700 1.000 39.82000  ? 303 ASP   B HB3    1 
ATOM   9030 N N      . GLU   B 1 338 ? -4.93700  49.23500  -38.79600 1.000 32.19000  ? 304 GLU   B N      1 
ATOM   9031 C CA     . GLU   B 1 338 ? -6.24500  49.63300  -38.28500 1.000 33.47000  ? 304 GLU   B CA     1 
ATOM   9032 C C      . GLU   B 1 338 ? -6.94200  48.51600  -37.51300 1.000 44.94000  ? 304 GLU   B C      1 
ATOM   9033 O O      . GLU   B 1 338 ? -7.89400  48.79000  -36.78100 1.000 37.85000  ? 304 GLU   B O      1 
ATOM   9034 C CB     . GLU   B 1 338 ? -7.12800  50.12800  -39.43300 1.000 35.49000  ? 304 GLU   B CB     1 
ATOM   9035 C CG     . GLU   B 1 338 ? -6.54000  51.40900  -40.00700 1.000 38.71000  ? 304 GLU   B CG     1 
ATOM   9036 C CD     . GLU   B 1 338 ? -7.41800  52.10300  -41.01700 1.000 53.78000  ? 304 GLU   B CD     1 
ATOM   9037 O OE1    . GLU   B 1 338 ? -8.45800  51.53900  -41.40900 1.000 46.59000  ? 304 GLU   B OE1    1 
ATOM   9038 O OE2    . GLU   B 1 338 ? -7.04900  53.23200  -41.42500 1.000 62.03000  ? 304 GLU   B OE2    1 
ATOM   9039 H H      . GLU   B 1 338 ? -4.89100  49.13700  -39.64900 1.000 32.19000  ? 304 GLU   B H      1 
ATOM   9040 H HA     . GLU   B 1 338 ? -6.12200  50.37500  -37.67200 1.000 33.47000  ? 304 GLU   B HA     1 
ATOM   9041 H HB2    . GLU   B 1 338 ? -7.15800  49.45900  -40.13400 1.000 35.49000  ? 304 GLU   B HB2    1 
ATOM   9042 H HB3    . GLU   B 1 338 ? -8.02000  50.31700  -39.10100 1.000 35.49000  ? 304 GLU   B HB3    1 
ATOM   9043 H HG2    . GLU   B 1 338 ? -6.38100  52.03100  -39.28000 1.000 38.71000  ? 304 GLU   B HG2    1 
ATOM   9044 H HG3    . GLU   B 1 338 ? -5.70100  51.19600  -40.44400 1.000 38.71000  ? 304 GLU   B HG3    1 
ATOM   9045 N N      . PHE   B 1 339 ? -6.51600  47.25800  -37.66000 1.000 32.13000  ? 305 PHE   B N      1 
ATOM   9046 C CA     . PHE   B 1 339 ? -7.17200  46.20200  -36.89600 1.000 31.33000  ? 305 PHE   B CA     1 
ATOM   9047 C C      . PHE   B 1 339 ? -6.22800  45.15000  -36.33100 1.000 33.09000  ? 305 PHE   B C      1 
ATOM   9048 O O      . PHE   B 1 339 ? -6.70600  44.28800  -35.59000 1.000 33.75000  ? 305 PHE   B O      1 
ATOM   9049 C CB     . PHE   B 1 339 ? -8.25100  45.49400  -37.74200 1.000 30.42000  ? 305 PHE   B CB     1 
ATOM   9050 C CG     . PHE   B 1 339 ? -7.72700  44.80200  -38.98100 1.000 31.37000  ? 305 PHE   B CG     1 
ATOM   9051 C CD1    . PHE   B 1 339 ? -7.52400  45.51600  -40.16400 1.000 29.88000  ? 305 PHE   B CD1    1 
ATOM   9052 C CD2    . PHE   B 1 339 ? -7.45000  43.42800  -38.97200 1.000 31.35000  ? 305 PHE   B CD2    1 
ATOM   9053 C CE1    . PHE   B 1 339 ? -7.07400  44.87200  -41.30300 1.000 37.57000  ? 305 PHE   B CE1    1 
ATOM   9054 C CE2    . PHE   B 1 339 ? -6.98200  42.79500  -40.11100 1.000 28.94000  ? 305 PHE   B CE2    1 
ATOM   9055 C CZ     . PHE   B 1 339 ? -6.79500  43.51500  -41.27600 1.000 35.44000  ? 305 PHE   B CZ     1 
ATOM   9056 H H      . PHE   B 1 339 ? -5.87600  47.00000  -38.17400 1.000 32.13000  ? 305 PHE   B H      1 
ATOM   9057 H HA     . PHE   B 1 339 ? -7.62600  46.60400  -36.14000 1.000 31.33000  ? 305 PHE   B HA     1 
ATOM   9058 H HB2    . PHE   B 1 339 ? -8.68500  44.82300  -37.19200 1.000 30.42000  ? 305 PHE   B HB2    1 
ATOM   9059 H HB3    . PHE   B 1 339 ? -8.90200  46.15300  -38.02700 1.000 30.42000  ? 305 PHE   B HB3    1 
ATOM   9060 H HD1    . PHE   B 1 339 ? -7.71400  46.42600  -40.19300 1.000 29.88000  ? 305 PHE   B HD1    1 
ATOM   9061 H HD2    . PHE   B 1 339 ? -7.57800  42.93800  -38.19200 1.000 31.35000  ? 305 PHE   B HD2    1 
ATOM   9062 H HE1    . PHE   B 1 339 ? -6.93800  45.35700  -42.08500 1.000 37.57000  ? 305 PHE   B HE1    1 
ATOM   9063 H HE2    . PHE   B 1 339 ? -6.80100  41.88300  -40.09400 1.000 28.94000  ? 305 PHE   B HE2    1 
ATOM   9064 H HZ     . PHE   B 1 339 ? -6.48000  43.08900  -42.04100 1.000 35.44000  ? 305 PHE   B HZ     1 
ATOM   9065 N N      . ARG   B 1 340 ? -4.92700  45.18000  -36.64200 1.000 29.45000  ? 306 ARG   B N      1 
ATOM   9066 C CA     . ARG   B 1 340 ? -4.00700  44.18500  -36.09000 1.000 32.09000  ? 306 ARG   B CA     1 
ATOM   9067 C C      . ARG   B 1 340 ? -4.06400  44.18900  -34.57000 1.000 35.50000  ? 306 ARG   B C      1 
ATOM   9068 O O      . ARG   B 1 340 ? -3.89200  45.23600  -33.93200 1.000 32.38000  ? 306 ARG   B O      1 
ATOM   9069 C CB     . ARG   B 1 340 ? -2.57000  44.47500  -36.55200 1.000 31.96000  ? 306 ARG   B CB     1 
ATOM   9070 C CG     . ARG   B 1 340 ? -1.55100  43.45100  -36.04000 1.000 30.36000  ? 306 ARG   B CG     1 
ATOM   9071 C CD     . ARG   B 1 340 ? -0.17000  43.66500  -36.63000 1.000 33.12000  ? 306 ARG   B CD     1 
ATOM   9072 N NE     . ARG   B 1 340 ? -0.11300  43.42500  -38.06900 1.000 34.82000  ? 306 ARG   B NE     1 
ATOM   9073 C CZ     . ARG   B 1 340 ? 0.17800   44.33700  -38.99300 1.000 39.23000  ? 306 ARG   B CZ     1 
ATOM   9074 N NH1    . ARG   B 1 340 ? 0.25700   45.62000  -38.69600 1.000 34.42000  ? 306 ARG   B NH1    1 
ATOM   9075 N NH2    . ARG   B 1 340 ? 0.41700   43.94200  -40.24200 1.000 42.50000  ? 306 ARG   B NH2    1 
ATOM   9076 H H      . ARG   B 1 340 ? -4.55900  45.75700  -37.16200 1.000 29.45000  ? 306 ARG   B H      1 
ATOM   9077 H HA     . ARG   B 1 340 ? -4.26000  43.30500  -36.40600 1.000 32.09000  ? 306 ARG   B HA     1 
ATOM   9078 H HB2    . ARG   B 1 340 ? -2.54300  44.46300  -37.52200 1.000 31.96000  ? 306 ARG   B HB2    1 
ATOM   9079 H HB3    . ARG   B 1 340 ? -2.30500  45.34900  -36.22500 1.000 31.96000  ? 306 ARG   B HB3    1 
ATOM   9080 H HG2    . ARG   B 1 340 ? -1.47900  43.52700  -35.07600 1.000 30.36000  ? 306 ARG   B HG2    1 
ATOM   9081 H HG3    . ARG   B 1 340 ? -1.84700  42.56000  -36.28300 1.000 30.36000  ? 306 ARG   B HG3    1 
ATOM   9082 H HD2    . ARG   B 1 340 ? 0.11100   44.57300  -36.44800 1.000 33.12000  ? 306 ARG   B HD2    1 
ATOM   9083 H HD3    . ARG   B 1 340 ? 0.44400   43.04500  -36.20700 1.000 33.12000  ? 306 ARG   B HD3    1 
ATOM   9084 H HE     . ARG   B 1 340 ? -0.28600  42.62800  -38.34300 1.000 34.82000  ? 306 ARG   B HE     1 
ATOM   9085 H HH11   . ARG   B 1 340 ? 0.11500   45.89200  -37.89400 1.000 34.42000  ? 306 ARG   B HH11   1 
ATOM   9086 H HH12   . ARG   B 1 340 ? 0.44500   46.19000  -39.31200 1.000 34.42000  ? 306 ARG   B HH12   1 
ATOM   9087 H HH21   . ARG   B 1 340 ? 0.36500   43.10800  -40.44700 1.000 42.50000  ? 306 ARG   B HH21   1 
ATOM   9088 H HH22   . ARG   B 1 340 ? 0.59600   44.52300  -40.85000 1.000 42.50000  ? 306 ARG   B HH22   1 
ATOM   9089 N N      . GLY   B 1 341 ? -4.29700  43.01500  -33.98700 1.000 29.60000  ? 307 GLY   B N      1 
ATOM   9090 C CA     . GLY   B 1 341 ? -4.34100  42.88600  -32.54700 1.000 28.92000  ? 307 GLY   B CA     1 
ATOM   9091 C C      . GLY   B 1 341 ? -5.62600  43.36400  -31.89300 1.000 39.54000  ? 307 GLY   B C      1 
ATOM   9092 O O      . GLY   B 1 341 ? -5.71100  43.34500  -30.65600 1.000 33.84000  ? 307 GLY   B O      1 
ATOM   9093 H H      . GLY   B 1 341 ? -4.43200  42.27900  -34.41100 1.000 29.60000  ? 307 GLY   B H      1 
ATOM   9094 H HA2    . GLY   B 1 341 ? -4.21600  41.95300  -32.31200 1.000 28.92000  ? 307 GLY   B HA2    1 
ATOM   9095 H HA3    . GLY   B 1 341 ? -3.60700  43.39200  -32.16500 1.000 28.92000  ? 307 GLY   B HA3    1 
ATOM   9096 N N      . LYS   B 1 342 ? -6.62400  43.79500  -32.67500 1.000 31.47000  ? 308 LYS   B N      1 
ATOM   9097 C CA     . LYS   B 1 342 ? -7.82700  44.42200  -32.13900 1.000 35.22000  ? 308 LYS   B CA     1 
ATOM   9098 C C      . LYS   B 1 342 ? -8.99700  43.45700  -31.99100 1.000 43.40000  ? 308 LYS   B C      1 
ATOM   9099 O O      . LYS   B 1 342 ? -10.15200 43.88900  -31.95700 1.000 37.02000  ? 308 LYS   B O      1 
ATOM   9100 C CB     . LYS   B 1 342 ? -8.21200  45.60600  -33.02300 1.000 34.54000  ? 308 LYS   B CB     1 
ATOM   9101 C CG     . LYS   B 1 342 ? -7.03700  46.57100  -33.18200 1.000 41.79000  ? 308 LYS   B CG     1 
ATOM   9102 C CD     . LYS   B 1 342 ? -7.32300  47.99700  -32.77400 1.000 60.55000  ? 308 LYS   B CD     1 
ATOM   9103 C CE     . LYS   B 1 342 ? -5.98600  48.72000  -32.51100 1.000 62.65000  ? 308 LYS   B CE     1 
ATOM   9104 N NZ     . LYS   B 1 342 ? -5.94200  50.13500  -32.96900 1.000 69.52000  ? 308 LYS   B NZ     1 
ATOM   9105 H H      . LYS   B 1 342 ? -6.62300  43.73200  -33.53300 1.000 31.47000  ? 308 LYS   B H      1 
ATOM   9106 H HA     . LYS   B 1 342 ? -7.62500  44.77100  -31.25700 1.000 35.22000  ? 308 LYS   B HA     1 
