data_9C7M
# 
_entry.id   9C7M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9C7M         pdb_00009c7m 10.2210/pdb9c7m/pdb 
WWPDB D_1000284966 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C7M 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-10 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              oprian@brandeis.edu 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Oprian 
_pdbx_contact_author.name_mi            D 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6520-5459 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Prem Kumar, R.'  1 ? 
'Ellenburg, W.H.' 2 ? 
'Oprian, D.D.'    3 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biochemistry 
_citation.journal_id_ASTM           BICHAW 
_citation.journal_id_CSD            0033 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            63 
_citation.language                  ? 
_citation.page_first                2904 
_citation.page_last                 2915 
_citation.title                     
'Crystal Structure of Caryolan-1-ol Synthase, a Sesquiterpene Synthase Catalyzing an Initial Anti-Markovnikov Cyclization Reaction.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.biochem.4c00547 
_citation.pdbx_database_id_PubMed   39400323 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kumar, R.P.'     1  0000-0002-6555-8289 
primary 'Matos, J.O.'     2  ?                   
primary 'Black, B.Y.'     3  ?                   
primary 'Ellenburg, W.H.' 4  0000-0001-5726-1277 
primary 'Chen, J.'        5  0000-0002-7573-6333 
primary 'Patterson, M.'   6  ?                   
primary 'Gehtman, J.A.'   7  ?                   
primary 'Theobald, D.L.'  8  0000-0002-2695-8343 
primary 'Krauss, I.J.'    9  0000-0003-0984-4085 
primary 'Oprian, D.D.'    10 0000-0002-6520-5459 
# 
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 'Pentalenene synthase'                                                                             37974.316 2  
4.2.3.7 F76A ? ? 
2 non-polymer syn '(2E,6E)-12-fluoro-11-(fluoromethyl)-3,7-dimethyldodeca-2,6,10-trien-1-yl trihydrogen diphosphate' 418.307   1  
?       ?    ? ? 
3 non-polymer nat 'MAGNESIUM ION'                                                                                    24.305    3  
?       ?    ? ? 
4 water       nat water                                                                                              18.015    54 
?       ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PS,Pentalenolactone biosynthesis protein A,Sesquiterpene cyclase,Sesquiterpene synthase' 
# 
_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       
;MPQDVDFHIPLPGRQSPDHARAEAEQLAWPRSLGLIRSDAAAERHLRGGYADLASRFYPHATGADLDLGVDLMSWAFLFD
DLFDGPRGENPEDTKQLTDQVAAALDGPLPDTAPPIAHGFADIWRRTCEGMTPAWCARSARHWRNYFDGYVDEAESRFWN
APCDSAAQYLAMRRHTIGVQPTVDLAERAGRFEVPHRVFDSAVMSAMLQIAVDVNLLLNDIASLEKEEARGEQNNMVMIL
RREHGWSKSRSVSHMQNEVRARLEQYLLLESCLPKVGEIYQLDTAEREALERYRTDAVRTVIRGSYDWHRSSGRYDAEFA
LAAGAQGYLEELGSSAH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPQDVDFHIPLPGRQSPDHARAEAEQLAWPRSLGLIRSDAAAERHLRGGYADLASRFYPHATGADLDLGVDLMSWAFLFD
DLFDGPRGENPEDTKQLTDQVAAALDGPLPDTAPPIAHGFADIWRRTCEGMTPAWCARSARHWRNYFDGYVDEAESRFWN
APCDSAAQYLAMRRHTIGVQPTVDLAERAGRFEVPHRVFDSAVMSAMLQIAVDVNLLLNDIASLEKEEARGEQNNMVMIL
RREHGWSKSRSVSHMQNEVRARLEQYLLLESCLPKVGEIYQLDTAEREALERYRTDAVRTVIRGSYDWHRSSGRYDAEFA
LAAGAQGYLEELGSSAH
;
_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 '(2E,6E)-12-fluoro-11-(fluoromethyl)-3,7-dimethyldodeca-2,6,10-trien-1-yl trihydrogen diphosphate' FDF 
3 'MAGNESIUM ION'                                                                                    MG  
4 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   PRO n 
1 3   GLN n 
1 4   ASP n 
1 5   VAL n 
1 6   ASP n 
1 7   PHE n 
1 8   HIS n 
1 9   ILE n 
1 10  PRO n 
1 11  LEU n 
1 12  PRO n 
1 13  GLY n 
1 14  ARG n 
1 15  GLN n 
1 16  SER n 
1 17  PRO n 
1 18  ASP n 
1 19  HIS n 
1 20  ALA n 
1 21  ARG n 
1 22  ALA n 
1 23  GLU n 
1 24  ALA n 
1 25  GLU n 
1 26  GLN n 
1 27  LEU n 
1 28  ALA n 
1 29  TRP n 
1 30  PRO n 
1 31  ARG n 
1 32  SER n 
1 33  LEU n 
1 34  GLY n 
1 35  LEU n 
1 36  ILE n 
1 37  ARG n 
1 38  SER n 
1 39  ASP n 
1 40  ALA n 
1 41  ALA n 
1 42  ALA n 
1 43  GLU n 
1 44  ARG n 
1 45  HIS n 
1 46  LEU n 
1 47  ARG n 
1 48  GLY n 
1 49  GLY n 
1 50  TYR n 
1 51  ALA n 
1 52  ASP n 
1 53  LEU n 
1 54  ALA n 
1 55  SER n 
1 56  ARG n 
1 57  PHE n 
1 58  TYR n 
1 59  PRO n 
1 60  HIS n 
1 61  ALA n 
1 62  THR n 
1 63  GLY n 
1 64  ALA n 
1 65  ASP n 
1 66  LEU n 
1 67  ASP n 
1 68  LEU n 
1 69  GLY n 
1 70  VAL n 
1 71  ASP n 
1 72  LEU n 
1 73  MET n 
1 74  SER n 
1 75  TRP n 
1 76  ALA n 
1 77  PHE n 
1 78  LEU n 
1 79  PHE n 
1 80  ASP n 
1 81  ASP n 
1 82  LEU n 
1 83  PHE n 
1 84  ASP n 
1 85  GLY n 
1 86  PRO n 
1 87  ARG n 
1 88  GLY n 
1 89  GLU n 
1 90  ASN n 
1 91  PRO n 
1 92  GLU n 
1 93  ASP n 
1 94  THR n 
1 95  LYS n 
1 96  GLN n 
1 97  LEU n 
1 98  THR n 
1 99  ASP n 
1 100 GLN n 
1 101 VAL n 
1 102 ALA n 
1 103 ALA n 
1 104 ALA n 
1 105 LEU n 
1 106 ASP n 
1 107 GLY n 
1 108 PRO n 
1 109 LEU n 
1 110 PRO n 
1 111 ASP n 
1 112 THR n 
1 113 ALA n 
1 114 PRO n 
1 115 PRO n 
1 116 ILE n 
1 117 ALA n 
1 118 HIS n 
1 119 GLY n 
1 120 PHE n 
1 121 ALA n 
1 122 ASP n 
1 123 ILE n 
1 124 TRP n 
1 125 ARG n 
1 126 ARG n 
1 127 THR n 
1 128 CYS n 
1 129 GLU n 
1 130 GLY n 
1 131 MET n 
1 132 THR n 
1 133 PRO n 
1 134 ALA n 
1 135 TRP n 
1 136 CYS n 
1 137 ALA n 
1 138 ARG n 
1 139 SER n 
1 140 ALA n 
1 141 ARG n 
1 142 HIS n 
1 143 TRP n 
1 144 ARG n 
1 145 ASN n 
1 146 TYR n 
1 147 PHE n 
1 148 ASP n 
1 149 GLY n 
1 150 TYR n 
1 151 VAL n 
1 152 ASP n 
1 153 GLU n 
1 154 ALA n 
1 155 GLU n 
1 156 SER n 
1 157 ARG n 
1 158 PHE n 
1 159 TRP n 
1 160 ASN n 
1 161 ALA n 
1 162 PRO n 
1 163 CYS n 
1 164 ASP n 
1 165 SER n 
1 166 ALA n 
1 167 ALA n 
1 168 GLN n 
1 169 TYR n 
1 170 LEU n 
1 171 ALA n 
1 172 MET n 
1 173 ARG n 
1 174 ARG n 
1 175 HIS n 
1 176 THR n 
1 177 ILE n 
1 178 GLY n 
1 179 VAL n 
1 180 GLN n 
1 181 PRO n 
1 182 THR n 
1 183 VAL n 
1 184 ASP n 
1 185 LEU n 
1 186 ALA n 
1 187 GLU n 
1 188 ARG n 
1 189 ALA n 
1 190 GLY n 
1 191 ARG n 
1 192 PHE n 
1 193 GLU n 
1 194 VAL n 
1 195 PRO n 
1 196 HIS n 
1 197 ARG n 
1 198 VAL n 
1 199 PHE n 
1 200 ASP n 
1 201 SER n 
1 202 ALA n 
1 203 VAL n 
1 204 MET n 
1 205 SER n 
1 206 ALA n 
1 207 MET n 
1 208 LEU n 
1 209 GLN n 
1 210 ILE n 
1 211 ALA n 
1 212 VAL n 
1 213 ASP n 
1 214 VAL n 
1 215 ASN n 
1 216 LEU n 
1 217 LEU n 
1 218 LEU n 
1 219 ASN n 
1 220 ASP n 
1 221 ILE n 
1 222 ALA n 
1 223 SER n 
1 224 LEU n 
1 225 GLU n 
1 226 LYS n 
1 227 GLU n 
1 228 GLU n 
1 229 ALA n 
1 230 ARG n 
1 231 GLY n 
1 232 GLU n 
1 233 GLN n 
1 234 ASN n 
1 235 ASN n 
1 236 MET n 
1 237 VAL n 
1 238 MET n 
1 239 ILE n 
1 240 LEU n 
1 241 ARG n 
1 242 ARG n 
1 243 GLU n 
1 244 HIS n 
1 245 GLY n 
1 246 TRP n 
1 247 SER n 
1 248 LYS n 
1 249 SER n 
1 250 ARG n 
1 251 SER n 
1 252 VAL n 
1 253 SER n 
1 254 HIS n 
1 255 MET n 
1 256 GLN n 
1 257 ASN n 
1 258 GLU n 
1 259 VAL n 
1 260 ARG n 
1 261 ALA n 
1 262 ARG n 
1 263 LEU n 
1 264 GLU n 
1 265 GLN n 
1 266 TYR n 
1 267 LEU n 
1 268 LEU n 
1 269 LEU n 
1 270 GLU n 
1 271 SER n 
1 272 CYS n 
1 273 LEU n 
1 274 PRO n 
1 275 LYS n 
1 276 VAL n 
1 277 GLY n 
1 278 GLU n 
1 279 ILE n 
1 280 TYR n 
1 281 GLN n 
1 282 LEU n 
1 283 ASP n 
1 284 THR n 
1 285 ALA n 
1 286 GLU n 
1 287 ARG n 
1 288 GLU n 
1 289 ALA n 
1 290 LEU n 
1 291 GLU n 
1 292 ARG n 
1 293 TYR n 
1 294 ARG n 
1 295 THR n 
1 296 ASP n 
1 297 ALA n 
1 298 VAL n 
1 299 ARG n 
1 300 THR n 
1 301 VAL n 
1 302 ILE n 
1 303 ARG n 
1 304 GLY n 
1 305 SER n 
1 306 TYR n 
1 307 ASP n 
1 308 TRP n 
1 309 HIS n 
1 310 ARG n 
1 311 SER n 
1 312 SER n 
1 313 GLY n 
1 314 ARG n 
1 315 TYR n 
1 316 ASP n 
1 317 ALA n 
1 318 GLU n 
1 319 PHE n 
1 320 ALA n 
1 321 LEU n 
1 322 ALA n 
1 323 ALA n 
1 324 GLY n 
1 325 ALA n 
1 326 GLN n 
1 327 GLY n 
1 328 TYR n 
1 329 LEU n 
1 330 GLU n 
1 331 GLU n 
1 332 LEU n 
1 333 GLY n 
1 334 SER n 
1 335 SER n 
1 336 ALA n 
1 337 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   337 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 penA 
_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      'Streptomyces exfoliatus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1905 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
FDF non-polymer         . '(2E,6E)-12-fluoro-11-(fluoromethyl)-3,7-dimethyldodeca-2,6,10-trien-1-yl trihydrogen diphosphate' ? 
'C15 H26 F2 O7 P2' 418.307 
GLN 'L-peptide linking' y GLUTAMINE                                                                                          ? 
'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                    ? 
'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                                                            ? 
'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                          ? 
'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                                                              ? 
'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                         ? 
'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                            ? 
'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                                                             ? 
'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                                                         ? 
'C5 H11 N O2 S'    149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                                                                    ? 
'Mg 2'             24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                      ? 
'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                                                            ? 
'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                                                             ? 
'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                                                          ? 
'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                         ? 
'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                           ? 
'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                                                             ? 
'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   ?   ?   ?   A . n 
A 1 5   VAL 5   5   ?   ?   ?   A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  HIS 60  60  60  HIS HIS A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 HIS 118 118 118 HIS HIS A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 TRP 135 135 135 TRP TRP A . n 
A 1 136 CYS 136 136 136 CYS CYS A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 TRP 143 143 143 TRP TRP A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 TRP 159 159 159 TRP TRP A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 CYS 163 163 163 CYS CYS A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 ARG 173 173 173 ARG ARG A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 HIS 175 175 175 HIS HIS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 MET 204 204 204 MET MET A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 MET 207 207 207 MET MET A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 GLN 209 209 209 GLN GLN A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 ASN 234 234 234 ASN ASN A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 ILE 239 239 239 ILE ILE A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 TRP 246 246 246 TRP TRP A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 SER 253 253 253 SER SER A . n 
A 1 254 HIS 254 254 254 HIS HIS A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 ASN 257 257 257 ASN ASN A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 GLN 265 265 265 GLN GLN A . n 
A 1 266 TYR 266 266 266 TYR TYR A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 CYS 272 272 272 CYS CYS A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 PRO 274 274 274 PRO PRO A . n 
A 1 275 LYS 275 275 275 LYS LYS A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 GLN 281 281 281 GLN GLN A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 ASP 283 283 283 ASP ASP A . n 
A 1 284 THR 284 284 284 THR THR A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 GLU 286 286 286 GLU GLU A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 ARG 292 292 292 ARG ARG A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 ASP 296 296 296 ASP ASP A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ARG 299 299 299 ARG ARG A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 SER 305 305 305 SER SER A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 TRP 308 308 308 TRP TRP A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 ASP 316 316 ?   ?   ?   A . n 
A 1 317 ALA 317 317 ?   ?   ?   A . n 
A 1 318 GLU 318 318 ?   ?   ?   A . n 
A 1 319 PHE 319 319 ?   ?   ?   A . n 
A 1 320 ALA 320 320 ?   ?   ?   A . n 
A 1 321 LEU 321 321 ?   ?   ?   A . n 
A 1 322 ALA 322 322 ?   ?   ?   A . n 
A 1 323 ALA 323 323 ?   ?   ?   A . n 
A 1 324 GLY 324 324 ?   ?   ?   A . n 
A 1 325 ALA 325 325 ?   ?   ?   A . n 
A 1 326 GLN 326 326 ?   ?   ?   A . n 
A 1 327 GLY 327 327 ?   ?   ?   A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 SER 335 335 335 SER SER A . n 
A 1 336 ALA 336 336 ?   ?   ?   A . n 
A 1 337 HIS 337 337 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   ASP 4   4   ?   ?   ?   B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ASP 6   6   6   ASP ASP B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   HIS 8   8   8   HIS HIS B . n 
B 1 9   ILE 9   9   9   ILE ILE B . n 
B 1 10  PRO 10  10  10  PRO PRO B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  ARG 14  14  14  ARG ARG B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  PRO 17  17  17  PRO PRO B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  HIS 19  19  19  HIS HIS B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLN 26  26  26  GLN GLN B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  ARG 31  31  31  ARG ARG B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ARG 44  44  44  ARG ARG B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  TYR 50  50  50  TYR TYR B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  SER 55  55  55  SER SER B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  TYR 58  58  58  TYR TYR B . n 
B 1 59  PRO 59  59  59  PRO PRO B . n 
B 1 60  HIS 60  60  60  HIS HIS B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  LEU 68  68  68  LEU LEU B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  TRP 75  75  75  TRP TRP B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  PHE 77  77  77  PHE PHE B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  PHE 79  79  79  PHE PHE B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  PHE 83  83  83  PHE PHE B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  ASP 93  93  93  ASP ASP B . n 
B 1 94  THR 94  94  94  THR THR B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 GLN 100 100 100 GLN GLN B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 ASP 106 106 106 ASP ASP B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 PRO 110 110 110 PRO PRO B . n 
B 1 111 ASP 111 111 111 ASP ASP B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 PRO 114 114 114 PRO PRO B . n 
B 1 115 PRO 115 115 115 PRO PRO B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 HIS 118 118 118 HIS HIS B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 PHE 120 120 120 PHE PHE B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 TRP 124 124 124 TRP TRP B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 ARG 126 126 126 ARG ARG B . n 
B 1 127 THR 127 127 127 THR THR B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 TRP 135 135 135 TRP TRP B . n 
B 1 136 CYS 136 136 136 CYS CYS B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 ARG 138 138 138 ARG ARG B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 HIS 142 142 142 HIS HIS B . n 
B 1 143 TRP 143 143 143 TRP TRP B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 ASN 145 145 145 ASN ASN B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 PHE 147 147 147 PHE PHE B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 ASP 152 152 152 ASP ASP B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 ARG 157 157 157 ARG ARG B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 TRP 159 159 159 TRP TRP B . n 
B 1 160 ASN 160 160 160 ASN ASN B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 PRO 162 162 162 PRO PRO B . n 
B 1 163 CYS 163 163 163 CYS CYS B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 GLN 168 168 168 GLN GLN B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 ALA 171 171 171 ALA ALA B . n 
B 1 172 MET 172 172 172 MET MET B . n 
B 1 173 ARG 173 173 173 ARG ARG B . n 
B 1 174 ARG 174 174 174 ARG ARG B . n 
B 1 175 HIS 175 175 175 HIS HIS B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 GLN 180 180 180 GLN GLN B . n 
B 1 181 PRO 181 181 181 PRO PRO B . n 
B 1 182 THR 182 182 182 THR THR B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 ARG 191 191 191 ARG ARG B . n 
B 1 192 PHE 192 192 192 PHE PHE B . n 
B 1 193 GLU 193 193 193 GLU GLU B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 ARG 197 197 197 ARG ARG B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 PHE 199 199 199 PHE PHE B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 ALA 202 202 202 ALA ALA B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 MET 204 204 204 MET MET B . n 
B 1 205 SER 205 205 205 SER SER B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 MET 207 207 207 MET MET B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 GLN 209 209 209 GLN GLN B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 ASN 215 215 215 ASN ASN B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 GLU 225 225 225 GLU GLU B . n 
B 1 226 LYS 226 226 226 LYS LYS B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ALA 229 229 229 ALA ALA B . n 
B 1 230 ARG 230 230 230 ARG ARG B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 GLU 232 232 232 GLU GLU B . n 
B 1 233 GLN 233 233 233 GLN GLN B . n 
B 1 234 ASN 234 234 234 ASN ASN B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 MET 236 236 236 MET MET B . n 
B 1 237 VAL 237 237 237 VAL VAL B . n 
B 1 238 MET 238 238 238 MET MET B . n 
B 1 239 ILE 239 239 239 ILE ILE B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 ARG 242 242 242 ARG ARG B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 HIS 244 244 244 HIS HIS B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 TRP 246 246 246 TRP TRP B . n 
B 1 247 SER 247 247 247 SER SER B . n 
B 1 248 LYS 248 248 248 LYS LYS B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 SER 251 251 251 SER SER B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 SER 253 253 253 SER SER B . n 
B 1 254 HIS 254 254 254 HIS HIS B . n 
B 1 255 MET 255 255 255 MET MET B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 ASN 257 257 257 ASN ASN B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 ALA 261 261 261 ALA ALA B . n 
B 1 262 ARG 262 262 262 ARG ARG B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 GLU 264 264 264 GLU GLU B . n 
B 1 265 GLN 265 265 265 GLN GLN B . n 
B 1 266 TYR 266 266 266 TYR TYR B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 CYS 272 272 272 CYS CYS B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 PRO 274 274 274 PRO PRO B . n 
B 1 275 LYS 275 275 275 LYS LYS B . n 
B 1 276 VAL 276 276 276 VAL VAL B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 ILE 279 279 279 ILE ILE B . n 
B 1 280 TYR 280 280 280 TYR TYR B . n 
B 1 281 GLN 281 281 281 GLN GLN B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 ASP 283 283 283 ASP ASP B . n 
B 1 284 THR 284 284 284 THR THR B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 GLU 286 286 286 GLU GLU B . n 
B 1 287 ARG 287 287 287 ARG ARG B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 GLU 291 291 291 GLU GLU B . n 
B 1 292 ARG 292 292 292 ARG ARG B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 THR 295 295 295 THR THR B . n 
B 1 296 ASP 296 296 296 ASP ASP B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 ARG 299 299 299 ARG ARG B . n 
B 1 300 THR 300 300 300 THR THR B . n 
B 1 301 VAL 301 301 301 VAL VAL B . n 
B 1 302 ILE 302 302 302 ILE ILE B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 GLY 304 304 304 GLY GLY B . n 
B 1 305 SER 305 305 305 SER SER B . n 
B 1 306 TYR 306 306 306 TYR TYR B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 TRP 308 308 308 TRP TRP B . n 
B 1 309 HIS 309 309 309 HIS HIS B . n 
B 1 310 ARG 310 310 310 ARG ARG B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 SER 312 312 ?   ?   ?   B . n 
B 1 313 GLY 313 313 ?   ?   ?   B . n 
B 1 314 ARG 314 314 ?   ?   ?   B . n 
B 1 315 TYR 315 315 ?   ?   ?   B . n 
B 1 316 ASP 316 316 ?   ?   ?   B . n 
B 1 317 ALA 317 317 ?   ?   ?   B . n 
B 1 318 GLU 318 318 ?   ?   ?   B . n 
B 1 319 PHE 319 319 ?   ?   ?   B . n 
B 1 320 ALA 320 320 ?   ?   ?   B . n 
B 1 321 LEU 321 321 ?   ?   ?   B . n 
B 1 322 ALA 322 322 ?   ?   ?   B . n 
B 1 323 ALA 323 323 ?   ?   ?   B . n 
B 1 324 GLY 324 324 ?   ?   ?   B . n 
B 1 325 ALA 325 325 ?   ?   ?   B . n 
B 1 326 GLN 326 326 ?   ?   ?   B . n 
B 1 327 GLY 327 327 ?   ?   ?   B . n 
B 1 328 TYR 328 328 ?   ?   ?   B . n 
B 1 329 LEU 329 329 ?   ?   ?   B . n 
B 1 330 GLU 330 330 ?   ?   ?   B . n 
B 1 331 GLU 331 331 ?   ?   ?   B . n 
B 1 332 LEU 332 332 ?   ?   ?   B . n 
B 1 333 GLY 333 333 ?   ?   ?   B . n 
B 1 334 SER 334 334 ?   ?   ?   B . n 
B 1 335 SER 335 335 ?   ?   ?   B . n 
B 1 336 ALA 336 336 ?   ?   ?   B . n 
B 1 337 HIS 337 337 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FDF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FDF 
_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 FDF 1  401 401 FDF DFF A . 
D 3 MG  1  402 1   MG  MG  A . 
E 3 MG  1  403 2   MG  MG  A . 
F 3 MG  1  404 3   MG  MG  A . 
G 4 HOH 1  501 15  HOH HOH A . 
G 4 HOH 2  502 52  HOH HOH A . 
G 4 HOH 3  503 7   HOH HOH A . 
G 4 HOH 4  504 19  HOH HOH A . 
G 4 HOH 5  505 2   HOH HOH A . 
G 4 HOH 6  506 5   HOH HOH A . 
G 4 HOH 7  507 26  HOH HOH A . 
G 4 HOH 8  508 16  HOH HOH A . 
G 4 HOH 9  509 9   HOH HOH A . 
G 4 HOH 10 510 53  HOH HOH A . 
G 4 HOH 11 511 10  HOH HOH A . 
G 4 HOH 12 512 6   HOH HOH A . 
G 4 HOH 13 513 20  HOH HOH A . 
G 4 HOH 14 514 4   HOH HOH A . 
G 4 HOH 15 515 21  HOH HOH A . 
G 4 HOH 16 516 14  HOH HOH A . 
G 4 HOH 17 517 3   HOH HOH A . 
G 4 HOH 18 518 24  HOH HOH A . 
G 4 HOH 19 519 12  HOH HOH A . 
G 4 HOH 20 520 22  HOH HOH A . 
G 4 HOH 21 521 17  HOH HOH A . 
G 4 HOH 22 522 18  HOH HOH A . 
G 4 HOH 23 523 13  HOH HOH A . 
G 4 HOH 24 524 48  HOH HOH A . 
G 4 HOH 25 525 25  HOH HOH A . 
G 4 HOH 26 526 51  HOH HOH A . 
G 4 HOH 27 527 50  HOH HOH A . 
G 4 HOH 28 528 46  HOH HOH A . 
G 4 HOH 29 529 40  HOH HOH A . 
G 4 HOH 30 530 23  HOH HOH A . 
G 4 HOH 31 531 54  HOH HOH A . 
H 4 HOH 1  401 31  HOH HOH B . 
H 4 HOH 2  402 28  HOH HOH B . 
H 4 HOH 3  403 1   HOH HOH B . 
H 4 HOH 4  404 39  HOH HOH B . 
H 4 HOH 5  405 41  HOH HOH B . 
H 4 HOH 6  406 36  HOH HOH B . 
H 4 HOH 7  407 30  HOH HOH B . 
H 4 HOH 8  408 57  HOH HOH B . 
H 4 HOH 9  409 35  HOH HOH B . 
H 4 HOH 10 410 11  HOH HOH B . 
H 4 HOH 11 411 42  HOH HOH B . 
H 4 HOH 12 412 32  HOH HOH B . 
H 4 HOH 13 413 56  HOH HOH B . 
H 4 HOH 14 414 43  HOH HOH B . 
H 4 HOH 15 415 27  HOH HOH B . 
H 4 HOH 16 416 47  HOH HOH B . 
H 4 HOH 17 417 44  HOH HOH B . 
H 4 HOH 18 418 38  HOH HOH B . 
H 4 HOH 19 419 55  HOH HOH B . 
H 4 HOH 20 420 33  HOH HOH B . 
H 4 HOH 21 421 45  HOH HOH B . 
H 4 HOH 22 422 29  HOH HOH B . 
H 4 HOH 23 423 37  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 ASP 6   ? CG  ? A ASP 6   CG  
2  1 Y 1 A ASP 6   ? OD1 ? A ASP 6   OD1 
3  1 Y 1 A ASP 6   ? OD2 ? A ASP 6   OD2 
4  1 Y 1 A GLU 92  ? CG  ? A GLU 92  CG  
5  1 Y 1 A GLU 92  ? CD  ? A GLU 92  CD  
6  1 Y 1 A GLU 92  ? OE1 ? A GLU 92  OE1 
7  1 Y 1 A GLU 92  ? OE2 ? A GLU 92  OE2 
8  1 Y 1 A GLN 96  ? CD  ? A GLN 96  CD  
9  1 Y 1 A GLN 96  ? OE1 ? A GLN 96  OE1 
10 1 Y 1 A GLN 96  ? NE2 ? A GLN 96  NE2 
11 1 Y 1 A GLU 155 ? OE1 ? A GLU 155 OE1 
12 1 Y 1 A GLU 155 ? OE2 ? A GLU 155 OE2 
13 1 Y 1 A ASP 164 ? CG  ? A ASP 164 CG  
14 1 Y 1 A ASP 164 ? OD1 ? A ASP 164 OD1 
15 1 Y 1 A ASP 164 ? OD2 ? A ASP 164 OD2 
16 1 Y 1 A GLU 225 ? CD  ? A GLU 225 CD  
17 1 Y 1 A GLU 225 ? OE1 ? A GLU 225 OE1 
18 1 Y 1 A GLU 225 ? OE2 ? A GLU 225 OE2 
19 1 Y 1 A LYS 226 ? CG  ? A LYS 226 CG  
20 1 Y 1 A LYS 226 ? CD  ? A LYS 226 CD  
21 1 Y 1 A LYS 226 ? CE  ? A LYS 226 CE  
22 1 Y 1 A LYS 226 ? NZ  ? A LYS 226 NZ  
23 1 Y 1 A GLN 233 ? CG  ? A GLN 233 CG  
24 1 Y 1 A GLN 233 ? CD  ? A GLN 233 CD  
25 1 Y 1 A GLN 233 ? OE1 ? A GLN 233 OE1 
26 1 Y 1 A GLN 233 ? NE2 ? A GLN 233 NE2 
27 1 Y 1 A TRP 246 ? CG  ? A TRP 246 CG  
28 1 Y 1 A TRP 246 ? CD1 ? A TRP 246 CD1 
29 1 Y 1 A TRP 246 ? CD2 ? A TRP 246 CD2 
30 1 Y 1 A TRP 246 ? NE1 ? A TRP 246 NE1 
31 1 Y 1 A TRP 246 ? CE2 ? A TRP 246 CE2 
32 1 Y 1 A TRP 246 ? CE3 ? A TRP 246 CE3 
33 1 Y 1 A TRP 246 ? CZ2 ? A TRP 246 CZ2 
34 1 Y 1 A TRP 246 ? CZ3 ? A TRP 246 CZ3 
35 1 Y 1 A TRP 246 ? CH2 ? A TRP 246 CH2 
36 1 Y 1 A LYS 248 ? CG  ? A LYS 248 CG  
37 1 Y 1 A LYS 248 ? CD  ? A LYS 248 CD  
38 1 Y 1 A LYS 248 ? CE  ? A LYS 248 CE  
39 1 Y 1 A LYS 248 ? NZ  ? A LYS 248 NZ  
40 1 Y 1 A ARG 250 ? NE  ? A ARG 250 NE  
41 1 Y 1 A ARG 250 ? CZ  ? A ARG 250 CZ  
42 1 Y 1 A ARG 250 ? NH1 ? A ARG 250 NH1 
43 1 Y 1 A ARG 250 ? NH2 ? A ARG 250 NH2 
44 1 Y 1 A GLU 278 ? CG  ? A GLU 278 CG  
45 1 Y 1 A GLU 278 ? CD  ? A GLU 278 CD  
46 1 Y 1 A GLU 278 ? OE1 ? A GLU 278 OE1 
47 1 Y 1 A GLU 278 ? OE2 ? A GLU 278 OE2 
48 1 Y 1 A GLU 330 ? CG  ? A GLU 330 CG  
49 1 Y 1 A GLU 330 ? CD  ? A GLU 330 CD  
50 1 Y 1 A GLU 330 ? OE1 ? A GLU 330 OE1 
51 1 Y 1 A GLU 330 ? OE2 ? A GLU 330 OE2 
52 1 Y 1 A SER 334 ? OG  ? A SER 334 OG  
53 1 Y 1 B ASN 160 ? CG  ? B ASN 160 CG  
54 1 Y 1 B ASN 160 ? OD1 ? B ASN 160 OD1 
55 1 Y 1 B ASN 160 ? ND2 ? B ASN 160 ND2 
56 1 Y 1 B LYS 226 ? CG  ? B LYS 226 CG  
57 1 Y 1 B LYS 226 ? CD  ? B LYS 226 CD  
58 1 Y 1 B LYS 226 ? CE  ? B LYS 226 CE  
59 1 Y 1 B LYS 226 ? NZ  ? B LYS 226 NZ  
60 1 Y 1 B GLU 288 ? CG  ? B GLU 288 CG  
61 1 Y 1 B GLU 288 ? CD  ? B GLU 288 CD  
62 1 Y 1 B GLU 288 ? OE1 ? B GLU 288 OE1 
63 1 Y 1 B GLU 288 ? OE2 ? B GLU 288 OE2 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9C7M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     180.530 
_cell.length_a_esd                 ? 
_cell.length_b                     180.530 
_cell.length_b_esd                 ? 
_cell.length_c                     55.861 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9C7M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63' 
_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                   9C7M 
_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             3.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.38 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES, pH 7.5, containing 2 M ammonium sulfate and 2% PEG400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-12 
_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   0.979 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          72.27 
_reflns.entry_id                                       9C7M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.65 
_reflns.d_resolution_low                               20 
_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                                     30519 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.111 
_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                                    2.65 
_reflns_shell.d_res_low                                     2.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4036 
_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                               21.8 
_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                                  0.8 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.92 
_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                               ? 
_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                                 9C7M 
_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                            2.65 
_refine.ls_d_res_low                             19.80 
_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                     30478 
_refine.ls_number_reflns_R_free                  1535 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1997 
_refine.ls_R_factor_R_free                       0.2298 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1982 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 26.67 
_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                            0.35 
_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                       2.65 
_refine_hist.d_res_low                        19.80 
_refine_hist.number_atoms_solvent             54 
_refine_hist.number_atoms_total               5010 
_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        4927 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_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' ? 0.002  ? 5073 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.483  ? 6890 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.305 ? 1855 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.036  ? 722  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 919  ? f_plane_restr      ? ? 
# 
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' 2.65 2.74  . . 139 2586 100.00 . . . . 0.3021 . . . . . . . . . . . 0.3344 
'X-RAY DIFFRACTION' 2.74 2.83  . . 143 2607 100.00 . . . . 0.2825 . . . . . . . . . . . 0.3247 
'X-RAY DIFFRACTION' 2.83 2.95  . . 163 2593 100.00 . . . . 0.2620 . . . . . . . . . . . 0.3106 
'X-RAY DIFFRACTION' 2.95 3.08  . . 135 2596 100.00 . . . . 0.2589 . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 3.08 3.24  . . 118 2627 100.00 . . . . 0.2439 . . . . . . . . . . . 0.2712 
'X-RAY DIFFRACTION' 3.24 3.44  . . 159 2604 100.00 . . . . 0.2315 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 3.44 3.71  . . 128 2647 100.00 . . . . 0.2035 . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 3.71 4.08  . . 139 2625 100.00 . . . . 0.1923 . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 4.08 4.66  . . 145 2644 100.00 . . . . 0.1724 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 4.66 5.85  . . 110 2694 100.00 . . . . 0.1931 . . . . . . . . . . . 0.2112 
'X-RAY DIFFRACTION' 5.85 19.80 . . 156 2720 100.00 . . . . 0.1642 . . . . . . . . . . . 0.1856 
# 
_struct.entry_id                     9C7M 
_struct.title                        
'Crystal structure of pentalenene synthase variant F76A complexed with 12,13-difluorofarnesyl diphosphate' 
_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        9C7M 
_struct_keywords.text            
'Terpene synthase, Cyclase, Sesquiterpene synthase, complex, Inhibitor, Fluoro analog, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
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 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PENA_STREX 
_struct_ref.pdbx_db_accession          Q55012 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPQDVDFHIPLPGRQSPDHARAEAEQLAWPRSLGLIRSDAAAERHLRGGYADLASRFYPHATGADLDLGVDLMSWFFLFD
DLFDGPRGENPEDTKQLTDQVAAALDGPLPDTAPPIAHGFADIWRRTCEGMTPAWCARSARHWRNYFDGYVDEAESRFWN
APCDSAAQYLAMRRHTIGVQPTVDLAERAGRFEVPHRVFDSAVMSAMLQIAVDVNLLLNDIASLEKEEARGEQNNMVMIL
RREHGWSKSRSVSHMQNEVRARLEQYLLLESCLPKVGEIYQLDTAEREALERYRTDAVRTVIRGSYDWHRSSGRYDAEFA
LAAGAQGYLEELGSSAH
;
_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 9C7M A 1 ? 337 ? Q55012 1 ? 337 ? 1 337 
2 1 9C7M B 1 ? 337 ? Q55012 1 ? 337 ? 1 337 
# 
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 9C7M ALA A 76 ? UNP Q55012 PHE 76 'engineered mutation' 76 1 
2 9C7M ALA B 76 ? UNP Q55012 PHE 76 'engineered mutation' 76 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_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 ASP A 18  ? GLU A 25  ? ASP A 18  GLU A 25  1 ? 8  
HELX_P HELX_P2  AA2 LEU A 27  ? LEU A 33  ? LEU A 27  LEU A 33  1 ? 7  
HELX_P HELX_P3  AA3 SER A 38  ? ARG A 47  ? SER A 38  ARG A 47  1 ? 10 
HELX_P HELX_P4  AA4 GLY A 49  ? TYR A 58  ? GLY A 49  TYR A 58  1 ? 10 
HELX_P HELX_P5  AA5 THR A 62  ? LEU A 82  ? THR A 62  LEU A 82  1 ? 21 
HELX_P HELX_P6  AA6 PHE A 83  ? ASP A 84  ? PHE A 83  ASP A 84  5 ? 2  
HELX_P HELX_P7  AA7 GLY A 85  ? GLU A 89  ? GLY A 85  GLU A 89  5 ? 5  
HELX_P HELX_P8  AA8 ASN A 90  ? ALA A 103 ? ASN A 90  ALA A 103 1 ? 14 
HELX_P HELX_P9  AA9 ALA A 104 ? ASP A 106 ? ALA A 104 ASP A 106 5 ? 3  
HELX_P HELX_P10 AB1 PRO A 114 ? GLU A 129 ? PRO A 114 GLU A 129 1 ? 16 
HELX_P HELX_P11 AB2 THR A 132 ? TRP A 159 ? THR A 132 TRP A 159 1 ? 28 
HELX_P HELX_P12 AB3 SER A 165 ? ILE A 177 ? SER A 165 ILE A 177 1 ? 13 
HELX_P HELX_P13 AB4 GLY A 178 ? ARG A 191 ? GLY A 178 ARG A 191 1 ? 14 
HELX_P HELX_P14 AB5 PRO A 195 ? ASP A 200 ? PRO A 195 ASP A 200 1 ? 6  
HELX_P HELX_P15 AB6 SER A 201 ? SER A 223 ? SER A 201 SER A 223 1 ? 23 
HELX_P HELX_P16 AB7 SER A 223 ? ALA A 229 ? SER A 223 ALA A 229 1 ? 7  
HELX_P HELX_P17 AB8 ASN A 235 ? GLY A 245 ? ASN A 235 GLY A 245 1 ? 11 
HELX_P HELX_P18 AB9 SER A 247 ? TYR A 280 ? SER A 247 TYR A 280 1 ? 34 
HELX_P HELX_P19 AC1 ASP A 283 ? ALA A 297 ? ASP A 283 ALA A 297 1 ? 15 
HELX_P HELX_P20 AC2 ALA A 297 ? SER A 312 ? ALA A 297 SER A 312 1 ? 16 
HELX_P HELX_P21 AC3 LEU A 329 ? SER A 334 ? LEU A 329 SER A 334 5 ? 6  
HELX_P HELX_P22 AC4 ASP B 18  ? GLN B 26  ? ASP B 18  GLN B 26  1 ? 9  
HELX_P HELX_P23 AC5 LEU B 27  ? LEU B 33  ? LEU B 27  LEU B 33  1 ? 7  
HELX_P HELX_P24 AC6 SER B 38  ? ARG B 47  ? SER B 38  ARG B 47  1 ? 10 
HELX_P HELX_P25 AC7 GLY B 49  ? TYR B 58  ? GLY B 49  TYR B 58  1 ? 10 
HELX_P HELX_P26 AC8 GLY B 63  ? LEU B 82  ? GLY B 63  LEU B 82  1 ? 20 
HELX_P HELX_P27 AC9 PHE B 83  ? ASP B 84  ? PHE B 83  ASP B 84  5 ? 2  
HELX_P HELX_P28 AD1 GLY B 85  ? GLU B 89  ? GLY B 85  GLU B 89  5 ? 5  
HELX_P HELX_P29 AD2 ASN B 90  ? ALA B 103 ? ASN B 90  ALA B 103 1 ? 14 
HELX_P HELX_P30 AD3 ALA B 104 ? ASP B 106 ? ALA B 104 ASP B 106 5 ? 3  
HELX_P HELX_P31 AD4 PRO B 114 ? GLU B 129 ? PRO B 114 GLU B 129 1 ? 16 
HELX_P HELX_P32 AD5 THR B 132 ? TRP B 159 ? THR B 132 TRP B 159 1 ? 28 
HELX_P HELX_P33 AD6 SER B 165 ? ILE B 177 ? SER B 165 ILE B 177 1 ? 13 
HELX_P HELX_P34 AD7 GLY B 178 ? ARG B 191 ? GLY B 178 ARG B 191 1 ? 14 
HELX_P HELX_P35 AD8 PRO B 195 ? ASP B 200 ? PRO B 195 ASP B 200 1 ? 6  
HELX_P HELX_P36 AD9 SER B 201 ? SER B 223 ? SER B 201 SER B 223 1 ? 23 
HELX_P HELX_P37 AE1 SER B 223 ? ARG B 230 ? SER B 223 ARG B 230 1 ? 8  
HELX_P HELX_P38 AE2 ASN B 235 ? GLY B 245 ? ASN B 235 GLY B 245 1 ? 11 
HELX_P HELX_P39 AE3 SER B 247 ? SER B 271 ? SER B 247 SER B 271 1 ? 25 
HELX_P HELX_P40 AE4 CYS B 272 ? TYR B 280 ? CYS B 272 TYR B 280 1 ? 9  
HELX_P HELX_P41 AE5 ASP B 283 ? ALA B 297 ? ASP B 283 ALA B 297 1 ? 15 
HELX_P HELX_P42 AE6 ALA B 297 ? SER B 311 ? ALA B 297 SER B 311 1 ? 15 
# 
_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 
metalc1  metalc ? ? A ASP 80  OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 80  A MG  402 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc2  metalc ? ? A ASP 80  OD1 ? ? ? 1_555 E MG  . MG ? ? A ASP 80  A MG  403 1_555 ? ? ? ? ? ? ? 2.765 ? ? 
metalc3  metalc ? ? A ASN 219 OD1 ? ? ? 1_555 F MG  . MG ? ? A ASN 219 A MG  404 1_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc4  metalc ? ? A SER 223 OG  ? ? ? 1_555 F MG  . MG ? ? A SER 223 A MG  404 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc5  metalc ? ? A GLU 227 OE2 ? ? ? 1_555 F MG  . MG ? ? A GLU 227 A MG  404 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc6  metalc ? ? C FDF .   O3A ? ? ? 1_555 D MG  . MG ? ? A FDF 401 A MG  402 1_555 ? ? ? ? ? ? ? 2.525 ? ? 
metalc7  metalc ? ? C FDF .   O2A ? ? ? 1_555 E MG  . MG ? ? A FDF 401 A MG  403 1_555 ? ? ? ? ? ? ? 2.965 ? ? 
metalc8  metalc ? ? C FDF .   O1A ? ? ? 1_555 F MG  . MG ? ? A FDF 401 A MG  404 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc9  metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  402 A HOH 527 1_555 ? ? ? ? ? ? ? 2.803 ? ? 
metalc10 metalc ? ? E MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  403 A HOH 519 1_555 ? ? ? ? ? ? ? 2.424 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2 ? A ASP 80  ? A ASP 80  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O3A ? C FDF .   ? A FDF 401 ? 1_555 93.1  ? 
2  OD2 ? A ASP 80  ? A ASP 80  ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 527 ? 1_555 139.7 ? 
3  O3A ? C FDF .   ? A FDF 401 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? G HOH .   ? A HOH 527 ? 1_555 94.7  ? 
4  OD1 ? A ASP 80  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O2A ? C FDF .   ? A FDF 401 ? 1_555 72.7  ? 
5  OD1 ? A ASP 80  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? G HOH .   ? A HOH 519 ? 1_555 115.4 ? 
6  O2A ? C FDF .   ? A FDF 401 ? 1_555 MG ? E MG . ? A MG 403 ? 1_555 O   ? G HOH .   ? A HOH 519 ? 1_555 118.9 ? 
7  OD1 ? A ASN 219 ? A ASN 219 ? 1_555 MG ? F MG . ? A MG 404 ? 1_555 OG  ? A SER 223 ? A SER 223 ? 1_555 98.3  ? 
8  OD1 ? A ASN 219 ? A ASN 219 ? 1_555 MG ? F MG . ? A MG 404 ? 1_555 OE2 ? A GLU 227 ? A GLU 227 ? 1_555 165.7 ? 
9  OG  ? A SER 223 ? A SER 223 ? 1_555 MG ? F MG . ? A MG 404 ? 1_555 OE2 ? A GLU 227 ? A GLU 227 ? 1_555 91.8  ? 
10 OD1 ? A ASN 219 ? A ASN 219 ? 1_555 MG ? F MG . ? A MG 404 ? 1_555 O1A ? C FDF .   ? A FDF 401 ? 1_555 82.0  ? 
11 OG  ? A SER 223 ? A SER 223 ? 1_555 MG ? F MG . ? A MG 404 ? 1_555 O1A ? C FDF .   ? A FDF 401 ? 1_555 152.4 ? 
12 OE2 ? A GLU 227 ? A GLU 227 ? 1_555 MG ? F MG . ? A MG 404 ? 1_555 O1A ? C FDF .   ? A FDF 401 ? 1_555 93.6  ? 
# 
_pdbx_entry_details.entry_id                   9C7M 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 LEU A 82  ? ? -63.25  5.30    
2 1 ASN A 234 ? ? -100.71 68.77   
3 1 ALA A 297 ? ? -123.18 -50.72  
4 1 ASP B 283 ? ? -79.19  -169.09 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z        
2 x-y,x,z+1/2  
3 y,-x+y,z+1/2 
4 -y,x-y,z     
5 -x+y,-x,z    
6 -x,-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 1   ? A MET 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A GLN 3   ? A GLN 3   
4  1 Y 1 A ASP 4   ? A ASP 4   
5  1 Y 1 A VAL 5   ? A VAL 5   
6  1 Y 1 A ASP 316 ? A ASP 316 
7  1 Y 1 A ALA 317 ? A ALA 317 
8  1 Y 1 A GLU 318 ? A GLU 318 
9  1 Y 1 A PHE 319 ? A PHE 319 
10 1 Y 1 A ALA 320 ? A ALA 320 
11 1 Y 1 A LEU 321 ? A LEU 321 
12 1 Y 1 A ALA 322 ? A ALA 322 
13 1 Y 1 A ALA 323 ? A ALA 323 
14 1 Y 1 A GLY 324 ? A GLY 324 
15 1 Y 1 A ALA 325 ? A ALA 325 
16 1 Y 1 A GLN 326 ? A GLN 326 
17 1 Y 1 A GLY 327 ? A GLY 327 
18 1 Y 1 A ALA 336 ? A ALA 336 
19 1 Y 1 A HIS 337 ? A HIS 337 
20 1 Y 1 B MET 1   ? B MET 1   
21 1 Y 1 B PRO 2   ? B PRO 2   
22 1 Y 1 B GLN 3   ? B GLN 3   
23 1 Y 1 B ASP 4   ? B ASP 4   
24 1 Y 1 B SER 312 ? B SER 312 
25 1 Y 1 B GLY 313 ? B GLY 313 
26 1 Y 1 B ARG 314 ? B ARG 314 
27 1 Y 1 B TYR 315 ? B TYR 315 
28 1 Y 1 B ASP 316 ? B ASP 316 
29 1 Y 1 B ALA 317 ? B ALA 317 
30 1 Y 1 B GLU 318 ? B GLU 318 
31 1 Y 1 B PHE 319 ? B PHE 319 
32 1 Y 1 B ALA 320 ? B ALA 320 
33 1 Y 1 B LEU 321 ? B LEU 321 
34 1 Y 1 B ALA 322 ? B ALA 322 
35 1 Y 1 B ALA 323 ? B ALA 323 
36 1 Y 1 B GLY 324 ? B GLY 324 
37 1 Y 1 B ALA 325 ? B ALA 325 
38 1 Y 1 B GLN 326 ? B GLN 326 
39 1 Y 1 B GLY 327 ? B GLY 327 
40 1 Y 1 B TYR 328 ? B TYR 328 
41 1 Y 1 B LEU 329 ? B LEU 329 
42 1 Y 1 B GLU 330 ? B GLU 330 
43 1 Y 1 B GLU 331 ? B GLU 331 
44 1 Y 1 B LEU 332 ? B LEU 332 
45 1 Y 1 B GLY 333 ? B GLY 333 
46 1 Y 1 B SER 334 ? B SER 334 
47 1 Y 1 B SER 335 ? B SER 335 
48 1 Y 1 B ALA 336 ? B ALA 336 
49 1 Y 1 B HIS 337 ? B HIS 337 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
FDF PA   P  N S 88  
FDF PB   P  N N 89  
FDF C1   C  N N 90  
FDF O1   O  N N 91  
FDF O1A  O  N N 92  
FDF O1B  O  N N 93  
FDF C2   C  N N 94  
FDF O2A  O  N N 95  
FDF O2B  O  N N 96  
FDF C3   C  N N 97  
FDF O3A  O  N N 98  
FDF O3B  O  N N 99  
FDF C4   C  N N 100 
FDF C5   C  N N 101 
FDF C6   C  N N 102 
FDF C7   C  N N 103 
FDF C8   C  N N 104 
FDF C9   C  N N 105 
FDF C10  C  N N 106 
FDF C11  C  N N 107 
FDF C12  C  N N 108 
FDF C13  C  N N 109 
FDF C14  C  N N 110 
FDF C15  C  N N 111 
FDF F1   F  N N 112 
FDF F2   F  N N 113 
FDF H1   H  N N 114 
FDF H1A  H  N N 115 
FDF HO1A H  N N 116 
FDF HO1B H  N N 117 
FDF H2   H  N N 118 
FDF HO3B H  N N 119 
FDF H4   H  N N 120 
FDF H4A  H  N N 121 
FDF H4B  H  N N 122 
FDF H5   H  N N 123 
FDF H5A  H  N N 124 
FDF H6   H  N N 125 
FDF H6A  H  N N 126 
FDF H7   H  N N 127 
FDF H9   H  N N 128 
FDF H9A  H  N N 129 
FDF H10  H  N N 130 
FDF H10A H  N N 131 
FDF H10B H  N N 132 
FDF H11  H  N N 133 
FDF H11A H  N N 134 
FDF H12  H  N N 135 
FDF H14  H  N N 136 
FDF H14A H  N N 137 
FDF H15  H  N N 138 
FDF H15A H  N N 139 
GLN N    N  N N 140 
GLN CA   C  N S 141 
GLN C    C  N N 142 
GLN O    O  N N 143 
GLN CB   C  N N 144 
GLN CG   C  N N 145 
GLN CD   C  N N 146 
GLN OE1  O  N N 147 
GLN NE2  N  N N 148 
GLN OXT  O  N N 149 
GLN H    H  N N 150 
GLN H2   H  N N 151 
GLN HA   H  N N 152 
GLN HB2  H  N N 153 
GLN HB3  H  N N 154 
GLN HG2  H  N N 155 
GLN HG3  H  N N 156 
GLN HE21 H  N N 157 
GLN HE22 H  N N 158 
GLN HXT  H  N N 159 
GLU N    N  N N 160 
GLU CA   C  N S 161 
GLU C    C  N N 162 
GLU O    O  N N 163 
GLU CB   C  N N 164 
GLU CG   C  N N 165 
GLU CD   C  N N 166 
GLU OE1  O  N N 167 
GLU OE2  O  N N 168 
GLU OXT  O  N N 169 
GLU H    H  N N 170 
GLU H2   H  N N 171 
GLU HA   H  N N 172 
GLU HB2  H  N N 173 
GLU HB3  H  N N 174 
GLU HG2  H  N N 175 
GLU HG3  H  N N 176 
GLU HE2  H  N N 177 
GLU HXT  H  N N 178 
GLY N    N  N N 179 
GLY CA   C  N N 180 
GLY C    C  N N 181 
GLY O    O  N N 182 
GLY OXT  O  N N 183 
GLY H    H  N N 184 
GLY H2   H  N N 185 
GLY HA2  H  N N 186 
GLY HA3  H  N N 187 
GLY HXT  H  N N 188 
HIS N    N  N N 189 
HIS CA   C  N S 190 
HIS C    C  N N 191 
HIS O    O  N N 192 
HIS CB   C  N N 193 
HIS CG   C  Y N 194 
HIS ND1  N  Y N 195 
HIS CD2  C  Y N 196 
HIS CE1  C  Y N 197 
HIS NE2  N  Y N 198 
HIS OXT  O  N N 199 
HIS H    H  N N 200 
HIS H2   H  N N 201 
HIS HA   H  N N 202 
HIS HB2  H  N N 203 
HIS HB3  H  N N 204 
HIS HD1  H  N N 205 
HIS HD2  H  N N 206 
HIS HE1  H  N N 207 
HIS HE2  H  N N 208 
HIS HXT  H  N N 209 
HOH O    O  N N 210 
HOH H1   H  N N 211 
HOH H2   H  N N 212 
ILE N    N  N N 213 
ILE CA   C  N S 214 
ILE C    C  N N 215 
ILE O    O  N N 216 
ILE CB   C  N S 217 
ILE CG1  C  N N 218 
ILE CG2  C  N N 219 
ILE CD1  C  N N 220 
ILE OXT  O  N N 221 
ILE H    H  N N 222 
ILE H2   H  N N 223 
ILE HA   H  N N 224 
ILE HB   H  N N 225 
ILE HG12 H  N N 226 
ILE HG13 H  N N 227 
ILE HG21 H  N N 228 
ILE HG22 H  N N 229 
ILE HG23 H  N N 230 
ILE HD11 H  N N 231 
ILE HD12 H  N N 232 
ILE HD13 H  N N 233 
ILE HXT  H  N N 234 
LEU N    N  N N 235 
LEU CA   C  N S 236 
LEU C    C  N N 237 
LEU O    O  N N 238 
LEU CB   C  N N 239 
LEU CG   C  N N 240 
LEU CD1  C  N N 241 
LEU CD2  C  N N 242 
LEU OXT  O  N N 243 
LEU H    H  N N 244 
LEU H2   H  N N 245 
LEU HA   H  N N 246 
LEU HB2  H  N N 247 
LEU HB3  H  N N 248 
LEU HG   H  N N 249 
LEU HD11 H  N N 250 
LEU HD12 H  N N 251 
LEU HD13 H  N N 252 
LEU HD21 H  N N 253 
LEU HD22 H  N N 254 
LEU HD23 H  N N 255 
LEU HXT  H  N N 256 
LYS N    N  N N 257 
LYS CA   C  N S 258 
LYS C    C  N N 259 
LYS O    O  N N 260 
LYS CB   C  N N 261 
LYS CG   C  N N 262 
LYS CD   C  N N 263 
LYS CE   C  N N 264 
LYS NZ   N  N N 265 
LYS OXT  O  N N 266 
LYS H    H  N N 267 
LYS H2   H  N N 268 
LYS HA   H  N N 269 
LYS HB2  H  N N 270 
LYS HB3  H  N N 271 
LYS HG2  H  N N 272 
LYS HG3  H  N N 273 
LYS HD2  H  N N 274 
LYS HD3  H  N N 275 
LYS HE2  H  N N 276 
LYS HE3  H  N N 277 
LYS HZ1  H  N N 278 
LYS HZ2  H  N N 279 
LYS HZ3  H  N N 280 
LYS HXT  H  N N 281 
MET N    N  N N 282 
MET CA   C  N S 283 
MET C    C  N N 284 
MET O    O  N N 285 
MET CB   C  N N 286 
MET CG   C  N N 287 
MET SD   S  N N 288 
MET CE   C  N N 289 
MET OXT  O  N N 290 
MET H    H  N N 291 
MET H2   H  N N 292 
MET HA   H  N N 293 
MET HB2  H  N N 294 
MET HB3  H  N N 295 
MET HG2  H  N N 296 
MET HG3  H  N N 297 
MET HE1  H  N N 298 
MET HE2  H  N N 299 
MET HE3  H  N N 300 
MET HXT  H  N N 301 
MG  MG   MG N N 302 
PHE N    N  N N 303 
PHE CA   C  N S 304 
PHE C    C  N N 305 
PHE O    O  N N 306 
PHE CB   C  N N 307 
PHE CG   C  Y N 308 
PHE CD1  C  Y N 309 
PHE CD2  C  Y N 310 
PHE CE1  C  Y N 311 
PHE CE2  C  Y N 312 
PHE CZ   C  Y N 313 
PHE OXT  O  N N 314 
PHE H    H  N N 315 
PHE H2   H  N N 316 
PHE HA   H  N N 317 
PHE HB2  H  N N 318 
PHE HB3  H  N N 319 
PHE HD1  H  N N 320 
PHE HD2  H  N N 321 
PHE HE1  H  N N 322 
PHE HE2  H  N N 323 
PHE HZ   H  N N 324 
PHE HXT  H  N N 325 
PRO N    N  N N 326 
PRO CA   C  N S 327 
PRO C    C  N N 328 
PRO O    O  N N 329 
PRO CB   C  N N 330 
PRO CG   C  N N 331 
PRO CD   C  N N 332 
PRO OXT  O  N N 333 
PRO H    H  N N 334 
PRO HA   H  N N 335 
PRO HB2  H  N N 336 
PRO HB3  H  N N 337 
PRO HG2  H  N N 338 
PRO HG3  H  N N 339 
PRO HD2  H  N N 340 
PRO HD3  H  N N 341 
PRO HXT  H  N N 342 
SER N    N  N N 343 
SER CA   C  N S 344 
SER C    C  N N 345 
SER O    O  N N 346 
SER CB   C  N N 347 
SER OG   O  N N 348 
SER OXT  O  N N 349 
SER H    H  N N 350 
SER H2   H  N N 351 
SER HA   H  N N 352 
SER HB2  H  N N 353 
SER HB3  H  N N 354 
SER HG   H  N N 355 
SER HXT  H  N N 356 
THR N    N  N N 357 
THR CA   C  N S 358 
THR C    C  N N 359 
THR O    O  N N 360 
THR CB   C  N R 361 
THR OG1  O  N N 362 
THR CG2  C  N N 363 
THR OXT  O  N N 364 
THR H    H  N N 365 
THR H2   H  N N 366 
THR HA   H  N N 367 
THR HB   H  N N 368 
THR HG1  H  N N 369 
THR HG21 H  N N 370 
THR HG22 H  N N 371 
THR HG23 H  N N 372 
THR HXT  H  N N 373 
TRP N    N  N N 374 
TRP CA   C  N S 375 
TRP C    C  N N 376 
TRP O    O  N N 377 
TRP CB   C  N N 378 
TRP CG   C  Y N 379 
TRP CD1  C  Y N 380 
TRP CD2  C  Y N 381 
TRP NE1  N  Y N 382 
TRP CE2  C  Y N 383 
TRP CE3  C  Y N 384 
TRP CZ2  C  Y N 385 
TRP CZ3  C  Y N 386 
TRP CH2  C  Y N 387 
TRP OXT  O  N N 388 
TRP H    H  N N 389 
TRP H2   H  N N 390 
TRP HA   H  N N 391 
TRP HB2  H  N N 392 
TRP HB3  H  N N 393 
TRP HD1  H  N N 394 
TRP HE1  H  N N 395 
TRP HE3  H  N N 396 
TRP HZ2  H  N N 397 
TRP HZ3  H  N N 398 
TRP HH2  H  N N 399 
TRP HXT  H  N N 400 
TYR N    N  N N 401 
TYR CA   C  N S 402 
TYR C    C  N N 403 
TYR O    O  N N 404 
TYR CB   C  N N 405 
TYR CG   C  Y N 406 
TYR CD1  C  Y N 407 
TYR CD2  C  Y N 408 
TYR CE1  C  Y N 409 
TYR CE2  C  Y N 410 
TYR CZ   C  Y N 411 
TYR OH   O  N N 412 
TYR OXT  O  N N 413 
TYR H    H  N N 414 
TYR H2   H  N N 415 
TYR HA   H  N N 416 
TYR HB2  H  N N 417 
TYR HB3  H  N N 418 
TYR HD1  H  N N 419 
TYR HD2  H  N N 420 
TYR HE1  H  N N 421 
TYR HE2  H  N N 422 
TYR HH   H  N N 423 
TYR HXT  H  N N 424 
VAL N    N  N N 425 
VAL CA   C  N S 426 
VAL C    C  N N 427 
VAL O    O  N N 428 
VAL CB   C  N N 429 
VAL CG1  C  N N 430 
VAL CG2  C  N N 431 
VAL OXT  O  N N 432 
VAL H    H  N N 433 
VAL H2   H  N N 434 
VAL HA   H  N N 435 
VAL HB   H  N N 436 
VAL HG11 H  N N 437 
VAL HG12 H  N N 438 
VAL HG13 H  N N 439 
VAL HG21 H  N N 440 
VAL HG22 H  N N 441 
VAL HG23 H  N N 442 
VAL HXT  H  N N 443 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
FDF O2A PA   doub N N 83  
FDF O3A PA   sing N N 84  
FDF PA  O1A  sing N N 85  
FDF PA  O1   sing N N 86  
FDF O2B PB   doub N N 87  
FDF O1B PB   sing N N 88  
FDF O3B PB   sing N N 89  
FDF PB  O3A  sing N N 90  
FDF C1  O1   sing N N 91  
FDF C1  C2   sing N N 92  
FDF C1  H1   sing N E 93  
FDF C1  H1A  sing N N 94  
FDF O1A HO1A sing N N 95  
FDF O1B HO1B sing N N 96  
FDF C2  C3   doub N N 97  
FDF C2  H2   sing N N 98  
FDF C3  C4   sing N N 99  
FDF C3  C5   sing N N 100 
FDF O3B HO3B sing N N 101 
FDF C4  H4   sing N N 102 
FDF C4  H4A  sing N N 103 
FDF C4  H4B  sing N N 104 
FDF C6  C5   sing N N 105 
FDF C5  H5   sing N N 106 
FDF C5  H5A  sing N N 107 
FDF C7  C6   sing N N 108 
FDF C6  H6   sing N N 109 
FDF C6  H6A  sing N N 110 
FDF C8  C7   doub N N 111 
FDF C7  H7   sing N E 112 
FDF C9  C8   sing N N 113 
FDF C8  C10  sing N N 114 
FDF C11 C9   sing N N 115 
FDF C9  H9   sing N N 116 
FDF C9  H9A  sing N N 117 
FDF C10 H10  sing N N 118 
FDF C10 H10A sing N N 119 
FDF C10 H10B sing N N 120 
FDF C11 C12  sing N N 121 
FDF C11 H11  sing N N 122 
FDF C11 H11A sing N N 123 
FDF C13 C12  doub N N 124 
FDF C12 H12  sing N N 125 
FDF C15 C13  sing N N 126 
FDF C13 C14  sing N N 127 
FDF F2  C14  sing N N 128 
FDF C14 H14  sing N N 129 
FDF C14 H14A sing N N 130 
FDF C15 F1   sing N N 131 
FDF C15 H15  sing N N 132 
FDF C15 H15A sing N N 133 
GLN N   CA   sing N N 134 
GLN N   H    sing N N 135 
GLN N   H2   sing N N 136 
GLN CA  C    sing N N 137 
GLN CA  CB   sing N N 138 
GLN CA  HA   sing N N 139 
GLN C   O    doub N N 140 
GLN C   OXT  sing N N 141 
GLN CB  CG   sing N N 142 
GLN CB  HB2  sing N N 143 
GLN CB  HB3  sing N N 144 
GLN CG  CD   sing N N 145 
GLN CG  HG2  sing N N 146 
GLN CG  HG3  sing N N 147 
GLN CD  OE1  doub N N 148 
GLN CD  NE2  sing N N 149 
GLN NE2 HE21 sing N N 150 
GLN NE2 HE22 sing N N 151 
GLN OXT HXT  sing N N 152 
GLU N   CA   sing N N 153 
GLU N   H    sing N N 154 
GLU N   H2   sing N N 155 
GLU CA  C    sing N N 156 
GLU CA  CB   sing N N 157 
GLU CA  HA   sing N N 158 
GLU C   O    doub N N 159 
GLU C   OXT  sing N N 160 
GLU CB  CG   sing N N 161 
GLU CB  HB2  sing N N 162 
GLU CB  HB3  sing N N 163 
GLU CG  CD   sing N N 164 
GLU CG  HG2  sing N N 165 
GLU CG  HG3  sing N N 166 
GLU CD  OE1  doub N N 167 
GLU CD  OE2  sing N N 168 
GLU OE2 HE2  sing N N 169 
GLU OXT HXT  sing N N 170 
GLY N   CA   sing N N 171 
GLY N   H    sing N N 172 
GLY N   H2   sing N N 173 
GLY CA  C    sing N N 174 
GLY CA  HA2  sing N N 175 
GLY CA  HA3  sing N N 176 
GLY C   O    doub N N 177 
GLY C   OXT  sing N N 178 
GLY OXT HXT  sing N N 179 
HIS N   CA   sing N N 180 
HIS N   H    sing N N 181 
HIS N   H2   sing N N 182 
HIS CA  C    sing N N 183 
HIS CA  CB   sing N N 184 
HIS CA  HA   sing N N 185 
HIS C   O    doub N N 186 
HIS C   OXT  sing N N 187 
HIS CB  CG   sing N N 188 
HIS CB  HB2  sing N N 189 
HIS CB  HB3  sing N N 190 
HIS CG  ND1  sing Y N 191 
HIS CG  CD2  doub Y N 192 
HIS ND1 CE1  doub Y N 193 
HIS ND1 HD1  sing N N 194 
HIS CD2 NE2  sing Y N 195 
HIS CD2 HD2  sing N N 196 
HIS CE1 NE2  sing Y N 197 
HIS CE1 HE1  sing N N 198 
HIS NE2 HE2  sing N N 199 
HIS OXT HXT  sing N N 200 
HOH O   H1   sing N N 201 
HOH O   H2   sing N N 202 
ILE N   CA   sing N N 203 
ILE N   H    sing N N 204 
ILE N   H2   sing N N 205 
ILE CA  C    sing N N 206 
ILE CA  CB   sing N N 207 
ILE CA  HA   sing N N 208 
ILE C   O    doub N N 209 
ILE C   OXT  sing N N 210 
ILE CB  CG1  sing N N 211 
ILE CB  CG2  sing N N 212 
ILE CB  HB   sing N N 213 
ILE CG1 CD1  sing N N 214 
ILE CG1 HG12 sing N N 215 
ILE CG1 HG13 sing N N 216 
ILE CG2 HG21 sing N N 217 
ILE CG2 HG22 sing N N 218 
ILE CG2 HG23 sing N N 219 
ILE CD1 HD11 sing N N 220 
ILE CD1 HD12 sing N N 221 
ILE CD1 HD13 sing N N 222 
ILE OXT HXT  sing N N 223 
LEU N   CA   sing N N 224 
LEU N   H    sing N N 225 
LEU N   H2   sing N N 226 
LEU CA  C    sing N N 227 
LEU CA  CB   sing N N 228 
LEU CA  HA   sing N N 229 
LEU C   O    doub N N 230 
LEU C   OXT  sing N N 231 
LEU CB  CG   sing N N 232 
LEU CB  HB2  sing N N 233 
LEU CB  HB3  sing N N 234 
LEU CG  CD1  sing N N 235 
LEU CG  CD2  sing N N 236 
LEU CG  HG   sing N N 237 
LEU CD1 HD11 sing N N 238 
LEU CD1 HD12 sing N N 239 
LEU CD1 HD13 sing N N 240 
LEU CD2 HD21 sing N N 241 
LEU CD2 HD22 sing N N 242 
LEU CD2 HD23 sing N N 243 
LEU OXT HXT  sing N N 244 
LYS N   CA   sing N N 245 
LYS N   H    sing N N 246 
LYS N   H2   sing N N 247 
LYS CA  C    sing N N 248 
LYS CA  CB   sing N N 249 
LYS CA  HA   sing N N 250 
LYS C   O    doub N N 251 
LYS C   OXT  sing N N 252 
LYS CB  CG   sing N N 253 
LYS CB  HB2  sing N N 254 
LYS CB  HB3  sing N N 255 
LYS CG  CD   sing N N 256 
LYS CG  HG2  sing N N 257 
LYS CG  HG3  sing N N 258 
LYS CD  CE   sing N N 259 
LYS CD  HD2  sing N N 260 
LYS CD  HD3  sing N N 261 
LYS CE  NZ   sing N N 262 
LYS CE  HE2  sing N N 263 
LYS CE  HE3  sing N N 264 
LYS NZ  HZ1  sing N N 265 
LYS NZ  HZ2  sing N N 266 
LYS NZ  HZ3  sing N N 267 
LYS OXT HXT  sing N N 268 
MET N   CA   sing N N 269 
MET N   H    sing N N 270 
MET N   H2   sing N N 271 
MET CA  C    sing N N 272 
MET CA  CB   sing N N 273 
MET CA  HA   sing N N 274 
MET C   O    doub N N 275 
MET C   OXT  sing N N 276 
MET CB  CG   sing N N 277 
MET CB  HB2  sing N N 278 
MET CB  HB3  sing N N 279 
MET CG  SD   sing N N 280 
MET CG  HG2  sing N N 281 
MET CG  HG3  sing N N 282 
MET SD  CE   sing N N 283 
MET CE  HE1  sing N N 284 
MET CE  HE2  sing N N 285 
MET CE  HE3  sing N N 286 
MET OXT HXT  sing N N 287 
PHE N   CA   sing N N 288 
PHE N   H    sing N N 289 
PHE N   H2   sing N N 290 
PHE CA  C    sing N N 291 
PHE CA  CB   sing N N 292 
PHE CA  HA   sing N N 293 
PHE C   O    doub N N 294 
PHE C   OXT  sing N N 295 
PHE CB  CG   sing N N 296 
PHE CB  HB2  sing N N 297 
PHE CB  HB3  sing N N 298 
PHE CG  CD1  doub Y N 299 
PHE CG  CD2  sing Y N 300 
PHE CD1 CE1  sing Y N 301 
PHE CD1 HD1  sing N N 302 
PHE CD2 CE2  doub Y N 303 
PHE CD2 HD2  sing N N 304 
PHE CE1 CZ   doub Y N 305 
PHE CE1 HE1  sing N N 306 
PHE CE2 CZ   sing Y N 307 
PHE CE2 HE2  sing N N 308 
PHE CZ  HZ   sing N N 309 
PHE OXT HXT  sing N N 310 
PRO N   CA   sing N N 311 
PRO N   CD   sing N N 312 
PRO N   H    sing N N 313 
PRO CA  C    sing N N 314 
PRO CA  CB   sing N N 315 
PRO CA  HA   sing N N 316 
PRO C   O    doub N N 317 
PRO C   OXT  sing N N 318 
PRO CB  CG   sing N N 319 
PRO CB  HB2  sing N N 320 
PRO CB  HB3  sing N N 321 
PRO CG  CD   sing N N 322 
PRO CG  HG2  sing N N 323 
PRO CG  HG3  sing N N 324 
PRO CD  HD2  sing N N 325 
PRO CD  HD3  sing N N 326 
PRO OXT HXT  sing N N 327 
SER N   CA   sing N N 328 
SER N   H    sing N N 329 
SER N   H2   sing N N 330 
SER CA  C    sing N N 331 
SER CA  CB   sing N N 332 
SER CA  HA   sing N N 333 
SER C   O    doub N N 334 
SER C   OXT  sing N N 335 
SER CB  OG   sing N N 336 
SER CB  HB2  sing N N 337 
SER CB  HB3  sing N N 338 
SER OG  HG   sing N N 339 
SER OXT HXT  sing N N 340 
THR N   CA   sing N N 341 
THR N   H    sing N N 342 
THR N   H2   sing N N 343 
THR CA  C    sing N N 344 
THR CA  CB   sing N N 345 
THR CA  HA   sing N N 346 
THR C   O    doub N N 347 
THR C   OXT  sing N N 348 
THR CB  OG1  sing N N 349 
THR CB  CG2  sing N N 350 
THR CB  HB   sing N N 351 
THR OG1 HG1  sing N N 352 
THR CG2 HG21 sing N N 353 
THR CG2 HG22 sing N N 354 
THR CG2 HG23 sing N N 355 
THR OXT HXT  sing N N 356 
TRP N   CA   sing N N 357 
TRP N   H    sing N N 358 
TRP N   H2   sing N N 359 
TRP CA  C    sing N N 360 
TRP CA  CB   sing N N 361 
TRP CA  HA   sing N N 362 
TRP C   O    doub N N 363 
TRP C   OXT  sing N N 364 
TRP CB  CG   sing N N 365 
TRP CB  HB2  sing N N 366 
TRP CB  HB3  sing N N 367 
TRP CG  CD1  doub Y N 368 
TRP CG  CD2  sing Y N 369 
TRP CD1 NE1  sing Y N 370 
TRP CD1 HD1  sing N N 371 
TRP CD2 CE2  doub Y N 372 
TRP CD2 CE3  sing Y N 373 
TRP NE1 CE2  sing Y N 374 
TRP NE1 HE1  sing N N 375 
TRP CE2 CZ2  sing Y N 376 
TRP CE3 CZ3  doub Y N 377 
TRP CE3 HE3  sing N N 378 
TRP CZ2 CH2  doub Y N 379 
TRP CZ2 HZ2  sing N N 380 
TRP CZ3 CH2  sing Y N 381 
TRP CZ3 HZ3  sing N N 382 
TRP CH2 HH2  sing N N 383 
TRP OXT HXT  sing N N 384 
TYR N   CA   sing N N 385 
TYR N   H    sing N N 386 
TYR N   H2   sing N N 387 
TYR CA  C    sing N N 388 
TYR CA  CB   sing N N 389 
TYR CA  HA   sing N N 390 
TYR C   O    doub N N 391 
TYR C   OXT  sing N N 392 
TYR CB  CG   sing N N 393 
TYR CB  HB2  sing N N 394 
TYR CB  HB3  sing N N 395 
TYR CG  CD1  doub Y N 396 
TYR CG  CD2  sing Y N 397 
TYR CD1 CE1  sing Y N 398 
TYR CD1 HD1  sing N N 399 
TYR CD2 CE2  doub Y N 400 
TYR CD2 HD2  sing N N 401 
TYR CE1 CZ   doub Y N 402 
TYR CE1 HE1  sing N N 403 
TYR CE2 CZ   sing Y N 404 
TYR CE2 HE2  sing N N 405 
TYR CZ  OH   sing N N 406 
TYR OH  HH   sing N N 407 
TYR OXT HXT  sing N N 408 
VAL N   CA   sing N N 409 
VAL N   H    sing N N 410 
VAL N   H2   sing N N 411 
VAL CA  C    sing N N 412 
VAL CA  CB   sing N N 413 
VAL CA  HA   sing N N 414 
VAL C   O    doub N N 415 
VAL C   OXT  sing N N 416 
VAL CB  CG1  sing N N 417 
VAL CB  CG2  sing N N 418 
VAL CB  HB   sing N N 419 
VAL CG1 HG11 sing N N 420 
VAL CG1 HG12 sing N N 421 
VAL CG1 HG13 sing N N 422 
VAL CG2 HG21 sing N N 423 
VAL CG2 HG22 sing N N 424 
VAL CG2 HG23 sing N N 425 
VAL OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6WKD 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 63' 
_space_group.name_Hall        'P 6c' 
_space_group.IT_number        173 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9C7M 
_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]   0.005539 
_atom_sites.fract_transf_matrix[1][2]   0.003198 
_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]   0.006396 
_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]   0.017902 
_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.
;
? 