ATOM   9107 H HB2    . LYS   B 1 342 ? -8.46300  45.28300  -33.90200 1.000 34.54000  ? 308 LYS   B HB2    1 
ATOM   9108 H HB3    . LYS   B 1 342 ? -8.95000  46.08600  -32.61600 1.000 34.54000  ? 308 LYS   B HB3    1 
ATOM   9109 H HG2    . LYS   B 1 342 ? -6.30200  46.25900  -32.63200 1.000 41.79000  ? 308 LYS   B HG2    1 
ATOM   9110 H HG3    . LYS   B 1 342 ? -6.76500  46.58200  -34.11100 1.000 41.79000  ? 308 LYS   B HG3    1 
ATOM   9111 H HD2    . LYS   B 1 342 ? -7.79000  48.45600  -33.49000 1.000 60.55000  ? 308 LYS   B HD2    1 
ATOM   9112 H HD3    . LYS   B 1 342 ? -7.84800  48.00700  -31.95800 1.000 60.55000  ? 308 LYS   B HD3    1 
ATOM   9113 H HE2    . LYS   B 1 342 ? -5.81400  48.71500  -31.55600 1.000 62.65000  ? 308 LYS   B HE2    1 
ATOM   9114 H HE3    . LYS   B 1 342 ? -5.27900  48.24200  -32.97200 1.000 62.65000  ? 308 LYS   B HE3    1 
ATOM   9115 H HZ1    . LYS   B 1 342 ? -5.14600  50.48900  -32.78700 1.000 69.52000  ? 308 LYS   B HZ1    1 
ATOM   9116 H HZ2    . LYS   B 1 342 ? -6.08200  50.17500  -33.84700 1.000 69.52000  ? 308 LYS   B HZ2    1 
ATOM   9117 H HZ3    . LYS   B 1 342 ? -6.57100  50.60900  -32.55400 1.000 69.52000  ? 308 LYS   B HZ3    1 
ATOM   9118 N N      . VAL   B 1 343 ? -8.73300  42.15500  -31.90300 1.000 32.03000  ? 309 VAL   B N      1 
ATOM   9119 C CA     . VAL   B 1 343 ? -9.81300  41.22900  -31.58200 1.000 34.24000  ? 309 VAL   B CA     1 
ATOM   9120 C C      . VAL   B 1 343 ? -10.53900 41.74500  -30.34200 1.000 40.17000  ? 309 VAL   B C      1 
ATOM   9121 O O      . VAL   B 1 343 ? -9.91900  42.25800  -29.40500 1.000 41.70000  ? 309 VAL   B O      1 
ATOM   9122 C CB     . VAL   B 1 343 ? -9.25100  39.81100  -31.37300 1.000 36.04000  ? 309 VAL   B CB     1 
ATOM   9123 C CG1    . VAL   B 1 343 ? -8.22600  39.83000  -30.25400 1.000 36.96000  ? 309 VAL   B CG1    1 
ATOM   9124 C CG2    . VAL   B 1 343 ? -10.38800 38.79200  -31.09400 1.000 36.14000  ? 309 VAL   B CG2    1 
ATOM   9125 H H      . VAL   B 1 343 ? -7.96300  41.79300  -32.02300 1.000 32.03000  ? 309 VAL   B H      1 
ATOM   9126 H HA     . VAL   B 1 343 ? -10.44500 41.20300  -32.31800 1.000 34.24000  ? 309 VAL   B HA     1 
ATOM   9127 H HB     . VAL   B 1 343 ? -8.79800  39.53300  -32.18400 1.000 36.04000  ? 309 VAL   B HB     1 
ATOM   9128 H HG11   . VAL   B 1 343 ? -7.85100  38.94000  -30.16100 1.000 36.96000  ? 309 VAL   B HG11   1 
ATOM   9129 H HG12   . VAL   B 1 343 ? -7.52300  40.46000  -30.47300 1.000 36.96000  ? 309 VAL   B HG12   1 
ATOM   9130 H HG13   . VAL   B 1 343 ? -8.66000  40.09100  -29.42700 1.000 36.96000  ? 309 VAL   B HG13   1 
ATOM   9131 H HG21   . VAL   B 1 343 ? -10.00700 37.90100  -31.04700 1.000 36.14000  ? 309 VAL   B HG21   1 
ATOM   9132 H HG22   . VAL   B 1 343 ? -10.81400 39.01400  -30.25100 1.000 36.14000  ? 309 VAL   B HG22   1 
ATOM   9133 H HG23   . VAL   B 1 343 ? -11.03500 38.83700  -31.81500 1.000 36.14000  ? 309 VAL   B HG23   1 
ATOM   9134 N N      . LYS   B 1 344 ? -11.86500 41.65600  -30.35700 1.000 43.71000  ? 310 LYS   B N      1 
ATOM   9135 C CA     . LYS   B 1 344 ? -12.69500 42.17200  -29.27400 1.000 48.49000  ? 310 LYS   B CA     1 
ATOM   9136 C C      . LYS   B 1 344 ? -13.06000 41.05300  -28.29900 1.000 46.97000  ? 310 LYS   B C      1 
ATOM   9137 O O      . LYS   B 1 344 ? -13.38300 39.93600  -28.71100 1.000 44.73000  ? 310 LYS   B O      1 
ATOM   9138 C CB     . LYS   B 1 344 ? -13.97000 42.82100  -29.83500 1.000 42.65000  ? 310 LYS   B CB     1 
ATOM   9139 C CG     . LYS   B 1 344 ? -13.77700 44.25100  -30.36600 1.000 43.23000  ? 310 LYS   B CG     1 
ATOM   9140 C CD     . LYS   B 1 344 ? -13.67600 44.32300  -31.89200 1.000 57.27000  ? 310 LYS   B CD     1 
ATOM   9141 C CE     . LYS   B 1 344 ? -12.60500 45.35300  -32.32000 1.000 65.51000  ? 310 LYS   B CE     1 
ATOM   9142 N NZ     . LYS   B 1 344 ? -11.95000 45.13100  -33.66800 1.000 49.58000  ? 310 LYS   B NZ     1 
ATOM   9143 H H      . LYS   B 1 344 ? -12.31500 41.29500  -30.99500 1.000 43.71000  ? 310 LYS   B H      1 
ATOM   9144 H HA     . LYS   B 1 344 ? -12.20100 42.84800  -28.78500 1.000 48.49000  ? 310 LYS   B HA     1 
ATOM   9145 H HB2    . LYS   B 1 344 ? -14.30200 42.27500  -30.56500 1.000 42.65000  ? 310 LYS   B HB2    1 
ATOM   9146 H HB3    . LYS   B 1 344 ? -14.63400 42.85800  -29.12900 1.000 42.65000  ? 310 LYS   B HB3    1 
ATOM   9147 H HG2    . LYS   B 1 344 ? -14.53700 44.78900  -30.09500 1.000 43.23000  ? 310 LYS   B HG2    1 
ATOM   9148 H HG3    . LYS   B 1 344 ? -12.96500 44.61800  -29.98500 1.000 43.23000  ? 310 LYS   B HG3    1 
ATOM   9149 H HD2    . LYS   B 1 344 ? -13.42100 43.45500  -32.24200 1.000 57.27000  ? 310 LYS   B HD2    1 
ATOM   9150 H HD3    . LYS   B 1 344 ? -14.53000 44.59900  -32.25900 1.000 57.27000  ? 310 LYS   B HD3    1 
ATOM   9151 H HE2    . LYS   B 1 344 ? -13.02800 46.22500  -32.35300 1.000 65.51000  ? 310 LYS   B HE2    1 
ATOM   9152 H HE3    . LYS   B 1 344 ? -11.90000 45.37100  -31.65600 1.000 65.51000  ? 310 LYS   B HE3    1 
ATOM   9153 H HZ1    . LYS   B 1 344 ? -11.35200 45.77100  -33.82400 1.000 49.58000  ? 310 LYS   B HZ1    1 
ATOM   9154 H HZ2    . LYS   B 1 344 ? -11.53900 44.34200  -33.68000 1.000 49.58000  ? 310 LYS   B HZ2    1 
ATOM   9155 H HZ3    . LYS   B 1 344 ? -12.56500 45.14700  -34.31100 1.000 49.58000  ? 310 LYS   B HZ3    1 
ATOM   9156 N N      . ALA   B 1 345 ? -13.01500 41.35600  -27.00200 1.000 65.41000  ? 311 ALA   B N      1 
ATOM   9157 C CA     . ALA   B 1 345 ? -13.49500 40.41300  -25.99600 1.000 79.00000  ? 311 ALA   B CA     1 
ATOM   9158 C C      . ALA   B 1 345 ? -15.02900 40.41900  -25.95700 1.000 82.01000  ? 311 ALA   B C      1 
ATOM   9159 O O      . ALA   B 1 345 ? -15.69600 41.15100  -26.69900 1.000 72.19000  ? 311 ALA   B O      1 
ATOM   9160 C CB     . ALA   B 1 345 ? -12.90100 40.74100  -24.62400 1.000 66.29000  ? 311 ALA   B CB     1 
ATOM   9161 H H      . ALA   B 1 345 ? -12.71400 42.09500  -26.68200 1.000 65.41000  ? 311 ALA   B H      1 
ATOM   9162 H HA     . ALA   B 1 345 ? -13.20600 39.51900  -26.23900 1.000 79.00000  ? 311 ALA   B HA     1 
ATOM   9163 H HB1    . ALA   B 1 345 ? -13.23100 40.10000  -23.97600 1.000 66.29000  ? 311 ALA   B HB1    1 
ATOM   9164 H HB2    . ALA   B 1 345 ? -11.93400 40.68800  -24.67800 1.000 66.29000  ? 311 ALA   B HB2    1 
ATOM   9165 H HB3    . ALA   B 1 345 ? -13.17000 41.63800  -24.37000 1.000 66.29000  ? 311 ALA   B HB3    1 
ATOM   9166 N N      . MET   B 1 346 ? -15.60100 39.57300  -25.09800 1.000 89.98000  ? 312 MET   B N      1 
ATOM   9167 C CA     . MET   B 1 346 ? -17.05000 39.56100  -24.86600 1.000 91.39000  ? 312 MET   B CA     1 
ATOM   9168 C C      . MET   B 1 346 ? -17.37400 39.95300  -23.42200 1.000 86.35000  ? 312 MET   B C      1 
ATOM   9169 O O      . MET   B 1 346 ? -18.03000 40.96600  -23.17100 1.000 84.23000  ? 312 MET   B O      1 
ATOM   9170 C CB     . MET   B 1 346 ? -17.65000 38.18400  -25.18100 1.000 80.41000  ? 312 MET   B CB     1 
ATOM   9171 C CG     . MET   B 1 346 ? -18.45300 38.12000  -26.48400 1.000 85.87000  ? 312 MET   B CG     1 
ATOM   9172 S SD     . MET   B 1 346 ? -19.24500 36.51800  -26.77300 1.000 92.44000  ? 312 MET   B SD     1 
ATOM   9173 C CE     . MET   B 1 346 ? -19.67400 36.65600  -28.51300 1.000 70.41000  ? 312 MET   B CE     1 
ATOM   9174 H H      . MET   B 1 346 ? -15.17000 38.99200  -24.63400 1.000 89.98000  ? 312 MET   B H      1 
ATOM   9175 H HA     . MET   B 1 346 ? -17.46900 40.20300  -25.46000 1.000 91.39000  ? 312 MET   B HA     1 
ATOM   9176 H HB2    . MET   B 1 346 ? -16.92700 37.54100  -25.25100 1.000 80.41000  ? 312 MET   B HB2    1 
ATOM   9177 H HB3    . MET   B 1 346 ? -18.24400 37.93100  -24.45700 1.000 80.41000  ? 312 MET   B HB3    1 
ATOM   9178 H HG2    . MET   B 1 346 ? -19.14900 38.79500  -26.45600 1.000 85.87000  ? 312 MET   B HG2    1 
ATOM   9179 H HG3    . MET   B 1 346 ? -17.85600 38.29500  -27.22800 1.000 85.87000  ? 312 MET   B HG3    1 
ATOM   9180 H HE1    . MET   B 1 346 ? -19.92700 35.78100  -28.84500 1.000 70.41000  ? 312 MET   B HE1    1 
ATOM   9181 H HE2    . MET   B 1 346 ? -20.41700 37.27300  -28.60600 1.000 70.41000  ? 312 MET   B HE2    1 
ATOM   9182 H HE3    . MET   B 1 346 ? -18.90600 36.98700  -29.00300 1.000 70.41000  ? 312 MET   B HE3    1 
HETATM 9183 N N1     . FMN   C 2 .   ? -14.96100 16.31800  -20.47600 1.000 40.30000  ? 401 FMN   A N1     1 
HETATM 9184 C C2     . FMN   C 2 .   ? -14.86500 15.97500  -19.14200 1.000 45.50000  ? 401 FMN   A C2     1 