F  ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 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  ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-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   . ASP A 1 6   ? -69.002  -0.815 14.849  1.00 97.13  ? 6   ASP A N   1 
ATOM   2    C  CA  . ASP A 1 6   ? -69.406  -1.228 16.189  1.00 111.00 ? 6   ASP A CA  1 
ATOM   3    C  C   . ASP A 1 6   ? -68.886  -0.253 17.242  1.00 110.77 ? 6   ASP A C   1 
ATOM   4    O  O   . ASP A 1 6   ? -67.750  0.218  17.161  1.00 108.20 ? 6   ASP A O   1 
ATOM   5    C  CB  . ASP A 1 6   ? -68.909  -2.645 16.488  1.00 108.32 ? 6   ASP A CB  1 
ATOM   6    N  N   . PHE A 1 7   ? -69.725  0.049  18.231  1.00 110.63 ? 7   PHE A N   1 
ATOM   7    C  CA  . PHE A 1 7   ? -69.388  1.006  19.274  1.00 110.18 ? 7   PHE A CA  1 
ATOM   8    C  C   . PHE A 1 7   ? -69.915  0.504  20.610  1.00 107.49 ? 7   PHE A C   1 
ATOM   9    O  O   . PHE A 1 7   ? -70.632  -0.497 20.687  1.00 112.67 ? 7   PHE A O   1 
ATOM   10   C  CB  . PHE A 1 7   ? -69.958  2.397  18.972  1.00 108.40 ? 7   PHE A CB  1 
ATOM   11   C  CG  . PHE A 1 7   ? -69.527  2.955  17.647  1.00 108.35 ? 7   PHE A CG  1 
ATOM   12   C  CD1 . PHE A 1 7   ? -68.333  3.643  17.528  1.00 108.41 ? 7   PHE A CD1 1 
ATOM   13   C  CD2 . PHE A 1 7   ? -70.315  2.789  16.520  1.00 107.64 ? 7   PHE A CD2 1 
ATOM   14   C  CE1 . PHE A 1 7   ? -67.935  4.165  16.314  1.00 115.25 ? 7   PHE A CE1 1 
ATOM   15   C  CE2 . PHE A 1 7   ? -69.919  3.304  15.299  1.00 112.46 ? 7   PHE A CE2 1 
ATOM   16   C  CZ  . PHE A 1 7   ? -68.727  3.993  15.196  1.00 112.53 ? 7   PHE A CZ  1 
ATOM   17   N  N   . HIS A 1 8   ? -69.555  1.222  21.671  1.00 106.18 ? 8   HIS A N   1 
ATOM   18   C  CA  . HIS A 1 8   ? -69.997  0.908  23.028  1.00 112.76 ? 8   HIS A CA  1 
ATOM   19   C  C   . HIS A 1 8   ? -71.196  1.791  23.354  1.00 111.52 ? 8   HIS A C   1 
ATOM   20   O  O   . HIS A 1 8   ? -71.041  2.973  23.669  1.00 104.54 ? 8   HIS A O   1 
ATOM   21   C  CB  . HIS A 1 8   ? -68.867  1.117  24.031  1.00 107.28 ? 8   HIS A CB  1 
ATOM   22   C  CG  . HIS A 1 8   ? -69.291  0.974  25.460  1.00 110.25 ? 8   HIS A CG  1 
ATOM   23   N  ND1 . HIS A 1 8   ? -68.887  1.847  26.448  1.00 107.45 ? 8   HIS A ND1 1 
ATOM   24   C  CD2 . HIS A 1 8   ? -70.084  0.060  26.068  1.00 109.05 ? 8   HIS A CD2 1 
ATOM   25   C  CE1 . HIS A 1 8   ? -69.412  1.477  27.603  1.00 106.20 ? 8   HIS A CE1 1 
ATOM   26   N  NE2 . HIS A 1 8   ? -70.143  0.396  27.400  1.00 111.14 ? 8   HIS A NE2 1 
ATOM   27   N  N   . ILE A 1 9   ? -72.393  1.216  23.276  1.00 109.20 ? 9   ILE A N   1 
ATOM   28   C  CA  . ILE A 1 9   ? -73.624  1.918  23.635  1.00 100.67 ? 9   ILE A CA  1 
ATOM   29   C  C   . ILE A 1 9   ? -74.277  1.177  24.795  1.00 95.33  ? 9   ILE A C   1 
ATOM   30   O  O   . ILE A 1 9   ? -75.175  0.353  24.569  1.00 93.41  ? 9   ILE A O   1 
ATOM   31   C  CB  . ILE A 1 9   ? -74.592  2.017  22.443  1.00 101.34 ? 9   ILE A CB  1 
ATOM   32   C  CG1 . ILE A 1 9   ? -73.837  2.304  21.139  1.00 99.40  ? 9   ILE A CG1 1 
ATOM   33   C  CG2 . ILE A 1 9   ? -75.650  3.082  22.708  1.00 92.42  ? 9   ILE A CG2 1 
ATOM   34   C  CD1 . ILE A 1 9   ? -73.614  3.773  20.849  1.00 93.51  ? 9   ILE A CD1 1 
ATOM   35   N  N   . PRO A 1 10  ? -73.868  1.426  26.046  1.00 99.39  ? 10  PRO A N   1 
ATOM   36   C  CA  . PRO A 1 10  ? -74.443  0.675  27.173  1.00 89.86  ? 10  PRO A CA  1 
ATOM   37   C  C   . PRO A 1 10  ? -75.871  1.085  27.512  1.00 88.65  ? 10  PRO A C   1 
ATOM   38   O  O   . PRO A 1 10  ? -76.155  1.485  28.645  1.00 93.11  ? 10  PRO A O   1 
ATOM   39   C  CB  . PRO A 1 10  ? -73.481  0.990  28.325  1.00 85.23  ? 10  PRO A CB  1 
ATOM   40   C  CG  . PRO A 1 10  ? -72.908  2.319  27.977  1.00 95.29  ? 10  PRO A CG  1 
ATOM   41   C  CD  . PRO A 1 10  ? -72.790  2.335  26.477  1.00 97.05  ? 10  PRO A CD  1 
ATOM   42   N  N   . LEU A 1 11  ? -76.775  0.981  26.542  1.00 85.50  ? 11  LEU A N   1 
ATOM   43   C  CA  . LEU A 1 11  ? -78.183  1.296  26.716  1.00 82.43  ? 11  LEU A CA  1 
ATOM   44   C  C   . LEU A 1 11  ? -79.028  0.172  26.137  1.00 79.15  ? 11  LEU A C   1 
ATOM   45   O  O   . LEU A 1 11  ? -78.605  -0.501 25.192  1.00 84.68  ? 11  LEU A O   1 
ATOM   46   C  CB  . LEU A 1 11  ? -78.548  2.621  26.029  1.00 84.41  ? 11  LEU A CB  1 
ATOM   47   C  CG  . LEU A 1 11  ? -77.743  3.856  26.441  1.00 82.55  ? 11  LEU A CG  1 
ATOM   48   C  CD1 . LEU A 1 11  ? -78.128  5.059  25.592  1.00 77.07  ? 11  LEU A CD1 1 
ATOM   49   C  CD2 . LEU A 1 11  ? -77.933  4.156  27.919  1.00 75.86  ? 11  LEU A CD2 1 
ATOM   50   N  N   . PRO A 1 12  ? -80.221  -0.063 26.687  1.00 75.92  ? 12  PRO A N   1 
ATOM   51   C  CA  . PRO A 1 12  ? -81.063  -1.156 26.180  1.00 75.93  ? 12  PRO A CA  1 
ATOM   52   C  C   . PRO A 1 12  ? -81.778  -0.755 24.897  1.00 80.24  ? 12  PRO A C   1 
ATOM   53   O  O   . PRO A 1 12  ? -82.394  0.312  24.820  1.00 84.37  ? 12  PRO A O   1 
ATOM   54   C  CB  . PRO A 1 12  ? -82.059  -1.393 27.321  1.00 73.16  ? 12  PRO A CB  1 
ATOM   55   C  CG  . PRO A 1 12  ? -82.170  -0.067 27.984  1.00 80.05  ? 12  PRO A CG  1 
ATOM   56   C  CD  . PRO A 1 12  ? -80.807  0.578  27.876  1.00 80.99  ? 12  PRO A CD  1 
ATOM   57   N  N   . GLY A 1 13  ? -81.696  -1.619 23.889  1.00 75.53  ? 13  GLY A N   1 
ATOM   58   C  CA  . GLY A 1 13  ? -82.421  -1.379 22.653  1.00 73.27  ? 13  GLY A CA  1 
ATOM   59   C  C   . GLY A 1 13  ? -83.916  -1.530 22.872  1.00 74.49  ? 13  GLY A C   1 
ATOM   60   O  O   . GLY A 1 13  ? -84.372  -2.495 23.497  1.00 78.18  ? 13  GLY A O   1 
ATOM   61   N  N   . ARG A 1 14  ? -84.687  -0.569 22.365  1.00 71.70  ? 14  ARG A N   1 
ATOM   62   C  CA  . ARG A 1 14  ? -86.133  -0.554 22.539  1.00 66.99  ? 14  ARG A CA  1 
ATOM   63   C  C   . ARG A 1 14  ? -86.796  -0.213 21.213  1.00 70.85  ? 14  ARG A C   1 
ATOM   64   O  O   . ARG A 1 14  ? -86.231  0.509  20.387  1.00 74.71  ? 14  ARG A O   1 
ATOM   65   C  CB  . ARG A 1 14  ? -86.566  0.460  23.611  1.00 66.97  ? 14  ARG A CB  1 
ATOM   66   C  CG  . ARG A 1 14  ? -86.048  0.162  25.011  1.00 71.33  ? 14  ARG A CG  1 
ATOM   67   C  CD  . ARG A 1 14  ? -86.221  1.364  25.926  1.00 67.82  ? 14  ARG A CD  1 
ATOM   68   N  NE  . ARG A 1 14  ? -87.619  1.755  26.058  1.00 62.46  ? 14  ARG A NE  1 
ATOM   69   C  CZ  . ARG A 1 14  ? -88.026  2.904  26.579  1.00 64.30  ? 14  ARG A CZ  1 
ATOM   70   N  NH1 . ARG A 1 14  ? -87.164  3.813  27.006  1.00 59.91  ? 14  ARG A NH1 1 
ATOM   71   N  NH2 . ARG A 1 14  ? -89.331  3.149  26.668  1.00 61.82  ? 14  ARG A NH2 1 
ATOM   72   N  N   . GLN A 1 15  ? -88.005  -0.740 21.019  1.00 63.63  ? 15  GLN A N   1 
ATOM   73   C  CA  . GLN A 1 15  ? -88.788  -0.463 19.824  1.00 69.42  ? 15  GLN A CA  1 
ATOM   74   C  C   . GLN A 1 15  ? -90.266  -0.497 20.182  1.00 70.98  ? 15  GLN A C   1 
ATOM   75   O  O   . GLN A 1 15  ? -90.711  -1.384 20.914  1.00 69.94  ? 15  GLN A O   1 
ATOM   76   C  CB  . GLN A 1 15  ? -88.492  -1.466 18.700  1.00 71.40  ? 15  GLN A CB  1 
ATOM   77   C  CG  . GLN A 1 15  ? -89.300  -1.216 17.428  1.00 72.71  ? 15  GLN A CG  1 
ATOM   78   C  CD  . GLN A 1 15  ? -88.907  -2.133 16.284  1.00 76.61  ? 15  GLN A CD  1 
ATOM   79   O  OE1 . GLN A 1 15  ? -89.150  -3.337 16.328  1.00 80.02  ? 15  GLN A OE1 1 
ATOM   80   N  NE2 . GLN A 1 15  ? -88.298  -1.562 15.250  1.00 76.08  ? 15  GLN A NE2 1 
ATOM   81   N  N   . SER A 1 16  ? -91.015  0.470  19.656  1.00 71.81  ? 16  SER A N   1 
ATOM   82   C  CA  . SER A 1 16  ? -92.435  0.573  19.963  1.00 70.14  ? 16  SER A CA  1 
ATOM   83   C  C   . SER A 1 16  ? -93.155  -0.719 19.592  1.00 71.67  ? 16  SER A C   1 
ATOM   84   O  O   . SER A 1 16  ? -92.937  -1.253 18.496  1.00 72.08  ? 16  SER A O   1 
ATOM   85   C  CB  . SER A 1 16  ? -93.065  1.747  19.213  1.00 67.11  ? 16  SER A CB  1 
ATOM   86   O  OG  . SER A 1 16  ? -94.482  1.648  19.219  1.00 62.26  ? 16  SER A OG  1 
ATOM   87   N  N   . PRO A 1 17  ? -94.014  -1.249 20.465  1.00 79.32  ? 17  PRO A N   1 
ATOM   88   C  CA  . PRO A 1 17  ? -94.778  -2.453 20.100  1.00 79.20  ? 17  PRO A CA  1 
ATOM   89   C  C   . PRO A 1 17  ? -95.736  -2.235 18.943  1.00 75.60  ? 17  PRO A C   1 
ATOM   90   O  O   . PRO A 1 17  ? -96.217  -3.217 18.364  1.00 81.13  ? 17  PRO A O   1 
ATOM   91   C  CB  . PRO A 1 17  ? -95.528  -2.798 21.395  1.00 77.64  ? 17  PRO A CB  1 
ATOM   92   C  CG  . PRO A 1 17  ? -95.623  -1.494 22.135  1.00 77.35  ? 17  PRO A CG  1 
ATOM   93   C  CD  . PRO A 1 17  ? -94.352  -0.760 21.813  1.00 77.80  ? 17  PRO A CD  1 
ATOM   94   N  N   . ASP A 1 18  ? -96.029  -0.984 18.583  1.00 73.43  ? 18  ASP A N   1 
ATOM   95   C  CA  . ASP A 1 18  ? -96.917  -0.669 17.470  1.00 75.15  ? 18  ASP A CA  1 
ATOM   96   C  C   . ASP A 1 18  ? -96.146  -0.348 16.192  1.00 70.03  ? 18  ASP A C   1 
ATOM   97   O  O   . ASP A 1 18  ? -96.622  0.430  15.360  1.00 71.94  ? 18  ASP A O   1 
ATOM   98   C  CB  . ASP A 1 18  ? -97.835  0.495  17.843  1.00 76.29  ? 18  ASP A CB  1 
ATOM   99   C  CG  . ASP A 1 18  ? -99.102  0.530  17.011  1.00 75.32  ? 18  ASP A CG  1 
ATOM   100  O  OD1 . ASP A 1 18  ? -99.307  -0.400 16.204  1.00 80.36  ? 18  ASP A OD1 1 
ATOM   101  O  OD2 . ASP A 1 18  ? -99.892  1.487  17.164  1.00 75.61  ? 18  ASP A OD2 1 
ATOM   102  N  N   . HIS A 1 19  ? -94.962  -0.940 16.019  1.00 72.10  ? 19  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 19  ? -94.096  -0.578 14.902  1.00 74.70  ? 19  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 19  ? -94.546  -1.198 13.585  1.00 80.09  ? 19  HIS A C   1 
ATOM   105  O  O   . HIS A 1 19  ? -94.316  -0.610 12.522  1.00 80.45  ? 19  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 19  ? -92.653  -0.990 15.201  1.00 76.47  ? 19  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 19  ? -92.415  -2.465 15.109  1.00 83.06  ? 19  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 19  ? -93.157  -3.385 15.818  1.00 83.41  ? 19  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 19  ? -91.517  -3.179 14.390  1.00 87.09  ? 19  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 19  ? -92.726  -4.603 15.541  1.00 78.77  ? 19  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 19  ? -91.731  -4.506 14.678  1.00 88.27  ? 19  HIS A NE2 1 
ATOM   112  N  N   . ALA A 1 20  ? -95.173  -2.375 13.626  1.00 81.62  ? 20  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 20  ? -95.623  -3.013 12.393  1.00 78.69  ? 20  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 20  ? -96.676  -2.164 11.693  1.00 79.64  ? 20  ALA A C   1 
ATOM   115  O  O   . ALA A 1 20  ? -96.585  -1.908 10.486  1.00 74.22  ? 20  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 20  ? -96.164  -4.411 12.692  1.00 68.68  ? 20  ALA A CB  1 
ATOM   117  N  N   . ARG A 1 21  ? -97.686  -1.713 12.440  1.00 78.57  ? 21  ARG A N   1 
ATOM   118  C  CA  . ARG A 1 21  ? -98.688  -0.824 11.865  1.00 74.27  ? 21  ARG A CA  1 
ATOM   119  C  C   . ARG A 1 21  ? -98.054  0.474  11.380  1.00 79.21  ? 21  ARG A C   1 
ATOM   120  O  O   . ARG A 1 21  ? -98.377  0.964  10.291  1.00 76.22  ? 21  ARG A O   1 
ATOM   121  C  CB  . ARG A 1 21  ? -99.783  -0.532 12.891  1.00 65.77  ? 21  ARG A CB  1 
ATOM   122  C  CG  . ARG A 1 21  ? -100.952 0.256  12.329  1.00 75.52  ? 21  ARG A CG  1 
ATOM   123  C  CD  . ARG A 1 21  ? -101.660 1.059  13.410  1.00 77.10  ? 21  ARG A CD  1 
ATOM   124  N  NE  . ARG A 1 21  ? -100.729 1.872  14.183  1.00 76.06  ? 21  ARG A NE  1 
ATOM   125  C  CZ  . ARG A 1 21  ? -100.155 2.984  13.743  1.00 79.60  ? 21  ARG A CZ  1 
ATOM   126  N  NH1 . ARG A 1 21  ? -100.378 3.442  12.522  1.00 75.51  ? 21  ARG A NH1 1 
ATOM   127  N  NH2 . ARG A 1 21  ? -99.331  3.649  14.548  1.00 78.39  ? 21  ARG A NH2 1 
ATOM   128  N  N   . ALA A 1 22  ? -97.137  1.037  12.172  1.00 76.14  ? 22  ALA A N   1 
ATOM   129  C  CA  . ALA A 1 22  ? -96.514  2.304  11.806  1.00 73.80  ? 22  ALA A CA  1 
ATOM   130  C  C   . ALA A 1 22  ? -95.742  2.191  10.499  1.00 71.55  ? 22  ALA A C   1 
ATOM   131  O  O   . ALA A 1 22  ? -95.725  3.135  9.700   1.00 71.59  ? 22  ALA A O   1 
ATOM   132  C  CB  . ALA A 1 22  ? -95.593  2.780  12.927  1.00 69.19  ? 22  ALA A CB  1 
ATOM   133  N  N   . GLU A 1 23  ? -95.086  1.051  10.265  1.00 70.06  ? 23  GLU A N   1 
ATOM   134  C  CA  . GLU A 1 23  ? -94.373  0.857  9.008   1.00 73.36  ? 23  GLU A CA  1 
ATOM   135  C  C   . GLU A 1 23  ? -95.319  0.540  7.859   1.00 71.60  ? 23  GLU A C   1 
ATOM   136  O  O   . GLU A 1 23  ? -95.038  0.906  6.713   1.00 64.37  ? 23  GLU A O   1 
ATOM   137  C  CB  . GLU A 1 23  ? -93.340  -0.262 9.141   1.00 76.03  ? 23  GLU A CB  1 
ATOM   138  C  CG  . GLU A 1 23  ? -92.234  0.020  10.137  1.00 88.57  ? 23  GLU A CG  1 
ATOM   139  C  CD  . GLU A 1 23  ? -91.122  -1.004 10.068  1.00 94.42  ? 23  GLU A CD  1 
ATOM   140  O  OE1 . GLU A 1 23  ? -90.842  -1.497 8.953   1.00 88.91  ? 23  GLU A OE1 1 
ATOM   141  O  OE2 . GLU A 1 23  ? -90.534  -1.319 11.127  1.00 91.18  ? 23  GLU A OE2 1 
ATOM   142  N  N   . ALA A 1 24  ? -96.433  -0.138 8.140   1.00 74.09  ? 24  ALA A N   1 
ATOM   143  C  CA  . ALA A 1 24  ? -97.377  -0.479 7.084   1.00 68.83  ? 24  ALA A CA  1 
ATOM   144  C  C   . ALA A 1 24  ? -98.102  0.751  6.555   1.00 72.30  ? 24  ALA A C   1 
ATOM   145  O  O   . ALA A 1 24  ? -98.436  0.805  5.366   1.00 71.26  ? 24  ALA A O   1 
ATOM   146  C  CB  . ALA A 1 24  ? -98.387  -1.509 7.593   1.00 68.26  ? 24  ALA A CB  1 
ATOM   147  N  N   . GLU A 1 25  ? -98.345  1.745  7.409   1.00 67.88  ? 25  GLU A N   1 
ATOM   148  C  CA  . GLU A 1 25  ? -99.128  2.918  7.043   1.00 69.57  ? 25  GLU A CA  1 
ATOM   149  C  C   . GLU A 1 25  ? -98.276  4.165  6.835   1.00 65.42  ? 25  GLU A C   1 
ATOM   150  O  O   . GLU A 1 25  ? -98.829  5.257  6.660   1.00 62.23  ? 25  GLU A O   1 
ATOM   151  C  CB  . GLU A 1 25  ? -100.192 3.190  8.108   1.00 65.12  ? 25  GLU A CB  1 
ATOM   152  C  CG  . GLU A 1 25  ? -101.139 2.031  8.352   1.00 67.34  ? 25  GLU A CG  1 
ATOM   153  C  CD  . GLU A 1 25  ? -102.095 2.294  9.501   1.00 78.90  ? 25  GLU A CD  1 
ATOM   154  O  OE1 . GLU A 1 25  ? -101.837 3.225  10.293  1.00 85.85  ? 25  GLU A OE1 1 
ATOM   155  O  OE2 . GLU A 1 25  ? -103.106 1.570  9.612   1.00 89.58  ? 25  GLU A OE2 1 
ATOM   156  N  N   . GLN A 1 26  ? -96.947  4.029  6.827   1.00 56.32  ? 26  GLN A N   1 
ATOM   157  C  CA  . GLN A 1 26  ? -96.076  5.200  6.835   1.00 57.47  ? 26  GLN A CA  1 
ATOM   158  C  C   . GLN A 1 26  ? -96.226  6.069  5.590   1.00 66.26  ? 26  GLN A C   1 
ATOM   159  O  O   . GLN A 1 26  ? -95.863  7.249  5.632   1.00 67.78  ? 26  GLN A O   1 
ATOM   160  C  CB  . GLN A 1 26  ? -94.616  4.766  6.986   1.00 56.26  ? 26  GLN A CB  1 
ATOM   161  C  CG  . GLN A 1 26  ? -93.929  4.383  5.685   1.00 57.36  ? 26  GLN A CG  1 
ATOM   162  C  CD  . GLN A 1 26  ? -92.602  3.689  5.913   1.00 66.90  ? 26  GLN A CD  1 
ATOM   163  O  OE1 . GLN A 1 26  ? -92.561  2.549  6.374   1.00 70.63  ? 26  GLN A OE1 1 
ATOM   164  N  NE2 . GLN A 1 26  ? -91.507  4.372  5.590   1.00 67.90  ? 26  GLN A NE2 1 
ATOM   165  N  N   . LEU A 1 27  ? -96.761  5.529  4.492   1.00 64.03  ? 27  LEU A N   1 
ATOM   166  C  CA  . LEU A 1 27  ? -96.787  6.253  3.226   1.00 61.52  ? 27  LEU A CA  1 
ATOM   167  C  C   . LEU A 1 27  ? -98.021  7.126  3.040   1.00 62.89  ? 27  LEU A C   1 
ATOM   168  O  O   . LEU A 1 27  ? -97.994  8.033  2.201   1.00 65.24  ? 27  LEU A O   1 
ATOM   169  C  CB  . LEU A 1 27  ? -96.698  5.273  2.051   1.00 59.50  ? 27  LEU A CB  1 
ATOM   170  C  CG  . LEU A 1 27  ? -95.366  4.553  1.840   1.00 59.61  ? 27  LEU A CG  1 
ATOM   171  C  CD1 . LEU A 1 27  ? -95.513  3.489  0.767   1.00 55.73  ? 27  LEU A CD1 1 
ATOM   172  C  CD2 . LEU A 1 27  ? -94.273  5.541  1.470   1.00 60.84  ? 27  LEU A CD2 1 
ATOM   173  N  N   . ALA A 1 28  ? -99.096  6.886  3.795   1.00 61.33  ? 28  ALA A N   1 
ATOM   174  C  CA  . ALA A 1 28  ? -100.341 7.604  3.539   1.00 65.38  ? 28  ALA A CA  1 
ATOM   175  C  C   . ALA A 1 28  ? -100.191 9.100  3.794   1.00 66.35  ? 28  ALA A C   1 
ATOM   176  O  O   . ALA A 1 28  ? -100.713 9.921  3.029   1.00 68.83  ? 28  ALA A O   1 
ATOM   177  C  CB  . ALA A 1 28  ? -101.473 7.021  4.386   1.00 56.99  ? 28  ALA A CB  1 
ATOM   178  N  N   . TRP A 1 29  ? -99.473  9.478  4.858   1.00 68.82  ? 29  TRP A N   1 
ATOM   179  C  CA  . TRP A 1 29  ? -99.344  10.903 5.164   1.00 70.76  ? 29  TRP A CA  1 
ATOM   180  C  C   . TRP A 1 29  ? -98.529  11.655 4.120   1.00 63.42  ? 29  TRP A C   1 
ATOM   181  O  O   . TRP A 1 29  ? -99.020  12.677 3.610   1.00 65.41  ? 29  TRP A O   1 
ATOM   182  C  CB  . TRP A 1 29  ? -98.768  11.100 6.569   1.00 60.22  ? 29  TRP A CB  1 
ATOM   183  C  CG  . TRP A 1 29  ? -98.474  12.547 6.848   1.00 63.10  ? 29  TRP A CG  1 
ATOM   184  C  CD1 . TRP A 1 29  ? -99.366  13.501 7.245   1.00 60.04  ? 29  TRP A CD1 1 
ATOM   185  C  CD2 . TRP A 1 29  ? -97.206  13.210 6.726   1.00 57.80  ? 29  TRP A CD2 1 
ATOM   186  N  NE1 . TRP A 1 29  ? -98.732  14.711 7.387   1.00 63.24  ? 29  TRP A NE1 1 
ATOM   187  C  CE2 . TRP A 1 29  ? -97.406  14.560 7.075   1.00 58.15  ? 29  TRP A CE2 1 
ATOM   188  C  CE3 . TRP A 1 29  ? -95.923  12.791 6.360   1.00 57.47  ? 29  TRP A CE3 1 
ATOM   189  C  CZ2 . TRP A 1 29  ? -96.371  15.496 7.070   1.00 55.39  ? 29  TRP A CZ2 1 
ATOM   190  C  CZ3 . TRP A 1 29  ? -94.896  13.722 6.356   1.00 63.52  ? 29  TRP A CZ3 1 
ATOM   191  C  CH2 . TRP A 1 29  ? -95.126  15.058 6.709   1.00 56.19  ? 29  TRP A CH2 1 
ATOM   192  N  N   . PRO A 1 30  ? -97.302  11.247 3.766   1.00 59.35  ? 30  PRO A N   1 
ATOM   193  C  CA  . PRO A 1 30  ? -96.542  12.053 2.798   1.00 65.38  ? 30  PRO A CA  1 
ATOM   194  C  C   . PRO A 1 30  ? -97.143  12.039 1.403   1.00 64.87  ? 30  PRO A C   1 
ATOM   195  O  O   . PRO A 1 30  ? -96.980  13.019 0.666   1.00 68.44  ? 30  PRO A O   1 
ATOM   196  C  CB  . PRO A 1 30  ? -95.145  11.418 2.827   1.00 65.08  ? 30  PRO A CB  1 
ATOM   197  C  CG  . PRO A 1 30  ? -95.372  10.030 3.279   1.00 57.93  ? 30  PRO A CG  1 
ATOM   198  C  CD  . PRO A 1 30  ? -96.527  10.080 4.227   1.00 58.83  ? 30  PRO A CD  1 
ATOM   199  N  N   . ARG A 1 31  ? -97.839  10.966 1.019   1.00 66.13  ? 31  ARG A N   1 
ATOM   200  C  CA  . ARG A 1 31  ? -98.522  10.961 -0.270  1.00 71.87  ? 31  ARG A CA  1 
ATOM   201  C  C   . ARG A 1 31  ? -99.681  11.950 -0.285  1.00 73.24  ? 31  ARG A C   1 
ATOM   202  O  O   . ARG A 1 31  ? -99.944  12.588 -1.312  1.00 76.81  ? 31  ARG A O   1 
ATOM   203  C  CB  . ARG A 1 31  ? -99.016  9.554  -0.607  1.00 74.52  ? 31  ARG A CB  1 
ATOM   204  C  CG  . ARG A 1 31  ? -97.997  8.694  -1.339  1.00 80.17  ? 31  ARG A CG  1 
ATOM   205  C  CD  . ARG A 1 31  ? -98.650  7.448  -1.920  1.00 85.65  ? 31  ARG A CD  1 
ATOM   206  N  NE  . ARG A 1 31  ? -97.752  6.720  -2.811  1.00 94.04  ? 31  ARG A NE  1 
ATOM   207  C  CZ  . ARG A 1 31  ? -97.563  7.012  -4.091  1.00 88.73  ? 31  ARG A CZ  1 
ATOM   208  N  NH1 . ARG A 1 31  ? -98.183  8.030  -4.668  1.00 83.00  ? 31  ARG A NH1 1 
ATOM   209  N  NH2 . ARG A 1 31  ? -96.729  6.266  -4.811  1.00 82.29  ? 31  ARG A NH2 1 
ATOM   210  N  N   . SER A 1 32  ? -100.387 12.091 0.841   1.00 66.87  ? 32  SER A N   1 
ATOM   211  C  CA  . SER A 1 32  ? -101.489 13.044 0.905   1.00 70.70  ? 32  SER A CA  1 
ATOM   212  C  C   . SER A 1 32  ? -101.002 14.486 0.978   1.00 74.46  ? 32  SER A C   1 
ATOM   213  O  O   . SER A 1 32  ? -101.788 15.407 0.731   1.00 74.20  ? 32  SER A O   1 
ATOM   214  C  CB  . SER A 1 32  ? -102.386 12.743 2.106   1.00 64.10  ? 32  SER A CB  1 
ATOM   215  O  OG  . SER A 1 32  ? -101.923 13.416 3.263   1.00 66.80  ? 32  SER A OG  1 
ATOM   216  N  N   . LEU A 1 33  ? -99.732  14.701 1.315   1.00 69.68  ? 33  LEU A N   1 
ATOM   217  C  CA  . LEU A 1 33  ? -99.142  16.031 1.361   1.00 68.95  ? 33  LEU A CA  1 
ATOM   218  C  C   . LEU A 1 33  ? -98.397  16.387 0.082   1.00 72.32  ? 33  LEU A C   1 
ATOM   219  O  O   . LEU A 1 33  ? -97.855  17.492 -0.017  1.00 76.73  ? 33  LEU A O   1 
ATOM   220  C  CB  . LEU A 1 33  ? -98.191  16.145 2.560   1.00 71.79  ? 33  LEU A CB  1 
ATOM   221  C  CG  . LEU A 1 33  ? -98.746  16.638 3.901   1.00 65.98  ? 33  LEU A CG  1 
ATOM   222  C  CD1 . LEU A 1 33  ? -98.886  18.150 3.903   1.00 65.58  ? 33  LEU A CD1 1 
ATOM   223  C  CD2 . LEU A 1 33  ? -100.079 15.987 4.223   1.00 67.52  ? 33  LEU A CD2 1 
ATOM   224  N  N   . GLY A 1 34  ? -98.359  15.484 -0.895  1.00 68.50  ? 34  GLY A N   1 
ATOM   225  C  CA  . GLY A 1 34  ? -97.600  15.727 -2.102  1.00 65.10  ? 34  GLY A CA  1 
ATOM   226  C  C   . GLY A 1 34  ? -96.106  15.578 -1.949  1.00 65.20  ? 34  GLY A C   1 
ATOM   227  O  O   . GLY A 1 34  ? -95.354  16.107 -2.772  1.00 70.83  ? 34  GLY A O   1 
ATOM   228  N  N   . LEU A 1 35  ? -95.648  14.872 -0.918  1.00 68.21  ? 35  LEU A N   1 
ATOM   229  C  CA  . LEU A 1 35  ? -94.221  14.684 -0.692  1.00 71.81  ? 35  LEU A CA  1 
ATOM   230  C  C   . LEU A 1 35  ? -93.676  13.455 -1.406  1.00 67.18  ? 35  LEU A C   1 
ATOM   231  O  O   . LEU A 1 35  ? -92.481  13.406 -1.724  1.00 61.20  ? 35  LEU A O   1 
ATOM   232  C  CB  . LEU A 1 35  ? -93.943  14.585 0.810   1.00 68.49  ? 35  LEU A CB  1 
ATOM   233  C  CG  . LEU A 1 35  ? -94.417  15.789 1.628   1.00 70.46  ? 35  LEU A CG  1 
ATOM   234  C  CD1 . LEU A 1 35  ? -94.252  15.537 3.122   1.00 65.32  ? 35  LEU A CD1 1 
ATOM   235  C  CD2 . LEU A 1 35  ? -93.668  17.044 1.204   1.00 66.60  ? 35  LEU A CD2 1 
ATOM   236  N  N   . ILE A 1 36  ? -94.524  12.462 -1.656  1.00 64.61  ? 36  ILE A N   1 
ATOM   237  C  CA  . ILE A 1 36  ? -94.183  11.295 -2.459  1.00 73.92  ? 36  ILE A CA  1 
ATOM   238  C  C   . ILE A 1 36  ? -95.152  11.262 -3.631  1.00 78.99  ? 36  ILE A C   1 
ATOM   239  O  O   . ILE A 1 36  ? -96.362  11.084 -3.437  1.00 81.20  ? 36  ILE A O   1 
ATOM   240  C  CB  . ILE A 1 36  ? -94.255  9.994  -1.645  1.00 76.23  ? 36  ILE A CB  1 
ATOM   241  C  CG1 . ILE A 1 36  ? -93.299  10.046 -0.446  1.00 71.36  ? 36  ILE A CG1 1 
ATOM   242  C  CG2 . ILE A 1 36  ? -93.951  8.799  -2.536  1.00 76.90  ? 36  ILE A CG2 1 
ATOM   243  C  CD1 . ILE A 1 36  ? -91.836  10.191 -0.826  1.00 71.30  ? 36  ILE A CD1 1 
ATOM   244  N  N   . ARG A 1 37  ? -94.628  11.434 -4.846  1.00 74.00  ? 37  ARG A N   1 
ATOM   245  C  CA  . ARG A 1 37  ? -95.469  11.619 -6.020  1.00 88.42  ? 37  ARG A CA  1 
ATOM   246  C  C   . ARG A 1 37  ? -95.385  10.494 -7.041  1.00 86.42  ? 37  ARG A C   1 
ATOM   247  O  O   . ARG A 1 37  ? -96.324  10.337 -7.831  1.00 89.13  ? 37  ARG A O   1 
ATOM   248  C  CB  . ARG A 1 37  ? -95.126  12.951 -6.709  1.00 91.12  ? 37  ARG A CB  1 
ATOM   249  C  CG  . ARG A 1 37  ? -94.802  14.070 -5.722  1.00 85.90  ? 37  ARG A CG  1 
ATOM   250  C  CD  . ARG A 1 37  ? -94.741  15.425 -6.400  1.00 91.34  ? 37  ARG A CD  1 
ATOM   251  N  NE  . ARG A 1 37  ? -96.072  15.962 -6.653  1.00 92.88  ? 37  ARG A NE  1 
ATOM   252  C  CZ  . ARG A 1 37  ? -96.646  16.911 -5.927  1.00 90.48  ? 37  ARG A CZ  1 
ATOM   253  N  NH1 . ARG A 1 37  ? -96.020  17.475 -4.907  1.00 87.01  ? 37  ARG A NH1 1 
ATOM   254  N  NH2 . ARG A 1 37  ? -97.878  17.307 -6.235  1.00 99.17  ? 37  ARG A NH2 1 
ATOM   255  N  N   . SER A 1 38  ? -94.309  9.713  -7.053  1.00 83.81  ? 38  SER A N   1 
ATOM   256  C  CA  . SER A 1 38  ? -94.184  8.561  -7.931  1.00 71.36  ? 38  SER A CA  1 
ATOM   257  C  C   . SER A 1 38  ? -94.039  7.295  -7.099  1.00 76.96  ? 38  SER A C   1 
ATOM   258  O  O   . SER A 1 38  ? -93.639  7.334  -5.932  1.00 80.27  ? 38  SER A O   1 
ATOM   259  C  CB  . SER A 1 38  ? -92.985  8.703  -8.871  1.00 68.26  ? 38  SER A CB  1 
ATOM   260  O  OG  . SER A 1 38  ? -91.772  8.647  -8.149  1.00 65.08  ? 38  SER A OG  1 
ATOM   261  N  N   . ASP A 1 39  ? -94.368  6.159  -7.716  1.00 78.11  ? 39  ASP A N   1 
ATOM   262  C  CA  . ASP A 1 39  ? -94.253  4.889  -7.008  1.00 68.12  ? 39  ASP A CA  1 
ATOM   263  C  C   . ASP A 1 39  ? -92.799  4.534  -6.725  1.00 68.94  ? 39  ASP A C   1 
ATOM   264  O  O   . ASP A 1 39  ? -92.506  3.916  -5.696  1.00 70.48  ? 39  ASP A O   1 
ATOM   265  C  CB  . ASP A 1 39  ? -94.937  3.778  -7.801  1.00 70.69  ? 39  ASP A CB  1 
ATOM   266  C  CG  . ASP A 1 39  ? -96.450  3.859  -7.724  1.00 75.22  ? 39  ASP A CG  1 
ATOM   267  O  OD1 . ASP A 1 39  ? -96.958  4.683  -6.936  1.00 78.65  ? 39  ASP A OD1 1 
ATOM   268  O  OD2 . ASP A 1 39  ? -97.131  3.102  -8.449  1.00 77.09  ? 39  ASP A OD2 1 
ATOM   269  N  N   . ALA A 1 40  ? -91.878  4.912  -7.615  1.00 66.78  ? 40  ALA A N   1 
ATOM   270  C  CA  . ALA A 1 40  ? -90.462  4.712  -7.327  1.00 68.80  ? 40  ALA A CA  1 
ATOM   271  C  C   . ALA A 1 40  ? -90.024  5.552  -6.133  1.00 72.74  ? 40  ALA A C   1 
ATOM   272  O  O   . ALA A 1 40  ? -89.187  5.118  -5.332  1.00 67.41  ? 40  ALA A O   1 
ATOM   273  C  CB  . ALA A 1 40  ? -89.616  5.044  -8.554  1.00 57.61  ? 40  ALA A CB  1 
ATOM   274  N  N   . ALA A 1 41  ? -90.578  6.760  -6.001  1.00 72.26  ? 41  ALA A N   1 
ATOM   275  C  CA  . ALA A 1 41  ? -90.278  7.587  -4.836  1.00 73.17  ? 41  ALA A CA  1 
ATOM   276  C  C   . ALA A 1 41  ? -90.766  6.925  -3.553  1.00 67.28  ? 41  ALA A C   1 
ATOM   277  O  O   . ALA A 1 41  ? -90.121  7.038  -2.505  1.00 65.55  ? 41  ALA A O   1 
ATOM   278  C  CB  . ALA A 1 41  ? -90.901  8.974  -4.997  1.00 66.96  ? 41  ALA A CB  1 
ATOM   279  N  N   . ALA A 1 42  ? -91.900  6.222  -3.620  1.00 63.47  ? 42  ALA A N   1 
ATOM   280  C  CA  . ALA A 1 42  ? -92.412  5.514  -2.449  1.00 66.02  ? 42  ALA A CA  1 
ATOM   281  C  C   . ALA A 1 42  ? -91.466  4.398  -2.019  1.00 69.55  ? 42  ALA A C   1 
ATOM   282  O  O   . ALA A 1 42  ? -91.160  4.252  -0.830  1.00 67.13  ? 42  ALA A O   1 
ATOM   283  C  CB  . ALA A 1 42  ? -93.807  4.960  -2.740  1.00 63.14  ? 42  ALA A CB  1 
ATOM   284  N  N   . GLU A 1 43  ? -90.991  3.595  -2.977  1.00 67.82  ? 43  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 43  ? -90.084  2.502  -2.638  1.00 66.19  ? 43  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 43  ? -88.757  3.029  -2.107  1.00 64.20  ? 43  GLU A C   1 
ATOM   287  O  O   . GLU A 1 43  ? -88.221  2.499  -1.126  1.00 67.01  ? 43  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 43  ? -89.860  1.606  -3.855  1.00 62.61  ? 43  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 43  ? -88.778  0.553  -3.662  1.00 61.26  ? 43  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 43  ? -89.128  -0.474 -2.599  1.00 66.36  ? 43  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 43  ? -90.333  -0.684 -2.336  1.00 61.91  ? 43  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 43  ? -88.193  -1.073 -2.026  1.00 65.01  ? 43  GLU A OE2 1 
ATOM   293  N  N   . ARG A 1 44  ? -88.215  4.071  -2.743  1.00 64.89  ? 44  ARG A N   1 
ATOM   294  C  CA  . ARG A 1 44  ? -87.021  4.732  -2.225  1.00 71.19  ? 44  ARG A CA  1 
ATOM   295  C  C   . ARG A 1 44  ? -87.210  5.135  -0.769  1.00 70.95  ? 44  ARG A C   1 
ATOM   296  O  O   . ARG A 1 44  ? -86.269  5.082  0.032   1.00 71.04  ? 44  ARG A O   1 
ATOM   297  C  CB  . ARG A 1 44  ? -86.706  5.958  -3.082  1.00 75.76  ? 44  ARG A CB  1 
ATOM   298  C  CG  . ARG A 1 44  ? -85.258  6.408  -3.072  1.00 78.17  ? 44  ARG A CG  1 
ATOM   299  C  CD  . ARG A 1 44  ? -84.735  6.468  -4.500  1.00 86.32  ? 44  ARG A CD  1 
ATOM   300  N  NE  . ARG A 1 44  ? -85.772  6.912  -5.427  1.00 94.22  ? 44  ARG A NE  1 
ATOM   301  C  CZ  . ARG A 1 44  ? -85.693  6.825  -6.749  1.00 95.56  ? 44  ARG A CZ  1 
ATOM   302  N  NH1 . ARG A 1 44  ? -84.628  6.314  -7.346  1.00 87.54  ? 44  ARG A NH1 1 
ATOM   303  N  NH2 . ARG A 1 44  ? -86.711  7.256  -7.490  1.00 88.35  ? 44  ARG A NH2 1 
ATOM   304  N  N   . HIS A 1 45  ? -88.434  5.526  -0.409  1.00 65.31  ? 45  HIS A N   1 
ATOM   305  C  CA  . HIS A 1 45  ? -88.730  5.941  0.956   1.00 64.74  ? 45  HIS A CA  1 
ATOM   306  C  C   . HIS A 1 45  ? -88.725  4.746  1.903   1.00 67.16  ? 45  HIS A C   1 
ATOM   307  O  O   . HIS A 1 45  ? -88.059  4.769  2.944   1.00 65.55  ? 45  HIS A O   1 
ATOM   308  C  CB  . HIS A 1 45  ? -90.082  6.659  0.986   1.00 70.89  ? 45  HIS A CB  1 
ATOM   309  C  CG  . HIS A 1 45  ? -90.300  7.502  2.202   1.00 72.05  ? 45  HIS A CG  1 
ATOM   310  N  ND1 . HIS A 1 45  ? -89.538  8.616  2.483   1.00 63.81  ? 45  HIS A ND1 1 
ATOM   311  C  CD2 . HIS A 1 45  ? -91.207  7.402  3.204   1.00 69.44  ? 45  HIS A CD2 1 
ATOM   312  C  CE1 . HIS A 1 45  ? -89.960  9.161  3.610   1.00 73.25  ? 45  HIS A CE1 1 
ATOM   313  N  NE2 . HIS A 1 45  ? -90.971  8.444  4.067   1.00 70.01  ? 45  HIS A NE2 1 
ATOM   314  N  N   . LEU A 1 46  ? -89.461  3.686  1.549   1.00 67.15  ? 46  LEU A N   1 
ATOM   315  C  CA  . LEU A 1 46  ? -89.523  2.498  2.395   1.00 56.42  ? 46  LEU A CA  1 
ATOM   316  C  C   . LEU A 1 46  ? -88.144  1.890  2.612   1.00 60.28  ? 46  LEU A C   1 
ATOM   317  O  O   . LEU A 1 46  ? -87.891  1.279  3.658   1.00 70.35  ? 46  LEU A O   1 
ATOM   318  C  CB  . LEU A 1 46  ? -90.463  1.463  1.779   1.00 58.34  ? 46  LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 46  ? -91.920  1.862  1.538   1.00 63.55  ? 46  LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 46  ? -92.639  0.784  0.737   1.00 53.39  ? 46  LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 46  ? -92.635  2.113  2.855   1.00 58.12  ? 46  LEU A CD2 1 
ATOM   322  N  N   . ARG A 1 47  ? -87.240  2.045  1.646   1.00 60.44  ? 47  ARG A N   1 
ATOM   323  C  CA  . ARG A 1 47  ? -85.881  1.552  1.817   1.00 65.88  ? 47  ARG A CA  1 
ATOM   324  C  C   . ARG A 1 47  ? -85.101  2.332  2.865   1.00 67.90  ? 47  ARG A C   1 
ATOM   325  O  O   . ARG A 1 47  ? -84.039  1.868  3.291   1.00 65.51  ? 47  ARG A O   1 
ATOM   326  C  CB  . ARG A 1 47  ? -85.139  1.588  0.481   1.00 62.92  ? 47  ARG A CB  1 
ATOM   327  C  CG  . ARG A 1 47  ? -85.573  0.503  -0.492  1.00 69.73  ? 47  ARG A CG  1 
ATOM   328  C  CD  . ARG A 1 47  ? -85.085  0.797  -1.899  1.00 71.82  ? 47  ARG A CD  1 
ATOM   329  N  NE  . ARG A 1 47  ? -85.507  -0.220 -2.853  1.00 73.05  ? 47  ARG A NE  1 
ATOM   330  C  CZ  . ARG A 1 47  ? -84.728  -1.200 -3.291  1.00 82.04  ? 47  ARG A CZ  1 
ATOM   331  N  NH1 . ARG A 1 47  ? -83.479  -1.328 -2.872  1.00 74.47  ? 47  ARG A NH1 1 
ATOM   332  N  NH2 . ARG A 1 47  ? -85.213  -2.068 -4.176  1.00 77.00  ? 47  ARG A NH2 1 
ATOM   333  N  N   . GLY A 1 48  ? -85.594  3.498  3.288   1.00 65.57  ? 48  GLY A N   1 
ATOM   334  C  CA  . GLY A 1 48  ? -84.899  4.257  4.312   1.00 69.99  ? 48  GLY A CA  1 
ATOM   335  C  C   . GLY A 1 48  ? -85.101  3.720  5.711   1.00 69.60  ? 48  GLY A C   1 
ATOM   336  O  O   . GLY A 1 48  ? -84.250  3.928  6.582   1.00 68.75  ? 48  GLY A O   1 
ATOM   337  N  N   . GLY A 1 49  ? -86.207  3.019  5.948   1.00 68.14  ? 49  GLY A N   1 
ATOM   338  C  CA  . GLY A 1 49  ? -86.520  2.525  7.278   1.00 70.41  ? 49  GLY A CA  1 
ATOM   339  C  C   . GLY A 1 49  ? -86.901  3.632  8.233   1.00 75.04  ? 49  GLY A C   1 
ATOM   340  O  O   . GLY A 1 49  ? -86.490  3.613  9.400   1.00 72.16  ? 49  GLY A O   1 
ATOM   341  N  N   . TYR A 1 50  ? -87.683  4.603  7.763   1.00 78.12  ? 50  TYR A N   1 
ATOM   342  C  CA  . TYR A 1 50  ? -87.918  5.804  8.554   1.00 72.21  ? 50  TYR A CA  1 
ATOM   343  C  C   . TYR A 1 50  ? -88.936  5.552  9.660   1.00 69.27  ? 50  TYR A C   1 
ATOM   344  O  O   . TYR A 1 50  ? -88.825  6.121  10.753  1.00 70.30  ? 50  TYR A O   1 
ATOM   345  C  CB  . TYR A 1 50  ? -88.359  6.937  7.630   1.00 65.40  ? 50  TYR A CB  1 
ATOM   346  C  CG  . TYR A 1 50  ? -87.302  7.238  6.593   1.00 69.04  ? 50  TYR A CG  1 
ATOM   347  C  CD1 . TYR A 1 50  ? -85.974  7.385  6.964   1.00 63.79  ? 50  TYR A CD1 1 
ATOM   348  C  CD2 . TYR A 1 50  ? -87.619  7.333  5.244   1.00 66.50  ? 50  TYR A CD2 1 
ATOM   349  C  CE1 . TYR A 1 50  ? -84.995  7.643  6.032   1.00 66.60  ? 50  TYR A CE1 1 
ATOM   350  C  CE2 . TYR A 1 50  ? -86.644  7.593  4.301   1.00 59.03  ? 50  TYR A CE2 1 
ATOM   351  C  CZ  . TYR A 1 50  ? -85.332  7.746  4.704   1.00 63.93  ? 50  TYR A CZ  1 
ATOM   352  O  OH  . TYR A 1 50  ? -84.345  8.005  3.783   1.00 72.92  ? 50  TYR A OH  1 
ATOM   353  N  N   . ALA A 1 51  ? -89.934  4.699  9.403   1.00 69.14  ? 51  ALA A N   1 
ATOM   354  C  CA  . ALA A 1 51  ? -90.834  4.288  10.475  1.00 73.11  ? 51  ALA A CA  1 
ATOM   355  C  C   . ALA A 1 51  ? -90.114  3.404  11.485  1.00 72.92  ? 51  ALA A C   1 
ATOM   356  O  O   . ALA A 1 51  ? -90.436  3.435  12.678  1.00 67.57  ? 51  ALA A O   1 
ATOM   357  C  CB  . ALA A 1 51  ? -92.052  3.572  9.892   1.00 68.45  ? 51  ALA A CB  1 
ATOM   358  N  N   . ASP A 1 52  ? -89.136  2.621  11.024  1.00 76.43  ? 52  ASP A N   1 
ATOM   359  C  CA  . ASP A 1 52  ? -88.304  1.836  11.930  1.00 68.47  ? 52  ASP A CA  1 
ATOM   360  C  C   . ASP A 1 52  ? -87.515  2.745  12.864  1.00 73.56  ? 52  ASP A C   1 
ATOM   361  O  O   . ASP A 1 52  ? -87.459  2.513  14.078  1.00 71.84  ? 52  ASP A O   1 
ATOM   362  C  CB  . ASP A 1 52  ? -87.364  0.943  11.118  1.00 71.18  ? 52  ASP A CB  1 
ATOM   363  C  CG  . ASP A 1 52  ? -86.559  -0.004 11.981  1.00 75.91  ? 52  ASP A CG  1 
ATOM   364  O  OD1 . ASP A 1 52  ? -87.086  -1.082 12.330  1.00 80.41  ? 52  ASP A OD1 1 
ATOM   365  O  OD2 . ASP A 1 52  ? -85.398  0.326  12.307  1.00 79.59  ? 52  ASP A OD2 1 
ATOM   366  N  N   . LEU A 1 53  ? -86.903  3.795  12.309  1.00 71.59  ? 53  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 53  ? -86.130  4.725  13.127  1.00 71.53  ? 53  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 53  ? -87.016  5.434  14.142  1.00 70.35  ? 53  LEU A C   1 
ATOM   369  O  O   . LEU A 1 53  ? -86.632  5.594  15.307  1.00 66.07  ? 53  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 53  ? -85.419  5.741  12.233  1.00 69.29  ? 53  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 53  ? -84.500  6.755  12.916  1.00 74.40  ? 53  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 53  ? -83.608  6.075  13.947  1.00 69.14  ? 53  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 53  ? -83.656  7.481  11.880  1.00 69.15  ? 53  LEU A CD2 1 
ATOM   374  N  N   . ALA A 1 54  ? -88.208  5.864  13.719  1.00 62.95  ? 54  ALA A N   1 
ATOM   375  C  CA  . ALA A 1 54  ? -89.124  6.528  14.639  1.00 66.29  ? 54  ALA A CA  1 
ATOM   376  C  C   . ALA A 1 54  ? -89.535  5.600  15.775  1.00 70.85  ? 54  ALA A C   1 
ATOM   377  O  O   . ALA A 1 54  ? -89.566  6.011  16.941  1.00 66.52  ? 54  ALA A O   1 
ATOM   378  C  CB  . ALA A 1 54  ? -90.356  7.028  13.885  1.00 64.18  ? 54  ALA A CB  1 
ATOM   379  N  N   . SER A 1 55  ? -89.847  4.341  15.456  1.00 72.66  ? 55  SER A N   1 
ATOM   380  C  CA  . SER A 1 55  ? -90.263  3.390  16.480  1.00 68.20  ? 55  SER A CA  1 
ATOM   381  C  C   . SER A 1 55  ? -89.144  3.071  17.466  1.00 65.96  ? 55  SER A C   1 
ATOM   382  O  O   . SER A 1 55  ? -89.425  2.568  18.559  1.00 61.71  ? 55  SER A O   1 
ATOM   383  C  CB  . SER A 1 55  ? -90.767  2.104  15.825  1.00 62.74  ? 55  SER A CB  1 
ATOM   384  O  OG  . SER A 1 55  ? -89.747  1.494  15.053  1.00 68.85  ? 55  SER A OG  1 
ATOM   385  N  N   . ARG A 1 56  ? -87.888  3.344  17.107  1.00 65.26  ? 56  ARG A N   1 
ATOM   386  C  CA  . ARG A 1 56  ? -86.782  3.175  18.040  1.00 64.11  ? 56  ARG A CA  1 
ATOM   387  C  C   . ARG A 1 56  ? -86.414  4.473  18.740  1.00 66.33  ? 56  ARG A C   1 
ATOM   388  O  O   . ARG A 1 56  ? -85.887  4.438  19.858  1.00 76.16  ? 56  ARG A O   1 
ATOM   389  C  CB  . ARG A 1 56  ? -85.558  2.609  17.319  1.00 59.38  ? 56  ARG A CB  1 
ATOM   390  C  CG  . ARG A 1 56  ? -85.761  1.182  16.864  1.00 67.81  ? 56  ARG A CG  1 
ATOM   391  C  CD  . ARG A 1 56  ? -84.585  0.655  16.065  1.00 76.30  ? 56  ARG A CD  1 
ATOM   392  N  NE  . ARG A 1 56  ? -84.973  -0.540 15.326  1.00 79.69  ? 56  ARG A NE  1 
ATOM   393  C  CZ  . ARG A 1 56  ? -84.938  -1.770 15.820  1.00 77.30  ? 56  ARG A CZ  1 
ATOM   394  N  NH1 . ARG A 1 56  ? -84.470  -2.016 17.032  1.00 75.57  ? 56  ARG A NH1 1 
ATOM   395  N  NH2 . ARG A 1 56  ? -85.391  -2.778 15.079  1.00 80.89  ? 56  ARG A NH2 1 
ATOM   396  N  N   . PHE A 1 57  ? -86.679  5.620  18.108  1.00 65.65  ? 57  PHE A N   1 
ATOM   397  C  CA  . PHE A 1 57  ? -86.586  6.886  18.823  1.00 65.73  ? 57  PHE A CA  1 
ATOM   398  C  C   . PHE A 1 57  ? -87.711  7.031  19.840  1.00 65.53  ? 57  PHE A C   1 
ATOM   399  O  O   . PHE A 1 57  ? -87.512  7.635  20.901  1.00 68.56  ? 57  PHE A O   1 
ATOM   400  C  CB  . PHE A 1 57  ? -86.617  8.057  17.841  1.00 61.36  ? 57  PHE A CB  1 
ATOM   401  C  CG  . PHE A 1 57  ? -85.285  8.369  17.216  1.00 63.48  ? 57  PHE A CG  1 
ATOM   402  C  CD1 . PHE A 1 57  ? -84.105  8.045  17.863  1.00 57.98  ? 57  PHE A CD1 1 
ATOM   403  C  CD2 . PHE A 1 57  ? -85.217  8.993  15.976  1.00 61.82  ? 57  PHE A CD2 1 
ATOM   404  C  CE1 . PHE A 1 57  ? -82.879  8.337  17.286  1.00 66.94  ? 57  PHE A CE1 1 
ATOM   405  C  CE2 . PHE A 1 57  ? -83.997  9.291  15.393  1.00 56.84  ? 57  PHE A CE2 1 
ATOM   406  C  CZ  . PHE A 1 57  ? -82.826  8.961  16.046  1.00 66.68  ? 57  PHE A CZ  1 
ATOM   407  N  N   . TYR A 1 58  ? -88.886  6.474  19.546  1.00 58.99  ? 58  TYR A N   1 
ATOM   408  C  CA  . TYR A 1 58  ? -90.087  6.682  20.357  1.00 64.86  ? 58  TYR A CA  1 
ATOM   409  C  C   . TYR A 1 58  ? -90.733  5.351  20.736  1.00 65.46  ? 58  TYR A C   1 
ATOM   410  O  O   . TYR A 1 58  ? -91.889  5.087  20.388  1.00 64.33  ? 58  TYR A O   1 
ATOM   411  C  CB  . TYR A 1 58  ? -91.077  7.571  19.606  1.00 62.13  ? 58  TYR A CB  1 
ATOM   412  C  CG  . TYR A 1 58  ? -90.449  8.787  18.958  1.00 66.30  ? 58  TYR A CG  1 
ATOM   413  C  CD1 . TYR A 1 58  ? -89.783  9.738  19.721  1.00 62.75  ? 58  TYR A CD1 1 
ATOM   414  C  CD2 . TYR A 1 58  ? -90.533  8.992  17.583  1.00 66.78  ? 58  TYR A CD2 1 
ATOM   415  C  CE1 . TYR A 1 58  ? -89.210  10.853 19.135  1.00 60.60  ? 58  TYR A CE1 1 
ATOM   416  C  CE2 . TYR A 1 58  ? -89.965  10.108 16.988  1.00 63.88  ? 58  TYR A CE2 1 
ATOM   417  C  CZ  . TYR A 1 58  ? -89.305  11.035 17.770  1.00 67.86  ? 58  TYR A CZ  1 
ATOM   418  O  OH  . TYR A 1 58  ? -88.738  12.148 17.189  1.00 65.28  ? 58  TYR A OH  1 
ATOM   419  N  N   . PRO A 1 59  ? -90.024  4.496  21.482  1.00 65.22  ? 59  PRO A N   1 
ATOM   420  C  CA  . PRO A 1 59  ? -90.612  3.199  21.858  1.00 64.28  ? 59  PRO A CA  1 
ATOM   421  C  C   . PRO A 1 59  ? -91.814  3.330  22.766  1.00 63.62  ? 59  PRO A C   1 
ATOM   422  O  O   . PRO A 1 59  ? -92.646  2.415  22.813  1.00 64.47  ? 59  PRO A O   1 
ATOM   423  C  CB  . PRO A 1 59  ? -89.456  2.483  22.563  1.00 63.33  ? 59  PRO A CB  1 
ATOM   424  C  CG  . PRO A 1 59  ? -88.652  3.585  23.138  1.00 67.04  ? 59  PRO A CG  1 
ATOM   425  C  CD  . PRO A 1 59  ? -88.722  4.710  22.137  1.00 67.98  ? 59  PRO A CD  1 
ATOM   426  N  N   . HIS A 1 60  ? -91.935  4.445  23.478  1.00 67.13  ? 60  HIS A N   1 
ATOM   427  C  CA  . HIS A 1 60  ? -93.044  4.726  24.378  1.00 55.51  ? 60  HIS A CA  1 
ATOM   428  C  C   . HIS A 1 60  ? -94.291  5.231  23.664  1.00 67.90  ? 60  HIS A C   1 
ATOM   429  O  O   . HIS A 1 60  ? -95.288  5.526  24.332  1.00 60.40  ? 60  HIS A O   1 
ATOM   430  C  CB  . HIS A 1 60  ? -92.600  5.761  25.405  1.00 61.76  ? 60  HIS A CB  1 
ATOM   431  C  CG  . HIS A 1 60  ? -92.060  7.015  24.791  1.00 70.22  ? 60  HIS A CG  1 
ATOM   432  N  ND1 . HIS A 1 60  ? -90.845  7.063  24.141  1.00 69.21  ? 60  HIS A ND1 1 
ATOM   433  C  CD2 . HIS A 1 60  ? -92.574  8.266  24.720  1.00 68.79  ? 60  HIS A CD2 1 
ATOM   434  C  CE1 . HIS A 1 60  ? -90.632  8.290  23.701  1.00 67.98  ? 60  HIS A CE1 1 
ATOM   435  N  NE2 . HIS A 1 60  ? -91.664  9.040  24.041  1.00 65.81  ? 60  HIS A NE2 1 
ATOM   436  N  N   . ALA A 1 61  ? -94.263  5.356  22.339  1.00 67.74  ? 61  ALA A N   1 
ATOM   437  C  CA  . ALA A 1 61  ? -95.388  5.888  21.587  1.00 63.86  ? 61  ALA A CA  1 
ATOM   438  C  C   . ALA A 1 61  ? -96.057  4.785  20.779  1.00 62.96  ? 61  ALA A C   1 
ATOM   439  O  O   . ALA A 1 61  ? -95.398  3.871  20.276  1.00 68.12  ? 61  ALA A O   1 
ATOM   440  C  CB  . ALA A 1 61  ? -94.946  7.017  20.651  1.00 64.09  ? 61  ALA A CB  1 
ATOM   441  N  N   . THR A 1 62  ? -97.382  4.878  20.676  1.00 57.29  ? 62  THR A N   1 
ATOM   442  C  CA  . THR A 1 62  ? -98.181  4.001  19.833  1.00 64.67  ? 62  THR A CA  1 
ATOM   443  C  C   . THR A 1 62  ? -99.269  4.835  19.169  1.00 67.48  ? 62  THR A C   1 
ATOM   444  O  O   . THR A 1 62  ? -99.527  5.979  19.553  1.00 66.79  ? 62  THR A O   1 
ATOM   445  C  CB  . THR A 1 62  ? -98.820  2.848  20.628  1.00 69.79  ? 62  THR A CB  1 
ATOM   446  O  OG1 . THR A 1 62  ? -99.703  3.378  21.624  1.00 66.82  ? 62  THR A OG1 1 
ATOM   447  C  CG2 . THR A 1 62  ? -97.765  1.979  21.303  1.00 69.88  ? 62  THR A CG2 1 
ATOM   448  N  N   . GLY A 1 63  ? -99.908  4.249  18.159  1.00 71.77  ? 63  GLY A N   1 
ATOM   449  C  CA  . GLY A 1 63  ? -101.058 4.890  17.542  1.00 68.98  ? 63  GLY A CA  1 
ATOM   450  C  C   . GLY A 1 63  ? -100.708 6.199  16.862  1.00 71.78  ? 63  GLY A C   1 
ATOM   451  O  O   . GLY A 1 63  ? -99.705  6.313  16.145  1.00 66.39  ? 63  GLY A O   1 
ATOM   452  N  N   . ALA A 1 64  ? -101.555 7.208  17.088  1.00 69.99  ? 64  ALA A N   1 
ATOM   453  C  CA  . ALA A 1 64  ? -101.344 8.513  16.469  1.00 64.64  ? 64  ALA A CA  1 
ATOM   454  C  C   . ALA A 1 64  ? -100.050 9.157  16.952  1.00 69.61  ? 64  ALA A C   1 
ATOM   455  O  O   . ALA A 1 64  ? -99.337  9.796  16.168  1.00 68.95  ? 64  ALA A O   1 
ATOM   456  C  CB  . ALA A 1 64  ? -102.535 9.428  16.752  1.00 56.69  ? 64  ALA A CB  1 
ATOM   457  N  N   . ASP A 1 65  ? -99.732  9.001  18.242  1.00 68.63  ? 65  ASP A N   1 
ATOM   458  C  CA  . ASP A 1 65  ? -98.490  9.553  18.777  1.00 67.16  ? 65  ASP A CA  1 
ATOM   459  C  C   . ASP A 1 65  ? -97.281  9.020  18.019  1.00 63.09  ? 65  ASP A C   1 
ATOM   460  O  O   . ASP A 1 65  ? -96.383  9.782  17.645  1.00 64.84  ? 65  ASP A O   1 
ATOM   461  C  CB  . ASP A 1 65  ? -98.369  9.238  20.270  1.00 70.63  ? 65  ASP A CB  1 
ATOM   462  C  CG  . ASP A 1 65  ? -99.303  10.077 21.125  1.00 73.06  ? 65  ASP A CG  1 
ATOM   463  O  OD1 . ASP A 1 65  ? -99.983  10.968 20.576  1.00 76.49  ? 65  ASP A OD1 1 
ATOM   464  O  OD2 . ASP A 1 65  ? -99.357  9.845  22.351  1.00 82.94  ? 65  ASP A OD2 1 
ATOM   465  N  N   . LEU A 1 66  ? -97.242  7.707  17.780  1.00 69.48  ? 66  LEU A N   1 
ATOM   466  C  CA  . LEU A 1 66  ? -96.137  7.137  17.015  1.00 68.62  ? 66  LEU A CA  1 
ATOM   467  C  C   . LEU A 1 66  ? -96.173  7.603  15.565  1.00 63.38  ? 66  LEU A C   1 
ATOM   468  O  O   . LEU A 1 66  ? -95.122  7.859  14.965  1.00 60.47  ? 66  LEU A O   1 
ATOM   469  C  CB  . LEU A 1 66  ? -96.167  5.610  17.094  1.00 62.34  ? 66  LEU A CB  1 
ATOM   470  C  CG  . LEU A 1 66  ? -95.137  4.868  16.232  1.00 69.27  ? 66  LEU A CG  1 
ATOM   471  C  CD1 . LEU A 1 66  ? -93.714  5.314  16.549  1.00 61.24  ? 66  LEU A CD1 1 
ATOM   472  C  CD2 . LEU A 1 66  ? -95.278  3.366  16.404  1.00 64.11  ? 66  LEU A CD2 1 
ATOM   473  N  N   . ASP A 1 67  ? -97.372  7.735  14.989  1.00 62.64  ? 67  ASP A N   1 
ATOM   474  C  CA  . ASP A 1 67  ? -97.481  8.197  13.609  1.00 64.33  ? 67  ASP A CA  1 
ATOM   475  C  C   . ASP A 1 67  ? -96.908  9.596  13.438  1.00 67.53  ? 67  ASP A C   1 
ATOM   476  O  O   . ASP A 1 67  ? -96.372  9.917  12.371  1.00 63.09  ? 67  ASP A O   1 
ATOM   477  C  CB  . ASP A 1 67  ? -98.937  8.164  13.148  1.00 62.05  ? 67  ASP A CB  1 
ATOM   478  C  CG  . ASP A 1 67  ? -99.431  6.758  12.877  1.00 69.02  ? 67  ASP A CG  1 
ATOM   479  O  OD1 . ASP A 1 67  ? -98.591  5.875  12.602  1.00 70.61  ? 67  ASP A OD1 1 
ATOM   480  O  OD2 . ASP A 1 67  ? -100.659 6.538  12.934  1.00 74.20  ? 67  ASP A OD2 1 
ATOM   481  N  N   . LEU A 1 68  ? -97.007  10.441 14.469  1.00 63.95  ? 68  LEU A N   1 
ATOM   482  C  CA  . LEU A 1 68  ? -96.393  11.762 14.388  1.00 58.97  ? 68  LEU A CA  1 
ATOM   483  C  C   . LEU A 1 68  ? -94.874  11.654 14.348  1.00 59.51  ? 68  LEU A C   1 
ATOM   484  O  O   . LEU A 1 68  ? -94.209  12.428 13.649  1.00 67.33  ? 68  LEU A O   1 
ATOM   485  C  CB  . LEU A 1 68  ? -96.843  12.634 15.560  1.00 62.53  ? 68  LEU A CB  1 
ATOM   486  C  CG  . LEU A 1 68  ? -96.289  14.062 15.570  1.00 62.60  ? 68  LEU A CG  1 
ATOM   487  C  CD1 . LEU A 1 68  ? -96.631  14.775 14.273  1.00 65.86  ? 68  LEU A CD1 1 
ATOM   488  C  CD2 . LEU A 1 68  ? -96.812  14.845 16.765  1.00 65.56  ? 68  LEU A CD2 1 
ATOM   489  N  N   . GLY A 1 69  ? -94.308  10.696 15.083  1.00 62.78  ? 69  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 69  ? -92.875  10.470 15.001  1.00 58.33  ? 69  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 69  ? -92.460  9.899  13.660  1.00 63.60  ? 69  GLY A C   1 
ATOM   492  O  O   . GLY A 1 69  ? -91.408  10.256 13.122  1.00 56.81  ? 69  GLY A O   1 
ATOM   493  N  N   . VAL A 1 70  ? -93.281  9.004  13.104  1.00 61.33  ? 70  VAL A N   1 
ATOM   494  C  CA  . VAL A 1 70  ? -93.007  8.454  11.778  1.00 68.12  ? 70  VAL A CA  1 
ATOM   495  C  C   . VAL A 1 70  ? -92.970  9.572  10.744  1.00 65.66  ? 70  VAL A C   1 
ATOM   496  O  O   . VAL A 1 70  ? -92.038  9.665  9.935   1.00 65.46  ? 70  VAL A O   1 
ATOM   497  C  CB  . VAL A 1 70  ? -94.053  7.383  11.413  1.00 71.12  ? 70  VAL A CB  1 
ATOM   498  C  CG1 . VAL A 1 70  ? -93.801  6.845  10.008  1.00 58.85  ? 70  VAL A CG1 1 
ATOM   499  C  CG2 . VAL A 1 70  ? -94.043  6.255  12.431  1.00 66.52  ? 70  VAL A CG2 1 
ATOM   500  N  N   . ASP A 1 71  ? -93.982  10.445 10.764  1.00 63.86  ? 71  ASP A N   1 
ATOM   501  C  CA  . ASP A 1 71  ? -94.053  11.529 9.791   1.00 58.27  ? 71  ASP A CA  1 
ATOM   502  C  C   . ASP A 1 71  ? -92.903  12.513 9.962   1.00 61.90  ? 71  ASP A C   1 
ATOM   503  O  O   . ASP A 1 71  ? -92.415  13.070 8.972   1.00 67.77  ? 71  ASP A O   1 
ATOM   504  C  CB  . ASP A 1 71  ? -95.398  12.247 9.905   1.00 55.41  ? 71  ASP A CB  1 
ATOM   505  C  CG  . ASP A 1 71  ? -96.576  11.318 9.673   1.00 61.07  ? 71  ASP A CG  1 
ATOM   506  O  OD1 . ASP A 1 71  ? -96.351  10.180 9.209   1.00 67.97  ? 71  ASP A OD1 1 
ATOM   507  O  OD2 . ASP A 1 71  ? -97.726  11.715 9.963   1.00 56.28  ? 71  ASP A OD2 1 
ATOM   508  N  N   . LEU A 1 72  ? -92.449  12.734 11.198  1.00 60.31  ? 72  LEU A N   1 
ATOM   509  C  CA  . LEU A 1 72  ? -91.308  13.619 11.407  1.00 61.93  ? 72  LEU A CA  1 
ATOM   510  C  C   . LEU A 1 72  ? -90.063  13.078 10.718  1.00 60.21  ? 72  LEU A C   1 
ATOM   511  O  O   . LEU A 1 72  ? -89.328  13.831 10.071  1.00 66.15  ? 72  LEU A O   1 
ATOM   512  C  CB  . LEU A 1 72  ? -91.049  13.820 12.901  1.00 64.05  ? 72  LEU A CB  1 
ATOM   513  C  CG  . LEU A 1 72  ? -89.778  14.615 13.225  1.00 59.38  ? 72  LEU A CG  1 
ATOM   514  C  CD1 . LEU A 1 72  ? -89.830  16.000 12.604  1.00 61.76  ? 72  LEU A CD1 1 
ATOM   515  C  CD2 . LEU A 1 72  ? -89.547  14.717 14.719  1.00 60.13  ? 72  LEU A CD2 1 
ATOM   516  N  N   . MET A 1 73  ? -89.812  11.775 10.838  1.00 62.20  ? 73  MET A N   1 
ATOM   517  C  CA  . MET A 1 73  ? -88.649  11.189 10.180  1.00 57.82  ? 73  MET A CA  1 
ATOM   518  C  C   . MET A 1 73  ? -88.823  11.185 8.667   1.00 67.13  ? 73  MET A C   1 
ATOM   519  O  O   . MET A 1 73  ? -87.863  11.425 7.924   1.00 61.92  ? 73  MET A O   1 
ATOM   520  C  CB  . MET A 1 73  ? -88.412  9.773  10.703  1.00 63.16  ? 73  MET A CB  1 
ATOM   521  C  CG  . MET A 1 73  ? -88.447  9.654  12.224  1.00 69.64  ? 73  MET A CG  1 
ATOM   522  S  SD  . MET A 1 73  ? -87.293  10.770 13.046  1.00 76.92  ? 73  MET A SD  1 
ATOM   523  C  CE  . MET A 1 73  ? -85.767  10.197 12.337  1.00 65.43  ? 73  MET A CE  1 
ATOM   524  N  N   . SER A 1 74  ? -90.041  10.915 8.193   1.00 65.68  ? 74  SER A N   1 
ATOM   525  C  CA  . SER A 1 74  ? -90.320  10.998 6.764   1.00 63.07  ? 74  SER A CA  1 
ATOM   526  C  C   . SER A 1 74  ? -90.016  12.393 6.236   1.00 65.44  ? 74  SER A C   1 
ATOM   527  O  O   . SER A 1 74  ? -89.206  12.559 5.317   1.00 65.58  ? 74  SER A O   1 
ATOM   528  C  CB  . SER A 1 74  ? -91.777  10.625 6.485   1.00 61.59  ? 74  SER A CB  1 
ATOM   529  O  OG  . SER A 1 74  ? -92.006  9.246  6.701   1.00 57.73  ? 74  SER A OG  1 
ATOM   530  N  N   . TRP A 1 75  ? -90.657  13.413 6.818   1.00 65.00  ? 75  TRP A N   1 
ATOM   531  C  CA  . TRP A 1 75  ? -90.432  14.784 6.367   1.00 63.21  ? 75  TRP A CA  1 
ATOM   532  C  C   . TRP A 1 75  ? -88.967  15.175 6.495   1.00 63.52  ? 75  TRP A C   1 
ATOM   533  O  O   . TRP A 1 75  ? -88.406  15.815 5.598   1.00 58.00  ? 75  TRP A O   1 
ATOM   534  C  CB  . TRP A 1 75  ? -91.302  15.765 7.157   1.00 61.18  ? 75  TRP A CB  1 
ATOM   535  C  CG  . TRP A 1 75  ? -91.031  17.194 6.773   1.00 64.35  ? 75  TRP A CG  1 
ATOM   536  C  CD1 . TRP A 1 75  ? -91.671  17.915 5.809   1.00 64.36  ? 75  TRP A CD1 1 
ATOM   537  C  CD2 . TRP A 1 75  ? -90.024  18.062 7.320   1.00 66.12  ? 75  TRP A CD2 1 
ATOM   538  N  NE1 . TRP A 1 75  ? -91.135  19.177 5.727   1.00 65.48  ? 75  TRP A NE1 1 
ATOM   539  C  CE2 . TRP A 1 75  ? -90.121  19.293 6.641   1.00 63.57  ? 75  TRP A CE2 1 
ATOM   540  C  CE3 . TRP A 1 75  ? -89.055  17.918 8.321   1.00 62.51  ? 75  TRP A CE3 1 
ATOM   541  C  CZ2 . TRP A 1 75  ? -89.288  20.373 6.929   1.00 64.28  ? 75  TRP A CZ2 1 
ATOM   542  C  CZ3 . TRP A 1 75  ? -88.225  18.992 8.603   1.00 61.83  ? 75  TRP A CZ3 1 
ATOM   543  C  CH2 . TRP A 1 75  ? -88.348  20.205 7.911   1.00 67.15  ? 75  TRP A CH2 1 
ATOM   544  N  N   . ALA A 1 76  ? -88.332  14.798 7.605   1.00 62.00  ? 76  ALA A N   1 
ATOM   545  C  CA  . ALA A 1 76  ? -86.971  15.249 7.870   1.00 68.56  ? 76  ALA A CA  1 
ATOM   546  C  C   . ALA A 1 76  ? -86.000  14.757 6.804   1.00 64.63  ? 76  ALA A C   1 
ATOM   547  O  O   . ALA A 1 76  ? -85.116  15.503 6.367   1.00 60.16  ? 76  ALA A O   1 
ATOM   548  C  CB  . ALA A 1 76  ? -86.535  14.787 9.257   1.00 62.93  ? 76  ALA A CB  1 
ATOM   549  N  N   . PHE A 1 77  ? -86.151  13.508 6.366   1.00 64.40  ? 77  PHE A N   1 
ATOM   550  C  CA  . PHE A 1 77  ? -85.231  12.974 5.369   1.00 68.10  ? 77  PHE A CA  1 
ATOM   551  C  C   . PHE A 1 77  ? -85.614  13.395 3.957   1.00 69.38  ? 77  PHE A C   1 
ATOM   552  O  O   . PHE A 1 77  ? -84.729  13.597 3.118   1.00 65.75  ? 77  PHE A O   1 
ATOM   553  C  CB  . PHE A 1 77  ? -85.155  11.452 5.489   1.00 65.83  ? 77  PHE A CB  1 
ATOM   554  C  CG  . PHE A 1 77  ? -84.295  10.988 6.628   1.00 70.19  ? 77  PHE A CG  1 
ATOM   555  C  CD1 . PHE A 1 77  ? -82.926  10.856 6.466   1.00 76.11  ? 77  PHE A CD1 1 
ATOM   556  C  CD2 . PHE A 1 77  ? -84.849  10.709 7.866   1.00 71.67  ? 77  PHE A CD2 1 
ATOM   557  C  CE1 . PHE A 1 77  ? -82.126  10.441 7.513   1.00 81.06  ? 77  PHE A CE1 1 
ATOM   558  C  CE2 . PHE A 1 77  ? -84.056  10.294 8.917   1.00 67.29  ? 77  PHE A CE2 1 
ATOM   559  C  CZ  . PHE A 1 77  ? -82.692  10.159 8.740   1.00 76.38  ? 77  PHE A CZ  1 
ATOM   560  N  N   . LEU A 1 78  ? -86.912  13.539 3.679   1.00 66.88  ? 78  LEU A N   1 
ATOM   561  C  CA  . LEU A 1 78  ? -87.331  14.173 2.433   1.00 61.75  ? 78  LEU A CA  1 
ATOM   562  C  C   . LEU A 1 78  ? -86.787  15.593 2.337   1.00 66.37  ? 78  LEU A C   1 
ATOM   563  O  O   . LEU A 1 78  ? -86.311  16.015 1.276   1.00 72.34  ? 78  LEU A O   1 
ATOM   564  C  CB  . LEU A 1 78  ? -88.856  14.174 2.334   1.00 53.93  ? 78  LEU A CB  1 
ATOM   565  C  CG  . LEU A 1 78  ? -89.484  12.809 2.053   1.00 65.31  ? 78  LEU A CG  1 
ATOM   566  C  CD1 . LEU A 1 78  ? -91.000  12.877 2.148   1.00 62.14  ? 78  LEU A CD1 1 
ATOM   567  C  CD2 . LEU A 1 78  ? -89.047  12.298 0.683   1.00 64.88  ? 78  LEU A CD2 1 
ATOM   568  N  N   . PHE A 1 79  ? -86.840  16.337 3.444   1.00 69.33  ? 79  PHE A N   1 
ATOM   569  C  CA  . PHE A 1 79  ? -86.316  17.699 3.470   1.00 70.33  ? 79  PHE A CA  1 
ATOM   570  C  C   . PHE A 1 79  ? -84.813  17.716 3.211   1.00 64.59  ? 79  PHE A C   1 
ATOM   571  O  O   . PHE A 1 79  ? -84.320  18.500 2.390   1.00 62.79  ? 79  PHE A O   1 
ATOM   572  C  CB  . PHE A 1 79  ? -86.648  18.346 4.820   1.00 67.75  ? 79  PHE A CB  1 
ATOM   573  C  CG  . PHE A 1 79  ? -86.092  19.729 4.992   1.00 67.06  ? 79  PHE A CG  1 
ATOM   574  C  CD1 . PHE A 1 79  ? -86.728  20.823 4.421   1.00 68.52  ? 79  PHE A CD1 1 
ATOM   575  C  CD2 . PHE A 1 79  ? -84.940  19.938 5.735   1.00 65.10  ? 79  PHE A CD2 1 
ATOM   576  C  CE1 . PHE A 1 79  ? -86.219  22.100 4.579   1.00 63.52  ? 79  PHE A CE1 1 
ATOM   577  C  CE2 . PHE A 1 79  ? -84.424  21.211 5.898   1.00 68.65  ? 79  PHE A CE2 1 
ATOM   578  C  CZ  . PHE A 1 79  ? -85.065  22.295 5.319   1.00 70.45  ? 79  PHE A CZ  1 
ATOM   579  N  N   . ASP A 1 80  ? -84.067  16.847 3.899   1.00 63.02  ? 80  ASP A N   1 
ATOM   580  C  CA  . ASP A 1 80  ? -82.614  16.847 3.767   1.00 68.07  ? 80  ASP A CA  1 
ATOM   581  C  C   . ASP A 1 80  ? -82.173  16.469 2.357   1.00 68.88  ? 80  ASP A C   1 
ATOM   582  O  O   . ASP A 1 80  ? -81.100  16.894 1.911   1.00 70.91  ? 80  ASP A O   1 
ATOM   583  C  CB  . ASP A 1 80  ? -81.997  15.900 4.799   1.00 65.19  ? 80  ASP A CB  1 
ATOM   584  C  CG  . ASP A 1 80  ? -80.480  15.913 4.774   1.00 75.28  ? 80  ASP A CG  1 
ATOM   585  O  OD1 . ASP A 1 80  ? -79.885  16.946 5.145   1.00 80.39  ? 80  ASP A OD1 1 
ATOM   586  O  OD2 . ASP A 1 80  ? -79.879  14.891 4.381   1.00 84.16  ? 80  ASP A OD2 1 
ATOM   587  N  N   . ASP A 1 81  ? -82.986  15.687 1.638   1.00 68.08  ? 81  ASP A N   1 
ATOM   588  C  CA  . ASP A 1 81  ? -82.617  15.280 0.283   1.00 80.00  ? 81  ASP A CA  1 
ATOM   589  C  C   . ASP A 1 81  ? -82.619  16.457 -0.688  1.00 76.17  ? 81  ASP A C   1 
ATOM   590  O  O   . ASP A 1 81  ? -81.829  16.469 -1.638  1.00 77.14  ? 81  ASP A O   1 
ATOM   591  C  CB  . ASP A 1 81  ? -83.559  14.184 -0.224  1.00 80.27  ? 81  ASP A CB  1 
ATOM   592  C  CG  . ASP A 1 81  ? -83.306  12.831 0.432   1.00 88.85  ? 81  ASP A CG  1 
ATOM   593  O  OD1 . ASP A 1 81  ? -82.192  12.616 0.958   1.00 81.82  ? 81  ASP A OD1 1 
ATOM   594  O  OD2 . ASP A 1 81  ? -84.224  11.981 0.411   1.00 88.28  ? 81  ASP A OD2 1 
ATOM   595  N  N   . LEU A 1 82  ? -83.491  17.458 -0.468  1.00 70.43  ? 82  LEU A N   1 
ATOM   596  C  CA  . LEU A 1 82  ? -83.575  18.664 -1.295  1.00 65.71  ? 82  LEU A CA  1 
ATOM   597  C  C   . LEU A 1 82  ? -82.304  19.511 -1.259  1.00 68.72  ? 82  LEU A C   1 
ATOM   598  O  O   . LEU A 1 82  ? -82.319  20.599 -1.840  1.00 78.62  ? 82  LEU A O   1 
ATOM   599  C  CB  . LEU A 1 82  ? -84.760  19.532 -0.864  1.00 61.75  ? 82  LEU A CB  1 
ATOM   600  C  CG  . LEU A 1 82  ? -86.121  18.860 -0.741  1.00 64.40  ? 82  LEU A CG  1 
ATOM   601  C  CD1 . LEU A 1 82  ? -87.187  19.885 -0.391  1.00 63.85  ? 82  LEU A CD1 1 
ATOM   602  C  CD2 . LEU A 1 82  ? -86.469  18.141 -2.024  1.00 72.91  ? 82  LEU A CD2 1 
ATOM   603  N  N   . PHE A 1 83  ? -81.222  19.079 -0.611  1.00 63.16  ? 83  PHE A N   1 
ATOM   604  C  CA  . PHE A 1 83  ? -80.009  19.874 -0.510  1.00 66.53  ? 83  PHE A CA  1 
ATOM   605  C  C   . PHE A 1 83  ? -78.764  19.104 -0.924  1.00 70.18  ? 83  PHE A C   1 
ATOM   606  O  O   . PHE A 1 83  ? -77.660  19.654 -0.843  1.00 72.65  ? 83  PHE A O   1 
ATOM   607  C  CB  . PHE A 1 83  ? -79.832  20.405 0.927   1.00 66.11  ? 83  PHE A CB  1 
ATOM   608  C  CG  . PHE A 1 83  ? -80.940  21.320 1.378   1.00 67.52  ? 83  PHE A CG  1 
ATOM   609  C  CD1 . PHE A 1 83  ? -82.103  20.806 1.931   1.00 69.36  ? 83  PHE A CD1 1 
ATOM   610  C  CD2 . PHE A 1 83  ? -80.819  22.692 1.245   1.00 69.79  ? 83  PHE A CD2 1 
ATOM   611  C  CE1 . PHE A 1 83  ? -83.127  21.647 2.342   1.00 65.59  ? 83  PHE A CE1 1 
ATOM   612  C  CE2 . PHE A 1 83  ? -81.838  23.537 1.654   1.00 68.78  ? 83  PHE A CE2 1 
ATOM   613  C  CZ  . PHE A 1 83  ? -82.993  23.013 2.203   1.00 65.95  ? 83  PHE A CZ  1 
ATOM   614  N  N   . ASP A 1 84  ? -78.905  17.847 -1.351  1.00 71.04  ? 84  ASP A N   1 
ATOM   615  C  CA  . ASP A 1 84  ? -77.763  17.099 -1.861  1.00 81.23  ? 84  ASP A CA  1 
ATOM   616  C  C   . ASP A 1 84  ? -77.320  17.591 -3.235  1.00 89.11  ? 84  ASP A C   1 
ATOM   617  O  O   . ASP A 1 84  ? -76.195  17.293 -3.653  1.00 87.59  ? 84  ASP A O   1 
ATOM   618  C  CB  . ASP A 1 84  ? -78.096  15.607 -1.927  1.00 72.61  ? 84  ASP A CB  1 
ATOM   619  C  CG  . ASP A 1 84  ? -78.401  15.015 -0.567  1.00 93.14  ? 84  ASP A CG  1 
ATOM   620  O  OD1 . ASP A 1 84  ? -77.709  15.369 0.414   1.00 94.60  ? 84  ASP A OD1 1 
ATOM   621  O  OD2 . ASP A 1 84  ? -79.338  14.193 -0.480  1.00 99.12  ? 84  ASP A OD2 1 
ATOM   622  N  N   . GLY A 1 85  ? -78.170  18.339 -3.937  1.00 80.06  ? 85  GLY A N   1 
ATOM   623  C  CA  . GLY A 1 85  ? -77.850  18.834 -5.253  1.00 90.22  ? 85  GLY A CA  1 
ATOM   624  C  C   . GLY A 1 85  ? -77.360  20.269 -5.253  1.00 93.16  ? 85  GLY A C   1 
ATOM   625  O  O   . GLY A 1 85  ? -76.779  20.756 -4.277  1.00 87.23  ? 85  GLY A O   1 
ATOM   626  N  N   . PRO A 1 86  ? -77.589  20.975 -6.365  1.00 91.19  ? 86  PRO A N   1 
ATOM   627  C  CA  . PRO A 1 86  ? -77.066  22.347 -6.486  1.00 87.73  ? 86  PRO A CA  1 
ATOM   628  C  C   . PRO A 1 86  ? -77.631  23.321 -5.464  1.00 87.72  ? 86  PRO A C   1 
ATOM   629  O  O   . PRO A 1 86  ? -76.976  24.328 -5.168  1.00 86.45  ? 86  PRO A O   1 
ATOM   630  C  CB  . PRO A 1 86  ? -77.459  22.742 -7.917  1.00 85.11  ? 86  PRO A CB  1 
ATOM   631  C  CG  . PRO A 1 86  ? -77.635  21.444 -8.638  1.00 83.00  ? 86  PRO A CG  1 
ATOM   632  C  CD  . PRO A 1 86  ? -78.195  20.500 -7.619  1.00 82.23  ? 86  PRO A CD  1 
ATOM   633  N  N   . ARG A 1 87  ? -78.825  23.063 -4.918  1.00 85.17  ? 87  ARG A N   1 
ATOM   634  C  CA  . ARG A 1 87  ? -79.395  23.987 -3.941  1.00 81.76  ? 87  ARG A CA  1 
ATOM   635  C  C   . ARG A 1 87  ? -78.548  24.052 -2.676  1.00 81.13  ? 87  ARG A C   1 
ATOM   636  O  O   . ARG A 1 87  ? -78.296  25.140 -2.144  1.00 82.00  ? 87  ARG A O   1 
ATOM   637  C  CB  . ARG A 1 87  ? -80.836  23.597 -3.607  1.00 75.79  ? 87  ARG A CB  1 
ATOM   638  C  CG  . ARG A 1 87  ? -81.458  24.484 -2.539  1.00 78.06  ? 87  ARG A CG  1 
ATOM   639  C  CD  . ARG A 1 87  ? -82.825  23.998 -2.086  1.00 80.72  ? 87  ARG A CD  1 
ATOM   640  N  NE  . ARG A 1 87  ? -83.874  24.283 -3.059  1.00 78.28  ? 87  ARG A NE  1 
ATOM   641  C  CZ  . ARG A 1 87  ? -84.337  23.406 -3.938  1.00 81.65  ? 87  ARG A CZ  1 
ATOM   642  N  NH1 . ARG A 1 87  ? -83.851  22.177 -4.008  1.00 77.66  ? 87  ARG A NH1 1 
ATOM   643  N  NH2 . ARG A 1 87  ? -85.314  23.769 -4.764  1.00 93.79  ? 87  ARG A NH2 1 
ATOM   644  N  N   . GLY A 1 88  ? -78.085  22.903 -2.189  1.00 84.24  ? 88  GLY A N   1 
ATOM   645  C  CA  . GLY A 1 88  ? -77.143  22.880 -1.089  1.00 82.13  ? 88  GLY A CA  1 
ATOM   646  C  C   . GLY A 1 88  ? -75.808  23.538 -1.366  1.00 87.67  ? 88  GLY A C   1 
ATOM   647  O  O   . GLY A 1 88  ? -74.978  23.614 -0.456  1.00 85.23  ? 88  GLY A O   1 
ATOM   648  N  N   . GLU A 1 89  ? -75.579  24.009 -2.592  1.00 92.09  ? 89  GLU A N   1 
ATOM   649  C  CA  . GLU A 1 89  ? -74.359  24.707 -2.967  1.00 95.29  ? 89  GLU A CA  1 
ATOM   650  C  C   . GLU A 1 89  ? -74.524  26.217 -2.988  1.00 95.65  ? 89  GLU A C   1 
ATOM   651  O  O   . GLU A 1 89  ? -73.516  26.931 -2.936  1.00 100.33 ? 89  GLU A O   1 
ATOM   652  C  CB  . GLU A 1 89  ? -73.881  24.244 -4.356  1.00 94.22  ? 89  GLU A CB  1 
ATOM   653  C  CG  . GLU A 1 89  ? -72.364  24.229 -4.552  1.00 101.43 ? 89  GLU A CG  1 
ATOM   654  C  CD  . GLU A 1 89  ? -71.695  23.054 -3.866  1.00 106.47 ? 89  GLU A CD  1 
ATOM   655  O  OE1 . GLU A 1 89  ? -72.402  22.071 -3.555  1.00 106.66 ? 89  GLU A OE1 1 
ATOM   656  O  OE2 . GLU A 1 89  ? -70.468  23.118 -3.629  1.00 106.11 ? 89  GLU A OE2 1 
ATOM   657  N  N   . ASN A 1 90  ? -75.758  26.714 -3.078  1.00 93.86  ? 90  ASN A N   1 
ATOM   658  C  CA  . ASN A 1 90  ? -76.030  28.145 -3.132  1.00 96.35  ? 90  ASN A CA  1 
ATOM   659  C  C   . ASN A 1 90  ? -76.744  28.583 -1.861  1.00 89.97  ? 90  ASN A C   1 
ATOM   660  O  O   . ASN A 1 90  ? -77.915  28.223 -1.660  1.00 84.27  ? 90  ASN A O   1 
ATOM   661  C  CB  . ASN A 1 90  ? -76.873  28.486 -4.363  1.00 97.68  ? 90  ASN A CB  1 
ATOM   662  C  CG  . ASN A 1 90  ? -77.118  29.971 -4.506  1.00 102.42 ? 90  ASN A CG  1 
ATOM   663  O  OD1 . ASN A 1 90  ? -78.240  30.445 -4.327  1.00 101.39 ? 90  ASN A OD1 1 
ATOM   664  N  ND2 . ASN A 1 90  ? -76.063  30.717 -4.815  1.00 100.43 ? 90  ASN A ND2 1 
ATOM   665  N  N   . PRO A 1 91  ? -76.093  29.351 -0.985  1.00 89.77  ? 91  PRO A N   1 
ATOM   666  C  CA  . PRO A 1 91  ? -76.754  29.762 0.263   1.00 84.82  ? 91  PRO A CA  1 
ATOM   667  C  C   . PRO A 1 91  ? -77.958  30.660 0.049   1.00 84.27  ? 91  PRO A C   1 
ATOM   668  O  O   . PRO A 1 91  ? -78.853  30.687 0.903   1.00 84.76  ? 91  PRO A O   1 
ATOM   669  C  CB  . PRO A 1 91  ? -75.634  30.486 1.024   1.00 86.05  ? 91  PRO A CB  1 
ATOM   670  C  CG  . PRO A 1 91  ? -74.682  30.930 -0.035  1.00 85.68  ? 91  PRO A CG  1 
ATOM   671  C  CD  . PRO A 1 91  ? -74.720  29.867 -1.086  1.00 92.35  ? 91  PRO A CD  1 
ATOM   672  N  N   . GLU A 1 92  ? -78.009  31.400 -1.062  1.00 87.77  ? 92  GLU A N   1 
ATOM   673  C  CA  . GLU A 1 92  ? -79.176  32.233 -1.334  1.00 83.31  ? 92  GLU A CA  1 
ATOM   674  C  C   . GLU A 1 92  ? -80.404  31.378 -1.620  1.00 83.63  ? 92  GLU A C   1 
ATOM   675  O  O   . GLU A 1 92  ? -81.512  31.707 -1.179  1.00 76.93  ? 92  GLU A O   1 
ATOM   676  C  CB  . GLU A 1 92  ? -78.888  33.174 -2.504  1.00 83.91  ? 92  GLU A CB  1 
ATOM   677  N  N   . ASP A 1 93  ? -80.226  30.274 -2.350  1.00 89.04  ? 93  ASP A N   1 
ATOM   678  C  CA  . ASP A 1 93  ? -81.342  29.387 -2.659  1.00 86.65  ? 93  ASP A CA  1 
ATOM   679  C  C   . ASP A 1 93  ? -81.687  28.466 -1.495  1.00 82.76  ? 93  ASP A C   1 
ATOM   680  O  O   . ASP A 1 93  ? -82.859  28.110 -1.324  1.00 79.03  ? 93  ASP A O   1 
ATOM   681  C  CB  . ASP A 1 93  ? -81.029  28.563 -3.910  1.00 92.65  ? 93  ASP A CB  1 
ATOM   682  C  CG  . ASP A 1 93  ? -81.268  29.339 -5.192  1.00 104.59 ? 93  ASP A CG  1 
ATOM   683  O  OD1 . ASP A 1 93  ? -82.284  30.066 -5.267  1.00 95.16  ? 93  ASP A OD1 1 
ATOM   684  O  OD2 . ASP A 1 93  ? -80.439  29.224 -6.122  1.00 108.75 ? 93  ASP A OD2 1 
ATOM   685  N  N   . THR A 1 94  ? -80.693  28.066 -0.696  1.00 80.32  ? 94  THR A N   1 
ATOM   686  C  CA  . THR A 1 94  ? -80.981  27.337 0.537   1.00 76.13  ? 94  THR A CA  1 
ATOM   687  C  C   . THR A 1 94  ? -81.824  28.183 1.481   1.00 73.36  ? 94  THR A C   1 
ATOM   688  O  O   . THR A 1 94  ? -82.870  27.738 1.969   1.00 72.01  ? 94  THR A O   1 
ATOM   689  C  CB  . THR A 1 94  ? -79.679  26.916 1.220   1.00 74.83  ? 94  THR A CB  1 
ATOM   690  O  OG1 . THR A 1 94  ? -79.051  25.877 0.461   1.00 80.88  ? 94  THR A OG1 1 
ATOM   691  C  CG2 . THR A 1 94  ? -79.955  26.414 2.626   1.00 76.18  ? 94  THR A CG2 1 
ATOM   692  N  N   . LYS A 1 95  ? -81.380  29.416 1.743   1.00 72.97  ? 95  LYS A N   1 
ATOM   693  C  CA  . LYS A 1 95  ? -82.131  30.324 2.603   1.00 71.19  ? 95  LYS A CA  1 
ATOM   694  C  C   . LYS A 1 95  ? -83.536  30.560 2.067   1.00 72.09  ? 95  LYS A C   1 
ATOM   695  O  O   . LYS A 1 95  ? -84.501  30.614 2.839   1.00 72.92  ? 95  LYS A O   1 
ATOM   696  C  CB  . LYS A 1 95  ? -81.375  31.647 2.734   1.00 74.01  ? 95  LYS A CB  1 
ATOM   697  C  CG  . LYS A 1 95  ? -82.089  32.719 3.540   1.00 77.28  ? 95  LYS A CG  1 
ATOM   698  C  CD  . LYS A 1 95  ? -81.978  32.470 5.035   1.00 85.29  ? 95  LYS A CD  1 
ATOM   699  C  CE  . LYS A 1 95  ? -82.400  33.701 5.829   1.00 83.26  ? 95  LYS A CE  1 
ATOM   700  N  NZ  . LYS A 1 95  ? -82.294  33.485 7.300   1.00 94.99  ? 95  LYS A NZ  1 
ATOM   701  N  N   . GLN A 1 96  ? -83.670  30.695 0.745   1.00 72.73  ? 96  GLN A N   1 
ATOM   702  C  CA  . GLN A 1 96  ? -84.980  30.918 0.142   1.00 68.52  ? 96  GLN A CA  1 
ATOM   703  C  C   . GLN A 1 96  ? -85.958  29.812 0.514   1.00 68.90  ? 96  GLN A C   1 
ATOM   704  O  O   . GLN A 1 96  ? -87.141  30.075 0.758   1.00 77.37  ? 96  GLN A O   1 
ATOM   705  C  CB  . GLN A 1 96  ? -84.843  31.027 -1.378  1.00 75.80  ? 96  GLN A CB  1 
ATOM   706  C  CG  . GLN A 1 96  ? -86.165  31.065 -2.130  1.00 70.05  ? 96  GLN A CG  1 
ATOM   707  N  N   . LEU A 1 97  ? -85.481  28.567 0.577   1.00 69.63  ? 97  LEU A N   1 
ATOM   708  C  CA  . LEU A 1 97  ? -86.378  27.463 0.897   1.00 68.79  ? 97  LEU A CA  1 
ATOM   709  C  C   . LEU A 1 97  ? -86.577  27.313 2.401   1.00 67.33  ? 97  LEU A C   1 
ATOM   710  O  O   . LEU A 1 97  ? -87.708  27.105 2.854   1.00 72.02  ? 97  LEU A O   1 
ATOM   711  C  CB  . LEU A 1 97  ? -85.856  26.157 0.294   1.00 68.91  ? 97  LEU A CB  1 
ATOM   712  C  CG  . LEU A 1 97  ? -86.728  24.922 0.547   1.00 71.12  ? 97  LEU A CG  1 
ATOM   713  C  CD1 . LEU A 1 97  ? -88.186  25.197 0.200   1.00 60.93  ? 97  LEU A CD1 1 
ATOM   714  C  CD2 . LEU A 1 97  ? -86.209  23.729 -0.237  1.00 72.90  ? 97  LEU A CD2 1 
ATOM   715  N  N   . THR A 1 98  ? -85.500  27.414 3.190   1.00 65.19  ? 98  THR A N   1 
ATOM   716  C  CA  . THR A 1 98  ? -85.641  27.264 4.638   1.00 68.38  ? 98  THR A CA  1 
ATOM   717  C  C   . THR A 1 98  ? -86.579  28.313 5.221   1.00 67.68  ? 98  THR A C   1 
ATOM   718  O  O   . THR A 1 98  ? -87.320  28.022 6.167   1.00 67.87  ? 98  THR A O   1 
ATOM   719  C  CB  . THR A 1 98  ? -84.278  27.339 5.331   1.00 62.44  ? 98  THR A CB  1 
ATOM   720  O  OG1 . THR A 1 98  ? -83.687  28.622 5.101   1.00 73.68  ? 98  THR A OG1 1 
ATOM   721  C  CG2 . THR A 1 98  ? -83.350  26.254 4.812   1.00 64.31  ? 98  THR A CG2 1 
ATOM   722  N  N   . ASP A 1 99  ? -86.581  29.528 4.661   1.00 71.61  ? 99  ASP A N   1 
ATOM   723  C  CA  . ASP A 1 99  ? -87.470  30.572 5.163   1.00 70.35  ? 99  ASP A CA  1 
ATOM   724  C  C   . ASP A 1 99  ? -88.934  30.260 4.880   1.00 66.35  ? 99  ASP A C   1 
ATOM   725  O  O   . ASP A 1 99  ? -89.811  30.686 5.639   1.00 70.91  ? 99  ASP A O   1 
ATOM   726  C  CB  . ASP A 1 99  ? -87.099  31.926 4.560   1.00 65.06  ? 99  ASP A CB  1 
ATOM   727  C  CG  . ASP A 1 99  ? -85.727  32.404 4.992   1.00 82.98  ? 99  ASP A CG  1 
ATOM   728  O  OD1 . ASP A 1 99  ? -85.209  31.901 6.014   1.00 81.51  ? 99  ASP A OD1 1 
ATOM   729  O  OD2 . ASP A 1 99  ? -85.169  33.288 4.308   1.00 86.41  ? 99  ASP A OD2 1 
ATOM   730  N  N   . GLN A 1 100 ? -89.222  29.534 3.799   1.00 71.24  ? 100 GLN A N   1 
ATOM   731  C  CA  . GLN A 1 100 ? -90.604  29.165 3.513   1.00 71.28  ? 100 GLN A CA  1 
ATOM   732  C  C   . GLN A 1 100 ? -91.077  28.024 4.400   1.00 69.97  ? 100 GLN A C   1 
ATOM   733  O  O   . GLN A 1 100 ? -92.274  27.930 4.699   1.00 65.31  ? 100 GLN A O   1 
ATOM   734  C  CB  . GLN A 1 100 ? -90.756  28.781 2.042   1.00 73.88  ? 100 GLN A CB  1 
ATOM   735  C  CG  . GLN A 1 100 ? -90.335  29.873 1.081   1.00 73.71  ? 100 GLN A CG  1 
ATOM   736  C  CD  . GLN A 1 100 ? -90.628  29.513 -0.355  1.00 82.58  ? 100 GLN A CD  1 
ATOM   737  O  OE1 . GLN A 1 100 ? -91.785  29.481 -0.770  1.00 93.86  ? 100 GLN A OE1 1 
ATOM   738  N  NE2 . GLN A 1 100 ? -89.581  29.229 -1.123  1.00 83.95  ? 100 GLN A NE2 1 
ATOM   739  N  N   . VAL A 1 101 ? -90.160  27.151 4.819   1.00 69.20  ? 101 VAL A N   1 
ATOM   740  C  CA  . VAL A 1 101 ? -90.508  26.108 5.775   1.00 66.90  ? 101 VAL A CA  1 
ATOM   741  C  C   . VAL A 1 101 ? -90.643  26.702 7.171   1.00 66.37  ? 101 VAL A C   1 
ATOM   742  O  O   . VAL A 1 101 ? -91.672  26.538 7.839   1.00 62.82  ? 101 VAL A O   1 
ATOM   743  C  CB  . VAL A 1 101 ? -89.462  24.981 5.742   1.00 67.57  ? 101 VAL A CB  1 
ATOM   744  C  CG1 . VAL A 1 101 ? -89.837  23.886 6.725   1.00 60.77  ? 101 VAL A CG1 1 
ATOM   745  C  CG2 . VAL A 1 101 ? -89.328  24.425 4.332   1.00 63.05  ? 101 VAL A CG2 1 
ATOM   746  N  N   . ALA A 1 102 ? -89.611  27.424 7.622   1.00 64.84  ? 102 ALA A N   1 
ATOM   747  C  CA  . ALA A 1 102 ? -89.610  28.008 8.960   1.00 62.49  ? 102 ALA A CA  1 
ATOM   748  C  C   . ALA A 1 102 ? -90.747  28.999 9.167   1.00 67.37  ? 102 ALA A C   1 
ATOM   749  O  O   . ALA A 1 102 ? -91.067  29.325 10.315  1.00 73.74  ? 102 ALA A O   1 
ATOM   750  C  CB  . ALA A 1 102 ? -88.270  28.693 9.228   1.00 60.68  ? 102 ALA A CB  1 
ATOM   751  N  N   . ALA A 1 103 ? -91.367  29.481 8.088   1.00 66.81  ? 103 ALA A N   1 
ATOM   752  C  CA  . ALA A 1 103 ? -92.466  30.428 8.228   1.00 64.56  ? 103 ALA A CA  1 
ATOM   753  C  C   . ALA A 1 103 ? -93.656  29.814 8.955   1.00 71.81  ? 103 ALA A C   1 
ATOM   754  O  O   . ALA A 1 103 ? -94.432  30.535 9.592   1.00 75.03  ? 103 ALA A O   1 
ATOM   755  C  CB  . ALA A 1 103 ? -92.891  30.942 6.854   1.00 64.11  ? 103 ALA A CB  1 
ATOM   756  N  N   . ALA A 1 104 ? -93.818  28.491 8.873   1.00 71.02  ? 104 ALA A N   1 
ATOM   757  C  CA  . ALA A 1 104 ? -94.932  27.833 9.548   1.00 71.17  ? 104 ALA A CA  1 
ATOM   758  C  C   . ALA A 1 104 ? -94.817  27.905 11.065  1.00 70.23  ? 104 ALA A C   1 
ATOM   759  O  O   . ALA A 1 104 ? -95.825  27.735 11.759  1.00 68.22  ? 104 ALA A O   1 
ATOM   760  C  CB  . ALA A 1 104 ? -95.031  26.375 9.098   1.00 69.72  ? 104 ALA A CB  1 
ATOM   761  N  N   . LEU A 1 105 ? -93.616  28.154 11.595  1.00 70.61  ? 105 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 105 ? -93.457  28.358 13.030  1.00 73.03  ? 105 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 105 ? -94.131  29.635 13.511  1.00 73.37  ? 105 LEU A C   1 
ATOM   764  O  O   . LEU A 1 105 ? -94.376  29.779 14.713  1.00 82.98  ? 105 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 105 ? -91.972  28.400 13.398  1.00 66.16  ? 105 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 105 ? -91.127  27.165 13.089  1.00 65.33  ? 105 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 105 ? -89.660  27.469 13.317  1.00 61.25  ? 105 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 105 ? -91.568  25.982 13.937  1.00 61.33  ? 105 LEU A CD2 1 
ATOM   769  N  N   . ASP A 1 106 ? -94.436  30.562 12.604  1.00 72.43  ? 106 ASP A N   1 
ATOM   770  C  CA  . ASP A 1 106 ? -94.979  31.863 12.968  1.00 79.17  ? 106 ASP A CA  1 
ATOM   771  C  C   . ASP A 1 106 ? -96.456  32.022 12.651  1.00 78.55  ? 106 ASP A C   1 
ATOM   772  O  O   . ASP A 1 106 ? -97.151  32.745 13.367  1.00 81.72  ? 106 ASP A O   1 
ATOM   773  C  CB  . ASP A 1 106 ? -94.198  32.975 12.260  1.00 78.23  ? 106 ASP A CB  1 
ATOM   774  C  CG  . ASP A 1 106 ? -92.702  32.861 12.479  1.00 83.24  ? 106 ASP A CG  1 
ATOM   775  O  OD1 . ASP A 1 106 ? -92.284  32.600 13.628  1.00 85.32  ? 106 ASP A OD1 1 
ATOM   776  O  OD2 . ASP A 1 106 ? -91.945  33.020 11.498  1.00 84.60  ? 106 ASP A OD2 1 
ATOM   777  N  N   . GLY A 1 107 ? -96.951  31.374 11.603  1.00 72.91  ? 107 GLY A N   1 
ATOM   778  C  CA  . GLY A 1 107 ? -98.341  31.482 11.237  1.00 76.29  ? 107 GLY A CA  1 
ATOM   779  C  C   . GLY A 1 107 ? -98.697  30.620 10.044  1.00 80.17  ? 107 GLY A C   1 
ATOM   780  O  O   . GLY A 1 107 ? -97.889  29.820 9.562   1.00 76.65  ? 107 GLY A O   1 
ATOM   781  N  N   . PRO A 1 108 ? -99.923  30.770 9.546   1.00 80.16  ? 108 PRO A N   1 
ATOM   782  C  CA  . PRO A 1 108 ? -100.364 29.948 8.414   1.00 71.51  ? 108 PRO A CA  1 
ATOM   783  C  C   . PRO A 1 108 ? -99.523  30.205 7.173   1.00 77.56  ? 108 PRO A C   1 
ATOM   784  O  O   . PRO A 1 108 ? -99.139  31.340 6.879   1.00 78.91  ? 108 PRO A O   1 
ATOM   785  C  CB  . PRO A 1 108 ? -101.820 30.381 8.205   1.00 79.80  ? 108 PRO A CB  1 
ATOM   786  C  CG  . PRO A 1 108 ? -102.235 30.996 9.504   1.00 82.67  ? 108 PRO A CG  1 
ATOM   787  C  CD  . PRO A 1 108 ? -100.998 31.640 10.052  1.00 84.92  ? 108 PRO A CD  1 
ATOM   788  N  N   . LEU A 1 109 ? -99.234  29.131 6.445   1.00 78.91  ? 109 LEU A N   1 
ATOM   789  C  CA  . LEU A 1 109 ? -98.495  29.267 5.203   1.00 78.22  ? 109 LEU A CA  1 
ATOM   790  C  C   . LEU A 1 109 ? -99.432  29.668 4.067   1.00 75.00  ? 109 LEU A C   1 
ATOM   791  O  O   . LEU A 1 109 ? -100.597 29.262 4.040   1.00 76.38  ? 109 LEU A O   1 
ATOM   792  C  CB  . LEU A 1 109 ? -97.798  27.960 4.845   1.00 74.67  ? 109 LEU A CB  1 
ATOM   793  C  CG  . LEU A 1 109 ? -96.612  27.527 5.703   1.00 73.87  ? 109 LEU A CG  1 
ATOM   794  C  CD1 . LEU A 1 109 ? -95.955  26.310 5.083   1.00 66.55  ? 109 LEU A CD1 1 
ATOM   795  C  CD2 . LEU A 1 109 ? -95.612  28.661 5.857   1.00 70.55  ? 109 LEU A CD2 1 
ATOM   796  N  N   . PRO A 1 110 ? -98.950  30.467 3.120   1.00 72.75  ? 110 PRO A N   1 
ATOM   797  C  CA  . PRO A 1 110 ? -99.735  30.713 1.909   1.00 79.55  ? 110 PRO A CA  1 
ATOM   798  C  C   . PRO A 1 110 ? -99.854  29.441 1.085   1.00 77.57  ? 110 PRO A C   1 
ATOM   799  O  O   . PRO A 1 110 ? -98.943  28.611 1.049   1.00 78.17  ? 110 PRO A O   1 
ATOM   800  C  CB  . PRO A 1 110 ? -98.924  31.784 1.172   1.00 79.11  ? 110 PRO A CB  1 
ATOM   801  C  CG  . PRO A 1 110 ? -97.521  31.571 1.643   1.00 76.59  ? 110 PRO A CG  1 
ATOM   802  C  CD  . PRO A 1 110 ? -97.644  31.148 3.084   1.00 71.40  ? 110 PRO A CD  1 
ATOM   803  N  N   . ASP A 1 111 ? -100.999 29.294 0.414   1.00 79.28  ? 111 ASP A N   1 
ATOM   804  C  CA  . ASP A 1 111 ? -101.234 28.101 -0.394  1.00 85.07  ? 111 ASP A CA  1 
ATOM   805  C  C   . ASP A 1 111 ? -100.189 27.923 -1.490  1.00 81.83  ? 111 ASP A C   1 
ATOM   806  O  O   . ASP A 1 111 ? -100.066 26.825 -2.041  1.00 80.33  ? 111 ASP A O   1 
ATOM   807  C  CB  . ASP A 1 111 ? -102.634 28.146 -1.009  1.00 84.56  ? 111 ASP A CB  1 
ATOM   808  C  CG  . ASP A 1 111 ? -103.730 27.942 0.020   1.00 101.78 ? 111 ASP A CG  1 
ATOM   809  O  OD1 . ASP A 1 111 ? -103.408 27.830 1.224   1.00 101.51 ? 111 ASP A OD1 1 
ATOM   810  O  OD2 . ASP A 1 111 ? -104.913 27.890 -0.376  1.00 108.76 ? 111 ASP A OD2 1 
ATOM   811  N  N   . THR A 1 112 ? -99.429  28.968 -1.811  1.00 83.98  ? 112 THR A N   1 
ATOM   812  C  CA  . THR A 1 112 ? -98.357  28.883 -2.794  1.00 84.46  ? 112 THR A CA  1 
ATOM   813  C  C   . THR A 1 112 ? -97.077  28.279 -2.232  1.00 84.33  ? 112 THR A C   1 
ATOM   814  O  O   . THR A 1 112 ? -96.082  28.197 -2.961  1.00 88.33  ? 112 THR A O   1 
ATOM   815  C  CB  . THR A 1 112 ? -98.048  30.274 -3.358  1.00 91.24  ? 112 THR A CB  1 
ATOM   816  O  OG1 . THR A 1 112 ? -97.381  31.059 -2.360  1.00 83.94  ? 112 THR A OG1 1 
ATOM   817  C  CG2 . THR A 1 112 ? -99.331  30.979 -3.772  1.00 91.56  ? 112 THR A CG2 1 
ATOM   818  N  N   . ALA A 1 113 ? -97.069  27.865 -0.966  1.00 80.35  ? 113 ALA A N   1 
ATOM   819  C  CA  . ALA A 1 113 ? -95.856  27.341 -0.363  1.00 79.18  ? 113 ALA A CA  1 
ATOM   820  C  C   . ALA A 1 113 ? -95.512  25.975 -0.958  1.00 73.43  ? 113 ALA A C   1 
ATOM   821  O  O   . ALA A 1 113 ? -96.404  25.224 -1.361  1.00 75.57  ? 113 ALA A O   1 
ATOM   822  C  CB  . ALA A 1 113 ? -96.017  27.222 1.150   1.00 74.66  ? 113 ALA A CB  1 
ATOM   823  N  N   . PRO A 1 114 ? -94.226  25.636 -1.032  1.00 70.27  ? 114 PRO A N   1 
ATOM   824  C  CA  . PRO A 1 114 ? -93.851  24.331 -1.567  1.00 71.39  ? 114 PRO A CA  1 
ATOM   825  C  C   . PRO A 1 114 ? -94.365  23.219 -0.675  1.00 72.94  ? 114 PRO A C   1 
ATOM   826  O  O   . PRO A 1 114 ? -94.570  23.416 0.537   1.00 74.81  ? 114 PRO A O   1 
ATOM   827  C  CB  . PRO A 1 114 ? -92.315  24.382 -1.582  1.00 72.84  ? 114 PRO A CB  1 
ATOM   828  C  CG  . PRO A 1 114 ? -91.949  25.458 -0.626  1.00 73.14  ? 114 PRO A CG  1 
ATOM   829  C  CD  . PRO A 1 114 ? -93.053  26.460 -0.699  1.00 73.97  ? 114 PRO A CD  1 
ATOM   830  N  N   . PRO A 1 115 ? -94.599  22.027 -1.237  1.00 79.80  ? 115 PRO A N   1 
ATOM   831  C  CA  . PRO A 1 115 ? -95.173  20.937 -0.424  1.00 75.97  ? 115 PRO A CA  1 
ATOM   832  C  C   . PRO A 1 115 ? -94.346  20.586 0.799   1.00 67.29  ? 115 PRO A C   1 
ATOM   833  O  O   . PRO A 1 115 ? -94.911  20.234 1.842   1.00 67.74  ? 115 PRO A O   1 
ATOM   834  C  CB  . PRO A 1 115 ? -95.245  19.768 -1.417  1.00 75.55  ? 115 PRO A CB  1 
ATOM   835  C  CG  . PRO A 1 115 ? -95.319  20.418 -2.758  1.00 71.10  ? 115 PRO A CG  1 
ATOM   836  C  CD  . PRO A 1 115 ? -94.468  21.651 -2.655  1.00 73.13  ? 115 PRO A CD  1 
ATOM   837  N  N   . ILE A 1 116 ? -93.017  20.676 0.700   1.00 67.29  ? 116 ILE A N   1 
ATOM   838  C  CA  . ILE A 1 116 ? -92.168  20.385 1.848   1.00 61.05  ? 116 ILE A CA  1 
ATOM   839  C  C   . ILE A 1 116 ? -92.473  21.344 2.990   1.00 67.37  ? 116 ILE A C   1 
ATOM   840  O  O   . ILE A 1 116 ? -92.347  20.984 4.166   1.00 62.65  ? 116 ILE A O   1 
ATOM   841  C  CB  . ILE A 1 116 ? -90.682  20.430 1.432   1.00 65.68  ? 116 ILE A CB  1 
ATOM   842  C  CG1 . ILE A 1 116 ? -89.806  19.746 2.484   1.00 72.53  ? 116 ILE A CG1 1 
ATOM   843  C  CG2 . ILE A 1 116 ? -90.219  21.863 1.182   1.00 66.83  ? 116 ILE A CG2 1 
ATOM   844  C  CD1 . ILE A 1 116 ? -90.050  18.254 2.599   1.00 67.02  ? 116 ILE A CD1 1 
ATOM   845  N  N   . ALA A 1 117 ? -92.905  22.567 2.669   1.00 73.68  ? 117 ALA A N   1 
ATOM   846  C  CA  . ALA A 1 117 ? -93.270  23.513 3.716   1.00 65.03  ? 117 ALA A CA  1 
ATOM   847  C  C   . ALA A 1 117 ? -94.626  23.166 4.317   1.00 63.73  ? 117 ALA A C   1 
ATOM   848  O  O   . ALA A 1 117 ? -94.798  23.218 5.541   1.00 66.09  ? 117 ALA A O   1 
ATOM   849  C  CB  . ALA A 1 117 ? -93.269  24.935 3.160   1.00 65.27  ? 117 ALA A CB  1 
ATOM   850  N  N   . HIS A 1 118 ? -95.603  22.814 3.475   1.00 60.93  ? 118 HIS A N   1 
ATOM   851  C  CA  . HIS A 1 118 ? -96.893  22.363 3.990   1.00 65.73  ? 118 HIS A CA  1 
ATOM   852  C  C   . HIS A 1 118 ? -96.749  21.097 4.821   1.00 66.39  ? 118 HIS A C   1 
ATOM   853  O  O   . HIS A 1 118 ? -97.498  20.898 5.785   1.00 62.78  ? 118 HIS A O   1 
ATOM   854  C  CB  . HIS A 1 118 ? -97.874  22.116 2.844   1.00 64.81  ? 118 HIS A CB  1 
ATOM   855  C  CG  . HIS A 1 118 ? -98.258  23.351 2.091   1.00 75.89  ? 118 HIS A CG  1 
ATOM   856  N  ND1 . HIS A 1 118 ? -99.232  24.221 2.533   1.00 74.07  ? 118 HIS A ND1 1 
ATOM   857  C  CD2 . HIS A 1 118 ? -97.814  23.852 0.914   1.00 74.06  ? 118 HIS A CD2 1 
ATOM   858  C  CE1 . HIS A 1 118 ? -99.364  25.210 1.667   1.00 76.27  ? 118 HIS A CE1 1 
ATOM   859  N  NE2 . HIS A 1 118 ? -98.515  25.009 0.675   1.00 79.80  ? 118 HIS A NE2 1 
ATOM   860  N  N   . GLY A 1 119 ? -95.805  20.226 4.457   1.00 66.61  ? 119 GLY A N   1 
ATOM   861  C  CA  . GLY A 1 119 ? -95.562  19.040 5.261   1.00 64.33  ? 119 GLY A CA  1 
ATOM   862  C  C   . GLY A 1 119 ? -95.071  19.385 6.652   1.00 64.04  ? 119 GLY A C   1 
ATOM   863  O  O   . GLY A 1 119 ? -95.563  18.851 7.650   1.00 61.26  ? 119 GLY A O   1 
ATOM   864  N  N   . PHE A 1 120 ? -94.097  20.294 6.735   1.00 60.52  ? 120 PHE A N   1 
ATOM   865  C  CA  . PHE A 1 120 ? -93.611  20.742 8.035   1.00 62.68  ? 120 PHE A CA  1 
ATOM   866  C  C   . PHE A 1 120 ? -94.719  21.413 8.837   1.00 60.24  ? 120 PHE A C   1 
ATOM   867  O  O   . PHE A 1 120 ? -94.816  21.224 10.054  1.00 64.39  ? 120 PHE A O   1 
ATOM   868  C  CB  . PHE A 1 120 ? -92.432  21.696 7.855   1.00 60.72  ? 120 PHE A CB  1 
ATOM   869  C  CG  . PHE A 1 120 ? -91.846  22.183 9.149   1.00 68.23  ? 120 PHE A CG  1 
ATOM   870  C  CD1 . PHE A 1 120 ? -90.902  21.425 9.825   1.00 65.19  ? 120 PHE A CD1 1 
ATOM   871  C  CD2 . PHE A 1 120 ? -92.241  23.398 9.694   1.00 64.60  ? 120 PHE A CD2 1 
ATOM   872  C  CE1 . PHE A 1 120 ? -90.357  21.869 11.022  1.00 65.34  ? 120 PHE A CE1 1 
ATOM   873  C  CE2 . PHE A 1 120 ? -91.704  23.848 10.888  1.00 64.91  ? 120 PHE A CE2 1 
ATOM   874  C  CZ  . PHE A 1 120 ? -90.759  23.083 11.554  1.00 65.64  ? 120 PHE A CZ  1 
ATOM   875  N  N   . ALA A 1 121 ? -95.566  22.198 8.170   1.00 62.97  ? 121 ALA A N   1 
ATOM   876  C  CA  . ALA A 1 121 ? -96.637  22.893 8.873   1.00 57.50  ? 121 ALA A CA  1 
ATOM   877  C  C   . ALA A 1 121 ? -97.604  21.911 9.520   1.00 56.68  ? 121 ALA A C   1 
ATOM   878  O  O   . ALA A 1 121 ? -98.120  22.166 10.613  1.00 62.73  ? 121 ALA A O   1 
ATOM   879  C  CB  . ALA A 1 121 ? -97.378  23.822 7.914   1.00 53.53  ? 121 ALA A CB  1 
ATOM   880  N  N   . ASP A 1 122 ? -97.864  20.780 8.860   1.00 62.69  ? 122 ASP A N   1 
ATOM   881  C  CA  . ASP A 1 122 ? -98.776  19.798 9.435   1.00 63.57  ? 122 ASP A CA  1 
ATOM   882  C  C   . ASP A 1 122 ? -98.138  19.065 10.605  1.00 64.38  ? 122 ASP A C   1 
ATOM   883  O  O   . ASP A 1 122 ? -98.839  18.663 11.541  1.00 66.04  ? 122 ASP A O   1 
ATOM   884  C  CB  . ASP A 1 122 ? -99.224  18.802 8.367   1.00 60.56  ? 122 ASP A CB  1 
ATOM   885  C  CG  . ASP A 1 122 ? -100.286 17.849 8.874   1.00 68.31  ? 122 ASP A CG  1 
ATOM   886  O  OD1 . ASP A 1 122 ? -101.271 18.323 9.480   1.00 78.50  ? 122 ASP A OD1 1 
ATOM   887  O  OD2 . ASP A 1 122 ? -100.142 16.628 8.665   1.00 71.75  ? 122 ASP A OD2 1 
ATOM   888  N  N   . ILE A 1 123 ? -96.818  18.883 10.569  1.00 62.26  ? 123 ILE A N   1 
ATOM   889  C  CA  . ILE A 1 123 ? -96.125  18.241 11.678  1.00 61.09  ? 123 ILE A CA  1 
ATOM   890  C  C   . ILE A 1 123 ? -96.046  19.180 12.870  1.00 66.38  ? 123 ILE A C   1 
ATOM   891  O  O   . ILE A 1 123 ? -96.297  18.776 14.012  1.00 66.20  ? 123 ILE A O   1 
ATOM   892  C  CB  . ILE A 1 123 ? -94.730  17.772 11.230  1.00 63.99  ? 123 ILE A CB  1 
ATOM   893  C  CG1 . ILE A 1 123 ? -94.853  16.530 10.348  1.00 61.01  ? 123 ILE A CG1 1 
ATOM   894  C  CG2 . ILE A 1 123 ? -93.828  17.511 12.435  1.00 59.01  ? 123 ILE A CG2 1 
ATOM   895  C  CD1 . ILE A 1 123 ? -93.534  16.001 9.879   1.00 63.67  ? 123 ILE A CD1 1 
ATOM   896  N  N   . TRP A 1 124 ? -95.710  20.451 12.625  1.00 63.55  ? 124 TRP A N   1 
ATOM   897  C  CA  . TRP A 1 124 ? -95.558  21.402 13.720  1.00 67.11  ? 124 TRP A CA  1 
ATOM   898  C  C   . TRP A 1 124 ? -96.892  21.687 14.397  1.00 66.40  ? 124 TRP A C   1 
ATOM   899  O  O   . TRP A 1 124 ? -96.948  21.842 15.622  1.00 70.70  ? 124 TRP A O   1 
ATOM   900  C  CB  . TRP A 1 124 ? -94.928  22.698 13.216  1.00 64.27  ? 124 TRP A CB  1 
ATOM   901  C  CG  . TRP A 1 124 ? -94.751  23.717 14.301  1.00 72.97  ? 124 TRP A CG  1 
ATOM   902  C  CD1 . TRP A 1 124 ? -95.358  24.934 14.390  1.00 69.40  ? 124 TRP A CD1 1 
ATOM   903  C  CD2 . TRP A 1 124 ? -93.922  23.595 15.466  1.00 70.15  ? 124 TRP A CD2 1 
ATOM   904  N  NE1 . TRP A 1 124 ? -94.951  25.584 15.531  1.00 72.88  ? 124 TRP A NE1 1 
ATOM   905  C  CE2 . TRP A 1 124 ? -94.069  24.783 16.208  1.00 70.29  ? 124 TRP A CE2 1 
ATOM   906  C  CE3 . TRP A 1 124 ? -93.065  22.600 15.947  1.00 65.13  ? 124 TRP A CE3 1 
ATOM   907  C  CZ2 . TRP A 1 124 ? -93.388  25.005 17.404  1.00 68.92  ? 124 TRP A CZ2 1 
ATOM   908  C  CZ3 . TRP A 1 124 ? -92.395  22.820 17.137  1.00 71.71  ? 124 TRP A CZ3 1 
ATOM   909  C  CH2 . TRP A 1 124 ? -92.563  24.012 17.854  1.00 70.14  ? 124 TRP A CH2 1 
ATOM   910  N  N   . ARG A 1 125 ? -97.972  21.766 13.617  1.00 61.00  ? 125 ARG A N   1 
ATOM   911  C  CA  . ARG A 1 125 ? -99.296  21.914 14.211  1.00 63.42  ? 125 ARG A CA  1 
ATOM   912  C  C   . ARG A 1 125 ? -99.595  20.769 15.170  1.00 69.36  ? 125 ARG A C   1 
ATOM   913  O  O   . ARG A 1 125 ? -100.110 20.989 16.272  1.00 68.78  ? 125 ARG A O   1 
ATOM   914  C  CB  . ARG A 1 125 ? -100.361 21.987 13.116  1.00 66.09  ? 125 ARG A CB  1 
ATOM   915  C  CG  . ARG A 1 125 ? -101.786 22.017 13.648  1.00 77.09  ? 125 ARG A CG  1 
ATOM   916  C  CD  . ARG A 1 125 ? -102.811 21.951 12.528  1.00 82.30  ? 125 ARG A CD  1 
ATOM   917  N  NE  . ARG A 1 125 ? -102.717 20.709 11.770  1.00 88.09  ? 125 ARG A NE  1 
ATOM   918  C  CZ  . ARG A 1 125 ? -103.292 19.567 12.124  1.00 96.75  ? 125 ARG A CZ  1 
ATOM   919  N  NH1 . ARG A 1 125 ? -104.004 19.467 13.237  1.00 93.26  ? 125 ARG A NH1 1 
ATOM   920  N  NH2 . ARG A 1 125 ? -103.147 18.498 11.343  1.00 82.76  ? 125 ARG A NH2 1 
ATOM   921  N  N   . ARG A 1 126 ? -99.264  19.538 14.773  1.00 68.35  ? 126 ARG A N   1 
ATOM   922  C  CA  . ARG A 1 126 ? -99.533  18.377 15.610  1.00 71.42  ? 126 ARG A CA  1 
ATOM   923  C  C   . ARG A 1 126 ? -98.555  18.239 16.771  1.00 66.59  ? 126 ARG A C   1 
ATOM   924  O  O   . ARG A 1 126 ? -98.895  17.604 17.773  1.00 62.36  ? 126 ARG A O   1 
ATOM   925  C  CB  . ARG A 1 126 ? -99.513  17.105 14.761  1.00 61.97  ? 126 ARG A CB  1 
ATOM   926  C  CG  . ARG A 1 126 ? -100.776 16.884 13.946  1.00 73.25  ? 126 ARG A CG  1 
ATOM   927  C  CD  . ARG A 1 126 ? -100.732 15.540 13.242  1.00 69.51  ? 126 ARG A CD  1 
ATOM   928  N  NE  . ARG A 1 126 ? -99.754  15.524 12.162  1.00 62.88  ? 126 ARG A NE  1 
ATOM   929  C  CZ  . ARG A 1 126 ? -99.171  14.428 11.696  1.00 67.25  ? 126 ARG A CZ  1 
ATOM   930  N  NH1 . ARG A 1 126 ? -99.415  13.238 12.221  1.00 63.97  ? 126 ARG A NH1 1 
ATOM   931  N  NH2 . ARG A 1 126 ? -98.316  14.530 10.681  1.00 66.16  ? 126 ARG A NH2 1 
ATOM   932  N  N   . THR A 1 127 ? -97.353  18.812 16.660  1.00 63.66  ? 127 THR A N   1 
ATOM   933  C  CA  . THR A 1 127 ? -96.391  18.740 17.754  1.00 63.54  ? 127 THR A CA  1 
ATOM   934  C  C   . THR A 1 127 ? -96.802  19.630 18.921  1.00 72.77  ? 127 THR A C   1 
ATOM   935  O  O   . THR A 1 127 ? -96.542  19.291 20.082  1.00 69.50  ? 127 THR A O   1 
ATOM   936  C  CB  . THR A 1 127 ? -95.000  19.135 17.252  1.00 65.00  ? 127 THR A CB  1 
ATOM   937  O  OG1 . THR A 1 127 ? -94.596  18.253 16.197  1.00 66.82  ? 127 THR A OG1 1 
ATOM   938  C  CG2 . THR A 1 127 ? -93.976  19.064 18.375  1.00 68.89  ? 127 THR A CG2 1 
ATOM   939  N  N   . CYS A 1 128 ? -97.461  20.751 18.639  1.00 73.82  ? 128 CYS A N   1 
ATOM   940  C  CA  . CYS A 1 128 ? -97.741  21.765 19.647  1.00 67.40  ? 128 CYS A CA  1 
ATOM   941  C  C   . CYS A 1 128 ? -99.048  21.536 20.391  1.00 69.71  ? 128 CYS A C   1 
ATOM   942  O  O   . CYS A 1 128 ? -99.127  21.824 21.590  1.00 77.15  ? 128 CYS A O   1 
ATOM   943  C  CB  . CYS A 1 128 ? -97.770  23.146 18.998  1.00 74.91  ? 128 CYS A CB  1 
ATOM   944  S  SG  . CYS A 1 128 ? -96.144  23.750 18.585  1.00 88.59  ? 128 CYS A SG  1 
ATOM   945  N  N   . GLU A 1 129 ? -100.077 21.051 19.699  1.00 70.71  ? 129 GLU A N   1 
ATOM   946  C  CA  . GLU A 1 129 ? -101.392 20.879 20.304  1.00 73.06  ? 129 GLU A CA  1 
ATOM   947  C  C   . GLU A 1 129 ? -101.299 20.042 21.570  1.00 72.04  ? 129 GLU A C   1 
ATOM   948  O  O   . GLU A 1 129 ? -100.871 18.885 21.533  1.00 74.70  ? 129 GLU A O   1 
ATOM   949  C  CB  . GLU A 1 129 ? -102.348 20.231 19.300  1.00 73.88  ? 129 GLU A CB  1 
ATOM   950  C  CG  . GLU A 1 129 ? -102.755 21.150 18.159  1.00 85.01  ? 129 GLU A CG  1 
ATOM   951  C  CD  . GLU A 1 129 ? -103.593 20.451 17.106  1.00 94.91  ? 129 GLU A CD  1 
ATOM   952  O  OE1 . GLU A 1 129 ? -103.753 19.213 17.191  1.00 88.08  ? 129 GLU A OE1 1 
ATOM   953  O  OE2 . GLU A 1 129 ? -104.089 21.144 16.190  1.00 92.71  ? 129 GLU A OE2 1 
ATOM   954  N  N   . GLY A 1 130 ? -101.680 20.642 22.694  1.00 71.48  ? 130 GLY A N   1 
ATOM   955  C  CA  . GLY A 1 130 ? -101.664 19.954 23.966  1.00 71.96  ? 130 GLY A CA  1 
ATOM   956  C  C   . GLY A 1 130 ? -100.401 20.116 24.780  1.00 69.64  ? 130 GLY A C   1 
ATOM   957  O  O   . GLY A 1 130 ? -100.281 19.478 25.833  1.00 74.87  ? 130 GLY A O   1 
ATOM   958  N  N   . MET A 1 131 ? -99.454  20.930 24.329  1.00 63.07  ? 131 MET A N   1 
ATOM   959  C  CA  . MET A 1 131 ? -98.263  21.248 25.100  1.00 68.64  ? 131 MET A CA  1 
ATOM   960  C  C   . MET A 1 131 ? -98.381  22.656 25.674  1.00 70.38  ? 131 MET A C   1 
ATOM   961  O  O   . MET A 1 131 ? -99.230  23.450 25.260  1.00 69.03  ? 131 MET A O   1 
ATOM   962  C  CB  . MET A 1 131 ? -97.005  21.130 24.233  1.00 65.17  ? 131 MET A CB  1 
ATOM   963  C  CG  . MET A 1 131 ? -96.891  19.815 23.470  1.00 65.63  ? 131 MET A CG  1 
ATOM   964  S  SD  . MET A 1 131 ? -96.662  18.351 24.510  1.00 62.89  ? 131 MET A SD  1 
ATOM   965  C  CE  . MET A 1 131 ? -94.953  18.532 25.015  1.00 57.67  ? 131 MET A CE  1 
ATOM   966  N  N   . THR A 1 132 ? -97.525  22.959 26.647  1.00 66.14  ? 132 THR A N   1 
ATOM   967  C  CA  . THR A 1 132 ? -97.514  24.302 27.203  1.00 68.54  ? 132 THR A CA  1 
ATOM   968  C  C   . THR A 1 132 ? -96.953  25.287 26.177  1.00 65.41  ? 132 THR A C   1 
ATOM   969  O  O   . THR A 1 132 ? -96.078  24.934 25.381  1.00 63.98  ? 132 THR A O   1 
ATOM   970  C  CB  . THR A 1 132 ? -96.686  24.366 28.488  1.00 64.57  ? 132 THR A CB  1 
ATOM   971  O  OG1 . THR A 1 132 ? -95.345  23.930 28.228  1.00 63.28  ? 132 THR A OG1 1 
ATOM   972  C  CG2 . THR A 1 132 ? -97.300  23.497 29.571  1.00 61.60  ? 132 THR A CG2 1 
ATOM   973  N  N   . PRO A 1 133 ? -97.452  26.528 26.170  1.00 66.46  ? 133 PRO A N   1 
ATOM   974  C  CA  . PRO A 1 133 ? -96.916  27.522 25.223  1.00 58.53  ? 133 PRO A CA  1 
ATOM   975  C  C   . PRO A 1 133 ? -95.417  27.725 25.349  1.00 58.20  ? 133 PRO A C   1 
ATOM   976  O  O   . PRO A 1 133 ? -94.734  27.926 24.335  1.00 70.73  ? 133 PRO A O   1 
ATOM   977  C  CB  . PRO A 1 133 ? -97.693  28.796 25.581  1.00 55.05  ? 133 PRO A CB  1 
ATOM   978  C  CG  . PRO A 1 133 ? -98.959  28.302 26.209  1.00 62.70  ? 133 PRO A CG  1 
ATOM   979  C  CD  . PRO A 1 133 ? -98.581  27.058 26.955  1.00 65.50  ? 133 PRO A CD  1 
ATOM   980  N  N   . ALA A 1 134 ? -94.881  27.675 26.569  1.00 55.19  ? 134 ALA A N   1 
ATOM   981  C  CA  . ALA A 1 134 ? -93.440  27.822 26.746  1.00 64.90  ? 134 ALA A CA  1 
ATOM   982  C  C   . ALA A 1 134 ? -92.680  26.665 26.112  1.00 61.96  ? 134 ALA A C   1 
ATOM   983  O  O   . ALA A 1 134 ? -91.557  26.854 25.631  1.00 57.95  ? 134 ALA A O   1 
ATOM   984  C  CB  . ALA A 1 134 ? -93.097  27.934 28.232  1.00 57.92  ? 134 ALA A CB  1 
ATOM   985  N  N   . TRP A 1 135 ? -93.270  25.467 26.104  1.00 60.23  ? 135 TRP A N   1 
ATOM   986  C  CA  . TRP A 1 135 ? -92.640  24.346 25.417  1.00 65.99  ? 135 TRP A CA  1 
ATOM   987  C  C   . TRP A 1 135 ? -92.670  24.542 23.904  1.00 65.10  ? 135 TRP A C   1 
ATOM   988  O  O   . TRP A 1 135 ? -91.685  24.250 23.214  1.00 56.51  ? 135 TRP A O   1 
ATOM   989  C  CB  . TRP A 1 135 ? -93.327  23.037 25.812  1.00 63.49  ? 135 TRP A CB  1 
ATOM   990  C  CG  . TRP A 1 135 ? -92.678  21.824 25.222  1.00 67.38  ? 135 TRP A CG  1 
ATOM   991  C  CD1 . TRP A 1 135 ? -91.742  21.026 25.813  1.00 66.68  ? 135 TRP A CD1 1 
ATOM   992  C  CD2 . TRP A 1 135 ? -92.907  21.274 23.918  1.00 64.79  ? 135 TRP A CD2 1 
ATOM   993  N  NE1 . TRP A 1 135 ? -91.376  20.014 24.961  1.00 62.70  ? 135 TRP A NE1 1 
ATOM   994  C  CE2 . TRP A 1 135 ? -92.077  20.144 23.791  1.00 67.70  ? 135 TRP A CE2 1 
ATOM   995  C  CE3 . TRP A 1 135 ? -93.733  21.628 22.845  1.00 66.35  ? 135 TRP A CE3 1 
ATOM   996  C  CZ2 . TRP A 1 135 ? -92.050  19.364 22.636  1.00 65.83  ? 135 TRP A CZ2 1 
ATOM   997  C  CZ3 . TRP A 1 135 ? -93.704  20.853 21.700  1.00 69.12  ? 135 TRP A CZ3 1 
ATOM   998  C  CH2 . TRP A 1 135 ? -92.868  19.734 21.606  1.00 68.95  ? 135 TRP A CH2 1 
ATOM   999  N  N   . CYS A 1 136 ? -93.790  25.043 23.371  1.00 61.10  ? 136 CYS A N   1 
ATOM   1000 C  CA  . CYS A 1 136 ? -93.886  25.289 21.934  1.00 68.84  ? 136 CYS A CA  1 
ATOM   1001 C  C   . CYS A 1 136 ? -92.869  26.330 21.480  1.00 67.67  ? 136 CYS A C   1 
ATOM   1002 O  O   . CYS A 1 136 ? -92.305  26.221 20.385  1.00 68.93  ? 136 CYS A O   1 
ATOM   1003 C  CB  . CYS A 1 136 ? -95.302  25.736 21.566  1.00 66.48  ? 136 CYS A CB  1 
ATOM   1004 S  SG  . CYS A 1 136 ? -96.607  24.534 21.927  1.00 81.78  ? 136 CYS A SG  1 
ATOM   1005 N  N   . ALA A 1 137 ? -92.621  27.346 22.308  1.00 65.51  ? 137 ALA A N   1 
ATOM   1006 C  CA  . ALA A 1 137 ? -91.677  28.392 21.929  1.00 63.19  ? 137 ALA A CA  1 
ATOM   1007 C  C   . ALA A 1 137 ? -90.243  27.879 21.954  1.00 65.13  ? 137 ALA A C   1 
ATOM   1008 O  O   . ALA A 1 137 ? -89.446  28.199 21.063  1.00 71.04  ? 137 ALA A O   1 
ATOM   1009 C  CB  . ALA A 1 137 ? -91.835  29.598 22.854  1.00 62.01  ? 137 ALA A CB  1 
ATOM   1010 N  N   . ARG A 1 138 ? -89.896  27.082 22.968  1.00 64.31  ? 138 ARG A N   1 
ATOM   1011 C  CA  . ARG A 1 138 ? -88.553  26.518 23.044  1.00 65.14  ? 138 ARG A CA  1 
ATOM   1012 C  C   . ARG A 1 138 ? -88.288  25.557 21.893  1.00 62.81  ? 138 ARG A C   1 
ATOM   1013 O  O   . ARG A 1 138 ? -87.159  25.478 21.396  1.00 63.12  ? 138 ARG A O   1 
ATOM   1014 C  CB  . ARG A 1 138 ? -88.362  25.813 24.389  1.00 57.63  ? 138 ARG A CB  1 
ATOM   1015 C  CG  . ARG A 1 138 ? -86.964  25.266 24.628  1.00 56.62  ? 138 ARG A CG  1 
ATOM   1016 C  CD  . ARG A 1 138 ? -86.913  24.453 25.911  1.00 61.64  ? 138 ARG A CD  1 
ATOM   1017 N  NE  . ARG A 1 138 ? -87.676  23.214 25.812  1.00 64.76  ? 138 ARG A NE  1 
ATOM   1018 C  CZ  . ARG A 1 138 ? -88.053  22.478 26.850  1.00 69.65  ? 138 ARG A CZ  1 
ATOM   1019 N  NH1 . ARG A 1 138 ? -87.782  22.844 28.093  1.00 73.85  ? 138 ARG A NH1 1 
ATOM   1020 N  NH2 . ARG A 1 138 ? -88.722  21.347 26.636  1.00 66.44  ? 138 ARG A NH2 1 
ATOM   1021 N  N   . SER A 1 139 ? -89.315  24.826 21.453  1.00 62.93  ? 139 SER A N   1 
ATOM   1022 C  CA  . SER A 1 139 ? -89.152  23.901 20.337  1.00 63.79  ? 139 SER A CA  1 
ATOM   1023 C  C   . SER A 1 139 ? -89.063  24.640 19.007  1.00 66.01  ? 139 SER A C   1 
ATOM   1024 O  O   . SER A 1 139 ? -88.272  24.260 18.136  1.00 64.40  ? 139 SER A O   1 
ATOM   1025 C  CB  . SER A 1 139 ? -90.306  22.900 20.317  1.00 64.10  ? 139 SER A CB  1 
ATOM   1026 O  OG  . SER A 1 139 ? -90.325  22.114 21.495  1.00 66.17  ? 139 SER A OG  1 
ATOM   1027 N  N   . ALA A 1 140 ? -89.870  25.689 18.833  1.00 63.59  ? 140 ALA A N   1 
ATOM   1028 C  CA  . ALA A 1 140 ? -89.761  26.511 17.633  1.00 64.87  ? 140 ALA A CA  1 
ATOM   1029 C  C   . ALA A 1 140 ? -88.366  27.108 17.504  1.00 62.75  ? 140 ALA A C   1 
ATOM   1030 O  O   . ALA A 1 140 ? -87.849  27.263 16.392  1.00 64.79  ? 140 ALA A O   1 
ATOM   1031 C  CB  . ALA A 1 140 ? -90.820  27.612 17.651  1.00 64.65  ? 140 ALA A CB  1 
ATOM   1032 N  N   . ARG A 1 141 ? -87.739  27.445 18.633  1.00 63.21  ? 141 ARG A N   1 
ATOM   1033 C  CA  . ARG A 1 141 ? -86.360  27.918 18.594  1.00 63.49  ? 141 ARG A CA  1 
ATOM   1034 C  C   . ARG A 1 141 ? -85.416  26.817 18.132  1.00 65.49  ? 141 ARG A C   1 
ATOM   1035 O  O   . ARG A 1 141 ? -84.459  27.081 17.394  1.00 60.11  ? 141 ARG A O   1 
ATOM   1036 C  CB  . ARG A 1 141 ? -85.942  28.439 19.967  1.00 60.76  ? 141 ARG A CB  1 
ATOM   1037 C  CG  . ARG A 1 141 ? -86.628  29.731 20.365  1.00 75.61  ? 141 ARG A CG  1 
ATOM   1038 C  CD  . ARG A 1 141 ? -85.920  30.404 21.532  1.00 79.99  ? 141 ARG A CD  1 
ATOM   1039 N  NE  . ARG A 1 141 ? -86.039  29.648 22.773  1.00 76.86  ? 141 ARG A NE  1 
ATOM   1040 C  CZ  . ARG A 1 141 ? -87.079  29.724 23.592  1.00 76.28  ? 141 ARG A CZ  1 
ATOM   1041 N  NH1 . ARG A 1 141 ? -88.121  30.490 23.314  1.00 74.34  ? 141 ARG A NH1 1 
ATOM   1042 N  NH2 . ARG A 1 141 ? -87.072  29.014 24.717  1.00 65.90  ? 141 ARG A NH2 1 
ATOM   1043 N  N   . HIS A 1 142 ? -85.670  25.578 18.558  1.00 64.07  ? 142 HIS A N   1 
ATOM   1044 C  CA  . HIS A 1 142 ? -84.839  24.462 18.121  1.00 63.51  ? 142 HIS A CA  1 
ATOM   1045 C  C   . HIS A 1 142 ? -84.956  24.244 16.619  1.00 60.67  ? 142 HIS A C   1 
ATOM   1046 O  O   . HIS A 1 142 ? -83.971  23.905 15.955  1.00 58.65  ? 142 HIS A O   1 
ATOM   1047 C  CB  . HIS A 1 142 ? -85.223  23.193 18.878  1.00 63.94  ? 142 HIS A CB  1 
ATOM   1048 C  CG  . HIS A 1 142 ? -84.922  23.251 20.342  1.00 67.27  ? 142 HIS A CG  1 
ATOM   1049 N  ND1 . HIS A 1 142 ? -85.663  22.567 21.280  1.00 66.92  ? 142 HIS A ND1 1 
ATOM   1050 C  CD2 . HIS A 1 142 ? -83.956  23.907 21.028  1.00 63.18  ? 142 HIS A CD2 1 
ATOM   1051 C  CE1 . HIS A 1 142 ? -85.170  22.802 22.483  1.00 66.78  ? 142 HIS A CE1 1 
ATOM   1052 N  NE2 . HIS A 1 142 ? -84.134  23.611 22.357  1.00 69.45  ? 142 HIS A NE2 1 
ATOM   1053 N  N   . TRP A 1 143 ? -86.155  24.434 16.065  1.00 60.75  ? 143 TRP A N   1 
ATOM   1054 C  CA  . TRP A 1 143 ? -86.326  24.316 14.620  1.00 60.79  ? 143 TRP A CA  1 
ATOM   1055 C  C   . TRP A 1 143 ? -85.556  25.406 13.882  1.00 63.59  ? 143 TRP A C   1 
ATOM   1056 O  O   . TRP A 1 143 ? -84.855  25.129 12.901  1.00 67.39  ? 143 TRP A O   1 
ATOM   1057 C  CB  . TRP A 1 143 ? -87.809  24.363 14.258  1.00 60.14  ? 143 TRP A CB  1 
ATOM   1058 C  CG  . TRP A 1 143 ? -88.503  23.034 14.349  1.00 59.01  ? 143 TRP A CG  1 
ATOM   1059 C  CD1 . TRP A 1 143 ? -89.643  22.751 15.043  1.00 56.47  ? 143 TRP A CD1 1 
ATOM   1060 C  CD2 . TRP A 1 143 ? -88.102  21.809 13.721  1.00 59.99  ? 143 TRP A CD2 1 
ATOM   1061 N  NE1 . TRP A 1 143 ? -89.979  21.429 14.884  1.00 53.33  ? 143 TRP A NE1 1 
ATOM   1062 C  CE2 . TRP A 1 143 ? -89.048  20.828 14.078  1.00 60.93  ? 143 TRP A CE2 1 
ATOM   1063 C  CE3 . TRP A 1 143 ? -87.036  21.447 12.888  1.00 60.72  ? 143 TRP A CE3 1 
ATOM   1064 C  CZ2 . TRP A 1 143 ? -88.960  19.508 13.636  1.00 58.76  ? 143 TRP A CZ2 1 
ATOM   1065 C  CZ3 . TRP A 1 143 ? -86.950  20.137 12.449  1.00 59.17  ? 143 TRP A CZ3 1 
ATOM   1066 C  CH2 . TRP A 1 143 ? -87.906  19.184 12.823  1.00 62.02  ? 143 TRP A CH2 1 
ATOM   1067 N  N   . ARG A 1 144 ? -85.671  26.656 14.342  1.00 63.80  ? 144 ARG A N   1 
ATOM   1068 C  CA  . ARG A 1 144 ? -84.970  27.754 13.681  1.00 63.05  ? 144 ARG A CA  1 
ATOM   1069 C  C   . ARG A 1 144 ? -83.460  27.559 13.713  1.00 60.99  ? 144 ARG A C   1 
ATOM   1070 O  O   . ARG A 1 144 ? -82.762  27.986 12.787  1.00 68.38  ? 144 ARG A O   1 
ATOM   1071 C  CB  . ARG A 1 144 ? -85.349  29.089 14.322  1.00 60.62  ? 144 ARG A CB  1 
ATOM   1072 C  CG  . ARG A 1 144 ? -86.812  29.443 14.155  1.00 61.97  ? 144 ARG A CG  1 
ATOM   1073 C  CD  . ARG A 1 144 ? -87.100  30.871 14.570  1.00 59.07  ? 144 ARG A CD  1 
ATOM   1074 N  NE  . ARG A 1 144 ? -88.526  31.167 14.502  1.00 68.60  ? 144 ARG A NE  1 
ATOM   1075 C  CZ  . ARG A 1 144 ? -89.383  30.935 15.487  1.00 74.75  ? 144 ARG A CZ  1 
ATOM   1076 N  NH1 . ARG A 1 144 ? -88.987  30.415 16.637  1.00 65.48  ? 144 ARG A NH1 1 
ATOM   1077 N  NH2 . ARG A 1 144 ? -90.669  31.229 15.314  1.00 78.24  ? 144 ARG A NH2 1 
ATOM   1078 N  N   . ASN A 1 145 ? -82.937  26.921 14.761  1.00 60.54  ? 145 ASN A N   1 
ATOM   1079 C  CA  . ASN A 1 145 ? -81.516  26.586 14.776  1.00 68.00  ? 145 ASN A CA  1 
ATOM   1080 C  C   . ASN A 1 145 ? -81.187  25.563 13.696  1.00 66.80  ? 145 ASN A C   1 
ATOM   1081 O  O   . ASN A 1 145 ? -80.117  25.622 13.080  1.00 66.04  ? 145 ASN A O   1 
ATOM   1082 C  CB  . ASN A 1 145 ? -81.111  26.055 16.152  1.00 67.83  ? 145 ASN A CB  1 
ATOM   1083 C  CG  . ASN A 1 145 ? -81.135  27.127 17.226  1.00 70.26  ? 145 ASN A CG  1 
ATOM   1084 O  OD1 . ASN A 1 145 ? -81.391  28.296 16.945  1.00 68.86  ? 145 ASN A OD1 1 
ATOM   1085 N  ND2 . ASN A 1 145 ? -80.878  26.727 18.468  1.00 69.03  ? 145 ASN A ND2 1 
ATOM   1086 N  N   . TYR A 1 146 ? -82.100  24.620 13.458  1.00 65.68  ? 146 TYR A N   1 
ATOM   1087 C  CA  . TYR A 1 146 ? -81.884  23.578 12.461  1.00 67.65  ? 146 TYR A CA  1 
ATOM   1088 C  C   . TYR A 1 146 ? -81.902  24.158 11.048  1.00 70.50  ? 146 TYR A C   1 
ATOM   1089 O  O   . TYR A 1 146 ? -81.019  23.867 10.233  1.00 62.97  ? 146 TYR A O   1 
ATOM   1090 C  CB  . TYR A 1 146 ? -82.950  22.493 12.642  1.00 62.67  ? 146 TYR A CB  1 
ATOM   1091 C  CG  . TYR A 1 146 ? -83.012  21.428 11.570  1.00 71.01  ? 146 TYR A CG  1 
ATOM   1092 C  CD1 . TYR A 1 146 ? -82.100  20.378 11.548  1.00 70.28  ? 146 TYR A CD1 1 
ATOM   1093 C  CD2 . TYR A 1 146 ? -84.010  21.450 10.603  1.00 66.21  ? 146 TYR A CD2 1 
ATOM   1094 C  CE1 . TYR A 1 146 ? -82.167  19.393 10.578  1.00 67.11  ? 146 TYR A CE1 1 
ATOM   1095 C  CE2 . TYR A 1 146 ? -84.086  20.469 9.631   1.00 66.94  ? 146 TYR A CE2 1 
ATOM   1096 C  CZ  . TYR A 1 146 ? -83.162  19.443 9.620   1.00 74.91  ? 146 TYR A CZ  1 
ATOM   1097 O  OH  . TYR A 1 146 ? -83.233  18.466 8.648   1.00 81.57  ? 146 TYR A OH  1 
ATOM   1098 N  N   . PHE A 1 147 ? -82.893  25.003 10.750  1.00 67.32  ? 147 PHE A N   1 
ATOM   1099 C  CA  . PHE A 1 147 ? -82.993  25.595 9.420   1.00 64.69  ? 147 PHE A CA  1 
ATOM   1100 C  C   . PHE A 1 147 ? -81.820  26.524 9.132   1.00 69.00  ? 147 PHE A C   1 
ATOM   1101 O  O   . PHE A 1 147 ? -81.273  26.518 8.022   1.00 73.29  ? 147 PHE A O   1 
ATOM   1102 C  CB  . PHE A 1 147 ? -84.320  26.338 9.286   1.00 64.41  ? 147 PHE A CB  1 
ATOM   1103 C  CG  . PHE A 1 147 ? -85.521  25.442 9.362   1.00 64.09  ? 147 PHE A CG  1 
ATOM   1104 C  CD1 . PHE A 1 147 ? -85.603  24.305 8.575   1.00 65.71  ? 147 PHE A CD1 1 
ATOM   1105 C  CD2 . PHE A 1 147 ? -86.558  25.726 10.230  1.00 59.72  ? 147 PHE A CD2 1 
ATOM   1106 C  CE1 . PHE A 1 147 ? -86.707  23.475 8.643   1.00 62.16  ? 147 PHE A CE1 1 
ATOM   1107 C  CE2 . PHE A 1 147 ? -87.663  24.900 10.306  1.00 63.36  ? 147 PHE A CE2 1 
ATOM   1108 C  CZ  . PHE A 1 147 ? -87.737  23.772 9.513   1.00 61.40  ? 147 PHE A CZ  1 
ATOM   1109 N  N   . ASP A 1 148 ? -81.418  27.331 10.118  1.00 68.01  ? 148 ASP A N   1 
ATOM   1110 C  CA  . ASP A 1 148 ? -80.267  28.208 9.931   1.00 66.89  ? 148 ASP A CA  1 
ATOM   1111 C  C   . ASP A 1 148 ? -78.990  27.414 9.709   1.00 70.18  ? 148 ASP A C   1 
ATOM   1112 O  O   . ASP A 1 148 ? -78.073  27.889 9.030   1.00 76.26  ? 148 ASP A O   1 
ATOM   1113 C  CB  . ASP A 1 148 ? -80.103  29.137 11.136  1.00 69.09  ? 148 ASP A CB  1 
ATOM   1114 C  CG  . ASP A 1 148 ? -81.197  30.184 11.224  1.00 79.24  ? 148 ASP A CG  1 
ATOM   1115 O  OD1 . ASP A 1 148 ? -82.053  30.238 10.314  1.00 81.57  ? 148 ASP A OD1 1 
ATOM   1116 O  OD2 . ASP A 1 148 ? -81.198  30.956 12.207  1.00 83.73  ? 148 ASP A OD2 1 
ATOM   1117 N  N   . GLY A 1 149 ? -78.908  26.207 10.273  1.00 70.41  ? 149 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 149 ? -77.729  25.386 10.072  1.00 74.24  ? 149 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 149 ? -77.558  24.940 8.636   1.00 73.19  ? 149 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 149 ? -76.429  24.792 8.160   1.00 76.64  ? 149 GLY A O   1 
ATOM   1121 N  N   . TYR A 1 150 ? -78.668  24.714 7.929   1.00 73.21  ? 150 TYR A N   1 
ATOM   1122 C  CA  . TYR A 1 150 ? -78.585  24.361 6.517   1.00 74.32  ? 150 TYR A CA  1 
ATOM   1123 C  C   . TYR A 1 150 ? -78.081  25.526 5.679   1.00 79.40  ? 150 TYR A C   1 
ATOM   1124 O  O   . TYR A 1 150 ? -77.431  25.311 4.650   1.00 83.87  ? 150 TYR A O   1 
ATOM   1125 C  CB  . TYR A 1 150 ? -79.948  23.889 6.013   1.00 70.79  ? 150 TYR A CB  1 
ATOM   1126 C  CG  . TYR A 1 150 ? -80.228  22.433 6.297   1.00 75.08  ? 150 TYR A CG  1 
ATOM   1127 C  CD1 . TYR A 1 150 ? -80.348  21.970 7.600   1.00 75.08  ? 150 TYR A CD1 1 
ATOM   1128 C  CD2 . TYR A 1 150 ? -80.378  21.519 5.261   1.00 78.53  ? 150 TYR A CD2 1 
ATOM   1129 C  CE1 . TYR A 1 150 ? -80.604  20.640 7.866   1.00 73.72  ? 150 TYR A CE1 1 
ATOM   1130 C  CE2 . TYR A 1 150 ? -80.636  20.184 5.516   1.00 80.67  ? 150 TYR A CE2 1 
ATOM   1131 C  CZ  . TYR A 1 150 ? -80.750  19.750 6.821   1.00 80.78  ? 150 TYR A CZ  1 
ATOM   1132 O  OH  . TYR A 1 150 ? -81.008  18.422 7.082   1.00 79.97  ? 150 TYR A OH  1 
ATOM   1133 N  N   . VAL A 1 151 ? -78.367  26.760 6.098   1.00 80.87  ? 151 VAL A N   1 
ATOM   1134 C  CA  . VAL A 1 151 ? -77.846  27.918 5.381   1.00 76.36  ? 151 VAL A CA  1 
ATOM   1135 C  C   . VAL A 1 151 ? -76.354  28.087 5.646   1.00 75.99  ? 151 VAL A C   1 
ATOM   1136 O  O   . VAL A 1 151 ? -75.607  28.534 4.768   1.00 84.49  ? 151 VAL A O   1 
ATOM   1137 C  CB  . VAL A 1 151 ? -78.650  29.176 5.760   1.00 72.36  ? 151 VAL A CB  1 
ATOM   1138 C  CG1 . VAL A 1 151 ? -78.121  30.396 5.026   1.00 67.51  ? 151 VAL A CG1 1 
ATOM   1139 C  CG2 . VAL A 1 151 ? -80.125  28.968 5.450   1.00 65.76  ? 151 VAL A CG2 1 
ATOM   1140 N  N   . ASP A 1 152 ? -75.890  27.720 6.843   1.00 76.17  ? 152 ASP A N   1 
ATOM   1141 C  CA  . ASP A 1 152 ? -74.460  27.784 7.130   1.00 76.60  ? 152 ASP A CA  1 
ATOM   1142 C  C   . ASP A 1 152 ? -73.690  26.726 6.349   1.00 82.45  ? 152 ASP A C   1 
ATOM   1143 O  O   . ASP A 1 152 ? -72.582  26.987 5.866   1.00 81.91  ? 152 ASP A O   1 
ATOM   1144 C  CB  . ASP A 1 152 ? -74.215  27.621 8.630   1.00 82.04  ? 152 ASP A CB  1 
ATOM   1145 C  CG  . ASP A 1 152 ? -74.818  28.748 9.448   1.00 88.39  ? 152 ASP A CG  1 
ATOM   1146 O  OD1 . ASP A 1 152 ? -74.871  29.891 8.944   1.00 92.71  ? 152 ASP A OD1 1 
ATOM   1147 O  OD2 . ASP A 1 152 ? -75.235  28.490 10.598  1.00 86.93  ? 152 ASP A OD2 1 
ATOM   1148 N  N   . GLU A 1 153 ? -74.257  25.522 6.222   1.00 83.91  ? 153 GLU A N   1 
ATOM   1149 C  CA  . GLU A 1 153 ? -73.596  24.473 5.451   1.00 84.95  ? 153 GLU A CA  1 
ATOM   1150 C  C   . GLU A 1 153 ? -73.500  24.846 3.977   1.00 87.31  ? 153 GLU A C   1 
ATOM   1151 O  O   . GLU A 1 153 ? -72.496  24.548 3.320   1.00 85.51  ? 153 GLU A O   1 
ATOM   1152 C  CB  . GLU A 1 153 ? -74.336  23.146 5.618   1.00 81.08  ? 153 GLU A CB  1 
ATOM   1153 C  CG  . GLU A 1 153 ? -74.144  22.481 6.968   1.00 92.41  ? 153 GLU A CG  1 
ATOM   1154 C  CD  . GLU A 1 153 ? -74.648  21.049 6.987   1.00 101.40 ? 153 GLU A CD  1 
ATOM   1155 O  OE1 . GLU A 1 153 ? -75.515  20.705 6.153   1.00 93.85  ? 153 GLU A OE1 1 
ATOM   1156 O  OE2 . GLU A 1 153 ? -74.169  20.265 7.835   1.00 100.92 ? 153 GLU A OE2 1 
ATOM   1157 N  N   . ALA A 1 154 ? -74.538  25.491 3.439   1.00 83.17  ? 154 ALA A N   1 
ATOM   1158 C  CA  . ALA A 1 154 ? -74.479  25.964 2.061   1.00 88.23  ? 154 ALA A CA  1 
ATOM   1159 C  C   . ALA A 1 154 ? -73.452  27.078 1.897   1.00 91.80  ? 154 ALA A C   1 
ATOM   1160 O  O   . ALA A 1 154 ? -72.805  27.175 0.848   1.00 93.78  ? 154 ALA A O   1 
ATOM   1161 C  CB  . ALA A 1 154 ? -75.861  26.435 1.607   1.00 81.37  ? 154 ALA A CB  1 
ATOM   1162 N  N   . GLU A 1 155 ? -73.288  27.922 2.918   1.00 89.49  ? 155 GLU A N   1 
ATOM   1163 C  CA  . GLU A 1 155 ? -72.251  28.946 2.877   1.00 90.75  ? 155 GLU A CA  1 
ATOM   1164 C  C   . GLU A 1 155 ? -70.859  28.327 2.855   1.00 91.75  ? 155 GLU A C   1 
ATOM   1165 O  O   . GLU A 1 155 ? -69.955  28.860 2.202   1.00 96.79  ? 155 GLU A O   1 
ATOM   1166 C  CB  . GLU A 1 155 ? -72.402  29.890 4.071   1.00 85.26  ? 155 GLU A CB  1 
ATOM   1167 C  CG  . GLU A 1 155 ? -71.400  31.033 4.106   1.00 91.88  ? 155 GLU A CG  1 
ATOM   1168 C  CD  . GLU A 1 155 ? -71.567  31.921 5.326   1.00 83.22  ? 155 GLU A CD  1 
ATOM   1169 N  N   . SER A 1 156 ? -70.671  27.199 3.543   1.00 88.82  ? 156 SER A N   1 
ATOM   1170 C  CA  . SER A 1 156 ? -69.360  26.559 3.569   1.00 94.04  ? 156 SER A CA  1 
ATOM   1171 C  C   . SER A 1 156 ? -69.012  25.949 2.215   1.00 98.45  ? 156 SER A C   1 
ATOM   1172 O  O   . SER A 1 156 ? -67.854  26.005 1.783   1.00 99.52  ? 156 SER A O   1 
ATOM   1173 C  CB  . SER A 1 156 ? -69.318  25.494 4.666   1.00 98.73  ? 156 SER A CB  1 
ATOM   1174 O  OG  . SER A 1 156 ? -68.029  24.913 4.777   1.00 102.33 ? 156 SER A OG  1 
ATOM   1175 N  N   . ARG A 1 157 ? -69.998  25.364 1.530   1.00 94.79  ? 157 ARG A N   1 
ATOM   1176 C  CA  . ARG A 1 157 ? -69.734  24.758 0.228   1.00 95.49  ? 157 ARG A CA  1 
ATOM   1177 C  C   . ARG A 1 157 ? -69.549  25.819 -0.849  1.00 98.06  ? 157 ARG A C   1 
ATOM   1178 O  O   . ARG A 1 157 ? -68.707  25.665 -1.742  1.00 98.19  ? 157 ARG A O   1 
ATOM   1179 C  CB  . ARG A 1 157 ? -70.871  23.807 -0.151  1.00 94.52  ? 157 ARG A CB  1 
ATOM   1180 C  CG  . ARG A 1 157 ? -71.123  22.695 0.854   1.00 100.61 ? 157 ARG A CG  1 
ATOM   1181 C  CD  . ARG A 1 157 ? -72.328  21.852 0.459   1.00 102.43 ? 157 ARG A CD  1 
ATOM   1182 N  NE  . ARG A 1 157 ? -72.736  20.946 1.527   1.00 105.08 ? 157 ARG A NE  1 
ATOM   1183 C  CZ  . ARG A 1 157 ? -73.764  20.111 1.452   1.00 111.97 ? 157 ARG A CZ  1 
ATOM   1184 N  NH1 . ARG A 1 157 ? -74.513  20.033 0.363   1.00 111.14 ? 157 ARG A NH1 1 
ATOM   1185 N  NH2 . ARG A 1 157 ? -74.048  19.335 2.495   1.00 107.11 ? 157 ARG A NH2 1 
ATOM   1186 N  N   . PHE A 1 158 ? -70.326  26.902 -0.778  1.00 99.61  ? 158 PHE A N   1 
ATOM   1187 C  CA  . PHE A 1 158 ? -70.281  27.942 -1.802  1.00 96.41  ? 158 PHE A CA  1 
ATOM   1188 C  C   . PHE A 1 158 ? -68.905  28.594 -1.867  1.00 98.18  ? 158 PHE A C   1 
ATOM   1189 O  O   . PHE A 1 158 ? -68.254  28.599 -2.917  1.00 104.69 ? 158 PHE A O   1 
ATOM   1190 C  CB  . PHE A 1 158 ? -71.364  28.983 -1.518  1.00 100.20 ? 158 PHE A CB  1 
ATOM   1191 C  CG  . PHE A 1 158 ? -71.446  30.083 -2.541  1.00 106.52 ? 158 PHE A CG  1 
ATOM   1192 C  CD1 . PHE A 1 158 ? -72.204  29.924 -3.690  1.00 106.59 ? 158 PHE A CD1 1 
ATOM   1193 C  CD2 . PHE A 1 158 ? -70.786  31.285 -2.342  1.00 108.68 ? 158 PHE A CD2 1 
ATOM   1194 C  CE1 . PHE A 1 158 ? -72.290  30.939 -4.628  1.00 109.62 ? 158 PHE A CE1 1 
ATOM   1195 C  CE2 . PHE A 1 158 ? -70.868  32.303 -3.276  1.00 108.85 ? 158 PHE A CE2 1 
ATOM   1196 C  CZ  . PHE A 1 158 ? -71.621  32.130 -4.419  1.00 107.45 ? 158 PHE A CZ  1 
ATOM   1197 N  N   . TRP A 1 159 ? -68.445  29.150 -0.749  1.00 102.46 ? 159 TRP A N   1 
ATOM   1198 C  CA  . TRP A 1 159 ? -67.150  29.815 -0.699  1.00 102.01 ? 159 TRP A CA  1 
ATOM   1199 C  C   . TRP A 1 159 ? -65.985  28.837 -0.619  1.00 103.50 ? 159 TRP A C   1 
ATOM   1200 O  O   . TRP A 1 159 ? -64.859  29.269 -0.341  1.00 99.52  ? 159 TRP A O   1 
ATOM   1201 C  CB  . TRP A 1 159 ? -67.104  30.786 0.484   1.00 97.85  ? 159 TRP A CB  1 
ATOM   1202 C  CG  . TRP A 1 159 ? -68.281  31.714 0.525   1.00 106.50 ? 159 TRP A CG  1 
ATOM   1203 C  CD1 . TRP A 1 159 ? -69.347  31.648 1.374   1.00 105.65 ? 159 TRP A CD1 1 
ATOM   1204 C  CD2 . TRP A 1 159 ? -68.521  32.838 -0.333  1.00 114.14 ? 159 TRP A CD2 1 
ATOM   1205 N  NE1 . TRP A 1 159 ? -70.233  32.664 1.104   1.00 109.58 ? 159 TRP A NE1 1 
ATOM   1206 C  CE2 . TRP A 1 159 ? -69.749  33.409 0.061   1.00 112.02 ? 159 TRP A CE2 1 
ATOM   1207 C  CE3 . TRP A 1 159 ? -67.815  33.419 -1.392  1.00 110.66 ? 159 TRP A CE3 1 
ATOM   1208 C  CZ2 . TRP A 1 159 ? -70.287  34.533 -0.568  1.00 112.50 ? 159 TRP A CZ2 1 
ATOM   1209 C  CZ3 . TRP A 1 159 ? -68.351  34.535 -2.014  1.00 105.84 ? 159 TRP A CZ3 1 
ATOM   1210 C  CH2 . TRP A 1 159 ? -69.574  35.080 -1.600  1.00 108.86 ? 159 TRP A CH2 1 
ATOM   1211 N  N   . ASN A 1 160 ? -66.237  27.547 -0.860  1.00 106.94 ? 160 ASN A N   1 
ATOM   1212 C  CA  . ASN A 1 160 ? -65.229  26.491 -0.825  1.00 106.95 ? 160 ASN A CA  1 
ATOM   1213 C  C   . ASN A 1 160 ? -64.315  26.622 0.385   1.00 106.45 ? 160 ASN A C   1 
ATOM   1214 O  O   . ASN A 1 160 ? -63.098  26.439 0.278   1.00 109.41 ? 160 ASN A O   1 
ATOM   1215 C  CB  . ASN A 1 160 ? -64.411  26.485 -2.118  1.00 104.41 ? 160 ASN A CB  1 
ATOM   1216 C  CG  . ASN A 1 160 ? -65.177  25.893 -3.285  1.00 115.31 ? 160 ASN A CG  1 
ATOM   1217 O  OD1 . ASN A 1 160 ? -65.322  24.674 -3.393  1.00 113.76 ? 160 ASN A OD1 1 
ATOM   1218 N  ND2 . ASN A 1 160 ? -65.673  26.753 -4.167  1.00 118.90 ? 160 ASN A ND2 1 
ATOM   1219 N  N   . ALA A 1 161 ? -64.897  26.955 1.531   1.00 105.08 ? 161 ALA A N   1 
ATOM   1220 C  CA  . ALA A 1 161 ? -64.171  27.019 2.789   1.00 108.61 ? 161 ALA A CA  1 
ATOM   1221 C  C   . ALA A 1 161 ? -64.526  25.795 3.622   1.00 108.76 ? 161 ALA A C   1 
ATOM   1222 O  O   . ALA A 1 161 ? -65.531  25.806 4.346   1.00 104.67 ? 161 ALA A O   1 
ATOM   1223 C  CB  . ALA A 1 161 ? -64.501  28.307 3.545   1.00 103.15 ? 161 ALA A CB  1 
ATOM   1224 N  N   . PRO A 1 162 ? -63.749  24.719 3.535   1.00 110.82 ? 162 PRO A N   1 
ATOM   1225 C  CA  . PRO A 1 162 ? -64.050  23.536 4.343   1.00 111.09 ? 162 PRO A CA  1 
ATOM   1226 C  C   . PRO A 1 162 ? -63.762  23.795 5.812   1.00 113.29 ? 162 PRO A C   1 
ATOM   1227 O  O   . PRO A 1 162 ? -62.906  24.609 6.169   1.00 110.88 ? 162 PRO A O   1 
ATOM   1228 C  CB  . PRO A 1 162 ? -63.114  22.467 3.769   1.00 108.53 ? 162 PRO A CB  1 
ATOM   1229 C  CG  . PRO A 1 162 ? -61.963  23.243 3.220   1.00 108.10 ? 162 PRO A CG  1 
ATOM   1230 C  CD  . PRO A 1 162 ? -62.539  24.538 2.711   1.00 105.33 ? 162 PRO A CD  1 
ATOM   1231 N  N   . CYS A 1 163 ? -64.508  23.100 6.669   1.00 111.10 ? 163 CYS A N   1 
ATOM   1232 C  CA  . CYS A 1 163 ? -64.271  23.192 8.102   1.00 106.94 ? 163 CYS A CA  1 
ATOM   1233 C  C   . CYS A 1 163 ? -62.873  22.681 8.422   1.00 105.73 ? 163 CYS A C   1 
ATOM   1234 O  O   . CYS A 1 163 ? -62.564  21.506 8.201   1.00 102.36 ? 163 CYS A O   1 
ATOM   1235 C  CB  . CYS A 1 163 ? -65.331  22.400 8.866   1.00 103.63 ? 163 CYS A CB  1 
ATOM   1236 S  SG  . CYS A 1 163 ? -66.999  23.104 8.762   1.00 105.35 ? 163 CYS A SG  1 
ATOM   1237 N  N   . ASP A 1 164 ? -62.022  23.575 8.924   1.00 107.09 ? 164 ASP A N   1 
ATOM   1238 C  CA  . ASP A 1 164 ? -60.616  23.261 9.140   1.00 109.82 ? 164 ASP A CA  1 
ATOM   1239 C  C   . ASP A 1 164 ? -60.353  22.532 10.452  1.00 110.23 ? 164 ASP A C   1 
ATOM   1240 O  O   . ASP A 1 164 ? -59.249  22.008 10.637  1.00 108.38 ? 164 ASP A O   1 
ATOM   1241 C  CB  . ASP A 1 164 ? -59.782  24.545 9.094   1.00 108.96 ? 164 ASP A CB  1 
ATOM   1242 N  N   . SER A 1 165 ? -61.324  22.480 11.360  1.00 108.02 ? 165 SER A N   1 
ATOM   1243 C  CA  . SER A 1 165 ? -61.127  21.828 12.645  1.00 105.33 ? 165 SER A CA  1 
ATOM   1244 C  C   . SER A 1 165 ? -62.400  21.102 13.054  1.00 104.21 ? 165 SER A C   1 
ATOM   1245 O  O   . SER A 1 165 ? -63.499  21.413 12.587  1.00 100.50 ? 165 SER A O   1 
ATOM   1246 C  CB  . SER A 1 165 ? -60.720  22.833 13.732  1.00 105.56 ? 165 SER A CB  1 
ATOM   1247 O  OG  . SER A 1 165 ? -61.737  23.796 13.942  1.00 105.67 ? 165 SER A OG  1 
ATOM   1248 N  N   . ALA A 1 166 ? -62.229  20.114 13.937  1.00 102.86 ? 166 ALA A N   1 
ATOM   1249 C  CA  . ALA A 1 166 ? -63.379  19.437 14.524  1.00 99.39  ? 166 ALA A CA  1 
ATOM   1250 C  C   . ALA A 1 166 ? -64.264  20.422 15.273  1.00 98.37  ? 166 ALA A C   1 
ATOM   1251 O  O   . ALA A 1 166 ? -65.496  20.316 15.235  1.00 95.44  ? 166 ALA A O   1 
ATOM   1252 C  CB  . ALA A 1 166 ? -62.913  18.321 15.458  1.00 89.20  ? 166 ALA A CB  1 
ATOM   1253 N  N   . ALA A 1 167 ? -63.651  21.395 15.951  1.00 95.05  ? 167 ALA A N   1 
ATOM   1254 C  CA  . ALA A 1 167 ? -64.416  22.385 16.701  1.00 93.03  ? 167 ALA A CA  1 
ATOM   1255 C  C   . ALA A 1 167 ? -65.325  23.190 15.782  1.00 96.89  ? 167 ALA A C   1 
ATOM   1256 O  O   . ALA A 1 167 ? -66.512  23.376 16.072  1.00 99.35  ? 167 ALA A O   1 
ATOM   1257 C  CB  . ALA A 1 167 ? -63.466  23.307 17.465  1.00 98.89  ? 167 ALA A CB  1 
ATOM   1258 N  N   . GLN A 1 168 ? -64.783  23.679 14.662  1.00 101.79 ? 168 GLN A N   1 
ATOM   1259 C  CA  . GLN A 1 168 ? -65.598  24.441 13.721  1.00 100.30 ? 168 GLN A CA  1 
ATOM   1260 C  C   . GLN A 1 168 ? -66.678  23.577 13.085  1.00 97.75  ? 168 GLN A C   1 
ATOM   1261 O  O   . GLN A 1 168 ? -67.757  24.080 12.751  1.00 95.38  ? 168 GLN A O   1 
ATOM   1262 C  CB  . GLN A 1 168 ? -64.712  25.068 12.644  1.00 104.01 ? 168 GLN A CB  1 
ATOM   1263 C  CG  . GLN A 1 168 ? -63.786  26.154 13.166  1.00 109.25 ? 168 GLN A CG  1 
ATOM   1264 C  CD  . GLN A 1 168 ? -62.831  26.672 12.109  1.00 113.14 ? 168 GLN A CD  1 
ATOM   1265 O  OE1 . GLN A 1 168 ? -62.994  26.400 10.919  1.00 115.73 ? 168 GLN A OE1 1 
ATOM   1266 N  NE2 . GLN A 1 168 ? -61.822  27.422 12.540  1.00 112.09 ? 168 GLN A NE2 1 
ATOM   1267 N  N   . TYR A 1 169 ? -66.411  22.281 12.914  1.00 99.56  ? 169 TYR A N   1 
ATOM   1268 C  CA  . TYR A 1 169 ? -67.420  21.381 12.366  1.00 97.00  ? 169 TYR A CA  1 
ATOM   1269 C  C   . TYR A 1 169 ? -68.569  21.183 13.348  1.00 92.44  ? 169 TYR A C   1 
ATOM   1270 O  O   . TYR A 1 169 ? -69.742  21.342 12.988  1.00 86.15  ? 169 TYR A O   1 
ATOM   1271 C  CB  . TYR A 1 169 ? -66.777  20.042 12.007  1.00 88.82  ? 169 TYR A CB  1 
ATOM   1272 C  CG  . TYR A 1 169 ? -67.737  19.018 11.447  1.00 88.83  ? 169 TYR A CG  1 
ATOM   1273 C  CD1 . TYR A 1 169 ? -68.549  19.319 10.361  1.00 91.35  ? 169 TYR A CD1 1 
ATOM   1274 C  CD2 . TYR A 1 169 ? -67.813  17.740 11.987  1.00 90.79  ? 169 TYR A CD2 1 
ATOM   1275 C  CE1 . TYR A 1 169 ? -69.421  18.383 9.840   1.00 90.01  ? 169 TYR A CE1 1 
ATOM   1276 C  CE2 . TYR A 1 169 ? -68.682  16.797 11.472  1.00 91.54  ? 169 TYR A CE2 1 
ATOM   1277 C  CZ  . TYR A 1 169 ? -69.483  17.124 10.398  1.00 87.76  ? 169 TYR A CZ  1 
ATOM   1278 O  OH  . TYR A 1 169 ? -70.349  16.189 9.880   1.00 83.20  ? 169 TYR A OH  1 
ATOM   1279 N  N   . LEU A 1 170 ? -68.246  20.840 14.599  1.00 87.00  ? 170 LEU A N   1 
ATOM   1280 C  CA  . LEU A 1 170 ? -69.281  20.565 15.591  1.00 89.43  ? 170 LEU A CA  1 
ATOM   1281 C  C   . LEU A 1 170 ? -70.179  21.775 15.814  1.00 91.03  ? 170 LEU A C   1 
ATOM   1282 O  O   . LEU A 1 170 ? -71.400  21.632 15.952  1.00 83.20  ? 170 LEU A O   1 
ATOM   1283 C  CB  . LEU A 1 170 ? -68.638  20.122 16.905  1.00 86.08  ? 170 LEU A CB  1 
ATOM   1284 C  CG  . LEU A 1 170 ? -67.938  18.764 16.857  1.00 90.98  ? 170 LEU A CG  1 
ATOM   1285 C  CD1 . LEU A 1 170 ? -67.263  18.456 18.184  1.00 84.56  ? 170 LEU A CD1 1 
ATOM   1286 C  CD2 . LEU A 1 170 ? -68.931  17.674 16.486  1.00 86.59  ? 170 LEU A CD2 1 
ATOM   1287 N  N   . ALA A 1 171 ? -69.598  22.978 15.842  1.00 92.38  ? 171 ALA A N   1 
ATOM   1288 C  CA  . ALA A 1 171 ? -70.401  24.187 15.993  1.00 88.78  ? 171 ALA A CA  1 
ATOM   1289 C  C   . ALA A 1 171 ? -71.430  24.336 14.881  1.00 90.80  ? 171 ALA A C   1 
ATOM   1290 O  O   . ALA A 1 171 ? -72.431  25.038 15.064  1.00 86.24  ? 171 ALA A O   1 
ATOM   1291 C  CB  . ALA A 1 171 ? -69.495  25.418 16.038  1.00 89.22  ? 171 ALA A CB  1 
ATOM   1292 N  N   . MET A 1 172 ? -71.209  23.691 13.737  1.00 90.76  ? 172 MET A N   1 
ATOM   1293 C  CA  . MET A 1 172 ? -72.159  23.685 12.634  1.00 86.83  ? 172 MET A CA  1 
ATOM   1294 C  C   . MET A 1 172 ? -72.977  22.402 12.568  1.00 89.16  ? 172 MET A C   1 
ATOM   1295 O  O   . MET A 1 172 ? -74.190  22.458 12.332  1.00 84.32  ? 172 MET A O   1 
ATOM   1296 C  CB  . MET A 1 172 ? -71.420  23.888 11.308  1.00 90.74  ? 172 MET A CB  1 
ATOM   1297 C  CG  . MET A 1 172 ? -72.319  23.995 10.086  1.00 89.15  ? 172 MET A CG  1 
ATOM   1298 S  SD  . MET A 1 172 ? -71.363  24.130 8.562   1.00 100.75 ? 172 MET A SD  1 
ATOM   1299 C  CE  . MET A 1 172 ? -70.351  25.564 8.923   1.00 95.36  ? 172 MET A CE  1 
ATOM   1300 N  N   . ARG A 1 173 ? -72.344  21.246 12.789  1.00 83.70  ? 173 ARG A N   1 
ATOM   1301 C  CA  . ARG A 1 173 ? -73.047  19.977 12.631  1.00 82.29  ? 173 ARG A CA  1 
ATOM   1302 C  C   . ARG A 1 173 ? -74.035  19.727 13.762  1.00 80.66  ? 173 ARG A C   1 
ATOM   1303 O  O   . ARG A 1 173 ? -75.040  19.034 13.559  1.00 75.74  ? 173 ARG A O   1 
ATOM   1304 C  CB  . ARG A 1 173 ? -72.049  18.823 12.546  1.00 82.49  ? 173 ARG A CB  1 
ATOM   1305 C  CG  . ARG A 1 173 ? -72.666  17.545 12.015  1.00 82.86  ? 173 ARG A CG  1 
ATOM   1306 C  CD  . ARG A 1 173 ? -73.029  17.705 10.548  1.00 84.42  ? 173 ARG A CD  1 
ATOM   1307 N  NE  . ARG A 1 173 ? -74.172  16.891 10.152  1.00 87.66  ? 173 ARG A NE  1 
ATOM   1308 C  CZ  . ARG A 1 173 ? -74.141  15.576 9.986   1.00 95.61  ? 173 ARG A CZ  1 
ATOM   1309 N  NH1 . ARG A 1 173 ? -73.046  14.872 10.225  1.00 94.64  ? 173 ARG A NH1 1 
ATOM   1310 N  NH2 . ARG A 1 173 ? -75.239  14.950 9.574   1.00 92.63  ? 173 ARG A NH2 1 
ATOM   1311 N  N   . ARG A 1 174 ? -73.772  20.273 14.953  1.00 77.52  ? 174 ARG A N   1 
ATOM   1312 C  CA  . ARG A 1 174 ? -74.674  20.070 16.082  1.00 75.41  ? 174 ARG A CA  1 
ATOM   1313 C  C   . ARG A 1 174 ? -76.071  20.608 15.811  1.00 73.79  ? 174 ARG A C   1 
ATOM   1314 O  O   . ARG A 1 174 ? -77.031  20.144 16.435  1.00 69.86  ? 174 ARG A O   1 
ATOM   1315 C  CB  . ARG A 1 174 ? -74.100  20.718 17.342  1.00 76.84  ? 174 ARG A CB  1 
ATOM   1316 C  CG  . ARG A 1 174 ? -73.015  19.892 18.008  1.00 80.08  ? 174 ARG A CG  1 
ATOM   1317 C  CD  . ARG A 1 174 ? -72.175  20.726 18.956  1.00 78.92  ? 174 ARG A CD  1 
ATOM   1318 N  NE  . ARG A 1 174 ? -71.299  19.888 19.766  1.00 90.02  ? 174 ARG A NE  1 
ATOM   1319 C  CZ  . ARG A 1 174 ? -70.391  20.350 20.615  1.00 88.96  ? 174 ARG A CZ  1 
ATOM   1320 N  NH1 . ARG A 1 174 ? -70.195  21.649 20.777  1.00 88.92  ? 174 ARG A NH1 1 
ATOM   1321 N  NH2 . ARG A 1 174 ? -69.662  19.487 21.317  1.00 86.95  ? 174 ARG A NH2 1 
ATOM   1322 N  N   . HIS A 1 175 ? -76.210  21.562 14.891  1.00 77.42  ? 175 HIS A N   1 
ATOM   1323 C  CA  . HIS A 1 175 ? -77.523  22.084 14.534  1.00 78.29  ? 175 HIS A CA  1 
ATOM   1324 C  C   . HIS A 1 175 ? -78.150  21.334 13.366  1.00 74.09  ? 175 HIS A C   1 
ATOM   1325 O  O   . HIS A 1 175 ? -79.357  21.066 13.383  1.00 75.59  ? 175 HIS A O   1 