HETATM 9185 O O2     . FMN   C 2 .   ? -14.03500 15.13900  -18.76700 1.000 45.92000  ? 401 FMN   A O2     1 
HETATM 9186 N N3     . FMN   C 2 .   ? -15.72000 16.55200  -18.22500 1.000 50.08000  ? 401 FMN   A N3     1 
HETATM 9187 C C4     . FMN   C 2 .   ? -16.67200 17.47300  -18.61800 1.000 55.72000  ? 401 FMN   A C4     1 
HETATM 9188 O O4     . FMN   C 2 .   ? -17.42400 17.96600  -17.77300 1.000 49.55000  ? 401 FMN   A O4     1 
HETATM 9189 C C4A    . FMN   C 2 .   ? -16.77000 17.83400  -19.96200 1.000 49.90000  ? 401 FMN   A C4A    1 
HETATM 9190 N N5     . FMN   C 2 .   ? -17.71100 18.76800  -20.36700 1.000 47.59000  ? 401 FMN   A N5     1 
HETATM 9191 C C5A    . FMN   C 2 .   ? -17.81200 19.10100  -21.70500 1.000 46.06000  ? 401 FMN   A C5A    1 
HETATM 9192 C C6     . FMN   C 2 .   ? -18.76500 20.02100  -22.12500 1.000 48.66000  ? 401 FMN   A C6     1 
HETATM 9193 C C7     . FMN   C 2 .   ? -18.86000 20.35800  -23.47500 1.000 47.03000  ? 401 FMN   A C7     1 
HETATM 9194 C C7M    . FMN   C 2 .   ? -19.89800 21.35600  -23.89500 1.000 46.65000  ? 401 FMN   A C7M    1 
HETATM 9195 C C8     . FMN   C 2 .   ? -18.00300 19.77200  -24.41100 1.000 45.67000  ? 401 FMN   A C8     1 
HETATM 9196 C C8M    . FMN   C 2 .   ? -18.07300 20.11900  -25.87000 1.000 49.38000  ? 401 FMN   A C8M    1 
HETATM 9197 C C9     . FMN   C 2 .   ? -17.04800 18.85300  -23.98600 1.000 36.89000  ? 401 FMN   A C9     1 
HETATM 9198 C C9A    . FMN   C 2 .   ? -16.95000 18.52100  -22.64000 1.000 40.85000  ? 401 FMN   A C9A    1 
HETATM 9199 N N10    . FMN   C 2 .   ? -15.99200 17.60200  -22.22900 1.000 44.56000  ? 401 FMN   A N10    1 
HETATM 9200 C C10    . FMN   C 2 .   ? -15.90200 17.25400  -20.88900 1.000 48.04000  ? 401 FMN   A C10    1 
HETATM 9201 C "C1'"  . FMN   C 2 .   ? -15.05900 17.00000  -23.24600 1.000 36.83000  ? 401 FMN   A "C1'"  1 
HETATM 9202 C "C2'"  . FMN   C 2 .   ? -15.62900 15.78900  -23.94700 1.000 34.57000  ? 401 FMN   A "C2'"  1 
HETATM 9203 O "O2'"  . FMN   C 2 .   ? -15.86800 14.81100  -22.95000 1.000 38.94000  ? 401 FMN   A "O2'"  1 
HETATM 9204 C "C3'"  . FMN   C 2 .   ? -14.63100 15.26300  -24.97900 1.000 35.67000  ? 401 FMN   A "C3'"  1 
HETATM 9205 O "O3'"  . FMN   C 2 .   ? -13.44900 14.89700  -24.29700 1.000 36.20000  ? 401 FMN   A "O3'"  1 
HETATM 9206 C "C4'"  . FMN   C 2 .   ? -14.28800 16.27900  -26.08000 1.000 42.43000  ? 401 FMN   A "C4'"  1 
HETATM 9207 O "O4'"  . FMN   C 2 .   ? -15.43200 17.02400  -26.46600 1.000 37.42000  ? 401 FMN   A "O4'"  1 
HETATM 9208 C "C5'"  . FMN   C 2 .   ? -13.70800 15.60400  -27.31600 1.000 37.73000  ? 401 FMN   A "C5'"  1 
HETATM 9209 O "O5'"  . FMN   C 2 .   ? -14.68000 14.73600  -27.85200 1.000 35.27000  ? 401 FMN   A "O5'"  1 
HETATM 9210 P P      . FMN   C 2 .   ? -15.45900 15.12500  -29.20900 1.000 35.06000  ? 401 FMN   A P      1 
HETATM 9211 O O1P    . FMN   C 2 .   ? -16.39700 14.00700  -29.61500 1.000 34.76000  ? 401 FMN   A O1P    1 
HETATM 9212 O O2P    . FMN   C 2 .   ? -16.19000 16.41100  -28.85800 1.000 34.66000  ? 401 FMN   A O2P    1 
HETATM 9213 O O3P    . FMN   C 2 .   ? -14.46000 15.37000  -30.31300 1.000 34.66000  ? 401 FMN   A O3P    1 
HETATM 9214 H HN3    . FMN   C 2 .   ? -15.62600 16.31100  -17.21800 1.000 50.08000  ? 401 FMN   A HN3    1 
HETATM 9215 H H6     . FMN   C 2 .   ? -19.51000 20.39000  -21.42000 1.000 48.66000  ? 401 FMN   A H6     1 
HETATM 9216 H HM71   . FMN   C 2 .   ? -20.17400 21.21300  -24.93900 1.000 46.65000  ? 401 FMN   A HM71   1 
HETATM 9217 H HM72   . FMN   C 2 .   ? -19.50100 22.36300  -23.76400 1.000 46.65000  ? 401 FMN   A HM72   1 
HETATM 9218 H HM73   . FMN   C 2 .   ? -20.78300 21.23600  -23.27100 1.000 46.65000  ? 401 FMN   A HM73   1 
HETATM 9219 H HM81   . FMN   C 2 .   ? -17.26200 19.62000  -26.40100 1.000 49.38000  ? 401 FMN   A HM81   1 
HETATM 9220 H HM82   . FMN   C 2 .   ? -17.97800 21.19800  -25.99300 1.000 49.38000  ? 401 FMN   A HM82   1 
HETATM 9221 H HM83   . FMN   C 2 .   ? -19.02800 19.78800  -26.27700 1.000 49.38000  ? 401 FMN   A HM83   1 
HETATM 9222 H H9     . FMN   C 2 .   ? -16.59600 18.20000  -24.73200 1.000 36.89000  ? 401 FMN   A H9     1 
HETATM 9223 H "H1'1" . FMN   C 2 .   ? -14.14300 16.69500  -22.74100 1.000 36.83000  ? 401 FMN   A "H1'1" 1 
HETATM 9224 H "H1'2" . FMN   C 2 .   ? -14.76000 17.75100  -23.97500 1.000 36.83000  ? 401 FMN   A "H1'2" 1 
HETATM 9225 H "H2'"  . FMN   C 2 .   ? -16.55900 16.06100  -24.44600 1.000 34.57000  ? 401 FMN   A "H2'"  1 
HETATM 9226 H "HO2'" . FMN   C 2 .   ? -16.76500 14.43900  -23.05900 1.000 38.94000  ? 401 FMN   A "HO2'" 1 
HETATM 9227 H "H3'"  . FMN   C 2 .   ? -15.08000 14.39500  -25.45300 1.000 35.67000  ? 401 FMN   A "H3'"  1 
HETATM 9228 H "HO3'" . FMN   C 2 .   ? -12.67800 15.29500  -24.75200 1.000 36.20000  ? 401 FMN   A "HO3'" 1 
HETATM 9229 H "H4'"  . FMN   C 2 .   ? -13.53400 16.96200  -25.68800 1.000 42.43000  ? 401 FMN   A "H4'"  1 
HETATM 9230 H "HO4'" . FMN   C 2 .   ? -15.49700 17.04600  -27.44300 1.000 37.42000  ? 401 FMN   A "HO4'" 1 
HETATM 9231 H "H5'1" . FMN   C 2 .   ? -12.81400 15.04100  -27.04800 1.000 37.73000  ? 401 FMN   A "H5'1" 1 
HETATM 9232 H "H5'2" . FMN   C 2 .   ? -13.43200 16.35600  -28.05600 1.000 37.73000  ? 401 FMN   A "H5'2" 1 
HETATM 9233 C C1     . GOL   D 3 .   ? -3.35400  20.37200  -5.22700  1.000 81.57000  ? 402 GOL   A C1     1 
HETATM 9234 O O1     . GOL   D 3 .   ? -4.55200  20.78600  -5.84500  1.000 79.99000  ? 402 GOL   A O1     1 
HETATM 9235 C C2     . GOL   D 3 .   ? -3.67300  19.57000  -3.98500  1.000 80.78000  ? 402 GOL   A C2     1 
HETATM 9236 O O2     . GOL   D 3 .   ? -4.74300  18.69200  -4.26900  1.000 84.76000  ? 402 GOL   A O2     1 
HETATM 9237 C C3     . GOL   D 3 .   ? -2.46400  18.79200  -3.49000  1.000 86.11000  ? 402 GOL   A C3     1 
HETATM 9238 O O3     . GOL   D 3 .   ? -2.16600  17.78300  -4.43300  1.000 76.68000  ? 402 GOL   A O3     1 
HETATM 9239 H H11    . GOL   D 3 .   ? -2.79800  21.12700  -4.98100  1.000 97.89000  ? 402 GOL   A H11    1 
HETATM 9240 H H12    . GOL   D 3 .   ? -2.82500  19.81300  -5.81700  1.000 97.89000  ? 402 GOL   A H12    1 
HETATM 9241 H HO1    . GOL   D 3 .   ? -4.34900  21.23400  -6.53800  1.000 95.99000  ? 402 GOL   A HO1    1 
HETATM 9242 H H2     . GOL   D 3 .   ? -3.92500  20.19400  -3.28700  1.000 96.93000  ? 402 GOL   A H2     1 
HETATM 9243 H HO2    . GOL   D 3 .   ? -4.89800  18.26000  -3.55200  1.000 101.72000 ? 402 GOL   A HO2    1 
HETATM 9244 H H31    . GOL   D 3 .   ? -2.66200  18.41400  -2.61900  1.000 103.33000 ? 402 GOL   A H31    1 
HETATM 9245 H H32    . GOL   D 3 .   ? -1.71800  19.40200  -3.37500  1.000 103.33000 ? 402 GOL   A H32    1 
HETATM 9246 H HO3    . GOL   D 3 .   ? -2.50300  17.05100  -4.16300  1.000 92.01000  ? 402 GOL   A HO3    1 
HETATM 9247 C C1     . GOL   E 3 .   ? 4.92000   18.98600  -19.38400 1.000 75.54000  ? 403 GOL   A C1     1 
HETATM 9248 O O1     . GOL   E 3 .   ? 3.67500   19.63500  -19.22600 1.000 72.34000  ? 403 GOL   A O1     1 
HETATM 9249 C C2     . GOL   E 3 .   ? 5.96300   19.50400  -18.40500 1.000 79.23000  ? 403 GOL   A C2     1 
HETATM 9250 O O2     . GOL   E 3 .   ? 6.77600   18.41700  -18.01500 1.000 80.01000  ? 403 GOL   A O2     1 
HETATM 9251 C C3     . GOL   E 3 .   ? 6.78200   20.60600  -19.05500 1.000 68.26000  ? 403 GOL   A C3     1 
HETATM 9252 O O3     . GOL   E 3 .   ? 6.29500   21.84400  -18.58600 1.000 77.57000  ? 403 GOL   A O3     1 
HETATM 9253 H H11    . GOL   E 3 .   ? 5.24900   19.17500  -20.26500 1.000 90.65000  ? 403 GOL   A H11    1 
HETATM 9254 H H12    . GOL   E 3 .   ? 4.85200   18.02400  -19.28800 1.000 90.65000  ? 403 GOL   A H12    1 
HETATM 9255 H HO1    . GOL   E 3 .   ? 3.82400   20.45800  -19.07200 1.000 86.81000  ? 403 GOL   A HO1    1 
HETATM 9256 H H2     . GOL   E 3 .   ? 5.50100   19.88000  -17.63900 1.000 95.07000  ? 403 GOL   A H2     1 
HETATM 9257 H HO2    . GOL   E 3 .   ? 7.16100   18.12200  -18.71300 1.000 96.01000  ? 403 GOL   A HO2    1 
HETATM 9258 H H31    . GOL   E 3 .   ? 6.73300   20.55000  -20.02100 1.000 81.92000  ? 403 GOL   A H31    1 
HETATM 9259 H H32    . GOL   E 3 .   ? 7.71400   20.48500  -18.81500 1.000 81.92000  ? 403 GOL   A H32    1 
HETATM 9260 H HO3    . GOL   E 3 .   ? 5.46100   21.77100  -18.43800 1.000 93.09000  ? 403 GOL   A HO3    1 
HETATM 9261 C C02    . A1AVS F 4 .   ? -13.71100 20.72500  -21.60700 0.850 45.79000  ? 404 A1AVS A C02    1 
HETATM 9262 C C04    . A1AVS F 4 .   ? -14.68500 21.86100  -19.58800 0.850 58.43000  ? 404 A1AVS A C04    1 