ATOM   1326 C  CB  . HIS A 1 175 ? -77.425  23.577 14.204  1.00 75.80  ? 175 HIS A CB  1 
ATOM   1327 C  CG  . HIS A 1 175 ? -77.039  24.426 15.375  1.00 83.10  ? 175 HIS A CG  1 
ATOM   1328 N  ND1 . HIS A 1 175 ? -77.896  24.677 16.426  1.00 83.54  ? 175 HIS A ND1 1 
ATOM   1329 C  CD2 . HIS A 1 175 ? -75.887  25.077 15.665  1.00 83.54  ? 175 HIS A CD2 1 
ATOM   1330 C  CE1 . HIS A 1 175 ? -77.289  25.447 17.312  1.00 80.11  ? 175 HIS A CE1 1 
ATOM   1331 N  NE2 . HIS A 1 175 ? -76.069  25.704 16.874  1.00 82.43  ? 175 HIS A NE2 1 
ATOM   1332 N  N   . THR A 1 176 ? -77.361  20.979 12.352  1.00 75.53  ? 176 THR A N   1 
ATOM   1333 C  CA  . THR A 1 176 ? -77.923  20.329 11.174  1.00 80.53  ? 176 THR A CA  1 
ATOM   1334 C  C   . THR A 1 176 ? -78.238  18.858 11.394  1.00 79.49  ? 176 THR A C   1 
ATOM   1335 O  O   . THR A 1 176 ? -78.943  18.272 10.568  1.00 71.41  ? 176 THR A O   1 
ATOM   1336 C  CB  . THR A 1 176 ? -76.978  20.461 9.977   1.00 75.96  ? 176 THR A CB  1 
ATOM   1337 O  OG1 . THR A 1 176 ? -75.809  19.663 10.194  1.00 81.01  ? 176 THR A OG1 1 
ATOM   1338 C  CG2 . THR A 1 176 ? -76.569  21.906 9.783   1.00 80.92  ? 176 THR A CG2 1 
ATOM   1339 N  N   . ILE A 1 177 ? -77.739  18.250 12.476  1.00 74.24  ? 177 ILE A N   1 
ATOM   1340 C  CA  . ILE A 1 177 ? -78.015  16.840 12.731  1.00 75.41  ? 177 ILE A CA  1 
ATOM   1341 C  C   . ILE A 1 177 ? -79.472  16.615 13.122  1.00 75.52  ? 177 ILE A C   1 
ATOM   1342 O  O   . ILE A 1 177 ? -79.983  15.498 12.978  1.00 82.76  ? 177 ILE A O   1 
ATOM   1343 C  CB  . ILE A 1 177 ? -77.060  16.296 13.812  1.00 84.11  ? 177 ILE A CB  1 
ATOM   1344 C  CG1 . ILE A 1 177 ? -77.035  14.764 13.802  1.00 81.10  ? 177 ILE A CG1 1 
ATOM   1345 C  CG2 . ILE A 1 177 ? -77.450  16.816 15.190  1.00 79.56  ? 177 ILE A CG2 1 
ATOM   1346 C  CD1 . ILE A 1 177 ? -76.430  14.168 12.554  1.00 82.81  ? 177 ILE A CD1 1 
ATOM   1347 N  N   . GLY A 1 178 ? -80.159  17.649 13.605  1.00 70.91  ? 178 GLY A N   1 
ATOM   1348 C  CA  . GLY A 1 178 ? -81.571  17.536 13.917  1.00 72.81  ? 178 GLY A CA  1 
ATOM   1349 C  C   . GLY A 1 178 ? -81.911  16.655 15.098  1.00 72.14  ? 178 GLY A C   1 
ATOM   1350 O  O   . GLY A 1 178 ? -83.025  16.128 15.161  1.00 66.23  ? 178 GLY A O   1 
ATOM   1351 N  N   . VAL A 1 179 ? -80.988  16.483 16.046  1.00 66.04  ? 179 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 179 ? -81.269  15.626 17.194  1.00 70.42  ? 179 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 179 ? -82.228  16.312 18.159  1.00 70.79  ? 179 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 179 ? -83.173  15.690 18.660  1.00 65.71  ? 179 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 179 ? -79.960  15.212 17.890  1.00 71.85  ? 179 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 179 ? -80.247  14.649 19.274  1.00 70.86  ? 179 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 179 ? -79.226  14.185 17.051  1.00 68.65  ? 179 VAL A CG2 1 
ATOM   1358 N  N   . GLN A 1 180 ? -82.013  17.599 18.433  1.00 65.37  ? 180 GLN A N   1 
ATOM   1359 C  CA  . GLN A 1 180 ? -82.866  18.285 19.400  1.00 67.23  ? 180 GLN A CA  1 
ATOM   1360 C  C   . GLN A 1 180 ? -84.330  18.338 18.977  1.00 64.84  ? 180 GLN A C   1 
ATOM   1361 O  O   . GLN A 1 180 ? -85.196  18.100 19.839  1.00 65.08  ? 180 GLN A O   1 
ATOM   1362 C  CB  . GLN A 1 180 ? -82.324  19.693 19.680  1.00 67.80  ? 180 GLN A CB  1 
ATOM   1363 C  CG  . GLN A 1 180 ? -83.091  20.419 20.770  1.00 60.54  ? 180 GLN A CG  1 
ATOM   1364 C  CD  . GLN A 1 180 ? -83.110  19.645 22.074  1.00 69.84  ? 180 GLN A CD  1 
ATOM   1365 O  OE1 . GLN A 1 180 ? -82.060  19.327 22.633  1.00 65.48  ? 180 GLN A OE1 1 
ATOM   1366 N  NE2 . GLN A 1 180 ? -84.305  19.326 22.559  1.00 68.56  ? 180 GLN A NE2 1 
ATOM   1367 N  N   . PRO A 1 181 ? -84.687  18.639 17.724  1.00 65.07  ? 181 PRO A N   1 
ATOM   1368 C  CA  . PRO A 1 181 ? -86.099  18.498 17.334  1.00 64.25  ? 181 PRO A CA  1 
ATOM   1369 C  C   . PRO A 1 181 ? -86.619  17.079 17.476  1.00 63.33  ? 181 PRO A C   1 
ATOM   1370 O  O   . PRO A 1 181 ? -87.813  16.890 17.747  1.00 57.38  ? 181 PRO A O   1 
ATOM   1371 C  CB  . PRO A 1 181 ? -86.103  18.963 15.872  1.00 59.19  ? 181 PRO A CB  1 
ATOM   1372 C  CG  . PRO A 1 181 ? -84.963  19.913 15.794  1.00 59.28  ? 181 PRO A CG  1 
ATOM   1373 C  CD  . PRO A 1 181 ? -83.904  19.319 16.673  1.00 59.20  ? 181 PRO A CD  1 
ATOM   1374 N  N   . THR A 1 182 ? -85.755  16.076 17.299  1.00 65.93  ? 182 THR A N   1 
ATOM   1375 C  CA  . THR A 1 182 ? -86.162  14.687 17.493  1.00 66.10  ? 182 THR A CA  1 
ATOM   1376 C  C   . THR A 1 182 ? -86.457  14.405 18.960  1.00 63.57  ? 182 THR A C   1 
ATOM   1377 O  O   . THR A 1 182 ? -87.479  13.792 19.292  1.00 65.78  ? 182 THR A O   1 
ATOM   1378 C  CB  . THR A 1 182 ? -85.072  13.744 16.984  1.00 68.66  ? 182 THR A CB  1 
ATOM   1379 O  OG1 . THR A 1 182 ? -84.796  14.028 15.608  1.00 59.14  ? 182 THR A OG1 1 
ATOM   1380 C  CG2 . THR A 1 182 ? -85.508  12.292 17.132  1.00 63.98  ? 182 THR A CG2 1 
ATOM   1381 N  N   . VAL A 1 183 ? -85.564  14.838 19.853  1.00 59.48  ? 183 VAL A N   1 
ATOM   1382 C  CA  . VAL A 1 183 ? -85.792  14.670 21.285  1.00 61.19  ? 183 VAL A CA  1 
ATOM   1383 C  C   . VAL A 1 183 ? -87.051  15.410 21.713  1.00 60.63  ? 183 VAL A C   1 
ATOM   1384 O  O   . VAL A 1 183 ? -87.822  14.921 22.548  1.00 62.67  ? 183 VAL A O   1 
ATOM   1385 C  CB  . VAL A 1 183 ? -84.560  15.141 22.079  1.00 60.80  ? 183 VAL A CB  1 
ATOM   1386 C  CG1 . VAL A 1 183 ? -84.799  14.995 23.575  1.00 53.61  ? 183 VAL A CG1 1 
ATOM   1387 C  CG2 . VAL A 1 183 ? -83.326  14.360 21.650  1.00 59.21  ? 183 VAL A CG2 1 
ATOM   1388 N  N   . ASP A 1 184 ? -87.287  16.596 21.141  1.00 59.19  ? 184 ASP A N   1 
ATOM   1389 C  CA  . ASP A 1 184 ? -88.471  17.369 21.505  1.00 61.32  ? 184 ASP A CA  1 
ATOM   1390 C  C   . ASP A 1 184 ? -89.746  16.587 21.225  1.00 61.10  ? 184 ASP A C   1 
ATOM   1391 O  O   . ASP A 1 184 ? -90.716  16.673 21.987  1.00 62.54  ? 184 ASP A O   1 
ATOM   1392 C  CB  . ASP A 1 184 ? -88.487  18.703 20.757  1.00 54.46  ? 184 ASP A CB  1 
ATOM   1393 C  CG  . ASP A 1 184 ? -87.405  19.655 21.233  1.00 66.96  ? 184 ASP A CG  1 
ATOM   1394 O  OD1 . ASP A 1 184 ? -86.966  19.529 22.398  1.00 74.00  ? 184 ASP A OD1 1 
ATOM   1395 O  OD2 . ASP A 1 184 ? -86.997  20.534 20.442  1.00 66.44  ? 184 ASP A OD2 1 
ATOM   1396 N  N   . LEU A 1 185 ? -89.759  15.804 20.147  1.00 59.87  ? 185 LEU A N   1 
ATOM   1397 C  CA  . LEU A 1 185 ? -90.955  15.045 19.813  1.00 66.06  ? 185 LEU A CA  1 
ATOM   1398 C  C   . LEU A 1 185 ? -91.158  13.841 20.724  1.00 61.02  ? 185 LEU A C   1 
ATOM   1399 O  O   . LEU A 1 185 ? -92.292  13.366 20.854  1.00 59.32  ? 185 LEU A O   1 
ATOM   1400 C  CB  . LEU A 1 185 ? -90.911  14.601 18.349  1.00 61.57  ? 185 LEU A CB  1 
ATOM   1401 C  CG  . LEU A 1 185 ? -92.300  14.258 17.811  1.00 57.40  ? 185 LEU A CG  1 
ATOM   1402 C  CD1 . LEU A 1 185 ? -92.618  15.044 16.554  1.00 66.75  ? 185 LEU A CD1 1 
ATOM   1403 C  CD2 . LEU A 1 185 ? -92.420  12.770 17.570  1.00 61.92  ? 185 LEU A CD2 1 
ATOM   1404 N  N   . ALA A 1 186 ? -90.096  13.346 21.366  1.00 59.20  ? 186 ALA A N   1 
ATOM   1405 C  CA  . ALA A 1 186 ? -90.270  12.286 22.355  1.00 63.57  ? 186 ALA A CA  1 
ATOM   1406 C  C   . ALA A 1 186 ? -91.109  12.770 23.532  1.00 64.17  ? 186 ALA A C   1 
ATOM   1407 O  O   . ALA A 1 186 ? -91.902  12.007 24.095  1.00 64.93  ? 186 ALA A O   1 
ATOM   1408 C  CB  . ALA A 1 186 ? -88.912  11.777 22.835  1.00 57.29  ? 186 ALA A CB  1 
ATOM   1409 N  N   . GLU A 1 187 ? -90.947  14.039 23.916  1.00 62.29  ? 187 GLU A N   1 
ATOM   1410 C  CA  . GLU A 1 187 ? -91.815  14.626 24.933  1.00 61.85  ? 187 GLU A CA  1 
ATOM   1411 C  C   . GLU A 1 187 ? -93.255  14.705 24.441  1.00 64.68  ? 187 GLU A C   1 
ATOM   1412 O  O   . GLU A 1 187 ? -94.193  14.350 25.165  1.00 66.27  ? 187 GLU A O   1 
ATOM   1413 C  CB  . GLU A 1 187 ? -91.308  16.016 25.316  1.00 61.88  ? 187 GLU A CB  1 
ATOM   1414 C  CG  . GLU A 1 187 ? -89.952  16.040 26.000  1.00 65.20  ? 187 GLU A CG  1 
ATOM   1415 C  CD  . GLU A 1 187 ? -89.446  17.456 26.215  1.00 71.03  ? 187 GLU A CD  1 
ATOM   1416 O  OE1 . GLU A 1 187 ? -88.793  18.007 25.301  1.00 75.92  ? 187 GLU A OE1 1 
ATOM   1417 O  OE2 . GLU A 1 187 ? -89.717  18.024 27.295  1.00 71.70  ? 187 GLU A OE2 1 
ATOM   1418 N  N   . ARG A 1 188 ? -93.449  15.177 23.209  1.00 63.54  ? 188 ARG A N   1 
ATOM   1419 C  CA  . ARG A 1 188 ? -94.794  15.290 22.657  1.00 62.14  ? 188 ARG A CA  1 
ATOM   1420 C  C   . ARG A 1 188 ? -95.431  13.918 22.466  1.00 68.36  ? 188 ARG A C   1 
ATOM   1421 O  O   . ARG A 1 188 ? -96.612  13.728 22.779  1.00 69.37  ? 188 ARG A O   1 
ATOM   1422 C  CB  . ARG A 1 188 ? -94.743  16.063 21.338  1.00 63.42  ? 188 ARG A CB  1 
ATOM   1423 C  CG  . ARG A 1 188 ? -95.968  15.908 20.454  1.00 64.63  ? 188 ARG A CG  1 
ATOM   1424 C  CD  . ARG A 1 188 ? -97.233  16.417 21.123  1.00 62.59  ? 188 ARG A CD  1 
ATOM   1425 N  NE  . ARG A 1 188 ? -98.387  16.252 20.250  1.00 66.03  ? 188 ARG A NE  1 
ATOM   1426 C  CZ  . ARG A 1 188 ? -99.060  15.119 20.105  1.00 73.35  ? 188 ARG A CZ  1 
ATOM   1427 N  NH1 . ARG A 1 188 ? -98.739  14.033 20.789  1.00 71.91  ? 188 ARG A NH1 1 
ATOM   1428 N  NH2 . ARG A 1 188 ? -100.077 15.072 19.249  1.00 73.68  ? 188 ARG A NH2 1 
ATOM   1429 N  N   . ALA A 1 189 ? -94.665  12.948 21.960  1.00 66.64  ? 189 ALA A N   1 
ATOM   1430 C  CA  . ALA A 1 189 ? -95.214  11.609 21.770  1.00 67.98  ? 189 ALA A CA  1 
ATOM   1431 C  C   . ALA A 1 189 ? -95.452  10.906 23.100  1.00 67.38  ? 189 ALA A C   1 
ATOM   1432 O  O   . ALA A 1 189 ? -96.340  10.051 23.198  1.00 73.28  ? 189 ALA A O   1 
ATOM   1433 C  CB  . ALA A 1 189 ? -94.285  10.779 20.884  1.00 63.14  ? 189 ALA A CB  1 
ATOM   1434 N  N   . GLY A 1 190 ? -94.678  11.245 24.128  1.00 66.79  ? 190 GLY A N   1 
ATOM   1435 C  CA  . GLY A 1 190 ? -94.916  10.703 25.451  1.00 64.39  ? 190 GLY A CA  1 
ATOM   1436 C  C   . GLY A 1 190 ? -95.952  11.442 26.266  1.00 65.29  ? 190 GLY A C   1 
ATOM   1437 O  O   . GLY A 1 190 ? -96.377  10.930 27.306  1.00 68.03  ? 190 GLY A O   1 
ATOM   1438 N  N   . ARG A 1 191 ? -96.369  12.626 25.810  1.00 68.03  ? 191 ARG A N   1 
ATOM   1439 C  CA  . ARG A 1 191 ? -97.345  13.464 26.514  1.00 70.20  ? 191 ARG A CA  1 
ATOM   1440 C  C   . ARG A 1 191 ? -96.831  13.867 27.896  1.00 68.00  ? 191 ARG A C   1 
ATOM   1441 O  O   . ARG A 1 191 ? -97.556  13.826 28.893  1.00 63.10  ? 191 ARG A O   1 
ATOM   1442 C  CB  . ARG A 1 191 ? -98.710  12.775 26.601  1.00 61.04  ? 191 ARG A CB  1 
ATOM   1443 C  CG  . ARG A 1 191 ? -99.162  12.194 25.269  1.00 72.71  ? 191 ARG A CG  1 
ATOM   1444 C  CD  . ARG A 1 191 ? -100.673 12.187 25.114  1.00 76.86  ? 191 ARG A CD  1 
ATOM   1445 N  NE  . ARG A 1 191 ? -101.056 11.837 23.752  1.00 77.21  ? 191 ARG A NE  1 
ATOM   1446 C  CZ  . ARG A 1 191 ? -102.245 12.078 23.216  1.00 82.59  ? 191 ARG A CZ  1 
ATOM   1447 N  NH1 . ARG A 1 191 ? -103.210 12.663 23.908  1.00 81.03  ? 191 ARG A NH1 1 
ATOM   1448 N  NH2 . ARG A 1 191 ? -102.469 11.735 21.950  1.00 83.99  ? 191 ARG A NH2 1 
ATOM   1449 N  N   . PHE A 1 192 ? -95.561  14.265 27.948  1.00 66.04  ? 192 PHE A N   1 
ATOM   1450 C  CA  . PHE A 1 192 ? -94.939  14.787 29.151  1.00 66.53  ? 192 PHE A CA  1 
ATOM   1451 C  C   . PHE A 1 192 ? -93.957  15.875 28.746  1.00 65.08  ? 192 PHE A C   1 
ATOM   1452 O  O   . PHE A 1 192 ? -93.611  16.023 27.573  1.00 70.23  ? 192 PHE A O   1 
ATOM   1453 C  CB  . PHE A 1 192 ? -94.225  13.686 29.948  1.00 70.88  ? 192 PHE A CB  1 
ATOM   1454 C  CG  . PHE A 1 192 ? -92.954  13.197 29.307  1.00 65.41  ? 192 PHE A CG  1 
ATOM   1455 C  CD1 . PHE A 1 192 ? -92.982  12.173 28.377  1.00 65.75  ? 192 PHE A CD1 1 
ATOM   1456 C  CD2 . PHE A 1 192 ? -91.729  13.757 29.641  1.00 68.77  ? 192 PHE A CD2 1 
ATOM   1457 C  CE1 . PHE A 1 192 ? -91.814  11.721 27.786  1.00 65.79  ? 192 PHE A CE1 1 
ATOM   1458 C  CE2 . PHE A 1 192 ? -90.558  13.312 29.052  1.00 68.41  ? 192 PHE A CE2 1 
ATOM   1459 C  CZ  . PHE A 1 192 ? -90.601  12.292 28.125  1.00 63.74  ? 192 PHE A CZ  1 
ATOM   1460 N  N   . GLU A 1 193 ? -93.501  16.638 29.735  1.00 71.37  ? 193 GLU A N   1 
ATOM   1461 C  CA  . GLU A 1 193 ? -92.497  17.673 29.528  1.00 66.25  ? 193 GLU A CA  1 
ATOM   1462 C  C   . GLU A 1 193 ? -91.477  17.598 30.654  1.00 72.73  ? 193 GLU A C   1 
ATOM   1463 O  O   . GLU A 1 193 ? -91.852  17.503 31.827  1.00 71.11  ? 193 GLU A O   1 
ATOM   1464 C  CB  . GLU A 1 193 ? -93.128  19.071 29.482  1.00 65.37  ? 193 GLU A CB  1 
ATOM   1465 C  CG  . GLU A 1 193 ? -94.340  19.189 28.573  1.00 67.45  ? 193 GLU A CG  1 
ATOM   1466 C  CD  . GLU A 1 193 ? -94.801  20.622 28.387  1.00 70.09  ? 193 GLU A CD  1 
ATOM   1467 O  OE1 . GLU A 1 193 ? -94.022  21.552 28.693  1.00 64.51  ? 193 GLU A OE1 1 
ATOM   1468 O  OE2 . GLU A 1 193 ? -95.948  20.816 27.928  1.00 71.52  ? 193 GLU A OE2 1 
ATOM   1469 N  N   . VAL A 1 194 ? -90.200  17.627 30.298  1.00 71.82  ? 194 VAL A N   1 
ATOM   1470 C  CA  . VAL A 1 194 ? -89.153  17.731 31.321  1.00 66.70  ? 194 VAL A CA  1 
ATOM   1471 C  C   . VAL A 1 194 ? -89.293  19.075 32.028  1.00 67.31  ? 194 VAL A C   1 
ATOM   1472 O  O   . VAL A 1 194 ? -89.670  20.069 31.380  1.00 71.84  ? 194 VAL A O   1 
ATOM   1473 C  CB  . VAL A 1 194 ? -87.767  17.575 30.684  1.00 69.23  ? 194 VAL A CB  1 
ATOM   1474 C  CG1 . VAL A 1 194 ? -87.495  18.696 29.679  1.00 63.77  ? 194 VAL A CG1 1 
ATOM   1475 C  CG2 . VAL A 1 194 ? -86.670  17.508 31.747  1.00 63.65  ? 194 VAL A CG2 1 
ATOM   1476 N  N   . PRO A 1 195 ? -89.072  19.150 33.351  1.00 73.33  ? 195 PRO A N   1 
ATOM   1477 C  CA  . PRO A 1 195 ? -89.087  20.456 34.026  1.00 69.47  ? 195 PRO A CA  1 
ATOM   1478 C  C   . PRO A 1 195 ? -88.234  21.473 33.288  1.00 66.88  ? 195 PRO A C   1 
ATOM   1479 O  O   . PRO A 1 195 ? -87.046  21.242 33.044  1.00 69.54  ? 195 PRO A O   1 
ATOM   1480 C  CB  . PRO A 1 195 ? -88.528  20.133 35.416  1.00 68.36  ? 195 PRO A CB  1 
ATOM   1481 C  CG  . PRO A 1 195 ? -88.977  18.732 35.657  1.00 71.55  ? 195 PRO A CG  1 
ATOM   1482 C  CD  . PRO A 1 195 ? -88.961  18.038 34.313  1.00 70.82  ? 195 PRO A CD  1 
ATOM   1483 N  N   . HIS A 1 196 ? -88.850  22.595 32.911  1.00 67.19  ? 196 HIS A N   1 
ATOM   1484 C  CA  . HIS A 1 196 ? -88.204  23.523 31.989  1.00 60.21  ? 196 HIS A CA  1 
ATOM   1485 C  C   . HIS A 1 196 ? -86.929  24.108 32.580  1.00 62.78  ? 196 HIS A C   1 
ATOM   1486 O  O   . HIS A 1 196 ? -85.954  24.341 31.856  1.00 63.32  ? 196 HIS A O   1 
ATOM   1487 C  CB  . HIS A 1 196 ? -89.182  24.628 31.594  1.00 57.09  ? 196 HIS A CB  1 
ATOM   1488 C  CG  . HIS A 1 196 ? -90.334  24.143 30.769  1.00 68.03  ? 196 HIS A CG  1 
ATOM   1489 N  ND1 . HIS A 1 196 ? -91.241  24.997 30.179  1.00 67.61  ? 196 HIS A ND1 1 
ATOM   1490 C  CD2 . HIS A 1 196 ? -90.725  22.890 30.434  1.00 68.59  ? 196 HIS A CD2 1 
ATOM   1491 C  CE1 . HIS A 1 196 ? -92.142  24.292 29.519  1.00 67.29  ? 196 HIS A CE1 1 
ATOM   1492 N  NE2 . HIS A 1 196 ? -91.852  23.011 29.658  1.00 70.78  ? 196 HIS A NE2 1 
ATOM   1493 N  N   . ARG A 1 197 ? -86.906  24.346 33.893  1.00 71.63  ? 197 ARG A N   1 
ATOM   1494 C  CA  . ARG A 1 197 ? -85.680  24.832 34.514  1.00 63.94  ? 197 ARG A CA  1 
ATOM   1495 C  C   . ARG A 1 197 ? -84.597  23.760 34.551  1.00 66.17  ? 197 ARG A C   1 
ATOM   1496 O  O   . ARG A 1 197 ? -83.410  24.098 34.607  1.00 66.28  ? 197 ARG A O   1 
ATOM   1497 C  CB  . ARG A 1 197 ? -85.968  25.358 35.921  1.00 67.04  ? 197 ARG A CB  1 
ATOM   1498 C  CG  . ARG A 1 197 ? -86.523  24.336 36.902  1.00 67.15  ? 197 ARG A CG  1 
ATOM   1499 C  CD  . ARG A 1 197 ? -87.054  25.037 38.151  1.00 63.39  ? 197 ARG A CD  1 
ATOM   1500 N  NE  . ARG A 1 197 ? -87.403  24.108 39.219  1.00 72.18  ? 197 ARG A NE  1 
ATOM   1501 C  CZ  . ARG A 1 197 ? -88.568  23.482 39.322  1.00 69.25  ? 197 ARG A CZ  1 
ATOM   1502 N  NH1 . ARG A 1 197 ? -89.523  23.645 38.421  1.00 64.76  ? 197 ARG A NH1 1 
ATOM   1503 N  NH2 . ARG A 1 197 ? -88.780  22.671 40.353  1.00 68.11  ? 197 ARG A NH2 1 
ATOM   1504 N  N   . VAL A 1 198 ? -84.977  22.482 34.502  1.00 64.52  ? 198 VAL A N   1 
ATOM   1505 C  CA  . VAL A 1 198 ? -83.981  21.417 34.456  1.00 66.79  ? 198 VAL A CA  1 
ATOM   1506 C  C   . VAL A 1 198 ? -83.451  21.226 33.038  1.00 70.51  ? 198 VAL A C   1 
ATOM   1507 O  O   . VAL A 1 198 ? -82.272  20.900 32.854  1.00 68.52  ? 198 VAL A O   1 
ATOM   1508 C  CB  . VAL A 1 198 ? -84.568  20.112 35.023  1.00 66.74  ? 198 VAL A CB  1 
ATOM   1509 C  CG1 . VAL A 1 198 ? -83.542  18.993 34.972  1.00 66.57  ? 198 VAL A CG1 1 
ATOM   1510 C  CG2 . VAL A 1 198 ? -85.033  20.325 36.446  1.00 71.22  ? 198 VAL A CG2 1 
ATOM   1511 N  N   . PHE A 1 199 ? -84.298  21.420 32.020  1.00 65.11  ? 199 PHE A N   1 
ATOM   1512 C  CA  . PHE A 1 199 ? -83.819  21.383 30.640  1.00 63.63  ? 199 PHE A CA  1 
ATOM   1513 C  C   . PHE A 1 199 ? -82.688  22.382 30.428  1.00 65.63  ? 199 PHE A C   1 
ATOM   1514 O  O   . PHE A 1 199 ? -81.709  22.089 29.731  1.00 66.29  ? 199 PHE A O   1 
ATOM   1515 C  CB  . PHE A 1 199 ? -84.970  21.668 29.669  1.00 66.69  ? 199 PHE A CB  1 
ATOM   1516 C  CG  . PHE A 1 199 ? -84.565  21.630 28.215  1.00 68.05  ? 199 PHE A CG  1 
ATOM   1517 C  CD1 . PHE A 1 199 ? -83.977  22.732 27.610  1.00 63.92  ? 199 PHE A CD1 1 
ATOM   1518 C  CD2 . PHE A 1 199 ? -84.775  20.491 27.455  1.00 70.80  ? 199 PHE A CD2 1 
ATOM   1519 C  CE1 . PHE A 1 199 ? -83.596  22.692 26.283  1.00 66.85  ? 199 PHE A CE1 1 
ATOM   1520 C  CE2 . PHE A 1 199 ? -84.402  20.449 26.125  1.00 68.58  ? 199 PHE A CE2 1 
ATOM   1521 C  CZ  . PHE A 1 199 ? -83.812  21.551 25.539  1.00 69.99  ? 199 PHE A CZ  1 
ATOM   1522 N  N   . ASP A 1 200 ? -82.809  23.570 31.019  1.00 63.66  ? 200 ASP A N   1 
ATOM   1523 C  CA  . ASP A 1 200 ? -81.808  24.620 30.874  1.00 64.95  ? 200 ASP A CA  1 
ATOM   1524 C  C   . ASP A 1 200 ? -80.580  24.403 31.749  1.00 63.36  ? 200 ASP A C   1 
ATOM   1525 O  O   . ASP A 1 200 ? -79.630  25.186 31.652  1.00 69.59  ? 200 ASP A O   1 
ATOM   1526 C  CB  . ASP A 1 200 ? -82.427  25.984 31.196  1.00 62.42  ? 200 ASP A CB  1 
ATOM   1527 C  CG  . ASP A 1 200 ? -83.504  26.389 30.205  1.00 78.79  ? 200 ASP A CG  1 
ATOM   1528 O  OD1 . ASP A 1 200 ? -83.395  26.023 29.012  1.00 78.64  ? 200 ASP A OD1 1 
ATOM   1529 O  OD2 . ASP A 1 200 ? -84.459  27.081 30.622  1.00 77.17  ? 200 ASP A OD2 1 
ATOM   1530 N  N   . SER A 1 201 ? -80.570  23.373 32.589  1.00 64.01  ? 201 SER A N   1 
ATOM   1531 C  CA  . SER A 1 201 ? -79.464  23.173 33.514  1.00 70.66  ? 201 SER A CA  1 
ATOM   1532 C  C   . SER A 1 201 ? -78.187  22.798 32.766  1.00 67.66  ? 201 SER A C   1 
ATOM   1533 O  O   . SER A 1 201 ? -78.213  22.298 31.638  1.00 62.34  ? 201 SER A O   1 
ATOM   1534 C  CB  . SER A 1 201 ? -79.807  22.086 34.533  1.00 69.07  ? 201 SER A CB  1 
ATOM   1535 O  OG  . SER A 1 201 ? -79.930  20.822 33.903  1.00 68.03  ? 201 SER A OG  1 
ATOM   1536 N  N   . ALA A 1 202 ? -77.050  23.049 33.419  1.00 66.15  ? 202 ALA A N   1 
ATOM   1537 C  CA  . ALA A 1 202 ? -75.767  22.710 32.815  1.00 67.81  ? 202 ALA A CA  1 
ATOM   1538 C  C   . ALA A 1 202 ? -75.602  21.204 32.653  1.00 66.75  ? 202 ALA A C   1 
ATOM   1539 O  O   . ALA A 1 202 ? -75.003  20.750 31.672  1.00 70.36  ? 202 ALA A O   1 
ATOM   1540 C  CB  . ALA A 1 202 ? -74.625  23.287 33.650  1.00 54.55  ? 202 ALA A CB  1 
ATOM   1541 N  N   . VAL A 1 203 ? -76.132  20.419 33.594  1.00 69.05  ? 203 VAL A N   1 
ATOM   1542 C  CA  . VAL A 1 203 ? -75.992  18.968 33.519  1.00 67.45  ? 203 VAL A CA  1 
ATOM   1543 C  C   . VAL A 1 203 ? -76.803  18.411 32.357  1.00 65.24  ? 203 VAL A C   1 
ATOM   1544 O  O   . VAL A 1 203 ? -76.319  17.566 31.593  1.00 65.47  ? 203 VAL A O   1 
ATOM   1545 C  CB  . VAL A 1 203 ? -76.399  18.325 34.859  1.00 67.34  ? 203 VAL A CB  1 
ATOM   1546 C  CG1 . VAL A 1 203 ? -76.460  16.808 34.731  1.00 59.56  ? 203 VAL A CG1 1 
ATOM   1547 C  CG2 . VAL A 1 203 ? -75.431  18.738 35.963  1.00 62.75  ? 203 VAL A CG2 1 
ATOM   1548 N  N   . MET A 1 204 ? -78.044  18.874 32.200  1.00 66.91  ? 204 MET A N   1 
ATOM   1549 C  CA  . MET A 1 204 ? -78.878  18.384 31.109  1.00 68.59  ? 204 MET A CA  1 
ATOM   1550 C  C   . MET A 1 204 ? -78.316  18.796 29.753  1.00 68.57  ? 204 MET A C   1 
ATOM   1551 O  O   . MET A 1 204 ? -78.338  18.008 28.801  1.00 67.88  ? 204 MET A O   1 
ATOM   1552 C  CB  . MET A 1 204 ? -80.310  18.891 31.272  1.00 67.58  ? 204 MET A CB  1 
ATOM   1553 C  CG  . MET A 1 204 ? -81.300  18.315 30.266  1.00 73.83  ? 204 MET A CG  1 
ATOM   1554 S  SD  . MET A 1 204 ? -81.689  16.578 30.564  1.00 80.67  ? 204 MET A SD  1 
ATOM   1555 C  CE  . MET A 1 204 ? -80.572  15.764 29.431  1.00 68.52  ? 204 MET A CE  1 
ATOM   1556 N  N   . SER A 1 205 ? -77.803  20.025 29.648  1.00 62.41  ? 205 SER A N   1 
ATOM   1557 C  CA  . SER A 1 205 ? -77.209  20.472 28.394  1.00 63.23  ? 205 SER A CA  1 
ATOM   1558 C  C   . SER A 1 205 ? -76.016  19.607 28.010  1.00 66.34  ? 205 SER A C   1 
ATOM   1559 O  O   . SER A 1 205 ? -75.807  19.313 26.827  1.00 72.91  ? 205 SER A O   1 
ATOM   1560 C  CB  . SER A 1 205 ? -76.797  21.940 28.498  1.00 59.05  ? 205 SER A CB  1 
ATOM   1561 O  OG  . SER A 1 205 ? -77.934  22.773 28.641  1.00 71.83  ? 205 SER A OG  1 
ATOM   1562 N  N   . ALA A 1 206 ? -75.222  19.187 28.997  1.00 65.01  ? 206 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 206 ? -74.095  18.308 28.706  1.00 70.21  ? 206 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 206 ? -74.576  16.952 28.207  1.00 66.92  ? 206 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 206 ? -74.019  16.404 27.248  1.00 65.58  ? 206 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 206 ? -73.216  18.151 29.947  1.00 60.33  ? 206 ALA A CB  1 
ATOM   1567 N  N   . MET A 1 207 ? -75.615  16.402 28.837  1.00 57.50  ? 207 MET A N   1 
ATOM   1568 C  CA  . MET A 1 207 ? -76.177  15.139 28.375  1.00 60.46  ? 207 MET A CA  1 
ATOM   1569 C  C   . MET A 1 207 ? -76.766  15.287 26.980  1.00 66.03  ? 207 MET A C   1 
ATOM   1570 O  O   . MET A 1 207 ? -76.543  14.442 26.106  1.00 65.28  ? 207 MET A O   1 
ATOM   1571 C  CB  . MET A 1 207 ? -77.236  14.647 29.358  1.00 62.15  ? 207 MET A CB  1 
ATOM   1572 C  CG  . MET A 1 207 ? -76.696  14.327 30.734  1.00 71.72  ? 207 MET A CG  1 
ATOM   1573 S  SD  . MET A 1 207 ? -77.982  13.946 31.934  1.00 65.59  ? 207 MET A SD  1 
ATOM   1574 C  CE  . MET A 1 207 ? -78.973  12.768 31.023  1.00 70.09  ? 207 MET A CE  1 
ATOM   1575 N  N   . LEU A 1 208 ? -77.527  16.364 26.755  1.00 66.05  ? 208 LEU A N   1 
ATOM   1576 C  CA  . LEU A 1 208 ? -78.085  16.611 25.430  1.00 65.30  ? 208 LEU A CA  1 
ATOM   1577 C  C   . LEU A 1 208 ? -76.984  16.776 24.392  1.00 61.18  ? 208 LEU A C   1 
ATOM   1578 O  O   . LEU A 1 208 ? -77.101  16.269 23.271  1.00 67.37  ? 208 LEU A O   1 
ATOM   1579 C  CB  . LEU A 1 208 ? -78.991  17.844 25.454  1.00 58.98  ? 208 LEU A CB  1 
ATOM   1580 C  CG  . LEU A 1 208 ? -80.363  17.674 26.112  1.00 64.82  ? 208 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A 1 208 ? -81.101  19.004 26.206  1.00 61.08  ? 208 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A 1 208 ? -81.199  16.654 25.358  1.00 61.47  ? 208 LEU A CD2 1 
ATOM   1583 N  N   . GLN A 1 209 ? -75.897  17.464 24.749  1.00 59.97  ? 209 GLN A N   1 
ATOM   1584 C  CA  . GLN A 1 209 ? -74.802  17.640 23.799  1.00 63.41  ? 209 GLN A CA  1 
ATOM   1585 C  C   . GLN A 1 209 ? -74.090  16.324 23.512  1.00 65.94  ? 209 GLN A C   1 
ATOM   1586 O  O   . GLN A 1 209 ? -73.592  16.123 22.399  1.00 68.98  ? 209 GLN A O   1 
ATOM   1587 C  CB  . GLN A 1 209 ? -73.808  18.677 24.316  1.00 62.34  ? 209 GLN A CB  1 
ATOM   1588 C  CG  . GLN A 1 209 ? -72.756  19.074 23.290  1.00 82.48  ? 209 GLN A CG  1 
ATOM   1589 C  CD  . GLN A 1 209 ? -71.633  19.899 23.886  1.00 91.47  ? 209 GLN A CD  1 
ATOM   1590 O  OE1 . GLN A 1 209 ? -70.723  19.365 24.524  1.00 83.13  ? 209 GLN A OE1 1 
ATOM   1591 N  NE2 . GLN A 1 209 ? -71.688  21.210 23.676  1.00 98.94  ? 209 GLN A NE2 1 
ATOM   1592 N  N   . ILE A 1 210 ? -74.021  15.425 24.497  1.00 67.40  ? 210 ILE A N   1 
ATOM   1593 C  CA  . ILE A 1 210 ? -73.461  14.099 24.252  1.00 65.81  ? 210 ILE A CA  1 
ATOM   1594 C  C   . ILE A 1 210 ? -74.316  13.342 23.245  1.00 66.97  ? 210 ILE A C   1 
ATOM   1595 O  O   . ILE A 1 210 ? -73.797  12.712 22.317  1.00 67.61  ? 210 ILE A O   1 
ATOM   1596 C  CB  . ILE A 1 210 ? -73.328  13.321 25.573  1.00 64.61  ? 210 ILE A CB  1 
ATOM   1597 C  CG1 . ILE A 1 210 ? -72.131  13.826 26.376  1.00 63.27  ? 210 ILE A CG1 1 
ATOM   1598 C  CG2 . ILE A 1 210 ? -73.217  11.823 25.307  1.00 64.55  ? 210 ILE A CG2 1 
ATOM   1599 C  CD1 . ILE A 1 210 ? -72.034  13.216 27.754  1.00 68.83  ? 210 ILE A CD1 1 
ATOM   1600 N  N   . ALA A 1 211 ? -75.640  13.396 23.413  1.00 62.77  ? 211 ALA A N   1 
ATOM   1601 C  CA  . ALA A 1 211 ? -76.536  12.705 22.492  1.00 68.26  ? 211 ALA A CA  1 
ATOM   1602 C  C   . ALA A 1 211 ? -76.393  13.241 21.072  1.00 74.52  ? 211 ALA A C   1 
ATOM   1603 O  O   . ALA A 1 211 ? -76.454  12.476 20.102  1.00 74.65  ? 211 ALA A O   1 
ATOM   1604 C  CB  . ALA A 1 211 ? -77.980  12.833 22.975  1.00 64.92  ? 211 ALA A CB  1 
ATOM   1605 N  N   . VAL A 1 212 ? -76.193  14.553 20.932  1.00 73.00  ? 212 VAL A N   1 
ATOM   1606 C  CA  . VAL A 1 212 ? -75.998  15.144 19.612  1.00 68.65  ? 212 VAL A CA  1 
ATOM   1607 C  C   . VAL A 1 212 ? -74.676  14.682 19.011  1.00 70.46  ? 212 VAL A C   1 
ATOM   1608 O  O   . VAL A 1 212 ? -74.617  14.259 17.851  1.00 74.22  ? 212 VAL A O   1 
ATOM   1609 C  CB  . VAL A 1 212 ? -76.071  16.679 19.698  1.00 69.84  ? 212 VAL A CB  1 
ATOM   1610 C  CG1 . VAL A 1 212 ? -75.686  17.306 18.369  1.00 65.29  ? 212 VAL A CG1 1 
ATOM   1611 C  CG2 . VAL A 1 212 ? -77.464  17.121 20.119  1.00 67.84  ? 212 VAL A CG2 1 
ATOM   1612 N  N   . ASP A 1 213 ? -73.597  14.755 19.795  1.00 70.08  ? 213 ASP A N   1 
ATOM   1613 C  CA  . ASP A 1 213 ? -72.278  14.397 19.280  1.00 75.78  ? 213 ASP A CA  1 
ATOM   1614 C  C   . ASP A 1 213 ? -72.212  12.927 18.888  1.00 76.41  ? 213 ASP A C   1 
ATOM   1615 O  O   . ASP A 1 213 ? -71.654  12.583 17.840  1.00 76.70  ? 213 ASP A O   1 
ATOM   1616 C  CB  . ASP A 1 213 ? -71.202  14.723 20.317  1.00 77.02  ? 213 ASP A CB  1 
ATOM   1617 C  CG  . ASP A 1 213 ? -70.923  16.209 20.419  1.00 87.10  ? 213 ASP A CG  1 
ATOM   1618 O  OD1 . ASP A 1 213 ? -71.561  16.983 19.675  1.00 88.01  ? 213 ASP A OD1 1 
ATOM   1619 O  OD2 . ASP A 1 213 ? -70.065  16.603 21.240  1.00 91.20  ? 213 ASP A OD2 1 
ATOM   1620 N  N   . VAL A 1 214 ? -72.768  12.044 19.720  1.00 77.57  ? 214 VAL A N   1 
ATOM   1621 C  CA  . VAL A 1 214 ? -72.764  10.620 19.396  1.00 76.86  ? 214 VAL A CA  1 
ATOM   1622 C  C   . VAL A 1 214 ? -73.525  10.371 18.101  1.00 77.44  ? 214 VAL A C   1 
ATOM   1623 O  O   . VAL A 1 214 ? -73.113  9.554  17.269  1.00 78.41  ? 214 VAL A O   1 
ATOM   1624 C  CB  . VAL A 1 214 ? -73.343  9.805  20.569  1.00 70.05  ? 214 VAL A CB  1 
ATOM   1625 C  CG1 . VAL A 1 214 ? -73.631  8.373  20.149  1.00 66.76  ? 214 VAL A CG1 1 
ATOM   1626 C  CG2 . VAL A 1 214 ? -72.382  9.827  21.746  1.00 77.66  ? 214 VAL A CG2 1 
ATOM   1627 N  N   . ASN A 1 215 ? -74.626  11.094 17.894  1.00 77.78  ? 215 ASN A N   1 
ATOM   1628 C  CA  . ASN A 1 215 ? -75.436  10.888 16.697  1.00 78.72  ? 215 ASN A CA  1 
ATOM   1629 C  C   . ASN A 1 215 ? -74.689  11.308 15.437  1.00 78.51  ? 215 ASN A C   1 
ATOM   1630 O  O   . ASN A 1 215 ? -74.649  10.561 14.453  1.00 78.52  ? 215 ASN A O   1 
ATOM   1631 C  CB  . ASN A 1 215 ? -76.753  11.651 16.819  1.00 76.87  ? 215 ASN A CB  1 
ATOM   1632 C  CG  . ASN A 1 215 ? -77.861  10.811 17.418  1.00 79.44  ? 215 ASN A CG  1 
ATOM   1633 O  OD1 . ASN A 1 215 ? -78.698  10.268 16.699  1.00 83.18  ? 215 ASN A OD1 1 
ATOM   1634 N  ND2 . ASN A 1 215 ? -77.873  10.700 18.741  1.00 72.86  ? 215 ASN A ND2 1 
ATOM   1635 N  N   . LEU A 1 216 ? -74.092  12.503 15.442  1.00 72.47  ? 216 LEU A N   1 
ATOM   1636 C  CA  . LEU A 1 216 ? -73.405  12.967 14.242  1.00 80.88  ? 216 LEU A CA  1 
ATOM   1637 C  C   . LEU A 1 216 ? -72.143  12.158 13.970  1.00 82.36  ? 216 LEU A C   1 
ATOM   1638 O  O   . LEU A 1 216 ? -71.758  11.991 12.807  1.00 82.76  ? 216 LEU A O   1 
ATOM   1639 C  CB  . LEU A 1 216 ? -73.088  14.462 14.352  1.00 79.61  ? 216 LEU A CB  1 
ATOM   1640 C  CG  . LEU A 1 216 ? -71.964  14.961 15.261  1.00 79.64  ? 216 LEU A CG  1 
ATOM   1641 C  CD1 . LEU A 1 216 ? -70.651  15.079 14.500  1.00 79.34  ? 216 LEU A CD1 1 
ATOM   1642 C  CD2 . LEU A 1 216 ? -72.344  16.297 15.881  1.00 86.78  ? 216 LEU A CD2 1 
ATOM   1643 N  N   . LEU A 1 217 ? -71.490  11.648 15.018  1.00 78.54  ? 217 LEU A N   1 
ATOM   1644 C  CA  . LEU A 1 217 ? -70.345  10.765 14.812  1.00 80.97  ? 217 LEU A CA  1 
ATOM   1645 C  C   . LEU A 1 217 ? -70.776  9.432  14.211  1.00 81.25  ? 217 LEU A C   1 
ATOM   1646 O  O   . LEU A 1 217 ? -70.105  8.903  13.318  1.00 78.57  ? 217 LEU A O   1 
ATOM   1647 C  CB  . LEU A 1 217 ? -69.604  10.541 16.130  1.00 76.36  ? 217 LEU A CB  1 
ATOM   1648 C  CG  . LEU A 1 217 ? -68.840  11.726 16.719  1.00 85.15  ? 217 LEU A CG  1 
ATOM   1649 C  CD1 . LEU A 1 217 ? -68.170  11.325 18.029  1.00 83.09  ? 217 LEU A CD1 1 
ATOM   1650 C  CD2 . LEU A 1 217 ? -67.823  12.271 15.726  1.00 75.21  ? 217 LEU A CD2 1 
ATOM   1651 N  N   . LEU A 1 218 ? -71.886  8.865  14.699  1.00 79.71  ? 218 LEU A N   1 
ATOM   1652 C  CA  . LEU A 1 218 ? -72.423  7.650  14.095  1.00 82.36  ? 218 LEU A CA  1 
ATOM   1653 C  C   . LEU A 1 218 ? -72.791  7.883  12.636  1.00 88.51  ? 218 LEU A C   1 
ATOM   1654 O  O   . LEU A 1 218 ? -72.536  7.030  11.777  1.00 88.26  ? 218 LEU A O   1 
ATOM   1655 C  CB  . LEU A 1 218 ? -73.646  7.162  14.874  1.00 78.61  ? 218 LEU A CB  1 
ATOM   1656 C  CG  . LEU A 1 218 ? -73.452  6.631  16.297  1.00 91.58  ? 218 LEU A CG  1 
ATOM   1657 C  CD1 . LEU A 1 218 ? -74.794  6.292  16.929  1.00 88.49  ? 218 LEU A CD1 1 
ATOM   1658 C  CD2 . LEU A 1 218 ? -72.539  5.425  16.304  1.00 94.57  ? 218 LEU A CD2 1 
ATOM   1659 N  N   . ASN A 1 219 ? -73.387  9.040  12.339  1.00 87.94  ? 219 ASN A N   1 
ATOM   1660 C  CA  . ASN A 1 219 ? -73.828  9.326  10.980  1.00 87.10  ? 219 ASN A CA  1 
ATOM   1661 C  C   . ASN A 1 219 ? -72.645  9.564  10.050  1.00 89.10  ? 219 ASN A C   1 
ATOM   1662 O  O   . ASN A 1 219 ? -72.675  9.151  8.884   1.00 88.93  ? 219 ASN A O   1 
ATOM   1663 C  CB  . ASN A 1 219 ? -74.761  10.536 10.982  1.00 88.22  ? 219 ASN A CB  1 
ATOM   1664 C  CG  . ASN A 1 219 ? -75.308  10.852 9.606   1.00 91.73  ? 219 ASN A CG  1 
ATOM   1665 O  OD1 . ASN A 1 219 ? -74.688  11.579 8.830   1.00 94.63  ? 219 ASN A OD1 1 
ATOM   1666 N  ND2 . ASN A 1 219 ? -76.480  10.308 9.297   1.00 92.54  ? 219 ASN A ND2 1 
ATOM   1667 N  N   . ASP A 1 220 ? -71.594  10.229 10.541  1.00 84.52  ? 220 ASP A N   1 
ATOM   1668 C  CA  . ASP A 1 220 ? -70.447  10.513 9.685   1.00 87.42  ? 220 ASP A CA  1 
ATOM   1669 C  C   . ASP A 1 220 ? -69.685  9.246  9.320   1.00 88.37  ? 220 ASP A C   1 
ATOM   1670 O  O   . ASP A 1 220 ? -68.997  9.214  8.294   1.00 91.17  ? 220 ASP A O   1 
ATOM   1671 C  CB  . ASP A 1 220 ? -69.509  11.513 10.361  1.00 85.16  ? 220 ASP A CB  1 
ATOM   1672 C  CG  . ASP A 1 220 ? -69.871  12.949 10.052  1.00 89.74  ? 220 ASP A CG  1 
ATOM   1673 O  OD1 . ASP A 1 220 ? -71.059  13.218 9.771   1.00 90.61  ? 220 ASP A OD1 1 
ATOM   1674 O  OD2 . ASP A 1 220 ? -68.966  13.806 10.070  1.00 95.18  ? 220 ASP A OD2 1 
ATOM   1675 N  N   . ILE A 1 221 ? -69.786  8.198  10.138  1.00 87.31  ? 221 ILE A N   1 
ATOM   1676 C  CA  . ILE A 1 221 ? -69.139  6.939  9.792   1.00 87.73  ? 221 ILE A CA  1 
ATOM   1677 C  C   . ILE A 1 221 ? -70.040  6.102  8.892   1.00 88.26  ? 221 ILE A C   1 
ATOM   1678 O  O   . ILE A 1 221 ? -69.574  5.495  7.921   1.00 89.60  ? 221 ILE A O   1 
ATOM   1679 C  CB  . ILE A 1 221 ? -68.746  6.184  11.074  1.00 84.84  ? 221 ILE A CB  1 
ATOM   1680 C  CG1 . ILE A 1 221 ? -67.527  6.846  11.717  1.00 83.62  ? 221 ILE A CG1 1 
ATOM   1681 C  CG2 . ILE A 1 221 ? -68.462  4.724  10.773  1.00 90.06  ? 221 ILE A CG2 1 
ATOM   1682 C  CD1 . ILE A 1 221 ? -67.049  6.163  12.970  1.00 87.12  ? 221 ILE A CD1 1 
ATOM   1683 N  N   . ALA A 1 222 ? -71.344  6.079  9.180   1.00 84.51  ? 222 ALA A N   1 
ATOM   1684 C  CA  . ALA A 1 222 ? -72.264  5.246  8.412   1.00 89.40  ? 222 ALA A CA  1 
ATOM   1685 C  C   . ALA A 1 222 ? -72.405  5.725  6.973   1.00 93.91  ? 222 ALA A C   1 
ATOM   1686 O  O   . ALA A 1 222 ? -72.616  4.907  6.071   1.00 95.63  ? 222 ALA A O   1 
ATOM   1687 C  CB  . ALA A 1 222 ? -73.631  5.212  9.092   1.00 89.96  ? 222 ALA A CB  1 
ATOM   1688 N  N   . SER A 1 223 ? -72.298  7.032  6.736   1.00 95.10  ? 223 SER A N   1 
ATOM   1689 C  CA  . SER A 1 223 ? -72.474  7.603  5.406   1.00 98.21  ? 223 SER A CA  1 
ATOM   1690 C  C   . SER A 1 223 ? -71.167  8.150  4.841   1.00 99.36  ? 223 SER A C   1 
ATOM   1691 O  O   . SER A 1 223 ? -71.174  9.102  4.058   1.00 103.56 ? 223 SER A O   1 
ATOM   1692 C  CB  . SER A 1 223 ? -73.541  8.696  5.430   1.00 98.20  ? 223 SER A CB  1 
ATOM   1693 O  OG  . SER A 1 223 ? -73.071  9.851  6.103   1.00 96.01  ? 223 SER A OG  1 
ATOM   1694 N  N   . LEU A 1 224 ? -70.038  7.556  5.229   1.00 98.85  ? 224 LEU A N   1 
ATOM   1695 C  CA  . LEU A 1 224 ? -68.756  8.014  4.706   1.00 100.42 ? 224 LEU A CA  1 
ATOM   1696 C  C   . LEU A 1 224 ? -68.588  7.630  3.239   1.00 107.95 ? 224 LEU A C   1 
ATOM   1697 O  O   . LEU A 1 224 ? -68.035  8.404  2.449   1.00 107.77 ? 224 LEU A O   1 
ATOM   1698 C  CB  . LEU A 1 224 ? -67.614  7.451  5.553   1.00 97.44  ? 224 LEU A CB  1 
ATOM   1699 C  CG  . LEU A 1 224 ? -66.231  8.070  5.337   1.00 100.97 ? 224 LEU A CG  1 
ATOM   1700 C  CD1 . LEU A 1 224 ? -65.407  7.279  4.329   1.00 109.04 ? 224 LEU A CD1 1 
ATOM   1701 C  CD2 . LEU A 1 224 ? -66.379  9.516  4.890   1.00 106.45 ? 224 LEU A CD2 1 
ATOM   1702 N  N   . GLU A 1 225 ? -69.055  6.439  2.857   1.00 107.14 ? 225 GLU A N   1 
ATOM   1703 C  CA  . GLU A 1 225 ? -68.930  6.012  1.468   1.00 105.82 ? 225 GLU A CA  1 
ATOM   1704 C  C   . GLU A 1 225 ? -69.751  6.898  0.539   1.00 105.23 ? 225 GLU A C   1 
ATOM   1705 O  O   . GLU A 1 225 ? -69.270  7.304  -0.525  1.00 105.32 ? 225 GLU A O   1 
ATOM   1706 C  CB  . GLU A 1 225 ? -69.349  4.548  1.331   1.00 103.10 ? 225 GLU A CB  1 
ATOM   1707 C  CG  . GLU A 1 225 ? -68.454  3.574  2.082   1.00 94.97  ? 225 GLU A CG  1 
ATOM   1708 N  N   . LYS A 1 226 ? -70.989  7.218  0.928   1.00 104.19 ? 226 LYS A N   1 
ATOM   1709 C  CA  . LYS A 1 226 ? -71.832  8.062  0.089   1.00 102.06 ? 226 LYS A CA  1 
ATOM   1710 C  C   . LYS A 1 226 ? -71.267  9.470  -0.042  1.00 111.85 ? 226 LYS A C   1 
ATOM   1711 O  O   . LYS A 1 226 ? -71.525  10.151 -1.041  1.00 115.00 ? 226 LYS A O   1 
ATOM   1712 C  CB  . LYS A 1 226 ? -73.253  8.113  0.651   1.00 100.75 ? 226 LYS A CB  1 
ATOM   1713 N  N   . GLU A 1 227 ? -70.496  9.923  0.947   1.00 114.00 ? 227 GLU A N   1 
ATOM   1714 C  CA  . GLU A 1 227 ? -69.892  11.248 0.897   1.00 115.81 ? 227 GLU A CA  1 
ATOM   1715 C  C   . GLU A 1 227 ? -68.479  11.236 0.331   1.00 116.60 ? 227 GLU A C   1 
ATOM   1716 O  O   . GLU A 1 227 ? -68.029  12.264 -0.189  1.00 115.87 ? 227 GLU A O   1 
ATOM   1717 C  CB  . GLU A 1 227 ? -69.886  11.877 2.293   1.00 110.77 ? 227 GLU A CB  1 
ATOM   1718 C  CG  . GLU A 1 227 ? -71.282  12.133 2.844   1.00 111.84 ? 227 GLU A CG  1 
ATOM   1719 C  CD  . GLU A 1 227 ? -71.268  12.798 4.206   1.00 112.35 ? 227 GLU A CD  1 
ATOM   1720 O  OE1 . GLU A 1 227 ? -70.166  13.072 4.728   1.00 114.84 ? 227 GLU A OE1 1 
ATOM   1721 O  OE2 . GLU A 1 227 ? -72.362  13.049 4.753   1.00 108.21 ? 227 GLU A OE2 1 
ATOM   1722 N  N   . GLU A 1 228 ? -67.773  10.107 0.418   1.00 117.42 ? 228 GLU A N   1 
ATOM   1723 C  CA  . GLU A 1 228 ? -66.483  9.992  -0.254  1.00 118.81 ? 228 GLU A CA  1 
ATOM   1724 C  C   . GLU A 1 228 ? -66.660  9.920  -1.766  1.00 120.70 ? 228 GLU A C   1 
ATOM   1725 O  O   . GLU A 1 228 ? -65.892  10.531 -2.519  1.00 118.45 ? 228 GLU A O   1 
ATOM   1726 C  CB  . GLU A 1 228 ? -65.728  8.765  0.260   1.00 115.99 ? 228 GLU A CB  1 
ATOM   1727 C  CG  . GLU A 1 228 ? -64.388  8.514  -0.417  1.00 122.55 ? 228 GLU A CG  1 
ATOM   1728 C  CD  . GLU A 1 228 ? -63.327  9.531  -0.033  1.00 127.92 ? 228 GLU A CD  1 
ATOM   1729 O  OE1 . GLU A 1 228 ? -63.546  10.294 0.933   1.00 125.72 ? 228 GLU A OE1 1 
ATOM   1730 O  OE2 . GLU A 1 228 ? -62.269  9.567  -0.698  1.00 126.68 ? 228 GLU A OE2 1 
ATOM   1731 N  N   . ALA A 1 229 ? -67.678  9.189  -2.227  1.00 119.69 ? 229 ALA A N   1 
ATOM   1732 C  CA  . ALA A 1 229 ? -67.989  9.088  -3.648  1.00 116.01 ? 229 ALA A CA  1 
ATOM   1733 C  C   . ALA A 1 229 ? -68.597  10.363 -4.214  1.00 115.05 ? 229 ALA A C   1 
ATOM   1734 O  O   . ALA A 1 229 ? -68.958  10.384 -5.397  1.00 117.40 ? 229 ALA A O   1 
ATOM   1735 C  CB  . ALA A 1 229 ? -68.936  7.911  -3.892  1.00 107.38 ? 229 ALA A CB  1 
ATOM   1736 N  N   . ARG A 1 230 ? -68.723  11.418 -3.407  1.00 114.07 ? 230 ARG A N   1 
ATOM   1737 C  CA  . ARG A 1 230 ? -69.271  12.690 -3.856  1.00 115.83 ? 230 ARG A CA  1 
ATOM   1738 C  C   . ARG A 1 230 ? -68.345  13.857 -3.526  1.00 117.95 ? 230 ARG A C   1 
ATOM   1739 O  O   . ARG A 1 230 ? -68.751  15.017 -3.665  1.00 113.01 ? 230 ARG A O   1 
ATOM   1740 C  CB  . ARG A 1 230 ? -70.660  12.910 -3.240  1.00 117.43 ? 230 ARG A CB  1 
ATOM   1741 C  CG  . ARG A 1 230 ? -71.603  13.780 -4.056  1.00 110.14 ? 230 ARG A CG  1 
ATOM   1742 C  CD  . ARG A 1 230 ? -73.043  13.653 -3.565  1.00 109.96 ? 230 ARG A CD  1 
ATOM   1743 N  NE  . ARG A 1 230 ? -73.152  13.784 -2.116  1.00 119.65 ? 230 ARG A NE  1 
ATOM   1744 C  CZ  . ARG A 1 230 ? -73.327  12.768 -1.282  1.00 127.06 ? 230 ARG A CZ  1 
ATOM   1745 N  NH1 . ARG A 1 230 ? -73.431  11.523 -1.721  1.00 124.89 ? 230 ARG A NH1 1 
ATOM   1746 N  NH2 . ARG A 1 230 ? -73.396  13.005 0.027   1.00 116.10 ? 230 ARG A NH2 1 
ATOM   1747 N  N   . GLY A 1 231 ? -67.117  13.580 -3.088  1.00 116.97 ? 231 GLY A N   1 
ATOM   1748 C  CA  . GLY A 1 231 ? -66.140  14.624 -2.847  1.00 118.01 ? 231 GLY A CA  1 
ATOM   1749 C  C   . GLY A 1 231 ? -66.450  15.552 -1.696  1.00 118.94 ? 231 GLY A C   1 
ATOM   1750 O  O   . GLY A 1 231 ? -65.882  16.645 -1.628  1.00 117.90 ? 231 GLY A O   1 
ATOM   1751 N  N   . GLU A 1 232 ? -67.334  15.152 -0.786  1.00 122.56 ? 232 GLU A N   1 
ATOM   1752 C  CA  . GLU A 1 232 ? -67.677  15.999 0.348   1.00 117.54 ? 232 GLU A CA  1 
ATOM   1753 C  C   . GLU A 1 232 ? -66.505  16.085 1.317   1.00 116.50 ? 232 GLU A C   1 
ATOM   1754 O  O   . GLU A 1 232 ? -65.876  15.073 1.639   1.00 115.81 ? 232 GLU A O   1 
ATOM   1755 C  CB  . GLU A 1 232 ? -68.916  15.458 1.059   1.00 115.73 ? 232 GLU A CB  1 
ATOM   1756 C  CG  . GLU A 1 232 ? -69.279  16.217 2.323   1.00 114.67 ? 232 GLU A CG  1 
ATOM   1757 C  CD  . GLU A 1 232 ? -69.556  17.684 2.059   1.00 115.71 ? 232 GLU A CD  1 
ATOM   1758 O  OE1 . GLU A 1 232 ? -70.373  17.986 1.164   1.00 121.18 ? 232 GLU A OE1 1 
ATOM   1759 O  OE2 . GLU A 1 232 ? -68.950  18.536 2.741   1.00 106.61 ? 232 GLU A OE2 1 
ATOM   1760 N  N   . GLN A 1 233 ? -66.209  17.299 1.782   1.00 113.62 ? 233 GLN A N   1 
ATOM   1761 C  CA  . GLN A 1 233 ? -65.091  17.529 2.684   1.00 113.60 ? 233 GLN A CA  1 
ATOM   1762 C  C   . GLN A 1 233 ? -65.507  17.800 4.124   1.00 111.46 ? 233 GLN A C   1 
ATOM   1763 O  O   . GLN A 1 233 ? -64.637  17.835 5.002   1.00 105.49 ? 233 GLN A O   1 
ATOM   1764 C  CB  . GLN A 1 233 ? -64.233  18.699 2.175   1.00 108.13 ? 233 GLN A CB  1 
ATOM   1765 N  N   . ASN A 1 234 ? -66.797  17.989 4.396   1.00 106.64 ? 234 ASN A N   1 
ATOM   1766 C  CA  . ASN A 1 234 ? -67.266  18.250 5.757   1.00 104.39 ? 234 ASN A CA  1 
ATOM   1767 C  C   . ASN A 1 234 ? -67.843  16.970 6.363   1.00 100.35 ? 234 ASN A C   1 
ATOM   1768 O  O   . ASN A 1 234 ? -69.045  16.823 6.597   1.00 93.70  ? 234 ASN A O   1 
ATOM   1769 C  CB  . ASN A 1 234 ? -68.277  19.394 5.765   1.00 103.23 ? 234 ASN A CB  1 
ATOM   1770 C  CG  . ASN A 1 234 ? -67.616  20.756 5.634   1.00 101.69 ? 234 ASN A CG  1 
ATOM   1771 O  OD1 . ASN A 1 234 ? -66.408  20.895 5.834   1.00 103.21 ? 234 ASN A OD1 1 
ATOM   1772 N  ND2 . ASN A 1 234 ? -68.409  21.771 5.307   1.00 95.26  ? 234 ASN A ND2 1 
ATOM   1773 N  N   . ASN A 1 235 ? -66.936  16.030 6.610   1.00 97.97  ? 235 ASN A N   1 
ATOM   1774 C  CA  . ASN A 1 235 ? -67.238  14.784 7.294   1.00 93.89  ? 235 ASN A CA  1 
ATOM   1775 C  C   . ASN A 1 235 ? -66.142  14.546 8.318   1.00 99.30  ? 235 ASN A C   1 
ATOM   1776 O  O   . ASN A 1 235 ? -64.960  14.736 8.017   1.00 100.54 ? 235 ASN A O   1 
ATOM   1777 C  CB  . ASN A 1 235 ? -67.329  13.613 6.311   1.00 98.15  ? 235 ASN A CB  1 
ATOM   1778 C  CG  . ASN A 1 235 ? -67.724  12.313 6.981   1.00 96.59  ? 235 ASN A CG  1 
ATOM   1779 O  OD1 . ASN A 1 235 ? -66.924  11.695 7.684   1.00 96.23  ? 235 ASN A OD1 1 
ATOM   1780 N  ND2 . ASN A 1 235 ? -68.957  11.880 6.749   1.00 94.54  ? 235 ASN A ND2 1 
ATOM   1781 N  N   . MET A 1 236 ? -66.541  14.125 9.523   1.00 99.27  ? 236 MET A N   1 
ATOM   1782 C  CA  . MET A 1 236 ? -65.620  14.108 10.658  1.00 91.06  ? 236 MET A CA  1 
ATOM   1783 C  C   . MET A 1 236 ? -64.356  13.308 10.370  1.00 97.16  ? 236 MET A C   1 
ATOM   1784 O  O   . MET A 1 236 ? -63.280  13.660 10.866  1.00 96.65  ? 236 MET A O   1 
ATOM   1785 C  CB  . MET A 1 236 ? -66.326  13.559 11.899  1.00 93.77  ? 236 MET A CB  1 
ATOM   1786 C  CG  . MET A 1 236 ? -65.507  13.654 13.182  1.00 100.71 ? 236 MET A CG  1 
ATOM   1787 S  SD  . MET A 1 236 ? -65.089  15.344 13.669  1.00 96.78  ? 236 MET A SD  1 
ATOM   1788 C  CE  . MET A 1 236 ? -64.312  15.045 15.255  1.00 109.35 ? 236 MET A CE  1 
ATOM   1789 N  N   . VAL A 1 237 ? -64.449  12.242 9.569   1.00 102.98 ? 237 VAL A N   1 
ATOM   1790 C  CA  . VAL A 1 237 ? -63.241  11.482 9.260   1.00 100.78 ? 237 VAL A CA  1 
ATOM   1791 C  C   . VAL A 1 237 ? -62.345  12.261 8.303   1.00 100.47 ? 237 VAL A C   1 
ATOM   1792 O  O   . VAL A 1 237 ? -61.115  12.168 8.383   1.00 104.34 ? 237 VAL A O   1 
ATOM   1793 C  CB  . VAL A 1 237 ? -63.584  10.085 8.703   1.00 97.23  ? 237 VAL A CB  1 
ATOM   1794 C  CG1 . VAL A 1 237 ? -64.683  9.430  9.516   1.00 94.18  ? 237 VAL A CG1 1 
ATOM   1795 C  CG2 . VAL A 1 237 ? -63.980  10.161 7.255   1.00 101.02 ? 237 VAL A CG2 1 
ATOM   1796 N  N   . MET A 1 238 ? -62.931  13.049 7.396   1.00 96.82  ? 238 MET A N   1 
ATOM   1797 C  CA  . MET A 1 238 ? -62.115  13.866 6.503   1.00 104.39 ? 238 MET A CA  1 
ATOM   1798 C  C   . MET A 1 238 ? -61.497  15.040 7.248   1.00 105.30 ? 238 MET A C   1 
ATOM   1799 O  O   . MET A 1 238 ? -60.349  15.416 6.985   1.00 104.21 ? 238 MET A O   1 
ATOM   1800 C  CB  . MET A 1 238 ? -62.950  14.370 5.325   1.00 104.47 ? 238 MET A CB  1 
ATOM   1801 C  CG  . MET A 1 238 ? -62.848  13.510 4.083   1.00 111.09 ? 238 MET A CG  1 
ATOM   1802 S  SD  . MET A 1 238 ? -63.863  12.029 4.180   1.00 124.02 ? 238 MET A SD  1 
ATOM   1803 C  CE  . MET A 1 238 ? -65.412  12.649 3.533   1.00 114.51 ? 238 MET A CE  1 
ATOM   1804 N  N   . ILE A 1 239 ? -62.245  15.627 8.183   1.00 102.38 ? 239 ILE A N   1 
ATOM   1805 C  CA  . ILE A 1 239 ? -61.759  16.802 8.893   1.00 103.66 ? 239 ILE A CA  1 
ATOM   1806 C  C   . ILE A 1 239 ? -60.648  16.430 9.866   1.00 108.31 ? 239 ILE A C   1 
ATOM   1807 O  O   . ILE A 1 239 ? -59.710  17.209 10.075  1.00 109.89 ? 239 ILE A O   1 
ATOM   1808 C  CB  . ILE A 1 239 ? -62.934  17.502 9.595   1.00 100.32 ? 239 ILE A CB  1 
ATOM   1809 C  CG1 . ILE A 1 239 ? -64.056  17.753 8.587   1.00 98.04  ? 239 ILE A CG1 1 
ATOM   1810 C  CG2 . ILE A 1 239 ? -62.485  18.809 10.224  1.00 103.04 ? 239 ILE A CG2 1 
ATOM   1811 C  CD1 . ILE A 1 239 ? -65.270  18.420 9.171   1.00 99.28  ? 239 ILE A CD1 1 
ATOM   1812 N  N   . LEU A 1 240 ? -60.720  15.240 10.468  1.00 105.83 ? 240 LEU A N   1 
ATOM   1813 C  CA  . LEU A 1 240 ? -59.653  14.812 11.367  1.00 112.04 ? 240 LEU A CA  1 
ATOM   1814 C  C   . LEU A 1 240 ? -58.360  14.536 10.610  1.00 116.90 ? 240 LEU A C   1 
ATOM   1815 O  O   . LEU A 1 240 ? -57.269  14.769 11.145  1.00 116.41 ? 240 LEU A O   1 
ATOM   1816 C  CB  . LEU A 1 240 ? -60.089  13.578 12.156  1.00 107.39 ? 240 LEU A CB  1 
ATOM   1817 C  CG  . LEU A 1 240 ? -61.175  13.803 13.211  1.00 103.29 ? 240 LEU A CG  1 
ATOM   1818 C  CD1 . LEU A 1 240 ? -61.620  12.481 13.818  1.00 102.93 ? 240 LEU A CD1 1 
ATOM   1819 C  CD2 . LEU A 1 240 ? -60.692  14.760 14.291  1.00 99.52  ? 240 LEU A CD2 1 
ATOM   1820 N  N   . ARG A 1 241 ? -58.457  14.046 9.371   1.00 116.70 ? 241 ARG A N   1 
ATOM   1821 C  CA  . ARG A 1 241 ? -57.259  13.847 8.564   1.00 114.24 ? 241 ARG A CA  1 
ATOM   1822 C  C   . ARG A 1 241 ? -56.645  15.173 8.134   1.00 116.69 ? 241 ARG A C   1 
ATOM   1823 O  O   . ARG A 1 241 ? -55.425  15.261 7.961   1.00 119.64 ? 241 ARG A O   1 
ATOM   1824 C  CB  . ARG A 1 241 ? -57.577  12.993 7.337   1.00 113.80 ? 241 ARG A CB  1 
ATOM   1825 C  CG  . ARG A 1 241 ? -58.080  11.598 7.655   1.00 115.42 ? 241 ARG A CG  1 
ATOM   1826 C  CD  . ARG A 1 241 ? -58.083  10.732 6.409   1.00 116.06 ? 241 ARG A CD  1 
ATOM   1827 N  NE  . ARG A 1 241 ? -56.738  10.570 5.869   1.00 121.69 ? 241 ARG A NE  1 
ATOM   1828 C  CZ  . ARG A 1 241 ? -56.457  9.959  4.727   1.00 123.93 ? 241 ARG A CZ  1 
ATOM   1829 N  NH1 . ARG A 1 241 ? -57.409  9.445  3.964   1.00 120.61 ? 241 ARG A NH1 1 
ATOM   1830 N  NH2 . ARG A 1 241 ? -55.188  9.862  4.339   1.00 124.72 ? 241 ARG A NH2 1 
ATOM   1831 N  N   . ARG A 1 242 ? -57.467  16.208 7.950   1.00 113.16 ? 242 ARG A N   1 
ATOM   1832 C  CA  . ARG A 1 242 ? -56.932  17.521 7.605   1.00 113.01 ? 242 ARG A CA  1 
ATOM   1833 C  C   . ARG A 1 242 ? -56.437  18.262 8.840   1.00 117.53 ? 242 ARG A C   1 
ATOM   1834 O  O   . ARG A 1 242 ? -55.399  18.932 8.791   1.00 117.51 ? 242 ARG A O   1 
ATOM   1835 C  CB  . ARG A 1 242 ? -57.990  18.354 6.879   1.00 109.02 ? 242 ARG A CB  1 
ATOM   1836 C  CG  . ARG A 1 242 ? -58.489  17.748 5.580   1.00 109.10 ? 242 ARG A CG  1 
ATOM   1837 C  CD  . ARG A 1 242 ? -59.227  18.781 4.741   1.00 106.09 ? 242 ARG A CD  1 
ATOM   1838 N  NE  . ARG A 1 242 ? -60.344  19.387 5.458   1.00 108.51 ? 242 ARG A NE  1 
ATOM   1839 C  CZ  . ARG A 1 242 ? -61.592  18.941 5.415   1.00 107.11 ? 242 ARG A CZ  1 
ATOM   1840 N  NH1 . ARG A 1 242 ? -61.922  17.874 4.706   1.00 106.46 ? 242 ARG A NH1 1 
ATOM   1841 N  NH2 . ARG A 1 242 ? -62.534  19.584 6.101   1.00 107.42 ? 242 ARG A NH2 1 
ATOM   1842 N  N   . GLU A 1 243 ? -57.161  18.149 9.955   1.00 117.05 ? 243 GLU A N   1 
ATOM   1843 C  CA  . GLU A 1 243 ? -56.784  18.883 11.158  1.00 116.62 ? 243 GLU A CA  1 
ATOM   1844 C  C   . GLU A 1 243 ? -55.562  18.269 11.829  1.00 119.36 ? 243 GLU A C   1 
ATOM   1845 O  O   . GLU A 1 243 ? -54.690  18.994 12.323  1.00 120.27 ? 243 GLU A O   1 
ATOM   1846 C  CB  . GLU A 1 243 ? -57.961  18.935 12.134  1.00 117.77 ? 243 GLU A CB  1 
ATOM   1847 C  CG  . GLU A 1 243 ? -57.717  19.810 13.355  1.00 118.64 ? 243 GLU A CG  1 
ATOM   1848 C  CD  . GLU A 1 243 ? -58.881  19.800 14.331  1.00 113.98 ? 243 GLU A CD  1 
ATOM   1849 O  OE1 . GLU A 1 243 ? -59.788  18.954 14.176  1.00 109.11 ? 243 GLU A OE1 1 
ATOM   1850 O  OE2 . GLU A 1 243 ? -58.890  20.644 15.252  1.00 111.32 ? 243 GLU A OE2 1 
ATOM   1851 N  N   . HIS A 1 244 ? -55.474  16.939 11.857  1.00 118.76 ? 244 HIS A N   1 
ATOM   1852 C  CA  . HIS A 1 244 ? -54.410  16.254 12.577  1.00 118.33 ? 244 HIS A CA  1 
ATOM   1853 C  C   . HIS A 1 244 ? -53.465  15.469 11.679  1.00 119.73 ? 244 HIS A C   1 
ATOM   1854 O  O   . HIS A 1 244 ? -52.528  14.847 12.192  1.00 118.98 ? 244 HIS A O   1 
ATOM   1855 C  CB  . HIS A 1 244 ? -55.006  15.314 13.633  1.00 116.77 ? 244 HIS A CB  1 
ATOM   1856 C  CG  . HIS A 1 244 ? -55.982  15.983 14.549  1.00 121.38 ? 244 HIS A CG  1 
ATOM   1857 N  ND1 . HIS A 1 244 ? -55.589  16.817 15.574  1.00 121.28 ? 244 HIS A ND1 1 
ATOM   1858 C  CD2 . HIS A 1 244 ? -57.335  15.945 14.592  1.00 123.19 ? 244 HIS A CD2 1 
ATOM   1859 C  CE1 . HIS A 1 244 ? -56.658  17.262 16.211  1.00 118.45 ? 244 HIS A CE1 1 
ATOM   1860 N  NE2 . HIS A 1 244 ? -57.730  16.748 15.635  1.00 123.54 ? 244 HIS A NE2 1 
ATOM   1861 N  N   . GLY A 1 245 ? -53.677  15.475 10.366  1.00 119.83 ? 245 GLY A N   1 
ATOM   1862 C  CA  . GLY A 1 245 ? -52.783  14.755 9.473   1.00 120.50 ? 245 GLY A CA  1 
ATOM   1863 C  C   . GLY A 1 245 ? -52.764  13.259 9.696   1.00 124.23 ? 245 GLY A C   1 
ATOM   1864 O  O   . GLY A 1 245 ? -51.712  12.624 9.549   1.00 127.23 ? 245 GLY A O   1 
ATOM   1865 N  N   . TRP A 1 246 ? -53.904  12.679 10.051  1.00 126.24 ? 246 TRP A N   1 
ATOM   1866 C  CA  . TRP A 1 246 ? -54.003  11.254 10.326  1.00 123.10 ? 246 TRP A CA  1 
ATOM   1867 C  C   . TRP A 1 246 ? -54.522  10.511 9.100   1.00 120.88 ? 246 TRP A C   1 
ATOM   1868 O  O   . TRP A 1 246 ? -54.938  11.108 8.105   1.00 121.62 ? 246 TRP A O   1 
ATOM   1869 C  CB  . TRP A 1 246 ? -54.912  11.002 11.533  1.00 117.44 ? 246 TRP A CB  1 
ATOM   1870 N  N   . SER A 1 247 ? -54.483  9.185  9.182   1.00 120.24 ? 247 SER A N   1 
ATOM   1871 C  CA  . SER A 1 247 ? -55.001  8.334  8.120   1.00 117.60 ? 247 SER A CA  1 
ATOM   1872 C  C   . SER A 1 247 ? -56.504  8.147  8.317   1.00 120.53 ? 247 SER A C   1 
ATOM   1873 O  O   . SER A 1 247 ? -57.128  8.774  9.178   1.00 121.60 ? 247 SER A O   1 
ATOM   1874 C  CB  . SER A 1 247 ? -54.257  7.002  8.102   1.00 117.84 ? 247 SER A CB  1 
ATOM   1875 O  OG  . SER A 1 247 ? -54.479  6.280  9.302   1.00 116.07 ? 247 SER A OG  1 
ATOM   1876 N  N   . LYS A 1 248 ? -57.111  7.275  7.511   1.00 122.15 ? 248 LYS A N   1 
ATOM   1877 C  CA  . LYS A 1 248 ? -58.516  6.947  7.712   1.00 116.58 ? 248 LYS A CA  1 
ATOM   1878 C  C   . LYS A 1 248 ? -58.710  5.988  8.878   1.00 120.27 ? 248 LYS A C   1 
ATOM   1879 O  O   . LYS A 1 248 ? -59.719  6.075  9.586   1.00 121.96 ? 248 LYS A O   1 
ATOM   1880 C  CB  . LYS A 1 248 ? -59.111  6.350  6.435   1.00 101.98 ? 248 LYS A CB  1 
ATOM   1881 N  N   . SER A 1 249 ? -57.754  5.082  9.103   1.00 119.40 ? 249 SER A N   1 
ATOM   1882 C  CA  . SER A 1 249 ? -57.897  4.108  10.180  1.00 118.56 ? 249 SER A CA  1 
ATOM   1883 C  C   . SER A 1 249 ? -57.666  4.736  11.549  1.00 123.63 ? 249 SER A C   1 
ATOM   1884 O  O   . SER A 1 249 ? -58.226  4.264  12.547  1.00 118.69 ? 249 SER A O   1 
ATOM   1885 C  CB  . SER A 1 249 ? -56.936  2.940  9.959   1.00 118.16 ? 249 SER A CB  1 
ATOM   1886 O  OG  . SER A 1 249 ? -57.118  1.936  10.942  1.00 121.70 ? 249 SER A OG  1 
ATOM   1887 N  N   . ARG A 1 250 ? -56.847  5.790  11.624  1.00 121.95 ? 250 ARG A N   1 
ATOM   1888 C  CA  . ARG A 1 250 ? -56.620  6.459  12.901  1.00 115.04 ? 250 ARG A CA  1 
ATOM   1889 C  C   . ARG A 1 250 ? -57.791  7.360  13.276  1.00 116.32 ? 250 ARG A C   1 
ATOM   1890 O  O   . ARG A 1 250 ? -58.198  7.397  14.443  1.00 117.70 ? 250 ARG A O   1 
ATOM   1891 C  CB  . ARG A 1 250 ? -55.322  7.267  12.856  1.00 110.11 ? 250 ARG A CB  1 
ATOM   1892 C  CG  . ARG A 1 250 ? -55.058  8.076  14.120  1.00 105.69 ? 250 ARG A CG  1 
ATOM   1893 C  CD  . ARG A 1 250 ? -53.715  8.785  14.068  1.00 101.12 ? 250 ARG A CD  1 
ATOM   1894 N  N   . SER A 1 251 ? -58.345  8.088  12.304  1.00 114.98 ? 251 SER A N   1 
ATOM   1895 C  CA  . SER A 1 251 ? -59.462  8.980  12.597  1.00 113.62 ? 251 SER A CA  1 
ATOM   1896 C  C   . SER A 1 251 ? -60.716  8.199  12.968  1.00 112.16 ? 251 SER A C   1 
ATOM   1897 O  O   . SER A 1 251 ? -61.487  8.628  13.834  1.00 109.19 ? 251 SER A O   1 
ATOM   1898 C  CB  . SER A 1 251 ? -59.735  9.895  11.401  1.00 113.39 ? 251 SER A CB  1 
ATOM   1899 O  OG  . SER A 1 251 ? -58.678  10.820 11.214  1.00 113.55 ? 251 SER A OG  1 
ATOM   1900 N  N   . VAL A 1 252 ? -60.937  7.048  12.329  1.00 111.79 ? 252 VAL A N   1 
ATOM   1901 C  CA  . VAL A 1 252 ? -62.128  6.255  12.624  1.00 111.74 ? 252 VAL A CA  1 
ATOM   1902 C  C   . VAL A 1 252 ? -62.033  5.638  14.014  1.00 111.04 ? 252 VAL A C   1 
ATOM   1903 O  O   . VAL A 1 252 ? -63.008  5.641  14.775  1.00 107.44 ? 252 VAL A O   1 
ATOM   1904 C  CB  . VAL A 1 252 ? -62.342  5.188  11.535  1.00 109.07 ? 252 VAL A CB  1 
ATOM   1905 C  CG1 . VAL A 1 252 ? -63.332  4.136  12.007  1.00 104.37 ? 252 VAL A CG1 1 
ATOM   1906 C  CG2 . VAL A 1 252 ? -62.839  5.841  10.256  1.00 102.66 ? 252 VAL A CG2 1 
ATOM   1907 N  N   . SER A 1 253 ? -60.862  5.103  14.372  1.00 113.18 ? 253 SER A N   1 
ATOM   1908 C  CA  . SER A 1 253 ? -60.679  4.579  15.722  1.00 113.71 ? 253 SER A CA  1 
ATOM   1909 C  C   . SER A 1 253 ? -60.708  5.693  16.761  1.00 109.63 ? 253 SER A C   1 
ATOM   1910 O  O   . SER A 1 253 ? -61.150  5.471  17.895  1.00 104.29 ? 253 SER A O   1 
ATOM   1911 C  CB  . SER A 1 253 ? -59.369  3.796  15.815  1.00 114.27 ? 253 SER A CB  1 
ATOM   1912 O  OG  . SER A 1 253 ? -58.255  4.629  15.543  1.00 117.11 ? 253 SER A OG  1 
ATOM   1913 N  N   . HIS A 1 254 ? -60.245  6.892  16.397  1.00 106.86 ? 254 HIS A N   1 
ATOM   1914 C  CA  . HIS A 1 254 ? -60.360  8.031  17.301  1.00 106.19 ? 254 HIS A CA  1 
ATOM   1915 C  C   . HIS A 1 254 ? -61.820  8.373  17.565  1.00 105.78 ? 254 HIS A C   1 
ATOM   1916 O  O   . HIS A 1 254 ? -62.193  8.712  18.695  1.00 106.26 ? 254 HIS A O   1 
ATOM   1917 C  CB  . HIS A 1 254 ? -59.623  9.238  16.721  1.00 101.48 ? 254 HIS A CB  1 
ATOM   1918 C  CG  . HIS A 1 254 ? -59.859  10.508 17.476  1.00 100.03 ? 254 HIS A CG  1 
ATOM   1919 N  ND1 . HIS A 1 254 ? -59.283  10.762 18.702  1.00 101.02 ? 254 HIS A ND1 1 
ATOM   1920 C  CD2 . HIS A 1 254 ? -60.614  11.593 17.183  1.00 98.95  ? 254 HIS A CD2 1 
ATOM   1921 C  CE1 . HIS A 1 254 ? -59.670  11.951 19.130  1.00 101.55 ? 254 HIS A CE1 1 
ATOM   1922 N  NE2 . HIS A 1 254 ? -60.478  12.476 18.227  1.00 102.81 ? 254 HIS A NE2 1 
ATOM   1923 N  N   . MET A 1 255 ? -62.664  8.284  16.534  1.00 104.53 ? 255 MET A N   1 
ATOM   1924 C  CA  . MET A 1 255 ? -64.084  8.563  16.715  1.00 100.36 ? 255 MET A CA  1 
ATOM   1925 C  C   . MET A 1 255 ? -64.768  7.484  17.541  1.00 99.43  ? 255 MET A C   1 
ATOM   1926 O  O   . MET A 1 255 ? -65.754  7.767  18.229  1.00 100.33 ? 255 MET A O   1 
ATOM   1927 C  CB  . MET A 1 255 ? -64.766  8.712  15.356  1.00 93.99  ? 255 MET A CB  1 
ATOM   1928 C  CG  . MET A 1 255 ? -64.318  9.940  14.588  1.00 97.20  ? 255 MET A CG  1 
ATOM   1929 S  SD  . MET A 1 255 ? -64.900  9.955  12.887  1.00 92.87  ? 255 MET A SD  1 
ATOM   1930 C  CE  . MET A 1 255 ? -66.673  9.987  13.124  1.00 90.33  ? 255 MET A CE  1 
ATOM   1931 N  N   . GLN A 1 256 ? -64.268  6.246  17.484  1.00 102.63 ? 256 GLN A N   1 
ATOM   1932 C  CA  . GLN A 1 256 ? -64.787  5.204  18.363  1.00 100.77 ? 256 GLN A CA  1 
ATOM   1933 C  C   . GLN A 1 256 ? -64.428  5.490  19.814  1.00 99.94  ? 256 GLN A C   1 
ATOM   1934 O  O   . GLN A 1 256 ? -65.236  5.254  20.719  1.00 93.96  ? 256 GLN A O   1 
ATOM   1935 C  CB  . GLN A 1 256 ? -64.251  3.837  17.945  1.00 104.54 ? 256 GLN A CB  1 
ATOM   1936 C  CG  . GLN A 1 256 ? -64.598  3.431  16.527  1.00 112.42 ? 256 GLN A CG  1 
ATOM   1937 C  CD  . GLN A 1 256 ? -64.155  2.019  16.209  1.00 117.59 ? 256 GLN A CD  1 
ATOM   1938 O  OE1 . GLN A 1 256 ? -62.960  1.728  16.157  1.00 119.28 ? 256 GLN A OE1 1 
ATOM   1939 N  NE2 . GLN A 1 256 ? -65.119  1.128  16.003  1.00 115.09 ? 256 GLN A NE2 1 
ATOM   1940 N  N   . ASN A 1 257 ? -63.216  5.994  20.055  1.00 101.37 ? 257 ASN A N   1 
ATOM   1941 C  CA  . ASN A 1 257 ? -62.827  6.353  21.413  1.00 97.67  ? 257 ASN A CA  1 
ATOM   1942 C  C   . ASN A 1 257 ? -63.642  7.533  21.923  1.00 95.06  ? 257 ASN A C   1 
ATOM   1943 O  O   . ASN A 1 257 ? -63.991  7.588  23.108  1.00 98.69  ? 257 ASN A O   1 
ATOM   1944 C  CB  . ASN A 1 257 ? -61.332  6.670  21.470  1.00 105.77 ? 257 ASN A CB  1 
ATOM   1945 C  CG  . ASN A 1 257 ? -60.466  5.479  21.106  1.00 111.70 ? 257 ASN A CG  1 
ATOM   1946 O  OD1 . ASN A 1 257 ? -60.920  4.334  21.137  1.00 104.38 ? 257 ASN A OD1 1 
ATOM   1947 N  ND2 . ASN A 1 257 ? -59.209  5.743  20.766  1.00 110.06 ? 257 ASN A ND2 1 
ATOM   1948 N  N   . GLU A 1 258 ? -63.960  8.485  21.043  1.00 93.79  ? 258 GLU A N   1 
ATOM   1949 C  CA  . GLU A 1 258 ? -64.717  9.658  21.466  1.00 91.38  ? 258 GLU A CA  1 
ATOM   1950 C  C   . GLU A 1 258 ? -66.148  9.287  21.837  1.00 87.71  ? 258 GLU A C   1 
ATOM   1951 O  O   . GLU A 1 258 ? -66.657  9.712  22.879  1.00 85.93  ? 258 GLU A O   1 
ATOM   1952 C  CB  . GLU A 1 258 ? -64.691  10.725 20.371  1.00 95.68  ? 258 GLU A CB  1 
ATOM   1953 C  CG  . GLU A 1 258 ? -63.327  11.377 20.177  1.00 92.89  ? 258 GLU A CG  1 
ATOM   1954 C  CD  . GLU A 1 258 ? -62.865  12.155 21.398  1.00 101.79 ? 258 GLU A CD  1 
ATOM   1955 O  OE1 . GLU A 1 258 ? -63.719  12.747 22.092  1.00 103.39 ? 258 GLU A OE1 1 
ATOM   1956 O  OE2 . GLU A 1 258 ? -61.645  12.172 21.667  1.00 102.78 ? 258 GLU A OE2 1 
ATOM   1957 N  N   . VAL A 1 259 ? -66.814  8.486  21.002  1.00 88.61  ? 259 VAL A N   1 
ATOM   1958 C  CA  . VAL A 1 259 ? -68.147  8.021  21.371  1.00 89.93  ? 259 VAL A CA  1 
ATOM   1959 C  C   . VAL A 1 259 ? -68.065  7.101  22.583  1.00 89.39  ? 259 VAL A C   1 
ATOM   1960 O  O   . VAL A 1 259 ? -69.015  7.009  23.370  1.00 89.22  ? 259 VAL A O   1 
ATOM   1961 C  CB  . VAL A 1 259 ? -68.830  7.338  20.169  1.00 89.34  ? 259 VAL A CB  1 
ATOM   1962 C  CG1 . VAL A 1 259 ? -68.059  6.121  19.749  1.00 97.31  ? 259 VAL A CG1 1 
ATOM   1963 C  CG2 . VAL A 1 259 ? -70.267  6.965  20.500  1.00 89.82  ? 259 VAL A CG2 1 
ATOM   1964 N  N   . ARG A 1 260 ? -66.926  6.429  22.767  1.00 94.62  ? 260 ARG A N   1 
ATOM   1965 C  CA  . ARG A 1 260 ? -66.708  5.628  23.968  1.00 90.11  ? 260 ARG A CA  1 
ATOM   1966 C  C   . ARG A 1 260 ? -66.632  6.513  25.206  1.00 89.23  ? 260 ARG A C   1 
ATOM   1967 O  O   . ARG A 1 260 ? -67.330  6.273  26.198  1.00 88.63  ? 260 ARG A O   1 
ATOM   1968 C  CB  . ARG A 1 260 ? -65.427  4.804  23.813  1.00 94.56  ? 260 ARG A CB  1 
ATOM   1969 C  CG  . ARG A 1 260 ? -65.052  3.960  25.017  1.00 101.40 ? 260 ARG A CG  1 
ATOM   1970 C  CD  . ARG A 1 260 ? -66.165  2.998  25.358  1.00 108.60 ? 260 ARG A CD  1 
ATOM   1971 N  NE  . ARG A 1 260 ? -65.694  1.810  26.060  1.00 113.62 ? 260 ARG A NE  1 
ATOM   1972 C  CZ  . ARG A 1 260 ? -65.445  0.646  25.475  1.00 112.11 ? 260 ARG A CZ  1 
ATOM   1973 N  NH1 . ARG A 1 260 ? -65.600  0.480  24.172  1.00 108.47 ? 260 ARG A NH1 1 
ATOM   1974 N  NH2 . ARG A 1 260 ? -65.034  -0.379 26.217  1.00 111.39 ? 260 ARG A NH2 1 
ATOM   1975 N  N   . ALA A 1 261 ? -65.796  7.552  25.157  1.00 83.83  ? 261 ALA A N   1 
ATOM   1976 C  CA  . ALA A 1 261 ? -65.617  8.419  26.317  1.00 83.27  ? 261 ALA A CA  1 
ATOM   1977 C  C   . ALA A 1 261 ? -66.878  9.220  26.621  1.00 85.42  ? 261 ALA A C   1 
ATOM   1978 O  O   . ALA A 1 261 ? -67.194  9.468  27.790  1.00 80.95  ? 261 ALA A O   1 
ATOM   1979 C  CB  . ALA A 1 261 ? -64.430  9.355  26.091  1.00 80.63  ? 261 ALA A CB  1 
ATOM   1980 N  N   . ARG A 1 262 ? -67.613  9.633  25.584  1.00 85.93  ? 262 ARG A N   1 
ATOM   1981 C  CA  . ARG A 1 262 ? -68.794  10.460 25.809  1.00 82.77  ? 262 ARG A CA  1 
ATOM   1982 C  C   . ARG A 1 262 ? -69.919  9.660  26.454  1.00 81.58  ? 262 ARG A C   1 
ATOM   1983 O  O   . ARG A 1 262 ? -70.671  10.192 27.279  1.00 79.88  ? 262 ARG A O   1 
ATOM   1984 C  CB  . ARG A 1 262 ? -69.262  11.089 24.496  1.00 79.15  ? 262 ARG A CB  1 
ATOM   1985 C  CG  . ARG A 1 262 ? -68.284  12.098 23.930  1.00 81.99  ? 262 ARG A CG  1 
ATOM   1986 C  CD  . ARG A 1 262 ? -68.910  12.952 22.842  1.00 85.92  ? 262 ARG A CD  1 
ATOM   1987 N  NE  . ARG A 1 262 ? -67.895  13.646 22.056  1.00 88.81  ? 262 ARG A NE  1 
ATOM   1988 C  CZ  . ARG A 1 262 ? -67.174  14.671 22.492  1.00 100.58 ? 262 ARG A CZ  1 
ATOM   1989 N  NH1 . ARG A 1 262 ? -67.315  15.146 23.721  1.00 86.02  ? 262 ARG A NH1 1 
ATOM   1990 N  NH2 . ARG A 1 262 ? -66.284  15.230 21.676  1.00 98.72  ? 262 ARG A NH2 1 
ATOM   1991 N  N   . LEU A 1 263 ? -70.048  8.381  26.100  1.00 82.63  ? 263 LEU A N   1 
ATOM   1992 C  CA  . LEU A 1 263 ? -71.116  7.576  26.682  1.00 82.70  ? 263 LEU A CA  1 
ATOM   1993 C  C   . LEU A 1 263 ? -70.807  7.186  28.121  1.00 84.30  ? 263 LEU A C   1 
ATOM   1994 O  O   . LEU A 1 263 ? -71.731  6.987  28.919  1.00 83.82  ? 263 LEU A O   1 
ATOM   1995 C  CB  . LEU A 1 263 ? -71.369  6.342  25.821  1.00 86.41  ? 263 LEU A CB  1 
ATOM   1996 C  CG  . LEU A 1 263 ? -72.594  6.545  24.929  1.00 86.32  ? 263 LEU A CG  1 
ATOM   1997 C  CD1 . LEU A 1 263 ? -72.544  5.658  23.711  1.00 87.52  ? 263 LEU A CD1 1 
ATOM   1998 C  CD2 . LEU A 1 263 ? -73.861  6.287  25.729  1.00 84.69  ? 263 LEU A CD2 1 
ATOM   1999 N  N   . GLU A 1 264 ? -69.527  7.079  28.476  1.00 84.22  ? 264 GLU A N   1 
ATOM   2000 C  CA  . GLU A 1 264 ? -69.180  6.884  29.878  1.00 80.67  ? 264 GLU A CA  1 
ATOM   2001 C  C   . GLU A 1 264 ? -69.397  8.164  30.674  1.00 81.55  ? 264 GLU A C   1 
ATOM   2002 O  O   . GLU A 1 264 ? -69.896  8.122  31.806  1.00 85.81  ? 264 GLU A O   1 
ATOM   2003 C  CB  . GLU A 1 264 ? -67.738  6.397  30.000  1.00 84.27  ? 264 GLU A CB  1 
ATOM   2004 C  CG  . GLU A 1 264 ? -67.530  4.990  29.459  1.00 94.09  ? 264 GLU A CG  1 
ATOM   2005 C  CD  . GLU A 1 264 ? -66.098  4.511  29.596  1.00 105.28 ? 264 GLU A CD  1 
ATOM   2006 O  OE1 . GLU A 1 264 ? -65.291  5.215  30.239  1.00 103.57 ? 264 GLU A OE1 1 
ATOM   2007 O  OE2 . GLU A 1 264 ? -65.779  3.429  29.058  1.00 113.91 ? 264 GLU A OE2 1 
ATOM   2008 N  N   . GLN A 1 265 ? -69.036  9.314  30.097  1.00 81.48  ? 265 GLN A N   1 
ATOM   2009 C  CA  . GLN A 1 265 ? -69.367  10.588 30.727  1.00 78.61  ? 265 GLN A CA  1 
ATOM   2010 C  C   . GLN A 1 265 ? -70.872  10.790 30.808  1.00 76.71  ? 265 GLN A C   1 
ATOM   2011 O  O   . GLN A 1 265 ? -71.362  11.444 31.735  1.00 75.88  ? 265 GLN A O   1 
ATOM   2012 C  CB  . GLN A 1 265 ? -68.729  11.748 29.963  1.00 76.18  ? 265 GLN A CB  1 
ATOM   2013 C  CG  . GLN A 1 265 ? -67.217  11.788 30.013  1.00 79.64  ? 265 GLN A CG  1 
ATOM   2014 C  CD  . GLN A 1 265 ? -66.652  12.956 29.229  1.00 82.91  ? 265 GLN A CD  1 
ATOM   2015 O  OE1 . GLN A 1 265 ? -66.655  14.095 29.699  1.00 82.36  ? 265 GLN A OE1 1 
ATOM   2016 N  NE2 . GLN A 1 265 ? -66.169  12.680 28.022  1.00 76.77  ? 265 GLN A NE2 1 
ATOM   2017 N  N   . TYR A 1 266 ? -71.621  10.246 29.846  1.00 77.11  ? 266 TYR A N   1 
ATOM   2018 C  CA  . TYR A 1 266 ? -73.074  10.363 29.899  1.00 77.37  ? 266 TYR A CA  1 
ATOM   2019 C  C   . TYR A 1 266 ? -73.640  9.614  31.098  1.00 73.73  ? 266 TYR A C   1 
ATOM   2020 O  O   . TYR A 1 266 ? -74.615  10.062 31.714  1.00 74.29  ? 266 TYR A O   1 
ATOM   2021 C  CB  . TYR A 1 266 ? -73.701  9.848  28.604  1.00 69.94  ? 266 TYR A CB  1 
ATOM   2022 C  CG  . TYR A 1 266 ? -75.199  9.741  28.707  1.00 65.70  ? 266 TYR A CG  1 
ATOM   2023 C  CD1 . TYR A 1 266 ? -75.999  10.867 28.589  1.00 69.20  ? 266 TYR A CD1 1 
ATOM   2024 C  CD2 . TYR A 1 266 ? -75.813  8.521  28.954  1.00 69.00  ? 266 TYR A CD2 1 
ATOM   2025 C  CE1 . TYR A 1 266 ? -77.370  10.780 28.701  1.00 71.58  ? 266 TYR A CE1 1 
ATOM   2026 C  CE2 . TYR A 1 266 ? -77.184  8.424  29.070  1.00 71.16  ? 266 TYR A CE2 1 
ATOM   2027 C  CZ  . TYR A 1 266 ? -77.959  9.557  28.944  1.00 73.67  ? 266 TYR A CZ  1 
ATOM   2028 O  OH  . TYR A 1 266 ? -79.327  9.468  29.056  1.00 78.03  ? 266 TYR A OH  1 
ATOM   2029 N  N   . LEU A 1 267 ? -73.050  8.467  31.436  1.00 77.95  ? 267 LEU A N   1 
ATOM   2030 C  CA  . LEU A 1 267 ? -73.494  7.734  32.615  1.00 73.83  ? 267 LEU A CA  1 
ATOM   2031 C  C   . LEU A 1 267 ? -73.199  8.517  33.886  1.00 72.24  ? 267 LEU A C   1 
ATOM   2032 O  O   . LEU A 1 267 ? -74.046  8.592  34.783  1.00 72.57  ? 267 LEU A O   1 
ATOM   2033 C  CB  . LEU A 1 267 ? -72.829  6.360  32.656  1.00 70.73  ? 267 LEU A CB  1 
ATOM   2034 C  CG  . LEU A 1 267 ? -73.150  5.440  31.477  1.00 78.53  ? 267 LEU A CG  1 
ATOM   2035 C  CD1 . LEU A 1 267 ? -72.245  4.217  31.487  1.00 72.71  ? 267 LEU A CD1 1 
ATOM   2036 C  CD2 . LEU A 1 267 ? -74.618  5.033  31.500  1.00 70.60  ? 267 LEU A CD2 1 
ATOM   2037 N  N   . LEU A 1 268 ? -72.004  9.112  33.973  1.00 73.23  ? 268 LEU A N   1 
ATOM   2038 C  CA  . LEU A 1 268 ? -71.669  9.968  35.108  1.00 73.24  ? 268 LEU A CA  1 
ATOM   2039 C  C   . LEU A 1 268 ? -72.720  11.047 35.318  1.00 80.06  ? 268 LEU A C   1 
ATOM   2040 O  O   . LEU A 1 268 ? -73.119  11.328 36.455  1.00 73.00  ? 268 LEU A O   1 
ATOM   2041 C  CB  . LEU A 1 268 ? -70.301  10.617 34.896  1.00 71.74  ? 268 LEU A CB  1 
ATOM   2042 C  CG  . LEU A 1 268 ? -69.065  9.724  34.881  1.00 80.80  ? 268 LEU A CG  1 
ATOM   2043 C  CD1 . LEU A 1 268 ? -67.814  10.578 34.754  1.00 83.02  ? 268 LEU A CD1 1 
ATOM   2044 C  CD2 . LEU A 1 268 ? -69.020  8.882  36.139  1.00 82.84  ? 268 LEU A CD2 1 
ATOM   2045 N  N   . LEU A 1 269 ? -73.182  11.665 34.228  1.00 70.49  ? 269 LEU A N   1 
ATOM   2046 C  CA  . LEU A 1 269 ? -74.145  12.751 34.345  1.00 67.22  ? 269 LEU A CA  1 
ATOM   2047 C  C   . LEU A 1 269 ? -75.523  12.241 34.743  1.00 69.89  ? 269 LEU A C   1 
ATOM   2048 O  O   . LEU A 1 269 ? -76.257  12.936 35.454  1.00 71.55  ? 269 LEU A O   1 
ATOM   2049 C  CB  . LEU A 1 269 ? -74.211  13.527 33.031  1.00 76.55  ? 269 LEU A CB  1 
ATOM   2050 C  CG  . LEU A 1 269 ? -72.886  14.141 32.575  1.00 75.17  ? 269 LEU A CG  1 
ATOM   2051 C  CD1 . LEU A 1 269 ? -73.000  14.708 31.175  1.00 64.51  ? 269 LEU A CD1 1 
ATOM   2052 C  CD2 . LEU A 1 269 ? -72.429  15.211 33.555  1.00 76.37  ? 269 LEU A CD2 1 
ATOM   2053 N  N   . GLU A 1 270 ? -75.892  11.036 34.303  1.00 71.23  ? 270 GLU A N   1 
ATOM   2054 C  CA  . GLU A 1 270 ? -77.167  10.466 34.725  1.00 73.03  ? 270 GLU A CA  1 
ATOM   2055 C  C   . GLU A 1 270 ? -77.218  10.266 36.232  1.00 68.93  ? 270 GLU A C   1 
ATOM   2056 O  O   . GLU A 1 270 ? -78.284  10.417 36.843  1.00 66.13  ? 270 GLU A O   1 
ATOM   2057 C  CB  . GLU A 1 270 ? -77.419  9.139  34.011  1.00 72.84  ? 270 GLU A CB  1 
ATOM   2058 C  CG  . GLU A 1 270 ? -78.115  9.269  32.676  1.00 76.18  ? 270 GLU A CG  1 
ATOM   2059 C  CD  . GLU A 1 270 ? -78.557  7.927  32.125  1.00 80.19  ? 270 GLU A CD  1 
ATOM   2060 O  OE1 . GLU A 1 270 ? -78.078  6.889  32.629  1.00 82.43  ? 270 GLU A OE1 1 
ATOM   2061 O  OE2 . GLU A 1 270 ? -79.385  7.911  31.190  1.00 78.23  ? 270 GLU A OE2 1 
ATOM   2062 N  N   . SER A 1 271 ? -76.084  9.927  36.848  1.00 66.53  ? 271 SER A N   1 
ATOM   2063 C  CA  . SER A 1 271 ? -76.054  9.732  38.292  1.00 74.89  ? 271 SER A CA  1 
ATOM   2064 C  C   . SER A 1 271 ? -76.140  11.048 39.053  1.00 70.42  ? 271 SER A C   1 
ATOM   2065 O  O   . SER A 1 271 ? -76.462  11.038 40.245  1.00 77.76  ? 271 SER A O   1 
ATOM   2066 C  CB  . SER A 1 271 ? -74.789  8.975  38.696  1.00 69.47  ? 271 SER A CB  1 
ATOM   2067 O  OG  . SER A 1 271 ? -73.636  9.775  38.511  1.00 78.17  ? 271 SER A OG  1 
ATOM   2068 N  N   . CYS A 1 272 ? -75.862  12.175 38.397  1.00 71.58  ? 272 CYS A N   1 
ATOM   2069 C  CA  . CYS A 1 272 ? -75.983  13.481 39.031  1.00 68.65  ? 272 CYS A CA  1 
ATOM   2070 C  C   . CYS A 1 272 ? -77.414  14.000 39.054  1.00 67.19  ? 272 CYS A C   1 
ATOM   2071 O  O   . CYS A 1 272 ? -77.689  14.970 39.769  1.00 68.83  ? 272 CYS A O   1 
ATOM   2072 C  CB  . CYS A 1 272 ? -75.091  14.501 38.317  1.00 68.52  ? 272 CYS A CB  1 
ATOM   2073 S  SG  . CYS A 1 272 ? -73.328  14.103 38.312  1.00 84.85  ? 272 CYS A SG  1 
ATOM   2074 N  N   . LEU A 1 273 ? -78.323  13.383 38.300  1.00 67.16  ? 273 LEU A N   1 
ATOM   2075 C  CA  . LEU A 1 273 ? -79.677  13.921 38.187  1.00 70.11  ? 273 LEU A CA  1 
ATOM   2076 C  C   . LEU A 1 273 ? -80.438  13.961 39.507  1.00 70.82  ? 273 LEU A C   1 
ATOM   2077 O  O   . LEU A 1 273 ? -81.153  14.954 39.734  1.00 72.38  ? 273 LEU A O   1 
ATOM   2078 C  CB  . LEU A 1 273 ? -80.467  13.135 37.130  1.00 68.00  ? 273 LEU A CB  1 
ATOM   2079 C  CG  . LEU A 1 273 ? -80.000  13.300 35.682  1.00 70.24  ? 273 LEU A CG  1 
ATOM   2080 C  CD1 . LEU A 1 273 ? -80.989  12.654 34.723  1.00 71.68  ? 273 LEU A CD1 1 
ATOM   2081 C  CD2 . LEU A 1 273 ? -79.795  14.770 35.344  1.00 64.97  ? 273 LEU A CD2 1 
ATOM   2082 N  N   . PRO A 1 274 ? -80.365  12.954 40.394  1.00 75.54  ? 274 PRO A N   1 
ATOM   2083 C  CA  . PRO A 1 274 ? -81.016  13.110 41.712  1.00 73.47  ? 274 PRO A CA  1 
ATOM   2084 C  C   . PRO A 1 274 ? -80.597  14.373 42.447  1.00 66.30  ? 274 PRO A C   1 
ATOM   2085 O  O   . PRO A 1 274 ? -81.452  15.096 42.975  1.00 61.55  ? 274 PRO A O   1 
ATOM   2086 C  CB  . PRO A 1 274 ? -80.589  11.839 42.457  1.00 67.97  ? 274 PRO A CB  1 
ATOM   2087 C  CG  . PRO A 1 274 ? -80.399  10.833 41.383  1.00 73.69  ? 274 PRO A CG  1 
ATOM   2088 C  CD  . PRO A 1 274 ? -79.838  11.587 40.210  1.00 67.57  ? 274 PRO A CD  1 
ATOM   2089 N  N   . LYS A 1 275 ? -79.295  14.668 42.482  1.00 65.28  ? 275 LYS A N   1 
ATOM   2090 C  CA  . LYS A 1 275 ? -78.838  15.905 43.106  1.00 70.82  ? 275 LYS A CA  1 
ATOM   2091 C  C   . LYS A 1 275 ? -79.301  17.128 42.320  1.00 73.90  ? 275 LYS A C   1 
ATOM   2092 O  O   . LYS A 1 275 ? -79.654  18.154 42.913  1.00 64.88  ? 275 LYS A O   1 
ATOM   2093 C  CB  . LYS A 1 275 ? -77.315  15.895 43.242  1.00 76.68  ? 275 LYS A CB  1 
ATOM   2094 C  CG  . LYS A 1 275 ? -76.761  14.704 44.013  1.00 85.04  ? 275 LYS A CG  1 
ATOM   2095 C  CD  . LYS A 1 275 ? -75.388  15.013 44.599  1.00 91.65  ? 275 LYS A CD  1 
ATOM   2096 C  CE  . LYS A 1 275 ? -74.778  13.799 45.294  1.00 86.31  ? 275 LYS A CE  1 
ATOM   2097 N  NZ  . LYS A 1 275 ? -74.373  12.740 44.322  1.00 96.07  ? 275 LYS A NZ  1 
ATOM   2098 N  N   . VAL A 1 276 ? -79.310  17.036 40.984  1.00 72.13  ? 276 VAL A N   1 
ATOM   2099 C  CA  . VAL A 1 276 ? -79.760  18.154 40.154  1.00 68.87  ? 276 VAL A CA  1 
ATOM   2100 C  C   . VAL A 1 276 ? -81.208  18.508 40.471  1.00 68.82  ? 276 VAL A C   1 
ATOM   2101 O  O   . VAL A 1 276 ? -81.579  19.688 40.517  1.00 65.57  ? 276 VAL A O   1 
ATOM   2102 C  CB  . VAL A 1 276 ? -79.570  17.825 38.660  1.00 72.69  ? 276 VAL A CB  1 
ATOM   2103 C  CG1 . VAL A 1 276 ? -80.323  18.824 37.786  1.00 67.72  ? 276 VAL A CG1 1 
ATOM   2104 C  CG2 . VAL A 1 276 ? -78.093  17.820 38.297  1.00 67.34  ? 276 VAL A CG2 1 
ATOM   2105 N  N   . GLY A 1 277 ? -82.045  17.495 40.705  1.00 67.99  ? 277 GLY A N   1 
ATOM   2106 C  CA  . GLY A 1 277 ? -83.439  17.760 41.025  1.00 68.13  ? 277 GLY A CA  1 
ATOM   2107 C  C   . GLY A 1 277 ? -83.620  18.448 42.365  1.00 77.41  ? 277 GLY A C   1 
ATOM   2108 O  O   . GLY A 1 277 ? -84.492  19.310 42.518  1.00 76.92  ? 277 GLY A O   1 
ATOM   2109 N  N   . GLU A 1 278 ? -82.807  18.075 43.358  1.00 71.18  ? 278 GLU A N   1 
ATOM   2110 C  CA  . GLU A 1 278 ? -82.863  18.761 44.644  1.00 76.06  ? 278 GLU A CA  1 
ATOM   2111 C  C   . GLU A 1 278 ? -82.428  20.214 44.505  1.00 72.40  ? 278 GLU A C   1 
ATOM   2112 O  O   . GLU A 1 278 ? -82.972  21.100 45.176  1.00 75.73  ? 278 GLU A O   1 
ATOM   2113 C  CB  . GLU A 1 278 ? -81.992  18.034 45.671  1.00 68.34  ? 278 GLU A CB  1 
ATOM   2114 N  N   . ILE A 1 279 ? -81.450  20.476 43.634  1.00 66.85  ? 279 ILE A N   1 
ATOM   2115 C  CA  . ILE A 1 279 ? -80.970  21.840 43.421  1.00 65.97  ? 279 ILE A CA  1 
ATOM   2116 C  C   . ILE A 1 279 ? -82.088  22.722 42.877  1.00 68.08  ? 279 ILE A C   1 
ATOM   2117 O  O   . ILE A 1 279 ? -82.217  23.893 43.257  1.00 65.06  ? 279 ILE A O   1 
ATOM   2118 C  CB  . ILE A 1 279 ? -79.745  21.828 42.487  1.00 69.20  ? 279 ILE A CB  1 
ATOM   2119 C  CG1 . ILE A 1 279 ? -78.561  21.151 43.177  1.00 66.86  ? 279 ILE A CG1 1 
ATOM   2120 C  CG2 . ILE A 1 279 ? -79.380  23.237 42.049  1.00 66.17  ? 279 ILE A CG2 1 
ATOM   2121 C  CD1 . ILE A 1 279 ? -77.415  20.807 42.242  1.00 64.61  ? 279 ILE A CD1 1 
ATOM   2122 N  N   . TYR A 1 280 ? -82.918  22.177 41.989  1.00 69.43  ? 280 TYR A N   1 
ATOM   2123 C  CA  . TYR A 1 280 ? -84.045  22.907 41.426  1.00 72.77  ? 280 TYR A CA  1 
ATOM   2124 C  C   . TYR A 1 280 ? -85.345  22.638 42.168  1.00 72.66  ? 280 TYR A C   1 
ATOM   2125 O  O   . TYR A 1 280 ? -86.413  23.025 41.681  1.00 70.76  ? 280 TYR A O   1 
ATOM   2126 C  CB  . TYR A 1 280 ? -84.207  22.574 39.940  1.00 70.00  ? 280 TYR A CB  1 
ATOM   2127 C  CG  . TYR A 1 280 ? -83.116  23.168 39.080  1.00 70.00  ? 280 TYR A CG  1 
ATOM   2128 C  CD1 . TYR A 1 280 ? -83.206  24.475 38.619  1.00 68.44  ? 280 TYR A CD1 1 
ATOM   2129 C  CD2 . TYR A 1 280 ? -81.990  22.428 38.744  1.00 65.83  ? 280 TYR A CD2 1 
ATOM   2130 C  CE1 . TYR A 1 280 ? -82.207  25.028 37.843  1.00 67.36  ? 280 TYR A CE1 1 
ATOM   2131 C  CE2 . TYR A 1 280 ? -80.986  22.972 37.967  1.00 64.14  ? 280 TYR A CE2 1 
ATOM   2132 C  CZ  . TYR A 1 280 ? -81.100  24.271 37.521  1.00 62.33  ? 280 TYR A CZ  1 
ATOM   2133 O  OH  . TYR A 1 280 ? -80.105  24.817 36.748  1.00 69.41  ? 280 TYR A OH  1 
ATOM   2134 N  N   . GLN A 1 281 ? -85.275  21.980 43.328  1.00 72.87  ? 281 GLN A N   1 
ATOM   2135 C  CA  . GLN A 1 281 ? -86.428  21.755 44.204  1.00 76.73  ? 281 GLN A CA  1 
ATOM   2136 C  C   . GLN A 1 281 ? -87.595  21.125 43.448  1.00 73.01  ? 281 GLN A C   1 
ATOM   2137 O  O   . GLN A 1 281 ? -88.738  21.580 43.526  1.00 72.29  ? 281 GLN A O   1 
ATOM   2138 C  CB  . GLN A 1 281 ? -86.859  23.054 44.884  1.00 73.12  ? 281 GLN A CB  1 
ATOM   2139 C  CG  . GLN A 1 281 ? -85.838  23.611 45.860  1.00 77.91  ? 281 GLN A CG  1 
ATOM   2140 C  CD  . GLN A 1 281 ? -86.411  24.707 46.738  1.00 93.87  ? 281 GLN A CD  1 
ATOM   2141 O  OE1 . GLN A 1 281 ? -86.999  25.671 46.247  1.00 89.80  ? 281 GLN A OE1 1 
ATOM   2142 N  NE2 . GLN A 1 281 ? -86.251  24.558 48.049  1.00 103.73 ? 281 GLN A NE2 1 
ATOM   2143 N  N   . LEU A 1 282 ? -87.296  20.061 42.706  1.00 67.02  ? 282 LEU A N   1 
ATOM   2144 C  CA  . LEU A 1 282 ? -88.330  19.354 41.963  1.00 72.70  ? 282 LEU A CA  1 
ATOM   2145 C  C   . LEU A 1 282 ? -89.243  18.592 42.914  1.00 75.58  ? 282 LEU A C   1 
ATOM   2146 O  O   . LEU A 1 282 ? -88.771  17.879 43.806  1.00 79.47  ? 282 LEU A O   1 
ATOM   2147 C  CB  . LEU A 1 282 ? -87.703  18.383 40.962  1.00 73.66  ? 282 LEU A CB  1 
ATOM   2148 C  CG  . LEU A 1 282 ? -86.754  18.924 39.893  1.00 73.89  ? 282 LEU A CG  1 
ATOM   2149 C  CD1 . LEU A 1 282 ? -86.333  17.802 38.958  1.00 71.89  ? 282 LEU A CD1 1 
ATOM   2150 C  CD2 . LEU A 1 282 ? -87.399  20.054 39.117  1.00 65.42  ? 282 LEU A CD2 1 
ATOM   2151 N  N   . ASP A 1 283 ? -90.553  18.742 42.726  1.00 74.61  ? 283 ASP A N   1 
ATOM   2152 C  CA  . ASP A 1 283 ? -91.496  17.878 43.416  1.00 81.63  ? 283 ASP A CA  1 
ATOM   2153 C  C   . ASP A 1 283 ? -91.524  16.508 42.742  1.00 82.89  ? 283 ASP A C   1 
ATOM   2154 O  O   . ASP A 1 283 ? -90.945  16.305 41.673  1.00 82.76  ? 283 ASP A O   1 
ATOM   2155 C  CB  . ASP A 1 283 ? -92.890  18.508 43.448  1.00 82.16  ? 283 ASP A CB  1 
ATOM   2156 C  CG  . ASP A 1 283 ? -93.512  18.634 42.073  1.00 88.21  ? 283 ASP A CG  1 
ATOM   2157 O  OD1 . ASP A 1 283 ? -93.973  17.609 41.529  1.00 91.90  ? 283 ASP A OD1 1 
ATOM   2158 O  OD2 . ASP A 1 283 ? -93.554  19.763 41.540  1.00 97.07  ? 283 ASP A OD2 1 
ATOM   2159 N  N   . THR A 1 284 ? -92.221  15.559 43.376  1.00 85.75  ? 284 THR A N   1 
ATOM   2160 C  CA  . THR A 1 284 ? -92.165  14.170 42.923  1.00 86.38  ? 284 THR A CA  1 
ATOM   2161 C  C   . THR A 1 284 ? -92.632  14.025 41.479  1.00 79.60  ? 284 THR A C   1 
ATOM   2162 O  O   . THR A 1 284 ? -92.085  13.212 40.726  1.00 80.71  ? 284 THR A O   1 
ATOM   2163 C  CB  . THR A 1 284 ? -92.998  13.274 43.841  1.00 82.94  ? 284 THR A CB  1 
ATOM   2164 O  OG1 . THR A 1 284 ? -94.308  13.831 44.000  1.00 90.73  ? 284 THR A OG1 1 
ATOM   2165 C  CG2 . THR A 1 284 ? -92.332  13.136 45.198  1.00 79.28  ? 284 THR A CG2 1 
ATOM   2166 N  N   . ALA A 1 285 ? -93.640  14.801 41.072  1.00 78.48  ? 285 ALA A N   1 
ATOM   2167 C  CA  . ALA A 1 285 ? -94.103  14.734 39.688  1.00 72.24  ? 285 ALA A CA  1 
ATOM   2168 C  C   . ALA A 1 285 ? -93.019  15.199 38.724  1.00 79.85  ? 285 ALA A C   1 
ATOM   2169 O  O   . ALA A 1 285 ? -92.795  14.575 37.679  1.00 79.89  ? 285 ALA A O   1 
ATOM   2170 C  CB  . ALA A 1 285 ? -95.372  15.565 39.513  1.00 71.89  ? 285 ALA A CB  1 
ATOM   2171 N  N   . GLU A 1 286 ? -92.333  16.294 39.060  1.00 76.35  ? 286 GLU A N   1 
ATOM   2172 C  CA  . GLU A 1 286 ? -91.224  16.755 38.233  1.00 72.36  ? 286 GLU A CA  1 
ATOM   2173 C  C   . GLU A 1 286 ? -90.078  15.750 38.238  1.00 73.17  ? 286 GLU A C   1 
ATOM   2174 O  O   . GLU A 1 286 ? -89.404  15.564 37.218  1.00 75.12  ? 286 GLU A O   1 
ATOM   2175 C  CB  . GLU A 1 286 ? -90.745  18.123 38.717  1.00 74.51  ? 286 GLU A CB  1 
ATOM   2176 C  CG  . GLU A 1 286 ? -91.820  19.199 38.689  1.00 75.52  ? 286 GLU A CG  1 
ATOM   2177 C  CD  . GLU A 1 286 ? -91.286  20.572 39.050  1.00 78.73  ? 286 GLU A CD  1 
ATOM   2178 O  OE1 . GLU A 1 286 ? -90.433  20.663 39.957  1.00 80.13  ? 286 GLU A OE1 1 
ATOM   2179 O  OE2 . GLU A 1 286 ? -91.712  21.563 38.422  1.00 79.37  ? 286 GLU A OE2 1 
ATOM   2180 N  N   . ARG A 1 287 ? -89.840  15.096 39.380  1.00 77.06  ? 287 ARG A N   1 
ATOM   2181 C  CA  . ARG A 1 287 ? -88.827  14.046 39.435  1.00 78.53  ? 287 ARG A CA  1 
ATOM   2182 C  C   . ARG A 1 287 ? -89.142  12.936 38.440  1.00 74.01  ? 287 ARG A C   1 
ATOM   2183 O  O   . ARG A 1 287 ? -88.237  12.390 37.798  1.00 66.10  ? 287 ARG A O   1 
ATOM   2184 C  CB  . ARG A 1 287 ? -88.725  13.471 40.853  1.00 76.98  ? 287 ARG A CB  1 
ATOM   2185 C  CG  . ARG A 1 287 ? -88.551  14.499 41.969  1.00 87.94  ? 287 ARG A CG  1 
ATOM   2186 C  CD  . ARG A 1 287 ? -87.092  14.800 42.281  1.00 92.73  ? 287 ARG A CD  1 
ATOM   2187 N  NE  . ARG A 1 287 ? -86.485  13.779 43.127  1.00 93.07  ? 287 ARG A NE  1 
ATOM   2188 C  CZ  . ARG A 1 287 ? -85.237  13.823 43.576  1.00 91.49  ? 287 ARG A CZ  1 
ATOM   2189 N  NH1 . ARG A 1 287 ? -84.433  14.835 43.291  1.00 80.54  ? 287 ARG A NH1 1 
ATOM   2190 N  NH2 . ARG A 1 287 ? -84.784  12.825 44.329  1.00 97.78  ? 287 ARG A NH2 1 
ATOM   2191 N  N   . GLU A 1 288 ? -90.425  12.597 38.291  1.00 69.60  ? 288 GLU A N   1 
ATOM   2192 C  CA  . GLU A 1 288 ? -90.811  11.535 37.368  1.00 78.06  ? 288 GLU A CA  1 
ATOM   2193 C  C   . GLU A 1 288 ? -90.697  11.992 35.920  1.00 76.72  ? 288 GLU A C   1 
ATOM   2194 O  O   . GLU A 1 288 ? -90.188  11.251 35.070  1.00 73.67  ? 288 GLU A O   1 
ATOM   2195 C  CB  . GLU A 1 288 ? -92.233  11.065 37.667  1.00 82.01  ? 288 GLU A CB  1 
ATOM   2196 C  CG  . GLU A 1 288 ? -92.406  10.434 39.040  1.00 92.04  ? 288 GLU A CG  1 
ATOM   2197 C  CD  . GLU A 1 288 ? -93.812  9.913  39.270  1.00 103.27 ? 288 GLU A CD  1 
ATOM   2198 O  OE1 . GLU A 1 288 ? -94.640  9.998  38.336  1.00 105.35 ? 288 GLU A OE1 1 
ATOM   2199 O  OE2 . GLU A 1 288 ? -94.088  9.418  40.385  1.00 95.45  ? 288 GLU A OE2 1 
ATOM   2200 N  N   . ALA A 1 289 ? -91.174  13.203 35.619  1.00 75.78  ? 289 ALA A N   1 
ATOM   2201 C  CA  . ALA A 1 289 ? -91.071  13.725 34.260  1.00 71.78  ? 289 ALA A CA  1 
ATOM   2202 C  C   . ALA A 1 289 ? -89.617  13.825 33.818  1.00 71.82  ? 289 ALA A C   1 
ATOM   2203 O  O   . ALA A 1 289 ? -89.296  13.572 32.651  1.00 68.27  ? 289 ALA A O   1 
ATOM   2204 C  CB  . ALA A 1 289 ? -91.758  15.087 34.169  1.00 67.59  ? 289 ALA A CB  1 
ATOM   2205 N  N   . LEU A 1 290 ? -88.722  14.187 34.741  1.00 65.60  ? 290 LEU A N   1 
ATOM   2206 C  CA  . LEU A 1 290 ? -87.298  14.193 34.427  1.00 68.75  ? 290 LEU A CA  1 
ATOM   2207 C  C   . LEU A 1 290 ? -86.765  12.780 34.237  1.00 67.36  ? 290 LEU A C   1 
ATOM   2208 O  O   . LEU A 1 290 ? -85.849  12.566 33.434  1.00 73.06  ? 290 LEU A O   1 
ATOM   2209 C  CB  . LEU A 1 290 ? -86.519  14.912 35.529  1.00 68.37  ? 290 LEU A CB  1 
ATOM   2210 C  CG  . LEU A 1 290 ? -84.994  14.821 35.463  1.00 65.13  ? 290 LEU A CG  1 
ATOM   2211 C  CD1 . LEU A 1 290 ? -84.471  15.471 34.190  1.00 64.69  ? 290 LEU A CD1 1 
ATOM   2212 C  CD2 . LEU A 1 290 ? -84.362  15.445 36.698  1.00 63.47  ? 290 LEU A CD2 1 
ATOM   2213 N  N   . GLU A 1 291 ? -87.322  11.807 34.959  1.00 66.87  ? 291 GLU A N   1 
ATOM   2214 C  CA  . GLU A 1 291 ? -86.924  10.420 34.753  1.00 68.86  ? 291 GLU A CA  1 
ATOM   2215 C  C   . GLU A 1 291 ? -87.390  9.914  33.394  1.00 71.98  ? 291 GLU A C   1 
ATOM   2216 O  O   . GLU A 1 291 ? -86.647  9.210  32.699  1.00 69.46  ? 291 GLU A O   1 
ATOM   2217 C  CB  . GLU A 1 291 ? -87.474  9.546  35.882  1.00 68.04  ? 291 GLU A CB  1 
ATOM   2218 C  CG  . GLU A 1 291 ? -87.277  8.047  35.683  1.00 70.83  ? 291 GLU A CG  1 
ATOM   2219 C  CD  . GLU A 1 291 ? -85.813  7.634  35.644  1.00 79.52  ? 291 GLU A CD  1 
ATOM   2220 O  OE1 . GLU A 1 291 ? -84.947  8.413  36.101  1.00 74.61  ? 291 GLU A OE1 1 
ATOM   2221 O  OE2 . GLU A 1 291 ? -85.531  6.522  35.153  1.00 81.60  ? 291 GLU A OE2 1 
ATOM   2222 N  N   . ARG A 1 292 ? -88.615  10.269 32.996  1.00 67.52  ? 292 ARG A N   1 
ATOM   2223 C  CA  . ARG A 1 292 ? -89.100  9.896  31.672  1.00 71.58  ? 292 ARG A CA  1 
ATOM   2224 C  C   . ARG A 1 292 ? -88.242  10.515 30.578  1.00 70.46  ? 292 ARG A C   1 
ATOM   2225 O  O   . ARG A 1 292 ? -87.889  9.844  29.601  1.00 70.46  ? 292 ARG A O   1 
ATOM   2226 C  CB  . ARG A 1 292 ? -90.557  10.319 31.501  1.00 69.04  ? 292 ARG A CB  1 
ATOM   2227 C  CG  . ARG A 1 292 ? -91.543  9.530  32.335  1.00 68.28  ? 292 ARG A CG  1 
ATOM   2228 C  CD  . ARG A 1 292 ? -92.870  9.422  31.609  1.00 67.96  ? 292 ARG A CD  1 
ATOM   2229 N  NE  . ARG A 1 292 ? -92.724  8.701  30.351  1.00 65.25  ? 292 ARG A NE  1 
ATOM   2230 C  CZ  . ARG A 1 292 ? -93.639  8.670  29.392  1.00 71.61  ? 292 ARG A CZ  1 
ATOM   2231 N  NH1 . ARG A 1 292 ? -94.784  9.325  29.507  1.00 64.75  ? 292 ARG A NH1 1 
ATOM   2232 N  NH2 . ARG A 1 292 ? -93.398  7.967  28.286  1.00 72.98  ? 292 ARG A NH2 1 
ATOM   2233 N  N   . TYR A 1 293 ? -87.898  11.796 30.726  1.00 69.61  ? 293 TYR A N   1 
ATOM   2234 C  CA  . TYR A 1 293 ? -87.055  12.461 29.739  1.00 70.57  ? 293 TYR A CA  1 
ATOM   2235 C  C   . TYR A 1 293 ? -85.713  11.754 29.600  1.00 70.15  ? 293 TYR A C   1 
ATOM   2236 O  O   . TYR A 1 293 ? -85.173  11.640 28.493  1.00 66.65  ? 293 TYR A O   1 
ATOM   2237 C  CB  . TYR A 1 293 ? -86.861  13.926 30.133  1.00 69.75  ? 293 TYR A CB  1 
ATOM   2238 C  CG  . TYR A 1 293 ? -86.242  14.796 29.062  1.00 64.69  ? 293 TYR A CG  1 
ATOM   2239 C  CD1 . TYR A 1 293 ? -86.980  15.201 27.959  1.00 63.95  ? 293 TYR A CD1 1 
ATOM   2240 C  CD2 . TYR A 1 293 ? -84.928  15.234 29.168  1.00 64.98  ? 293 TYR A CD2 1 
ATOM   2241 C  CE1 . TYR A 1 293 ? -86.423  16.003 26.983  1.00 65.65  ? 293 TYR A CE1 1 
ATOM   2242 C  CE2 . TYR A 1 293 ? -84.362  16.037 28.197  1.00 65.99  ? 293 TYR A CE2 1 
ATOM   2243 C  CZ  . TYR A 1 293 ? -85.115  16.419 27.106  1.00 68.83  ? 293 TYR A CZ  1 
ATOM   2244 O  OH  . TYR A 1 293 ? -84.558  17.219 26.133  1.00 67.27  ? 293 TYR A OH  1 
ATOM   2245 N  N   . ARG A 1 294 ? -85.168  11.258 30.712  1.00 72.50  ? 294 ARG A N   1 
ATOM   2246 C  CA  . ARG A 1 294 ? -83.877  10.579 30.670  1.00 71.84  ? 294 ARG A CA  1 
ATOM   2247 C  C   . ARG A 1 294 ? -83.961  9.267  29.900  1.00 68.50  ? 294 ARG A C   1 
ATOM   2248 O  O   . ARG A 1 294 ? -83.060  8.940  29.118  1.00 64.93  ? 294 ARG A O   1 
ATOM   2249 C  CB  . ARG A 1 294 ? -83.373  10.328 32.091  1.00 75.26  ? 294 ARG A CB  1 
ATOM   2250 C  CG  . ARG A 1 294 ? -82.062  9.559  32.155  1.00 79.28  ? 294 ARG A CG  1 
ATOM   2251 C  CD  . ARG A 1 294 ? -81.669  9.230  33.588  1.00 80.70  ? 294 ARG A CD  1 
ATOM   2252 N  NE  . ARG A 1 294 ? -82.518  8.196  34.169  1.00 84.86  ? 294 ARG A NE  1 
ATOM   2253 C  CZ  . ARG A 1 294 ? -82.284  6.895  34.070  1.00 81.90  ? 294 ARG A CZ  1 
ATOM   2254 N  NH1 . ARG A 1 294 ? -81.238  6.429  33.407  1.00 79.51  ? 294 ARG A NH1 1 
ATOM   2255 N  NH2 . ARG A 1 294 ? -83.120  6.040  34.651  1.00 76.35  ? 294 ARG A NH2 1 
ATOM   2256 N  N   . THR A 1 295 ? -85.032  8.503  30.107  1.00 64.91  ? 295 THR A N   1 
ATOM   2257 C  CA  . THR A 1 295 ? -85.134  7.155  29.564  1.00 69.20  ? 295 THR A CA  1 
ATOM   2258 C  C   . THR A 1 295 ? -85.886  7.080  28.242  1.00 69.26  ? 295 THR A C   1 
ATOM   2259 O  O   . THR A 1 295 ? -85.567  6.222  27.413  1.00 68.52  ? 295 THR A O   1 
ATOM   2260 C  CB  . THR A 1 295 ? -85.815  6.227  30.576  1.00 65.82  ? 295 THR A CB  1 
ATOM   2261 O  OG1 . THR A 1 295 ? -87.169  6.651  30.778  1.00 66.05  ? 295 THR A OG1 1 
ATOM   2262 C  CG2 . THR A 1 295 ? -85.074  6.260  31.903  1.00 64.79  ? 295 THR A CG2 1 
ATOM   2263 N  N   . ASP A 1 296 ? -86.872  7.948  28.019  1.00 65.60  ? 296 ASP A N   1 
ATOM   2264 C  CA  . ASP A 1 296 ? -87.687  7.883  26.814  1.00 65.60  ? 296 ASP A CA  1 
ATOM   2265 C  C   . ASP A 1 296 ? -87.347  8.953  25.784  1.00 70.79  ? 296 ASP A C   1 
ATOM   2266 O  O   . ASP A 1 296 ? -87.884  8.906  24.674  1.00 69.30  ? 296 ASP A O   1 
ATOM   2267 C  CB  . ASP A 1 296 ? -89.174  7.981  27.175  1.00 64.10  ? 296 ASP A CB  1 
ATOM   2268 C  CG  . ASP A 1 296 ? -89.685  6.738  27.870  1.00 71.23  ? 296 ASP A CG  1 
ATOM   2269 O  OD1 . ASP A 1 296 ? -88.885  5.794  28.058  1.00 70.97  ? 296 ASP A OD1 1 
ATOM   2270 O  OD2 . ASP A 1 296 ? -90.884  6.703  28.225  1.00 69.70  ? 296 ASP A OD2 1 
ATOM   2271 N  N   . ALA A 1 297 ? -86.473  9.903  26.109  1.00 66.59  ? 297 ALA A N   1 
ATOM   2272 C  CA  . ALA A 1 297 ? -86.094  10.941 25.160  1.00 57.72  ? 297 ALA A CA  1 
ATOM   2273 C  C   . ALA A 1 297 ? -84.595  10.992 24.914  1.00 65.55  ? 297 ALA A C   1 
ATOM   2274 O  O   . ALA A 1 297 ? -84.163  10.978 23.755  1.00 60.80  ? 297 ALA A O   1 
ATOM   2275 C  CB  . ALA A 1 297 ? -86.597  12.312 25.642  1.00 64.75  ? 297 ALA A CB  1 
ATOM   2276 N  N   . VAL A 1 298 ? -83.783  11.041 25.968  1.00 61.94  ? 298 VAL A N   1 
ATOM   2277 C  CA  . VAL A 1 298 ? -82.342  11.176 25.777  1.00 64.54  ? 298 VAL A CA  1 
ATOM   2278 C  C   . VAL A 1 298 ? -81.704  9.822  25.495  1.00 70.11  ? 298 VAL A C   1 
ATOM   2279 O  O   . VAL A 1 298 ? -80.893  9.681  24.572  1.00 66.15  ? 298 VAL A O   1 
ATOM   2280 C  CB  . VAL A 1 298 ? -81.701  11.863 26.995  1.00 61.48  ? 298 VAL A CB  1 
ATOM   2281 C  CG1 . VAL A 1 298 ? -80.202  11.999 26.793  1.00 64.04  ? 298 VAL A CG1 1 
ATOM   2282 C  CG2 . VAL A 1 298 ? -82.338  13.225 27.225  1.00 64.78  ? 298 VAL A CG2 1 
ATOM   2283 N  N   . ARG A 1 299 ? -82.055  8.805  26.286  1.00 71.82  ? 299 ARG A N   1 
ATOM   2284 C  CA  . ARG A 1 299 ? -81.503  7.475  26.054  1.00 72.30  ? 299 ARG A CA  1 
ATOM   2285 C  C   . ARG A 1 299 ? -81.955  6.916  24.712  1.00 67.94  ? 299 ARG A C   1 
ATOM   2286 O  O   . ARG A 1 299 ? -81.171  6.281  23.998  1.00 67.57  ? 299 ARG A O   1 
ATOM   2287 C  CB  . ARG A 1 299 ? -81.900  6.533  27.192  1.00 70.58  ? 299 ARG A CB  1 
ATOM   2288 C  CG  . ARG A 1 299 ? -80.868  6.452  28.302  1.00 70.91  ? 299 ARG A CG  1 
ATOM   2289 C  CD  . ARG A 1 299 ? -81.366  5.649  29.493  1.00 72.15  ? 299 ARG A CD  1 
ATOM   2290 N  NE  . ARG A 1 299 ? -80.331  5.534  30.514  1.00 80.69  ? 299 ARG A NE  1 
ATOM   2291 C  CZ  . ARG A 1 299 ? -79.720  4.405  30.849  1.00 75.29  ? 299 ARG A CZ  1 
ATOM   2292 N  NH1 . ARG A 1 299 ? -80.069  3.246  30.317  1.00 79.18  ? 299 ARG A NH1 1 
ATOM   2293 N  NH2 . ARG A 1 299 ? -78.735  4.442  31.742  1.00 74.52  ? 299 ARG A NH2 1 
ATOM   2294 N  N   . THR A 1 300 ? -83.213  7.162  24.343  1.00 64.20  ? 300 THR A N   1 
ATOM   2295 C  CA  . THR A 1 300 ? -83.755  6.581  23.121  1.00 67.47  ? 300 THR A CA  1 
ATOM   2296 C  C   . THR A 1 300 ? -83.148  7.202  21.868  1.00 70.28  ? 300 THR A C   1 
ATOM   2297 O  O   . THR A 1 300 ? -83.001  6.514  20.853  1.00 70.01  ? 300 THR A O   1 
ATOM   2298 C  CB  . THR A 1 300 ? -85.274  6.729  23.105  1.00 67.17  ? 300 THR A CB  1 
ATOM   2299 O  OG1 . THR A 1 300 ? -85.623  8.068  23.473  1.00 69.73  ? 300 THR A OG1 1 
ATOM   2300 C  CG2 . THR A 1 300 ? -85.909  5.764  24.085  1.00 60.92  ? 300 THR A CG2 1 
ATOM   2301 N  N   . VAL A 1 301 ? -82.789  8.488  21.910  1.00 68.48  ? 301 VAL A N   1 
ATOM   2302 C  CA  . VAL A 1 301 ? -82.196  9.105  20.727  1.00 65.60  ? 301 VAL A CA  1 
ATOM   2303 C  C   . VAL A 1 301 ? -80.754  8.643  20.543  1.00 69.99  ? 301 VAL A C   1 
ATOM   2304 O  O   . VAL A 1 301 ? -80.233  8.646  19.421  1.00 73.48  ? 301 VAL A O   1 
ATOM   2305 C  CB  . VAL A 1 301 ? -82.296  10.641 20.798  1.00 65.43  ? 301 VAL A CB  1 
ATOM   2306 C  CG1 . VAL A 1 301 ? -81.202  11.222 21.682  1.00 71.38  ? 301 VAL A CG1 1 
ATOM   2307 C  CG2 . VAL A 1 301 ? -82.229  11.241 19.406  1.00 66.64  ? 301 VAL A CG2 1 
ATOM   2308 N  N   . ILE A 1 302 ? -80.088  8.235  21.622  1.00 71.19  ? 302 ILE A N   1 
ATOM   2309 C  CA  . ILE A 1 302 ? -78.736  7.695  21.506  1.00 69.65  ? 302 ILE A CA  1 
ATOM   2310 C  C   . ILE A 1 302 ? -78.775  6.264  20.986  1.00 77.89  ? 302 ILE A C   1 
ATOM   2311 O  O   . ILE A 1 302 ? -78.161  5.935  19.964  1.00 77.83  ? 302 ILE A O   1 
ATOM   2312 C  CB  . ILE A 1 302 ? -78.005  7.776  22.857  1.00 68.00  ? 302 ILE A CB  1 
ATOM   2313 C  CG1 . ILE A 1 302 ? -77.764  9.232  23.251  1.00 71.88  ? 302 ILE A CG1 1 
ATOM   2314 C  CG2 . ILE A 1 302 ? -76.693  7.014  22.796  1.00 76.56  ? 302 ILE A CG2 1 
ATOM   2315 C  CD1 . ILE A 1 302 ? -77.258  9.399  24.672  1.00 77.82  ? 302 ILE A CD1 1 
ATOM   2316 N  N   . ARG A 1 303 ? -79.510  5.393  21.680  1.00 75.21  ? 303 ARG A N   1 
ATOM   2317 C  CA  . ARG A 1 303 ? -79.525  3.982  21.313  1.00 80.09  ? 303 ARG A CA  1 
ATOM   2318 C  C   . ARG A 1 303 ? -80.250  3.753  19.991  1.00 75.30  ? 303 ARG A C   1 
ATOM   2319 O  O   . ARG A 1 303 ? -79.799  2.953  19.164  1.00 72.56  ? 303 ARG A O   1 
ATOM   2320 C  CB  . ARG A 1 303 ? -80.166  3.158  22.431  1.00 72.48  ? 303 ARG A CB  1 
ATOM   2321 C  CG  . ARG A 1 303 ? -80.131  1.658  22.189  1.00 81.30  ? 303 ARG A CG  1 
ATOM   2322 C  CD  . ARG A 1 303 ? -78.705  1.172  21.966  1.00 84.42  ? 303 ARG A CD  1 
ATOM   2323 N  NE  . ARG A 1 303 ? -78.664  -0.076 21.213  1.00 89.50  ? 303 ARG A NE  1 
ATOM   2324 C  CZ  . ARG A 1 303 ? -78.318  -1.252 21.719  1.00 84.40  ? 303 ARG A CZ  1 
ATOM   2325 N  NH1 . ARG A 1 303 ? -77.954  -1.380 22.983  1.00 91.14  ? 303 ARG A NH1 1 
ATOM   2326 N  NH2 . ARG A 1 303 ? -78.330  -2.325 20.933  1.00 85.57  ? 303 ARG A NH2 1 
ATOM   2327 N  N   . GLY A 1 304 ? -81.373  4.443  19.775  1.00 72.89  ? 304 GLY A N   1 
ATOM   2328 C  CA  . GLY A 1 304 ? -82.163  4.198  18.577  1.00 72.47  ? 304 GLY A CA  1 
ATOM   2329 C  C   . GLY A 1 304 ? -81.404  4.488  17.297  1.00 75.94  ? 304 GLY A C   1 
ATOM   2330 O  O   . GLY A 1 304 ? -81.568  3.790  16.294  1.00 76.70  ? 304 GLY A O   1 
ATOM   2331 N  N   . SER A 1 305 ? -80.555  5.515  17.317  1.00 77.69  ? 305 SER A N   1 
ATOM   2332 C  CA  . SER A 1 305 ? -79.771  5.849  16.135  1.00 78.84  ? 305 SER A CA  1 
ATOM   2333 C  C   . SER A 1 305 ? -78.731  4.776  15.838  1.00 86.15  ? 305 SER A C   1 
ATOM   2334 O  O   . SER A 1 305 ? -78.452  4.478  14.671  1.00 87.92  ? 305 SER A O   1 
ATOM   2335 C  CB  . SER A 1 305 ? -79.101  7.208  16.328  1.00 80.57  ? 305 SER A CB  1 
ATOM   2336 O  OG  . SER A 1 305 ? -78.338  7.574  15.193  1.00 96.82  ? 305 SER A OG  1 
ATOM   2337 N  N   . TYR A 1 306 ? -78.149  4.184  16.883  1.00 82.02  ? 306 TYR A N   1 
ATOM   2338 C  CA  . TYR A 1 306 ? -77.098  3.189  16.689  1.00 86.18  ? 306 TYR A CA  1 
ATOM   2339 C  C   . TYR A 1 306 ? -77.635  1.930  16.018  1.00 87.33  ? 306 TYR A C   1 
ATOM   2340 O  O   . TYR A 1 306 ? -76.996  1.383  15.112  1.00 91.00  ? 306 TYR A O   1 
ATOM   2341 C  CB  . TYR A 1 306 ? -76.455  2.855  18.033  1.00 87.26  ? 306 TYR A CB  1 
ATOM   2342 C  CG  . TYR A 1 306 ? -75.459  1.721  17.986  1.00 93.13  ? 306 TYR A CG  1 
ATOM   2343 C  CD1 . TYR A 1 306 ? -74.211  1.890  17.401  1.00 95.79  ? 306 TYR A CD1 1 
ATOM   2344 C  CD2 . TYR A 1 306 ? -75.760  0.485  18.545  1.00 94.26  ? 306 TYR A CD2 1 
ATOM   2345 C  CE1 . TYR A 1 306 ? -73.292  0.856  17.364  1.00 101.03 ? 306 TYR A CE1 1 
ATOM   2346 C  CE2 . TYR A 1 306 ? -74.848  -0.554 18.515  1.00 101.84 ? 306 TYR A CE2 1 
ATOM   2347 C  CZ  . TYR A 1 306 ? -73.616  -0.364 17.922  1.00 104.77 ? 306 TYR A CZ  1 
ATOM   2348 O  OH  . TYR A 1 306 ? -72.705  -1.397 17.890  1.00 106.41 ? 306 TYR A OH  1 
ATOM   2349 N  N   . ASP A 1 307 ? -78.804  1.454  16.450  1.00 83.67  ? 307 ASP A N   1 
ATOM   2350 C  CA  . ASP A 1 307 ? -79.383  0.262  15.839  1.00 89.67  ? 307 ASP A CA  1 
ATOM   2351 C  C   . ASP A 1 307 ? -79.765  0.515  14.386  1.00 92.37  ? 307 ASP A C   1 
ATOM   2352 O  O   . ASP A 1 307 ? -79.602  -0.365 13.532  1.00 95.98  ? 307 ASP A O   1 
ATOM   2353 C  CB  . ASP A 1 307 ? -80.606  -0.193 16.636  1.00 86.15  ? 307 ASP A CB  1 
ATOM   2354 C  CG  . ASP A 1 307 ? -80.296  -0.429 18.102  1.00 91.89  ? 307 ASP A CG  1 
ATOM   2355 O  OD1 . ASP A 1 307 ? -79.150  -0.817 18.413  1.00 92.97  ? 307 ASP A OD1 1 
ATOM   2356 O  OD2 . ASP A 1 307 ? -81.200  -0.228 18.942  1.00 88.16  ? 307 ASP A OD2 1 
ATOM   2357 N  N   . TRP A 1 308 ? -80.258  1.717  14.086  1.00 94.44  ? 308 TRP A N   1 
ATOM   2358 C  CA  . TRP A 1 308 ? -80.840  1.996  12.779  1.00 91.10  ? 308 TRP A CA  1 
ATOM   2359 C  C   . TRP A 1 308 ? -79.791  2.350  11.732  1.00 94.49  ? 308 TRP A C   1 
ATOM   2360 O  O   . TRP A 1 308 ? -80.001  2.081  10.545  1.00 99.23  ? 308 TRP A O   1 
ATOM   2361 C  CB  . TRP A 1 308 ? -81.866  3.120  12.912  1.00 83.78  ? 308 TRP A CB  1 
ATOM   2362 C  CG  . TRP A 1 308 ? -82.416  3.638  11.620  1.00 83.61  ? 308 TRP A CG  1 
ATOM   2363 C  CD1 . TRP A 1 308 ? -83.526  3.193  10.963  1.00 79.96  ? 308 TRP A CD1 1 
ATOM   2364 C  CD2 . TRP A 1 308 ? -81.894  4.721  10.839  1.00 80.79  ? 308 TRP A CD2 1 
ATOM   2365 N  NE1 . TRP A 1 308 ? -83.723  3.928  9.817   1.00 79.26  ? 308 TRP A NE1 1 
ATOM   2366 C  CE2 . TRP A 1 308 ? -82.734  4.872  9.719   1.00 80.70  ? 308 TRP A CE2 1 
ATOM   2367 C  CE3 . TRP A 1 308 ? -80.794  5.574  10.978  1.00 85.84  ? 308 TRP A CE3 1 
ATOM   2368 C  CZ2 . TRP A 1 308 ? -82.510  5.842  8.743   1.00 80.56  ? 308 TRP A CZ2 1 
ATOM   2369 C  CZ3 . TRP A 1 308 ? -80.573  6.537  10.008  1.00 86.80  ? 308 TRP A CZ3 1 
ATOM   2370 C  CH2 . TRP A 1 308 ? -81.426  6.662  8.905   1.00 81.45  ? 308 TRP A CH2 1 
ATOM   2371 N  N   . HIS A 1 309 ? -78.668  2.950  12.139  1.00 96.83  ? 309 HIS A N   1 
ATOM   2372 C  CA  . HIS A 1 309 ? -77.610  3.255  11.179  1.00 94.99  ? 309 HIS A CA  1 
ATOM   2373 C  C   . HIS A 1 309 ? -77.021  1.989  10.574  1.00 101.69 ? 309 HIS A C   1 
ATOM   2374 O  O   . HIS A 1 309 ? -76.518  2.015  9.444   1.00 100.26 ? 309 HIS A O   1 
ATOM   2375 C  CB  . HIS A 1 309 ? -76.508  4.084  11.843  1.00 87.05  ? 309 HIS A CB  1 
ATOM   2376 C  CG  . HIS A 1 309 ? -76.713  5.563  11.727  1.00 96.84  ? 309 HIS A CG  1 
ATOM   2377 N  ND1 . HIS A 1 309 ? -77.348  6.308  12.698  1.00 103.08 ? 309 HIS A ND1 1 
ATOM   2378 C  CD2 . HIS A 1 309 ? -76.371  6.436  10.749  1.00 98.36  ? 309 HIS A CD2 1 
ATOM   2379 C  CE1 . HIS A 1 309 ? -77.386  7.575  12.325  1.00 99.71  ? 309 HIS A CE1 1 
ATOM   2380 N  NE2 . HIS A 1 309 ? -76.800  7.679  11.146  1.00 97.08  ? 309 HIS A NE2 1 
ATOM   2381 N  N   . ARG A 1 310 ? -77.079  0.874  11.301  1.00 98.11  ? 310 ARG A N   1 
ATOM   2382 C  CA  . ARG A 1 310 ? -76.562  -0.385 10.786  1.00 104.95 ? 310 ARG A CA  1 
ATOM   2383 C  C   . ARG A 1 310 ? -77.565  -1.120 9.908   1.00 106.86 ? 310 ARG A C   1 
ATOM   2384 O  O   . ARG A 1 310 ? -77.160  -1.982 9.121   1.00 116.01 ? 310 ARG A O   1 
ATOM   2385 C  CB  . ARG A 1 310 ? -76.132  -1.280 11.950  1.00 104.31 ? 310 ARG A CB  1 
ATOM   2386 C  CG  . ARG A 1 310 ? -75.035  -0.668 12.806  1.00 104.75 ? 310 ARG A CG  1 
ATOM   2387 C  CD  . ARG A 1 310 ? -75.142  -1.123 14.249  1.00 105.64 ? 310 ARG A CD  1 
ATOM   2388 N  NE  . ARG A 1 310 ? -74.803  -2.530 14.416  1.00 111.71 ? 310 ARG A NE  1 
ATOM   2389 C  CZ  . ARG A 1 310 ? -75.149  -3.263 15.465  1.00 120.80 ? 310 ARG A CZ  1 
ATOM   2390 N  NH1 . ARG A 1 310 ? -75.880  -2.760 16.448  1.00 113.47 ? 310 ARG A NH1 1 
ATOM   2391 N  NH2 . ARG A 1 310 ? -74.759  -4.533 15.527  1.00 121.47 ? 310 ARG A NH2 1 
ATOM   2392 N  N   . SER A 1 311 ? -78.855  -0.791 10.008  1.00 105.63 ? 311 SER A N   1 
ATOM   2393 C  CA  . SER A 1 311 ? -79.898  -1.505 9.282   1.00 106.32 ? 311 SER A CA  1 
ATOM   2394 C  C   . SER A 1 311 ? -80.562  -0.689 8.181   1.00 100.89 ? 311 SER A C   1 
ATOM   2395 O  O   . SER A 1 311 ? -81.319  -1.258 7.388   1.00 108.49 ? 311 SER A O   1 
ATOM   2396 C  CB  . SER A 1 311 ? -80.980  -1.995 10.257  1.00 102.03 ? 311 SER A CB  1 
ATOM   2397 O  OG  . SER A 1 311 ? -81.611  -0.903 10.905  1.00 98.08  ? 311 SER A OG  1 
ATOM   2398 N  N   . SER A 1 312 ? -80.306  0.614  8.104   1.00 97.41  ? 312 SER A N   1 
ATOM   2399 C  CA  . SER A 1 312 ? -81.002  1.462  7.146   1.00 94.30  ? 312 SER A CA  1 
ATOM   2400 C  C   . SER A 1 312 ? -80.471  1.248  5.736   1.00 96.58  ? 312 SER A C   1 
ATOM   2401 O  O   . SER A 1 312 ? -79.258  1.185  5.513   1.00 97.20  ? 312 SER A O   1 
ATOM   2402 C  CB  . SER A 1 312 ? -80.861  2.935  7.530   1.00 91.93  ? 312 SER A CB  1 
ATOM   2403 O  OG  . SER A 1 312 ? -81.509  3.767  6.581   1.00 88.81  ? 312 SER A OG  1 
ATOM   2404 N  N   . GLY A 1 313 ? -81.394  1.140  4.778   1.00 93.96  ? 313 GLY A N   1 
ATOM   2405 C  CA  . GLY A 1 313 ? -81.004  1.077  3.382   1.00 92.12  ? 313 GLY A CA  1 
ATOM   2406 C  C   . GLY A 1 313 ? -80.399  2.362  2.862   1.00 96.54  ? 313 GLY A C   1 
ATOM   2407 O  O   . GLY A 1 313 ? -79.676  2.334  1.860   1.00 97.59  ? 313 GLY A O   1 
ATOM   2408 N  N   . ARG A 1 314 ? -80.671  3.489  3.529   1.00 97.49  ? 314 ARG A N   1 
ATOM   2409 C  CA  . ARG A 1 314 ? -80.089  4.766  3.133   1.00 97.33  ? 314 ARG A CA  1 
ATOM   2410 C  C   . ARG A 1 314 ? -78.566  4.734  3.161   1.00 98.99  ? 314 ARG A C   1 
ATOM   2411 O  O   . ARG A 1 314 ? -77.926  5.556  2.495   1.00 100.82 ? 314 ARG A O   1 
ATOM   2412 C  CB  . ARG A 1 314 ? -80.621  5.878  4.046   1.00 95.24  ? 314 ARG A CB  1 
ATOM   2413 C  CG  . ARG A 1 314 ? -80.407  7.298  3.532   1.00 96.70  ? 314 ARG A CG  1 
ATOM   2414 C  CD  . ARG A 1 314 ? -81.089  8.318  4.437   1.00 92.26  ? 314 ARG A CD  1 
ATOM   2415 N  NE  . ARG A 1 314 ? -80.782  9.695  4.064   1.00 93.38  ? 314 ARG A NE  1 
ATOM   2416 C  CZ  . ARG A 1 314 ? -81.578  10.479 3.350   1.00 92.63  ? 314 ARG A CZ  1 
ATOM   2417 N  NH1 . ARG A 1 314 ? -82.749  10.054 2.903   1.00 88.82  ? 314 ARG A NH1 1 
ATOM   2418 N  NH2 . ARG A 1 314 ? -81.193  11.725 3.081   1.00 91.70  ? 314 ARG A NH2 1 
ATOM   2419 N  N   . TYR A 1 315 ? -77.975  3.802  3.903   1.00 95.91  ? 315 TYR A N   1 
ATOM   2420 C  CA  . TYR A 1 315 ? -76.526  3.647  3.938   1.00 100.99 ? 315 TYR A CA  1 
ATOM   2421 C  C   . TYR A 1 315 ? -76.131  2.233  3.522   1.00 96.94  ? 315 TYR A C   1 
ATOM   2422 O  O   . TYR A 1 315 ? -74.947  1.905  3.443   1.00 90.85  ? 315 TYR A O   1 
ATOM   2423 C  CB  . TYR A 1 315 ? -75.986  3.962  5.335   1.00 99.04  ? 315 TYR A CB  1 
ATOM   2424 C  CG  . TYR A 1 315 ? -76.644  5.162  5.975   1.00 101.72 ? 315 TYR A CG  1 
ATOM   2425 C  CD1 . TYR A 1 315 ? -76.362  6.450  5.537   1.00 99.81  ? 315 TYR A CD1 1 
ATOM   2426 C  CD2 . TYR A 1 315 ? -77.552  5.007  7.016   1.00 98.06  ? 315 TYR A CD2 1 
ATOM   2427 C  CE1 . TYR A 1 315 ? -76.966  7.551  6.117   1.00 102.72 ? 315 TYR A CE1 1 
ATOM   2428 C  CE2 . TYR A 1 315 ? -78.160  6.101  7.603   1.00 95.78  ? 315 TYR A CE2 1 
ATOM   2429 C  CZ  . TYR A 1 315 ? -77.864  7.371  7.150   1.00 102.89 ? 315 TYR A CZ  1 
ATOM   2430 O  OH  . TYR A 1 315 ? -78.468  8.463  7.732   1.00 97.50  ? 315 TYR A OH  1 
ATOM   2431 N  N   . TYR A 1 328 ? -85.229  14.063 -8.447  1.00 92.22  ? 328 TYR A N   1 
ATOM   2432 C  CA  . TYR A 1 328 ? -86.589  13.562 -8.616  1.00 95.84  ? 328 TYR A CA  1 
ATOM   2433 C  C   . TYR A 1 328 ? -87.523  14.159 -7.565  1.00 95.43  ? 328 TYR A C   1 
ATOM   2434 O  O   . TYR A 1 328 ? -88.747  14.116 -7.708  1.00 94.43  ? 328 TYR A O   1 
ATOM   2435 C  CB  . TYR A 1 328 ? -86.612  12.029 -8.547  1.00 94.58  ? 328 TYR A CB  1 
ATOM   2436 C  CG  . TYR A 1 328 ? -86.553  11.451 -7.145  1.00 97.37  ? 328 TYR A CG  1 
ATOM   2437 C  CD1 . TYR A 1 328 ? -85.358  11.410 -6.434  1.00 98.01  ? 328 TYR A CD1 1 
ATOM   2438 C  CD2 . TYR A 1 328 ? -87.691  10.927 -6.541  1.00 93.05  ? 328 TYR A CD2 1 
ATOM   2439 C  CE1 . TYR A 1 328 ? -85.302  10.877 -5.154  1.00 96.67  ? 328 TYR A CE1 1 
ATOM   2440 C  CE2 . TYR A 1 328 ? -87.645  10.391 -5.264  1.00 93.18  ? 328 TYR A CE2 1 
ATOM   2441 C  CZ  . TYR A 1 328 ? -86.450  10.368 -4.575  1.00 94.87  ? 328 TYR A CZ  1 
ATOM   2442 O  OH  . TYR A 1 328 ? -86.407  9.836  -3.304  1.00 90.20  ? 328 TYR A OH  1 
ATOM   2443 N  N   . LEU A 1 329 ? -86.937  14.723 -6.510  1.00 96.53  ? 329 LEU A N   1 
ATOM   2444 C  CA  . LEU A 1 329 ? -87.694  15.349 -5.434  1.00 95.13  ? 329 LEU A CA  1 
ATOM   2445 C  C   . LEU A 1 329 ? -87.718  16.869 -5.531  1.00 97.96  ? 329 LEU A C   1 
ATOM   2446 O  O   . LEU A 1 329 ? -88.176  17.528 -4.593  1.00 97.68  ? 329 LEU A O   1 
ATOM   2447 C  CB  . LEU A 1 329 ? -87.131  14.928 -4.074  1.00 93.47  ? 329 LEU A CB  1 
ATOM   2448 C  CG  . LEU A 1 329 ? -87.406  13.500 -3.600  1.00 89.94  ? 329 LEU A CG  1 
ATOM   2449 C  CD1 . LEU A 1 329 ? -86.735  13.243 -2.256  1.00 82.60  ? 329 LEU A CD1 1 
ATOM   2450 C  CD2 . LEU A 1 329 ? -88.905  13.226 -3.524  1.00 86.69  ? 329 LEU A CD2 1 
ATOM   2451 N  N   . GLU A 1 330 ? -87.242  17.443 -6.642  1.00 99.37  ? 330 GLU A N   1 
ATOM   2452 C  CA  . GLU A 1 330 ? -87.243  18.896 -6.789  1.00 96.49  ? 330 GLU A CA  1 
ATOM   2453 C  C   . GLU A 1 330 ? -88.648  19.486 -6.732  1.00 100.69 ? 330 GLU A C   1 
ATOM   2454 O  O   . GLU A 1 330 ? -88.796  20.673 -6.419  1.00 100.12 ? 330 GLU A O   1 
ATOM   2455 C  CB  . GLU A 1 330 ? -86.565  19.294 -8.102  1.00 90.02  ? 330 GLU A CB  1 
ATOM   2456 N  N   . GLU A 1 331 ? -89.679  18.682 -7.018  1.00 99.57  ? 331 GLU A N   1 
ATOM   2457 C  CA  . GLU A 1 331 ? -91.054  19.170 -6.957  1.00 99.79  ? 331 GLU A CA  1 
ATOM   2458 C  C   . GLU A 1 331 ? -91.437  19.627 -5.555  1.00 93.98  ? 331 GLU A C   1 
ATOM   2459 O  O   . GLU A 1 331 ? -92.267  20.532 -5.405  1.00 88.66  ? 331 GLU A O   1 
ATOM   2460 C  CB  . GLU A 1 331 ? -92.024  18.080 -7.409  1.00 99.45  ? 331 GLU A CB  1 
ATOM   2461 C  CG  . GLU A 1 331 ? -91.742  17.484 -8.768  1.00 94.63  ? 331 GLU A CG  1 
ATOM   2462 C  CD  . GLU A 1 331 ? -92.496  16.187 -8.974  1.00 100.50 ? 331 GLU A CD  1 
ATOM   2463 O  OE1 . GLU A 1 331 ? -92.188  15.207 -8.262  1.00 99.48  ? 331 GLU A OE1 1 
ATOM   2464 O  OE2 . GLU A 1 331 ? -93.409  16.154 -9.828  1.00 94.33  ? 331 GLU A OE2 1 
ATOM   2465 N  N   . LEU A 1 332 ? -90.864  19.006 -4.521  1.00 95.48  ? 332 LEU A N   1 
ATOM   2466 C  CA  . LEU A 1 332 ? -91.260  19.313 -3.150  1.00 97.28  ? 332 LEU A CA  1 
ATOM   2467 C  C   . LEU A 1 332 ? -90.814  20.703 -2.710  1.00 92.43  ? 332 LEU A C   1 
ATOM   2468 O  O   . LEU A 1 332 ? -91.385  21.249 -1.761  1.00 76.87  ? 332 LEU A O   1 
ATOM   2469 C  CB  . LEU A 1 332 ? -90.698  18.266 -2.181  1.00 82.16  ? 332 LEU A CB  1 
ATOM   2470 C  CG  . LEU A 1 332 ? -90.782  16.784 -2.559  1.00 88.01  ? 332 LEU A CG  1 
ATOM   2471 C  CD1 . LEU A 1 332 ? -90.392  15.914 -1.368  1.00 77.61  ? 332 LEU A CD1 1 
ATOM   2472 C  CD2 . LEU A 1 332 ? -92.164  16.412 -3.086  1.00 82.81  ? 332 LEU A CD2 1 
ATOM   2473 N  N   . GLY A 1 333 ? -89.816  21.284 -3.375  1.00 97.58  ? 333 GLY A N   1 
ATOM   2474 C  CA  . GLY A 1 333 ? -89.314  22.590 -2.996  1.00 93.78  ? 333 GLY A CA  1 
ATOM   2475 C  C   . GLY A 1 333 ? -89.580  23.659 -4.034  1.00 93.47  ? 333 GLY A C   1 
ATOM   2476 O  O   . GLY A 1 333 ? -88.859  24.660 -4.102  1.00 94.29  ? 333 GLY A O   1 
ATOM   2477 N  N   . SER A 1 334 ? -90.613  23.459 -4.850  1.00 95.98  ? 334 SER A N   1 
ATOM   2478 C  CA  . SER A 1 334 ? -90.998  24.401 -5.893  1.00 104.43 ? 334 SER A CA  1 
ATOM   2479 C  C   . SER A 1 334 ? -92.408  24.904 -5.618  1.00 103.27 ? 334 SER A C   1 
ATOM   2480 O  O   . SER A 1 334 ? -93.313  24.109 -5.339  1.00 96.42  ? 334 SER A O   1 
ATOM   2481 C  CB  . SER A 1 334 ? -90.918  23.755 -7.281  1.00 92.16  ? 334 SER A CB  1 
ATOM   2482 N  N   . SER A 1 335 ? -92.590  26.219 -5.696  1.00 107.21 ? 335 SER A N   1 
ATOM   2483 C  CA  . SER A 1 335 ? -93.871  26.845 -5.379  1.00 104.83 ? 335 SER A CA  1 
ATOM   2484 C  C   . SER A 1 335 ? -94.914  26.590 -6.464  1.00 106.30 ? 335 SER A C   1 
ATOM   2485 O  O   . SER A 1 335 ? -96.110  26.511 -6.180  1.00 104.01 ? 335 SER A O   1 
ATOM   2486 C  CB  . SER A 1 335 ? -93.687  28.351 -5.171  1.00 102.25 ? 335 SER A CB  1 
ATOM   2487 O  OG  . SER A 1 335 ? -92.820  28.610 -4.077  1.00 101.13 ? 335 SER A OG  1 
ATOM   2488 N  N   . VAL B 1 5   ? -77.362  43.709 45.344  1.00 105.25 ? 5   VAL B N   1 
ATOM   2489 C  CA  . VAL B 1 5   ? -77.719  42.296 45.380  1.00 101.79 ? 5   VAL B CA  1 
ATOM   2490 C  C   . VAL B 1 5   ? -76.490  41.452 45.697  1.00 100.52 ? 5   VAL B C   1 
ATOM   2491 O  O   . VAL B 1 5   ? -75.357  41.915 45.565  1.00 104.41 ? 5   VAL B O   1 
ATOM   2492 C  CB  . VAL B 1 5   ? -78.364  41.849 44.055  1.00 97.02  ? 5   VAL B CB  1 
ATOM   2493 C  CG1 . VAL B 1 5   ? -79.602  42.683 43.761  1.00 94.15  ? 5   VAL B CG1 1 
ATOM   2494 C  CG2 . VAL B 1 5   ? -77.362  41.949 42.916  1.00 95.39  ? 5   VAL B CG2 1 
ATOM   2495 N  N   . ASP B 1 6   ? -76.719  40.210 46.118  1.00 97.09  ? 6   ASP B N   1 
ATOM   2496 C  CA  . ASP B 1 6   ? -75.649  39.300 46.495  1.00 95.50  ? 6   ASP B CA  1 
ATOM   2497 C  C   . ASP B 1 6   ? -75.901  37.939 45.860  1.00 92.27  ? 6   ASP B C   1 
ATOM   2498 O  O   . ASP B 1 6   ? -77.027  37.607 45.481  1.00 90.50  ? 6   ASP B O   1 
ATOM   2499 C  CB  . ASP B 1 6   ? -75.537  39.168 48.021  1.00 98.44  ? 6   ASP B CB  1 
ATOM   2500 C  CG  . ASP B 1 6   ? -74.158  38.723 48.470  1.00 103.84 ? 6   ASP B CG  1 
ATOM   2501 O  OD1 . ASP B 1 6   ? -73.292  38.498 47.596  1.00 92.18  ? 6   ASP B OD1 1 
ATOM   2502 O  OD2 . ASP B 1 6   ? -73.940  38.606 49.696  1.00 107.45 ? 6   ASP B OD2 1 
ATOM   2503 N  N   . PHE B 1 7   ? -74.835  37.149 45.746  1.00 89.59  ? 7   PHE B N   1 
ATOM   2504 C  CA  . PHE B 1 7   ? -74.898  35.858 45.079  1.00 85.32  ? 7   PHE B CA  1 
ATOM   2505 C  C   . PHE B 1 7   ? -74.190  34.799 45.914  1.00 87.98  ? 7   PHE B C   1 
ATOM   2506 O  O   . PHE B 1 7   ? -73.414  35.103 46.824  1.00 90.00  ? 7   PHE B O   1 
ATOM   2507 C  CB  . PHE B 1 7   ? -74.284  35.924 43.671  1.00 83.81  ? 7   PHE B CB  1 
ATOM   2508 C  CG  . PHE B 1 7   ? -74.868  37.002 42.804  1.00 84.39  ? 7   PHE B CG  1 
ATOM   2509 C  CD1 . PHE B 1 7   ? -74.367  38.294 42.849  1.00 86.79  ? 7   PHE B CD1 1 
ATOM   2510 C  CD2 . PHE B 1 7   ? -75.917  36.724 41.945  1.00 86.69  ? 7   PHE B CD2 1 
ATOM   2511 C  CE1 . PHE B 1 7   ? -74.904  39.291 42.056  1.00 86.56  ? 7   PHE B CE1 1 
ATOM   2512 C  CE2 . PHE B 1 7   ? -76.458  37.716 41.147  1.00 87.04  ? 7   PHE B CE2 1 
ATOM   2513 C  CZ  . PHE B 1 7   ? -75.951  39.000 41.202  1.00 86.08  ? 7   PHE B CZ  1 
ATOM   2514 N  N   . HIS B 1 8   ? -74.469  33.540 45.582  1.00 88.69  ? 8   HIS B N   1 
ATOM   2515 C  CA  . HIS B 1 8   ? -73.974  32.380 46.323  1.00 80.96  ? 8   HIS B CA  1 
ATOM   2516 C  C   . HIS B 1 8   ? -72.793  31.791 45.558  1.00 82.58  ? 8   HIS B C   1 
ATOM   2517 O  O   . HIS B 1 8   ? -72.962  30.958 44.668  1.00 86.87  ? 8   HIS B O   1 
ATOM   2518 C  CB  . HIS B 1 8   ? -75.098  31.365 46.512  1.00 84.87  ? 8   HIS B CB  1 
ATOM   2519 C  CG  . HIS B 1 8   ? -74.651  30.048 47.068  1.00 91.81  ? 8   HIS B CG  1 
ATOM   2520 N  ND1 . HIS B 1 8   ? -74.471  29.831 48.417  1.00 95.25  ? 8   HIS B ND1 1 
ATOM   2521 C  CD2 . HIS B 1 8   ? -74.367  28.873 46.457  1.00 89.76  ? 8   HIS B CD2 1 
ATOM   2522 C  CE1 . HIS B 1 8   ? -74.086  28.582 48.613  1.00 97.63  ? 8   HIS B CE1 1 
ATOM   2523 N  NE2 . HIS B 1 8   ? -74.015  27.980 47.439  1.00 96.84  ? 8   HIS B NE2 1 
ATOM   2524 N  N   . ILE B 1 9   ? -71.585  32.233 45.903  1.00 82.28  ? 9   ILE B N   1 
ATOM   2525 C  CA  . ILE B 1 9   ? -70.369  31.693 45.296  1.00 84.03  ? 9   ILE B CA  1 
ATOM   2526 C  C   . ILE B 1 9   ? -69.568  30.951 46.360  1.00 81.54  ? 9   ILE B C   1 
ATOM   2527 O  O   . ILE B 1 9   ? -68.796  31.571 47.109  1.00 82.59  ? 9   ILE B O   1 
ATOM   2528 C  CB  . ILE B 1 9   ? -69.523  32.787 44.617  1.00 83.29  ? 9   ILE B CB  1 
ATOM   2529 C  CG1 . ILE B 1 9   ? -70.197  33.304 43.344  1.00 83.23  ? 9   ILE B CG1 1 
ATOM   2530 C  CG2 . ILE B 1 9   ? -68.166  32.235 44.204  1.00 84.28  ? 9   ILE B CG2 1 
ATOM   2531 C  CD1 . ILE B 1 9   ? -71.254  34.327 43.567  1.00 90.73  ? 9   ILE B CD1 1 
ATOM   2532 N  N   . PRO B 1 10  ? -69.728  29.630 46.477  1.00 82.10  ? 10  PRO B N   1 
ATOM   2533 C  CA  . PRO B 1 10  ? -68.926  28.844 47.431  1.00 81.04  ? 10  PRO B CA  1 
ATOM   2534 C  C   . PRO B 1 10  ? -67.542  28.511 46.883  1.00 81.18  ? 10  PRO B C   1 
ATOM   2535 O  O   . PRO B 1 10  ? -67.192  27.350 46.654  1.00 80.12  ? 10  PRO B O   1 
ATOM   2536 C  CB  . PRO B 1 10  ? -69.796  27.598 47.635  1.00 76.71  ? 10  PRO B CB  1 
ATOM   2537 C  CG  . PRO B 1 10  ? -70.479  27.421 46.322  1.00 82.41  ? 10  PRO B CG  1 
ATOM   2538 C  CD  . PRO B 1 10  ? -70.751  28.809 45.805  1.00 80.62  ? 10  PRO B CD  1 
ATOM   2539 N  N   . LEU B 1 11  ? -66.739  29.547 46.661  1.00 75.14  ? 11  LEU B N   1 
ATOM   2540 C  CA  . LEU B 1 11  ? -65.401  29.391 46.120  1.00 77.87  ? 11  LEU B CA  1 
ATOM   2541 C  C   . LEU B 1 11  ? -64.437  30.286 46.883  1.00 83.89  ? 11  LEU B C   1 
ATOM   2542 O  O   . LEU B 1 11  ? -64.813  31.379 47.323  1.00 82.29  ? 11  LEU B O   1 
ATOM   2543 C  CB  . LEU B 1 11  ? -65.350  29.735 44.623  1.00 81.56  ? 11  LEU B CB  1 
ATOM   2544 C  CG  . LEU B 1 11  ? -66.056  28.748 43.693  1.00 79.66  ? 11  LEU B CG  1 
ATOM   2545 C  CD1 . LEU B 1 11  ? -65.959  29.205 42.248  1.00 81.28  ? 11  LEU B CD1 1 
ATOM   2546 C  CD2 . LEU B 1 11  ? -65.470  27.356 43.860  1.00 77.45  ? 11  LEU B CD2 1 
ATOM   2547 N  N   . PRO B 1 12  ? -63.190  29.848 47.054  1.00 83.46  ? 12  PRO B N   1 
ATOM   2548 C  CA  . PRO B 1 12  ? -62.222  30.657 47.804  1.00 78.98  ? 12  PRO B CA  1 
ATOM   2549 C  C   . PRO B 1 12  ? -61.810  31.893 47.017  1.00 80.54  ? 12  PRO B C   1 
ATOM   2550 O  O   . PRO B 1 12  ? -61.406  31.801 45.855  1.00 81.98  ? 12  PRO B O   1 
ATOM   2551 C  CB  . PRO B 1 12  ? -61.043  29.699 48.005  1.00 78.71  ? 12  PRO B CB  1 
ATOM   2552 C  CG  . PRO B 1 12  ? -61.135  28.757 46.847  1.00 82.28  ? 12  PRO B CG  1 
ATOM   2553 C  CD  . PRO B 1 12  ? -62.609  28.575 46.593  1.00 80.14  ? 12  PRO B CD  1 
ATOM   2554 N  N   . GLY B 1 13  ? -61.919  33.053 47.660  1.00 82.15  ? 13  GLY B N   1 
ATOM   2555 C  CA  . GLY B 1 13  ? -61.418  34.283 47.070  1.00 77.21  ? 13  GLY B CA  1 
ATOM   2556 C  C   . GLY B 1 13  ? -59.909  34.362 47.218  1.00 79.46  ? 13  GLY B C   1 
ATOM   2557 O  O   . GLY B 1 13  ? -59.372  34.231 48.323  1.00 91.16  ? 13  GLY B O   1 
ATOM   2558 N  N   . ARG B 1 14  ? -59.221  34.572 46.099  1.00 77.71  ? 14  ARG B N   1 
ATOM   2559 C  CA  . ARG B 1 14  ? -57.768  34.640 46.066  1.00 79.45  ? 14  ARG B CA  1 
ATOM   2560 C  C   . ARG B 1 14  ? -57.336  35.928 45.378  1.00 83.00  ? 14  ARG B C   1 
ATOM   2561 O  O   . ARG B 1 14  ? -58.156  36.684 44.848  1.00 83.62  ? 14  ARG B O   1 
ATOM   2562 C  CB  . ARG B 1 14  ? -57.173  33.422 45.345  1.00 75.15  ? 14  ARG B CB  1 
ATOM   2563 C  CG  . ARG B 1 14  ? -57.629  32.086 45.908  1.00 78.99  ? 14  ARG B CG  1 
ATOM   2564 C  CD  . ARG B 1 14  ? -57.336  30.959 44.937  1.00 72.56  ? 14  ARG B CD  1 
ATOM   2565 N  NE  . ARG B 1 14  ? -55.939  30.957 44.524  1.00 74.61  ? 14  ARG B NE  1 
ATOM   2566 C  CZ  . ARG B 1 14  ? -55.448  30.197 43.556  1.00 76.82  ? 14  ARG B CZ  1 
ATOM   2567 N  NH1 . ARG B 1 14  ? -56.217  29.363 42.875  1.00 74.34  ? 14  ARG B NH1 1 
ATOM   2568 N  NH2 . ARG B 1 14  ? -54.154  30.279 43.260  1.00 82.53  ? 14  ARG B NH2 1 
ATOM   2569 N  N   . GLN B 1 15  ? -56.027  36.172 45.395  1.00 82.14  ? 15  GLN B N   1 
ATOM   2570 C  CA  . GLN B 1 15  ? -55.441  37.328 44.731  1.00 80.88  ? 15  GLN B CA  1 
ATOM   2571 C  C   . GLN B 1 15  ? -53.940  37.110 44.618  1.00 84.04  ? 15  GLN B C   1 
ATOM   2572 O  O   . GLN B 1 15  ? -53.326  36.517 45.509  1.00 87.34  ? 15  GLN B O   1 
ATOM   2573 C  CB  . GLN B 1 15  ? -55.739  38.629 45.489  1.00 79.14  ? 15  GLN B CB  1 
ATOM   2574 C  CG  . GLN B 1 15  ? -55.189  39.885 44.818  1.00 86.43  ? 15  GLN B CG  1 
ATOM   2575 C  CD  . GLN B 1 15  ? -55.683  41.167 45.464  1.00 91.30  ? 15  GLN B CD  1 
ATOM   2576 O  OE1 . GLN B 1 15  ? -56.345  41.140 46.501  1.00 93.83  ? 15  GLN B OE1 1 
ATOM   2577 N  NE2 . GLN B 1 15  ? -55.369  42.300 44.847  1.00 90.86  ? 15  GLN B NE2 1 
ATOM   2578 N  N   . SER B 1 16  ? -53.360  37.580 43.519  1.00 89.51  ? 16  SER B N   1 
ATOM   2579 C  CA  . SER B 1 16  ? -51.922  37.465 43.343  1.00 92.10  ? 16  SER B CA  1 
ATOM   2580 C  C   . SER B 1 16  ? -51.200  38.340 44.363  1.00 94.19  ? 16  SER B C   1 
ATOM   2581 O  O   . SER B 1 16  ? -51.588  39.493 44.579  1.00 95.37  ? 16  SER B O   1 
ATOM   2582 C  CB  . SER B 1 16  ? -51.513  37.873 41.929  1.00 88.69  ? 16  SER B CB  1 
ATOM   2583 O  OG  . SER B 1 16  ? -50.105  37.817 41.774  1.00 88.47  ? 16  SER B OG  1 
ATOM   2584 N  N   . PRO B 1 17  ? -50.150  37.826 45.005  1.00 94.83  ? 17  PRO B N   1 
ATOM   2585 C  CA  . PRO B 1 17  ? -49.376  38.668 45.931  1.00 93.93  ? 17  PRO B CA  1 
ATOM   2586 C  C   . PRO B 1 17  ? -48.676  39.828 45.244  1.00 95.30  ? 17  PRO B C   1 
ATOM   2587 O  O   . PRO B 1 17  ? -48.252  40.769 45.926  1.00 94.65  ? 17  PRO B O   1 
ATOM   2588 C  CB  . PRO B 1 17  ? -48.370  37.684 46.540  1.00 96.78  ? 17  PRO B CB  1 
ATOM   2589 C  CG  . PRO B 1 17  ? -48.234  36.605 45.506  1.00 91.80  ? 17  PRO B CG  1 
ATOM   2590 C  CD  . PRO B 1 17  ? -49.596  36.466 44.892  1.00 89.13  ? 17  PRO B CD  1 
ATOM   2591 N  N   . ASP B 1 18  ? -48.547  39.792 43.918  1.00 90.16  ? 18  ASP B N   1 
ATOM   2592 C  CA  . ASP B 1 18  ? -47.889  40.840 43.152  1.00 90.90  ? 18  ASP B CA  1 
ATOM   2593 C  C   . ASP B 1 18  ? -48.868  41.895 42.642  1.00 92.59  ? 18  ASP B C   1 
ATOM   2594 O  O   . ASP B 1 18  ? -48.551  42.616 41.688  1.00 88.49  ? 18  ASP B O   1 
ATOM   2595 C  CB  . ASP B 1 18  ? -47.122  40.218 41.982  1.00 89.19  ? 18  ASP B CB  1 
ATOM   2596 C  CG  . ASP B 1 18  ? -46.001  41.101 41.483  1.00 90.90  ? 18  ASP B CG  1 
ATOM   2597 O  OD1 . ASP B 1 18  ? -45.723  42.131 42.131  1.00 94.50  ? 18  ASP B OD1 1 
ATOM   2598 O  OD2 . ASP B 1 18  ? -45.400  40.765 40.441  1.00 94.05  ? 18  ASP B OD2 1 
ATOM   2599 N  N   . HIS B 1 19  ? -50.043  42.007 43.266  1.00 89.80  ? 19  HIS B N   1 
ATOM   2600 C  CA  . HIS B 1 19  ? -51.086  42.887 42.747  1.00 88.41  ? 19  HIS B CA  1 
ATOM   2601 C  C   . HIS B 1 19  ? -50.668  44.352 42.795  1.00 91.95  ? 19  HIS B C   1 
ATOM   2602 O  O   . HIS B 1 19  ? -51.000  45.129 41.891  1.00 91.02  ? 19  HIS B O   1 
ATOM   2603 C  CB  . HIS B 1 19  ? -52.378  42.682 43.535  1.00 87.08  ? 19  HIS B CB  1 
ATOM   2604 C  CG  . HIS B 1 19  ? -52.260  43.038 44.985  1.00 99.57  ? 19  HIS B CG  1 
ATOM   2605 N  ND1 . HIS B 1 19  ? -51.917  42.118 45.952  1.00 102.35 ? 19  HIS B ND1 1 
ATOM   2606 C  CD2 . HIS B 1 19  ? -52.433  44.216 45.631  1.00 99.83  ? 19  HIS B CD2 1 
ATOM   2607 C  CE1 . HIS B 1 19  ? -51.888  42.712 47.132  1.00 98.75  ? 19  HIS B CE1 1 
ATOM   2608 N  NE2 . HIS B 1 19  ? -52.196  43.985 46.965  1.00 99.75  ? 19  HIS B NE2 1 
ATOM   2609 N  N   . ALA B 1 20  ? -49.944  44.751 43.844  1.00 97.44  ? 20  ALA B N   1 
ATOM   2610 C  CA  . ALA B 1 20  ? -49.634  46.165 44.037  1.00 89.47  ? 20  ALA B CA  1 
ATOM   2611 C  C   . ALA B 1 20  ? -48.724  46.693 42.935  1.00 89.29  ? 20  ALA B C   1 
ATOM   2612 O  O   . ALA B 1 20  ? -48.928  47.806 42.435  1.00 85.79  ? 20  ALA B O   1 
ATOM   2613 C  CB  . ALA B 1 20  ? -48.999  46.378 45.409  1.00 84.32  ? 20  ALA B CB  1 
ATOM   2614 N  N   . ARG B 1 21  ? -47.714  45.913 42.543  1.00 85.22  ? 21  ARG B N   1 
ATOM   2615 C  CA  . ARG B 1 21  ? -46.838  46.340 41.458  1.00 85.18  ? 21  ARG B CA  1 
ATOM   2616 C  C   . ARG B 1 21  ? -47.601  46.437 40.142  1.00 92.10  ? 21  ARG B C   1 
ATOM   2617 O  O   . ARG B 1 21  ? -47.409  47.387 39.373  1.00 91.75  ? 21  ARG B O   1 
ATOM   2618 C  CB  . ARG B 1 21  ? -45.660  45.376 41.323  1.00 83.20  ? 21  ARG B CB  1 
ATOM   2619 C  CG  . ARG B 1 21  ? -44.658  45.779 40.256  1.00 82.28  ? 21  ARG B CG  1 
ATOM   2620 C  CD  . ARG B 1 21  ? -43.945  44.568 39.682  1.00 87.67  ? 21  ARG B CD  1 
ATOM   2621 N  NE  . ARG B 1 21  ? -44.887  43.532 39.273  1.00 90.73  ? 21  ARG B NE  1 
ATOM   2622 C  CZ  . ARG B 1 21  ? -45.643  43.591 38.185  1.00 88.63  ? 21  ARG B CZ  1 
ATOM   2623 N  NH1 . ARG B 1 21  ? -45.604  44.634 37.371  1.00 84.94  ? 21  ARG B NH1 1 
ATOM   2624 N  NH2 . ARG B 1 21  ? -46.466  42.583 37.911  1.00 90.47  ? 21  ARG B NH2 1 
ATOM   2625 N  N   . ALA B 1 22  ? -48.476  45.465 39.869  1.00 92.17  ? 22  ALA B N   1 
ATOM   2626 C  CA  . ALA B 1 22  ? -49.230  45.474 38.621  1.00 87.90  ? 22  ALA B CA  1 
ATOM   2627 C  C   . ALA B 1 22  ? -50.237  46.615 38.578  1.00 88.53  ? 22  ALA B C   1 
ATOM   2628 O  O   . ALA B 1 22  ? -50.475  47.190 37.510  1.00 89.31  ? 22  ALA B O   1 
ATOM   2629 C  CB  . ALA B 1 22  ? -49.934  44.131 38.422  1.00 77.27  ? 22  ALA B CB  1 
ATOM   2630 N  N   . GLU B 1 23  ? -50.831  46.961 39.723  1.00 83.91  ? 23  GLU B N   1 
ATOM   2631 C  CA  . GLU B 1 23  ? -51.785  48.064 39.749  1.00 87.89  ? 23  GLU B CA  1 
ATOM   2632 C  C   . GLU B 1 23  ? -51.103  49.403 39.501  1.00 90.80  ? 23  GLU B C   1 
ATOM   2633 O  O   . GLU B 1 23  ? -51.707  50.306 38.911  1.00 90.62  ? 23  GLU B O   1 
ATOM   2634 C  CB  . GLU B 1 23  ? -52.530  48.079 41.083  1.00 88.50  ? 23  GLU B CB  1 
ATOM   2635 C  CG  . GLU B 1 23  ? -53.563  49.187 41.213  1.00 91.33  ? 23  GLU B CG  1 
ATOM   2636 C  CD  . GLU B 1 23  ? -54.260  49.179 42.560  1.00 100.53 ? 23  GLU B CD  1 
ATOM   2637 O  OE1 . GLU B 1 23  ? -54.569  48.082 43.072  1.00 105.46 ? 23  GLU B OE1 1 
ATOM   2638 O  OE2 . GLU B 1 23  ? -54.492  50.275 43.111  1.00 105.69 ? 23  GLU B OE2 1 
ATOM   2639 N  N   . ALA B 1 24  ? -49.848  49.546 39.929  1.00 89.05  ? 24  ALA B N   1 
ATOM   2640 C  CA  . ALA B 1 24  ? -49.144  50.811 39.761  1.00 86.63  ? 24  ALA B CA  1 
ATOM   2641 C  C   . ALA B 1 24  ? -48.572  50.973 38.359  1.00 89.25  ? 24  ALA B C   1 
ATOM   2642 O  O   . ALA B 1 24  ? -48.423  52.104 37.885  1.00 89.08  ? 24  ALA B O   1 
ATOM   2643 C  CB  . ALA B 1 24  ? -48.026  50.931 40.796  1.00 85.99  ? 24  ALA B CB  1 
ATOM   2644 N  N   . GLU B 1 25  ? -48.251  49.871 37.685  1.00 89.23  ? 25  GLU B N   1 
ATOM   2645 C  CA  . GLU B 1 25  ? -47.619  49.909 36.374  1.00 84.76  ? 25  GLU B CA  1 
ATOM   2646 C  C   . GLU B 1 25  ? -48.602  49.708 35.227  1.00 88.34  ? 25  GLU B C   1 
ATOM   2647 O  O   . GLU B 1 25  ? -48.177  49.653 34.069  1.00 89.43  ? 25  GLU B O   1 
ATOM   2648 C  CB  . GLU B 1 25  ? -46.518  48.845 36.294  1.00 84.84  ? 25  GLU B CB  1 
ATOM   2649 C  CG  . GLU B 1 25  ? -45.391  49.031 37.298  1.00 87.43  ? 25  GLU B CG  1 
ATOM   2650 C  CD  . GLU B 1 25  ? -44.323  47.954 37.191  1.00 96.01  ? 25  GLU B CD  1 
ATOM   2651 O  OE1 . GLU B 1 25  ? -44.614  46.875 36.634  1.00 97.97  ? 25  GLU B OE1 1 
ATOM   2652 O  OE2 . GLU B 1 25  ? -43.189  48.189 37.661  1.00 98.23  ? 25  GLU B OE2 1 
ATOM   2653 N  N   . GLN B 1 26  ? -49.903  49.622 35.518  1.00 90.00  ? 26  GLN B N   1 
ATOM   2654 C  CA  . GLN B 1 26  ? -50.867  49.181 34.514  1.00 82.80  ? 26  GLN B CA  1 
ATOM   2655 C  C   . GLN B 1 26  ? -51.002  50.165 33.357  1.00 81.45  ? 26  GLN B C   1 