HETATM 9263 C C05    . A1AVS F 4 .   ? -14.54600 20.61600  -18.69700 0.850 53.16000  ? 404 A1AVS A C05    1 
HETATM 9264 C C06    . A1AVS F 4 .   ? -13.96400 20.71800  -17.29100 0.850 63.34000  ? 404 A1AVS A C06    1 
HETATM 9265 C C14    . A1AVS F 4 .   ? -15.07600 20.81200  -16.24200 0.850 62.15000  ? 404 A1AVS A C14    1 
HETATM 9266 C C15    . A1AVS F 4 .   ? -15.97500 21.78100  -16.21100 0.850 77.62000  ? 404 A1AVS A C15    1 
HETATM 9267 C C16    . A1AVS F 4 .   ? -17.05500 21.77500  -15.12800 0.850 76.42000  ? 404 A1AVS A C16    1 
HETATM 9268 C C17    . A1AVS F 4 .   ? -17.10700 20.81700  -14.22500 0.850 77.94000  ? 404 A1AVS A C17    1 
HETATM 9269 C C18    . A1AVS F 4 .   ? -16.07100 19.69800  -14.26700 0.850 76.21000  ? 404 A1AVS A C18    1 
HETATM 9270 C C19    . A1AVS F 4 .   ? -15.13500 19.69000  -15.20200 0.850 74.21000  ? 404 A1AVS A C19    1 
HETATM 9271 C C22    . A1AVS F 4 .   ? -13.86000 19.50800  -19.48800 0.850 44.22000  ? 404 A1AVS A C22    1 
HETATM 9272 N N03    . A1AVS F 4 .   ? -14.29700 21.85200  -20.99200 0.850 48.57000  ? 404 A1AVS A N03    1 
HETATM 9273 N N21    . A1AVS F 4 .   ? -13.50300 19.56800  -20.87100 0.850 40.45000  ? 404 A1AVS A N21    1 
HETATM 9274 O O01    . A1AVS F 4 .   ? -13.36400 20.72100  -22.73000 0.850 46.68000  ? 404 A1AVS A O01    1 
HETATM 9275 O O20    . A1AVS F 4 .   ? -15.17800 22.83400  -19.16900 0.850 58.47000  ? 404 A1AVS A O20    1 
HETATM 9276 O O23    . A1AVS F 4 .   ? -13.66700 18.50300  -18.98500 0.850 48.00000  ? 404 A1AVS A O23    1 
HETATM 9277 H H051   . A1AVS F 4 .   ? -15.45400 20.29800  -18.57400 0.850 63.79000  ? 404 A1AVS A H051   1 
HETATM 9278 H H061   . A1AVS F 4 .   ? -13.58700 19.86000  -17.07700 0.850 76.00000  ? 404 A1AVS A H061   1 
HETATM 9279 H H151   . A1AVS F 4 .   ? -15.96000 22.46800  -16.83000 0.850 93.14000  ? 404 A1AVS A H151   1 
HETATM 9280 H H161   . A1AVS F 4 .   ? -17.67500 22.45100  -15.10700 0.850 91.70000  ? 404 A1AVS A H161   1 
HETATM 9281 H H171   . A1AVS F 4 .   ? -17.76800 20.82300  -13.57100 0.850 93.53000  ? 404 A1AVS A H171   1 
HETATM 9282 H H181   . A1AVS F 4 .   ? -16.10600 19.01800  -13.63700 0.850 91.46000  ? 404 A1AVS A H181   1 
HETATM 9283 H H191   . A1AVS F 4 .   ? -14.50600 19.00300  -15.22400 0.850 89.06000  ? 404 A1AVS A H191   1 
HETATM 9284 H H031   . A1AVS F 4 .   ? -14.41000 22.56700  -21.45700 0.850 58.28000  ? 404 A1AVS A H031   1 
HETATM 9285 H H211   . A1AVS F 4 .   ? -13.14300 18.88700  -21.24700 0.850 48.54000  ? 404 A1AVS A H211   1 
HETATM 9286 C C1     . GOL   G 3 .   ? 10.23900  12.29700  -27.95100 0.700 57.24000  ? 401 GOL   B C1     1 
HETATM 9287 O O1     . GOL   G 3 .   ? 11.14800  11.55600  -28.72600 0.700 66.07000  ? 401 GOL   B O1     1 
HETATM 9288 C C2     . GOL   G 3 .   ? 9.46700   13.24600  -28.83400 0.700 57.75000  ? 401 GOL   B C2     1 
HETATM 9289 O O2     . GOL   G 3 .   ? 10.42000  14.00900  -29.55700 0.700 74.32000  ? 401 GOL   B O2     1 
HETATM 9290 C C3     . GOL   G 3 .   ? 8.52100   12.54700  -29.79200 0.700 45.78000  ? 401 GOL   B C3     1 
HETATM 9291 O O3     . GOL   G 3 .   ? 9.09300   12.56900  -31.08700 0.700 70.88000  ? 401 GOL   B O3     1 
HETATM 9292 H H11    . GOL   G 3 .   ? 10.71400  12.79900  -27.28900 0.700 68.69000  ? 401 GOL   B H11    1 
HETATM 9293 H H12    . GOL   G 3 .   ? 9.62300   11.74800  -27.45500 0.700 68.69000  ? 401 GOL   B H12    1 
HETATM 9294 H HO1    . GOL   G 3 .   ? 10.92500  10.73700  -28.68300 0.700 79.28000  ? 401 GOL   B HO1    1 
HETATM 9295 H H2     . GOL   G 3 .   ? 8.95600   13.81600  -28.25400 0.700 69.29000  ? 401 GOL   B H2     1 
HETATM 9296 H HO2    . GOL   G 3 .   ? 11.15700  13.58500  -29.53600 0.700 89.18000  ? 401 GOL   B HO2    1 
HETATM 9297 H H31    . GOL   G 3 .   ? 7.66700   13.00600  -29.79200 0.700 54.93000  ? 401 GOL   B H31    1 
HETATM 9298 H H32    . GOL   G 3 .   ? 8.36600   11.64000  -29.51800 0.700 54.93000  ? 401 GOL   B H32    1 
HETATM 9299 H HO3    . GOL   G 3 .   ? 8.56400   12.17600  -31.62400 0.700 85.05000  ? 401 GOL   B HO3    1 
HETATM 9300 N N1     . FMN   H 2 .   ? 8.33300   24.10300  -40.04600 1.000 27.96000  ? 402 FMN   B N1     1 
HETATM 9301 C C2     . FMN   H 2 .   ? 9.61000   24.51000  -39.77800 1.000 33.41000  ? 402 FMN   B C2     1 
HETATM 9302 O O2     . FMN   H 2 .   ? 9.80400   25.37600  -38.92200 1.000 29.96000  ? 402 FMN   B O2     1 
HETATM 9303 N N3     . FMN   H 2 .   ? 10.67600  24.01200  -40.50400 1.000 29.14000  ? 402 FMN   B N3     1 
HETATM 9304 C C4     . FMN   H 2 .   ? 10.45800  23.06100  -41.49300 1.000 31.94000  ? 402 FMN   B C4     1 
HETATM 9305 O O4     . FMN   H 2 .   ? 11.40000  22.62000  -42.15800 1.000 35.06000  ? 402 FMN   B O4     1 
HETATM 9306 C C4A    . FMN   H 2 .   ? 9.16400   22.62900  -41.76500 1.000 32.26000  ? 402 FMN   B C4A    1 
HETATM 9307 N N5     . FMN   H 2 .   ? 8.93700   21.68400  -42.74900 1.000 31.24000  ? 402 FMN   B N5     1 
HETATM 9308 C C5A    . FMN   H 2 .   ? 7.63900   21.32300  -43.02600 1.000 33.53000  ? 402 FMN   B C5A    1 
HETATM 9309 C C6     . FMN   H 2 .   ? 7.41500   20.41100  -44.04300 1.000 32.34000  ? 402 FMN   B C6     1 
HETATM 9310 C C7     . FMN   H 2 .   ? 6.11000   20.04700  -44.31900 1.000 36.84000  ? 402 FMN   B C7     1 
HETATM 9311 C C7M    . FMN   H 2 .   ? 5.86900   19.04100  -45.41400 1.000 37.67000  ? 402 FMN   B C7M    1 
HETATM 9312 C C8     . FMN   H 2 .   ? 5.04900   20.58700  -43.58700 1.000 35.42000  ? 402 FMN   B C8     1 
HETATM 9313 C C8M    . FMN   H 2 .   ? 3.64700   20.16600  -43.89300 1.000 38.71000  ? 402 FMN   B C8M    1 
HETATM 9314 C C9     . FMN   H 2 .   ? 5.26200   21.53600  -42.58400 1.000 23.72000  ? 402 FMN   B C9     1 
HETATM 9315 C C9A    . FMN   H 2 .   ? 6.57700   21.86600  -42.28900 1.000 25.90000  ? 402 FMN   B C9A    1 
HETATM 9316 N N10    . FMN   H 2 .   ? 6.82500   22.77200  -41.28600 1.000 30.26000  ? 402 FMN   B N10    1 
HETATM 9317 C C10    . FMN   H 2 .   ? 8.11200   23.16100  -41.03300 1.000 29.60000  ? 402 FMN   B C10    1 
HETATM 9318 C "C1'"  . FMN   H 2 .   ? 5.71200   23.38100  -40.49100 1.000 30.06000  ? 402 FMN   B "C1'"  1 
HETATM 9319 C "C2'"  . FMN   H 2 .   ? 5.10200   24.58500  -41.20800 1.000 27.89000  ? 402 FMN   B "C2'"  1 
HETATM 9320 O "O2'"  . FMN   H 2 .   ? 6.10600   25.56200  -41.28000 1.000 27.36000  ? 402 FMN   B "O2'"  1 
HETATM 9321 C "C3'"  . FMN   H 2 .   ? 3.90200   25.13200  -40.42400 1.000 28.96000  ? 402 FMN   B "C3'"  1 
HETATM 9322 O "O3'"  . FMN   H 2 .   ? 4.31100   25.58000  -39.15900 1.000 28.14000  ? 402 FMN   B "O3'"  1 
HETATM 9323 C "C4'"  . FMN   H 2 .   ? 2.78200   24.09900  -40.25400 1.000 26.92000  ? 402 FMN   B "C4'"  1 
HETATM 9324 O "O4'"  . FMN   H 2 .   ? 2.65000   23.34600  -41.43800 1.000 29.30000  ? 402 FMN   B "O4'"  1 
HETATM 9325 C "C5'"  . FMN   H 2 .   ? 1.44300   24.76800  -39.91400 1.000 27.14000  ? 402 FMN   B "C5'"  1 
HETATM 9326 O "O5'"  . FMN   H 2 .   ? 1.04800   25.59100  -41.00300 1.000 26.27000  ? 402 FMN   B "O5'"  1 
HETATM 9327 P P      . FMN   H 2 .   ? -0.12800  25.18400  -42.02400 1.000 26.66000  ? 402 FMN   B P      1 
HETATM 9328 O O1P    . FMN   H 2 .   ? 0.36200   23.94100  -42.76200 1.000 26.44000  ? 402 FMN   B O1P    1 
HETATM 9329 O O2P    . FMN   H 2 .   ? -1.40400  24.91100  -41.28500 1.000 27.18000  ? 402 FMN   B O2P    1 
HETATM 9330 O O3P    . FMN   H 2 .   ? -0.34600  26.32300  -42.98200 1.000 26.80000  ? 402 FMN   B O3P    1 
HETATM 9331 H HN3    . FMN   H 2 .   ? 11.64700  24.23000  -40.20500 1.000 29.14000  ? 402 FMN   B HN3    1 
HETATM 9332 H H6     . FMN   H 2 .   ? 8.24100   19.81600  -44.43400 1.000 32.34000  ? 402 FMN   B H6     1 
HETATM 9333 H HM71   . FMN   H 2 .   ? 4.90300   19.20600  -45.88900 1.000 37.67000  ? 402 FMN   B HM71   1 
HETATM 9334 H HM72   . FMN   H 2 .   ? 5.89100   18.03800  -44.98900 1.000 37.67000  ? 402 FMN   B HM72   1 
HETATM 9335 H HM73   . FMN   H 2 .   ? 6.65600   19.13100  -46.16300 1.000 37.67000  ? 402 FMN   B HM73   1 
HETATM 9336 H HM81   . FMN   H 2 .   ? 2.96800   20.61700  -43.16900 1.000 38.71000  ? 402 FMN   B HM81   1 
HETATM 9337 H HM82   . FMN   H 2 .   ? 3.57100   19.08000  -43.83600 1.000 38.71000  ? 402 FMN   B HM82   1 
HETATM 9338 H HM83   . FMN   H 2 .   ? 3.37700   20.49900  -44.89500 1.000 38.71000  ? 402 FMN   B HM83   1 
HETATM 9339 H H9     . FMN   H 2 .   ? 4.45500   22.21700  -42.31400 1.000 23.72000  ? 402 FMN   B H9     1 