ATOM   2656 O  O   . GLN B 1 26  ? -51.340  49.755 32.242  1.00 85.52  ? 26  GLN B O   1 
ATOM   2657 C  CB  . GLN B 1 26  ? -52.231  48.950 35.164  1.00 84.32  ? 26  GLN B CB  1 
ATOM   2658 C  CG  . GLN B 1 26  ? -52.807  50.175 35.857  1.00 83.39  ? 26  GLN B CG  1 
ATOM   2659 C  CD  . GLN B 1 26  ? -54.192  49.927 36.424  1.00 85.91  ? 26  GLN B CD  1 
ATOM   2660 O  OE1 . GLN B 1 26  ? -55.174  49.850 35.685  1.00 84.35  ? 26  GLN B OE1 1 
ATOM   2661 N  NE2 . GLN B 1 26  ? -54.277  49.800 37.745  1.00 85.44  ? 26  GLN B NE2 1 
ATOM   2662 N  N   . LEU B 1 27  ? -50.745  51.453 33.590  1.00 80.78  ? 27  LEU B N   1 
ATOM   2663 C  CA  . LEU B 1 27  ? -50.999  52.463 32.569  1.00 78.21  ? 27  LEU B CA  1 
ATOM   2664 C  C   . LEU B 1 27  ? -49.913  52.548 31.503  1.00 79.22  ? 27  LEU B C   1 
ATOM   2665 O  O   . LEU B 1 27  ? -50.108  53.251 30.507  1.00 81.13  ? 27  LEU B O   1 
ATOM   2666 C  CB  . LEU B 1 27  ? -51.170  53.841 33.214  1.00 77.38  ? 27  LEU B CB  1 
ATOM   2667 C  CG  . LEU B 1 27  ? -52.431  54.065 34.047  1.00 80.94  ? 27  LEU B CG  1 
ATOM   2668 C  CD1 . LEU B 1 27  ? -52.535  55.525 34.466  1.00 75.80  ? 27  LEU B CD1 1 
ATOM   2669 C  CD2 . LEU B 1 27  ? -53.665  53.629 33.273  1.00 72.74  ? 27  LEU B CD2 1 
ATOM   2670 N  N   . ALA B 1 28  ? -48.787  51.856 31.675  1.00 79.63  ? 28  ALA B N   1 
ATOM   2671 C  CA  . ALA B 1 28  ? -47.686  51.996 30.727  1.00 78.99  ? 28  ALA B CA  1 
ATOM   2672 C  C   . ALA B 1 28  ? -48.032  51.381 29.374  1.00 83.79  ? 28  ALA B C   1 
ATOM   2673 O  O   . ALA B 1 28  ? -47.805  51.993 28.323  1.00 76.45  ? 28  ALA B O   1 
ATOM   2674 C  CB  . ALA B 1 28  ? -46.421  51.363 31.301  1.00 81.71  ? 28  ALA B CB  1 
ATOM   2675 N  N   . TRP B 1 29  ? -48.588  50.166 29.382  1.00 80.79  ? 29  TRP B N   1 
ATOM   2676 C  CA  . TRP B 1 29  ? -48.839  49.470 28.120  1.00 77.96  ? 29  TRP B CA  1 
ATOM   2677 C  C   . TRP B 1 29  ? -49.903  50.158 27.272  1.00 80.52  ? 29  TRP B C   1 
ATOM   2678 O  O   . TRP B 1 29  ? -49.680  50.321 26.059  1.00 82.49  ? 29  TRP B O   1 
ATOM   2679 C  CB  . TRP B 1 29  ? -49.185  48.005 28.400  1.00 80.50  ? 29  TRP B CB  1 
ATOM   2680 C  CG  . TRP B 1 29  ? -49.488  47.208 27.174  1.00 81.23  ? 29  TRP B CG  1 
ATOM   2681 C  CD1 . TRP B 1 29  ? -48.589  46.600 26.346  1.00 80.82  ? 29  TRP B CD1 1 
ATOM   2682 C  CD2 . TRP B 1 29  ? -50.784  46.921 26.640  1.00 80.54  ? 29  TRP B CD2 1 
ATOM   2683 N  NE1 . TRP B 1 29  ? -49.246  45.955 25.327  1.00 86.16  ? 29  TRP B NE1 1 
ATOM   2684 C  CE2 . TRP B 1 29  ? -50.595  46.136 25.485  1.00 85.65  ? 29  TRP B CE2 1 
ATOM   2685 C  CE3 . TRP B 1 29  ? -52.087  47.252 27.025  1.00 79.56  ? 29  TRP B CE3 1 
ATOM   2686 C  CZ2 . TRP B 1 29  ? -51.659  45.679 24.712  1.00 83.01  ? 29  TRP B CZ2 1 
ATOM   2687 C  CZ3 . TRP B 1 29  ? -53.142  46.796 26.256  1.00 80.57  ? 29  TRP B CZ3 1 
ATOM   2688 C  CH2 . TRP B 1 29  ? -52.922  46.018 25.113  1.00 83.94  ? 29  TRP B CH2 1 
ATOM   2689 N  N   . PRO B 1 30  ? -51.059  50.574 27.805  1.00 81.37  ? 30  PRO B N   1 
ATOM   2690 C  CA  . PRO B 1 30  ? -52.009  51.307 26.953  1.00 79.23  ? 30  PRO B CA  1 
ATOM   2691 C  C   . PRO B 1 30  ? -51.500  52.668 26.513  1.00 80.18  ? 30  PRO B C   1 
ATOM   2692 O  O   . PRO B 1 30  ? -51.809  53.093 25.393  1.00 81.25  ? 30  PRO B O   1 
ATOM   2693 C  CB  . PRO B 1 30  ? -53.259  51.428 27.837  1.00 82.21  ? 30  PRO B CB  1 
ATOM   2694 C  CG  . PRO B 1 30  ? -52.757  51.289 29.225  1.00 76.62  ? 30  PRO B CG  1 
ATOM   2695 C  CD  . PRO B 1 30  ? -51.635  50.303 29.136  1.00 80.56  ? 30  PRO B CD  1 
ATOM   2696 N  N   . ARG B 1 31  ? -50.734  53.366 27.356  1.00 80.76  ? 31  ARG B N   1 
ATOM   2697 C  CA  . ARG B 1 31  ? -50.196  54.666 26.962  1.00 77.10  ? 31  ARG B CA  1 
ATOM   2698 C  C   . ARG B 1 31  ? -49.203  54.532 25.816  1.00 77.16  ? 31  ARG B C   1 
ATOM   2699 O  O   . ARG B 1 31  ? -49.169  55.380 24.916  1.00 79.46  ? 31  ARG B O   1 
ATOM   2700 C  CB  . ARG B 1 31  ? -49.535  55.350 28.157  1.00 74.85  ? 31  ARG B CB  1 
ATOM   2701 C  CG  . ARG B 1 31  ? -50.474  56.185 29.009  1.00 76.49  ? 31  ARG B CG  1 
ATOM   2702 C  CD  . ARG B 1 31  ? -49.747  56.716 30.232  1.00 73.30  ? 31  ARG B CD  1 
ATOM   2703 N  NE  . ARG B 1 31  ? -50.573  57.607 31.037  1.00 78.64  ? 31  ARG B NE  1 
ATOM   2704 C  CZ  . ARG B 1 31  ? -50.263  58.002 32.265  1.00 79.14  ? 31  ARG B CZ  1 
ATOM   2705 N  NH1 . ARG B 1 31  ? -49.159  57.588 32.865  1.00 78.06  ? 31  ARG B NH1 1 
ATOM   2706 N  NH2 . ARG B 1 31  ? -51.084  58.828 32.909  1.00 76.35  ? 31  ARG B NH2 1 
ATOM   2707 N  N   . SER B 1 32  ? -48.384  53.478 25.831  1.00 73.63  ? 32  SER B N   1 
ATOM   2708 C  CA  . SER B 1 32  ? -47.395  53.302 24.774  1.00 75.24  ? 32  SER B CA  1 
ATOM   2709 C  C   . SER B 1 32  ? -48.055  53.071 23.422  1.00 84.69  ? 32  SER B C   1 
ATOM   2710 O  O   . SER B 1 32  ? -47.489  53.438 22.386  1.00 83.46  ? 32  SER B O   1 
ATOM   2711 C  CB  . SER B 1 32  ? -46.461  52.139 25.109  1.00 74.78  ? 32  SER B CB  1 
ATOM   2712 O  OG  . SER B 1 32  ? -47.151  50.903 25.084  1.00 82.12  ? 32  SER B OG  1 
ATOM   2713 N  N   . LEU B 1 33  ? -49.245  52.471 23.410  1.00 84.00  ? 33  LEU B N   1 
ATOM   2714 C  CA  . LEU B 1 33  ? -49.981  52.217 22.180  1.00 78.32  ? 33  LEU B CA  1 
ATOM   2715 C  C   . LEU B 1 33  ? -50.860  53.387 21.754  1.00 78.36  ? 33  LEU B C   1 
ATOM   2716 O  O   . LEU B 1 33  ? -51.407  53.355 20.647  1.00 81.54  ? 33  LEU B O   1 
ATOM   2717 C  CB  . LEU B 1 33  ? -50.855  50.963 22.330  1.00 85.50  ? 33  LEU B CB  1 
ATOM   2718 C  CG  . LEU B 1 33  ? -50.254  49.592 22.007  1.00 84.39  ? 33  LEU B CG  1 
ATOM   2719 C  CD1 . LEU B 1 33  ? -49.749  49.553 20.569  1.00 89.64  ? 33  LEU B CD1 1 
ATOM   2720 C  CD2 . LEU B 1 33  ? -49.148  49.221 22.982  1.00 82.79  ? 33  LEU B CD2 1 
ATOM   2721 N  N   . GLY B 1 34  ? -51.008  54.410 22.593  1.00 80.54  ? 34  GLY B N   1 
ATOM   2722 C  CA  . GLY B 1 34  ? -51.913  55.502 22.299  1.00 70.53  ? 34  GLY B CA  1 
ATOM   2723 C  C   . GLY B 1 34  ? -53.349  55.270 22.711  1.00 72.11  ? 34  GLY B C   1 
ATOM   2724 O  O   . GLY B 1 34  ? -54.202  56.118 22.429  1.00 68.16  ? 34  GLY B O   1 
ATOM   2725 N  N   . LEU B 1 35  ? -53.643  54.147 23.374  1.00 75.83  ? 35  LEU B N   1 
ATOM   2726 C  CA  . LEU B 1 35  ? -55.013  53.850 23.782  1.00 68.99  ? 35  LEU B CA  1 
ATOM   2727 C  C   . LEU B 1 35  ? -55.482  54.771 24.901  1.00 73.07  ? 35  LEU B C   1 
ATOM   2728 O  O   . LEU B 1 35  ? -56.685  55.030 25.025  1.00 70.44  ? 35  LEU B O   1 
ATOM   2729 C  CB  . LEU B 1 35  ? -55.120  52.386 24.211  1.00 79.23  ? 35  LEU B CB  1 
ATOM   2730 C  CG  . LEU B 1 35  ? -54.734  51.345 23.156  1.00 76.58  ? 35  LEU B CG  1 
ATOM   2731 C  CD1 . LEU B 1 35  ? -54.745  49.947 23.752  1.00 79.51  ? 35  LEU B CD1 1 
ATOM   2732 C  CD2 . LEU B 1 35  ? -55.665  51.425 21.957  1.00 72.53  ? 35  LEU B CD2 1 
ATOM   2733 N  N   . ILE B 1 36  ? -54.559  55.267 25.721  1.00 75.49  ? 36  ILE B N   1 
ATOM   2734 C  CA  . ILE B 1 36  ? -54.848  56.263 26.745  1.00 72.42  ? 36  ILE B CA  1 
ATOM   2735 C  C   . ILE B 1 36  ? -53.877  57.418 26.555  1.00 76.08  ? 36  ILE B C   1 
ATOM   2736 O  O   . ILE B 1 36  ? -52.659  57.206 26.514  1.00 79.58  ? 36  ILE B O   1 
ATOM   2737 C  CB  . ILE B 1 36  ? -54.723  55.683 28.167  1.00 74.11  ? 36  ILE B CB  1 
ATOM   2738 C  CG1 . ILE B 1 36  ? -55.712  54.536 28.375  1.00 67.60  ? 36  ILE B CG1 1 
ATOM   2739 C  CG2 . ILE B 1 36  ? -54.933  56.775 29.209  1.00 75.27  ? 36  ILE B CG2 1 
ATOM   2740 C  CD1 . ILE B 1 36  ? -55.583  53.875 29.726  1.00 68.44  ? 36  ILE B CD1 1 
ATOM   2741 N  N   . ARG B 1 37  ? -54.408  58.634 26.437  1.00 71.65  ? 37  ARG B N   1 
ATOM   2742 C  CA  . ARG B 1 37  ? -53.550  59.788 26.198  1.00 74.64  ? 37  ARG B CA  1 
ATOM   2743 C  C   . ARG B 1 37  ? -53.791  60.899 27.211  1.00 71.30  ? 37  ARG B C   1 
ATOM   2744 O  O   . ARG B 1 37  ? -52.837  61.425 27.792  1.00 76.56  ? 37  ARG B O   1 
ATOM   2745 C  CB  . ARG B 1 37  ? -53.748  60.324 24.777  1.00 72.84  ? 37  ARG B CB  1 
ATOM   2746 C  CG  . ARG B 1 37  ? -53.038  59.517 23.706  1.00 77.56  ? 37  ARG B CG  1 
ATOM   2747 C  CD  . ARG B 1 37  ? -52.727  60.380 22.495  1.00 79.99  ? 37  ARG B CD  1 
ATOM   2748 N  NE  . ARG B 1 37  ? -53.318  59.852 21.272  1.00 76.11  ? 37  ARG B NE  1 
ATOM   2749 C  CZ  . ARG B 1 37  ? -52.689  59.052 20.423  1.00 81.54  ? 37  ARG B CZ  1 
ATOM   2750 N  NH1 . ARG B 1 37  ? -51.442  58.662 20.637  1.00 86.53  ? 37  ARG B NH1 1 
ATOM   2751 N  NH2 . ARG B 1 37  ? -53.326  58.634 19.332  1.00 78.00  ? 37  ARG B NH2 1 
ATOM   2752 N  N   . SER B 1 38  ? -55.048  61.275 27.423  1.00 71.15  ? 38  SER B N   1 
ATOM   2753 C  CA  . SER B 1 38  ? -55.332  62.353 28.354  1.00 70.61  ? 38  SER B CA  1 
ATOM   2754 C  C   . SER B 1 38  ? -55.268  61.847 29.790  1.00 71.54  ? 38  SER B C   1 
ATOM   2755 O  O   . SER B 1 38  ? -55.304  60.643 30.057  1.00 72.70  ? 38  SER B O   1 
ATOM   2756 C  CB  . SER B 1 38  ? -56.703  62.971 28.075  1.00 70.03  ? 38  SER B CB  1 
ATOM   2757 O  OG  . SER B 1 38  ? -57.747  62.047 28.324  1.00 68.25  ? 38  SER B OG  1 
ATOM   2758 N  N   . ASP B 1 39  ? -55.160  62.794 30.725  1.00 76.40  ? 39  ASP B N   1 
ATOM   2759 C  CA  . ASP B 1 39  ? -55.164  62.430 32.138  1.00 70.83  ? 39  ASP B CA  1 
ATOM   2760 C  C   . ASP B 1 39  ? -56.526  61.893 32.560  1.00 74.00  ? 39  ASP B C   1 
ATOM   2761 O  O   . ASP B 1 39  ? -56.607  60.948 33.354  1.00 79.64  ? 39  ASP B O   1 
ATOM   2762 C  CB  . ASP B 1 39  ? -54.769  63.635 32.994  1.00 80.80  ? 39  ASP B CB  1 
ATOM   2763 C  CG  . ASP B 1 39  ? -55.702  64.829 32.802  1.00 89.26  ? 39  ASP B CG  1 
ATOM   2764 O  OD1 . ASP B 1 39  ? -56.493  64.833 31.833  1.00 76.29  ? 39  ASP B OD1 1 
ATOM   2765 O  OD2 . ASP B 1 39  ? -55.648  65.765 33.628  1.00 94.79  ? 39  ASP B OD2 1 
ATOM   2766 N  N   . ALA B 1 40  ? -57.605  62.486 32.040  1.00 73.28  ? 40  ALA B N   1 
ATOM   2767 C  CA  . ALA B 1 40  ? -58.945  62.007 32.362  1.00 72.55  ? 40  ALA B CA  1 
ATOM   2768 C  C   . ALA B 1 40  ? -59.149  60.577 31.881  1.00 75.52  ? 40  ALA B C   1 
ATOM   2769 O  O   . ALA B 1 40  ? -59.766  59.762 32.578  1.00 76.01  ? 40  ALA B O   1 
ATOM   2770 C  CB  . ALA B 1 40  ? -59.996  62.933 31.751  1.00 69.03  ? 40  ALA B CB  1 
ATOM   2771 N  N   . ALA B 1 41  ? -58.640  60.255 30.688  1.00 67.63  ? 41  ALA B N   1 
ATOM   2772 C  CA  . ALA B 1 41  ? -58.708  58.881 30.201  1.00 74.23  ? 41  ALA B CA  1 
ATOM   2773 C  C   . ALA B 1 41  ? -57.946  57.935 31.119  1.00 74.36  ? 41  ALA B C   1 
ATOM   2774 O  O   . ALA B 1 41  ? -58.361  56.789 31.325  1.00 78.36  ? 41  ALA B O   1 
ATOM   2775 C  CB  . ALA B 1 41  ? -58.166  58.800 28.772  1.00 66.07  ? 41  ALA B CB  1 
ATOM   2776 N  N   . ALA B 1 42  ? -56.826  58.398 31.682  1.00 73.51  ? 42  ALA B N   1 
ATOM   2777 C  CA  . ALA B 1 42  ? -56.071  57.572 32.618  1.00 72.53  ? 42  ALA B CA  1 
ATOM   2778 C  C   . ALA B 1 42  ? -56.835  57.376 33.921  1.00 73.04  ? 42  ALA B C   1 
ATOM   2779 O  O   . ALA B 1 42  ? -56.869  56.266 34.465  1.00 68.33  ? 42  ALA B O   1 
ATOM   2780 C  CB  . ALA B 1 42  ? -54.701  58.197 32.882  1.00 70.57  ? 42  ALA B CB  1 
ATOM   2781 N  N   . GLU B 1 43  ? -57.455  58.441 34.436  1.00 72.30  ? 43  GLU B N   1 
ATOM   2782 C  CA  . GLU B 1 43  ? -58.259  58.321 35.648  1.00 74.71  ? 43  GLU B CA  1 
ATOM   2783 C  C   . GLU B 1 43  ? -59.432  57.373 35.433  1.00 77.69  ? 43  GLU B C   1 
ATOM   2784 O  O   . GLU B 1 43  ? -59.702  56.502 36.268  1.00 78.04  ? 43  GLU B O   1 
ATOM   2785 C  CB  . GLU B 1 43  ? -58.758  59.698 36.090  1.00 73.88  ? 43  GLU B CB  1 
ATOM   2786 C  CG  . GLU B 1 43  ? -57.659  60.663 36.506  1.00 83.94  ? 43  GLU B CG  1 
ATOM   2787 C  CD  . GLU B 1 43  ? -57.005  60.279 37.823  1.00 98.98  ? 43  GLU B CD  1 
ATOM   2788 O  OE1 . GLU B 1 43  ? -57.597  59.478 38.579  1.00 95.36  ? 43  GLU B OE1 1 
ATOM   2789 O  OE2 . GLU B 1 43  ? -55.896  60.782 38.101  1.00 102.83 ? 43  GLU B OE2 1 
ATOM   2790 N  N   . ARG B 1 44  ? -60.141  57.531 34.311  1.00 76.66  ? 44  ARG B N   1 
ATOM   2791 C  CA  . ARG B 1 44  ? -61.275  56.659 34.019  1.00 76.78  ? 44  ARG B CA  1 
ATOM   2792 C  C   . ARG B 1 44  ? -60.842  55.200 33.964  1.00 74.13  ? 44  ARG B C   1 
ATOM   2793 O  O   . ARG B 1 44  ? -61.577  54.307 34.404  1.00 74.69  ? 44  ARG B O   1 
ATOM   2794 C  CB  . ARG B 1 44  ? -61.927  57.074 32.700  1.00 72.00  ? 44  ARG B CB  1 
ATOM   2795 C  CG  . ARG B 1 44  ? -63.358  56.593 32.537  1.00 78.19  ? 44  ARG B CG  1 
ATOM   2796 C  CD  . ARG B 1 44  ? -63.874  56.871 31.139  1.00 64.27  ? 44  ARG B CD  1 
ATOM   2797 N  NE  . ARG B 1 44  ? -63.495  55.813 30.212  1.00 74.07  ? 44  ARG B NE  1 
ATOM   2798 C  CZ  . ARG B 1 44  ? -64.350  54.978 29.639  1.00 65.35  ? 44  ARG B CZ  1 
ATOM   2799 N  NH1 . ARG B 1 44  ? -65.654  55.078 29.837  1.00 66.08  ? 44  ARG B NH1 1 
ATOM   2800 N  NH2 . ARG B 1 44  ? -63.884  54.022 28.841  1.00 58.78  ? 44  ARG B NH2 1 
ATOM   2801 N  N   . HIS B 1 45  ? -59.643  54.943 33.440  1.00 64.84  ? 45  HIS B N   1 
ATOM   2802 C  CA  . HIS B 1 45  ? -59.142  53.576 33.366  1.00 69.28  ? 45  HIS B CA  1 
ATOM   2803 C  C   . HIS B 1 45  ? -58.874  53.014 34.757  1.00 71.45  ? 45  HIS B C   1 
ATOM   2804 O  O   . HIS B 1 45  ? -59.268  51.884 35.067  1.00 73.28  ? 45  HIS B O   1 
ATOM   2805 C  CB  . HIS B 1 45  ? -57.875  53.534 32.510  1.00 63.25  ? 45  HIS B CB  1 
ATOM   2806 C  CG  . HIS B 1 45  ? -57.524  52.165 32.018  1.00 65.46  ? 45  HIS B CG  1 
ATOM   2807 N  ND1 . HIS B 1 45  ? -58.154  51.578 30.941  1.00 67.12  ? 45  HIS B ND1 1 
ATOM   2808 C  CD2 . HIS B 1 45  ? -56.610  51.267 32.454  1.00 66.03  ? 45  HIS B CD2 1 
ATOM   2809 C  CE1 . HIS B 1 45  ? -57.642  50.378 30.735  1.00 69.61  ? 45  HIS B CE1 1 
ATOM   2810 N  NE2 . HIS B 1 45  ? -56.704  50.164 31.640  1.00 67.16  ? 45  HIS B NE2 1 
ATOM   2811 N  N   . LEU B 1 46  ? -58.206  53.797 35.612  1.00 71.72  ? 46  LEU B N   1 
ATOM   2812 C  CA  . LEU B 1 46  ? -57.877  53.325 36.954  1.00 71.18  ? 46  LEU B CA  1 
ATOM   2813 C  C   . LEU B 1 46  ? -59.133  53.022 37.760  1.00 69.33  ? 46  LEU B C   1 
ATOM   2814 O  O   . LEU B 1 46  ? -59.181  52.030 38.494  1.00 76.15  ? 46  LEU B O   1 
ATOM   2815 C  CB  . LEU B 1 46  ? -57.015  54.357 37.681  1.00 64.42  ? 46  LEU B CB  1 
ATOM   2816 C  CG  . LEU B 1 46  ? -55.649  54.656 37.062  1.00 72.30  ? 46  LEU B CG  1 
ATOM   2817 C  CD1 . LEU B 1 46  ? -54.929  55.726 37.862  1.00 67.34  ? 46  LEU B CD1 1 
ATOM   2818 C  CD2 . LEU B 1 46  ? -54.809  53.393 36.966  1.00 67.31  ? 46  LEU B CD2 1 
ATOM   2819 N  N   . ARG B 1 47  ? -60.164  53.860 37.629  1.00 69.30  ? 47  ARG B N   1 
ATOM   2820 C  CA  . ARG B 1 47  ? -61.422  53.616 38.324  1.00 62.14  ? 47  ARG B CA  1 
ATOM   2821 C  C   . ARG B 1 47  ? -62.067  52.293 37.933  1.00 70.40  ? 47  ARG B C   1 
ATOM   2822 O  O   . ARG B 1 47  ? -63.013  51.865 38.604  1.00 71.38  ? 47  ARG B O   1 
ATOM   2823 C  CB  . ARG B 1 47  ? -62.404  54.759 38.059  1.00 64.24  ? 47  ARG B CB  1 
ATOM   2824 C  CG  . ARG B 1 47  ? -61.980  56.096 38.639  1.00 76.11  ? 47  ARG B CG  1 
ATOM   2825 C  CD  . ARG B 1 47  ? -63.134  57.091 38.629  1.00 80.45  ? 47  ARG B CD  1 
ATOM   2826 N  NE  . ARG B 1 47  ? -63.608  57.374 37.279  1.00 90.47  ? 47  ARG B NE  1 
ATOM   2827 C  CZ  . ARG B 1 47  ? -63.219  58.411 36.550  1.00 89.55  ? 47  ARG B CZ  1 
ATOM   2828 N  NH1 . ARG B 1 47  ? -62.354  59.298 37.016  1.00 87.67  ? 47  ARG B NH1 1 
ATOM   2829 N  NH2 . ARG B 1 47  ? -63.711  58.563 35.323  1.00 89.28  ? 47  ARG B NH2 1 
ATOM   2830 N  N   . GLY B 1 48  ? -61.594  51.644 36.867  1.00 75.69  ? 48  GLY B N   1 
ATOM   2831 C  CA  . GLY B 1 48  ? -62.131  50.347 36.499  1.00 76.37  ? 48  GLY B CA  1 
ATOM   2832 C  C   . GLY B 1 48  ? -61.589  49.206 37.331  1.00 77.61  ? 48  GLY B C   1 
ATOM   2833 O  O   . GLY B 1 48  ? -62.253  48.175 37.474  1.00 79.34  ? 48  GLY B O   1 
ATOM   2834 N  N   . GLY B 1 49  ? -60.394  49.366 37.894  1.00 72.71  ? 49  GLY B N   1 
ATOM   2835 C  CA  . GLY B 1 49  ? -59.787  48.297 38.664  1.00 67.43  ? 49  GLY B CA  1 
ATOM   2836 C  C   . GLY B 1 49  ? -59.414  47.089 37.838  1.00 80.46  ? 49  GLY B C   1 
ATOM   2837 O  O   . GLY B 1 49  ? -59.495  45.959 38.331  1.00 84.37  ? 49  GLY B O   1 
ATOM   2838 N  N   . TYR B 1 50  ? -59.006  47.299 36.584  1.00 79.39  ? 50  TYR B N   1 
ATOM   2839 C  CA  . TYR B 1 50  ? -58.702  46.179 35.700  1.00 75.81  ? 50  TYR B CA  1 
ATOM   2840 C  C   . TYR B 1 50  ? -57.452  45.436 36.148  1.00 79.44  ? 50  TYR B C   1 
ATOM   2841 O  O   . TYR B 1 50  ? -57.317  44.235 35.886  1.00 75.74  ? 50  TYR B O   1 
ATOM   2842 C  CB  . TYR B 1 50  ? -58.564  46.689 34.264  1.00 68.44  ? 50  TYR B CB  1 
ATOM   2843 C  CG  . TYR B 1 50  ? -59.738  47.551 33.861  1.00 71.59  ? 50  TYR B CG  1 
ATOM   2844 C  CD1 . TYR B 1 50  ? -61.040  47.101 34.040  1.00 73.49  ? 50  TYR B CD1 1 
ATOM   2845 C  CD2 . TYR B 1 50  ? -59.551  48.827 33.346  1.00 69.72  ? 50  TYR B CD2 1 
ATOM   2846 C  CE1 . TYR B 1 50  ? -62.121  47.884 33.696  1.00 72.46  ? 50  TYR B CE1 1 
ATOM   2847 C  CE2 . TYR B 1 50  ? -60.629  49.620 32.998  1.00 65.87  ? 50  TYR B CE2 1 
ATOM   2848 C  CZ  . TYR B 1 50  ? -61.912  49.141 33.176  1.00 72.01  ? 50  TYR B CZ  1 
ATOM   2849 O  OH  . TYR B 1 50  ? -62.994  49.919 32.836  1.00 71.85  ? 50  TYR B OH  1 
ATOM   2850 N  N   . ALA B 1 51  ? -56.535  46.124 36.829  1.00 81.17  ? 51  ALA B N   1 
ATOM   2851 C  CA  . ALA B 1 51  ? -55.405  45.432 37.434  1.00 77.91  ? 51  ALA B CA  1 
ATOM   2852 C  C   . ALA B 1 51  ? -55.859  44.594 38.621  1.00 77.79  ? 51  ALA B C   1 
ATOM   2853 O  O   . ALA B 1 51  ? -55.407  43.456 38.795  1.00 76.38  ? 51  ALA B O   1 
ATOM   2854 C  CB  . ALA B 1 51  ? -54.337  46.437 37.854  1.00 76.36  ? 51  ALA B CB  1 
ATOM   2855 N  N   . ASP B 1 52  ? -56.759  45.138 39.443  1.00 75.43  ? 52  ASP B N   1 
ATOM   2856 C  CA  . ASP B 1 52  ? -57.364  44.338 40.502  1.00 79.03  ? 52  ASP B CA  1 
ATOM   2857 C  C   . ASP B 1 52  ? -58.074  43.121 39.927  1.00 79.12  ? 52  ASP B C   1 
ATOM   2858 O  O   . ASP B 1 52  ? -57.937  42.010 40.449  1.00 76.55  ? 52  ASP B O   1 
ATOM   2859 C  CB  . ASP B 1 52  ? -58.335  45.188 41.321  1.00 76.49  ? 52  ASP B CB  1 
ATOM   2860 C  CG  . ASP B 1 52  ? -59.182  44.355 42.268  1.00 83.57  ? 52  ASP B CG  1 
ATOM   2861 O  OD1 . ASP B 1 52  ? -58.617  43.486 42.963  1.00 86.50  ? 52  ASP B OD1 1 
ATOM   2862 O  OD2 . ASP B 1 52  ? -60.411  44.573 42.324  1.00 91.95  ? 52  ASP B OD2 1 
ATOM   2863 N  N   . LEU B 1 53  ? -58.825  43.309 38.839  1.00 84.15  ? 53  LEU B N   1 
ATOM   2864 C  CA  . LEU B 1 53  ? -59.539  42.194 38.226  1.00 82.65  ? 53  LEU B CA  1 
ATOM   2865 C  C   . LEU B 1 53  ? -58.577  41.112 37.750  1.00 79.27  ? 53  LEU B C   1 
ATOM   2866 O  O   . LEU B 1 53  ? -58.816  39.918 37.970  1.00 76.80  ? 53  LEU B O   1 
ATOM   2867 C  CB  . LEU B 1 53  ? -60.396  42.697 37.066  1.00 75.94  ? 53  LEU B CB  1 
ATOM   2868 C  CG  . LEU B 1 53  ? -61.130  41.614 36.274  1.00 78.08  ? 53  LEU B CG  1 
ATOM   2869 C  CD1 . LEU B 1 53  ? -62.093  40.853 37.169  1.00 78.94  ? 53  LEU B CD1 1 
ATOM   2870 C  CD2 . LEU B 1 53  ? -61.860  42.217 35.085  1.00 79.30  ? 53  LEU B CD2 1 
ATOM   2871 N  N   . ALA B 1 54  ? -57.480  41.507 37.099  1.00 75.81  ? 54  ALA B N   1 
ATOM   2872 C  CA  . ALA B 1 54  ? -56.505  40.523 36.643  1.00 77.99  ? 54  ALA B CA  1 
ATOM   2873 C  C   . ALA B 1 54  ? -55.847  39.800 37.812  1.00 83.53  ? 54  ALA B C   1 
ATOM   2874 O  O   . ALA B 1 54  ? -55.521  38.612 37.701  1.00 83.08  ? 54  ALA B O   1 
ATOM   2875 C  CB  . ALA B 1 54  ? -55.447  41.197 35.770  1.00 74.53  ? 54  ALA B CB  1 
ATOM   2876 N  N   . SER B 1 55  ? -55.647  40.492 38.938  1.00 78.36  ? 55  SER B N   1 
ATOM   2877 C  CA  . SER B 1 55  ? -55.046  39.842 40.099  1.00 83.69  ? 55  SER B CA  1 
ATOM   2878 C  C   . SER B 1 55  ? -55.970  38.785 40.692  1.00 81.12  ? 55  SER B C   1 
ATOM   2879 O  O   . SER B 1 55  ? -55.493  37.806 41.276  1.00 82.77  ? 55  SER B O   1 
ATOM   2880 C  CB  . SER B 1 55  ? -54.681  40.879 41.162  1.00 80.62  ? 55  SER B CB  1 
ATOM   2881 O  OG  . SER B 1 55  ? -55.840  41.414 41.776  1.00 85.13  ? 55  SER B OG  1 
ATOM   2882 N  N   . ARG B 1 56  ? -57.287  38.963 40.559  1.00 77.67  ? 56  ARG B N   1 
ATOM   2883 C  CA  . ARG B 1 56  ? -58.217  37.929 41.004  1.00 80.94  ? 56  ARG B CA  1 
ATOM   2884 C  C   . ARG B 1 56  ? -58.241  36.756 40.032  1.00 82.32  ? 56  ARG B C   1 
ATOM   2885 O  O   . ARG B 1 56  ? -58.262  35.593 40.451  1.00 83.00  ? 56  ARG B O   1 
ATOM   2886 C  CB  . ARG B 1 56  ? -59.621  38.511 41.150  1.00 86.93  ? 56  ARG B CB  1 
ATOM   2887 C  CG  . ARG B 1 56  ? -59.688  39.859 41.831  1.00 82.59  ? 56  ARG B CG  1 
ATOM   2888 C  CD  . ARG B 1 56  ? -59.567  39.740 43.325  1.00 81.07  ? 56  ARG B CD  1 
ATOM   2889 N  NE  . ARG B 1 56  ? -59.907  40.996 43.979  1.00 90.32  ? 56  ARG B NE  1 
ATOM   2890 C  CZ  . ARG B 1 56  ? -60.035  41.142 45.290  1.00 91.14  ? 56  ARG B CZ  1 
ATOM   2891 N  NH1 . ARG B 1 56  ? -59.862  40.123 46.116  1.00 81.94  ? 56  ARG B NH1 1 
ATOM   2892 N  NH2 . ARG B 1 56  ? -60.348  42.337 45.783  1.00 88.54  ? 56  ARG B NH2 1 
ATOM   2893 N  N   . PHE B 1 57  ? -58.254  37.045 38.727  1.00 78.75  ? 57  PHE B N   1 
ATOM   2894 C  CA  . PHE B 1 57  ? -58.316  35.984 37.728  1.00 79.65  ? 57  PHE B CA  1 
ATOM   2895 C  C   . PHE B 1 57  ? -57.060  35.125 37.751  1.00 79.24  ? 57  PHE B C   1 
ATOM   2896 O  O   . PHE B 1 57  ? -57.131  33.904 37.571  1.00 76.64  ? 57  PHE B O   1 
ATOM   2897 C  CB  . PHE B 1 57  ? -58.522  36.584 36.337  1.00 79.58  ? 57  PHE B CB  1 
ATOM   2898 C  CG  . PHE B 1 57  ? -59.943  36.975 36.043  1.00 77.70  ? 57  PHE B CG  1 
ATOM   2899 C  CD1 . PHE B 1 57  ? -60.993  36.420 36.756  1.00 73.38  ? 57  PHE B CD1 1 
ATOM   2900 C  CD2 . PHE B 1 57  ? -60.227  37.895 35.045  1.00 76.97  ? 57  PHE B CD2 1 
ATOM   2901 C  CE1 . PHE B 1 57  ? -62.301  36.778 36.481  1.00 78.94  ? 57  PHE B CE1 1 
ATOM   2902 C  CE2 . PHE B 1 57  ? -61.533  38.255 34.763  1.00 71.42  ? 57  PHE B CE2 1 
ATOM   2903 C  CZ  . PHE B 1 57  ? -62.571  37.697 35.481  1.00 78.98  ? 57  PHE B CZ  1 
ATOM   2904 N  N   . TYR B 1 58  ? -55.901  35.738 37.970  1.00 82.30  ? 58  TYR B N   1 
ATOM   2905 C  CA  . TYR B 1 58  ? -54.617  35.046 37.881  1.00 86.13  ? 58  TYR B CA  1 
ATOM   2906 C  C   . TYR B 1 58  ? -53.815  35.269 39.157  1.00 84.55  ? 58  TYR B C   1 
ATOM   2907 O  O   . TYR B 1 58  ? -52.784  35.952 39.144  1.00 87.04  ? 58  TYR B O   1 
ATOM   2908 C  CB  . TYR B 1 58  ? -53.838  35.521 36.655  1.00 82.18  ? 58  TYR B CB  1 
ATOM   2909 C  CG  . TYR B 1 58  ? -54.708  35.773 35.441  1.00 84.84  ? 58  TYR B CG  1 
ATOM   2910 C  CD1 . TYR B 1 58  ? -55.202  34.718 34.684  1.00 86.28  ? 58  TYR B CD1 1 
ATOM   2911 C  CD2 . TYR B 1 58  ? -55.029  37.067 35.048  1.00 83.24  ? 58  TYR B CD2 1 
ATOM   2912 C  CE1 . TYR B 1 58  ? -55.994  34.945 33.572  1.00 82.51  ? 58  TYR B CE1 1 
ATOM   2913 C  CE2 . TYR B 1 58  ? -55.819  37.302 33.938  1.00 81.34  ? 58  TYR B CE2 1 
ATOM   2914 C  CZ  . TYR B 1 58  ? -56.298  36.239 33.204  1.00 81.59  ? 58  TYR B CZ  1 
ATOM   2915 O  OH  . TYR B 1 58  ? -57.083  36.470 32.097  1.00 81.57  ? 58  TYR B OH  1 
ATOM   2916 N  N   . PRO B 1 59  ? -54.254  34.693 40.283  1.00 83.11  ? 59  PRO B N   1 
ATOM   2917 C  CA  . PRO B 1 59  ? -53.462  34.829 41.515  1.00 87.49  ? 59  PRO B CA  1 
ATOM   2918 C  C   . PRO B 1 59  ? -52.160  34.055 41.464  1.00 87.77  ? 59  PRO B C   1 
ATOM   2919 O  O   . PRO B 1 59  ? -51.200  34.423 42.152  1.00 90.65  ? 59  PRO B O   1 
ATOM   2920 C  CB  . PRO B 1 59  ? -54.403  34.285 42.598  1.00 83.67  ? 59  PRO B CB  1 
ATOM   2921 C  CG  . PRO B 1 59  ? -55.240  33.288 41.877  1.00 83.50  ? 59  PRO B CG  1 
ATOM   2922 C  CD  . PRO B 1 59  ? -55.435  33.833 40.482  1.00 81.52  ? 59  PRO B CD  1 
ATOM   2923 N  N   . HIS B 1 60  ? -52.101  32.999 40.658  1.00 85.68  ? 60  HIS B N   1 
ATOM   2924 C  CA  . HIS B 1 60  ? -50.909  32.183 40.481  1.00 83.17  ? 60  HIS B CA  1 
ATOM   2925 C  C   . HIS B 1 60  ? -49.851  32.845 39.612  1.00 83.91  ? 60  HIS B C   1 
ATOM   2926 O  O   . HIS B 1 60  ? -48.824  32.215 39.334  1.00 92.14  ? 60  HIS B O   1 
ATOM   2927 C  CB  . HIS B 1 60  ? -51.301  30.841 39.863  1.00 87.89  ? 60  HIS B CB  1 
ATOM   2928 C  CG  . HIS B 1 60  ? -52.006  30.973 38.549  1.00 89.90  ? 60  HIS B CG  1 
ATOM   2929 N  ND1 . HIS B 1 60  ? -53.269  31.511 38.432  1.00 88.97  ? 60  HIS B ND1 1 
ATOM   2930 C  CD2 . HIS B 1 60  ? -51.621  30.643 37.293  1.00 94.89  ? 60  HIS B CD2 1 
ATOM   2931 C  CE1 . HIS B 1 60  ? -53.634  31.505 37.163  1.00 86.46  ? 60  HIS B CE1 1 
ATOM   2932 N  NE2 . HIS B 1 60  ? -52.652  30.983 36.450  1.00 91.26  ? 60  HIS B NE2 1 
ATOM   2933 N  N   . ALA B 1 61  ? -50.070  34.079 39.168  1.00 85.49  ? 61  ALA B N   1 
ATOM   2934 C  CA  . ALA B 1 61  ? -49.161  34.760 38.259  1.00 89.31  ? 61  ALA B CA  1 
ATOM   2935 C  C   . ALA B 1 61  ? -48.564  35.988 38.929  1.00 86.09  ? 61  ALA B C   1 
ATOM   2936 O  O   . ALA B 1 61  ? -49.219  36.659 39.734  1.00 80.72  ? 61  ALA B O   1 
ATOM   2937 C  CB  . ALA B 1 61  ? -49.874  35.171 36.966  1.00 83.90  ? 61  ALA B CB  1 
ATOM   2938 N  N   . THR B 1 62  ? -47.309  36.276 38.585  1.00 87.97  ? 62  THR B N   1 
ATOM   2939 C  CA  . THR B 1 62  ? -46.593  37.421 39.129  1.00 92.93  ? 62  THR B CA  1 
ATOM   2940 C  C   . THR B 1 62  ? -45.743  38.053 38.037  1.00 94.01  ? 62  THR B C   1 
ATOM   2941 O  O   . THR B 1 62  ? -45.310  37.382 37.096  1.00 94.45  ? 62  THR B O   1 
ATOM   2942 C  CB  . THR B 1 62  ? -45.682  37.036 40.306  1.00 93.20  ? 62  THR B CB  1 
ATOM   2943 O  OG1 . THR B 1 62  ? -44.816  35.963 39.913  1.00 92.81  ? 62  THR B OG1 1 
ATOM   2944 C  CG2 . THR B 1 62  ? -46.499  36.617 41.526  1.00 80.50  ? 62  THR B CG2 1 
ATOM   2945 N  N   . GLY B 1 63  ? -45.512  39.353 38.173  1.00 88.93  ? 63  GLY B N   1 
ATOM   2946 C  CA  . GLY B 1 63  ? -44.553  40.028 37.316  1.00 90.39  ? 63  GLY B CA  1 
ATOM   2947 C  C   . GLY B 1 63  ? -45.026  40.114 35.880  1.00 94.22  ? 63  GLY B C   1 
ATOM   2948 O  O   . GLY B 1 63  ? -46.061  40.720 35.577  1.00 92.98  ? 63  GLY B O   1 
ATOM   2949 N  N   . ALA B 1 64  ? -44.255  39.505 34.975  1.00 94.51  ? 64  ALA B N   1 
ATOM   2950 C  CA  . ALA B 1 64  ? -44.589  39.560 33.556  1.00 88.26  ? 64  ALA B CA  1 
ATOM   2951 C  C   . ALA B 1 64  ? -45.868  38.790 33.253  1.00 90.54  ? 64  ALA B C   1 
ATOM   2952 O  O   . ALA B 1 64  ? -46.712  39.258 32.480  1.00 87.83  ? 64  ALA B O   1 
ATOM   2953 C  CB  . ALA B 1 64  ? -43.430  39.016 32.724  1.00 83.61  ? 64  ALA B CB  1 
ATOM   2954 N  N   . ASP B 1 65  ? -46.023  37.603 33.846  1.00 93.13  ? 65  ASP B N   1 
ATOM   2955 C  CA  . ASP B 1 65  ? -47.227  36.812 33.617  1.00 91.25  ? 65  ASP B CA  1 
ATOM   2956 C  C   . ASP B 1 65  ? -48.471  37.541 34.110  1.00 88.48  ? 65  ASP B C   1 
ATOM   2957 O  O   . ASP B 1 65  ? -49.521  37.502 33.459  1.00 87.99  ? 65  ASP B O   1 
ATOM   2958 C  CB  . ASP B 1 65  ? -47.093  35.449 34.296  1.00 89.69  ? 65  ASP B CB  1 
ATOM   2959 C  CG  . ASP B 1 65  ? -45.933  34.642 33.751  1.00 94.37  ? 65  ASP B CG  1 
ATOM   2960 O  OD1 . ASP B 1 65  ? -45.655  34.746 32.536  1.00 93.07  ? 65  ASP B OD1 1 
ATOM   2961 O  OD2 . ASP B 1 65  ? -45.297  33.908 34.538  1.00 101.75 ? 65  ASP B OD2 1 
ATOM   2962 N  N   . LEU B 1 66  ? -48.372  38.219 35.255  1.00 84.85  ? 66  LEU B N   1 
ATOM   2963 C  CA  . LEU B 1 66  ? -49.503  39.007 35.729  1.00 84.81  ? 66  LEU B CA  1 
ATOM   2964 C  C   . LEU B 1 66  ? -49.723  40.247 34.869  1.00 87.36  ? 66  LEU B C   1 
ATOM   2965 O  O   . LEU B 1 66  ? -50.869  40.671 34.682  1.00 85.70  ? 66  LEU B O   1 
ATOM   2966 C  CB  . LEU B 1 66  ? -49.295  39.405 37.190  1.00 85.13  ? 66  LEU B CB  1 
ATOM   2967 C  CG  . LEU B 1 66  ? -50.463  40.149 37.842  1.00 83.21  ? 66  LEU B CG  1 
ATOM   2968 C  CD1 . LEU B 1 66  ? -51.717  39.287 37.838  1.00 78.18  ? 66  LEU B CD1 1 
ATOM   2969 C  CD2 . LEU B 1 66  ? -50.112  40.587 39.255  1.00 84.64  ? 66  LEU B CD2 1 
ATOM   2970 N  N   . ASP B 1 67  ? -48.647  40.833 34.335  1.00 90.68  ? 67  ASP B N   1 
ATOM   2971 C  CA  . ASP B 1 67  ? -48.781  42.053 33.542  1.00 84.94  ? 67  ASP B CA  1 
ATOM   2972 C  C   . ASP B 1 67  ? -49.538  41.797 32.245  1.00 85.11  ? 67  ASP B C   1 
ATOM   2973 O  O   . ASP B 1 67  ? -50.336  42.637 31.813  1.00 85.30  ? 67  ASP B O   1 
ATOM   2974 C  CB  . ASP B 1 67  ? -47.403  42.648 33.249  1.00 88.69  ? 67  ASP B CB  1 
ATOM   2975 C  CG  . ASP B 1 67  ? -46.944  43.609 34.328  1.00 90.68  ? 67  ASP B CG  1 
ATOM   2976 O  OD1 . ASP B 1 67  ? -47.726  43.861 35.269  1.00 90.46  ? 67  ASP B OD1 1 
ATOM   2977 O  OD2 . ASP B 1 67  ? -45.804  44.114 34.233  1.00 87.81  ? 67  ASP B OD2 1 
ATOM   2978 N  N   . LEU B 1 68  ? -49.300  40.647 31.606  1.00 85.62  ? 68  LEU B N   1 
ATOM   2979 C  CA  . LEU B 1 68  ? -50.057  40.306 30.406  1.00 83.37  ? 68  LEU B CA  1 
ATOM   2980 C  C   . LEU B 1 68  ? -51.537  40.120 30.717  1.00 84.24  ? 68  LEU B C   1 
ATOM   2981 O  O   . LEU B 1 68  ? -52.391  40.400 29.868  1.00 86.31  ? 68  LEU B O   1 
ATOM   2982 C  CB  . LEU B 1 68  ? -49.478  39.045 29.759  1.00 79.48  ? 68  LEU B CB  1 
ATOM   2983 C  CG  . LEU B 1 68  ? -50.221  38.459 28.555  1.00 76.55  ? 68  LEU B CG  1 
ATOM   2984 C  CD1 . LEU B 1 68  ? -50.217  39.426 27.380  1.00 81.33  ? 68  LEU B CD1 1 
ATOM   2985 C  CD2 . LEU B 1 68  ? -49.618  37.124 28.156  1.00 79.79  ? 68  LEU B CD2 1 
ATOM   2986 N  N   . GLY B 1 69  ? -51.861  39.656 31.925  1.00 81.44  ? 69  GLY B N   1 
ATOM   2987 C  CA  . GLY B 1 69  ? -53.256  39.578 32.326  1.00 79.84  ? 69  GLY B CA  1 
ATOM   2988 C  C   . GLY B 1 69  ? -53.868  40.945 32.561  1.00 81.88  ? 69  GLY B C   1 
ATOM   2989 O  O   . GLY B 1 69  ? -55.028  41.185 32.211  1.00 78.38  ? 69  GLY B O   1 
ATOM   2990 N  N   . VAL B 1 70  ? -53.102  41.858 33.163  1.00 82.95  ? 70  VAL B N   1 
ATOM   2991 C  CA  . VAL B 1 70  ? -53.560  43.236 33.306  1.00 81.21  ? 70  VAL B CA  1 
ATOM   2992 C  C   . VAL B 1 70  ? -53.734  43.875 31.936  1.00 78.60  ? 70  VAL B C   1 
ATOM   2993 O  O   . VAL B 1 70  ? -54.694  44.618 31.697  1.00 80.04  ? 70  VAL B O   1 
ATOM   2994 C  CB  . VAL B 1 70  ? -52.583  44.039 34.186  1.00 81.06  ? 70  VAL B CB  1 
ATOM   2995 C  CG1 . VAL B 1 70  ? -53.028  45.489 34.297  1.00 78.24  ? 70  VAL B CG1 1 
ATOM   2996 C  CG2 . VAL B 1 70  ? -52.469  43.410 35.565  1.00 83.07  ? 70  VAL B CG2 1 
ATOM   2997 N  N   . ASP B 1 71  ? -52.814  43.586 31.012  1.00 75.41  ? 71  ASP B N   1 
ATOM   2998 C  CA  . ASP B 1 71  ? -52.919  44.133 29.664  1.00 78.26  ? 71  ASP B CA  1 
ATOM   2999 C  C   . ASP B 1 71  ? -54.136  43.579 28.934  1.00 82.23  ? 71  ASP B C   1 
ATOM   3000 O  O   . ASP B 1 71  ? -54.783  44.298 28.163  1.00 80.69  ? 71  ASP B O   1 
ATOM   3001 C  CB  . ASP B 1 71  ? -51.642  43.839 28.876  1.00 82.99  ? 71  ASP B CB  1 
ATOM   3002 C  CG  . ASP B 1 71  ? -50.476  44.706 29.310  1.00 82.22  ? 71  ASP B CG  1 
ATOM   3003 O  OD1 . ASP B 1 71  ? -50.706  45.676 30.062  1.00 83.64  ? 71  ASP B OD1 1 
ATOM   3004 O  OD2 . ASP B 1 71  ? -49.331  44.416 28.899  1.00 81.67  ? 71  ASP B OD2 1 
ATOM   3005 N  N   . LEU B 1 72  ? -54.461  42.303 29.161  1.00 79.53  ? 72  LEU B N   1 
ATOM   3006 C  CA  . LEU B 1 72  ? -55.654  41.731 28.546  1.00 76.97  ? 72  LEU B CA  1 
ATOM   3007 C  C   . LEU B 1 72  ? -56.915  42.406 29.067  1.00 76.10  ? 72  LEU B C   1 
ATOM   3008 O  O   . LEU B 1 72  ? -57.824  42.722 28.291  1.00 78.17  ? 72  LEU B O   1 
ATOM   3009 C  CB  . LEU B 1 72  ? -55.714  40.225 28.799  1.00 76.99  ? 72  LEU B CB  1 
ATOM   3010 C  CG  . LEU B 1 72  ? -56.949  39.550 28.200  1.00 75.85  ? 72  LEU B CG  1 
ATOM   3011 C  CD1 . LEU B 1 72  ? -56.960  39.718 26.689  1.00 65.09  ? 72  LEU B CD1 1 
ATOM   3012 C  CD2 . LEU B 1 72  ? -57.025  38.079 28.582  1.00 75.69  ? 72  LEU B CD2 1 
ATOM   3013 N  N   . MET B 1 73  ? -56.989  42.634 30.381  1.00 70.37  ? 73  MET B N   1 
ATOM   3014 C  CA  . MET B 1 73  ? -58.142  43.330 30.941  1.00 75.61  ? 73  MET B CA  1 
ATOM   3015 C  C   . MET B 1 73  ? -58.206  44.771 30.450  1.00 77.22  ? 73  MET B C   1 
ATOM   3016 O  O   . MET B 1 73  ? -59.282  45.267 30.097  1.00 75.74  ? 73  MET B O   1 
ATOM   3017 C  CB  . MET B 1 73  ? -58.095  43.286 32.469  1.00 73.50  ? 73  MET B CB  1 
ATOM   3018 C  CG  . MET B 1 73  ? -58.143  41.884 33.053  1.00 75.22  ? 73  MET B CG  1 
ATOM   3019 S  SD  . MET B 1 73  ? -59.603  40.961 32.537  1.00 73.81  ? 73  MET B SD  1 
ATOM   3020 C  CE  . MET B 1 73  ? -58.860  39.659 31.558  1.00 72.16  ? 73  MET B CE  1 
ATOM   3021 N  N   . SER B 1 74  ? -57.060  45.458 30.419  1.00 77.11  ? 74  SER B N   1 
ATOM   3022 C  CA  . SER B 1 74  ? -57.031  46.829 29.920  1.00 72.12  ? 74  SER B CA  1 
ATOM   3023 C  C   . SER B 1 74  ? -57.472  46.895 28.465  1.00 76.53  ? 74  SER B C   1 
ATOM   3024 O  O   . SER B 1 74  ? -58.262  47.769 28.087  1.00 76.59  ? 74  SER B O   1 
ATOM   3025 C  CB  . SER B 1 74  ? -55.630  47.420 30.078  1.00 73.01  ? 74  SER B CB  1 
ATOM   3026 O  OG  . SER B 1 74  ? -55.295  47.587 31.443  1.00 74.15  ? 74  SER B OG  1 
ATOM   3027 N  N   . TRP B 1 75  ? -56.978  45.978 27.631  1.00 71.76  ? 75  TRP B N   1 
ATOM   3028 C  CA  . TRP B 1 75  ? -57.320  46.024 26.215  1.00 75.58  ? 75  TRP B CA  1 
ATOM   3029 C  C   . TRP B 1 75  ? -58.792  45.708 25.986  1.00 76.06  ? 75  TRP B C   1 
ATOM   3030 O  O   . TRP B 1 75  ? -59.447  46.355 25.161  1.00 70.86  ? 75  TRP B O   1 
ATOM   3031 C  CB  . TRP B 1 75  ? -56.440  45.058 25.422  1.00 73.81  ? 75  TRP B CB  1 
ATOM   3032 C  CG  . TRP B 1 75  ? -56.786  45.029 23.966  1.00 72.15  ? 75  TRP B CG  1 
ATOM   3033 C  CD1 . TRP B 1 75  ? -56.262  45.817 22.984  1.00 77.02  ? 75  TRP B CD1 1 
ATOM   3034 C  CD2 . TRP B 1 75  ? -57.749  44.180 23.329  1.00 74.16  ? 75  TRP B CD2 1 
ATOM   3035 N  NE1 . TRP B 1 75  ? -56.834  45.508 21.772  1.00 71.33  ? 75  TRP B NE1 1 
ATOM   3036 C  CE2 . TRP B 1 75  ? -57.751  44.507 21.957  1.00 73.52  ? 75  TRP B CE2 1 
ATOM   3037 C  CE3 . TRP B 1 75  ? -58.607  43.174 23.783  1.00 69.34  ? 75  TRP B CE3 1 
ATOM   3038 C  CZ2 . TRP B 1 75  ? -58.577  43.865 21.038  1.00 72.14  ? 75  TRP B CZ2 1 
ATOM   3039 C  CZ3 . TRP B 1 75  ? -59.427  42.539 22.868  1.00 71.51  ? 75  TRP B CZ3 1 
ATOM   3040 C  CH2 . TRP B 1 75  ? -59.405  42.885 21.512  1.00 72.49  ? 75  TRP B CH2 1 
ATOM   3041 N  N   . ALA B 1 76  ? -59.330  44.721 26.709  1.00 72.99  ? 76  ALA B N   1 
ATOM   3042 C  CA  . ALA B 1 76  ? -60.691  44.263 26.441  1.00 66.16  ? 76  ALA B CA  1 
ATOM   3043 C  C   . ALA B 1 76  ? -61.720  45.337 26.771  1.00 71.00  ? 76  ALA B C   1 
ATOM   3044 O  O   . ALA B 1 76  ? -62.735  45.463 26.076  1.00 73.26  ? 76  ALA B O   1 
ATOM   3045 C  CB  . ALA B 1 76  ? -60.980  42.983 27.223  1.00 69.75  ? 76  ALA B CB  1 
ATOM   3046 N  N   . PHE B 1 77  ? -61.481  46.120 27.826  1.00 71.98  ? 77  PHE B N   1 
ATOM   3047 C  CA  . PHE B 1 77  ? -62.403  47.198 28.167  1.00 72.23  ? 77  PHE B CA  1 
ATOM   3048 C  C   . PHE B 1 77  ? -62.217  48.412 27.269  1.00 73.50  ? 77  PHE B C   1 
ATOM   3049 O  O   . PHE B 1 77  ? -63.196  49.095 26.949  1.00 74.52  ? 77  PHE B O   1 
ATOM   3050 C  CB  . PHE B 1 77  ? -62.240  47.591 29.635  1.00 70.94  ? 77  PHE B CB  1 
ATOM   3051 C  CG  . PHE B 1 77  ? -62.928  46.656 30.588  1.00 74.45  ? 77  PHE B CG  1 
ATOM   3052 C  CD1 . PHE B 1 77  ? -62.280  45.526 31.063  1.00 73.74  ? 77  PHE B CD1 1 
ATOM   3053 C  CD2 . PHE B 1 77  ? -64.228  46.902 31.002  1.00 72.80  ? 77  PHE B CD2 1 
ATOM   3054 C  CE1 . PHE B 1 77  ? -62.913  44.660 31.938  1.00 69.51  ? 77  PHE B CE1 1 
ATOM   3055 C  CE2 . PHE B 1 77  ? -64.868  46.041 31.876  1.00 73.80  ? 77  PHE B CE2 1 
ATOM   3056 C  CZ  . PHE B 1 77  ? -64.209  44.917 32.344  1.00 74.92  ? 77  PHE B CZ  1 
ATOM   3057 N  N   . LEU B 1 78  ? -60.980  48.695 26.855  1.00 73.41  ? 78  LEU B N   1 
ATOM   3058 C  CA  . LEU B 1 78  ? -60.754  49.759 25.882  1.00 70.69  ? 78  LEU B CA  1 
ATOM   3059 C  C   . LEU B 1 78  ? -61.305  49.373 24.515  1.00 71.98  ? 78  LEU B C   1 
ATOM   3060 O  O   . LEU B 1 78  ? -61.872  50.214 23.807  1.00 71.98  ? 78  LEU B O   1 
ATOM   3061 C  CB  . LEU B 1 78  ? -59.262  50.081 25.797  1.00 70.66  ? 78  LEU B CB  1 
ATOM   3062 C  CG  . LEU B 1 78  ? -58.680  50.788 27.022  1.00 69.25  ? 78  LEU B CG  1 
ATOM   3063 C  CD1 . LEU B 1 78  ? -57.158  50.736 27.011  1.00 70.39  ? 78  LEU B CD1 1 
ATOM   3064 C  CD2 . LEU B 1 78  ? -59.175  52.228 27.085  1.00 57.68  ? 78  LEU B CD2 1 
ATOM   3065 N  N   . PHE B 1 79  ? -61.151  48.103 24.133  1.00 73.18  ? 79  PHE B N   1 
ATOM   3066 C  CA  . PHE B 1 79  ? -61.723  47.625 22.878  1.00 75.44  ? 79  PHE B CA  1 
ATOM   3067 C  C   . PHE B 1 79  ? -63.243  47.705 22.900  1.00 76.06  ? 79  PHE B C   1 
ATOM   3068 O  O   . PHE B 1 79  ? -63.870  48.036 21.886  1.00 76.68  ? 79  PHE B O   1 
ATOM   3069 C  CB  . PHE B 1 79  ? -61.259  46.191 22.613  1.00 74.04  ? 79  PHE B CB  1 
ATOM   3070 C  CG  . PHE B 1 79  ? -61.986  45.506 21.492  1.00 74.93  ? 79  PHE B CG  1 
ATOM   3071 C  CD1 . PHE B 1 79  ? -61.695  45.807 20.170  1.00 73.59  ? 79  PHE B CD1 1 
ATOM   3072 C  CD2 . PHE B 1 79  ? -62.943  44.538 21.760  1.00 71.81  ? 79  PHE B CD2 1 
ATOM   3073 C  CE1 . PHE B 1 79  ? -62.355  45.167 19.135  1.00 70.84  ? 79  PHE B CE1 1 
ATOM   3074 C  CE2 . PHE B 1 79  ? -63.608  43.894 20.734  1.00 72.17  ? 79  PHE B CE2 1 
ATOM   3075 C  CZ  . PHE B 1 79  ? -63.312  44.208 19.417  1.00 73.98  ? 79  PHE B CZ  1 
ATOM   3076 N  N   . ASP B 1 80  ? -63.854  47.414 24.052  1.00 74.20  ? 80  ASP B N   1 
ATOM   3077 C  CA  . ASP B 1 80  ? -65.309  47.430 24.144  1.00 74.09  ? 80  ASP B CA  1 
ATOM   3078 C  C   . ASP B 1 80  ? -65.865  48.844 24.046  1.00 73.02  ? 80  ASP B C   1 
ATOM   3079 O  O   . ASP B 1 80  ? -66.996  49.029 23.581  1.00 76.70  ? 80  ASP B O   1 
ATOM   3080 C  CB  . ASP B 1 80  ? -65.761  46.769 25.446  1.00 70.95  ? 80  ASP B CB  1 
ATOM   3081 C  CG  . ASP B 1 80  ? -67.270  46.706 25.573  1.00 74.28  ? 80  ASP B CG  1 
ATOM   3082 O  OD1 . ASP B 1 80  ? -67.900  45.963 24.792  1.00 74.13  ? 80  ASP B OD1 1 
ATOM   3083 O  OD2 . ASP B 1 80  ? -67.827  47.403 26.448  1.00 70.09  ? 80  ASP B OD2 1 
ATOM   3084 N  N   . ASP B 1 81  ? -65.091  49.847 24.475  1.00 73.41  ? 81  ASP B N   1 
ATOM   3085 C  CA  . ASP B 1 81  ? -65.548  51.231 24.390  1.00 72.17  ? 81  ASP B CA  1 
ATOM   3086 C  C   . ASP B 1 81  ? -65.909  51.611 22.962  1.00 75.49  ? 81  ASP B C   1 
ATOM   3087 O  O   . ASP B 1 81  ? -66.854  52.374 22.735  1.00 78.64  ? 81  ASP B O   1 
ATOM   3088 C  CB  . ASP B 1 81  ? -64.474  52.181 24.920  1.00 72.50  ? 81  ASP B CB  1 
ATOM   3089 C  CG  . ASP B 1 81  ? -64.403  52.203 26.429  1.00 76.06  ? 81  ASP B CG  1 
ATOM   3090 O  OD1 . ASP B 1 81  ? -65.406  51.843 27.081  1.00 81.12  ? 81  ASP B OD1 1 
ATOM   3091 O  OD2 . ASP B 1 81  ? -63.341  52.592 26.964  1.00 75.95  ? 81  ASP B OD2 1 
ATOM   3092 N  N   . LEU B 1 82  ? -65.173  51.077 21.986  1.00 74.70  ? 82  LEU B N   1 
ATOM   3093 C  CA  . LEU B 1 82  ? -65.321  51.477 20.594  1.00 67.96  ? 82  LEU B CA  1 
ATOM   3094 C  C   . LEU B 1 82  ? -66.654  51.060 19.986  1.00 78.56  ? 82  LEU B C   1 
ATOM   3095 O  O   . LEU B 1 82  ? -66.938  51.440 18.843  1.00 78.62  ? 82  LEU B O   1 
ATOM   3096 C  CB  . LEU B 1 82  ? -64.170  50.894 19.772  1.00 77.00  ? 82  LEU B CB  1 
ATOM   3097 C  CG  . LEU B 1 82  ? -62.764  51.191 20.297  1.00 70.48  ? 82  LEU B CG  1 
ATOM   3098 C  CD1 . LEU B 1 82  ? -61.714  50.382 19.545  1.00 63.55  ? 82  LEU B CD1 1 
ATOM   3099 C  CD2 . LEU B 1 82  ? -62.466  52.678 20.204  1.00 64.53  ? 82  LEU B CD2 1 
ATOM   3100 N  N   . PHE B 1 83  ? -67.475  50.298 20.707  1.00 74.84  ? 83  PHE B N   1 
ATOM   3101 C  CA  . PHE B 1 83  ? -68.743  49.815 20.180  1.00 72.86  ? 83  PHE B CA  1 
ATOM   3102 C  C   . PHE B 1 83  ? -69.945  50.375 20.927  1.00 75.95  ? 83  PHE B C   1 
ATOM   3103 O  O   . PHE B 1 83  ? -71.068  49.903 20.715  1.00 79.99  ? 83  PHE B O   1 
ATOM   3104 C  CB  . PHE B 1 83  ? -68.763  48.286 20.191  1.00 64.14  ? 83  PHE B CB  1 
ATOM   3105 C  CG  . PHE B 1 83  ? -67.653  47.674 19.392  1.00 68.70  ? 83  PHE B CG  1 
ATOM   3106 C  CD1 . PHE B 1 83  ? -67.802  47.448 18.034  1.00 70.87  ? 83  PHE B CD1 1 
ATOM   3107 C  CD2 . PHE B 1 83  ? -66.449  47.348 19.992  1.00 72.25  ? 83  PHE B CD2 1 
ATOM   3108 C  CE1 . PHE B 1 83  ? -66.774  46.895 17.293  1.00 74.20  ? 83  PHE B CE1 1 
ATOM   3109 C  CE2 . PHE B 1 83  ? -65.420  46.798 19.259  1.00 69.01  ? 83  PHE B CE2 1 
ATOM   3110 C  CZ  . PHE B 1 83  ? -65.581  46.569 17.908  1.00 75.32  ? 83  PHE B CZ  1 
ATOM   3111 N  N   . ASP B 1 84  ? -69.741  51.374 21.789  1.00 75.93  ? 84  ASP B N   1 
ATOM   3112 C  CA  . ASP B 1 84  ? -70.846  52.052 22.453  1.00 80.01  ? 84  ASP B CA  1 
ATOM   3113 C  C   . ASP B 1 84  ? -71.498  53.113 21.578  1.00 79.15  ? 84  ASP B C   1 
ATOM   3114 O  O   . ASP B 1 84  ? -72.588  53.588 21.913  1.00 83.06  ? 84  ASP B O   1 
ATOM   3115 C  CB  . ASP B 1 84  ? -70.370  52.693 23.760  1.00 84.78  ? 84  ASP B CB  1 
ATOM   3116 C  CG  . ASP B 1 84  ? -70.029  51.666 24.823  1.00 93.69  ? 84  ASP B CG  1 
ATOM   3117 O  OD1 . ASP B 1 84  ? -70.675  50.596 24.848  1.00 94.93  ? 84  ASP B OD1 1 
ATOM   3118 O  OD2 . ASP B 1 84  ? -69.117  51.930 25.635  1.00 93.76  ? 84  ASP B OD2 1 
ATOM   3119 N  N   . GLY B 1 85  ? -70.867  53.492 20.472  1.00 86.23  ? 85  GLY B N   1 
ATOM   3120 C  CA  . GLY B 1 85  ? -71.415  54.491 19.590  1.00 80.35  ? 85  GLY B CA  1 
ATOM   3121 C  C   . GLY B 1 85  ? -72.121  53.876 18.401  1.00 83.24  ? 85  GLY B C   1 
ATOM   3122 O  O   . GLY B 1 85  ? -72.639  52.756 18.464  1.00 81.07  ? 85  GLY B O   1 
ATOM   3123 N  N   . PRO B 1 86  ? -72.155  54.606 17.285  1.00 87.22  ? 86  PRO B N   1 
ATOM   3124 C  CA  . PRO B 1 86  ? -72.837  54.085 16.090  1.00 83.81  ? 86  PRO B CA  1 
ATOM   3125 C  C   . PRO B 1 86  ? -72.181  52.849 15.499  1.00 83.75  ? 86  PRO B C   1 
ATOM   3126 O  O   . PRO B 1 86  ? -72.836  52.131 14.733  1.00 83.06  ? 86  PRO B O   1 
ATOM   3127 C  CB  . PRO B 1 86  ? -72.786  55.268 15.112  1.00 81.10  ? 86  PRO B CB  1 
ATOM   3128 C  CG  . PRO B 1 86  ? -72.551  56.470 15.971  1.00 81.94  ? 86  PRO B CG  1 
ATOM   3129 C  CD  . PRO B 1 86  ? -71.696  55.992 17.099  1.00 80.60  ? 86  PRO B CD  1 
ATOM   3130 N  N   . ARG B 1 87  ? -70.913  52.574 15.824  1.00 79.36  ? 87  ARG B N   1 
ATOM   3131 C  CA  . ARG B 1 87  ? -70.252  51.398 15.267  1.00 77.85  ? 87  ARG B CA  1 
ATOM   3132 C  C   . ARG B 1 87  ? -70.947  50.115 15.705  1.00 81.06  ? 87  ARG B C   1 
ATOM   3133 O  O   . ARG B 1 87  ? -71.182  49.218 14.887  1.00 78.26  ? 87  ARG B O   1 
ATOM   3134 C  CB  . ARG B 1 87  ? -68.779  51.369 15.673  1.00 78.42  ? 87  ARG B CB  1 
ATOM   3135 C  CG  . ARG B 1 87  ? -68.073  50.080 15.277  1.00 73.43  ? 87  ARG B CG  1 
ATOM   3136 C  CD  . ARG B 1 87  ? -66.615  50.068 15.701  1.00 77.49  ? 87  ARG B CD  1 
ATOM   3137 N  NE  . ARG B 1 87  ? -65.812  51.017 14.939  1.00 77.75  ? 87  ARG B NE  1 
ATOM   3138 C  CZ  . ARG B 1 87  ? -65.447  52.212 15.379  1.00 83.58  ? 87  ARG B CZ  1 
ATOM   3139 N  NH1 . ARG B 1 87  ? -65.786  52.638 16.586  1.00 75.78  ? 87  ARG B NH1 1 
ATOM   3140 N  NH2 . ARG B 1 87  ? -64.720  52.999 14.590  1.00 78.20  ? 87  ARG B NH2 1 
ATOM   3141 N  N   . GLY B 1 88  ? -71.283  50.010 16.991  1.00 80.50  ? 88  GLY B N   1 
ATOM   3142 C  CA  . GLY B 1 88  ? -72.016  48.866 17.497  1.00 76.71  ? 88  GLY B CA  1 
ATOM   3143 C  C   . GLY B 1 88  ? -73.460  48.785 17.054  1.00 83.98  ? 88  GLY B C   1 
ATOM   3144 O  O   . GLY B 1 88  ? -74.155  47.837 17.432  1.00 84.42  ? 88  GLY B O   1 
ATOM   3145 N  N   . GLU B 1 89  ? -73.930  49.757 16.272  1.00 82.46  ? 89  GLU B N   1 
ATOM   3146 C  CA  . GLU B 1 89  ? -75.269  49.744 15.701  1.00 81.67  ? 89  GLU B CA  1 
ATOM   3147 C  C   . GLU B 1 89  ? -75.294  49.233 14.267  1.00 85.61  ? 89  GLU B C   1 
ATOM   3148 O  O   . GLU B 1 89  ? -76.380  49.057 13.705  1.00 86.59  ? 89  GLU B O   1 
ATOM   3149 C  CB  . GLU B 1 89  ? -75.873  51.154 15.739  1.00 82.30  ? 89  GLU B CB  1 
ATOM   3150 C  CG  . GLU B 1 89  ? -75.777  51.848 17.087  1.00 89.36  ? 89  GLU B CG  1 
ATOM   3151 C  CD  . GLU B 1 89  ? -76.986  51.593 17.962  1.00 98.27  ? 89  GLU B CD  1 
ATOM   3152 O  OE1 . GLU B 1 89  ? -77.962  50.991 17.468  1.00 103.92 ? 89  GLU B OE1 1 
ATOM   3153 O  OE2 . GLU B 1 89  ? -76.962  51.998 19.143  1.00 103.96 ? 89  GLU B OE2 1 
ATOM   3154 N  N   . ASN B 1 90  ? -74.130  48.999 13.665  1.00 81.36  ? 90  ASN B N   1 
ATOM   3155 C  CA  . ASN B 1 90  ? -74.031  48.594 12.269  1.00 75.06  ? 90  ASN B CA  1 
ATOM   3156 C  C   . ASN B 1 90  ? -73.087  47.403 12.187  1.00 76.86  ? 90  ASN B C   1 
ATOM   3157 O  O   . ASN B 1 90  ? -71.885  47.546 12.493  1.00 75.78  ? 90  ASN B O   1 
ATOM   3158 C  CB  . ASN B 1 90  ? -73.534  49.755 11.402  1.00 78.64  ? 90  ASN B CB  1 
ATOM   3159 C  CG  . ASN B 1 90  ? -73.545  49.426 9.925   1.00 80.98  ? 90  ASN B CG  1 
ATOM   3160 O  OD1 . ASN B 1 90  ? -72.634  48.777 9.417   1.00 77.52  ? 90  ASN B OD1 1 
ATOM   3161 N  ND2 . ASN B 1 90  ? -74.580  49.878 9.225   1.00 81.70  ? 90  ASN B ND2 1 
ATOM   3162 N  N   . PRO B 1 91  ? -73.566  46.221 11.798  1.00 76.18  ? 91  PRO B N   1 
ATOM   3163 C  CA  . PRO B 1 91  ? -72.667  45.059 11.709  1.00 75.08  ? 91  PRO B CA  1 
ATOM   3164 C  C   . PRO B 1 91  ? -71.580  45.205 10.663  1.00 70.63  ? 91  PRO B C   1 
ATOM   3165 O  O   . PRO B 1 91  ? -70.540  44.547 10.779  1.00 73.61  ? 91  PRO B O   1 
ATOM   3166 C  CB  . PRO B 1 91  ? -73.618  43.900 11.373  1.00 73.81  ? 91  PRO B CB  1 
ATOM   3167 C  CG  . PRO B 1 91  ? -74.852  44.553 10.833  1.00 77.13  ? 91  PRO B CG  1 
ATOM   3168 C  CD  . PRO B 1 91  ? -74.969  45.862 11.539  1.00 72.41  ? 91  PRO B CD  1 
ATOM   3169 N  N   . GLU B 1 92  ? -71.776  46.045 9.647   1.00 76.32  ? 92  GLU B N   1 
ATOM   3170 C  CA  . GLU B 1 92  ? -70.723  46.240 8.655   1.00 80.95  ? 92  GLU B CA  1 
ATOM   3171 C  C   . GLU B 1 92  ? -69.620  47.148 9.190   1.00 77.72  ? 92  GLU B C   1 
ATOM   3172 O  O   . GLU B 1 92  ? -68.434  46.883 8.969   1.00 74.71  ? 92  GLU B O   1 
ATOM   3173 C  CB  . GLU B 1 92  ? -71.317  46.807 7.365   1.00 78.13  ? 92  GLU B CB  1 
ATOM   3174 C  CG  . GLU B 1 92  ? -70.345  46.870 6.200   1.00 89.60  ? 92  GLU B CG  1 
ATOM   3175 C  CD  . GLU B 1 92  ? -70.961  47.507 4.966   1.00 99.99  ? 92  GLU B CD  1 
ATOM   3176 O  OE1 . GLU B 1 92  ? -72.081  48.051 5.073   1.00 96.70  ? 92  GLU B OE1 1 
ATOM   3177 O  OE2 . GLU B 1 92  ? -70.325  47.464 3.890   1.00 103.34 ? 92  GLU B OE2 1 
ATOM   3178 N  N   . ASP B 1 93  ? -69.990  48.218 9.899   1.00 77.56  ? 93  ASP B N   1 
ATOM   3179 C  CA  . ASP B 1 93  ? -68.984  49.065 10.532  1.00 75.88  ? 93  ASP B CA  1 
ATOM   3180 C  C   . ASP B 1 93  ? -68.242  48.312 11.631  1.00 79.36  ? 93  ASP B C   1 
ATOM   3181 O  O   . ASP B 1 93  ? -67.026  48.476 11.792  1.00 77.99  ? 93  ASP B O   1 
ATOM   3182 C  CB  . ASP B 1 93  ? -69.636  50.328 11.094  1.00 74.35  ? 93  ASP B CB  1 
ATOM   3183 C  CG  . ASP B 1 93  ? -70.264  51.191 10.015  1.00 88.52  ? 93  ASP B CG  1 
ATOM   3184 O  OD1 . ASP B 1 93  ? -69.878  51.051 8.833   1.00 86.17  ? 93  ASP B OD1 1 
ATOM   3185 O  OD2 . ASP B 1 93  ? -71.140  52.017 10.354  1.00 88.39  ? 93  ASP B OD2 1 
ATOM   3186 N  N   . THR B 1 94  ? -68.958  47.483 12.396  1.00 75.46  ? 94  THR B N   1 
ATOM   3187 C  CA  . THR B 1 94  ? -68.318  46.691 13.442  1.00 72.21  ? 94  THR B CA  1 
ATOM   3188 C  C   . THR B 1 94  ? -67.356  45.671 12.845  1.00 70.37  ? 94  THR B C   1 
ATOM   3189 O  O   . THR B 1 94  ? -66.223  45.517 13.316  1.00 72.37  ? 94  THR B O   1 
ATOM   3190 C  CB  . THR B 1 94  ? -69.379  45.998 14.302  1.00 72.95  ? 94  THR B CB  1 
ATOM   3191 O  OG1 . THR B 1 94  ? -69.990  46.958 15.171  1.00 74.04  ? 94  THR B OG1 1 
ATOM   3192 C  CG2 . THR B 1 94  ? -68.759  44.886 15.142  1.00 63.77  ? 94  THR B CG2 1 
ATOM   3193 N  N   . LYS B 1 95  ? -67.791  44.965 11.799  1.00 69.31  ? 95  LYS B N   1 
ATOM   3194 C  CA  . LYS B 1 95  ? -66.926  43.977 11.161  1.00 72.55  ? 95  LYS B CA  1 
ATOM   3195 C  C   . LYS B 1 95  ? -65.689  44.625 10.547  1.00 75.14  ? 95  LYS B C   1 
ATOM   3196 O  O   . LYS B 1 95  ? -64.637  43.982 10.444  1.00 75.55  ? 95  LYS B O   1 
ATOM   3197 C  CB  . LYS B 1 95  ? -67.722  43.197 10.110  1.00 69.43  ? 95  LYS B CB  1 
ATOM   3198 C  CG  . LYS B 1 95  ? -66.887  42.342 9.168   1.00 76.32  ? 95  LYS B CG  1 
ATOM   3199 C  CD  . LYS B 1 95  ? -67.162  40.854 9.327   1.00 79.16  ? 95  LYS B CD  1 
ATOM   3200 C  CE  . LYS B 1 95  ? -66.423  40.055 8.257   1.00 83.82  ? 95  LYS B CE  1 
ATOM   3201 N  NZ  . LYS B 1 95  ? -66.515  38.581 8.458   1.00 92.57  ? 95  LYS B NZ  1 
ATOM   3202 N  N   . GLN B 1 96  ? -65.784  45.899 10.155  1.00 76.99  ? 96  GLN B N   1 
ATOM   3203 C  CA  . GLN B 1 96  ? -64.618  46.591 9.613   1.00 79.56  ? 96  GLN B CA  1 
ATOM   3204 C  C   . GLN B 1 96  ? -63.529  46.744 10.669  1.00 82.50  ? 96  GLN B C   1 
ATOM   3205 O  O   . GLN B 1 96  ? -62.338  46.598 10.367  1.00 82.84  ? 96  GLN B O   1 
ATOM   3206 C  CB  . GLN B 1 96  ? -65.030  47.954 9.052   1.00 80.01  ? 96  GLN B CB  1 
ATOM   3207 C  CG  . GLN B 1 96  ? -63.925  48.699 8.309   1.00 80.90  ? 96  GLN B CG  1 
ATOM   3208 C  CD  . GLN B 1 96  ? -63.177  49.698 9.183   1.00 93.49  ? 96  GLN B CD  1 
ATOM   3209 O  OE1 . GLN B 1 96  ? -63.452  49.834 10.377  1.00 88.98  ? 96  GLN B OE1 1 
ATOM   3210 N  NE2 . GLN B 1 96  ? -62.225  50.406 8.584   1.00 92.79  ? 96  GLN B NE2 1 
ATOM   3211 N  N   . LEU B 1 97  ? -63.915  47.027 11.915  1.00 79.69  ? 97  LEU B N   1 
ATOM   3212 C  CA  . LEU B 1 97  ? -62.926  47.155 12.980  1.00 75.69  ? 97  LEU B CA  1 
ATOM   3213 C  C   . LEU B 1 97  ? -62.464  45.795 13.490  1.00 78.42  ? 97  LEU B C   1 
ATOM   3214 O  O   . LEU B 1 97  ? -61.261  45.583 13.681  1.00 84.67  ? 97  LEU B O   1 
ATOM   3215 C  CB  . LEU B 1 97  ? -63.490  47.990 14.130  1.00 76.92  ? 97  LEU B CB  1 
ATOM   3216 C  CG  . LEU B 1 97  ? -62.593  48.105 15.367  1.00 78.93  ? 97  LEU B CG  1 
ATOM   3217 C  CD1 . LEU B 1 97  ? -61.218  48.638 14.992  1.00 78.09  ? 97  LEU B CD1 1 
ATOM   3218 C  CD2 . LEU B 1 97  ? -63.238  48.985 16.427  1.00 74.60  ? 97  LEU B CD2 1 
ATOM   3219 N  N   . THR B 1 98  ? -63.397  44.863 13.712  1.00 75.89  ? 98  THR B N   1 
ATOM   3220 C  CA  . THR B 1 98  ? -63.027  43.576 14.298  1.00 81.61  ? 98  THR B CA  1 
ATOM   3221 C  C   . THR B 1 98  ? -62.076  42.795 13.400  1.00 80.10  ? 98  THR B C   1 
ATOM   3222 O  O   . THR B 1 98  ? -61.238  42.036 13.900  1.00 83.60  ? 98  THR B O   1 
ATOM   3223 C  CB  . THR B 1 98  ? -64.273  42.735 14.589  1.00 76.59  ? 98  THR B CB  1 
ATOM   3224 O  OG1 . THR B 1 98  ? -64.971  42.462 13.367  1.00 74.08  ? 98  THR B OG1 1 
ATOM   3225 C  CG2 . THR B 1 98  ? -65.197  43.460 15.562  1.00 70.68  ? 98  THR B CG2 1 
ATOM   3226 N  N   . ASP B 1 99  ? -62.180  42.969 12.081  1.00 81.43  ? 99  ASP B N   1 
ATOM   3227 C  CA  . ASP B 1 99  ? -61.316  42.218 11.176  1.00 83.30  ? 99  ASP B CA  1 
ATOM   3228 C  C   . ASP B 1 99  ? -59.890  42.755 11.171  1.00 84.07  ? 99  ASP B C   1 
ATOM   3229 O  O   . ASP B 1 99  ? -58.941  41.979 11.007  1.00 83.81  ? 99  ASP B O   1 
ATOM   3230 C  CB  . ASP B 1 99  ? -61.897  42.225 9.763   1.00 77.39  ? 99  ASP B CB  1 
ATOM   3231 C  CG  . ASP B 1 99  ? -63.048  41.251 9.606   1.00 84.50  ? 99  ASP B CG  1 
ATOM   3232 O  OD1 . ASP B 1 99  ? -63.605  40.813 10.636  1.00 92.15  ? 99  ASP B OD1 1 
ATOM   3233 O  OD2 . ASP B 1 99  ? -63.386  40.912 8.452   1.00 86.79  ? 99  ASP B OD2 1 
ATOM   3234 N  N   . GLN B 1 100 ? -59.713  44.068 11.339  1.00 81.41  ? 100 GLN B N   1 
ATOM   3235 C  CA  . GLN B 1 100 ? -58.363  44.607 11.470  1.00 77.28  ? 100 GLN B CA  1 
ATOM   3236 C  C   . GLN B 1 100 ? -57.689  44.096 12.736  1.00 84.54  ? 100 GLN B C   1 
ATOM   3237 O  O   . GLN B 1 100 ? -56.465  43.922 12.763  1.00 87.73  ? 100 GLN B O   1 
ATOM   3238 C  CB  . GLN B 1 100 ? -58.400  46.135 11.464  1.00 78.51  ? 100 GLN B CB  1 
ATOM   3239 C  CG  . GLN B 1 100 ? -59.034  46.739 10.218  1.00 80.57  ? 100 GLN B CG  1 
ATOM   3240 C  CD  . GLN B 1 100 ? -58.895  48.248 10.165  1.00 86.46  ? 100 GLN B CD  1 
ATOM   3241 O  OE1 . GLN B 1 100 ? -57.829  48.774 9.842   1.00 86.49  ? 100 GLN B OE1 1 
ATOM   3242 N  NE2 . GLN B 1 100 ? -59.974  48.955 10.485  1.00 85.05  ? 100 GLN B NE2 1 
ATOM   3243 N  N   . VAL B 1 101 ? -58.471  43.845 13.786  1.00 81.93  ? 101 VAL B N   1 
ATOM   3244 C  CA  . VAL B 1 101 ? -57.924  43.287 15.018  1.00 77.89  ? 101 VAL B CA  1 
ATOM   3245 C  C   . VAL B 1 101 ? -57.663  41.796 14.859  1.00 79.16  ? 101 VAL B C   1 
ATOM   3246 O  O   . VAL B 1 101 ? -56.559  41.310 15.132  1.00 80.40  ? 101 VAL B O   1 
ATOM   3247 C  CB  . VAL B 1 101 ? -58.874  43.568 16.199  1.00 77.02  ? 101 VAL B CB  1 
ATOM   3248 C  CG1 . VAL B 1 101 ? -58.276  43.048 17.494  1.00 72.13  ? 101 VAL B CG1 1 
ATOM   3249 C  CG2 . VAL B 1 101 ? -59.181  45.055 16.301  1.00 75.19  ? 101 VAL B CG2 1 
ATOM   3250 N  N   . ALA B 1 102 ? -58.675  41.051 14.405  1.00 76.48  ? 102 ALA B N   1 
ATOM   3251 C  CA  . ALA B 1 102 ? -58.543  39.606 14.257  1.00 80.91  ? 102 ALA B CA  1 
ATOM   3252 C  C   . ALA B 1 102 ? -57.451  39.216 13.270  1.00 83.57  ? 102 ALA B C   1 
ATOM   3253 O  O   . ALA B 1 102 ? -56.971  38.078 13.314  1.00 87.17  ? 102 ALA B O   1 
ATOM   3254 C  CB  . ALA B 1 102 ? -59.877  39.000 13.818  1.00 74.28  ? 102 ALA B CB  1 
ATOM   3255 N  N   . ALA B 1 103 ? -57.045  40.133 12.387  1.00 85.93  ? 103 ALA B N   1 
ATOM   3256 C  CA  . ALA B 1 103 ? -55.979  39.840 11.436  1.00 86.54  ? 103 ALA B CA  1 
ATOM   3257 C  C   . ALA B 1 103 ? -54.660  39.512 12.126  1.00 92.91  ? 103 ALA B C   1 
ATOM   3258 O  O   . ALA B 1 103 ? -53.773  38.928 11.494  1.00 95.01  ? 103 ALA B O   1 
ATOM   3259 C  CB  . ALA B 1 103 ? -55.791  41.019 10.481  1.00 74.60  ? 103 ALA B CB  1 
ATOM   3260 N  N   . ALA B 1 104 ? -54.512  39.870 13.404  1.00 88.09  ? 104 ALA B N   1 
ATOM   3261 C  CA  . ALA B 1 104 ? -53.293  39.534 14.131  1.00 86.00  ? 104 ALA B CA  1 
ATOM   3262 C  C   . ALA B 1 104 ? -53.162  38.032 14.350  1.00 88.22  ? 104 ALA B C   1 
ATOM   3263 O  O   . ALA B 1 104 ? -52.041  37.516 14.432  1.00 88.32  ? 104 ALA B O   1 
ATOM   3264 C  CB  . ALA B 1 104 ? -53.260  40.271 15.469  1.00 86.01  ? 104 ALA B CB  1 
ATOM   3265 N  N   . LEU B 1 105 ? -54.285  37.315 14.441  1.00 86.62  ? 105 LEU B N   1 
ATOM   3266 C  CA  . LEU B 1 105 ? -54.234  35.873 14.657  1.00 89.68  ? 105 LEU B CA  1 
ATOM   3267 C  C   . LEU B 1 105 ? -53.650  35.124 13.466  1.00 94.05  ? 105 LEU B C   1 
ATOM   3268 O  O   . LEU B 1 105 ? -53.229  33.973 13.621  1.00 95.29  ? 105 LEU B O   1 
ATOM   3269 C  CB  . LEU B 1 105 ? -55.631  35.326 14.957  1.00 86.41  ? 105 LEU B CB  1 
ATOM   3270 C  CG  . LEU B 1 105 ? -56.419  35.900 16.134  1.00 82.05  ? 105 LEU B CG  1 
ATOM   3271 C  CD1 . LEU B 1 105 ? -57.751  35.181 16.256  1.00 78.59  ? 105 LEU B CD1 1 
ATOM   3272 C  CD2 . LEU B 1 105 ? -55.632  35.791 17.427  1.00 82.36  ? 105 LEU B CD2 1 
ATOM   3273 N  N   . ASP B 1 106 ? -53.619  35.744 12.288  1.00 89.50  ? 106 ASP B N   1 
ATOM   3274 C  CA  . ASP B 1 106 ? -53.170  35.085 11.068  1.00 93.11  ? 106 ASP B CA  1 
ATOM   3275 C  C   . ASP B 1 106 ? -51.765  35.493 10.648  1.00 95.44  ? 106 ASP B C   1 
ATOM   3276 O  O   . ASP B 1 106 ? -51.017  34.663 10.121  1.00 94.81  ? 106 ASP B O   1 
ATOM   3277 C  CB  . ASP B 1 106 ? -54.146  35.379 9.924   1.00 94.73  ? 106 ASP B CB  1 
ATOM   3278 C  CG  . ASP B 1 106 ? -55.576  35.011 10.270  1.00 95.28  ? 106 ASP B CG  1 
ATOM   3279 O  OD1 . ASP B 1 106 ? -55.773  34.081 11.080  1.00 97.23  ? 106 ASP B OD1 1 
ATOM   3280 O  OD2 . ASP B 1 106 ? -56.503  35.654 9.731   1.00 94.79  ? 106 ASP B OD2 1 
ATOM   3281 N  N   . GLY B 1 107 ? -51.388  36.750 10.864  1.00 95.54  ? 107 GLY B N   1 
ATOM   3282 C  CA  . GLY B 1 107 ? -50.076  37.224 10.497  1.00 94.30  ? 107 GLY B CA  1 
ATOM   3283 C  C   . GLY B 1 107 ? -49.739  38.547 11.151  1.00 96.41  ? 107 GLY B C   1 
ATOM   3284 O  O   . GLY B 1 107 ? -50.458  39.033 12.031  1.00 96.43  ? 107 GLY B O   1 
ATOM   3285 N  N   . PRO B 1 108 ? -48.626  39.151 10.742  1.00 98.33  ? 108 PRO B N   1 
ATOM   3286 C  CA  . PRO B 1 108 ? -48.261  40.463 11.285  1.00 94.18  ? 108 PRO B CA  1 
ATOM   3287 C  C   . PRO B 1 108 ? -49.229  41.541 10.826  1.00 93.49  ? 108 PRO B C   1 
ATOM   3288 O  O   . PRO B 1 108 ? -49.821  41.462 9.747   1.00 93.91  ? 108 PRO B O   1 
ATOM   3289 C  CB  . PRO B 1 108 ? -46.854  40.706 10.722  1.00 91.21  ? 108 PRO B CB  1 
ATOM   3290 C  CG  . PRO B 1 108 ? -46.358  39.350 10.312  1.00 92.13  ? 108 PRO B CG  1 
ATOM   3291 C  CD  . PRO B 1 108 ? -47.576  38.603 9.868   1.00 95.47  ? 108 PRO B CD  1 
ATOM   3292 N  N   . LEU B 1 109 ? -49.389  42.557 11.669  1.00 95.12  ? 109 LEU B N   1 
ATOM   3293 C  CA  . LEU B 1 109 ? -50.309  43.608 11.254  1.00 96.97  ? 109 LEU B CA  1 
ATOM   3294 C  C   . LEU B 1 109 ? -49.559  44.712 10.513  1.00 101.55 ? 109 LEU B C   1 
ATOM   3295 O  O   . LEU B 1 109 ? -48.433  45.057 10.887  1.00 101.34 ? 109 LEU B O   1 
ATOM   3296 C  CB  . LEU B 1 109 ? -51.028  44.208 12.457  1.00 95.71  ? 109 LEU B CB  1 
ATOM   3297 C  CG  . LEU B 1 109 ? -52.101  43.354 13.133  1.00 93.29  ? 109 LEU B CG  1 
ATOM   3298 C  CD1 . LEU B 1 109 ? -52.572  44.027 14.410  1.00 87.40  ? 109 LEU B CD1 1 
ATOM   3299 C  CD2 . LEU B 1 109 ? -53.268  43.122 12.189  1.00 92.33  ? 109 LEU B CD2 1 
ATOM   3300 N  N   . PRO B 1 110 ? -50.159  45.272 9.467   1.00 101.66 ? 110 PRO B N   1 
ATOM   3301 C  CA  . PRO B 1 110 ? -49.552  46.429 8.806   1.00 99.13  ? 110 PRO B CA  1 
ATOM   3302 C  C   . PRO B 1 110 ? -49.535  47.631 9.735   1.00 101.97 ? 110 PRO B C   1 
ATOM   3303 O  O   . PRO B 1 110 ? -50.335  47.745 10.666  1.00 102.32 ? 110 PRO B O   1 
ATOM   3304 C  CB  . PRO B 1 110 ? -50.465  46.671 7.601   1.00 101.65 ? 110 PRO B CB  1 
ATOM   3305 C  CG  . PRO B 1 110 ? -51.781  46.101 8.018   1.00 94.21  ? 110 PRO B CG  1 
ATOM   3306 C  CD  . PRO B 1 110 ? -51.448  44.902 8.859   1.00 98.86  ? 110 PRO B CD  1 
ATOM   3307 N  N   . ASP B 1 111 ? -48.596  48.540 9.466   1.00 106.91 ? 111 ASP B N   1 
ATOM   3308 C  CA  . ASP B 1 111 ? -48.481  49.744 10.280  1.00 103.19 ? 111 ASP B CA  1 
ATOM   3309 C  C   . ASP B 1 111 ? -49.732  50.609 10.202  1.00 101.32 ? 111 ASP B C   1 
ATOM   3310 O  O   . ASP B 1 111 ? -49.979  51.406 11.115  1.00 99.79  ? 111 ASP B O   1 
ATOM   3311 C  CB  . ASP B 1 111 ? -47.253  50.549 9.851   1.00 107.37 ? 111 ASP B CB  1 
ATOM   3312 C  CG  . ASP B 1 111 ? -45.995  49.701 9.788   1.00 115.92 ? 111 ASP B CG  1 
ATOM   3313 O  OD1 . ASP B 1 111 ? -45.830  48.948 8.804   1.00 113.91 ? 111 ASP B OD1 1 
ATOM   3314 O  OD2 . ASP B 1 111 ? -45.171  49.784 10.724  1.00 118.62 ? 111 ASP B OD2 1 
ATOM   3315 N  N   . THR B 1 112 ? -50.531  50.460 9.143   1.00 99.44  ? 112 THR B N   1 
ATOM   3316 C  CA  . THR B 1 112 ? -51.770  51.215 8.998   1.00 99.81  ? 112 THR B CA  1 
ATOM   3317 C  C   . THR B 1 112 ? -52.858  50.762 9.964   1.00 100.46 ? 112 THR B C   1 
ATOM   3318 O  O   . THR B 1 112 ? -53.874  51.456 10.089  1.00 100.22 ? 112 THR B O   1 
ATOM   3319 C  CB  . THR B 1 112 ? -52.288  51.102 7.561   1.00 104.16 ? 112 THR B CB  1 
ATOM   3320 O  OG1 . THR B 1 112 ? -52.741  49.764 7.317   1.00 101.93 ? 112 THR B OG1 1 
ATOM   3321 C  CG2 . THR B 1 112 ? -51.185  51.441 6.568   1.00 98.94  ? 112 THR B CG2 1 
ATOM   3322 N  N   . ALA B 1 113 ? -52.676  49.628 10.639  1.00 97.65  ? 113 ALA B N   1 
ATOM   3323 C  CA  . ALA B 1 113 ? -53.690  49.121 11.549  1.00 92.93  ? 113 ALA B CA  1 
ATOM   3324 C  C   . ALA B 1 113 ? -53.916  50.106 12.696  1.00 88.88  ? 113 ALA B C   1 
ATOM   3325 O  O   . ALA B 1 113 ? -53.008  50.854 13.070  1.00 92.59  ? 113 ALA B O   1 
ATOM   3326 C  CB  . ALA B 1 113 ? -53.277  47.757 12.101  1.00 91.14  ? 113 ALA B CB  1 
ATOM   3327 N  N   . PRO B 1 114 ? -55.120  50.135 13.264  1.00 83.66  ? 114 PRO B N   1 
ATOM   3328 C  CA  . PRO B 1 114 ? -55.402  51.060 14.369  1.00 82.68  ? 114 PRO B CA  1 
ATOM   3329 C  C   . PRO B 1 114 ? -54.628  50.673 15.616  1.00 84.58  ? 114 PRO B C   1 
ATOM   3330 O  O   . PRO B 1 114 ? -54.189  49.521 15.753  1.00 86.03  ? 114 PRO B O   1 
ATOM   3331 C  CB  . PRO B 1 114 ? -56.917  50.908 14.585  1.00 78.01  ? 114 PRO B CB  1 
ATOM   3332 C  CG  . PRO B 1 114 ? -57.429  50.267 13.334  1.00 83.28  ? 114 PRO B CG  1 
ATOM   3333 C  CD  . PRO B 1 114 ? -56.321  49.394 12.847  1.00 82.53  ? 114 PRO B CD  1 
ATOM   3334 N  N   . PRO B 1 115 ? -54.431  51.611 16.547  1.00 82.80  ? 115 PRO B N   1 
ATOM   3335 C  CA  . PRO B 1 115 ? -53.721  51.264 17.791  1.00 83.52  ? 115 PRO B CA  1 
ATOM   3336 C  C   . PRO B 1 115 ? -54.366  50.127 18.564  1.00 86.61  ? 115 PRO B C   1 
ATOM   3337 O  O   . PRO B 1 115 ? -53.653  49.318 19.172  1.00 86.69  ? 115 PRO B O   1 
ATOM   3338 C  CB  . PRO B 1 115 ? -53.751  52.579 18.580  1.00 79.67  ? 115 PRO B CB  1 
ATOM   3339 C  CG  . PRO B 1 115 ? -53.845  53.636 17.534  1.00 86.39  ? 115 PRO B CG  1 
ATOM   3340 C  CD  . PRO B 1 115 ? -54.698  53.055 16.444  1.00 83.07  ? 115 PRO B CD  1 
ATOM   3341 N  N   . ILE B 1 116 ? -55.699  50.037 18.557  1.00 83.67  ? 116 ILE B N   1 
ATOM   3342 C  CA  . ILE B 1 116 ? -56.367  48.952 19.270  1.00 77.68  ? 116 ILE B CA  1 
ATOM   3343 C  C   . ILE B 1 116 ? -56.010  47.607 18.651  1.00 78.92  ? 116 ILE B C   1 
ATOM   3344 O  O   . ILE B 1 116 ? -56.000  46.579 19.340  1.00 77.01  ? 116 ILE B O   1 
ATOM   3345 C  CB  . ILE B 1 116 ? -57.893  49.185 19.299  1.00 76.03  ? 116 ILE B CB  1 
ATOM   3346 C  CG1 . ILE B 1 116 ? -58.569  48.230 20.285  1.00 77.01  ? 116 ILE B CG1 1 
ATOM   3347 C  CG2 . ILE B 1 116 ? -58.497  49.035 17.911  1.00 77.12  ? 116 ILE B CG2 1 
ATOM   3348 C  CD1 . ILE B 1 116 ? -58.208  48.489 21.731  1.00 65.21  ? 116 ILE B CD1 1 
ATOM   3349 N  N   . ALA B 1 117 ? -55.693  47.589 17.355  1.00 83.28  ? 117 ALA B N   1 
ATOM   3350 C  CA  . ALA B 1 117 ? -55.280  46.346 16.712  1.00 79.54  ? 117 ALA B CA  1 
ATOM   3351 C  C   . ALA B 1 117 ? -53.863  45.967 17.120  1.00 83.48  ? 117 ALA B C   1 
ATOM   3352 O  O   . ALA B 1 117 ? -53.590  44.806 17.449  1.00 82.89  ? 117 ALA B O   1 
ATOM   3353 C  CB  . ALA B 1 117 ? -55.391  46.479 15.194  1.00 78.84  ? 117 ALA B CB  1 
ATOM   3354 N  N   . HIS B 1 118 ? -52.945  46.938 17.112  1.00 86.27  ? 118 HIS B N   1 
ATOM   3355 C  CA  . HIS B 1 118 ? -51.569  46.655 17.505  1.00 87.13  ? 118 HIS B CA  1 
ATOM   3356 C  C   . HIS B 1 118 ? -51.477  46.238 18.965  1.00 82.11  ? 118 HIS B C   1 
ATOM   3357 O  O   . HIS B 1 118 ? -50.613  45.430 19.324  1.00 80.38  ? 118 HIS B O   1 
ATOM   3358 C  CB  . HIS B 1 118 ? -50.684  47.873 17.243  1.00 87.59  ? 118 HIS B CB  1 
ATOM   3359 C  CG  . HIS B 1 118 ? -50.492  48.175 15.790  1.00 85.78  ? 118 HIS B CG  1 
ATOM   3360 N  ND1 . HIS B 1 118 ? -49.660  47.432 14.980  1.00 85.33  ? 118 HIS B ND1 1 
ATOM   3361 C  CD2 . HIS B 1 118 ? -51.028  49.135 15.000  1.00 87.64  ? 118 HIS B CD2 1 
ATOM   3362 C  CE1 . HIS B 1 118 ? -49.690  47.922 13.754  1.00 92.07  ? 118 HIS B CE1 1 
ATOM   3363 N  NE2 . HIS B 1 118 ? -50.512  48.956 13.739  1.00 90.57  ? 118 HIS B NE2 1 
ATOM   3364 N  N   . GLY B 1 119 ? -52.352  46.776 19.817  1.00 81.70  ? 119 GLY B N   1 
ATOM   3365 C  CA  . GLY B 1 119 ? -52.394  46.321 21.197  1.00 80.91  ? 119 GLY B CA  1 
ATOM   3366 C  C   . GLY B 1 119 ? -52.776  44.858 21.310  1.00 79.62  ? 119 GLY B C   1 
ATOM   3367 O  O   . GLY B 1 119 ? -52.175  44.107 22.082  1.00 80.61  ? 119 GLY B O   1 
ATOM   3368 N  N   . PHE B 1 120 ? -53.772  44.429 20.531  1.00 77.46  ? 120 PHE B N   1 
ATOM   3369 C  CA  . PHE B 1 120 ? -54.175  43.027 20.558  1.00 78.63  ? 120 PHE B CA  1 
ATOM   3370 C  C   . PHE B 1 120 ? -53.072  42.122 20.024  1.00 81.43  ? 120 PHE B C   1 
ATOM   3371 O  O   . PHE B 1 120 ? -52.898  40.996 20.507  1.00 79.86  ? 120 PHE B O   1 
ATOM   3372 C  CB  . PHE B 1 120 ? -55.460  42.832 19.754  1.00 81.48  ? 120 PHE B CB  1 
ATOM   3373 C  CG  . PHE B 1 120 ? -55.913  41.400 19.677  1.00 79.45  ? 120 PHE B CG  1 
ATOM   3374 C  CD1 . PHE B 1 120 ? -56.601  40.820 20.730  1.00 75.80  ? 120 PHE B CD1 1 
ATOM   3375 C  CD2 . PHE B 1 120 ? -55.650  40.634 18.553  1.00 75.75  ? 120 PHE B CD2 1 
ATOM   3376 C  CE1 . PHE B 1 120 ? -57.017  39.501 20.666  1.00 76.02  ? 120 PHE B CE1 1 
ATOM   3377 C  CE2 . PHE B 1 120 ? -56.062  39.315 18.484  1.00 81.04  ? 120 PHE B CE2 1 
ATOM   3378 C  CZ  . PHE B 1 120 ? -56.747  38.748 19.541  1.00 76.36  ? 120 PHE B CZ  1 
ATOM   3379 N  N   . ALA B 1 121 ? -52.323  42.589 19.022  1.00 81.95  ? 121 ALA B N   1 
ATOM   3380 C  CA  . ALA B 1 121 ? -51.235  41.782 18.479  1.00 82.77  ? 121 ALA B CA  1 
ATOM   3381 C  C   . ALA B 1 121 ? -50.140  41.565 19.516  1.00 82.74  ? 121 ALA B C   1 
ATOM   3382 O  O   . ALA B 1 121 ? -49.583  40.465 19.616  1.00 81.72  ? 121 ALA B O   1 
ATOM   3383 C  CB  . ALA B 1 121 ? -50.667  42.442 17.224  1.00 80.36  ? 121 ALA B CB  1 
ATOM   3384 N  N   . ASP B 1 122 ? -49.824  42.600 20.299  1.00 81.54  ? 122 ASP B N   1 
ATOM   3385 C  CA  . ASP B 1 122 ? -48.809  42.459 21.338  1.00 81.82  ? 122 ASP B CA  1 
ATOM   3386 C  C   . ASP B 1 122 ? -49.259  41.477 22.413  1.00 87.64  ? 122 ASP B C   1 
ATOM   3387 O  O   . ASP B 1 122 ? -48.446  40.715 22.949  1.00 87.20  ? 122 ASP B O   1 
ATOM   3388 C  CB  . ASP B 1 122 ? -48.493  43.826 21.946  1.00 81.07  ? 122 ASP B CB  1 
ATOM   3389 C  CG  . ASP B 1 122 ? -47.369  43.767 22.963  1.00 92.82  ? 122 ASP B CG  1 
ATOM   3390 O  OD1 . ASP B 1 122 ? -46.267  43.301 22.604  1.00 98.83  ? 122 ASP B OD1 1 
ATOM   3391 O  OD2 . ASP B 1 122 ? -47.583  44.193 24.118  1.00 95.11  ? 122 ASP B OD2 1 
ATOM   3392 N  N   . ILE B 1 123 ? -50.553  41.479 22.738  1.00 84.17  ? 123 ILE B N   1 
ATOM   3393 C  CA  . ILE B 1 123 ? -51.083  40.494 23.673  1.00 81.72  ? 123 ILE B CA  1 
ATOM   3394 C  C   . ILE B 1 123 ? -50.999  39.096 23.076  1.00 83.80  ? 123 ILE B C   1 
ATOM   3395 O  O   . ILE B 1 123 ? -50.588  38.141 23.747  1.00 83.58  ? 123 ILE B O   1 
ATOM   3396 C  CB  . ILE B 1 123 ? -52.529  40.852 24.062  1.00 77.33  ? 123 ILE B CB  1 
ATOM   3397 C  CG1 . ILE B 1 123 ? -52.572  42.202 24.776  1.00 80.19  ? 123 ILE B CG1 1 
ATOM   3398 C  CG2 . ILE B 1 123 ? -53.138  39.761 24.929  1.00 73.49  ? 123 ILE B CG2 1 
ATOM   3399 C  CD1 . ILE B 1 123 ? -53.949  42.580 25.252  1.00 80.96  ? 123 ILE B CD1 1 
ATOM   3400 N  N   . TRP B 1 124 ? -51.382  38.954 21.805  1.00 81.51  ? 124 TRP B N   1 
ATOM   3401 C  CA  . TRP B 1 124 ? -51.401  37.636 21.184  1.00 83.19  ? 124 TRP B CA  1 
ATOM   3402 C  C   . TRP B 1 124 ? -49.994  37.108 20.940  1.00 85.62  ? 124 TRP B C   1 
ATOM   3403 O  O   . TRP B 1 124 ? -49.782  35.890 20.943  1.00 89.08  ? 124 TRP B O   1 
ATOM   3404 C  CB  . TRP B 1 124 ? -52.191  37.682 19.878  1.00 81.82  ? 124 TRP B CB  1 
ATOM   3405 C  CG  . TRP B 1 124 ? -52.325  36.344 19.231  1.00 87.54  ? 124 TRP B CG  1 
ATOM   3406 C  CD1 . TRP B 1 124 ? -51.834  35.967 18.016  1.00 83.77  ? 124 TRP B CD1 1 
ATOM   3407 C  CD2 . TRP B 1 124 ? -52.980  35.192 19.777  1.00 87.11  ? 124 TRP B CD2 1 
ATOM   3408 N  NE1 . TRP B 1 124 ? -52.152  34.653 17.766  1.00 90.18  ? 124 TRP B NE1 1 
ATOM   3409 C  CE2 . TRP B 1 124 ? -52.854  34.155 18.832  1.00 86.22  ? 124 TRP B CE2 1 
ATOM   3410 C  CE3 . TRP B 1 124 ? -53.666  34.939 20.970  1.00 82.79  ? 124 TRP B CE3 1 
ATOM   3411 C  CZ2 . TRP B 1 124 ? -53.388  32.883 19.043  1.00 85.09  ? 124 TRP B CZ2 1 
ATOM   3412 C  CZ3 . TRP B 1 124 ? -54.194  33.677 21.178  1.00 84.45  ? 124 TRP B CZ3 1 
ATOM   3413 C  CH2 . TRP B 1 124 ? -54.053  32.665 20.219  1.00 88.91  ? 124 TRP B CH2 1 
ATOM   3414 N  N   . ARG B 1 125 ? -49.026  37.999 20.726  1.00 83.23  ? 125 ARG B N   1 
ATOM   3415 C  CA  . ARG B 1 125 ? -47.639  37.564 20.615  1.00 84.75  ? 125 ARG B CA  1 
ATOM   3416 C  C   . ARG B 1 125 ? -47.151  36.982 21.935  1.00 88.31  ? 125 ARG B C   1 
ATOM   3417 O  O   . ARG B 1 125 ? -46.511  35.924 21.964  1.00 89.62  ? 125 ARG B O   1 
ATOM   3418 C  CB  . ARG B 1 125 ? -46.757  38.735 20.181  1.00 88.07  ? 125 ARG B CB  1 
ATOM   3419 C  CG  . ARG B 1 125 ? -45.286  38.384 20.027  1.00 89.17  ? 125 ARG B CG  1 
ATOM   3420 C  CD  . ARG B 1 125 ? -44.437  39.634 19.856  1.00 90.87  ? 125 ARG B CD  1 
ATOM   3421 N  NE  . ARG B 1 125 ? -44.684  40.609 20.913  1.00 93.59  ? 125 ARG B NE  1 
ATOM   3422 C  CZ  . ARG B 1 125 ? -44.187  40.528 22.140  1.00 94.91  ? 125 ARG B CZ  1 
ATOM   3423 N  NH1 . ARG B 1 125 ? -43.421  39.514 22.510  1.00 96.66  ? 125 ARG B NH1 1 
ATOM   3424 N  NH2 . ARG B 1 125 ? -44.470  41.485 23.020  1.00 92.46  ? 125 ARG B NH2 1 
ATOM   3425 N  N   . ARG B 1 126 ? -47.458  37.660 23.045  1.00 90.04  ? 126 ARG B N   1 
ATOM   3426 C  CA  . ARG B 1 126 ? -47.026  37.189 24.357  1.00 91.22  ? 126 ARG B CA  1 
ATOM   3427 C  C   . ARG B 1 126 ? -47.801  35.956 24.803  1.00 91.54  ? 126 ARG B C   1 
ATOM   3428 O  O   . ARG B 1 126 ? -47.287  35.158 25.595  1.00 91.89  ? 126 ARG B O   1 
ATOM   3429 C  CB  . ARG B 1 126 ? -47.182  38.302 25.394  1.00 83.49  ? 126 ARG B CB  1 
ATOM   3430 C  CG  . ARG B 1 126 ? -46.232  39.469 25.213  1.00 85.31  ? 126 ARG B CG  1 
ATOM   3431 C  CD  . ARG B 1 126 ? -46.458  40.521 26.286  1.00 84.55  ? 126 ARG B CD  1 
ATOM   3432 N  NE  . ARG B 1 126 ? -47.592  41.385 25.983  1.00 84.75  ? 126 ARG B NE  1 
ATOM   3433 C  CZ  . ARG B 1 126 ? -48.155  42.215 26.851  1.00 90.50  ? 126 ARG B CZ  1 
ATOM   3434 N  NH1 . ARG B 1 126 ? -47.740  42.290 28.106  1.00 84.96  ? 126 ARG B NH1 1 
ATOM   3435 N  NH2 . ARG B 1 126 ? -49.162  42.987 26.450  1.00 88.95  ? 126 ARG B NH2 1 
ATOM   3436 N  N   . THR B 1 127 ? -49.031  35.786 24.314  1.00 90.12  ? 127 THR B N   1 
ATOM   3437 C  CA  . THR B 1 127 ? -49.864  34.680 24.776  1.00 90.71  ? 127 THR B CA  1 
ATOM   3438 C  C   . THR B 1 127 ? -49.355  33.343 24.253  1.00 92.03  ? 127 THR B C   1 
ATOM   3439 O  O   . THR B 1 127 ? -49.413  32.330 24.961  1.00 93.39  ? 127 THR B O   1 
ATOM   3440 C  CB  . THR B 1 127 ? -51.315  34.905 24.350  1.00 89.85  ? 127 THR B CB  1 
ATOM   3441 O  OG1 . THR B 1 127 ? -51.770  36.168 24.854  1.00 89.85  ? 127 THR B OG1 1 
ATOM   3442 C  CG2 . THR B 1 127 ? -52.211  33.800 24.890  1.00 85.07  ? 127 THR B CG2 1 
ATOM   3443 N  N   . CYS B 1 128 ? -48.838  33.321 23.024  1.00 93.56  ? 128 CYS B N   1 
ATOM   3444 C  CA  . CYS B 1 128 ? -48.455  32.068 22.384  1.00 96.03  ? 128 CYS B CA  1 
ATOM   3445 C  C   . CYS B 1 128 ? -47.079  31.571 22.807  1.00 95.87  ? 128 CYS B C   1 
ATOM   3446 O  O   . CYS B 1 128 ? -46.751  30.409 22.540  1.00 95.79  ? 128 CYS B O   1 
ATOM   3447 C  CB  . CYS B 1 128 ? -48.492  32.232 20.865  1.00 91.31  ? 128 CYS B CB  1 
ATOM   3448 S  SG  . CYS B 1 128 ? -50.128  32.630 20.218  1.00 97.87  ? 128 CYS B SG  1 
ATOM   3449 N  N   . GLU B 1 129 ? -46.276  32.415 23.455  1.00 94.09  ? 129 GLU B N   1 
ATOM   3450 C  CA  . GLU B 1 129 ? -44.911  32.051 23.815  1.00 96.64  ? 129 GLU B CA  1 
ATOM   3451 C  C   . GLU B 1 129 ? -44.889  30.792 24.671  1.00 99.42  ? 129 GLU B C   1 
ATOM   3452 O  O   . GLU B 1 129 ? -45.542  30.729 25.718  1.00 102.47 ? 129 GLU B O   1 
ATOM   3453 C  CB  . GLU B 1 129 ? -44.246  33.206 24.562  1.00 96.00  ? 129 GLU B CB  1 
ATOM   3454 C  CG  . GLU B 1 129 ? -44.104  34.481 23.751  1.00 104.90 ? 129 GLU B CG  1 
ATOM   3455 C  CD  . GLU B 1 129 ? -43.663  35.660 24.600  1.00 111.02 ? 129 GLU B CD  1 
ATOM   3456 O  OE1 . GLU B 1 129 ? -43.747  35.562 25.843  1.00 104.74 ? 129 GLU B OE1 1 
ATOM   3457 O  OE2 . GLU B 1 129 ? -43.233  36.683 24.025  1.00 115.79 ? 129 GLU B OE2 1 
ATOM   3458 N  N   . GLY B 1 130 ? -44.136  29.790 24.223  1.00 97.51  ? 130 GLY B N   1 
ATOM   3459 C  CA  . GLY B 1 130 ? -43.997  28.566 24.986  1.00 98.63  ? 130 GLY B CA  1 
ATOM   3460 C  C   . GLY B 1 130 ? -45.250  27.729 25.078  1.00 94.56  ? 130 GLY B C   1 
ATOM   3461 O  O   . GLY B 1 130 ? -45.327  26.838 25.927  1.00 97.26  ? 130 GLY B O   1 
ATOM   3462 N  N   . MET B 1 131 ? -46.239  27.995 24.233  1.00 94.16  ? 131 MET B N   1 
ATOM   3463 C  CA  . MET B 1 131 ? -47.465  27.215 24.181  1.00 92.19  ? 131 MET B CA  1 
ATOM   3464 C  C   . MET B 1 131 ? -47.448  26.345 22.934  1.00 92.03  ? 131 MET B C   1 
ATOM   3465 O  O   . MET B 1 131 ? -46.923  26.751 21.892  1.00 100.34 ? 131 MET B O   1 
ATOM   3466 C  CB  . MET B 1 131 ? -48.697  28.126 24.176  1.00 93.64  ? 131 MET B CB  1 
ATOM   3467 C  CG  . MET B 1 131 ? -48.792  29.043 25.385  1.00 91.27  ? 131 MET B CG  1 
ATOM   3468 S  SD  . MET B 1 131 ? -49.133  28.144 26.910  1.00 97.46  ? 131 MET B SD  1 
ATOM   3469 C  CE  . MET B 1 131 ? -47.921  28.870 28.010  1.00 95.02  ? 131 MET B CE  1 
ATOM   3470 N  N   . THR B 1 132 ? -48.014  25.146 23.046  1.00 87.65  ? 132 THR B N   1 
ATOM   3471 C  CA  . THR B 1 132 ? -48.028  24.225 21.922  1.00 90.00  ? 132 THR B CA  1 
ATOM   3472 C  C   . THR B 1 132 ? -48.778  24.846 20.744  1.00 94.06  ? 132 THR B C   1 
ATOM   3473 O  O   . THR B 1 132 ? -49.651  25.698 20.934  1.00 94.28  ? 132 THR B O   1 
ATOM   3474 C  CB  . THR B 1 132 ? -48.686  22.903 22.314  1.00 89.97  ? 132 THR B CB  1 
ATOM   3475 O  OG1 . THR B 1 132 ? -50.093  23.103 22.496  1.00 91.33  ? 132 THR B OG1 1 
ATOM   3476 C  CG2 . THR B 1 132 ? -48.086  22.369 23.605  1.00 85.41  ? 132 THR B CG2 1 
ATOM   3477 N  N   . PRO B 1 133 ? -48.441  24.456 19.512  1.00 96.07  ? 133 PRO B N   1 
ATOM   3478 C  CA  . PRO B 1 133 ? -49.233  24.924 18.364  1.00 93.93  ? 133 PRO B CA  1 
ATOM   3479 C  C   . PRO B 1 133 ? -50.700  24.552 18.467  1.00 91.83  ? 133 PRO B C   1 
ATOM   3480 O  O   . PRO B 1 133 ? -51.560  25.327 18.027  1.00 94.43  ? 133 PRO B O   1 
ATOM   3481 C  CB  . PRO B 1 133 ? -48.556  24.238 17.170  1.00 90.30  ? 133 PRO B CB  1 
ATOM   3482 C  CG  . PRO B 1 133 ? -47.162  23.980 17.627  1.00 85.35  ? 133 PRO B CG  1 
ATOM   3483 C  CD  . PRO B 1 133 ? -47.264  23.675 19.092  1.00 91.02  ? 133 PRO B CD  1 
ATOM   3484 N  N   . ALA B 1 134 ? -51.013  23.389 19.043  1.00 87.27  ? 134 ALA B N   1 
ATOM   3485 C  CA  . ALA B 1 134 ? -52.407  22.994 19.208  1.00 87.84  ? 134 ALA B CA  1 
ATOM   3486 C  C   . ALA B 1 134 ? -53.144  23.924 20.161  1.00 92.17  ? 134 ALA B C   1 
ATOM   3487 O  O   . ALA B 1 134 ? -54.351  24.142 20.005  1.00 91.84  ? 134 ALA B O   1 
ATOM   3488 C  CB  . ALA B 1 134 ? -52.489  21.551 19.705  1.00 84.86  ? 134 ALA B CB  1 
ATOM   3489 N  N   . TRP B 1 135 ? -52.441  24.483 21.147  1.00 88.49  ? 135 TRP B N   1 
ATOM   3490 C  CA  . TRP B 1 135 ? -53.085  25.400 22.079  1.00 88.93  ? 135 TRP B CA  1 
ATOM   3491 C  C   . TRP B 1 135 ? -53.327  26.761 21.435  1.00 89.10  ? 135 TRP B C   1 
ATOM   3492 O  O   . TRP B 1 135 ? -54.370  27.386 21.667  1.00 87.97  ? 135 TRP B O   1 
ATOM   3493 C  CB  . TRP B 1 135 ? -52.240  25.540 23.344  1.00 88.41  ? 135 TRP B CB  1 
ATOM   3494 C  CG  . TRP B 1 135 ? -52.914  26.335 24.408  1.00 86.22  ? 135 TRP B CG  1 
ATOM   3495 C  CD1 . TRP B 1 135 ? -53.717  25.859 25.402  1.00 85.50  ? 135 TRP B CD1 1 
ATOM   3496 C  CD2 . TRP B 1 135 ? -52.856  27.754 24.582  1.00 87.15  ? 135 TRP B CD2 1 
ATOM   3497 N  NE1 . TRP B 1 135 ? -54.160  26.895 26.188  1.00 89.82  ? 135 TRP B NE1 1 
ATOM   3498 C  CE2 . TRP B 1 135 ? -53.645  28.069 25.705  1.00 86.89  ? 135 TRP B CE2 1 
ATOM   3499 C  CE3 . TRP B 1 135 ? -52.212  28.789 23.898  1.00 88.79  ? 135 TRP B CE3 1 
ATOM   3500 C  CZ2 . TRP B 1 135 ? -53.808  29.373 26.158  1.00 84.46  ? 135 TRP B CZ2 1 
ATOM   3501 C  CZ3 . TRP B 1 135 ? -52.375  30.085 24.350  1.00 86.65  ? 135 TRP B CZ3 1 
ATOM   3502 C  CH2 . TRP B 1 135 ? -53.166  30.365 25.470  1.00 88.58  ? 135 TRP B CH2 1 
ATOM   3503 N  N   . CYS B 1 136 ? -52.378  27.235 20.623  1.00 89.56  ? 136 CYS B N   1 
ATOM   3504 C  CA  . CYS B 1 136 ? -52.547  28.520 19.952  1.00 87.63  ? 136 CYS B CA  1 
ATOM   3505 C  C   . CYS B 1 136 ? -53.707  28.482 18.967  1.00 85.35  ? 136 CYS B C   1 
ATOM   3506 O  O   . CYS B 1 136 ? -54.496  29.431 18.890  1.00 85.14  ? 136 CYS B O   1 
ATOM   3507 C  CB  . CYS B 1 136 ? -51.258  28.916 19.232  1.00 87.24  ? 136 CYS B CB  1 
ATOM   3508 S  SG  . CYS B 1 136 ? -49.826  29.094 20.307  1.00 100.95 ? 136 CYS B SG  1 
ATOM   3509 N  N   . ALA B 1 137 ? -53.823  27.395 18.201  1.00 87.12  ? 137 ALA B N   1 
ATOM   3510 C  CA  . ALA B 1 137 ? -54.899  27.289 17.220  1.00 88.96  ? 137 ALA B CA  1 
ATOM   3511 C  C   . ALA B 1 137 ? -56.265  27.287 17.895  1.00 88.16  ? 137 ALA B C   1 
ATOM   3512 O  O   . ALA B 1 137 ? -57.224  27.869 17.375  1.00 84.07  ? 137 ALA B O   1 
ATOM   3513 C  CB  . ALA B 1 137 ? -54.715  26.029 16.375  1.00 83.45  ? 137 ALA B CB  1 
ATOM   3514 N  N   . ARG B 1 138 ? -56.369  26.641 19.058  1.00 90.67  ? 138 ARG B N   1 
ATOM   3515 C  CA  . ARG B 1 138 ? -57.632  26.609 19.787  1.00 86.41  ? 138 ARG B CA  1 
ATOM   3516 C  C   . ARG B 1 138 ? -57.981  27.986 20.340  1.00 82.34  ? 138 ARG B C   1 
ATOM   3517 O  O   . ARG B 1 138 ? -59.122  28.445 20.220  1.00 80.82  ? 138 ARG B O   1 
ATOM   3518 C  CB  . ARG B 1 138 ? -57.554  25.574 20.910  1.00 84.20  ? 138 ARG B CB  1 
ATOM   3519 C  CG  . ARG B 1 138 ? -58.849  25.363 21.672  1.00 82.75  ? 138 ARG B CG  1 
ATOM   3520 C  CD  . ARG B 1 138 ? -58.679  24.288 22.730  1.00 78.10  ? 138 ARG B CD  1 
ATOM   3521 N  NE  . ARG B 1 138 ? -57.798  24.717 23.810  1.00 85.41  ? 138 ARG B NE  1 
ATOM   3522 C  CZ  . ARG B 1 138 ? -57.247  23.900 24.697  1.00 87.85  ? 138 ARG B CZ  1 
ATOM   3523 N  NH1 . ARG B 1 138 ? -57.433  22.591 24.639  1.00 83.54  ? 138 ARG B NH1 1 
ATOM   3524 N  NH2 . ARG B 1 138 ? -56.488  24.408 25.665  1.00 88.91  ? 138 ARG B NH2 1 
ATOM   3525 N  N   . SER B 1 139 ? -57.002  28.664 20.946  1.00 84.29  ? 139 SER B N   1 
ATOM   3526 C  CA  . SER B 1 139 ? -57.258  29.982 21.520  1.00 83.04  ? 139 SER B CA  1 
ATOM   3527 C  C   . SER B 1 139 ? -57.513  31.028 20.443  1.00 79.51  ? 139 SER B C   1 
ATOM   3528 O  O   . SER B 1 139 ? -58.273  31.976 20.670  1.00 77.69  ? 139 SER B O   1 
ATOM   3529 C  CB  . SER B 1 139 ? -56.086  30.398 22.406  1.00 80.54  ? 139 SER B CB  1 
ATOM   3530 O  OG  . SER B 1 139 ? -55.842  29.421 23.402  1.00 81.43  ? 139 SER B OG  1 
ATOM   3531 N  N   . ALA B 1 140 ? -56.887  30.881 19.274  1.00 82.39  ? 140 ALA B N   1 
ATOM   3532 C  CA  . ALA B 1 140 ? -57.228  31.744 18.149  1.00 80.43  ? 140 ALA B CA  1 
ATOM   3533 C  C   . ALA B 1 140 ? -58.676  31.537 17.728  1.00 78.84  ? 140 ALA B C   1 
ATOM   3534 O  O   . ALA B 1 140 ? -59.378  32.501 17.399  1.00 77.08  ? 140 ALA B O   1 
ATOM   3535 C  CB  . ALA B 1 140 ? -56.283  31.483 16.977  1.00 75.51  ? 140 ALA B CB  1 
ATOM   3536 N  N   . ARG B 1 141 ? -59.143  30.284 17.738  1.00 78.86  ? 141 ARG B N   1 
ATOM   3537 C  CA  . ARG B 1 141 ? -60.546  30.016 17.438  1.00 78.01  ? 141 ARG B CA  1 
ATOM   3538 C  C   . ARG B 1 141 ? -61.460  30.658 18.473  1.00 78.56  ? 141 ARG B C   1 
ATOM   3539 O  O   . ARG B 1 141 ? -62.536  31.163 18.132  1.00 76.00  ? 141 ARG B O   1 
ATOM   3540 C  CB  . ARG B 1 141 ? -60.799  28.510 17.368  1.00 78.62  ? 141 ARG B CB  1 
ATOM   3541 C  CG  . ARG B 1 141 ? -60.200  27.823 16.154  1.00 91.88  ? 141 ARG B CG  1 
ATOM   3542 C  CD  . ARG B 1 141 ? -60.795  26.434 15.960  1.00 98.39  ? 141 ARG B CD  1 
ATOM   3543 N  NE  . ARG B 1 141 ? -60.622  25.585 17.134  1.00 100.56 ? 141 ARG B NE  1 
ATOM   3544 C  CZ  . ARG B 1 141 ? -59.654  24.690 17.279  1.00 99.98  ? 141 ARG B CZ  1 
ATOM   3545 N  NH1 . ARG B 1 141 ? -58.746  24.493 16.335  1.00 98.39  ? 141 ARG B NH1 1 
ATOM   3546 N  NH2 . ARG B 1 141 ? -59.596  23.973 18.398  1.00 96.02  ? 141 ARG B NH2 1 
ATOM   3547 N  N   . HIS B 1 142 ? -61.050  30.644 19.745  1.00 78.00  ? 142 HIS B N   1 
ATOM   3548 C  CA  . HIS B 1 142 ? -61.832  31.303 20.788  1.00 76.11  ? 142 HIS B CA  1 
ATOM   3549 C  C   . HIS B 1 142 ? -61.909  32.802 20.541  1.00 76.49  ? 142 HIS B C   1 
ATOM   3550 O  O   . HIS B 1 142 ? -62.978  33.411 20.661  1.00 74.37  ? 142 HIS B O   1 
ATOM   3551 C  CB  . HIS B 1 142 ? -61.226  31.016 22.162  1.00 73.63  ? 142 HIS B CB  1 
ATOM   3552 C  CG  . HIS B 1 142 ? -61.340  29.586 22.586  1.00 72.74  ? 142 HIS B CG  1 
ATOM   3553 N  ND1 . HIS B 1 142 ? -60.420  28.980 23.415  1.00 74.53  ? 142 HIS B ND1 1 
ATOM   3554 C  CD2 . HIS B 1 142 ? -62.267  28.642 22.300  1.00 71.96  ? 142 HIS B CD2 1 
ATOM   3555 C  CE1 . HIS B 1 142 ? -60.774  27.724 23.617  1.00 76.57  ? 142 HIS B CE1 1 
ATOM   3556 N  NE2 . HIS B 1 142 ? -61.892  27.493 22.952  1.00 69.10  ? 142 HIS B NE2 1 
ATOM   3557 N  N   . TRP B 1 143 ? -60.776  33.414 20.191  1.00 75.98  ? 143 TRP B N   1 
ATOM   3558 C  CA  . TRP B 1 143 ? -60.778  34.834 19.862  1.00 74.69  ? 143 TRP B CA  1 
ATOM   3559 C  C   . TRP B 1 143 ? -61.692  35.128 18.680  1.00 72.27  ? 143 TRP B C   1 
ATOM   3560 O  O   . TRP B 1 143 ? -62.417  36.129 18.684  1.00 72.30  ? 143 TRP B O   1 
ATOM   3561 C  CB  . TRP B 1 143 ? -59.355  35.306 19.572  1.00 77.30  ? 143 TRP B CB  1 
ATOM   3562 C  CG  . TRP B 1 143 ? -58.600  35.670 20.801  1.00 71.82  ? 143 TRP B CG  1 
ATOM   3563 C  CD1 . TRP B 1 143 ? -57.452  35.098 21.260  1.00 70.98  ? 143 TRP B CD1 1 
ATOM   3564 C  CD2 . TRP B 1 143 ? -58.948  36.690 21.742  1.00 75.13  ? 143 TRP B CD2 1 
ATOM   3565 N  NE1 . TRP B 1 143 ? -57.058  35.705 22.428  1.00 73.32  ? 143 TRP B NE1 1 
ATOM   3566 C  CE2 . TRP B 1 143 ? -57.961  36.685 22.746  1.00 68.91  ? 143 TRP B CE2 1 
ATOM   3567 C  CE3 . TRP B 1 143 ? -59.998  37.610 21.832  1.00 74.60  ? 143 TRP B CE3 1 
ATOM   3568 C  CZ2 . TRP B 1 143 ? -57.991  37.564 23.825  1.00 68.58  ? 143 TRP B CZ2 1 
ATOM   3569 C  CZ3 . TRP B 1 143 ? -60.028  38.481 22.904  1.00 72.61  ? 143 TRP B CZ3 1 
ATOM   3570 C  CH2 . TRP B 1 143 ? -59.030  38.453 23.887  1.00 71.43  ? 143 TRP B CH2 1 
ATOM   3571 N  N   . ARG B 1 144 ? -61.682  34.263 17.663  1.00 75.51  ? 144 ARG B N   1 
ATOM   3572 C  CA  . ARG B 1 144 ? -62.525  34.498 16.494  1.00 80.05  ? 144 ARG B CA  1 
ATOM   3573 C  C   . ARG B 1 144 ? -64.005  34.432 16.853  1.00 79.38  ? 144 ARG B C   1 
ATOM   3574 O  O   . ARG B 1 144 ? -64.815  35.183 16.296  1.00 77.81  ? 144 ARG B O   1 
ATOM   3575 C  CB  . ARG B 1 144 ? -62.184  33.503 15.385  1.00 75.83  ? 144 ARG B CB  1 
ATOM   3576 C  CG  . ARG B 1 144 ? -60.816  33.738 14.755  1.00 75.72  ? 144 ARG B CG  1 
ATOM   3577 C  CD  . ARG B 1 144 ? -60.583  32.840 13.548  1.00 84.88  ? 144 ARG B CD  1 
ATOM   3578 N  NE  . ARG B 1 144 ? -59.205  32.922 13.076  1.00 85.52  ? 144 ARG B NE  1 
ATOM   3579 C  CZ  . ARG B 1 144 ? -58.254  32.048 13.380  1.00 86.74  ? 144 ARG B CZ  1 
ATOM   3580 N  NH1 . ARG B 1 144 ? -58.504  30.987 14.130  1.00 82.29  ? 144 ARG B NH1 1 
ATOM   3581 N  NH2 . ARG B 1 144 ? -57.022  32.244 12.919  1.00 84.38  ? 144 ARG B NH2 1 
ATOM   3582 N  N   . ASN B 1 145 ? -64.379  33.546 17.781  1.00 72.23  ? 145 ASN B N   1 
ATOM   3583 C  CA  . ASN B 1 145 ? -65.756  33.536 18.265  1.00 73.45  ? 145 ASN B CA  1 
ATOM   3584 C  C   . ASN B 1 145 ? -66.097  34.855 18.945  1.00 78.87  ? 145 ASN B C   1 
ATOM   3585 O  O   . ASN B 1 145 ? -67.185  35.408 18.742  1.00 78.23  ? 145 ASN B O   1 
ATOM   3586 C  CB  . ASN B 1 145 ? -65.975  32.371 19.231  1.00 76.30  ? 145 ASN B CB  1 
ATOM   3587 C  CG  . ASN B 1 145 ? -65.718  31.021 18.590  1.00 77.96  ? 145 ASN B CG  1 
ATOM   3588 O  OD1 . ASN B 1 145 ? -65.758  30.883 17.368  1.00 75.99  ? 145 ASN B OD1 1 
ATOM   3589 N  ND2 . ASN B 1 145 ? -65.460  30.014 19.417  1.00 78.30  ? 145 ASN B ND2 1 
ATOM   3590 N  N   . TYR B 1 146 ? -65.169  35.371 19.753  1.00 73.12  ? 146 TYR B N   1 
ATOM   3591 C  CA  . TYR B 1 146 ? -65.368  36.645 20.434  1.00 70.63  ? 146 TYR B CA  1 
ATOM   3592 C  C   . TYR B 1 146 ? -65.623  37.772 19.438  1.00 75.74  ? 146 TYR B C   1 
ATOM   3593 O  O   . TYR B 1 146 ? -66.569  38.553 19.596  1.00 74.06  ? 146 TYR B O   1 
ATOM   3594 C  CB  . TYR B 1 146 ? -64.142  36.939 21.304  1.00 72.90  ? 146 TYR B CB  1 
ATOM   3595 C  CG  . TYR B 1 146 ? -64.129  38.282 21.995  1.00 73.91  ? 146 TYR B CG  1 
ATOM   3596 C  CD1 . TYR B 1 146 ? -64.844  38.488 23.167  1.00 68.87  ? 146 TYR B CD1 1 
ATOM   3597 C  CD2 . TYR B 1 146 ? -63.373  39.335 21.493  1.00 74.24  ? 146 TYR B CD2 1 
ATOM   3598 C  CE1 . TYR B 1 146 ? -64.824  39.711 23.809  1.00 70.10  ? 146 TYR B CE1 1 
ATOM   3599 C  CE2 . TYR B 1 146 ? -63.345  40.561 22.129  1.00 74.90  ? 146 TYR B CE2 1 
ATOM   3600 C  CZ  . TYR B 1 146 ? -64.072  40.742 23.288  1.00 74.07  ? 146 TYR B CZ  1 
ATOM   3601 O  OH  . TYR B 1 146 ? -64.051  41.961 23.927  1.00 76.15  ? 146 TYR B OH  1 
ATOM   3602 N  N   . PHE B 1 147 ? -64.796  37.859 18.391  1.00 76.96  ? 147 PHE B N   1 
ATOM   3603 C  CA  . PHE B 1 147 ? -64.936  38.945 17.423  1.00 74.39  ? 147 PHE B CA  1 
ATOM   3604 C  C   . PHE B 1 147 ? -66.172  38.765 16.551  1.00 72.13  ? 147 PHE B C   1 
ATOM   3605 O  O   . PHE B 1 147 ? -66.878  39.739 16.262  1.00 71.65  ? 147 PHE B O   1 
ATOM   3606 C  CB  . PHE B 1 147 ? -63.682  39.048 16.555  1.00 70.34  ? 147 PHE B CB  1 
ATOM   3607 C  CG  . PHE B 1 147 ? -62.464  39.513 17.300  1.00 72.36  ? 147 PHE B CG  1 
ATOM   3608 C  CD1 . PHE B 1 147 ? -62.440  40.759 17.904  1.00 69.58  ? 147 PHE B CD1 1 
ATOM   3609 C  CD2 . PHE B 1 147 ? -61.339  38.711 17.384  1.00 65.86  ? 147 PHE B CD2 1 
ATOM   3610 C  CE1 . PHE B 1 147 ? -61.320  41.190 18.585  1.00 70.14  ? 147 PHE B CE1 1 
ATOM   3611 C  CE2 . PHE B 1 147 ? -60.218  39.137 18.063  1.00 68.15  ? 147 PHE B CE2 1 
ATOM   3612 C  CZ  . PHE B 1 147 ? -60.208  40.377 18.665  1.00 71.62  ? 147 PHE B CZ  1 
ATOM   3613 N  N   . ASP B 1 148 ? -66.443  37.533 16.111  1.00 74.52  ? 148 ASP B N   1 
ATOM   3614 C  CA  . ASP B 1 148 ? -67.659  37.283 15.342  1.00 72.60  ? 148 ASP B CA  1 
ATOM   3615 C  C   . ASP B 1 148 ? -68.904  37.593 16.160  1.00 76.55  ? 148 ASP B C   1 
ATOM   3616 O  O   . ASP B 1 148 ? -69.916  38.037 15.605  1.00 69.11  ? 148 ASP B O   1 
ATOM   3617 C  CB  . ASP B 1 148 ? -67.692  35.834 14.853  1.00 70.76  ? 148 ASP B CB  1 
ATOM   3618 C  CG  . ASP B 1 148 ? -66.721  35.577 13.715  1.00 86.43  ? 148 ASP B CG  1 
ATOM   3619 O  OD1 . ASP B 1 148 ? -66.406  36.529 12.966  1.00 79.76  ? 148 ASP B OD1 1 
ATOM   3620 O  OD2 . ASP B 1 148 ? -66.277  34.418 13.569  1.00 90.06  ? 148 ASP B OD2 1 
ATOM   3621 N  N   . GLY B 1 149 ? -68.846  37.375 17.477  1.00 76.28  ? 149 GLY B N   1 
ATOM   3622 C  CA  . GLY B 1 149 ? -69.979  37.695 18.326  1.00 74.30  ? 149 GLY B CA  1 
ATOM   3623 C  C   . GLY B 1 149 ? -70.268  39.180 18.398  1.00 76.35  ? 149 GLY B C   1 
ATOM   3624 O  O   . GLY B 1 149 ? -71.429  39.582 18.530  1.00 75.16  ? 149 GLY B O   1 
ATOM   3625 N  N   . TYR B 1 150 ? -69.228  40.014 18.319  1.00 76.58  ? 150 TYR B N   1 
ATOM   3626 C  CA  . TYR B 1 150 ? -69.446  41.457 18.319  1.00 77.77  ? 150 TYR B CA  1 
ATOM   3627 C  C   . TYR B 1 150 ? -70.218  41.893 17.082  1.00 70.64  ? 150 TYR B C   1 
ATOM   3628 O  O   . TYR B 1 150 ? -71.067  42.789 17.157  1.00 68.19  ? 150 TYR B O   1 
ATOM   3629 C  CB  . TYR B 1 150 ? -68.112  42.198 18.416  1.00 74.56  ? 150 TYR B CB  1 
ATOM   3630 C  CG  . TYR B 1 150 ? -67.742  42.561 19.836  1.00 75.90  ? 150 TYR B CG  1 
ATOM   3631 C  CD1 . TYR B 1 150 ? -67.237  41.606 20.706  1.00 75.47  ? 150 TYR B CD1 1 
ATOM   3632 C  CD2 . TYR B 1 150 ? -67.908  43.856 20.309  1.00 73.60  ? 150 TYR B CD2 1 
ATOM   3633 C  CE1 . TYR B 1 150 ? -66.904  41.929 22.004  1.00 75.52  ? 150 TYR B CE1 1 
ATOM   3634 C  CE2 . TYR B 1 150 ? -67.577  44.188 21.606  1.00 69.28  ? 150 TYR B CE2 1 
ATOM   3635 C  CZ  . TYR B 1 150 ? -67.075  43.220 22.449  1.00 73.13  ? 150 TYR B CZ  1 
ATOM   3636 O  OH  . TYR B 1 150 ? -66.741  43.540 23.743  1.00 77.84  ? 150 TYR B OH  1 
ATOM   3637 N  N   . VAL B 1 151 ? -69.942  41.267 15.937  1.00 72.43  ? 151 VAL B N   1 
ATOM   3638 C  CA  . VAL B 1 151 ? -70.736  41.537 14.743  1.00 72.76  ? 151 VAL B CA  1 
ATOM   3639 C  C   . VAL B 1 151 ? -72.173  41.074 14.949  1.00 71.56  ? 151 VAL B C   1 
ATOM   3640 O  O   . VAL B 1 151 ? -73.123  41.730 14.504  1.00 76.91  ? 151 VAL B O   1 
ATOM   3641 C  CB  . VAL B 1 151 ? -70.094  40.873 13.510  1.00 71.27  ? 151 VAL B CB  1 
ATOM   3642 C  CG1 . VAL B 1 151 ? -70.899  41.186 12.259  1.00 60.97  ? 151 VAL B CG1 1 
ATOM   3643 C  CG2 . VAL B 1 151 ? -68.651  41.329 13.350  1.00 67.55  ? 151 VAL B CG2 1 
ATOM   3644 N  N   . ASP B 1 152 ? -72.356  39.944 15.638  1.00 75.30  ? 152 ASP B N   1 
ATOM   3645 C  CA  . ASP B 1 152 ? -73.701  39.432 15.882  1.00 73.38  ? 152 ASP B CA  1 
ATOM   3646 C  C   . ASP B 1 152 ? -74.534  40.415 16.699  1.00 75.76  ? 152 ASP B C   1 
ATOM   3647 O  O   . ASP B 1 152 ? -75.714  40.634 16.400  1.00 73.46  ? 152 ASP B O   1 
ATOM   3648 C  CB  . ASP B 1 152 ? -73.632  38.077 16.589  1.00 76.55  ? 152 ASP B CB  1 
ATOM   3649 C  CG  . ASP B 1 152 ? -73.045  36.986 15.711  1.00 78.77  ? 152 ASP B CG  1 
ATOM   3650 O  OD1 . ASP B 1 152 ? -73.000  37.170 14.478  1.00 82.18  ? 152 ASP B OD1 1 
ATOM   3651 O  OD2 . ASP B 1 152 ? -72.638  35.936 16.254  1.00 88.41  ? 152 ASP B OD2 1 
ATOM   3652 N  N   . GLU B 1 153 ? -73.940  41.017 17.734  1.00 74.83  ? 153 GLU B N   1 
ATOM   3653 C  CA  . GLU B 1 153 ? -74.680  41.970 18.557  1.00 76.28  ? 153 GLU B CA  1 
ATOM   3654 C  C   . GLU B 1 153 ? -75.020  43.234 17.777  1.00 75.26  ? 153 GLU B C   1 
ATOM   3655 O  O   . GLU B 1 153 ? -76.118  43.784 17.927  1.00 72.24  ? 153 GLU B O   1 
ATOM   3656 C  CB  . GLU B 1 153 ? -73.884  42.317 19.816  1.00 78.28  ? 153 GLU B CB  1 
ATOM   3657 C  CG  . GLU B 1 153 ? -73.787  41.179 20.814  1.00 79.84  ? 153 GLU B CG  1 
ATOM   3658 C  CD  . GLU B 1 153 ? -73.084  41.579 22.090  1.00 91.52  ? 153 GLU B CD  1 
ATOM   3659 O  OE1 . GLU B 1 153 ? -72.462  42.662 22.109  1.00 101.39 ? 153 GLU B OE1 1 
ATOM   3660 O  OE2 . GLU B 1 153 ? -73.157  40.812 23.074  1.00 92.22  ? 153 GLU B OE2 1 
ATOM   3661 N  N   . ALA B 1 154 ? -74.090  43.715 16.947  1.00 75.79  ? 154 ALA B N   1 
ATOM   3662 C  CA  . ALA B 1 154 ? -74.372  44.883 16.118  1.00 75.09  ? 154 ALA B CA  1 
ATOM   3663 C  C   . ALA B 1 154 ? -75.496  44.595 15.133  1.00 77.19  ? 154 ALA B C   1 
ATOM   3664 O  O   . ALA B 1 154 ? -76.338  45.461 14.865  1.00 74.99  ? 154 ALA B O   1 
ATOM   3665 C  CB  . ALA B 1 154 ? -73.108  45.320 15.379  1.00 71.90  ? 154 ALA B CB  1 
ATOM   3666 N  N   . GLU B 1 155 ? -75.527  43.377 14.588  1.00 74.74  ? 155 GLU B N   1 
ATOM   3667 C  CA  . GLU B 1 155 ? -76.602  42.994 13.680  1.00 78.65  ? 155 GLU B CA  1 
ATOM   3668 C  C   . GLU B 1 155 ? -77.952  43.014 14.387  1.00 78.42  ? 155 GLU B C   1 
ATOM   3669 O  O   . GLU B 1 155 ? -78.957  43.449 13.812  1.00 82.38  ? 155 GLU B O   1 
ATOM   3670 C  CB  . GLU B 1 155 ? -76.312  41.612 13.097  1.00 77.93  ? 155 GLU B CB  1 
ATOM   3671 C  CG  . GLU B 1 155 ? -77.217  41.199 11.956  1.00 87.37  ? 155 GLU B CG  1 
ATOM   3672 C  CD  . GLU B 1 155 ? -76.728  39.939 11.270  1.00 99.49  ? 155 GLU B CD  1 
ATOM   3673 O  OE1 . GLU B 1 155 ? -75.650  39.435 11.653  1.00 96.06  ? 155 GLU B OE1 1 
ATOM   3674 O  OE2 . GLU B 1 155 ? -77.419  39.454 10.349  1.00 111.06 ? 155 GLU B OE2 1 
ATOM   3675 N  N   . SER B 1 156 ? -77.993  42.554 15.640  1.00 77.73  ? 156 SER B N   1 
ATOM   3676 C  CA  . SER B 1 156 ? -79.233  42.594 16.406  1.00 76.71  ? 156 SER B CA  1 
ATOM   3677 C  C   . SER B 1 156 ? -79.716  44.027 16.603  1.00 77.19  ? 156 SER B C   1 
ATOM   3678 O  O   . SER B 1 156 ? -80.906  44.317 16.439  1.00 77.76  ? 156 SER B O   1 
ATOM   3679 C  CB  . SER B 1 156 ? -79.032  41.902 17.755  1.00 80.11  ? 156 SER B CB  1 
ATOM   3680 O  OG  . SER B 1 156 ? -80.213  41.940 18.537  1.00 79.18  ? 156 SER B OG  1 
ATOM   3681 N  N   . ARG B 1 157 ? -78.804  44.938 16.953  1.00 76.79  ? 157 ARG B N   1 
ATOM   3682 C  CA  . ARG B 1 157 ? -79.189  46.333 17.144  1.00 77.55  ? 157 ARG B CA  1 
ATOM   3683 C  C   . ARG B 1 157 ? -79.610  46.978 15.830  1.00 81.01  ? 157 ARG B C   1 
ATOM   3684 O  O   . ARG B 1 157 ? -80.529  47.805 15.805  1.00 81.87  ? 157 ARG B O   1 
ATOM   3685 C  CB  . ARG B 1 157 ? -78.037  47.112 17.779  1.00 79.21  ? 157 ARG B CB  1 
ATOM   3686 C  CG  . ARG B 1 157 ? -77.808  46.791 19.246  1.00 85.46  ? 157 ARG B CG  1 
ATOM   3687 C  CD  . ARG B 1 157 ? -76.424  47.216 19.701  1.00 83.46  ? 157 ARG B CD  1 
ATOM   3688 N  NE  . ARG B 1 157 ? -76.104  46.680 21.017  1.00 92.25  ? 157 ARG B NE  1 
ATOM   3689 C  CZ  . ARG B 1 157 ? -74.877  46.383 21.425  1.00 99.56  ? 157 ARG B CZ  1 
ATOM   3690 N  NH1 . ARG B 1 157 ? -73.828  46.547 20.634  1.00 93.96  ? 157 ARG B NH1 1 
ATOM   3691 N  NH2 . ARG B 1 157 ? -74.700  45.902 22.654  1.00 90.72  ? 157 ARG B NH2 1 
ATOM   3692 N  N   . PHE B 1 158 ? -78.955  46.607 14.728  1.00 83.37  ? 158 PHE B N   1 
ATOM   3693 C  CA  . PHE B 1 158 ? -79.257  47.219 13.438  1.00 80.48  ? 158 PHE B CA  1 
ATOM   3694 C  C   . PHE B 1 158 ? -80.680  46.905 12.997  1.00 84.24  ? 158 PHE B C   1 
ATOM   3695 O  O   . PHE B 1 158 ? -81.426  47.800 12.583  1.00 90.37  ? 158 PHE B O   1 
ATOM   3696 C  CB  . PHE B 1 158 ? -78.250  46.745 12.391  1.00 81.55  ? 158 PHE B CB  1 
ATOM   3697 C  CG  . PHE B 1 158 ? -78.489  47.307 11.020  1.00 89.92  ? 158 PHE B CG  1 
ATOM   3698 C  CD1 . PHE B 1 158 ? -78.473  48.676 10.804  1.00 90.85  ? 158 PHE B CD1 1 
ATOM   3699 C  CD2 . PHE B 1 158 ? -78.711  46.465 9.940   1.00 94.15  ? 158 PHE B CD2 1 
ATOM   3700 C  CE1 . PHE B 1 158 ? -78.687  49.195 9.540   1.00 91.36  ? 158 PHE B CE1 1 
ATOM   3701 C  CE2 . PHE B 1 158 ? -78.924  46.978 8.673   1.00 90.59  ? 158 PHE B CE2 1 
ATOM   3702 C  CZ  . PHE B 1 158 ? -78.912  48.344 8.473   1.00 89.29  ? 158 PHE B CZ  1 
ATOM   3703 N  N   . TRP B 1 159 ? -81.078  45.637 13.081  1.00 85.33  ? 159 TRP B N   1 
ATOM   3704 C  CA  . TRP B 1 159 ? -82.409  45.226 12.653  1.00 87.50  ? 159 TRP B CA  1 
ATOM   3705 C  C   . TRP B 1 159 ? -83.475  45.445 13.717  1.00 83.68  ? 159 TRP B C   1 
ATOM   3706 O  O   . TRP B 1 159 ? -84.632  45.072 13.489  1.00 83.80  ? 159 TRP B O   1 
ATOM   3707 C  CB  . TRP B 1 159 ? -82.395  43.752 12.237  1.00 87.10  ? 159 TRP B CB  1 
ATOM   3708 C  CG  . TRP B 1 159 ? -81.492  43.467 11.075  1.00 91.54  ? 159 TRP B CG  1 
ATOM   3709 C  CD1 . TRP B 1 159 ? -80.263  42.874 11.117  1.00 92.10  ? 159 TRP B CD1 1 
ATOM   3710 C  CD2 . TRP B 1 159 ? -81.743  43.772 9.699   1.00 94.26  ? 159 TRP B CD2 1 
ATOM   3711 N  NE1 . TRP B 1 159 ? -79.736  42.787 9.852   1.00 86.56  ? 159 TRP B NE1 1 
ATOM   3712 C  CE2 . TRP B 1 159 ? -80.625  43.332 8.963   1.00 93.74  ? 159 TRP B CE2 1 
ATOM   3713 C  CE3 . TRP B 1 159 ? -82.806  44.372 9.017   1.00 94.07  ? 159 TRP B CE3 1 
ATOM   3714 C  CZ2 . TRP B 1 159 ? -80.539  43.472 7.581   1.00 97.74  ? 159 TRP B CZ2 1 
ATOM   3715 C  CZ3 . TRP B 1 159 ? -82.719  44.511 7.646   1.00 95.77  ? 159 TRP B CZ3 1 
ATOM   3716 C  CH2 . TRP B 1 159 ? -81.593  44.063 6.942   1.00 97.50  ? 159 TRP B CH2 1 
ATOM   3717 N  N   . ASN B 1 160 ? -83.121  46.045 14.856  1.00 88.57  ? 160 ASN B N   1 
ATOM   3718 C  CA  . ASN B 1 160 ? -84.051  46.240 15.970  1.00 91.41  ? 160 ASN B CA  1 
ATOM   3719 C  C   . ASN B 1 160 ? -84.732  44.926 16.347  1.00 90.82  ? 160 ASN B C   1 
ATOM   3720 O  O   . ASN B 1 160 ? -85.935  44.875 16.610  1.00 95.38  ? 160 ASN B O   1 
ATOM   3721 C  CB  . ASN B 1 160 ? -85.085  47.321 15.647  1.00 88.73  ? 160 ASN B CB  1 
ATOM   3722 N  N   . ALA B 1 161 ? -83.946  43.847 16.360  1.00 86.63  ? 161 ALA B N   1 
ATOM   3723 C  CA  . ALA B 1 161 ? -84.429  42.500 16.653  1.00 87.20  ? 161 ALA B CA  1 
ATOM   3724 C  C   . ALA B 1 161 ? -83.859  42.044 17.990  1.00 87.22  ? 161 ALA B C   1 
ATOM   3725 O  O   . ALA B 1 161 ? -82.792  41.415 18.035  1.00 87.88  ? 161 ALA B O   1 
ATOM   3726 C  CB  . ALA B 1 161 ? -84.039  41.529 15.537  1.00 84.63  ? 161 ALA B CB  1 
ATOM   3727 N  N   . PRO B 1 162 ? -84.524  42.334 19.105  1.00 84.66  ? 162 PRO B N   1 
ATOM   3728 C  CA  . PRO B 1 162 ? -84.002  41.902 20.405  1.00 84.92  ? 162 PRO B CA  1 
ATOM   3729 C  C   . PRO B 1 162 ? -84.195  40.409 20.619  1.00 83.20  ? 162 PRO B C   1 
ATOM   3730 O  O   . PRO B 1 162 ? -85.112  39.791 20.074  1.00 86.80  ? 162 PRO B O   1 
ATOM   3731 C  CB  . PRO B 1 162 ? -84.828  42.720 21.403  1.00 84.50  ? 162 PRO B CB  1 
ATOM   3732 C  CG  . PRO B 1 162 ? -86.118  42.958 20.694  1.00 81.04  ? 162 PRO B CG  1 
ATOM   3733 C  CD  . PRO B 1 162 ? -85.767  43.113 19.239  1.00 84.82  ? 162 PRO B CD  1 
ATOM   3734 N  N   . CYS B 1 163 ? -83.305  39.832 21.427  1.00 82.42  ? 163 CYS B N   1 
ATOM   3735 C  CA  . CYS B 1 163 ? -83.393  38.412 21.745  1.00 83.52  ? 163 CYS B CA  1 
ATOM   3736 C  C   . CYS B 1 163 ? -84.676  38.122 22.511  1.00 81.20  ? 163 CYS B C   1 
ATOM   3737 O  O   . CYS B 1 163 ? -85.034  38.844 23.446  1.00 76.88  ? 163 CYS B O   1 
ATOM   3738 C  CB  . CYS B 1 163 ? -82.171  37.976 22.554  1.00 74.37  ? 163 CYS B CB  1 
ATOM   3739 S  SG  . CYS B 1 163 ? -80.643  37.900 21.586  1.00 85.52  ? 163 CYS B SG  1 
ATOM   3740 N  N   . ASP B 1 164 ? -85.373  37.061 22.108  1.00 89.25  ? 164 ASP B N   1 
ATOM   3741 C  CA  . ASP B 1 164 ? -86.698  36.756 22.633  1.00 86.77  ? 164 ASP B CA  1 
ATOM   3742 C  C   . ASP B 1 164 ? -86.676  35.799 23.818  1.00 79.33  ? 164 ASP B C   1 
ATOM   3743 O  O   . ASP B 1 164 ? -87.740  35.503 24.371  1.00 86.13  ? 164 ASP B O   1 
ATOM   3744 C  CB  . ASP B 1 164 ? -87.588  36.176 21.524  1.00 87.18  ? 164 ASP B CB  1 
ATOM   3745 C  CG  . ASP B 1 164 ? -87.150  34.783 21.071  1.00 99.61  ? 164 ASP B CG  1 
ATOM   3746 O  OD1 . ASP B 1 164 ? -86.056  34.319 21.463  1.00 94.37  ? 164 ASP B OD1 1 
ATOM   3747 O  OD2 . ASP B 1 164 ? -87.914  34.144 20.315  1.00 100.00 ? 164 ASP B OD2 1 
ATOM   3748 N  N   . SER B 1 165 ? -85.507  35.303 24.214  1.00 78.05  ? 165 SER B N   1 
ATOM   3749 C  CA  . SER B 1 165 ? -85.434  34.319 25.284  1.00 81.55  ? 165 SER B CA  1 
ATOM   3750 C  C   . SER B 1 165 ? -84.019  34.287 25.839  1.00 77.21  ? 165 SER B C   1 
ATOM   3751 O  O   . SER B 1 165 ? -83.075  34.781 25.218  1.00 75.37  ? 165 SER B O   1 
ATOM   3752 C  CB  . SER B 1 165 ? -85.845  32.928 24.790  1.00 83.51  ? 165 SER B CB  1 
ATOM   3753 O  OG  . SER B 1 165 ? -85.003  32.502 23.731  1.00 83.16  ? 165 SER B OG  1 
ATOM   3754 N  N   . ALA B 1 166 ? -83.889  33.698 27.029  1.00 77.28  ? 166 ALA B N   1 
ATOM   3755 C  CA  . ALA B 1 166 ? -82.567  33.510 27.614  1.00 72.51  ? 166 ALA B CA  1 
ATOM   3756 C  C   . ALA B 1 166 ? -81.709  32.600 26.745  1.00 81.68  ? 166 ALA B C   1 
ATOM   3757 O  O   . ALA B 1 166 ? -80.501  32.824 26.603  1.00 81.37  ? 166 ALA B O   1 
ATOM   3758 C  CB  . ALA B 1 166 ? -82.696  32.939 29.025  1.00 63.60  ? 166 ALA B CB  1 
ATOM   3759 N  N   . ALA B 1 167 ? -82.321  31.574 26.147  1.00 81.82  ? 167 ALA B N   1 
ATOM   3760 C  CA  . ALA B 1 167 ? -81.574  30.635 25.315  1.00 77.08  ? 167 ALA B CA  1 
ATOM   3761 C  C   . ALA B 1 167 ? -80.946  31.336 24.117  1.00 81.50  ? 167 ALA B C   1 
ATOM   3762 O  O   . ALA B 1 167 ? -79.742  31.202 23.868  1.00 83.97  ? 167 ALA B O   1 
ATOM   3763 C  CB  . ALA B 1 167 ? -82.491  29.501 24.853  1.00 78.46  ? 167 ALA B CB  1 
ATOM   3764 N  N   . GLN B 1 168 ? -81.751  32.084 23.357  1.00 81.50  ? 168 GLN B N   1 
ATOM   3765 C  CA  . GLN B 1 168 ? -81.218  32.807 22.206  1.00 80.48  ? 168 GLN B CA  1 
ATOM   3766 C  C   . GLN B 1 168 ? -80.194  33.854 22.627  1.00 80.86  ? 168 GLN B C   1 
ATOM   3767 O  O   . GLN B 1 168 ? -79.248  34.134 21.882  1.00 80.86  ? 168 GLN B O   1 
ATOM   3768 C  CB  . GLN B 1 168 ? -82.359  33.458 21.419  1.00 82.73  ? 168 GLN B CB  1 
ATOM   3769 C  CG  . GLN B 1 168 ? -81.900  34.306 20.237  1.00 92.26  ? 168 GLN B CG  1 
ATOM   3770 C  CD  . GLN B 1 168 ? -83.054  34.842 19.410  1.00 97.45  ? 168 GLN B CD  1 
ATOM   3771 O  OE1 . GLN B 1 168 ? -84.182  34.367 19.521  1.00 98.06  ? 168 GLN B OE1 1 
ATOM   3772 N  NE2 . GLN B 1 168 ? -82.773  35.836 18.573  1.00 96.87  ? 168 GLN B NE2 1 
ATOM   3773 N  N   . TYR B 1 169 ? -80.353  34.428 23.821  1.00 77.31  ? 169 TYR B N   1 
ATOM   3774 C  CA  . TYR B 1 169 ? -79.416  35.448 24.277  1.00 72.97  ? 169 TYR B CA  1 
ATOM   3775 C  C   . TYR B 1 169 ? -78.075  34.840 24.660  1.00 73.90  ? 169 TYR B C   1 
ATOM   3776 O  O   . TYR B 1 169 ? -77.020  35.414 24.367  1.00 72.99  ? 169 TYR B O   1 
ATOM   3777 C  CB  . TYR B 1 169 ? -80.011  36.215 25.454  1.00 76.02  ? 169 TYR B CB  1 
ATOM   3778 C  CG  . TYR B 1 169 ? -79.068  37.227 26.062  1.00 81.12  ? 169 TYR B CG  1 
ATOM   3779 C  CD1 . TYR B 1 169 ? -78.554  38.270 25.299  1.00 76.19  ? 169 TYR B CD1 1 
ATOM   3780 C  CD2 . TYR B 1 169 ? -78.704  37.151 27.402  1.00 72.35  ? 169 TYR B CD2 1 
ATOM   3781 C  CE1 . TYR B 1 169 ? -77.699  39.203 25.852  1.00 74.56  ? 169 TYR B CE1 1 
ATOM   3782 C  CE2 . TYR B 1 169 ? -77.848  38.080 27.962  1.00 69.14  ? 169 TYR B CE2 1 
ATOM   3783 C  CZ  . TYR B 1 169 ? -77.349  39.103 27.182  1.00 69.77  ? 169 TYR B CZ  1 
ATOM   3784 O  OH  . TYR B 1 169 ? -76.497  40.031 27.732  1.00 76.45  ? 169 TYR B OH  1 
ATOM   3785 N  N   . LEU B 1 170 ? -78.095  33.679 25.318  1.00 76.40  ? 170 LEU B N   1 
ATOM   3786 C  CA  . LEU B 1 170 ? -76.851  33.054 25.751  1.00 77.68  ? 170 LEU B CA  1 
ATOM   3787 C  C   . LEU B 1 170 ? -76.016  32.596 24.563  1.00 77.50  ? 170 LEU B C   1 
ATOM   3788 O  O   . LEU B 1 170 ? -74.783  32.688 24.595  1.00 77.76  ? 170 LEU B O   1 
ATOM   3789 C  CB  . LEU B 1 170 ? -77.152  31.884 26.685  1.00 76.79  ? 170 LEU B CB  1 
ATOM   3790 C  CG  . LEU B 1 170 ? -77.701  32.279 28.056  1.00 79.55  ? 170 LEU B CG  1 
ATOM   3791 C  CD1 . LEU B 1 170 ? -78.275  31.071 28.777  1.00 79.54  ? 170 LEU B CD1 1 
ATOM   3792 C  CD2 . LEU B 1 170 ? -76.617  32.941 28.894  1.00 72.11  ? 170 LEU B CD2 1 
ATOM   3793 N  N   . ALA B 1 171 ? -76.667  32.113 23.500  1.00 81.95  ? 171 ALA B N   1 
ATOM   3794 C  CA  . ALA B 1 171 ? -75.935  31.648 22.325  1.00 80.93  ? 171 ALA B CA  1 
ATOM   3795 C  C   . ALA B 1 171 ? -75.010  32.729 21.780  1.00 81.68  ? 171 ALA B C   1 
ATOM   3796 O  O   . ALA B 1 171 ? -73.918  32.432 21.281  1.00 84.76  ? 171 ALA B O   1 
ATOM   3797 C  CB  . ALA B 1 171 ? -76.916  31.193 21.243  1.00 74.14  ? 171 ALA B CB  1 
ATOM   3798 N  N   . MET B 1 172 ? -75.425  33.990 21.879  1.00 78.34  ? 172 MET B N   1 
ATOM   3799 C  CA  . MET B 1 172 ? -74.629  35.113 21.402  1.00 75.87  ? 172 MET B CA  1 
ATOM   3800 C  C   . MET B 1 172 ? -73.723  35.690 22.486  1.00 76.70  ? 172 MET B C   1 
ATOM   3801 O  O   . MET B 1 172 ? -72.552  35.983 22.221  1.00 75.31  ? 172 MET B O   1 
ATOM   3802 C  CB  . MET B 1 172 ? -75.559  36.198 20.862  1.00 74.17  ? 172 MET B CB  1 
ATOM   3803 C  CG  . MET B 1 172 ? -74.877  37.494 20.494  1.00 78.44  ? 172 MET B CG  1 
ATOM   3804 S  SD  . MET B 1 172 ? -76.109  38.740 20.078  1.00 94.34  ? 172 MET B SD  1 
ATOM   3805 C  CE  . MET B 1 172 ? -76.946  38.927 21.653  1.00 82.08  ? 172 MET B CE  1 
ATOM   3806 N  N   . ARG B 1 173 ? -74.241  35.850 23.706  1.00 67.87  ? 173 ARG B N   1 
ATOM   3807 C  CA  . ARG B 1 173 ? -73.489  36.508 24.767  1.00 73.85  ? 173 ARG B CA  1 
ATOM   3808 C  C   . ARG B 1 173 ? -72.408  35.619 25.374  1.00 76.47  ? 173 ARG B C   1 
ATOM   3809 O  O   . ARG B 1 173 ? -71.509  36.135 26.049  1.00 74.38  ? 173 ARG B O   1 
ATOM   3810 C  CB  . ARG B 1 173 ? -74.442  36.986 25.867  1.00 75.80  ? 173 ARG B CB  1 
ATOM   3811 C  CG  . ARG B 1 173 ? -73.835  38.005 26.825  1.00 78.68  ? 173 ARG B CG  1 
ATOM   3812 C  CD  . ARG B 1 173 ? -73.661  39.363 26.158  1.00 83.14  ? 173 ARG B CD  1 
ATOM   3813 N  NE  . ARG B 1 173 ? -72.487  40.077 26.649  1.00 88.54  ? 173 ARG B NE  1 
ATOM   3814 C  CZ  . ARG B 1 173 ? -72.439  40.758 27.786  1.00 95.03  ? 173 ARG B CZ  1 
ATOM   3815 N  NH1 . ARG B 1 173 ? -73.484  40.828 28.596  1.00 92.65  ? 173 ARG B NH1 1 
ATOM   3816 N  NH2 . ARG B 1 173 ? -71.313  41.383 28.121  1.00 95.23  ? 173 ARG B NH2 1 
ATOM   3817 N  N   . ARG B 1 174 ? -72.466  34.303 25.158  1.00 68.64  ? 174 ARG B N   1 
ATOM   3818 C  CA  . ARG B 1 174 ? -71.410  33.443 25.682  1.00 64.68  ? 174 ARG B CA  1 
ATOM   3819 C  C   . ARG B 1 174 ? -70.069  33.749 25.031  1.00 72.82  ? 174 ARG B C   1 
ATOM   3820 O  O   . ARG B 1 174 ? -69.018  33.566 25.658  1.00 71.92  ? 174 ARG B O   1 
ATOM   3821 C  CB  . ARG B 1 174 ? -71.772  31.971 25.488  1.00 67.87  ? 174 ARG B CB  1 
ATOM   3822 C  CG  . ARG B 1 174 ? -72.758  31.435 26.516  1.00 74.81  ? 174 ARG B CG  1 
ATOM   3823 C  CD  . ARG B 1 174 ? -72.846  29.919 26.467  1.00 82.23  ? 174 ARG B CD  1 
ATOM   3824 N  NE  . ARG B 1 174 ? -73.652  29.384 27.559  1.00 84.65  ? 174 ARG B NE  1 
ATOM   3825 C  CZ  . ARG B 1 174 ? -74.865  28.868 27.412  1.00 79.14  ? 174 ARG B CZ  1 
ATOM   3826 N  NH1 . ARG B 1 174 ? -75.439  28.780 26.224  1.00 73.75  ? 174 ARG B NH1 1 
ATOM   3827 N  NH2 . ARG B 1 174 ? -75.517  28.425 28.484  1.00 73.52  ? 174 ARG B NH2 1 
ATOM   3828 N  N   . HIS B 1 175 ? -70.082  34.229 23.787  1.00 75.00  ? 175 HIS B N   1 
ATOM   3829 C  CA  . HIS B 1 175 ? -68.855  34.561 23.075  1.00 73.95  ? 175 HIS B CA  1 
ATOM   3830 C  C   . HIS B 1 175 ? -68.391  35.986 23.346  1.00 71.38  ? 175 HIS B C   1 
ATOM   3831 O  O   . HIS B 1 175 ? -67.184  36.236 23.433  1.00 74.44  ? 175 HIS B O   1 
ATOM   3832 C  CB  . HIS B 1 175 ? -69.051  34.363 21.572  1.00 74.63  ? 175 HIS B CB  1 
ATOM   3833 C  CG  . HIS B 1 175 ? -69.639  33.036 21.213  1.00 76.41  ? 175 HIS B CG  1 
ATOM   3834 N  ND1 . HIS B 1 175 ? -68.920  31.862 21.276  1.00 78.41  ? 175 HIS B ND1 1 
ATOM   3835 C  CD2 . HIS B 1 175 ? -70.880  32.696 20.791  1.00 77.08  ? 175 HIS B CD2 1 
ATOM   3836 C  CE1 . HIS B 1 175 ? -69.692  30.856 20.907  1.00 77.31  ? 175 HIS B CE1 1 
ATOM   3837 N  NE2 . HIS B 1 175 ? -70.886  31.334 20.608  1.00 78.07  ? 175 HIS B NE2 1 
ATOM   3838 N  N   . THR B 1 176 ? -69.325  36.926 23.487  1.00 72.06  ? 176 THR B N   1 
ATOM   3839 C  CA  . THR B 1 176 ? -68.958  38.327 23.652  1.00 75.48  ? 176 THR B CA  1 
ATOM   3840 C  C   . THR B 1 176 ? -68.569  38.682 25.082  1.00 76.50  ? 176 THR B C   1 
ATOM   3841 O  O   . THR B 1 176 ? -67.931  39.719 25.292  1.00 80.42  ? 176 THR B O   1 
ATOM   3842 C  CB  . THR B 1 176 ? -70.107  39.226 23.196  1.00 76.24  ? 176 THR B CB  1 
ATOM   3843 O  OG1 . THR B 1 176 ? -71.253  39.003 24.028  1.00 71.06  ? 176 THR B OG1 1 
ATOM   3844 C  CG2 . THR B 1 176 ? -70.471  38.914 21.756  1.00 78.96  ? 176 THR B CG2 1 
ATOM   3845 N  N   . ILE B 1 177 ? -68.932  37.855 26.067  1.00 74.28  ? 177 ILE B N   1 
ATOM   3846 C  CA  . ILE B 1 177 ? -68.550  38.149 27.445  1.00 71.91  ? 177 ILE B CA  1 
ATOM   3847 C  C   . ILE B 1 177 ? -67.040  38.027 27.619  1.00 73.45  ? 177 ILE B C   1 
ATOM   3848 O  O   . ILE B 1 177 ? -66.454  38.673 28.498  1.00 70.19  ? 177 ILE B O   1 
ATOM   3849 C  CB  . ILE B 1 177 ? -69.321  37.238 28.422  1.00 74.07  ? 177 ILE B CB  1 
ATOM   3850 C  CG1 . ILE B 1 177 ? -69.093  37.679 29.870  1.00 67.34  ? 177 ILE B CG1 1 
ATOM   3851 C  CG2 . ILE B 1 177 ? -68.932  35.778 28.231  1.00 68.23  ? 177 ILE B CG2 1 
ATOM   3852 C  CD1 . ILE B 1 177 ? -69.532  39.100 30.149  1.00 67.51  ? 177 ILE B CD1 1 
ATOM   3853 N  N   . GLY B 1 178 ? -66.385  37.220 26.786  1.00 72.02  ? 178 GLY B N   1 
ATOM   3854 C  CA  . GLY B 1 178 ? -64.939  37.128 26.803  1.00 69.92  ? 178 GLY B CA  1 
ATOM   3855 C  C   . GLY B 1 178 ? -64.352  36.237 27.872  1.00 66.72  ? 178 GLY B C   1 
ATOM   3856 O  O   . GLY B 1 178 ? -63.170  36.379 28.195  1.00 65.31  ? 178 GLY B O   1 
ATOM   3857 N  N   . VAL B 1 179 ? -65.135  35.309 28.424  1.00 68.16  ? 179 VAL B N   1 
ATOM   3858 C  CA  . VAL B 1 179 ? -64.633  34.470 29.509  1.00 69.79  ? 179 VAL B CA  1 
ATOM   3859 C  C   . VAL B 1 179 ? -63.617  33.457 28.990  1.00 72.63  ? 179 VAL B C   1 
ATOM   3860 O  O   . VAL B 1 179 ? -62.603  33.186 29.644  1.00 69.67  ? 179 VAL B O   1 
ATOM   3861 C  CB  . VAL B 1 179 ? -65.804  33.780 30.229  1.00 67.98  ? 179 VAL B CB  1 
ATOM   3862 C  CG1 . VAL B 1 179 ? -65.292  32.709 31.174  1.00 67.08  ? 179 VAL B CG1 1 
ATOM   3863 C  CG2 . VAL B 1 179 ? -66.622  34.805 30.982  1.00 67.25  ? 179 VAL B CG2 1 
ATOM   3864 N  N   . GLN B 1 180 ? -63.864  32.885 27.812  1.00 69.94  ? 180 GLN B N   1 
ATOM   3865 C  CA  . GLN B 1 180 ? -62.977  31.833 27.318  1.00 71.29  ? 180 GLN B CA  1 
ATOM   3866 C  C   . GLN B 1 180 ? -61.556  32.322 27.057  1.00 74.69  ? 180 GLN B C   1 
ATOM   3867 O  O   . GLN B 1 180 ? -60.609  31.638 27.484  1.00 76.89  ? 180 GLN B O   1 
ATOM   3868 C  CB  . GLN B 1 180 ? -63.585  31.177 26.075  1.00 67.76  ? 180 GLN B CB  1 
ATOM   3869 C  CG  . GLN B 1 180 ? -62.936  29.846 25.731  1.00 72.64  ? 180 GLN B CG  1 
ATOM   3870 C  CD  . GLN B 1 180 ? -62.893  28.897 26.921  1.00 84.14  ? 180 GLN B CD  1 
ATOM   3871 O  OE1 . GLN B 1 180 ? -61.852  28.725 27.559  1.00 82.07  ? 180 GLN B OE1 1 
ATOM   3872 N  NE2 . GLN B 1 180 ? -64.027  28.277 27.223  1.00 86.31  ? 180 GLN B NE2 1 
ATOM   3873 N  N   . PRO B 1 181 ? -61.319  33.459 26.388  1.00 71.22  ? 181 PRO B N   1 
ATOM   3874 C  CA  . PRO B 1 181 ? -59.930  33.933 26.270  1.00 70.10  ? 181 PRO B CA  1 
ATOM   3875 C  C   . PRO B 1 181 ? -59.317  34.302 27.607  1.00 74.11  ? 181 PRO B C   1 
ATOM   3876 O  O   . PRO B 1 181 ? -58.088  34.255 27.751  1.00 75.27  ? 181 PRO B O   1 
ATOM   3877 C  CB  . PRO B 1 181 ? -60.049  35.154 25.346  1.00 71.12  ? 181 PRO B CB  1 
ATOM   3878 C  CG  . PRO B 1 181 ? -61.350  34.987 24.647  1.00 71.96  ? 181 PRO B CG  1 
ATOM   3879 C  CD  . PRO B 1 181 ? -62.245  34.331 25.646  1.00 69.96  ? 181 PRO B CD  1 
ATOM   3880 N  N   . THR B 1 182 ? -60.142  34.675 28.589  1.00 73.44  ? 182 THR B N   1 
ATOM   3881 C  CA  . THR B 1 182 ? -59.640  34.937 29.934  1.00 72.43  ? 182 THR B CA  1 
ATOM   3882 C  C   . THR B 1 182 ? -59.147  33.652 30.588  1.00 75.84  ? 182 THR B C   1 
ATOM   3883 O  O   . THR B 1 182 ? -58.052  33.613 31.161  1.00 79.21  ? 182 THR B O   1 
ATOM   3884 C  CB  . THR B 1 182 ? -60.736  35.584 30.782  1.00 72.86  ? 182 THR B CB  1 
ATOM   3885 O  OG1 . THR B 1 182 ? -61.158  36.809 30.169  1.00 70.42  ? 182 THR B OG1 1 
ATOM   3886 C  CG2 . THR B 1 182 ? -60.234  35.867 32.186  1.00 67.08  ? 182 THR B CG2 1 
ATOM   3887 N  N   . VAL B 1 183 ? -59.950  32.588 30.513  1.00 71.41  ? 183 VAL B N   1 
ATOM   3888 C  CA  . VAL B 1 183 ? -59.524  31.294 31.035  1.00 75.30  ? 183 VAL B CA  1 
ATOM   3889 C  C   . VAL B 1 183 ? -58.297  30.799 30.282  1.00 73.95  ? 183 VAL B C   1 
ATOM   3890 O  O   . VAL B 1 183 ? -57.362  30.251 30.879  1.00 80.24  ? 183 VAL B O   1 
ATOM   3891 C  CB  . VAL B 1 183 ? -60.684  30.281 30.962  1.00 76.27  ? 183 VAL B CB  1 
ATOM   3892 C  CG1 . VAL B 1 183 ? -60.223  28.903 31.409  1.00 73.51  ? 183 VAL B CG1 1 
ATOM   3893 C  CG2 . VAL B 1 183 ? -61.857  30.755 31.805  1.00 62.70  ? 183 VAL B CG2 1 
ATOM   3894 N  N   . ASP B 1 184 ? -58.276  30.995 28.960  1.00 75.51  ? 184 ASP B N   1 
ATOM   3895 C  CA  . ASP B 1 184 ? -57.114  30.600 28.169  1.00 81.02  ? 184 ASP B CA  1 
ATOM   3896 C  C   . ASP B 1 184 ? -55.846  31.277 28.672  1.00 82.68  ? 184 ASP B C   1 
ATOM   3897 O  O   . ASP B 1 184 ? -54.779  30.655 28.719  1.00 86.92  ? 184 ASP B O   1 
ATOM   3898 C  CB  . ASP B 1 184 ? -57.341  30.931 26.693  1.00 74.78  ? 184 ASP B CB  1 
ATOM   3899 C  CG  . ASP B 1 184 ? -58.442  30.101 26.072  1.00 75.06  ? 184 ASP B CG  1 
ATOM   3900 O  OD1 . ASP B 1 184 ? -58.759  29.021 26.615  1.00 78.28  ? 184 ASP B OD1 1 
ATOM   3901 O  OD2 . ASP B 1 184 ? -58.989  30.530 25.034  1.00 77.66  ? 184 ASP B OD2 1 
ATOM   3902 N  N   . LEU B 1 185 ? -55.941  32.551 29.059  1.00 79.51  ? 185 LEU B N   1 
ATOM   3903 C  CA  . LEU B 1 185 ? -54.756  33.244 29.548  1.00 82.34  ? 185 LEU B CA  1 
ATOM   3904 C  C   . LEU B 1 185 ? -54.289  32.679 30.882  1.00 84.23  ? 185 LEU B C   1 
ATOM   3905 O  O   . LEU B 1 185 ? -53.087  32.697 31.173  1.00 83.55  ? 185 LEU B O   1 
ATOM   3906 C  CB  . LEU B 1 185 ? -55.025  34.742 29.673  1.00 80.10  ? 185 LEU B CB  1 
ATOM   3907 C  CG  . LEU B 1 185 ? -53.739  35.564 29.569  1.00 83.65  ? 185 LEU B CG  1 
ATOM   3908 C  CD1 . LEU B 1 185 ? -53.180  35.486 28.156  1.00 84.12  ? 185 LEU B CD1 1 
ATOM   3909 C  CD2 . LEU B 1 185 ? -53.956  37.004 29.986  1.00 85.40  ? 185 LEU B CD2 1 
ATOM   3910 N  N   . ALA B 1 186 ? -55.214  32.171 31.700  1.00 82.13  ? 186 ALA B N   1 
ATOM   3911 C  CA  . ALA B 1 186 ? -54.821  31.558 32.964  1.00 87.43  ? 186 ALA B CA  1 
ATOM   3912 C  C   . ALA B 1 186 ? -53.897  30.368 32.745  1.00 90.41  ? 186 ALA B C   1 
ATOM   3913 O  O   . ALA B 1 186 ? -53.040  30.084 33.590  1.00 87.15  ? 186 ALA B O   1 
ATOM   3914 C  CB  . ALA B 1 186 ? -56.060  31.137 33.753  1.00 86.86  ? 186 ALA B CB  1 
ATOM   3915 N  N   . GLU B 1 187 ? -54.055  29.660 31.624  1.00 88.84  ? 187 GLU B N   1 
ATOM   3916 C  CA  . GLU B 1 187 ? -53.101  28.616 31.267  1.00 90.40  ? 187 GLU B CA  1 
ATOM   3917 C  C   . GLU B 1 187 ? -51.733  29.213 30.958  1.00 92.61  ? 187 GLU B C   1 
ATOM   3918 O  O   . GLU B 1 187 ? -50.710  28.753 31.479  1.00 95.01  ? 187 GLU B O   1 
ATOM   3919 C  CB  . GLU B 1 187 ? -53.625  27.809 30.077  1.00 87.12  ? 187 GLU B CB  1 
ATOM   3920 C  CG  . GLU B 1 187 ? -54.629  26.725 30.449  1.00 87.20  ? 187 GLU B CG  1 
ATOM   3921 C  CD  . GLU B 1 187 ? -55.247  26.051 29.236  1.00 90.98  ? 187 GLU B CD  1 
ATOM   3922 O  OE1 . GLU B 1 187 ? -56.068  26.696 28.547  1.00 92.27  ? 187 GLU B OE1 1 
ATOM   3923 O  OE2 . GLU B 1 187 ? -54.909  24.877 28.969  1.00 89.24  ? 187 GLU B OE2 1 
ATOM   3924 N  N   . ARG B 1 188 ? -51.700  30.251 30.118  1.00 91.19  ? 188 ARG B N   1 
ATOM   3925 C  CA  . ARG B 1 188 ? -50.438  30.905 29.783  1.00 90.47  ? 188 ARG B CA  1 
ATOM   3926 C  C   . ARG B 1 188 ? -49.787  31.524 31.015  1.00 90.35  ? 188 ARG B C   1 
ATOM   3927 O  O   . ARG B 1 188 ? -48.558  31.495 31.156  1.00 92.04  ? 188 ARG B O   1 
ATOM   3928 C  CB  . ARG B 1 188 ? -50.677  31.964 28.703  1.00 89.89  ? 188 ARG B CB  1 
ATOM   3929 C  CG  . ARG B 1 188 ? -49.595  33.033 28.583  1.00 88.04  ? 188 ARG B CG  1 
ATOM   3930 C  CD  . ARG B 1 188 ? -48.272  32.460 28.102  1.00 88.30  ? 188 ARG B CD  1 
ATOM   3931 N  NE  . ARG B 1 188 ? -47.273  33.500 27.893  1.00 90.14  ? 188 ARG B NE  1 
ATOM   3932 C  CZ  . ARG B 1 188 ? -46.549  34.052 28.858  1.00 95.47  ? 188 ARG B CZ  1 
ATOM   3933 N  NH1 . ARG B 1 188 ? -46.696  33.696 30.124  1.00 88.98  ? 188 ARG B NH1 1 
ATOM   3934 N  NH2 . ARG B 1 188 ? -45.657  34.988 28.545  1.00 96.81  ? 188 ARG B NH2 1 
ATOM   3935 N  N   . ALA B 1 189 ? -50.594  32.079 31.922  1.00 86.94  ? 189 ALA B N   1 
ATOM   3936 C  CA  . ALA B 1 189 ? -50.041  32.749 33.096  1.00 88.87  ? 189 ALA B CA  1 
ATOM   3937 C  C   . ALA B 1 189 ? -49.350  31.762 34.031  1.00 95.24  ? 189 ALA B C   1 
ATOM   3938 O  O   . ALA B 1 189 ? -48.327  32.091 34.644  1.00 96.21  ? 189 ALA B O   1 
ATOM   3939 C  CB  . ALA B 1 189 ? -51.144  33.508 33.834  1.00 89.09  ? 189 ALA B CB  1 
ATOM   3940 N  N   . GLY B 1 190 ? -49.893  30.555 34.157  1.00 95.81  ? 190 GLY B N   1 
ATOM   3941 C  CA  . GLY B 1 190 ? -49.302  29.520 34.975  1.00 94.34  ? 190 GLY B CA  1 
ATOM   3942 C  C   . GLY B 1 190 ? -48.363  28.585 34.253  1.00 97.09  ? 190 GLY B C   1 
ATOM   3943 O  O   . GLY B 1 190 ? -47.816  27.671 34.878  1.00 100.07 ? 190 GLY B O   1 
ATOM   3944 N  N   . ARG B 1 191 ? -48.167  28.784 32.947  1.00 99.90  ? 191 ARG B N   1 
ATOM   3945 C  CA  . ARG B 1 191 ? -47.250  27.974 32.142  1.00 100.54 ? 191 ARG B CA  1 
ATOM   3946 C  C   . ARG B 1 191 ? -47.618  26.492 32.191  1.00 100.97 ? 191 ARG B C   1 
ATOM   3947 O  O   . ARG B 1 191 ? -46.752  25.619 32.272  1.00 104.03 ? 191 ARG B O   1 
ATOM   3948 C  CB  . ARG B 1 191 ? -45.797  28.191 32.575  1.00 101.38 ? 191 ARG B CB  1 
ATOM   3949 C  CG  . ARG B 1 191 ? -45.308  29.619 32.389  1.00 98.54  ? 191 ARG B CG  1 
ATOM   3950 C  CD  . ARG B 1 191 ? -45.102  29.949 30.919  1.00 101.97 ? 191 ARG B CD  1 
ATOM   3951 N  NE  . ARG B 1 191 ? -44.893  31.377 30.708  1.00 107.24 ? 191 ARG B NE  1 
ATOM   3952 C  CZ  . ARG B 1 191 ? -43.740  32.004 30.898  1.00 107.24 ? 191 ARG B CZ  1 
ATOM   3953 N  NH1 . ARG B 1 191 ? -42.662  31.358 31.312  1.00 110.42 ? 191 ARG B NH1 1 
ATOM   3954 N  NH2 . ARG B 1 191 ? -43.668  33.313 30.672  1.00 105.59 ? 191 ARG B NH2 1 
ATOM   3955 N  N   . PHE B 1 192 ? -48.917  26.206 32.144  1.00 97.36  ? 192 PHE B N   1 
ATOM   3956 C  CA  . PHE B 1 192 ? -49.416  24.844 32.049  1.00 95.22  ? 192 PHE B CA  1 
ATOM   3957 C  C   . PHE B 1 192 ? -50.467  24.773 30.950  1.00 95.37  ? 192 PHE B C   1 
ATOM   3958 O  O   . PHE B 1 192 ? -50.950  25.792 30.449  1.00 98.61  ? 192 PHE B O   1 
ATOM   3959 C  CB  . PHE B 1 192 ? -49.999  24.352 33.385  1.00 92.78  ? 192 PHE B CB  1 
ATOM   3960 C  CG  . PHE B 1 192 ? -51.262  25.057 33.804  1.00 95.41  ? 192 PHE B CG  1 
ATOM   3961 C  CD1 . PHE B 1 192 ? -51.207  26.197 34.591  1.00 95.14  ? 192 PHE B CD1 1 
ATOM   3962 C  CD2 . PHE B 1 192 ? -52.506  24.569 33.428  1.00 92.43  ? 192 PHE B CD2 1 
ATOM   3963 C  CE1 . PHE B 1 192 ? -52.367  26.844 34.986  1.00 95.10  ? 192 PHE B CE1 1 
ATOM   3964 C  CE2 . PHE B 1 192 ? -53.669  25.211 33.815  1.00 92.17  ? 192 PHE B CE2 1 
ATOM   3965 C  CZ  . PHE B 1 192 ? -53.599  26.349 34.597  1.00 94.72  ? 192 PHE B CZ  1 
ATOM   3966 N  N   . GLU B 1 193 ? -50.815  23.547 30.569  1.00 89.78  ? 193 GLU B N   1 
ATOM   3967 C  CA  . GLU B 1 193 ? -51.877  23.309 29.600  1.00 91.24  ? 193 GLU B CA  1 
ATOM   3968 C  C   . GLU B 1 193 ? -52.694  22.119 30.074  1.00 92.68  ? 193 GLU B C   1 
ATOM   3969 O  O   . GLU B 1 193 ? -52.157  21.017 30.216  1.00 97.26  ? 193 GLU B O   1 
ATOM   3970 C  CB  . GLU B 1 193 ? -51.315  23.057 28.196  1.00 86.07  ? 193 GLU B CB  1 
ATOM   3971 C  CG  . GLU B 1 193 ? -50.584  24.250 27.594  1.00 88.40  ? 193 GLU B CG  1 
ATOM   3972 C  CD  . GLU B 1 193 ? -50.155  24.020 26.156  1.00 89.20  ? 193 GLU B CD  1 
ATOM   3973 O  OE1 . GLU B 1 193 ? -50.700  23.105 25.499  1.00 81.81  ? 193 GLU B OE1 1 
ATOM   3974 O  OE2 . GLU B 1 193 ? -49.268  24.759 25.682  1.00 89.93  ? 193 GLU B OE2 1 
ATOM   3975 N  N   . VAL B 1 194 ? -53.978  22.352 30.339  1.00 91.06  ? 194 VAL B N   1 
ATOM   3976 C  CA  . VAL B 1 194 ? -54.873  21.246 30.694  1.00 91.10  ? 194 VAL B CA  1 
ATOM   3977 C  C   . VAL B 1 194 ? -54.858  20.224 29.563  1.00 90.18  ? 194 VAL B C   1 
ATOM   3978 O  O   . VAL B 1 194 ? -54.728  20.615 28.383  1.00 90.60  ? 194 VAL B O   1 
ATOM   3979 C  CB  . VAL B 1 194 ? -56.297  21.771 30.961  1.00 87.18  ? 194 VAL B CB  1 
ATOM   3980 C  CG1 . VAL B 1 194 ? -56.926  22.334 29.688  1.00 87.77  ? 194 VAL B CG1 1 
ATOM   3981 C  CG2 . VAL B 1 194 ? -57.182  20.698 31.580  1.00 84.69  ? 194 VAL B CG2 1 
ATOM   3982 N  N   . PRO B 1 195 ? -54.912  18.922 29.849  1.00 90.37  ? 195 PRO B N   1 
ATOM   3983 C  CA  . PRO B 1 195 ? -54.944  17.925 28.770  1.00 88.16  ? 195 PRO B CA  1 
ATOM   3984 C  C   . PRO B 1 195 ? -56.016  18.245 27.740  1.00 88.77  ? 195 PRO B C   1 
ATOM   3985 O  O   . PRO B 1 195 ? -57.175  18.497 28.079  1.00 93.74  ? 195 PRO B O   1 
ATOM   3986 C  CB  . PRO B 1 195 ? -55.241  16.621 29.513  1.00 87.89  ? 195 PRO B CB  1 
ATOM   3987 C  CG  . PRO B 1 195 ? -54.620  16.825 30.847  1.00 91.73  ? 195 PRO B CG  1 
ATOM   3988 C  CD  . PRO B 1 195 ? -54.739  18.293 31.171  1.00 91.90  ? 195 PRO B CD  1 