HETATM 9340 H "H1'1" . FMN   H 2 .   ? 6.07500   23.70300  -39.51700 1.000 30.06000  ? 402 FMN   B "H1'1" 1 
HETATM 9341 H "H1'2" . FMN   H 2 .   ? 4.94500   22.63300  -40.29600 1.000 30.06000  ? 402 FMN   B "H1'2" 1 
HETATM 9342 H "H2'"  . FMN   H 2 .   ? 4.78300   24.29300  -42.20800 1.000 27.89000  ? 402 FMN   B "H2'"  1 
HETATM 9343 H "HO2'" . FMN   H 2 .   ? 5.77700   26.39300  -40.87900 1.000 27.36000  ? 402 FMN   B "HO2'" 1 
HETATM 9344 H "H3'"  . FMN   H 2 .   ? 3.49600   25.96600  -40.99300 1.000 28.96000  ? 402 FMN   B "H3'"  1 
HETATM 9345 H "HO3'" . FMN   H 2 .   ? 3.70600   25.21800  -38.47800 1.000 28.14000  ? 402 FMN   B "HO3'" 1 
HETATM 9346 H "H4'"  . FMN   H 2 .   ? 3.04700   23.43600  -39.43100 1.000 26.92000  ? 402 FMN   B "H4'"  1 
HETATM 9347 H "HO4'" . FMN   H 2 .   ? 1.71400   23.34600  -41.72600 1.000 29.30000  ? 402 FMN   B "HO4'" 1 
HETATM 9348 H "H5'1" . FMN   H 2 .   ? 1.54800   25.37100  -39.01200 1.000 27.14000  ? 402 FMN   B "H5'1" 1 
HETATM 9349 H "H5'2" . FMN   H 2 .   ? 0.68500   24.00700  -39.73000 1.000 27.14000  ? 402 FMN   B "H5'2" 1 
HETATM 9350 C C1     . GOL   I 3 .   ? 20.40900  20.14000  -26.00600 1.000 67.72000  ? 403 GOL   B C1     1 
HETATM 9351 O O1     . GOL   I 3 .   ? 19.78600  19.89800  -27.24500 1.000 59.78000  ? 403 GOL   B O1     1 
HETATM 9352 C C2     . GOL   I 3 .   ? 21.88300  20.31500  -26.28800 1.000 58.27000  ? 403 GOL   B C2     1 
HETATM 9353 O O2     . GOL   I 3 .   ? 22.27500  19.24100  -27.12100 1.000 73.95000  ? 403 GOL   B O2     1 
HETATM 9354 C C3     . GOL   I 3 .   ? 22.12500  21.63700  -26.98000 1.000 55.72000  ? 403 GOL   B C3     1 
HETATM 9355 O O3     . GOL   I 3 .   ? 23.49500  21.96400  -26.87100 1.000 69.23000  ? 403 GOL   B O3     1 
HETATM 9356 H H11    . GOL   I 3 .   ? 20.27100  19.42600  -25.36400 1.000 81.27000  ? 403 GOL   B H11    1 
HETATM 9357 H H12    . GOL   I 3 .   ? 20.07600  20.96100  -25.62100 1.000 81.27000  ? 403 GOL   B H12    1 
HETATM 9358 H HO1    . GOL   I 3 .   ? 18.95400  19.79600  -27.10600 1.000 71.74000  ? 403 GOL   B HO1    1 
HETATM 9359 H H2     . GOL   I 3 .   ? 22.36700  20.30900  -25.44800 1.000 69.92000  ? 403 GOL   B H2     1 
HETATM 9360 H HO2    . GOL   I 3 .   ? 23.07500  19.38800  -27.36900 1.000 88.74000  ? 403 GOL   B HO2    1 
HETATM 9361 H H31    . GOL   I 3 .   ? 21.51700  22.34000  -26.71600 1.000 66.86000  ? 403 GOL   B H31    1 
HETATM 9362 H H32    . GOL   I 3 .   ? 21.89200  21.41700  -27.88900 1.000 66.86000  ? 403 GOL   B H32    1 
HETATM 9363 H HO3    . GOL   I 3 .   ? 23.94300  21.24300  -26.82100 1.000 83.08000  ? 403 GOL   B HO3    1 
HETATM 9364 C C02    . A1AVS J 4 .   ? 7.18200   19.74600  -39.07700 0.870 31.87000  ? 404 A1AVS B C02    1 
HETATM 9365 C C04    . A1AVS J 4 .   ? 9.26200   20.98500  -38.76300 0.870 40.12000  ? 404 A1AVS B C04    1 
HETATM 9366 C C05    . A1AVS J 4 .   ? 10.20500  19.87000  -39.21800 0.870 45.77000  ? 404 A1AVS B C05    1 
HETATM 9367 C C06    . A1AVS J 4 .   ? 11.48600  19.84400  -38.37600 0.870 55.21000  ? 404 A1AVS B C06    1 
HETATM 9368 C C14    . A1AVS J 4 .   ? 12.87700  19.94000  -39.05800 0.870 50.50000  ? 404 A1AVS B C14    1 
HETATM 9369 C C15    . A1AVS J 4 .   ? 13.05600  20.34100  -40.31000 0.870 50.12000  ? 404 A1AVS B C15    1 
HETATM 9370 C C16    . A1AVS J 4 .   ? 14.46400  20.44700  -40.89600 0.870 51.16000  ? 404 A1AVS B C16    1 
HETATM 9371 C C17    . A1AVS J 4 .   ? 15.52800  20.15900  -40.17900 0.870 55.23000  ? 404 A1AVS B C17    1 
HETATM 9372 C C18    . A1AVS J 4 .   ? 15.34700  19.71900  -38.73000 0.870 57.84000  ? 404 A1AVS B C18    1 
HETATM 9373 C C19    . A1AVS J 4 .   ? 14.13200  19.62800  -38.21600 0.870 63.65000  ? 404 A1AVS B C19    1 
HETATM 9374 C C22    . A1AVS J 4 .   ? 9.38600   18.59400  -39.49900 0.870 52.99000  ? 404 A1AVS B C22    1 
HETATM 9375 N N03    . A1AVS J 4 .   ? 7.83600   20.91700  -38.74000 0.870 32.07000  ? 404 A1AVS B N03    1 
HETATM 9376 N N21    . A1AVS J 4 .   ? 7.92500   18.60700  -39.46400 0.870 42.49000  ? 404 A1AVS B N21    1 
HETATM 9377 O O01    . A1AVS J 4 .   ? 6.01200   19.76200  -39.00400 0.870 35.99000  ? 404 A1AVS B O01    1 
HETATM 9378 O O20    . A1AVS J 4 .   ? 9.68000   22.01100  -38.49400 0.870 35.58000  ? 404 A1AVS B O20    1 
HETATM 9379 O O23    . A1AVS J 4 .   ? 9.91800   17.59900  -39.84400 0.870 49.92000  ? 404 A1AVS B O23    1 
HETATM 9380 H H051   . A1AVS J 4 .   ? 10.45700  20.16300  -40.10100 0.870 54.92000  ? 404 A1AVS B H051   1 
HETATM 9381 H H061   . A1AVS J 4 .   ? 11.49200  20.66600  -37.87800 0.870 66.26000  ? 404 A1AVS B H061   1 
HETATM 9382 H H151   . A1AVS J 4 .   ? 12.33300  20.54700  -40.85000 0.870 60.14000  ? 404 A1AVS B H151   1 
HETATM 9383 H H161   . A1AVS J 4 .   ? 14.57200  20.70600  -41.77500 0.870 61.39000  ? 404 A1AVS B H161   1 
HETATM 9384 H H171   . A1AVS J 4 .   ? 16.37900  20.22400  -40.55000 0.870 66.28000  ? 404 A1AVS B H171   1 
HETATM 9385 H H181   . A1AVS J 4 .   ? 16.09100  19.51600  -38.21000 0.870 69.41000  ? 404 A1AVS B H181   1 
HETATM 9386 H H191   . A1AVS J 4 .   ? 14.05700  19.36200  -37.33200 0.870 76.38000  ? 404 A1AVS B H191   1 
HETATM 9387 H H031   . A1AVS J 4 .   ? 7.38000   21.60700  -38.50900 0.870 38.48000  ? 404 A1AVS B H031   1 
HETATM 9388 H H211   . A1AVS J 4 .   ? 7.50100   17.88200  -39.65100 0.870 50.99000  ? 404 A1AVS B H211   1 
HETATM 9389 O O      . HOH   K 5 .   ? -28.87400 10.05100  -36.57100 1.000 64.32000  ? 501 HOH   A O      1 
HETATM 9390 O O      . HOH   K 5 .   ? -21.80500 21.61200  -32.35400 1.000 65.23000  ? 502 HOH   A O      1 
HETATM 9391 O O      . HOH   K 5 .   ? -11.99500 26.36000  -38.27200 1.000 46.61000  ? 503 HOH   A O      1 
HETATM 9392 O O      . HOH   K 5 .   ? -13.80800 -1.76800  -28.59300 1.000 45.39000  ? 504 HOH   A O      1 
HETATM 9393 O O      . HOH   K 5 .   ? -18.73700 35.84700  -39.28900 1.000 57.14000  ? 505 HOH   A O      1 
HETATM 9394 O O      . HOH   K 5 .   ? -3.57100  -5.39600  -30.35600 1.000 46.32000  ? 506 HOH   A O      1 
HETATM 9395 O O      . HOH   K 5 .   ? -1.27500  12.29700  -2.78000  1.000 58.44000  ? 507 HOH   A O      1 
HETATM 9396 O O      . HOH   K 5 .   ? -17.94000 13.93700  -31.65500 1.000 37.37000  ? 508 HOH   A O      1 
HETATM 9397 O O      . HOH   K 5 .   ? -14.53400 -8.55500  -29.06700 1.000 48.89000  ? 509 HOH   A O      1 
HETATM 9398 O O      . HOH   K 5 .   ? -24.69800 -1.93800  -22.59400 1.000 45.44000  ? 510 HOH   A O      1 
HETATM 9399 O O      . HOH   K 5 .   ? -24.74200 -6.14600  -28.92500 1.000 51.82000  ? 511 HOH   A O      1 
HETATM 9400 O O      . HOH   K 5 .   ? -21.34000 -12.83900 -27.45600 1.000 47.70000  ? 512 HOH   A O      1 
HETATM 9401 O O      . HOH   K 5 .   ? -15.55700 11.32400  -20.92800 1.000 41.65000  ? 513 HOH   A O      1 
HETATM 9402 O O      . HOH   K 5 .   ? -7.79800  23.85200  -16.80800 1.000 55.18000  ? 514 HOH   A O      1 
HETATM 9403 O O      . HOH   K 5 .   ? -25.30800 5.70900   -42.13300 1.000 57.52000  ? 515 HOH   A O      1 
HETATM 9404 O O      . HOH   K 5 .   ? -15.32900 2.82000   -9.65400  1.000 50.10000  ? 516 HOH   A O      1 
HETATM 9405 O O      . HOH   K 5 .   ? -13.61700 32.15100  -28.75700 1.000 44.25000  ? 517 HOH   A O      1 
HETATM 9406 O O      . HOH   K 5 .   ? -12.68800 7.80600   -40.43300 1.000 52.79000  ? 518 HOH   A O      1 
HETATM 9407 O O      . HOH   K 5 .   ? -8.42800  -0.92300  -24.66000 1.000 32.57000  ? 519 HOH   A O      1 
HETATM 9408 O O      . HOH   K 5 .   ? -14.27800 12.76000  -17.06200 1.000 44.73000  ? 520 HOH   A O      1 
HETATM 9409 O O      . HOH   K 5 .   ? -21.49000 20.27600  -20.02500 1.000 51.48000  ? 521 HOH   A O      1 
HETATM 9410 O O      . HOH   K 5 .   ? 8.66100   6.48300   -26.54200 1.000 51.58000  ? 522 HOH   A O      1 
HETATM 9411 O O      . HOH   K 5 .   ? -27.57700 -1.89700  -23.11900 1.000 61.14000  ? 523 HOH   A O      1 
HETATM 9412 O O      . HOH   K 5 .   ? -23.54200 14.43300  -35.64400 1.000 56.45000  ? 524 HOH   A O      1 
HETATM 9413 O O      . HOH   K 5 .   ? -7.62900  18.87800  -22.15500 1.000 42.66000  ? 525 HOH   A O      1 
HETATM 9414 O O      . HOH   K 5 .   ? -19.98900 -2.37000  -12.69600 1.000 50.41000  ? 526 HOH   A O      1 
HETATM 9415 O O      . HOH   K 5 .   ? -10.65900 -14.42500 -35.00900 1.000 46.82000  ? 527 HOH   A O      1 
HETATM 9416 O O      . HOH   K 5 .   ? -0.37600  -2.38500  -33.80800 1.000 53.12000  ? 528 HOH   A O      1 
HETATM 9417 O O      . HOH   K 5 .   ? -6.07800  16.54600  -34.13400 1.000 31.96000  ? 529 HOH   A O      1 
HETATM 9418 O O      . HOH   K 5 .   ? -13.91900 7.61500   -42.72600 1.000 51.39000  ? 530 HOH   A O      1 
HETATM 9419 O O      . HOH   K 5 .   ? -16.03400 11.99800  -39.79900 1.000 56.18000  ? 531 HOH   A O      1 
HETATM 9420 O O      . HOH   K 5 .   ? 5.86000   2.45400   -14.39000 1.000 46.46000  ? 532 HOH   A O      1 
HETATM 9421 O O      . HOH   K 5 .   ? -13.49800 13.32300  -37.45400 1.000 35.87000  ? 533 HOH   A O      1 
HETATM 9422 O O      . HOH   K 5 .   ? -15.49000 11.49100  -30.11400 1.000 34.76000  ? 534 HOH   A O      1 
HETATM 9423 O O      . HOH   K 5 .   ? -11.31700 14.87600  -38.31200 1.000 35.37000  ? 535 HOH   A O      1 
HETATM 9424 O O      . HOH   K 5 .   ? 0.86000   3.35900   -34.54300 1.000 40.50000  ? 536 HOH   A O      1 
HETATM 9425 O O      . HOH   K 5 .   ? -14.80600 -7.87200  -25.27000 1.000 45.04000  ? 537 HOH   A O      1 
HETATM 9426 O O      . HOH   K 5 .   ? -0.96200  13.74200  -30.19600 1.000 32.63000  ? 538 HOH   A O      1 
HETATM 9427 O O      . HOH   K 5 .   ? -1.55700  15.55600  -32.24300 1.000 30.67000  ? 539 HOH   A O      1 
HETATM 9428 O O      . HOH   K 5 .   ? -24.95600 18.70500  -23.49100 1.000 53.85000  ? 540 HOH   A O      1 
HETATM 9429 O O      . HOH   K 5 .   ? -4.09100  11.47100  -23.56300 1.000 32.37000  ? 541 HOH   A O      1 
HETATM 9430 O O      . HOH   K 5 .   ? -19.06600 19.43800  -36.13700 1.000 49.87000  ? 542 HOH   A O      1 
HETATM 9431 O O      . HOH   K 5 .   ? -3.69900  26.69600  -27.87000 1.000 31.69000  ? 543 HOH   A O      1 
HETATM 9432 O O      . HOH   K 5 .   ? -23.78600 -6.49400  -31.40300 1.000 55.70000  ? 544 HOH   A O      1 
HETATM 9433 O O      . HOH   K 5 .   ? 0.11700   -1.48000  -18.11400 1.000 42.77000  ? 545 HOH   A O      1 
HETATM 9434 O O      . HOH   K 5 .   ? -14.19100 37.43300  -24.02600 1.000 58.25000  ? 546 HOH   A O      1 
HETATM 9435 O O      . HOH   K 5 .   ? -15.76000 8.85200   -41.77100 1.000 49.41000  ? 547 HOH   A O      1 
HETATM 9436 O O      . HOH   K 5 .   ? -17.31300 -7.45000  -30.46400 1.000 38.13000  ? 548 HOH   A O      1 
HETATM 9437 O O      . HOH   K 5 .   ? -30.04200 5.62000   -30.02200 1.000 52.95000  ? 549 HOH   A O      1 
HETATM 9438 O O      . HOH   K 5 .   ? -17.00800 0.45800   -9.63000  1.000 57.39000  ? 550 HOH   A O      1 
HETATM 9439 O O      . HOH   K 5 .   ? -7.295    -11.078   -35.369   1.000 52.50000  ? 551 HOH   A O      1 
HETATM 9440 O O      . HOH   K 5 .   ? -3.39100  -1.27600  -23.68900 1.000 38.12000  ? 552 HOH   A O      1 
HETATM 9441 O O      . HOH   K 5 .   ? -10.26300 -4.59900  -24.63400 1.000 48.42000  ? 553 HOH   A O      1 
HETATM 9442 O O      . HOH   K 5 .   ? -6.63600  -5.25100  -27.28400 1.000 43.21000  ? 554 HOH   A O      1 
HETATM 9443 O O      . HOH   K 5 .   ? -9.49000  25.67400  -22.69400 1.000 47.89000  ? 555 HOH   A O      1 
HETATM 9444 O O      . HOH   K 5 .   ? -15.64500 21.87100  -27.33300 1.000 39.16000  ? 556 HOH   A O      1 
HETATM 9445 O O      . HOH   K 5 .   ? -0.37700  -0.97500  -12.45400 1.000 43.38000  ? 557 HOH   A O      1 
HETATM 9446 O O      . HOH   K 5 .   ? -22.52300 0.27800   -13.97800 1.000 51.31000  ? 558 HOH   A O      1 
HETATM 9447 O O      . HOH   K 5 .   ? 9.95200   10.74100  -20.69700 1.000 48.95000  ? 559 HOH   A O      1 
HETATM 9448 O O      . HOH   K 5 .   ? -5.46800  20.31400  -23.40700 1.000 38.56000  ? 560 HOH   A O      1 
HETATM 9449 O O      . HOH   K 5 .   ? -5.96400  25.50100  -18.84700 1.000 56.14000  ? 561 HOH   A O      1 
HETATM 9450 O O      . HOH   K 5 .   ? -6.07900  -2.04900  -23.88300 1.000 40.66000  ? 562 HOH   A O      1 
HETATM 9451 O O      . HOH   K 5 .   ? -3.29400  -5.09100  -15.33500 1.000 39.37000  ? 563 HOH   A O      1 
HETATM 9452 O O      . HOH   K 5 .   ? -4.17700  -1.90800  -13.68500 1.000 45.31000  ? 564 HOH   A O      1 
HETATM 9453 O O      . HOH   K 5 .   ? -14.96400 -6.63300  -27.71300 1.000 39.01000  ? 565 HOH   A O      1 
HETATM 9454 O O      . HOH   K 5 .   ? -11.75700 31.64400  -35.65600 1.000 47.86000  ? 566 HOH   A O      1 
HETATM 9455 O O      . HOH   K 5 .   ? 3.03200   17.00200  -24.91400 1.000 43.22000  ? 567 HOH   A O      1 
HETATM 9456 O O      . HOH   K 5 .   ? -22.51500 2.29700   -43.69300 1.000 56.83000  ? 568 HOH   A O      1 
HETATM 9457 O O      . HOH   K 5 .   ? -0.16600  -2.98200  -26.14900 1.000 42.68000  ? 569 HOH   A O      1 
HETATM 9458 O O      . HOH   K 5 .   ? -0.92900  -0.90600  -31.73600 1.000 41.42000  ? 570 HOH   A O      1 
HETATM 9459 O O      . HOH   K 5 .   ? 2.47300   -3.30500  -25.37000 1.000 49.29000  ? 571 HOH   A O      1 
HETATM 9460 O O      . HOH   K 5 .   ? -3.60700  2.04600   -7.46400  1.000 40.26000  ? 572 HOH   A O      1 
HETATM 9461 O O      . HOH   K 5 .   ? -7.42700  19.74500  -14.74900 1.000 54.53000  ? 573 HOH   A O      1 
HETATM 9462 O O      . HOH   K 5 .   ? 5.40100   1.87300   -20.58600 1.000 59.40000  ? 574 HOH   A O      1 
HETATM 9463 O O      . HOH   K 5 .   ? -6.59900  -7.27700  -37.45200 1.000 58.01000  ? 575 HOH   A O      1 
HETATM 9464 O O      . HOH   K 5 .   ? -1.80400  -4.94400  -26.17300 1.000 43.05000  ? 576 HOH   A O      1 
HETATM 9465 O O      . HOH   K 5 .   ? -25.265   -6.617    -22.928   1.000 58.42000  ? 577 HOH   A O      1 
HETATM 9466 O O      . HOH   K 5 .   ? -2.157    -7.088    -23.162   1.000 51.98000  ? 578 HOH   A O      1 
HETATM 9467 O O      . HOH   K 5 .   ? 6.40100   4.32900   -21.27700 1.000 51.06000  ? 579 HOH   A O      1 
HETATM 9468 O O      . HOH   K 5 .   ? 6.22300   1.25000   -16.81600 1.000 54.82000  ? 580 HOH   A O      1 
HETATM 9469 O O      . HOH   K 5 .   ? -0.46900  2.12300   -5.65600  1.000 53.24000  ? 581 HOH   A O      1 
HETATM 9470 O O      . HOH   K 5 .   ? -14.25200 16.29900  -42.54400 1.000 62.24000  ? 582 HOH   A O      1 
HETATM 9471 O O      . HOH   K 5 .   ? -13.02900 14.49900  -41.55800 1.000 57.38000  ? 583 HOH   A O      1 
HETATM 9472 O O      . HOH   L 5 .   ? 30.633    33.403    -55.933   1.000 55.68000  ? 501 HOH   B O      1 
HETATM 9473 O O      . HOH   L 5 .   ? 10.95400  10.56300  -30.56600 1.000 74.37000  ? 502 HOH   B O      1 
HETATM 9474 O O      . HOH   L 5 .   ? 22.44800  39.68300  -54.65300 1.000 70.92000  ? 503 HOH   B O      1 
HETATM 9475 O O      . HOH   L 5 .   ? 2.26600   20.88000  -40.54500 1.000 47.73000  ? 504 HOH   B O      1 
HETATM 9476 O O      . HOH   L 5 .   ? 25.50300  22.36100  -27.87200 1.000 51.24000  ? 505 HOH   B O      1 
HETATM 9477 O O      . HOH   L 5 .   ? -9.75400  14.19300  -40.48200 1.000 51.17000  ? 506 HOH   B O      1 
HETATM 9478 O O      . HOH   L 5 .   ? -4.54500  30.00500  -56.88000 1.000 48.41000  ? 507 HOH   B O      1 
HETATM 9479 O O      . HOH   L 5 .   ? 27.42100  23.74500  -42.79300 1.000 48.30000  ? 508 HOH   B O      1 
HETATM 9480 O O      . HOH   L 5 .   ? -1.68200  18.18300  -48.95600 1.000 47.51000  ? 509 HOH   B O      1 
HETATM 9481 O O      . HOH   L 5 .   ? 3.16300   44.77100  -37.10100 1.000 42.70000  ? 510 HOH   B O      1 
HETATM 9482 O O      . HOH   L 5 .   ? 24.74200  22.30100  -48.24000 1.000 49.24000  ? 511 HOH   B O      1 
HETATM 9483 O O      . HOH   L 5 .   ? 12.53100  21.90000  -57.21000 1.000 49.13000  ? 512 HOH   B O      1 
HETATM 9484 O O      . HOH   L 5 .   ? -4.15200  33.77600  -60.15200 1.000 49.57000  ? 513 HOH   B O      1 
HETATM 9485 O O      . HOH   L 5 .   ? 18.22700  43.53600  -47.71600 1.000 48.61000  ? 514 HOH   B O      1 
HETATM 9486 O O      . HOH   L 5 .   ? 11.55000  27.87500  -38.86200 1.000 32.97000  ? 515 HOH   B O      1 
HETATM 9487 O O      . HOH   L 5 .   ? 14.23300  38.52700  -59.78900 1.000 55.90000  ? 516 HOH   B O      1 
HETATM 9488 O O      . HOH   L 5 .   ? -11.546   38.260    -54.197   1.000 60.62000  ? 517 HOH   B O      1 
HETATM 9489 O O      . HOH   L 5 .   ? -5.42000  20.04500  -46.86900 1.000 50.23000  ? 518 HOH   B O      1 
HETATM 9490 O O      . HOH   L 5 .   ? 9.24400   29.85900  -61.39800 1.000 68.08000  ? 519 HOH   B O      1 
HETATM 9491 O O      . HOH   L 5 .   ? 10.88000  18.40500  -42.11200 0.930 57.95000  ? 520 HOH   B O      1 
HETATM 9492 O O      . HOH   L 5 .   ? 8.00600   29.14200  -40.66600 1.000 29.89000  ? 521 HOH   B O      1 
HETATM 9493 O O      . HOH   L 5 .   ? 17.72300  27.32200  -44.32300 1.000 40.68000  ? 522 HOH   B O      1 
HETATM 9494 O O      . HOH   L 5 .   ? 29.94500  33.19100  -43.84100 1.000 49.18000  ? 523 HOH   B O      1 
HETATM 9495 O O      . HOH   L 5 .   ? 30.50200  35.68800  -37.18600 1.000 55.57000  ? 524 HOH   B O      1 