ATOM   3989 N  N   . HIS B 1 196 ? -55.613  18.240 26.467  1.00 80.11  ? 196 HIS B N   1 
ATOM   3990 C  CA  . HIS B 1 196 ? -56.484  18.748 25.412  1.00 82.40  ? 196 HIS B CA  1 
ATOM   3991 C  C   . HIS B 1 196 ? -57.713  17.868 25.220  1.00 82.15  ? 196 HIS B C   1 
ATOM   3992 O  O   . HIS B 1 196 ? -58.800  18.373 24.915  1.00 82.37  ? 196 HIS B O   1 
ATOM   3993 C  CB  . HIS B 1 196 ? -55.699  18.880 24.107  1.00 80.77  ? 196 HIS B CB  1 
ATOM   3994 C  CG  . HIS B 1 196 ? -54.652  19.950 24.142  1.00 84.40  ? 196 HIS B CG  1 
ATOM   3995 N  ND1 . HIS B 1 196 ? -54.257  20.642 23.017  1.00 84.88  ? 196 HIS B ND1 1 
ATOM   3996 C  CD2 . HIS B 1 196 ? -53.921  20.450 25.166  1.00 83.97  ? 196 HIS B CD2 1 
ATOM   3997 C  CE1 . HIS B 1 196 ? -53.328  21.521 23.346  1.00 85.16  ? 196 HIS B CE1 1 
ATOM   3998 N  NE2 . HIS B 1 196 ? -53.105  21.425 24.644  1.00 82.69  ? 196 HIS B NE2 1 
ATOM   3999 N  N   . ARG B 1 197 ? -57.571  16.553 25.396  1.00 78.59  ? 197 ARG B N   1 
ATOM   4000 C  CA  . ARG B 1 197 ? -58.734  15.683 25.269  1.00 80.04  ? 197 ARG B CA  1 
ATOM   4001 C  C   . ARG B 1 197 ? -59.736  15.916 26.395  1.00 85.13  ? 197 ARG B C   1 
ATOM   4002 O  O   . ARG B 1 197 ? -60.933  15.662 26.219  1.00 85.61  ? 197 ARG B O   1 
ATOM   4003 C  CB  . ARG B 1 197 ? -58.297  14.218 25.222  1.00 81.71  ? 197 ARG B CB  1 
ATOM   4004 C  CG  . ARG B 1 197 ? -57.444  13.752 26.393  1.00 87.75  ? 197 ARG B CG  1 
ATOM   4005 C  CD  . ARG B 1 197 ? -56.850  12.378 26.100  1.00 91.21  ? 197 ARG B CD  1 
ATOM   4006 N  NE  . ARG B 1 197 ? -56.214  11.770 27.263  1.00 87.05  ? 197 ARG B NE  1 
ATOM   4007 C  CZ  . ARG B 1 197 ? -54.958  11.984 27.632  1.00 86.01  ? 197 ARG B CZ  1 
ATOM   4008 N  NH1 . ARG B 1 197 ? -54.174  12.817 26.968  1.00 85.24  ? 197 ARG B NH1 1 
ATOM   4009 N  NH2 . ARG B 1 197 ? -54.477  11.346 28.694  1.00 91.68  ? 197 ARG B NH2 1 
ATOM   4010 N  N   . VAL B 1 198 ? -59.273  16.407 27.546  1.00 82.61  ? 198 VAL B N   1 
ATOM   4011 C  CA  . VAL B 1 198 ? -60.182  16.715 28.647  1.00 88.54  ? 198 VAL B CA  1 
ATOM   4012 C  C   . VAL B 1 198 ? -60.894  18.044 28.410  1.00 87.01  ? 198 VAL B C   1 
ATOM   4013 O  O   . VAL B 1 198 ? -62.076  18.193 28.739  1.00 86.72  ? 198 VAL B O   1 
ATOM   4014 C  CB  . VAL B 1 198 ? -59.416  16.706 29.984  1.00 87.69  ? 198 VAL B CB  1 
ATOM   4015 C  CG1 . VAL B 1 198 ? -60.248  17.342 31.085  1.00 76.93  ? 198 VAL B CG1 1 
ATOM   4016 C  CG2 . VAL B 1 198 ? -59.037  15.283 30.364  1.00 88.77  ? 198 VAL B CG2 1 
ATOM   4017 N  N   . PHE B 1 199 ? -60.192  19.024 27.832  1.00 86.78  ? 199 PHE B N   1 
ATOM   4018 C  CA  . PHE B 1 199 ? -60.811  20.314 27.535  1.00 84.43  ? 199 PHE B CA  1 
ATOM   4019 C  C   . PHE B 1 199 ? -62.035  20.149 26.639  1.00 83.07  ? 199 PHE B C   1 
ATOM   4020 O  O   . PHE B 1 199 ? -63.039  20.850 26.811  1.00 81.52  ? 199 PHE B O   1 
ATOM   4021 C  CB  . PHE B 1 199 ? -59.782  21.244 26.886  1.00 82.77  ? 199 PHE B CB  1 
ATOM   4022 C  CG  . PHE B 1 199 ? -60.303  22.624 26.582  1.00 84.24  ? 199 PHE B CG  1 
ATOM   4023 C  CD1 . PHE B 1 199 ? -60.976  22.885 25.397  1.00 83.37  ? 199 PHE B CD1 1 
ATOM   4024 C  CD2 . PHE B 1 199 ? -60.101  23.665 27.472  1.00 82.42  ? 199 PHE B CD2 1 
ATOM   4025 C  CE1 . PHE B 1 199 ? -61.452  24.151 25.116  1.00 77.97  ? 199 PHE B CE1 1 
ATOM   4026 C  CE2 . PHE B 1 199 ? -60.572  24.934 27.192  1.00 82.65  ? 199 PHE B CE2 1 
ATOM   4027 C  CZ  . PHE B 1 199 ? -61.248  25.177 26.015  1.00 76.74  ? 199 PHE B CZ  1 
ATOM   4028 N  N   . ASP B 1 200 ? -61.972  19.225 25.682  1.00 80.82  ? 200 ASP B N   1 
ATOM   4029 C  CA  . ASP B 1 200 ? -63.076  18.969 24.767  1.00 85.70  ? 200 ASP B CA  1 
ATOM   4030 C  C   . ASP B 1 200 ? -64.096  17.985 25.324  1.00 83.07  ? 200 ASP B C   1 
ATOM   4031 O  O   . ASP B 1 200 ? -65.061  17.656 24.625  1.00 90.90  ? 200 ASP B O   1 
ATOM   4032 C  CB  . ASP B 1 200 ? -62.544  18.444 23.428  1.00 86.88  ? 200 ASP B CB  1 
ATOM   4033 C  CG  . ASP B 1 200 ? -61.619  19.428 22.739  1.00 89.83  ? 200 ASP B CG  1 
ATOM   4034 O  OD1 . ASP B 1 200 ? -61.547  20.594 23.183  1.00 91.63  ? 200 ASP B OD1 1 
ATOM   4035 O  OD2 . ASP B 1 200 ? -60.959  19.033 21.756  1.00 93.98  ? 200 ASP B OD2 1 
ATOM   4036 N  N   . SER B 1 201 ? -63.909  17.502 26.549  1.00 75.46  ? 201 SER B N   1 
ATOM   4037 C  CA  . SER B 1 201 ? -64.845  16.545 27.115  1.00 77.99  ? 201 SER B CA  1 
ATOM   4038 C  C   . SER B 1 201 ? -66.158  17.232 27.477  1.00 76.70  ? 201 SER B C   1 
ATOM   4039 O  O   . SER B 1 201 ? -66.240  18.456 27.598  1.00 81.38  ? 201 SER B O   1 
ATOM   4040 C  CB  . SER B 1 201 ? -64.248  15.869 28.349  1.00 81.85  ? 201 SER B CB  1 
ATOM   4041 O  OG  . SER B 1 201 ? -64.082  16.792 29.413  1.00 82.71  ? 201 SER B OG  1 
ATOM   4042 N  N   . ALA B 1 202 ? -67.199  16.417 27.654  1.00 70.37  ? 202 ALA B N   1 
ATOM   4043 C  CA  . ALA B 1 202 ? -68.513  16.965 27.971  1.00 72.74  ? 202 ALA B CA  1 
ATOM   4044 C  C   . ALA B 1 202 ? -68.538  17.584 29.364  1.00 77.21  ? 202 ALA B C   1 
ATOM   4045 O  O   . ALA B 1 202 ? -69.209  18.599 29.585  1.00 77.03  ? 202 ALA B O   1 
ATOM   4046 C  CB  . ALA B 1 202 ? -69.576  15.877 27.848  1.00 68.16  ? 202 ALA B CB  1 
ATOM   4047 N  N   . VAL B 1 203 ? -67.813  16.992 30.314  1.00 76.05  ? 203 VAL B N   1 
ATOM   4048 C  CA  . VAL B 1 203 ? -67.833  17.498 31.683  1.00 75.90  ? 203 VAL B CA  1 
ATOM   4049 C  C   . VAL B 1 203 ? -67.099  18.832 31.772  1.00 74.73  ? 203 VAL B C   1 
ATOM   4050 O  O   . VAL B 1 203 ? -67.598  19.795 32.365  1.00 71.39  ? 203 VAL B O   1 
ATOM   4051 C  CB  . VAL B 1 203 ? -67.243  16.458 32.652  1.00 73.38  ? 203 VAL B CB  1 
ATOM   4052 C  CG1 . VAL B 1 203 ? -67.028  17.073 34.026  1.00 67.81  ? 203 VAL B CG1 1 
ATOM   4053 C  CG2 . VAL B 1 203 ? -68.162  15.250 32.749  1.00 67.48  ? 203 VAL B CG2 1 
ATOM   4054 N  N   . MET B 1 204 ? -65.903  18.911 31.184  1.00 74.17  ? 204 MET B N   1 
ATOM   4055 C  CA  . MET B 1 204 ? -65.168  20.171 31.220  1.00 77.11  ? 204 MET B CA  1 
ATOM   4056 C  C   . MET B 1 204 ? -65.871  21.246 30.401  1.00 78.32  ? 204 MET B C   1 
ATOM   4057 O  O   . MET B 1 204 ? -65.753  22.437 30.714  1.00 77.53  ? 204 MET B O   1 
ATOM   4058 C  CB  . MET B 1 204 ? -63.736  19.965 30.728  1.00 77.27  ? 204 MET B CB  1 
ATOM   4059 C  CG  . MET B 1 204 ? -62.862  21.209 30.808  1.00 77.81  ? 204 MET B CG  1 
ATOM   4060 S  SD  . MET B 1 204 ? -62.809  21.931 32.462  1.00 85.32  ? 204 MET B SD  1 
ATOM   4061 C  CE  . MET B 1 204 ? -61.916  20.668 33.361  1.00 88.60  ? 204 MET B CE  1 
ATOM   4062 N  N   . SER B 1 205 ? -66.608  20.850 29.360  1.00 71.98  ? 205 SER B N   1 
ATOM   4063 C  CA  . SER B 1 205 ? -67.416  21.815 28.620  1.00 71.40  ? 205 SER B CA  1 
ATOM   4064 C  C   . SER B 1 205 ? -68.500  22.406 29.510  1.00 74.51  ? 205 SER B C   1 
ATOM   4065 O  O   . SER B 1 205 ? -68.701  23.625 29.538  1.00 75.88  ? 205 SER B O   1 
ATOM   4066 C  CB  . SER B 1 205 ? -68.035  21.155 27.386  1.00 73.63  ? 205 SER B CB  1 
ATOM   4067 O  OG  . SER B 1 205 ? -67.056  20.892 26.397  1.00 72.23  ? 205 SER B OG  1 
ATOM   4068 N  N   . ALA B 1 206 ? -69.206  21.551 30.254  1.00 70.56  ? 206 ALA B N   1 
ATOM   4069 C  CA  . ALA B 1 206 ? -70.273  22.034 31.124  1.00 70.63  ? 206 ALA B CA  1 
ATOM   4070 C  C   . ALA B 1 206 ? -69.735  22.924 32.238  1.00 72.55  ? 206 ALA B C   1 
ATOM   4071 O  O   . ALA B 1 206 ? -70.429  23.846 32.683  1.00 72.87  ? 206 ALA B O   1 
ATOM   4072 C  CB  . ALA B 1 206 ? -71.046  20.853 31.710  1.00 67.39  ? 206 ALA B CB  1 
ATOM   4073 N  N   . MET B 1 207 ? -68.509  22.666 32.702  1.00 72.92  ? 207 MET B N   1 
ATOM   4074 C  CA  . MET B 1 207 ? -67.911  23.521 33.724  1.00 70.83  ? 207 MET B CA  1 
ATOM   4075 C  C   . MET B 1 207 ? -67.548  24.886 33.157  1.00 73.52  ? 207 MET B C   1 
ATOM   4076 O  O   . MET B 1 207 ? -67.806  25.916 33.790  1.00 63.67  ? 207 MET B O   1 
ATOM   4077 C  CB  . MET B 1 207 ? -66.678  22.845 34.320  1.00 68.84  ? 207 MET B CB  1 
ATOM   4078 C  CG  . MET B 1 207 ? -66.985  21.630 35.174  1.00 75.92  ? 207 MET B CG  1 
ATOM   4079 S  SD  . MET B 1 207 ? -65.505  20.672 35.541  1.00 82.16  ? 207 MET B SD  1 
ATOM   4080 C  CE  . MET B 1 207 ? -64.451  21.936 36.246  1.00 75.86  ? 207 MET B CE  1 
ATOM   4081 N  N   . LEU B 1 208 ? -66.943  24.912 31.966  1.00 71.82  ? 208 LEU B N   1 
ATOM   4082 C  CA  . LEU B 1 208 ? -66.618  26.184 31.330  1.00 70.58  ? 208 LEU B CA  1 
ATOM   4083 C  C   . LEU B 1 208 ? -67.883  26.946 30.955  1.00 69.08  ? 208 LEU B C   1 
ATOM   4084 O  O   . LEU B 1 208 ? -67.917  28.181 31.022  1.00 70.20  ? 208 LEU B O   1 
ATOM   4085 C  CB  . LEU B 1 208 ? -65.740  25.947 30.102  1.00 67.92  ? 208 LEU B CB  1 
ATOM   4086 C  CG  . LEU B 1 208 ? -64.332  25.431 30.407  1.00 77.55  ? 208 LEU B CG  1 
ATOM   4087 C  CD1 . LEU B 1 208 ? -63.626  25.000 29.134  1.00 69.10  ? 208 LEU B CD1 1 
ATOM   4088 C  CD2 . LEU B 1 208 ? -63.522  26.491 31.142  1.00 70.40  ? 208 LEU B CD2 1 
ATOM   4089 N  N   . GLN B 1 209 ? -68.938  26.226 30.567  1.00 65.86  ? 209 GLN B N   1 
ATOM   4090 C  CA  . GLN B 1 209 ? -70.208  26.881 30.274  1.00 63.61  ? 209 GLN B CA  1 
ATOM   4091 C  C   . GLN B 1 209 ? -70.769  27.565 31.515  1.00 69.43  ? 209 GLN B C   1 
ATOM   4092 O  O   . GLN B 1 209 ? -71.329  28.664 31.428  1.00 65.40  ? 209 GLN B O   1 
ATOM   4093 C  CB  . GLN B 1 209 ? -71.204  25.863 29.719  1.00 62.02  ? 209 GLN B CB  1 
ATOM   4094 C  CG  . GLN B 1 209 ? -72.561  26.452 29.375  1.00 71.99  ? 209 GLN B CG  1 
ATOM   4095 C  CD  . GLN B 1 209 ? -73.611  25.392 29.095  1.00 74.60  ? 209 GLN B CD  1 
ATOM   4096 O  OE1 . GLN B 1 209 ? -73.985  25.168 27.944  1.00 81.02  ? 209 GLN B OE1 1 
ATOM   4097 N  NE2 . GLN B 1 209 ? -74.099  24.740 30.149  1.00 67.95  ? 209 GLN B NE2 1 
ATOM   4098 N  N   . ILE B 1 210 ? -70.623  26.931 32.682  1.00 68.22  ? 210 ILE B N   1 
ATOM   4099 C  CA  . ILE B 1 210 ? -71.070  27.549 33.928  1.00 64.11  ? 210 ILE B CA  1 
ATOM   4100 C  C   . ILE B 1 210 ? -70.255  28.801 34.221  1.00 64.01  ? 210 ILE B C   1 
ATOM   4101 O  O   . ILE B 1 210 ? -70.805  29.842 34.602  1.00 65.37  ? 210 ILE B O   1 
ATOM   4102 C  CB  . ILE B 1 210 ? -70.992  26.539 35.088  1.00 68.93  ? 210 ILE B CB  1 
ATOM   4103 C  CG1 . ILE B 1 210 ? -72.130  25.524 34.990  1.00 65.88  ? 210 ILE B CG1 1 
ATOM   4104 C  CG2 . ILE B 1 210 ? -71.016  27.256 36.435  1.00 71.87  ? 210 ILE B CG2 1 
ATOM   4105 C  CD1 . ILE B 1 210 ? -72.035  24.410 36.001  1.00 68.90  ? 210 ILE B CD1 1 
ATOM   4106 N  N   . ALA B 1 211 ? -68.934  28.722 34.040  1.00 63.17  ? 211 ALA B N   1 
ATOM   4107 C  CA  . ALA B 1 211 ? -68.074  29.879 34.272  1.00 63.81  ? 211 ALA B CA  1 
ATOM   4108 C  C   . ALA B 1 211 ? -68.453  31.037 33.360  1.00 67.10  ? 211 ALA B C   1 
ATOM   4109 O  O   . ALA B 1 211 ? -68.554  32.186 33.806  1.00 65.73  ? 211 ALA B O   1 
ATOM   4110 C  CB  . ALA B 1 211 ? -66.609  29.492 34.070  1.00 67.35  ? 211 ALA B CB  1 
ATOM   4111 N  N   . VAL B 1 212 ? -68.666  30.752 32.072  1.00 67.57  ? 212 VAL B N   1 
ATOM   4112 C  CA  . VAL B 1 212 ? -69.107  31.782 31.134  1.00 64.30  ? 212 VAL B CA  1 
ATOM   4113 C  C   . VAL B 1 212 ? -70.442  32.370 31.577  1.00 65.36  ? 212 VAL B C   1 
ATOM   4114 O  O   . VAL B 1 212 ? -70.617  33.593 31.631  1.00 65.57  ? 212 VAL B O   1 
ATOM   4115 C  CB  . VAL B 1 212 ? -69.193  31.204 29.710  1.00 67.08  ? 212 VAL B CB  1 
ATOM   4116 C  CG1 . VAL B 1 212 ? -69.955  32.150 28.797  1.00 68.18  ? 212 VAL B CG1 1 
ATOM   4117 C  CG2 . VAL B 1 212 ? -67.803  30.932 29.163  1.00 63.45  ? 212 VAL B CG2 1 
ATOM   4118 N  N   . ASP B 1 213 ? -71.400  31.503 31.913  1.00 65.37  ? 213 ASP B N   1 
ATOM   4119 C  CA  . ASP B 1 213 ? -72.750  31.967 32.224  1.00 65.50  ? 213 ASP B CA  1 
ATOM   4120 C  C   . ASP B 1 213 ? -72.782  32.802 33.498  1.00 70.47  ? 213 ASP B C   1 
ATOM   4121 O  O   . ASP B 1 213 ? -73.501  33.806 33.567  1.00 73.41  ? 213 ASP B O   1 
ATOM   4122 C  CB  . ASP B 1 213 ? -73.697  30.774 32.342  1.00 67.28  ? 213 ASP B CB  1 
ATOM   4123 C  CG  . ASP B 1 213 ? -74.044  30.168 30.994  1.00 78.06  ? 213 ASP B CG  1 
ATOM   4124 O  OD1 . ASP B 1 213 ? -73.718  30.786 29.956  1.00 80.78  ? 213 ASP B OD1 1 
ATOM   4125 O  OD2 . ASP B 1 213 ? -74.644  29.072 30.973  1.00 77.18  ? 213 ASP B OD2 1 
ATOM   4126 N  N   . VAL B 1 214 ? -72.019  32.408 34.518  1.00 67.97  ? 214 VAL B N   1 
ATOM   4127 C  CA  . VAL B 1 214 ? -72.036  33.152 35.775  1.00 71.30  ? 214 VAL B CA  1 
ATOM   4128 C  C   . VAL B 1 214 ? -71.462  34.550 35.578  1.00 67.30  ? 214 VAL B C   1 
ATOM   4129 O  O   . VAL B 1 214 ? -72.011  35.535 36.086  1.00 67.40  ? 214 VAL B O   1 
ATOM   4130 C  CB  . VAL B 1 214 ? -71.289  32.369 36.870  1.00 67.32  ? 214 VAL B CB  1 
ATOM   4131 C  CG1 . VAL B 1 214 ? -70.925  33.278 38.041  1.00 60.53  ? 214 VAL B CG1 1 
ATOM   4132 C  CG2 . VAL B 1 214 ? -72.148  31.216 37.344  1.00 66.33  ? 214 VAL B CG2 1 
ATOM   4133 N  N   . ASN B 1 215 ? -70.361  34.662 34.831  1.00 63.91  ? 215 ASN B N   1 
ATOM   4134 C  CA  . ASN B 1 215 ? -69.769  35.972 34.574  1.00 70.72  ? 215 ASN B CA  1 
ATOM   4135 C  C   . ASN B 1 215 ? -70.745  36.896 33.854  1.00 73.28  ? 215 ASN B C   1 
ATOM   4136 O  O   . ASN B 1 215 ? -70.868  38.075 34.208  1.00 70.06  ? 215 ASN B O   1 
ATOM   4137 C  CB  . ASN B 1 215 ? -68.490  35.822 33.756  1.00 71.86  ? 215 ASN B CB  1 
ATOM   4138 C  CG  . ASN B 1 215 ? -67.325  35.325 34.577  1.00 72.72  ? 215 ASN B CG  1 
ATOM   4139 O  OD1 . ASN B 1 215 ? -66.464  36.103 34.980  1.00 77.45  ? 215 ASN B OD1 1 
ATOM   4140 N  ND2 . ASN B 1 215 ? -67.283  34.021 34.823  1.00 73.94  ? 215 ASN B ND2 1 
ATOM   4141 N  N   . LEU B 1 216 ? -71.446  36.385 32.838  1.00 68.40  ? 216 LEU B N   1 
ATOM   4142 C  CA  . LEU B 1 216 ? -72.369  37.241 32.102  1.00 73.27  ? 216 LEU B CA  1 
ATOM   4143 C  C   . LEU B 1 216 ? -73.627  37.538 32.912  1.00 73.46  ? 216 LEU B C   1 
ATOM   4144 O  O   . LEU B 1 216 ? -74.203  38.623 32.774  1.00 78.98  ? 216 LEU B O   1 
ATOM   4145 C  CB  . LEU B 1 216 ? -72.716  36.617 30.746  1.00 73.75  ? 216 LEU B CB  1 
ATOM   4146 C  CG  . LEU B 1 216 ? -73.645  35.408 30.613  1.00 71.02  ? 216 LEU B CG  1 
ATOM   4147 C  CD1 . LEU B 1 216 ? -75.101  35.840 30.492  1.00 68.54  ? 216 LEU B CD1 1 
ATOM   4148 C  CD2 . LEU B 1 216 ? -73.237  34.567 29.413  1.00 70.14  ? 216 LEU B CD2 1 
ATOM   4149 N  N   . LEU B 1 217 ? -74.068  36.600 33.757  1.00 70.14  ? 217 LEU B N   1 
ATOM   4150 C  CA  . LEU B 1 217 ? -75.180  36.893 34.657  1.00 72.09  ? 217 LEU B CA  1 
ATOM   4151 C  C   . LEU B 1 217 ? -74.810  37.999 35.639  1.00 75.25  ? 217 LEU B C   1 
ATOM   4152 O  O   . LEU B 1 217 ? -75.602  38.919 35.879  1.00 73.84  ? 217 LEU B O   1 
ATOM   4153 C  CB  . LEU B 1 217 ? -75.607  35.632 35.411  1.00 68.64  ? 217 LEU B CB  1 
ATOM   4154 C  CG  . LEU B 1 217 ? -76.353  34.526 34.657  1.00 72.14  ? 217 LEU B CG  1 
ATOM   4155 C  CD1 . LEU B 1 217 ? -76.837  33.461 35.634  1.00 70.39  ? 217 LEU B CD1 1 
ATOM   4156 C  CD2 . LEU B 1 217 ? -77.513  35.082 33.845  1.00 66.86  ? 217 LEU B CD2 1 
ATOM   4157 N  N   . LEU B 1 218 ? -73.607  37.927 36.215  1.00 72.94  ? 218 LEU B N   1 
ATOM   4158 C  CA  . LEU B 1 218 ? -73.160  38.970 37.134  1.00 71.62  ? 218 LEU B CA  1 
ATOM   4159 C  C   . LEU B 1 218 ? -72.963  40.296 36.410  1.00 70.46  ? 218 LEU B C   1 
ATOM   4160 O  O   . LEU B 1 218 ? -73.296  41.359 36.947  1.00 66.89  ? 218 LEU B O   1 
ATOM   4161 C  CB  . LEU B 1 218 ? -71.865  38.542 37.825  1.00 73.43  ? 218 LEU B CB  1 
ATOM   4162 C  CG  . LEU B 1 218 ? -71.906  37.280 38.690  1.00 78.49  ? 218 LEU B CG  1 
ATOM   4163 C  CD1 . LEU B 1 218 ? -70.535  36.989 39.289  1.00 73.61  ? 218 LEU B CD1 1 
ATOM   4164 C  CD2 . LEU B 1 218 ? -72.958  37.401 39.777  1.00 72.41  ? 218 LEU B CD2 1 
ATOM   4165 N  N   . ASN B 1 219 ? -72.429  40.253 35.188  1.00 75.22  ? 219 ASN B N   1 
ATOM   4166 C  CA  . ASN B 1 219 ? -72.143  41.487 34.464  1.00 75.19  ? 219 ASN B CA  1 
ATOM   4167 C  C   . ASN B 1 219 ? -73.424  42.193 34.035  1.00 74.31  ? 219 ASN B C   1 
ATOM   4168 O  O   . ASN B 1 219 ? -73.483  43.429 34.023  1.00 71.31  ? 219 ASN B O   1 
ATOM   4169 C  CB  . ASN B 1 219 ? -71.260  41.193 33.252  1.00 70.03  ? 219 ASN B CB  1 
ATOM   4170 C  CG  . ASN B 1 219 ? -70.863  42.450 32.504  1.00 80.16  ? 219 ASN B CG  1 
ATOM   4171 O  OD1 . ASN B 1 219 ? -71.435  42.775 31.462  1.00 82.68  ? 219 ASN B OD1 1 
ATOM   4172 N  ND2 . ASN B 1 219 ? -69.883  43.170 33.039  1.00 78.09  ? 219 ASN B ND2 1 
ATOM   4173 N  N   . ASP B 1 220 ? -74.461  41.431 33.680  1.00 70.93  ? 220 ASP B N   1 
ATOM   4174 C  CA  . ASP B 1 220 ? -75.700  42.059 33.233  1.00 74.44  ? 220 ASP B CA  1 
ATOM   4175 C  C   . ASP B 1 220 ? -76.465  42.690 34.389  1.00 72.46  ? 220 ASP B C   1 
ATOM   4176 O  O   . ASP B 1 220 ? -77.243  43.626 34.174  1.00 76.46  ? 220 ASP B O   1 
ATOM   4177 C  CB  . ASP B 1 220 ? -76.576  41.044 32.499  1.00 71.56  ? 220 ASP B CB  1 
ATOM   4178 C  CG  . ASP B 1 220 ? -76.234  40.940 31.027  1.00 72.55  ? 220 ASP B CG  1 
ATOM   4179 O  OD1 . ASP B 1 220 ? -75.282  41.620 30.585  1.00 78.00  ? 220 ASP B OD1 1 
ATOM   4180 O  OD2 . ASP B 1 220 ? -76.921  40.185 30.311  1.00 71.98  ? 220 ASP B OD2 1 
ATOM   4181 N  N   . ILE B 1 221 ? -76.269  42.197 35.613  1.00 71.11  ? 221 ILE B N   1 
ATOM   4182 C  CA  . ILE B 1 221 ? -76.844  42.869 36.773  1.00 73.83  ? 221 ILE B CA  1 
ATOM   4183 C  C   . ILE B 1 221 ? -76.014  44.092 37.145  1.00 70.78  ? 221 ILE B C   1 
ATOM   4184 O  O   . ILE B 1 221 ? -76.559  45.140 37.508  1.00 69.17  ? 221 ILE B O   1 
ATOM   4185 C  CB  . ILE B 1 221 ? -76.985  41.879 37.945  1.00 70.62  ? 221 ILE B CB  1 
ATOM   4186 C  CG1 . ILE B 1 221 ? -78.312  41.125 37.827  1.00 64.74  ? 221 ILE B CG1 1 
ATOM   4187 C  CG2 . ILE B 1 221 ? -76.889  42.597 39.280  1.00 63.00  ? 221 ILE B CG2 1 
ATOM   4188 C  CD1 . ILE B 1 221 ? -78.464  39.994 38.793  1.00 64.56  ? 221 ILE B CD1 1 
ATOM   4189 N  N   . ALA B 1 222 ? -74.688  43.990 37.032  1.00 69.41  ? 222 ALA B N   1 
ATOM   4190 C  CA  . ALA B 1 222 ? -73.832  45.145 37.282  1.00 65.67  ? 222 ALA B CA  1 
ATOM   4191 C  C   . ALA B 1 222 ? -74.125  46.281 36.306  1.00 79.65  ? 222 ALA B C   1 
ATOM   4192 O  O   . ALA B 1 222 ? -74.056  47.459 36.678  1.00 75.19  ? 222 ALA B O   1 
ATOM   4193 C  CB  . ALA B 1 222 ? -72.364  44.732 37.197  1.00 71.54  ? 222 ALA B CB  1 
ATOM   4194 N  N   . SER B 1 223 ? -74.456  45.949 35.056  1.00 77.99  ? 223 SER B N   1 
ATOM   4195 C  CA  . SER B 1 223 ? -74.693  46.934 34.006  1.00 74.75  ? 223 SER B CA  1 
ATOM   4196 C  C   . SER B 1 223 ? -76.157  47.347 33.887  1.00 75.05  ? 223 SER B C   1 
ATOM   4197 O  O   . SER B 1 223 ? -76.515  48.033 32.924  1.00 78.22  ? 223 SER B O   1 
ATOM   4198 C  CB  . SER B 1 223 ? -74.217  46.391 32.654  1.00 77.26  ? 223 SER B CB  1 
ATOM   4199 O  OG  . SER B 1 223 ? -72.855  46.005 32.696  1.00 84.85  ? 223 SER B OG  1 
ATOM   4200 N  N   . LEU B 1 224 ? -77.005  46.955 34.840  1.00 72.33  ? 224 LEU B N   1 
ATOM   4201 C  CA  . LEU B 1 224 ? -78.445  47.108 34.650  1.00 76.80  ? 224 LEU B CA  1 
ATOM   4202 C  C   . LEU B 1 224 ? -78.852  48.574 34.534  1.00 80.14  ? 224 LEU B C   1 
ATOM   4203 O  O   . LEU B 1 224 ? -79.708  48.920 33.713  1.00 79.09  ? 224 LEU B O   1 
ATOM   4204 C  CB  . LEU B 1 224 ? -79.200  46.425 35.790  1.00 73.17  ? 224 LEU B CB  1 
ATOM   4205 C  CG  . LEU B 1 224 ? -80.706  46.299 35.563  1.00 70.76  ? 224 LEU B CG  1 
ATOM   4206 C  CD1 . LEU B 1 224 ? -80.974  45.637 34.221  1.00 73.97  ? 224 LEU B CD1 1 
ATOM   4207 C  CD2 . LEU B 1 224 ? -81.361  45.520 36.687  1.00 65.28  ? 224 LEU B CD2 1 
ATOM   4208 N  N   . GLU B 1 225 ? -78.249  49.452 35.336  1.00 79.58  ? 225 GLU B N   1 
ATOM   4209 C  CA  . GLU B 1 225 ? -78.639  50.859 35.305  1.00 77.53  ? 225 GLU B CA  1 
ATOM   4210 C  C   . GLU B 1 225 ? -78.262  51.511 33.980  1.00 81.16  ? 225 GLU B C   1 
ATOM   4211 O  O   . GLU B 1 225 ? -79.074  52.220 33.372  1.00 79.18  ? 225 GLU B O   1 
ATOM   4212 C  CB  . GLU B 1 225 ? -77.995  51.613 36.465  1.00 85.10  ? 225 GLU B CB  1 
ATOM   4213 C  CG  . GLU B 1 225 ? -78.208  53.116 36.396  1.00 88.70  ? 225 GLU B CG  1 
ATOM   4214 C  CD  . GLU B 1 225 ? -77.531  53.863 37.530  1.00 97.91  ? 225 GLU B CD  1 
ATOM   4215 O  OE1 . GLU B 1 225 ? -76.433  53.445 37.956  1.00 100.81 ? 225 GLU B OE1 1 
ATOM   4216 O  OE2 . GLU B 1 225 ? -78.100  54.871 37.999  1.00 97.07  ? 225 GLU B OE2 1 
ATOM   4217 N  N   . LYS B 1 226 ? -77.028  51.291 33.524  1.00 80.01  ? 226 LYS B N   1 
ATOM   4218 C  CA  . LYS B 1 226 ? -76.566  51.939 32.302  1.00 76.39  ? 226 LYS B CA  1 
ATOM   4219 C  C   . LYS B 1 226 ? -77.355  51.462 31.089  1.00 85.16  ? 226 LYS B C   1 
ATOM   4220 O  O   . LYS B 1 226 ? -77.668  52.254 30.192  1.00 86.10  ? 226 LYS B O   1 
ATOM   4221 C  CB  . LYS B 1 226 ? -75.071  51.683 32.107  1.00 70.00  ? 226 LYS B CB  1 
ATOM   4222 N  N   . GLU B 1 227 ? -77.695  50.173 31.045  1.00 84.28  ? 227 GLU B N   1 
ATOM   4223 C  CA  . GLU B 1 227 ? -78.397  49.631 29.889  1.00 84.52  ? 227 GLU B CA  1 
ATOM   4224 C  C   . GLU B 1 227 ? -79.905  49.845 29.960  1.00 81.06  ? 227 GLU B C   1 
ATOM   4225 O  O   . GLU B 1 227 ? -80.563  49.867 28.914  1.00 84.71  ? 227 GLU B O   1 
ATOM   4226 C  CB  . GLU B 1 227 ? -78.068  48.142 29.730  1.00 82.61  ? 227 GLU B CB  1 
ATOM   4227 C  CG  . GLU B 1 227 ? -76.597  47.885 29.390  1.00 80.76  ? 227 GLU B CG  1 
ATOM   4228 C  CD  . GLU B 1 227 ? -76.281  46.422 29.124  1.00 86.87  ? 227 GLU B CD  1 
ATOM   4229 O  OE1 . GLU B 1 227 ? -77.107  45.554 29.478  1.00 89.57  ? 227 GLU B OE1 1 
ATOM   4230 O  OE2 . GLU B 1 227 ? -75.203  46.139 28.558  1.00 83.73  ? 227 GLU B OE2 1 
ATOM   4231 N  N   . GLU B 1 228 ? -80.465  50.014 31.159  1.00 74.82  ? 228 GLU B N   1 
ATOM   4232 C  CA  . GLU B 1 228 ? -81.880  50.354 31.267  1.00 77.69  ? 228 GLU B CA  1 
ATOM   4233 C  C   . GLU B 1 228 ? -82.118  51.827 30.965  1.00 81.09  ? 228 GLU B C   1 
ATOM   4234 O  O   . GLU B 1 228 ? -83.142  52.185 30.374  1.00 83.07  ? 228 GLU B O   1 
ATOM   4235 C  CB  . GLU B 1 228 ? -82.406  50.008 32.661  1.00 76.77  ? 228 GLU B CB  1 
ATOM   4236 C  CG  . GLU B 1 228 ? -83.852  50.410 32.903  1.00 83.58  ? 228 GLU B CG  1 
ATOM   4237 C  CD  . GLU B 1 228 ? -84.313  50.108 34.317  1.00 99.55  ? 228 GLU B CD  1 
ATOM   4238 O  OE1 . GLU B 1 228 ? -83.471  49.704 35.147  1.00 94.29  ? 228 GLU B OE1 1 
ATOM   4239 O  OE2 . GLU B 1 228 ? -85.518  50.275 34.600  1.00 109.16 ? 228 GLU B OE2 1 
ATOM   4240 N  N   . ALA B 1 229 ? -81.183  52.692 31.364  1.00 84.60  ? 229 ALA B N   1 
ATOM   4241 C  CA  . ALA B 1 229 ? -81.314  54.115 31.069  1.00 80.65  ? 229 ALA B CA  1 
ATOM   4242 C  C   . ALA B 1 229 ? -81.227  54.380 29.573  1.00 77.27  ? 229 ALA B C   1 
ATOM   4243 O  O   . ALA B 1 229 ? -81.939  55.244 29.048  1.00 82.00  ? 229 ALA B O   1 
ATOM   4244 C  CB  . ALA B 1 229 ? -80.241  54.905 31.813  1.00 76.53  ? 229 ALA B CB  1 
ATOM   4245 N  N   . ARG B 1 230 ? -80.364  53.651 28.871  1.00 77.17  ? 230 ARG B N   1 
ATOM   4246 C  CA  . ARG B 1 230 ? -80.157  53.845 27.443  1.00 79.94  ? 230 ARG B CA  1 
ATOM   4247 C  C   . ARG B 1 230 ? -81.048  52.954 26.587  1.00 82.69  ? 230 ARG B C   1 
ATOM   4248 O  O   . ARG B 1 230 ? -80.881  52.925 25.363  1.00 79.07  ? 230 ARG B O   1 
ATOM   4249 C  CB  . ARG B 1 230 ? -78.687  53.613 27.091  1.00 76.64  ? 230 ARG B CB  1 
ATOM   4250 C  CG  . ARG B 1 230 ? -77.734  54.519 27.851  1.00 81.88  ? 230 ARG B CG  1 
ATOM   4251 C  CD  . ARG B 1 230 ? -76.329  54.458 27.277  1.00 88.01  ? 230 ARG B CD  1 
ATOM   4252 N  NE  . ARG B 1 230 ? -75.375  55.193 28.097  1.00 93.26  ? 230 ARG B NE  1 
ATOM   4253 C  CZ  . ARG B 1 230 ? -74.088  55.331 27.809  1.00 97.63  ? 230 ARG B CZ  1 
ATOM   4254 N  NH1 . ARG B 1 230 ? -73.565  54.807 26.712  1.00 100.13 ? 230 ARG B NH1 1 
ATOM   4255 N  NH2 . ARG B 1 230 ? -73.305  56.011 28.643  1.00 102.22 ? 230 ARG B NH2 1 
ATOM   4256 N  N   . GLY B 1 231 ? -81.981  52.229 27.197  1.00 83.77  ? 231 GLY B N   1 
ATOM   4257 C  CA  . GLY B 1 231 ? -82.946  51.461 26.434  1.00 83.58  ? 231 GLY B CA  1 
ATOM   4258 C  C   . GLY B 1 231 ? -82.408  50.210 25.777  1.00 87.55  ? 231 GLY B C   1 
ATOM   4259 O  O   . GLY B 1 231 ? -82.969  49.759 24.773  1.00 87.33  ? 231 GLY B O   1 
ATOM   4260 N  N   . GLU B 1 232 ? -81.330  49.635 26.306  1.00 83.22  ? 232 GLU B N   1 
ATOM   4261 C  CA  . GLU B 1 232 ? -80.854  48.358 25.796  1.00 81.36  ? 232 GLU B CA  1 
ATOM   4262 C  C   . GLU B 1 232 ? -81.842  47.256 26.160  1.00 80.43  ? 232 GLU B C   1 
ATOM   4263 O  O   . GLU B 1 232 ? -82.372  47.218 27.274  1.00 80.44  ? 232 GLU B O   1 
ATOM   4264 C  CB  . GLU B 1 232 ? -79.466  48.034 26.354  1.00 78.24  ? 232 GLU B CB  1 
ATOM   4265 C  CG  . GLU B 1 232 ? -78.921  46.666 25.935  1.00 78.13  ? 232 GLU B CG  1 
ATOM   4266 C  CD  . GLU B 1 232 ? -78.546  46.596 24.457  1.00 95.35  ? 232 GLU B CD  1 
ATOM   4267 O  OE1 . GLU B 1 232 ? -77.560  47.251 24.056  1.00 94.81  ? 232 GLU B OE1 1 
ATOM   4268 O  OE2 . GLU B 1 232 ? -79.237  45.886 23.693  1.00 88.79  ? 232 GLU B OE2 1 
ATOM   4269 N  N   . GLN B 1 233 ? -82.108  46.368 25.202  1.00 80.83  ? 233 GLN B N   1 
ATOM   4270 C  CA  . GLN B 1 233 ? -83.004  45.244 25.427  1.00 79.47  ? 233 GLN B CA  1 
ATOM   4271 C  C   . GLN B 1 233 ? -82.286  43.913 25.565  1.00 75.16  ? 233 GLN B C   1 
ATOM   4272 O  O   . GLN B 1 233 ? -82.868  42.972 26.112  1.00 73.60  ? 233 GLN B O   1 
ATOM   4273 C  CB  . GLN B 1 233 ? -84.029  45.137 24.290  1.00 81.63  ? 233 GLN B CB  1 
ATOM   4274 C  CG  . GLN B 1 233 ? -85.036  46.270 24.255  1.00 84.42  ? 233 GLN B CG  1 
ATOM   4275 C  CD  . GLN B 1 233 ? -86.061  46.095 23.153  1.00 102.07 ? 233 GLN B CD  1 
ATOM   4276 O  OE1 . GLN B 1 233 ? -87.211  45.740 23.412  1.00 103.89 ? 233 GLN B OE1 1 
ATOM   4277 N  NE2 . GLN B 1 233 ? -85.648  46.342 21.912  1.00 89.69  ? 233 GLN B NE2 1 
ATOM   4278 N  N   . ASN B 1 234 ? -81.048  43.809 25.087  1.00 78.28  ? 234 ASN B N   1 
ATOM   4279 C  CA  . ASN B 1 234 ? -80.280  42.572 25.212  1.00 75.88  ? 234 ASN B CA  1 
ATOM   4280 C  C   . ASN B 1 234 ? -79.471  42.604 26.508  1.00 74.73  ? 234 ASN B C   1 
ATOM   4281 O  O   . ASN B 1 234 ? -78.238  42.639 26.530  1.00 75.40  ? 234 ASN B O   1 
ATOM   4282 C  CB  . ASN B 1 234 ? -79.409  42.359 23.983  1.00 74.96  ? 234 ASN B CB  1 
ATOM   4283 C  CG  . ASN B 1 234 ? -80.206  41.850 22.798  1.00 82.67  ? 234 ASN B CG  1 
ATOM   4284 O  OD1 . ASN B 1 234 ? -81.438  41.850 22.822  1.00 74.53  ? 234 ASN B OD1 1 
ATOM   4285 N  ND2 . ASN B 1 234 ? -79.509  41.408 21.757  1.00 90.11  ? 234 ASN B ND2 1 
ATOM   4286 N  N   . ASN B 1 235 ? -80.220  42.617 27.606  1.00 67.57  ? 235 ASN B N   1 
ATOM   4287 C  CA  . ASN B 1 235 ? -79.716  42.375 28.948  1.00 70.93  ? 235 ASN B CA  1 
ATOM   4288 C  C   . ASN B 1 235 ? -80.567  41.268 29.550  1.00 71.08  ? 235 ASN B C   1 
ATOM   4289 O  O   . ASN B 1 235 ? -81.788  41.254 29.370  1.00 71.96  ? 235 ASN B O   1 
ATOM   4290 C  CB  . ASN B 1 235 ? -79.779  43.644 29.815  1.00 68.82  ? 235 ASN B CB  1 
ATOM   4291 C  CG  . ASN B 1 235 ? -79.246  43.424 31.222  1.00 70.68  ? 235 ASN B CG  1 
ATOM   4292 O  OD1 . ASN B 1 235 ? -79.884  42.773 32.049  1.00 69.88  ? 235 ASN B OD1 1 
ATOM   4293 N  ND2 . ASN B 1 235 ? -78.077  43.986 31.505  1.00 74.15  ? 235 ASN B ND2 1 
ATOM   4294 N  N   . MET B 1 236 ? -79.921  40.335 30.255  1.00 68.99  ? 236 MET B N   1 
ATOM   4295 C  CA  . MET B 1 236 ? -80.639  39.164 30.751  1.00 71.40  ? 236 MET B CA  1 
ATOM   4296 C  C   . MET B 1 236 ? -81.805  39.546 31.660  1.00 71.18  ? 236 MET B C   1 
ATOM   4297 O  O   . MET B 1 236 ? -82.814  38.834 31.698  1.00 68.49  ? 236 MET B O   1 
ATOM   4298 C  CB  . MET B 1 236 ? -79.680  38.221 31.481  1.00 69.59  ? 236 MET B CB  1 
ATOM   4299 C  CG  . MET B 1 236 ? -80.332  36.931 31.972  1.00 71.26  ? 236 MET B CG  1 
ATOM   4300 S  SD  . MET B 1 236 ? -80.873  35.837 30.637  1.00 74.84  ? 236 MET B SD  1 
ATOM   4301 C  CE  . MET B 1 236 ? -79.334  35.020 30.229  1.00 64.88  ? 236 MET B CE  1 
ATOM   4302 N  N   . VAL B 1 237 ? -81.698  40.662 32.388  1.00 65.97  ? 237 VAL B N   1 
ATOM   4303 C  CA  . VAL B 1 237 ? -82.816  41.105 33.219  1.00 69.42  ? 237 VAL B CA  1 
ATOM   4304 C  C   . VAL B 1 237 ? -84.015  41.458 32.348  1.00 69.89  ? 237 VAL B C   1 
ATOM   4305 O  O   . VAL B 1 237 ? -85.137  40.995 32.586  1.00 70.36  ? 237 VAL B O   1 
ATOM   4306 C  CB  . VAL B 1 237 ? -82.401  42.294 34.104  1.00 71.75  ? 237 VAL B CB  1 
ATOM   4307 C  CG1 . VAL B 1 237 ? -83.599  42.802 34.889  1.00 69.51  ? 237 VAL B CG1 1 
ATOM   4308 C  CG2 . VAL B 1 237 ? -81.273  41.905 35.043  1.00 69.02  ? 237 VAL B CG2 1 
ATOM   4309 N  N   . MET B 1 238 ? -83.793  42.283 31.321  1.00 73.03  ? 238 MET B N   1 
ATOM   4310 C  CA  . MET B 1 238 ? -84.890  42.677 30.442  1.00 70.21  ? 238 MET B CA  1 
ATOM   4311 C  C   . MET B 1 238 ? -85.436  41.484 29.671  1.00 72.30  ? 238 MET B C   1 
ATOM   4312 O  O   . MET B 1 238 ? -86.652  41.361 29.482  1.00 78.63  ? 238 MET B O   1 
ATOM   4313 C  CB  . MET B 1 238 ? -84.430  43.767 29.472  1.00 71.70  ? 238 MET B CB  1 
ATOM   4314 C  CG  . MET B 1 238 ? -84.260  45.147 30.087  1.00 68.11  ? 238 MET B CG  1 
ATOM   4315 S  SD  . MET B 1 238 ? -82.789  45.283 31.116  1.00 85.27  ? 238 MET B SD  1 
ATOM   4316 C  CE  . MET B 1 238 ? -82.032  46.754 30.427  1.00 74.66  ? 238 MET B CE  1 
ATOM   4317 N  N   . ILE B 1 239 ? -84.553  40.592 29.219  1.00 72.38  ? 239 ILE B N   1 
ATOM   4318 C  CA  . ILE B 1 239 ? -84.983  39.461 28.403  1.00 73.08  ? 239 ILE B CA  1 
ATOM   4319 C  C   . ILE B 1 239 ? -85.839  38.500 29.220  1.00 72.32  ? 239 ILE B C   1 
ATOM   4320 O  O   . ILE B 1 239 ? -86.820  37.939 28.714  1.00 71.85  ? 239 ILE B O   1 
ATOM   4321 C  CB  . ILE B 1 239 ? -83.755  38.766 27.789  1.00 76.03  ? 239 ILE B CB  1 
ATOM   4322 C  CG1 . ILE B 1 239 ? -83.098  39.702 26.773  1.00 75.63  ? 239 ILE B CG1 1 
ATOM   4323 C  CG2 . ILE B 1 239 ? -84.144  37.453 27.136  1.00 71.04  ? 239 ILE B CG2 1 
ATOM   4324 C  CD1 . ILE B 1 239 ? -81.755  39.243 26.303  1.00 74.85  ? 239 ILE B CD1 1 
ATOM   4325 N  N   . LEU B 1 240 ? -85.497  38.304 30.495  1.00 71.18  ? 240 LEU B N   1 
ATOM   4326 C  CA  . LEU B 1 240 ? -86.338  37.480 31.358  1.00 76.15  ? 240 LEU B CA  1 
ATOM   4327 C  C   . LEU B 1 240 ? -87.705  38.118 31.563  1.00 74.78  ? 240 LEU B C   1 
ATOM   4328 O  O   . LEU B 1 240 ? -88.719  37.415 31.642  1.00 79.87  ? 240 LEU B O   1 
ATOM   4329 C  CB  . LEU B 1 240 ? -85.649  37.242 32.701  1.00 73.92  ? 240 LEU B CB  1 
ATOM   4330 C  CG  . LEU B 1 240 ? -84.432  36.317 32.669  1.00 73.07  ? 240 LEU B CG  1 
ATOM   4331 C  CD1 . LEU B 1 240 ? -83.978  35.984 34.078  1.00 73.17  ? 240 LEU B CD1 1 
ATOM   4332 C  CD2 . LEU B 1 240 ? -84.738  35.053 31.885  1.00 74.13  ? 240 LEU B CD2 1 
ATOM   4333 N  N   . ARG B 1 241 ? -87.755  39.448 31.649  1.00 70.17  ? 241 ARG B N   1 
ATOM   4334 C  CA  . ARG B 1 241 ? -89.037  40.131 31.775  1.00 74.07  ? 241 ARG B CA  1 
ATOM   4335 C  C   . ARG B 1 241 ? -89.921  39.867 30.562  1.00 78.67  ? 241 ARG B C   1 
ATOM   4336 O  O   . ARG B 1 241 ? -91.105  39.544 30.702  1.00 84.80  ? 241 ARG B O   1 
ATOM   4337 C  CB  . ARG B 1 241 ? -88.822  41.632 31.961  1.00 77.39  ? 241 ARG B CB  1 
ATOM   4338 C  CG  . ARG B 1 241 ? -88.242  42.026 33.307  1.00 78.11  ? 241 ARG B CG  1 
ATOM   4339 C  CD  . ARG B 1 241 ? -88.463  43.505 33.560  1.00 76.21  ? 241 ARG B CD  1 
ATOM   4340 N  NE  . ARG B 1 241 ? -89.883  43.830 33.622  1.00 80.45  ? 241 ARG B NE  1 
ATOM   4341 C  CZ  . ARG B 1 241 ? -90.378  45.055 33.517  1.00 80.49  ? 241 ARG B CZ  1 
ATOM   4342 N  NH1 . ARG B 1 241 ? -89.594  46.102 33.315  1.00 81.16  ? 241 ARG B NH1 1 
ATOM   4343 N  NH2 . ARG B 1 241 ? -91.692  45.234 33.609  1.00 80.48  ? 241 ARG B NH2 1 
ATOM   4344 N  N   . ARG B 1 242 ? -89.361  40.000 29.358  1.00 75.00  ? 242 ARG B N   1 
ATOM   4345 C  CA  . ARG B 1 242 ? -90.163  39.817 28.153  1.00 76.32  ? 242 ARG B CA  1 
ATOM   4346 C  C   . ARG B 1 242 ? -90.551  38.356 27.959  1.00 85.55  ? 242 ARG B C   1 
ATOM   4347 O  O   . ARG B 1 242 ? -91.699  38.057 27.609  1.00 85.74  ? 242 ARG B O   1 
ATOM   4348 C  CB  . ARG B 1 242 ? -89.406  40.332 26.930  1.00 77.34  ? 242 ARG B CB  1 
ATOM   4349 C  CG  . ARG B 1 242 ? -88.980  41.785 27.025  1.00 79.44  ? 242 ARG B CG  1 
ATOM   4350 C  CD  . ARG B 1 242 ? -88.589  42.339 25.662  1.00 75.45  ? 242 ARG B CD  1 
ATOM   4351 N  NE  . ARG B 1 242 ? -87.558  41.542 25.005  1.00 74.73  ? 242 ARG B NE  1 
ATOM   4352 C  CZ  . ARG B 1 242 ? -86.253  41.721 25.164  1.00 76.45  ? 242 ARG B CZ  1 
ATOM   4353 N  NH1 . ARG B 1 242 ? -85.775  42.651 25.974  1.00 76.49  ? 242 ARG B NH1 1 
ATOM   4354 N  NH2 . ARG B 1 242 ? -85.406  40.945 24.494  1.00 75.19  ? 242 ARG B NH2 1 
ATOM   4355 N  N   . GLU B 1 243 ? -89.612  37.433 28.182  1.00 83.51  ? 243 GLU B N   1 
ATOM   4356 C  CA  . GLU B 1 243 ? -89.876  36.025 27.897  1.00 83.75  ? 243 GLU B CA  1 
ATOM   4357 C  C   . GLU B 1 243 ? -91.013  35.485 28.758  1.00 87.67  ? 243 GLU B C   1 
ATOM   4358 O  O   . GLU B 1 243 ? -91.910  34.796 28.257  1.00 90.74  ? 243 GLU B O   1 
ATOM   4359 C  CB  . GLU B 1 243 ? -88.606  35.195 28.104  1.00 84.93  ? 243 GLU B CB  1 
ATOM   4360 C  CG  . GLU B 1 243 ? -88.781  33.715 27.773  1.00 84.71  ? 243 GLU B CG  1 
ATOM   4361 C  CD  . GLU B 1 243 ? -87.516  32.897 27.979  1.00 88.78  ? 243 GLU B CD  1 
ATOM   4362 O  OE1 . GLU B 1 243 ? -86.592  33.380 28.669  1.00 83.26  ? 243 GLU B OE1 1 
ATOM   4363 O  OE2 . GLU B 1 243 ? -87.447  31.766 27.449  1.00 85.68  ? 243 GLU B OE2 1 
ATOM   4364 N  N   . HIS B 1 244 ? -91.001  35.794 30.054  1.00 80.25  ? 244 HIS B N   1 
ATOM   4365 C  CA  . HIS B 1 244 ? -91.932  35.197 31.003  1.00 85.25  ? 244 HIS B CA  1 
ATOM   4366 C  C   . HIS B 1 244 ? -92.965  36.172 31.553  1.00 90.99  ? 244 HIS B C   1 
ATOM   4367 O  O   . HIS B 1 244 ? -93.827  35.757 32.335  1.00 90.77  ? 244 HIS B O   1 
ATOM   4368 C  CB  . HIS B 1 244 ? -91.165  34.574 32.177  1.00 89.52  ? 244 HIS B CB  1 
ATOM   4369 C  CG  . HIS B 1 244 ? -90.114  33.591 31.767  1.00 86.86  ? 244 HIS B CG  1 
ATOM   4370 N  ND1 . HIS B 1 244 ? -88.780  33.924 31.676  1.00 89.78  ? 244 HIS B ND1 1 
ATOM   4371 C  CD2 . HIS B 1 244 ? -90.199  32.283 31.428  1.00 83.78  ? 244 HIS B CD2 1 
ATOM   4372 C  CE1 . HIS B 1 244 ? -88.089  32.864 31.297  1.00 89.85  ? 244 HIS B CE1 1 
ATOM   4373 N  NE2 . HIS B 1 244 ? -88.927  31.855 31.139  1.00 88.60  ? 244 HIS B NE2 1 
ATOM   4374 N  N   . GLY B 1 245 ? -92.903  37.448 31.183  1.00 91.04  ? 245 GLY B N   1 
ATOM   4375 C  CA  . GLY B 1 245 ? -93.810  38.427 31.749  1.00 83.21  ? 245 GLY B CA  1 
ATOM   4376 C  C   . GLY B 1 245 ? -93.582  38.647 33.231  1.00 83.91  ? 245 GLY B C   1 
ATOM   4377 O  O   . GLY B 1 245 ? -94.524  38.577 34.026  1.00 87.28  ? 245 GLY B O   1 
ATOM   4378 N  N   . TRP B 1 246 ? -92.334  38.910 33.614  1.00 84.64  ? 246 TRP B N   1 
ATOM   4379 C  CA  . TRP B 1 246 ? -91.953  39.115 35.004  1.00 83.36  ? 246 TRP B CA  1 
ATOM   4380 C  C   . TRP B 1 246 ? -91.623  40.578 35.267  1.00 81.59  ? 246 TRP B C   1 
ATOM   4381 O  O   . TRP B 1 246 ? -91.219  41.315 34.364  1.00 80.05  ? 246 TRP B O   1 
ATOM   4382 C  CB  . TRP B 1 246 ? -90.732  38.273 35.380  1.00 85.02  ? 246 TRP B CB  1 
ATOM   4383 C  CG  . TRP B 1 246 ? -90.952  36.800 35.416  1.00 91.92  ? 246 TRP B CG  1 
ATOM   4384 C  CD1 . TRP B 1 246 ? -92.144  36.139 35.360  1.00 93.57  ? 246 TRP B CD1 1 
ATOM   4385 C  CD2 . TRP B 1 246 ? -89.939  35.796 35.521  1.00 90.87  ? 246 TRP B CD2 1 
ATOM   4386 N  NE1 . TRP B 1 246 ? -91.933  34.781 35.424  1.00 89.17  ? 246 TRP B NE1 1 
ATOM   4387 C  CE2 . TRP B 1 246 ? -90.587  34.546 35.524  1.00 88.09  ? 246 TRP B CE2 1 
ATOM   4388 C  CE3 . TRP B 1 246 ? -88.545  35.835 35.612  1.00 84.18  ? 246 TRP B CE3 1 
ATOM   4389 C  CZ2 . TRP B 1 246 ? -89.889  33.347 35.612  1.00 87.49  ? 246 TRP B CZ2 1 
ATOM   4390 C  CZ3 . TRP B 1 246 ? -87.856  34.645 35.699  1.00 84.57  ? 246 TRP B CZ3 1 
ATOM   4391 C  CH2 . TRP B 1 246 ? -88.526  33.417 35.701  1.00 86.27  ? 246 TRP B CH2 1 
ATOM   4392 N  N   . SER B 1 247 ? -91.774  40.984 36.524  1.00 80.37  ? 247 SER B N   1 
ATOM   4393 C  CA  . SER B 1 247 ? -91.295  42.288 36.945  1.00 76.61  ? 247 SER B CA  1 
ATOM   4394 C  C   . SER B 1 247 ? -89.768  42.300 36.962  1.00 74.41  ? 247 SER B C   1 
ATOM   4395 O  O   . SER B 1 247 ? -89.109  41.264 36.836  1.00 75.19  ? 247 SER B O   1 
ATOM   4396 C  CB  . SER B 1 247 ? -91.843  42.641 38.327  1.00 76.69  ? 247 SER B CB  1 
ATOM   4397 O  OG  . SER B 1 247 ? -91.341  41.753 39.313  1.00 81.16  ? 247 SER B OG  1 
ATOM   4398 N  N   . LYS B 1 248 ? -89.200  43.498 37.126  1.00 75.21  ? 248 LYS B N   1 
ATOM   4399 C  CA  . LYS B 1 248 ? -87.747  43.608 37.198  1.00 76.77  ? 248 LYS B CA  1 
ATOM   4400 C  C   . LYS B 1 248 ? -87.200  42.872 38.415  1.00 75.52  ? 248 LYS B C   1 
ATOM   4401 O  O   . LYS B 1 248 ? -86.119  42.273 38.356  1.00 73.67  ? 248 LYS B O   1 
ATOM   4402 C  CB  . LYS B 1 248 ? -87.322  45.077 37.230  1.00 76.68  ? 248 LYS B CB  1 
ATOM   4403 C  CG  . LYS B 1 248 ? -85.815  45.272 37.121  1.00 71.87  ? 248 LYS B CG  1 
ATOM   4404 C  CD  . LYS B 1 248 ? -85.305  46.408 37.999  1.00 79.77  ? 248 LYS B CD  1 
ATOM   4405 C  CE  . LYS B 1 248 ? -85.239  47.725 37.245  1.00 91.68  ? 248 LYS B CE  1 
ATOM   4406 N  NZ  . LYS B 1 248 ? -84.557  48.781 38.050  1.00 89.01  ? 248 LYS B NZ  1 
ATOM   4407 N  N   . SER B 1 249 ? -87.940  42.892 39.526  1.00 79.21  ? 249 SER B N   1 
ATOM   4408 C  CA  . SER B 1 249 ? -87.442  42.281 40.753  1.00 73.85  ? 249 SER B CA  1 
ATOM   4409 C  C   . SER B 1 249 ? -87.442  40.760 40.662  1.00 72.97  ? 249 SER B C   1 
ATOM   4410 O  O   . SER B 1 249 ? -86.524  40.108 41.172  1.00 73.00  ? 249 SER B O   1 
ATOM   4411 C  CB  . SER B 1 249 ? -88.268  42.756 41.948  1.00 74.96  ? 249 SER B CB  1 
ATOM   4412 O  OG  . SER B 1 249 ? -89.651  42.550 41.728  1.00 86.28  ? 249 SER B OG  1 
ATOM   4413 N  N   . ARG B 1 250 ? -88.452  40.170 40.015  1.00 71.48  ? 250 ARG B N   1 
ATOM   4414 C  CA  . ARG B 1 250 ? -88.459  38.714 39.894  1.00 79.32  ? 250 ARG B CA  1 
ATOM   4415 C  C   . ARG B 1 250 ? -87.379  38.220 38.937  1.00 78.41  ? 250 ARG B C   1 
ATOM   4416 O  O   . ARG B 1 250 ? -86.801  37.151 39.163  1.00 80.57  ? 250 ARG B O   1 
ATOM   4417 C  CB  . ARG B 1 250 ? -89.828  38.201 39.441  1.00 79.28  ? 250 ARG B CB  1 
ATOM   4418 C  CG  . ARG B 1 250 ? -89.878  36.671 39.366  1.00 87.90  ? 250 ARG B CG  1 
ATOM   4419 C  CD  . ARG B 1 250 ? -91.179  36.127 38.797  1.00 91.93  ? 250 ARG B CD  1 
ATOM   4420 N  NE  . ARG B 1 250 ? -92.291  36.275 39.726  1.00 99.19  ? 250 ARG B NE  1 
ATOM   4421 C  CZ  . ARG B 1 250 ? -93.200  37.235 39.649  1.00 102.22 ? 250 ARG B CZ  1 
ATOM   4422 N  NH1 . ARG B 1 250 ? -93.169  38.137 38.682  1.00 99.49  ? 250 ARG B NH1 1 
ATOM   4423 N  NH2 . ARG B 1 250 ? -94.165  37.291 40.562  1.00 102.00 ? 250 ARG B NH2 1 
ATOM   4424 N  N   . SER B 1 251 ? -87.092  38.973 37.871  1.00 72.81  ? 251 SER B N   1 
ATOM   4425 C  CA  . SER B 1 251 ? -86.029  38.574 36.952  1.00 77.29  ? 251 SER B CA  1 
ATOM   4426 C  C   . SER B 1 251 ? -84.673  38.579 37.648  1.00 76.11  ? 251 SER B C   1 
ATOM   4427 O  O   . SER B 1 251 ? -83.896  37.624 37.530  1.00 72.75  ? 251 SER B O   1 
ATOM   4428 C  CB  . SER B 1 251 ? -86.015  39.495 35.731  1.00 77.09  ? 251 SER B CB  1 
ATOM   4429 O  OG  . SER B 1 251 ? -87.174  39.306 34.941  1.00 82.85  ? 251 SER B OG  1 
ATOM   4430 N  N   . VAL B 1 252 ? -84.371  39.654 38.380  1.00 69.52  ? 252 VAL B N   1 
ATOM   4431 C  CA  . VAL B 1 252 ? -83.144  39.694 39.171  1.00 72.26  ? 252 VAL B CA  1 
ATOM   4432 C  C   . VAL B 1 252 ? -83.133  38.559 40.185  1.00 73.10  ? 252 VAL B C   1 
ATOM   4433 O  O   . VAL B 1 252 ? -82.093  37.935 40.435  1.00 72.44  ? 252 VAL B O   1 
ATOM   4434 C  CB  . VAL B 1 252 ? -82.995  41.067 39.852  1.00 66.40  ? 252 VAL B CB  1 
ATOM   4435 C  CG1 . VAL B 1 252 ? -81.811  41.067 40.802  1.00 62.85  ? 252 VAL B CG1 1 
ATOM   4436 C  CG2 . VAL B 1 252 ? -82.847  42.159 38.805  1.00 70.29  ? 252 VAL B CG2 1 
ATOM   4437 N  N   . SER B 1 253 ? -84.294  38.263 40.773  1.00 71.49  ? 253 SER B N   1 
ATOM   4438 C  CA  . SER B 1 253 ? -84.376  37.184 41.751  1.00 75.43  ? 253 SER B CA  1 
ATOM   4439 C  C   . SER B 1 253 ? -84.136  35.829 41.097  1.00 77.20  ? 253 SER B C   1 
ATOM   4440 O  O   . SER B 1 253 ? -83.490  34.954 41.686  1.00 71.18  ? 253 SER B O   1 
ATOM   4441 C  CB  . SER B 1 253 ? -85.737  37.218 42.447  1.00 77.90  ? 253 SER B CB  1 
ATOM   4442 O  OG  . SER B 1 253 ? -85.761  36.356 43.568  1.00 82.10  ? 253 SER B OG  1 
ATOM   4443 N  N   . HIS B 1 254 ? -84.640  35.641 39.875  1.00 79.05  ? 254 HIS B N   1 
ATOM   4444 C  CA  . HIS B 1 254 ? -84.424  34.380 39.171  1.00 74.48  ? 254 HIS B CA  1 
ATOM   4445 C  C   . HIS B 1 254 ? -82.966  34.220 38.760  1.00 73.54  ? 254 HIS B C   1 
ATOM   4446 O  O   . HIS B 1 254 ? -82.424  33.108 38.795  1.00 76.08  ? 254 HIS B O   1 
ATOM   4447 C  CB  . HIS B 1 254 ? -85.339  34.298 37.950  1.00 72.17  ? 254 HIS B CB  1 
ATOM   4448 C  CG  . HIS B 1 254 ? -85.192  33.029 37.168  1.00 74.46  ? 254 HIS B CG  1 
ATOM   4449 N  ND1 . HIS B 1 254 ? -84.659  32.995 35.898  1.00 72.98  ? 254 HIS B ND1 1 
ATOM   4450 C  CD2 . HIS B 1 254 ? -85.505  31.749 37.480  1.00 80.75  ? 254 HIS B CD2 1 
ATOM   4451 C  CE1 . HIS B 1 254 ? -84.650  31.749 35.460  1.00 74.94  ? 254 HIS B CE1 1 
ATOM   4452 N  NE2 . HIS B 1 254 ? -85.158  30.973 36.401  1.00 82.73  ? 254 HIS B NE2 1 
ATOM   4453 N  N   . MET B 1 255 ? -82.313  35.317 38.372  1.00 67.72  ? 255 MET B N   1 
ATOM   4454 C  CA  . MET B 1 255 ? -80.908  35.235 37.988  1.00 71.46  ? 255 MET B CA  1 
ATOM   4455 C  C   . MET B 1 255 ? -80.029  34.880 39.181  1.00 74.07  ? 255 MET B C   1 
ATOM   4456 O  O   . MET B 1 255 ? -79.035  34.160 39.031  1.00 70.75  ? 255 MET B O   1 
ATOM   4457 C  CB  . MET B 1 255 ? -80.462  36.550 37.352  1.00 70.85  ? 255 MET B CB  1 
ATOM   4458 C  CG  . MET B 1 255 ? -81.099  36.805 36.003  1.00 67.91  ? 255 MET B CG  1 
ATOM   4459 S  SD  . MET B 1 255 ? -80.786  38.459 35.371  1.00 71.46  ? 255 MET B SD  1 
ATOM   4460 C  CE  . MET B 1 255 ? -79.002  38.443 35.213  1.00 65.12  ? 255 MET B CE  1 
ATOM   4461 N  N   . GLN B 1 256 ? -80.377  35.378 40.371  1.00 78.38  ? 256 GLN B N   1 
ATOM   4462 C  CA  . GLN B 1 256 ? -79.677  34.955 41.580  1.00 76.70  ? 256 GLN B CA  1 
ATOM   4463 C  C   . GLN B 1 256 ? -79.834  33.459 41.808  1.00 74.93  ? 256 GLN B C   1 
ATOM   4464 O  O   . GLN B 1 256 ? -78.866  32.770 42.148  1.00 75.77  ? 256 GLN B O   1 
ATOM   4465 C  CB  . GLN B 1 256 ? -80.192  35.729 42.792  1.00 77.34  ? 256 GLN B CB  1 
ATOM   4466 C  CG  . GLN B 1 256 ? -79.801  37.190 42.821  1.00 84.32  ? 256 GLN B CG  1 
ATOM   4467 C  CD  . GLN B 1 256 ? -80.301  37.889 44.068  1.00 85.50  ? 256 GLN B CD  1 
ATOM   4468 O  OE1 . GLN B 1 256 ? -81.485  38.203 44.184  1.00 82.47  ? 256 GLN B OE1 1 
ATOM   4469 N  NE2 . GLN B 1 256 ? -79.399  38.130 45.013  1.00 88.05  ? 256 GLN B NE2 1 
ATOM   4470 N  N   . ASN B 1 257 ? -81.051  32.938 41.621  1.00 73.99  ? 257 ASN B N   1 
ATOM   4471 C  CA  . ASN B 1 257 ? -81.272  31.501 41.752  1.00 79.66  ? 257 ASN B CA  1 
ATOM   4472 C  C   . ASN B 1 257 ? -80.464  30.712 40.730  1.00 80.21  ? 257 ASN B C   1 
ATOM   4473 O  O   . ASN B 1 257 ? -80.006  29.603 41.027  1.00 84.09  ? 257 ASN B O   1 
ATOM   4474 C  CB  . ASN B 1 257 ? -82.760  31.179 41.606  1.00 83.04  ? 257 ASN B CB  1 
ATOM   4475 C  CG  . ASN B 1 257 ? -83.587  31.700 42.763  1.00 84.62  ? 257 ASN B CG  1 
ATOM   4476 O  OD1 . ASN B 1 257 ? -83.117  31.760 43.901  1.00 91.13  ? 257 ASN B OD1 1 
ATOM   4477 N  ND2 . ASN B 1 257 ? -84.828  32.081 42.479  1.00 77.99  ? 257 ASN B ND2 1 
ATOM   4478 N  N   . GLU B 1 258 ? -80.279  31.261 39.528  1.00 70.64  ? 258 GLU B N   1 
ATOM   4479 C  CA  . GLU B 1 258 ? -79.521  30.551 38.503  1.00 73.62  ? 258 GLU B CA  1 
ATOM   4480 C  C   . GLU B 1 258 ? -78.036  30.513 38.835  1.00 72.65  ? 258 GLU B C   1 
ATOM   4481 O  O   . GLU B 1 258 ? -77.379  29.485 38.636  1.00 71.50  ? 258 GLU B O   1 
ATOM   4482 C  CB  . GLU B 1 258 ? -79.755  31.193 37.135  1.00 75.13  ? 258 GLU B CB  1 
ATOM   4483 C  CG  . GLU B 1 258 ? -81.130  30.910 36.553  1.00 73.14  ? 258 GLU B CG  1 
ATOM   4484 C  CD  . GLU B 1 258 ? -81.404  29.423 36.404  1.00 85.15  ? 258 GLU B CD  1 
ATOM   4485 O  OE1 . GLU B 1 258 ? -80.457  28.668 36.088  1.00 87.09  ? 258 GLU B OE1 1 
ATOM   4486 O  OE2 . GLU B 1 258 ? -82.567  29.009 36.610  1.00 86.17  ? 258 GLU B OE2 1 
ATOM   4487 N  N   . VAL B 1 259 ? -77.486  31.624 39.331  1.00 72.52  ? 259 VAL B N   1 
ATOM   4488 C  CA  . VAL B 1 259 ? -76.090  31.636 39.764  1.00 73.46  ? 259 VAL B CA  1 
ATOM   4489 C  C   . VAL B 1 259 ? -75.861  30.569 40.825  1.00 71.99  ? 259 VAL B C   1 
ATOM   4490 O  O   . VAL B 1 259 ? -74.888  29.807 40.768  1.00 67.49  ? 259 VAL B O   1 
ATOM   4491 C  CB  . VAL B 1 259 ? -75.698  33.033 40.278  1.00 72.65  ? 259 VAL B CB  1 
ATOM   4492 C  CG1 . VAL B 1 259 ? -74.324  32.994 40.930  1.00 71.48  ? 259 VAL B CG1 1 
ATOM   4493 C  CG2 . VAL B 1 259 ? -75.727  34.041 39.144  1.00 70.75  ? 259 VAL B CG2 1 
ATOM   4494 N  N   . ARG B 1 260 ? -76.768  30.490 41.802  1.00 68.84  ? 260 ARG B N   1 
ATOM   4495 C  CA  . ARG B 1 260 ? -76.641  29.502 42.869  1.00 78.22  ? 260 ARG B CA  1 
ATOM   4496 C  C   . ARG B 1 260 ? -76.764  28.086 42.323  1.00 74.77  ? 260 ARG B C   1 
ATOM   4497 O  O   . ARG B 1 260 ? -75.933  27.219 42.620  1.00 71.61  ? 260 ARG B O   1 
ATOM   4498 C  CB  . ARG B 1 260 ? -77.699  29.752 43.945  1.00 79.04  ? 260 ARG B CB  1 
ATOM   4499 C  CG  . ARG B 1 260 ? -77.593  28.821 45.141  1.00 85.49  ? 260 ARG B CG  1 
ATOM   4500 C  CD  . ARG B 1 260 ? -78.904  28.734 45.913  1.00 90.50  ? 260 ARG B CD  1 
ATOM   4501 N  NE  . ARG B 1 260 ? -79.969  28.137 45.113  1.00 97.64  ? 260 ARG B NE  1 
ATOM   4502 C  CZ  . ARG B 1 260 ? -81.072  28.770 44.735  1.00 103.67 ? 260 ARG B CZ  1 
ATOM   4503 N  NH1 . ARG B 1 260 ? -81.316  30.016 45.108  1.00 96.42  ? 260 ARG B NH1 1 
ATOM   4504 N  NH2 . ARG B 1 260 ? -81.954  28.133 43.967  1.00 96.74  ? 260 ARG B NH2 1 
ATOM   4505 N  N   . ALA B 1 261 ? -77.799  27.835 41.519  1.00 75.70  ? 261 ALA B N   1 
ATOM   4506 C  CA  . ALA B 1 261 ? -78.025  26.494 40.992  1.00 73.00  ? 261 ALA B CA  1 
ATOM   4507 C  C   . ALA B 1 261 ? -76.861  26.034 40.125  1.00 70.82  ? 261 ALA B C   1 
ATOM   4508 O  O   . ALA B 1 261 ? -76.488  24.855 40.148  1.00 74.96  ? 261 ALA B O   1 
ATOM   4509 C  CB  . ALA B 1 261 ? -79.332  26.457 40.200  1.00 67.42  ? 261 ALA B CB  1 
ATOM   4510 N  N   . ARG B 1 262 ? -76.265  26.948 39.360  1.00 65.54  ? 262 ARG B N   1 
ATOM   4511 C  CA  . ARG B 1 262 ? -75.172  26.550 38.483  1.00 69.81  ? 262 ARG B CA  1 
ATOM   4512 C  C   . ARG B 1 262 ? -73.873  26.338 39.245  1.00 67.53  ? 262 ARG B C   1 
ATOM   4513 O  O   . ARG B 1 262 ? -73.046  25.520 38.828  1.00 66.17  ? 262 ARG B O   1 
ATOM   4514 C  CB  . ARG B 1 262 ? -74.993  27.582 37.369  1.00 70.36  ? 262 ARG B CB  1 
ATOM   4515 C  CG  . ARG B 1 262 ? -76.203  27.609 36.460  1.00 79.18  ? 262 ARG B CG  1 
ATOM   4516 C  CD  . ARG B 1 262 ? -76.055  28.467 35.220  1.00 79.32  ? 262 ARG B CD  1 
ATOM   4517 N  NE  . ARG B 1 262 ? -77.332  28.488 34.517  1.00 85.66  ? 262 ARG B NE  1 
ATOM   4518 C  CZ  . ARG B 1 262 ? -77.811  27.475 33.806  1.00 84.46  ? 262 ARG B CZ  1 
ATOM   4519 N  NH1 . ARG B 1 262 ? -77.104  26.375 33.605  1.00 78.88  ? 262 ARG B NH1 1 
ATOM   4520 N  NH2 . ARG B 1 262 ? -79.034  27.565 33.292  1.00 79.43  ? 262 ARG B NH2 1 
ATOM   4521 N  N   . LEU B 1 263 ? -73.679  27.041 40.362  1.00 71.19  ? 263 LEU B N   1 
ATOM   4522 C  CA  . LEU B 1 263 ? -72.488  26.800 41.170  1.00 73.63  ? 263 LEU B CA  1 
ATOM   4523 C  C   . LEU B 1 263 ? -72.612  25.507 41.967  1.00 72.70  ? 263 LEU B C   1 
ATOM   4524 O  O   . LEU B 1 263 ? -71.615  24.804 42.177  1.00 68.47  ? 263 LEU B O   1 
ATOM   4525 C  CB  . LEU B 1 263 ? -72.223  27.986 42.090  1.00 70.86  ? 263 LEU B CB  1 
ATOM   4526 C  CG  . LEU B 1 263 ? -71.090  28.853 41.551  1.00 72.48  ? 263 LEU B CG  1 
ATOM   4527 C  CD1 . LEU B 1 263 ? -71.329  29.208 40.104  1.00 66.56  ? 263 LEU B CD1 1 
ATOM   4528 C  CD2 . LEU B 1 263 ? -70.993  30.095 42.352  1.00 77.47  ? 263 LEU B CD2 1 
ATOM   4529 N  N   . GLU B 1 264 ? -73.823  25.174 42.418  1.00 68.71  ? 264 GLU B N   1 
ATOM   4530 C  CA  . GLU B 1 264 ? -74.047  23.847 42.978  1.00 68.76  ? 264 GLU B CA  1 
ATOM   4531 C  C   . GLU B 1 264 ? -73.775  22.772 41.937  1.00 71.96  ? 264 GLU B C   1 
ATOM   4532 O  O   . GLU B 1 264 ? -73.182  21.730 42.244  1.00 74.80  ? 264 GLU B O   1 
ATOM   4533 C  CB  . GLU B 1 264 ? -75.474  23.732 43.516  1.00 70.99  ? 264 GLU B CB  1 
ATOM   4534 C  CG  . GLU B 1 264 ? -75.782  24.654 44.689  1.00 74.95  ? 264 GLU B CG  1 
ATOM   4535 C  CD  . GLU B 1 264 ? -74.933  24.364 45.918  1.00 89.85  ? 264 GLU B CD  1 
ATOM   4536 O  OE1 . GLU B 1 264 ? -74.367  23.252 46.018  1.00 88.29  ? 264 GLU B OE1 1 
ATOM   4537 O  OE2 . GLU B 1 264 ? -74.833  25.254 46.790  1.00 97.34  ? 264 GLU B OE2 1 
ATOM   4538 N  N   . GLN B 1 265 ? -74.189  23.014 40.691  1.00 72.98  ? 265 GLN B N   1 
ATOM   4539 C  CA  . GLN B 1 265 ? -73.887  22.070 39.623  1.00 66.63  ? 265 GLN B CA  1 
ATOM   4540 C  C   . GLN B 1 265 ? -72.404  22.061 39.289  1.00 64.00  ? 265 GLN B C   1 
ATOM   4541 O  O   . GLN B 1 265 ? -71.862  21.010 38.930  1.00 68.67  ? 265 GLN B O   1 
ATOM   4542 C  CB  . GLN B 1 265 ? -74.709  22.400 38.381  1.00 72.10  ? 265 GLN B CB  1 
ATOM   4543 C  CG  . GLN B 1 265 ? -76.200  22.199 38.551  1.00 68.82  ? 265 GLN B CG  1 
ATOM   4544 C  CD  . GLN B 1 265 ? -76.967  22.526 37.286  1.00 73.96  ? 265 GLN B CD  1 
ATOM   4545 O  OE1 . GLN B 1 265 ? -76.757  21.907 36.242  1.00 67.18  ? 265 GLN B OE1 1 
ATOM   4546 N  NE2 . GLN B 1 265 ? -77.854  23.510 37.369  1.00 70.73  ? 265 GLN B NE2 1 
ATOM   4547 N  N   . TYR B 1 266 ? -71.732  23.210 39.394  1.00 67.49  ? 266 TYR B N   1 
ATOM   4548 C  CA  . TYR B 1 266 ? -70.295  23.243 39.147  1.00 71.22  ? 266 TYR B CA  1 
ATOM   4549 C  C   . TYR B 1 266 ? -69.559  22.291 40.080  1.00 74.26  ? 266 TYR B C   1 
ATOM   4550 O  O   . TYR B 1 266 ? -68.731  21.486 39.639  1.00 68.92  ? 266 TYR B O   1 
ATOM   4551 C  CB  . TYR B 1 266 ? -69.753  24.665 39.303  1.00 66.07  ? 266 TYR B CB  1 
ATOM   4552 C  CG  . TYR B 1 266 ? -68.242  24.715 39.234  1.00 69.15  ? 266 TYR B CG  1 
ATOM   4553 C  CD1 . TYR B 1 266 ? -67.581  24.567 38.023  1.00 72.28  ? 266 TYR B CD1 1 
ATOM   4554 C  CD2 . TYR B 1 266 ? -67.476  24.886 40.381  1.00 76.19  ? 266 TYR B CD2 1 
ATOM   4555 C  CE1 . TYR B 1 266 ? -66.201  24.600 37.951  1.00 72.69  ? 266 TYR B CE1 1 
ATOM   4556 C  CE2 . TYR B 1 266 ? -66.094  24.921 40.319  1.00 76.13  ? 266 TYR B CE2 1 
ATOM   4557 C  CZ  . TYR B 1 266 ? -65.462  24.777 39.100  1.00 77.37  ? 266 TYR B CZ  1 
ATOM   4558 O  OH  . TYR B 1 266 ? -64.088  24.811 39.027  1.00 79.52  ? 266 TYR B OH  1 
ATOM   4559 N  N   . LEU B 1 267 ? -69.855  22.371 41.382  1.00 74.28  ? 267 LEU B N   1 
ATOM   4560 C  CA  . LEU B 1 267 ? -69.225  21.473 42.346  1.00 74.72  ? 267 LEU B CA  1 
ATOM   4561 C  C   . LEU B 1 267 ? -69.562  20.017 42.046  1.00 76.15  ? 267 LEU B C   1 
ATOM   4562 O  O   . LEU B 1 267 ? -68.695  19.140 42.143  1.00 78.53  ? 267 LEU B O   1 
ATOM   4563 C  CB  . LEU B 1 267 ? -69.653  21.852 43.764  1.00 69.89  ? 267 LEU B CB  1 
ATOM   4564 C  CG  . LEU B 1 267 ? -69.176  23.231 44.230  1.00 68.81  ? 267 LEU B CG  1 
ATOM   4565 C  CD1 . LEU B 1 267 ? -69.848  23.634 45.531  1.00 55.41  ? 267 LEU B CD1 1 
ATOM   4566 C  CD2 . LEU B 1 267 ? -67.663  23.251 44.379  1.00 64.60  ? 267 LEU B CD2 1 
ATOM   4567 N  N   . LEU B 1 268 ? -70.815  19.745 41.672  1.00 72.06  ? 268 LEU B N   1 
ATOM   4568 C  CA  . LEU B 1 268 ? -71.196  18.403 41.239  1.00 72.55  ? 268 LEU B CA  1 
ATOM   4569 C  C   . LEU B 1 268 ? -70.323  17.922 40.086  1.00 78.79  ? 268 LEU B C   1 
ATOM   4570 O  O   . LEU B 1 268 ? -69.887  16.765 40.064  1.00 79.28  ? 268 LEU B O   1 
ATOM   4571 C  CB  . LEU B 1 268 ? -72.667  18.391 40.827  1.00 69.32  ? 268 LEU B CB  1 
ATOM   4572 C  CG  . LEU B 1 268 ? -73.625  17.489 41.596  1.00 85.42  ? 268 LEU B CG  1 
ATOM   4573 C  CD1 . LEU B 1 268 ? -73.568  17.799 43.085  1.00 85.03  ? 268 LEU B CD1 1 
ATOM   4574 C  CD2 . LEU B 1 268 ? -75.037  17.661 41.054  1.00 81.79  ? 268 LEU B CD2 1 
ATOM   4575 N  N   . LEU B 1 269 ? -70.061  18.800 39.113  1.00 73.66  ? 269 LEU B N   1 
ATOM   4576 C  CA  . LEU B 1 269 ? -69.215  18.426 37.985  1.00 74.35  ? 269 LEU B CA  1 
ATOM   4577 C  C   . LEU B 1 269 ? -67.759  18.269 38.403  1.00 75.31  ? 269 LEU B C   1 
ATOM   4578 O  O   . LEU B 1 269 ? -67.048  17.422 37.850  1.00 70.54  ? 269 LEU B O   1 
ATOM   4579 C  CB  . LEU B 1 269 ? -69.342  19.465 36.869  1.00 73.20  ? 269 LEU B CB  1 
ATOM   4580 C  CG  . LEU B 1 269 ? -70.740  19.639 36.273  1.00 68.35  ? 269 LEU B CG  1 
ATOM   4581 C  CD1 . LEU B 1 269 ? -70.825  20.932 35.485  1.00 67.40  ? 269 LEU B CD1 1 
ATOM   4582 C  CD2 . LEU B 1 269 ? -71.102  18.454 35.398  1.00 63.61  ? 269 LEU B CD2 1 
ATOM   4583 N  N   . GLU B 1 270 ? -67.300  19.070 39.370  1.00 79.67  ? 270 GLU B N   1 
ATOM   4584 C  CA  . GLU B 1 270 ? -65.942  18.913 39.885  1.00 81.97  ? 270 GLU B CA  1 
ATOM   4585 C  C   . GLU B 1 270 ? -65.727  17.522 40.465  1.00 80.82  ? 270 GLU B C   1 
ATOM   4586 O  O   . GLU B 1 270 ? -64.670  16.912 40.261  1.00 78.79  ? 270 GLU B O   1 
ATOM   4587 C  CB  . GLU B 1 270 ? -65.651  19.974 40.947  1.00 77.96  ? 270 GLU B CB  1 
ATOM   4588 C  CG  . GLU B 1 270 ? -65.068  21.268 40.416  1.00 78.19  ? 270 GLU B CG  1 
ATOM   4589 C  CD  . GLU B 1 270 ? -64.619  22.190 41.534  1.00 78.72  ? 270 GLU B CD  1 
ATOM   4590 O  OE1 . GLU B 1 270 ? -65.108  22.026 42.670  1.00 82.21  ? 270 GLU B OE1 1 
ATOM   4591 O  OE2 . GLU B 1 270 ? -63.774  23.074 41.283  1.00 85.37  ? 270 GLU B OE2 1 
ATOM   4592 N  N   . SER B 1 271 ? -66.722  17.001 41.189  1.00 74.09  ? 271 SER B N   1 
ATOM   4593 C  CA  . SER B 1 271 ? -66.592  15.684 41.799  1.00 74.22  ? 271 SER B CA  1 
ATOM   4594 C  C   . SER B 1 271 ? -66.492  14.571 40.764  1.00 81.10  ? 271 SER B C   1 
ATOM   4595 O  O   . SER B 1 271 ? -66.083  13.457 41.111  1.00 80.21  ? 271 SER B O   1 
ATOM   4596 C  CB  . SER B 1 271 ? -67.772  15.420 42.737  1.00 75.07  ? 271 SER B CB  1 
ATOM   4597 O  OG  . SER B 1 271 ? -68.967  15.205 42.008  1.00 82.19  ? 271 SER B OG  1 
ATOM   4598 N  N   . CYS B 1 272 ? -66.852  14.843 39.510  1.00 80.68  ? 272 CYS B N   1 
ATOM   4599 C  CA  . CYS B 1 272 ? -66.734  13.860 38.442  1.00 71.48  ? 272 CYS B CA  1 
ATOM   4600 C  C   . CYS B 1 272 ? -65.356  13.848 37.794  1.00 79.47  ? 272 CYS B C   1 
ATOM   4601 O  O   . CYS B 1 272 ? -65.052  12.916 37.043  1.00 85.04  ? 272 CYS B O   1 
ATOM   4602 C  CB  . CYS B 1 272 ? -67.792  14.116 37.363  1.00 72.21  ? 272 CYS B CB  1 
ATOM   4603 S  SG  . CYS B 1 272 ? -69.501  13.966 37.926  1.00 82.67  ? 272 CYS B SG  1 
ATOM   4604 N  N   . LEU B 1 273 ? -64.523  14.851 38.066  1.00 81.11  ? 273 LEU B N   1 
ATOM   4605 C  CA  . LEU B 1 273 ? -63.219  14.923 37.417  1.00 83.57  ? 273 LEU B CA  1 
ATOM   4606 C  C   . LEU B 1 273 ? -62.286  13.756 37.743  1.00 88.08  ? 273 LEU B C   1 
ATOM   4607 O  O   . LEU B 1 273 ? -61.504  13.379 36.852  1.00 88.13  ? 273 LEU B O   1 
ATOM   4608 C  CB  . LEU B 1 273 ? -62.549  16.260 37.760  1.00 76.32  ? 273 LEU B CB  1 
ATOM   4609 C  CG  . LEU B 1 273 ? -63.213  17.462 37.089  1.00 80.60  ? 273 LEU B CG  1 
ATOM   4610 C  CD1 . LEU B 1 273 ? -62.552  18.757 37.516  1.00 84.77  ? 273 LEU B CD1 1 
ATOM   4611 C  CD2 . LEU B 1 273 ? -63.167  17.312 35.578  1.00 78.39  ? 273 LEU B CD2 1 
ATOM   4612 N  N   . PRO B 1 274 ? -62.284  13.170 38.949  1.00 89.78  ? 274 PRO B N   1 
ATOM   4613 C  CA  . PRO B 1 274 ? -61.495  11.939 39.142  1.00 85.71  ? 274 PRO B CA  1 
ATOM   4614 C  C   . PRO B 1 274 ? -61.829  10.847 38.137  1.00 87.44  ? 274 PRO B C   1 
ATOM   4615 O  O   . PRO B 1 274 ? -60.922  10.291 37.504  1.00 91.07  ? 274 PRO B O   1 
ATOM   4616 C  CB  . PRO B 1 274 ? -61.846  11.533 40.578  1.00 79.17  ? 274 PRO B CB  1 
ATOM   4617 C  CG  . PRO B 1 274 ? -62.121  12.812 41.255  1.00 77.81  ? 274 PRO B CG  1 
ATOM   4618 C  CD  . PRO B 1 274 ? -62.799  13.682 40.234  1.00 84.38  ? 274 PRO B CD  1 
ATOM   4619 N  N   . LYS B 1 275 ? -63.115  10.531 37.962  1.00 85.94  ? 275 LYS B N   1 
ATOM   4620 C  CA  . LYS B 1 275 ? -63.492  9.485  37.018  1.00 84.65  ? 275 LYS B CA  1 
ATOM   4621 C  C   . LYS B 1 275 ? -63.272  9.922  35.575  1.00 89.70  ? 275 LYS B C   1 
ATOM   4622 O  O   . LYS B 1 275 ? -62.978  9.085  34.715  1.00 91.32  ? 275 LYS B O   1 
ATOM   4623 C  CB  . LYS B 1 275 ? -64.947  9.070  37.243  1.00 83.29  ? 275 LYS B CB  1 
ATOM   4624 C  CG  . LYS B 1 275 ? -65.392  7.901  36.379  1.00 88.91  ? 275 LYS B CG  1 
ATOM   4625 C  CD  . LYS B 1 275 ? -66.216  6.899  37.170  1.00 94.56  ? 275 LYS B CD  1 
ATOM   4626 C  CE  . LYS B 1 275 ? -66.595  5.703  36.309  1.00 96.66  ? 275 LYS B CE  1 
ATOM   4627 N  NZ  . LYS B 1 275 ? -67.347  6.106  35.087  1.00 91.57  ? 275 LYS B NZ  1 
ATOM   4628 N  N   . VAL B 1 276 ? -63.401  11.221 35.290  1.00 88.67  ? 276 VAL B N   1 
ATOM   4629 C  CA  . VAL B 1 276 ? -63.079  11.715 33.955  1.00 87.92  ? 276 VAL B CA  1 
ATOM   4630 C  C   . VAL B 1 276 ? -61.591  11.549 33.669  1.00 91.47  ? 276 VAL B C   1 
ATOM   4631 O  O   . VAL B 1 276 ? -61.193  11.300 32.523  1.00 87.31  ? 276 VAL B O   1 
ATOM   4632 C  CB  . VAL B 1 276 ? -63.536  13.180 33.804  1.00 85.08  ? 276 VAL B CB  1 
ATOM   4633 C  CG1 . VAL B 1 276 ? -62.972  13.802 32.535  1.00 85.61  ? 276 VAL B CG1 1 
ATOM   4634 C  CG2 . VAL B 1 276 ? -65.054  13.257 33.795  1.00 82.59  ? 276 VAL B CG2 1 
ATOM   4635 N  N   . GLY B 1 277 ? -60.748  11.663 34.699  1.00 85.88  ? 277 GLY B N   1 
ATOM   4636 C  CA  . GLY B 1 277 ? -59.328  11.419 34.508  1.00 89.81  ? 277 GLY B CA  1 
ATOM   4637 C  C   . GLY B 1 277 ? -59.032  9.994  34.083  1.00 93.88  ? 277 GLY B C   1 
ATOM   4638 O  O   . GLY B 1 277 ? -58.113  9.746  33.299  1.00 93.80  ? 277 GLY B O   1 
ATOM   4639 N  N   . GLU B 1 278 ? -59.815  9.036  34.588  1.00 88.60  ? 278 GLU B N   1 
ATOM   4640 C  CA  . GLU B 1 278 ? -59.611  7.640  34.216  1.00 93.20  ? 278 GLU B CA  1 
ATOM   4641 C  C   . GLU B 1 278 ? -60.122  7.358  32.810  1.00 95.93  ? 278 GLU B C   1 
ATOM   4642 O  O   . GLU B 1 278 ? -59.459  6.659  32.034  1.00 98.57  ? 278 GLU B O   1 
ATOM   4643 C  CB  . GLU B 1 278 ? -60.303  6.722  35.222  1.00 92.69  ? 278 GLU B CB  1 
ATOM   4644 C  CG  . GLU B 1 278 ? -59.880  6.938  36.658  1.00 97.52  ? 278 GLU B CG  1 
ATOM   4645 C  CD  . GLU B 1 278 ? -60.823  6.271  37.637  1.00 106.37 ? 278 GLU B CD  1 
ATOM   4646 O  OE1 . GLU B 1 278 ? -61.774  5.600  37.181  1.00 107.27 ? 278 GLU B OE1 1 
ATOM   4647 O  OE2 . GLU B 1 278 ? -60.617  6.420  38.860  1.00 101.47 ? 278 GLU B OE2 1 
ATOM   4648 N  N   . ILE B 1 279 ? -61.301  7.887  32.468  1.00 95.20  ? 279 ILE B N   1 
ATOM   4649 C  CA  . ILE B 1 279 ? -61.904  7.620  31.163  1.00 89.54  ? 279 ILE B CA  1 
ATOM   4650 C  C   . ILE B 1 279 ? -60.949  8.005  30.041  1.00 89.72  ? 279 ILE B C   1 
ATOM   4651 O  O   . ILE B 1 279 ? -60.833  7.298  29.033  1.00 98.72  ? 279 ILE B O   1 
ATOM   4652 C  CB  . ILE B 1 279 ? -63.251  8.357  31.036  1.00 89.17  ? 279 ILE B CB  1 
ATOM   4653 C  CG1 . ILE B 1 279 ? -64.239  7.862  32.093  1.00 86.95  ? 279 ILE B CG1 1 
ATOM   4654 C  CG2 . ILE B 1 279 ? -63.835  8.174  29.643  1.00 91.02  