HETATM 9496 O O      . HOH   L 5 .   ? 0.86800   31.10800  -15.09200 1.000 55.80000  ? 525 HOH   B O      1 
HETATM 9497 O O      . HOH   L 5 .   ? 30.78800  24.58300  -48.67100 1.000 37.72000  ? 526 HOH   B O      1 
HETATM 9498 O O      . HOH   L 5 .   ? 10.34500  22.60100  -49.26200 1.000 38.35000  ? 527 HOH   B O      1 
HETATM 9499 O O      . HOH   L 5 .   ? 23.55600  28.18100  -23.73900 1.000 49.30000  ? 528 HOH   B O      1 
HETATM 9500 O O      . HOH   L 5 .   ? -12.03100 31.45200  -51.09300 1.000 39.97000  ? 529 HOH   B O      1 
HETATM 9501 O O      . HOH   L 5 .   ? 11.62400  10.48600  -26.35600 1.000 65.40000  ? 530 HOH   B O      1 
HETATM 9502 O O      . HOH   L 5 .   ? 1.37700   46.40100  -51.43900 1.000 52.26000  ? 531 HOH   B O      1 
HETATM 9503 O O      . HOH   L 5 .   ? -9.64600  4.03600   -46.87200 1.000 55.15000  ? 532 HOH   B O      1 
HETATM 9504 O O      . HOH   L 5 .   ? 3.34700   28.97800  -29.86800 1.000 32.07000  ? 533 HOH   B O      1 
HETATM 9505 O O      . HOH   L 5 .   ? 16.74300  43.02800  -43.62000 1.000 38.06000  ? 534 HOH   B O      1 
HETATM 9506 O O      . HOH   L 5 .   ? 3.95700   36.57900  -59.82900 1.000 53.49000  ? 535 HOH   B O      1 
HETATM 9507 O O      . HOH   L 5 .   ? -6.78100  23.77900  -33.71800 1.000 28.90000  ? 536 HOH   B O      1 
HETATM 9508 O O      . HOH   L 5 .   ? 7.57800   42.38600  -50.27400 1.000 30.00000  ? 537 HOH   B O      1 
HETATM 9509 O O      . HOH   L 5 .   ? -5.51400  24.82900  -28.87400 1.000 33.14000  ? 538 HOH   B O      1 
HETATM 9510 O O      . HOH   L 5 .   ? 6.03500   31.79400  -58.99900 1.000 41.38000  ? 539 HOH   B O      1 
HETATM 9511 O O      . HOH   L 5 .   ? -11.85800 32.13400  -41.24300 1.000 46.88000  ? 540 HOH   B O      1 
HETATM 9512 O O      . HOH   L 5 .   ? -12.61400 31.28100  -44.91900 1.000 48.41000  ? 541 HOH   B O      1 
HETATM 9513 O O      . HOH   L 5 .   ? -5.65000  -4.92000  -38.72300 1.000 52.81000  ? 542 HOH   B O      1 
HETATM 9514 O O      . HOH   L 5 .   ? 14.26300  43.33400  -49.55600 1.000 38.85000  ? 543 HOH   B O      1 
HETATM 9515 O O      . HOH   L 5 .   ? -3.08200  47.69000  -34.64100 1.000 44.93000  ? 544 HOH   B O      1 
HETATM 9516 O O      . HOH   L 5 .   ? 5.54000   21.53200  -33.02200 1.000 37.68000  ? 545 HOH   B O      1 
HETATM 9517 O O      . HOH   L 5 .   ? -0.17300  8.06300   -40.02900 1.000 41.09000  ? 546 HOH   B O      1 
HETATM 9518 O O      . HOH   L 5 .   ? 17.65400  21.14300  -31.61200 1.000 52.46000  ? 547 HOH   B O      1 
HETATM 9519 O O      . HOH   L 5 .   ? -1.13900  47.90200  -44.36900 1.000 32.13000  ? 548 HOH   B O      1 
HETATM 9520 O O      . HOH   L 5 .   ? 0.87700   23.46800  -23.35800 1.000 42.41000  ? 549 HOH   B O      1 
HETATM 9521 O O      . HOH   L 5 .   ? 12.72900  46.25700  -47.36800 1.000 53.49000  ? 550 HOH   B O      1 
HETATM 9522 O O      . HOH   L 5 .   ? 5.81700   49.94200  -38.44100 1.000 42.62000  ? 551 HOH   B O      1 
HETATM 9523 O O      . HOH   L 5 .   ? 3.16100   41.68100  -29.18500 1.000 36.74000  ? 552 HOH   B O      1 
HETATM 9524 O O      . HOH   L 5 .   ? -0.96700  39.34200  -54.97400 1.000 41.55000  ? 553 HOH   B O      1 
HETATM 9525 O O      . HOH   L 5 .   ? 18.75000  38.03800  -38.50500 1.000 31.21000  ? 554 HOH   B O      1 
HETATM 9526 O O      . HOH   L 5 .   ? -8.76400  27.14600  -41.56600 1.000 38.76000  ? 555 HOH   B O      1 
HETATM 9527 O O      . HOH   L 5 .   ? -10.55100 28.08600  -44.25500 1.000 47.17000  ? 556 HOH   B O      1 
HETATM 9528 O O      . HOH   L 5 .   ? -1.14900  28.84100  -42.30500 1.000 27.74000  ? 557 HOH   B O      1 
HETATM 9529 O O      . HOH   L 5 .   ? 15.71500  42.93500  -40.56000 1.000 48.63000  ? 558 HOH   B O      1 
HETATM 9530 O O      . HOH   L 5 .   ? 22.50800  44.05600  -36.27100 1.000 55.45000  ? 559 HOH   B O      1 
HETATM 9531 O O      . HOH   L 5 .   ? 8.28700   15.18000  -30.87300 1.000 50.00000  ? 560 HOH   B O      1 
HETATM 9532 O O      . HOH   L 5 .   ? 15.62700  42.94600  -47.37200 1.000 39.12000  ? 561 HOH   B O      1 
HETATM 9533 O O      . HOH   L 5 .   ? -2.22300  26.19500  -44.97900 1.000 31.28000  ? 562 HOH   B O      1 
HETATM 9534 O O      . HOH   L 5 .   ? 9.39600   44.23200  -50.38200 1.000 45.87000  ? 563 HOH   B O      1 
HETATM 9535 O O      . HOH   L 5 .   ? 7.55800   3.15800   -38.21400 1.000 52.58000  ? 564 HOH   B O      1 
HETATM 9536 O O      . HOH   L 5 .   ? 27.90100  28.41800  -48.64200 1.000 43.23000  ? 565 HOH   B O      1 
HETATM 9537 O O      . HOH   L 5 .   ? 7.52200   11.76300  -36.68500 1.000 60.55000  ? 566 HOH   B O      1 
HETATM 9538 O O      . HOH   L 5 .   ? 29.25300  41.64700  -43.72800 1.000 58.68000  ? 567 HOH   B O      1 
HETATM 9539 O O      . HOH   L 5 .   ? 1.44800   34.62700  -56.49000 1.000 31.99000  ? 568 HOH   B O      1 
HETATM 9540 O O      . HOH   L 5 .   ? 17.04700  20.34200  -20.41700 1.000 58.75000  ? 569 HOH   B O      1 
HETATM 9541 O O      . HOH   L 5 .   ? -4.44200  27.50800  -18.60100 1.000 54.00000  ? 570 HOH   B O      1 
HETATM 9542 O O      . HOH   L 5 .   ? -7.36100  42.82900  -28.49500 1.000 49.10000  ? 571 HOH   B O      1 
HETATM 9543 O O      . HOH   L 5 .   ? -4.59300  32.91100  -57.72500 1.000 44.71000  ? 572 HOH   B O      1 
HETATM 9544 O O      . HOH   L 5 .   ? -10.55300 47.58800  -35.43700 1.000 57.23000  ? 573 HOH   B O      1 
HETATM 9545 O O      . HOH   L 5 .   ? -4.57500  39.45000  -56.55400 1.000 42.77000  ? 574 HOH   B O      1 
HETATM 9546 O O      . HOH   L 5 .   ? -8.55900  37.14600  -26.94400 1.000 39.10000  ? 575 HOH   B O      1 
HETATM 9547 O O      . HOH   L 5 .   ? 3.96100   29.58300  -15.63900 1.000 49.18000  ? 576 HOH   B O      1 
HETATM 9548 O O      . HOH   L 5 .   ? 0.40800   45.60300  -33.30400 1.000 34.38000  ? 577 HOH   B O      1 
HETATM 9549 O O      . HOH   L 5 .   ? 7.81500   42.06300  -24.77700 1.000 41.84000  ? 578 HOH   B O      1 
HETATM 9550 O O      . HOH   L 5 .   ? 3.320     53.286    -48.073   1.000 52.63000  ? 579 HOH   B O      1 
HETATM 9551 O O      . HOH   L 5 .   ? 9.66000   34.13500  -40.83000 1.000 43.16000  ? 580 HOH   B O      1 
HETATM 9552 O O      . HOH   L 5 .   ? 1.78400   18.35700  -41.78400 1.000 29.26000  ? 581 HOH   B O      1 
HETATM 9553 O O      . HOH   L 5 .   ? -3.60600  46.06200  -31.08000 1.000 46.74000  ? 582 HOH   B O      1 
HETATM 9554 O O      . HOH   L 5 .   ? 2.82100   41.47600  -34.18800 1.000 30.91000  ? 583 HOH   B O      1 
HETATM 9555 O O      . HOH   L 5 .   ? 11.04000  5.74600   -37.61300 1.000 60.66000  ? 584 HOH   B O      1 
HETATM 9556 O O      . HOH   L 5 .   ? -9.79800  42.27300  -53.83100 1.000 44.64000  ? 585 HOH   B O      1 
HETATM 9557 O O      . HOH   L 5 .   ? 18.80400  22.12400  -20.71200 1.000 58.12000  ? 586 HOH   B O      1 
HETATM 9558 O O      . HOH   L 5 .   ? -7.25500  12.18400  -47.15000 1.000 56.21000  ? 587 HOH   B O      1 
HETATM 9559 O O      . HOH   L 5 .   ? 21.67500  37.47200  -53.03900 1.000 47.01000  ? 588 HOH   B O      1 
HETATM 9560 O O      . HOH   L 5 .   ? 0.95000   46.82200  -41.59200 1.000 35.98000  ? 589 HOH   B O      1 
HETATM 9561 O O      . HOH   L 5 .   ? 9.53000   20.85500  -51.18300 1.000 51.10000  ? 590 HOH   B O      1 
HETATM 9562 O O      . HOH   L 5 .   ? 13.49600  22.14500  -33.97100 1.000 52.30000  ? 591 HOH   B O      1 
HETATM 9563 O O      . HOH   L 5 .   ? 0.02000   43.43000  -26.86800 1.000 40.34000  ? 592 HOH   B O      1 
HETATM 9564 O O      . HOH   L 5 .   ? 6.79900   21.76800  -50.45400 1.000 40.89000  ? 593 HOH   B O      1 
HETATM 9565 O O      . HOH   L 5 .   ? -11.45700 50.31700  -47.12600 1.000 49.00000  ? 594 HOH   B O      1 
HETATM 9566 O O      . HOH   L 5 .   ? 4.03900   27.19700  -57.48900 1.000 41.27000  ? 595 HOH   B O      1 
HETATM 9567 O O      . HOH   L 5 .   ? 15.29500  33.29400  -56.34500 1.000 43.79000  ? 596 HOH   B O      1 
HETATM 9568 O O      . HOH   L 5 .   ? 3.60900   23.94300  -53.49400 1.000 47.26000  ? 597 HOH   B O      1 
HETATM 9569 O O      . HOH   L 5 .   ? 3.80300   20.15500  -30.99000 1.000 33.49000  ? 598 HOH   B O      1 
HETATM 9570 O O      . HOH   L 5 .   ? 18.80600  27.06200  -19.10300 1.000 52.77000  ? 599 HOH   B O      1 
HETATM 9571 O O      . HOH   L 5 .   ? 5.28900   14.87600  -34.94600 1.000 41.16000  ? 600 HOH   B O      1 
HETATM 9572 O O      . HOH   L 5 .   ? 6.30100   11.16400  -49.06300 1.000 56.32000  ? 601 HOH   B O      1 
HETATM 9573 O O      . HOH   L 5 .   ? -0.68100  48.99400  -41.60200 1.000 36.47000  ? 602 HOH   B O      1 
HETATM 9574 O O      . HOH   L 5 .   ? 3.30800   47.93100  -40.57400 1.000 38.14000  ? 603 HOH   B O      1 
HETATM 9575 O O      . HOH   L 5 .   ? 26.12700  22.20100  -45.77500 1.000 43.52000  ? 604 HOH   B O      1 
HETATM 9576 O O      . HOH   L 5 .   ? 15.85600  40.22600  -46.33900 1.000 31.23000  ? 605 HOH   B O      1 
HETATM 9577 O O      . HOH   L 5 .   ? 20.66200  42.99400  -50.27000 1.000 49.30000  ? 606 HOH   B O      1 
HETATM 9578 O O      . HOH   L 5 .   ? 16.11600  21.87700  -33.91700 1.000 74.90000  ? 607 HOH   B O      1 
HETATM 9579 O O      . HOH   L 5 .   ? -1.89000  33.93200  -17.70600 1.000 54.08000  ? 608 HOH   B O      1 
HETATM 9580 O O      . HOH   L 5 .   ? -9.82900  25.49800  -39.60000 1.000 34.53000  ? 609 HOH   B O      1 
HETATM 9581 O O      . HOH   L 5 .   ? 15.91500  35.56800  -56.50700 1.000 52.58000  ? 610 HOH   B O      1 
HETATM 9582 O O      . HOH   L 5 .   ? -12.83000 44.19400  -26.63900 1.000 61.87000  ? 611 HOH   B O      1 
HETATM 9583 O O      . HOH   L 5 .   ? 10.16600  19.95800  -46.27700 1.000 37.60000  ? 612 HOH   B O      1 
HETATM 9584 O O      . HOH   L 5 .   ? -12.58900 37.43800  -48.71600 1.000 39.55000  ? 613 HOH   B O      1 
HETATM 9585 O O      . HOH   L 5 .   ? -7.15500  8.50000   -39.25900 1.000 50.24000  ? 614 HOH   B O      1 
HETATM 9586 O O      . HOH   L 5 .   ? 17.23600  24.06400  -33.57000 1.000 48.74000  ? 615 HOH   B O      1 
HETATM 9587 O O      . HOH   L 5 .   ? 10.78100  16.26400  -32.32500 1.000 53.12000  ? 616 HOH   B O      1 
HETATM 9588 O O      . HOH   L 5 .   ? 9.74600   30.93400  -17.47100 1.000 51.14000  ? 617 HOH   B O      1 
HETATM 9589 O O      . HOH   L 5 .   ? 3.29800   42.58600  -31.89300 1.000 39.14000  ? 618 HOH   B O      1 
HETATM 9590 O O      . HOH   L 5 .   ? 11.27500  28.46700  -60.60000 1.000 51.96000  ? 619 HOH   B O      1 
HETATM 9591 O O      . HOH   L 5 .   ? -4.69400  44.91000  -28.43600 1.000 53.02000  ? 620 HOH   B O      1 
HETATM 9592 O O      . HOH   L 5 .   ? 27.36500  30.54700  -28.22300 1.000 46.52000  ? 621 HOH   B O      1 
HETATM 9593 O O      . HOH   L 5 .   ? 16.50200  23.71400  -58.31100 1.000 37.46000  ? 622 HOH   B O      1 
HETATM 9594 O O      . HOH   L 5 .   ? -5.24900  25.22000  -51.34100 1.000 52.56000  ? 623 HOH   B O      1 
HETATM 9595 O O      . HOH   L 5 .   ? 0.95400   42.79500  -52.70900 1.000 39.22000  ? 624 HOH   B O      1 
HETATM 9596 O O      . HOH   L 5 .   ? 25.84700  41.45000  -29.79300 1.000 52.57000  ? 625 HOH   B O      1 
HETATM 9597 O O      . HOH   L 5 .   ? 19.54900  41.67000  -54.49600 1.000 44.73000  ? 626 HOH   B O      1 
HETATM 9598 O O      . HOH   L 5 .   ? 18.49300  23.52300  -56.43800 1.000 37.47000  ? 627 HOH   B O      1 
HETATM 9599 O O      . HOH   L 5 .   ? -9.46900  6.20600   -44.29500 1.000 47.52000  ? 628 HOH   B O      1 
HETATM 9600 O O      . HOH   L 5 .   ? 19.01500  38.35000  -26.80600 1.000 32.63000  ? 629 HOH   B O      1 
HETATM 9601 O O      . HOH   L 5 .   ? 19.59900  16.23600  -51.54500 1.000 48.56000  ? 630 HOH   B O      1 
HETATM 9602 O O      . HOH   L 5 .   ? 19.45200  39.50000  -21.10500 1.000 67.52000  ? 631 HOH   B O      1 
HETATM 9603 O O      . HOH   L 5 .   ? 7.92100   39.20200  -19.15600 1.000 43.03000  ? 632 HOH   B O      1 
HETATM 9604 O O      . HOH   L 5 .   ? -4.54200  41.58200  -54.74500 1.000 45.95000  ? 633 HOH   B O      1 
HETATM 9605 O O      . HOH   L 5 .   ? 23.79900  18.10400  -40.08400 1.000 47.16000  ? 634 HOH   B O      1 
HETATM 9606 O O      . HOH   L 5 .   ? -1.41400  12.26800  -49.96700 1.000 47.10000  ? 635 HOH   B O      1 
HETATM 9607 O O      . HOH   L 5 .   ? -13.454   27.069    -46.476   1.000 49.26000  ? 636 HOH   B O      1 
HETATM 9608 O O      . HOH   L 5 .   ? 16.00400  19.74400  -35.32600 1.000 59.20000  ? 637 HOH   B O      1 
HETATM 9609 O O      . HOH   L 5 .   ? 9.92800   43.85600  -58.08000 1.000 61.55000  ? 638 HOH   B O      1 
HETATM 9610 O O      . HOH   L 5 .   ? -1.52500  46.18000  -51.13000 1.000 48.12000  ? 639 HOH   B O      1 
HETATM 9611 O O      . HOH   L 5 .   ? 16.162    17.818    -55.290   1.000 56.81000  ? 640 HOH   B O      1 
HETATM 9612 O O      . HOH   L 5 .   ? 22.17900  27.96900  -53.44300 1.000 52.52000  ? 641 HOH   B O      1 
HETATM 9613 O O      . HOH   L 5 .   ? 26.98400  38.45500  -30.99500 1.000 60.98000  ? 642 HOH   B O      1 
HETATM 9614 O O      . HOH   L 5 .   ? 12.86600  20.95100  -31.77200 1.000 49.77000  ? 643 HOH   B O      1 
HETATM 9615 O O      . HOH   L 5 .   ? -5.37400  41.19700  -28.01600 1.000 50.43000  ? 644 HOH   B O      1 
HETATM 9616 O O      . HOH   L 5 .   ? 11.88300  19.85300  -52.51900 1.000 59.92000  ? 645 HOH   B O      1 
HETATM 9617 O O      . HOH   L 5 .   ? 25.23100  43.15400  -31.24000 1.000 58.27000  ? 646 HOH   B O      1 
HETATM 9618 O O      . HOH   L 5 .   ? -11.86000 34.90300  -47.82700 1.000 38.65000  ? 647 HOH   B O      1 
HETATM 9619 O O      . HOH   L 5 .   ? -13.45800 37.26100  -51.27800 1.000 53.63000  ? 648 HOH   B O      1 
HETATM 9620 O O      . HOH   L 5 .   ? 12.37200  44.02700  -58.50200 1.000 54.31000  ? 649 HOH   B O      1 
HETATM 9621 O O      . HOH   L 5 .   ? -9.952    27.977    -49.470   1.000 39.28000  ? 650 HOH   B O      1 
HETATM 9622 O O      . HOH   L 5 .   ? 23.978    39.312    -26.662   1.000 54.34000  ? 651 HOH   B O      1 
HETATM 9623 O O      . HOH   L 5 .   ? -2.24000  46.54700  -28.85400 1.000 53.10000  ? 652 HOH   B O      1 
HETATM 9624 O O      . HOH   L 5 .   ? -0.62800  47.22400  -35.31100 1.000 43.15000  ? 653 HOH   B O      1 
HETATM 9625 O O      . HOH   L 5 .   ? 32.56400  36.75300  -54.58400 1.000 49.81000  ? 654 HOH   B O      1 
HETATM 9626 O O      . HOH   L 5 .   ? 21.31800  42.49300  -52.82900 1.000 56.10000  ? 655 HOH   B O      1 
HETATM 9627 O O      . HOH   L 5 .   ? -3.34400  47.22700  -52.53100 1.000 61.88000  ? 656 HOH   B O      1 
HETATM 9628 O O      . HOH   L 5 .   ? -14.73000 38.22800  -47.50000 1.000 54.92000  ? 657 HOH   B O      1 
HETATM 9629 O O      . HOH   L 5 .   ? 2.65000   44.37000  -34.22100 1.000 41.96000  ? 658 HOH   B O      1 
HETATM 9630 O O      . HOH   L 5 .   ? -3.30600  27.83700  -16.88400 1.000 70.96000  ? 659 HOH   B O      1 
HETATM 9631 O O      . HOH   L 5 .   ? 22.21700  26.67800  -55.96300 1.000 49.03000  ? 660 HOH   B O      1 
HETATM 9632 O O      . HOH   L 5 .   ? 0.55700   45.31400  -28.41800 1.000 47.82000  ? 661 HOH   B O      1 
HETATM 9633 O O      . HOH   L 5 .   ? -8.69100  13.86000  -48.28500 1.000 55.47000  ? 662 HOH   B O      1 
HETATM 9634 O O      . HOH   L 5 .   ? 7.68900   46.40600  -51.09400 1.000 56.81000  ? 663 HOH   B O      1 
HETATM 9635 O O      . HOH   L 5 .   ? 12.79200  48.65500  -47.87300 1.000 60.23000  ? 664 HOH   B O      1 
HETATM 9636 O O      . HOH   L 5 .   ? -1.86000  29.14800  -14.93200 1.000 66.12000  ? 665 HOH   B O      1 
HETATM 9637 O O      . HOH   L 5 .   ? 23.668    9.691     -51.682   1.000 51.99000  ? 666 HOH   B O      1 
HETATM 9638 O O      . HOH   L 5 .   ? 7.360     48.093    -28.466   1.000 48.22000  ? 667 HOH   B O      1 
HETATM 9639 O O      . HOH   L 5 .   ? 15.89500  18.87000  -49.79300 1.000 51.48000  ? 668 HOH   B O      1 
HETATM 9640 O O      . HOH   L 5 .   ? 14.68500  18.77400  -52.10000 1.000 54.22000  ? 669 HOH   B O      1 
HETATM 9641 O O      . HOH   L 5 .   ? 5.32400   22.15000  -52.50700 1.000 48.45000  ? 670 HOH   B O      1 
HETATM 9642 O O      . HOH   L 5 .   ? -1.91900  39.91500  -57.17000 1.000 58.60000  ? 671 HOH   B O      1 
HETATM 9643 O O      . HOH   L 5 .   ? -2.60800  43.32400  -54.56200 1.000 59.24000  ? 672 HOH   B O      1 
HETATM 9644 O O      . HOH   L 5 .   ? 15.69500  21.35000  -58.73300 1.000 57.53000  ? 673 HOH   B O      1 
HETATM 9645 O O      . HOH   L 5 .   ? 27.78200  40.25200  -28.97100 1.000 68.14000  ? 674 HOH   B O      1 
HETATM 9646 O O      . HOH   L 5 .   ? -13.626   33.058    -49.343   1.000 52.05000  ? 675 HOH   B O      1 
HETATM 9647 O O      . HOH   L 5 .   ? 2.11600   45.26100  -53.87900 1.000 58.58000  ? 676 HOH   B O      1 
HETATM 9648 O O      . HOH   L 5 .   ? -1.41100  43.67800  -52.18500 1.000 53.01000  ? 677 HOH   B O      1 
HETATM 9649 O O      . HOH   L 5 .   ? 21.011    38.137    -23.274   1.000 61.51000  ? 678 HOH   B O      1 
HETATM 9650 O O      . HOH   L 5 .   ? 3.860     14.702    -51.666   1.000 65.54000  ? 679 HOH   B O      1 
# 
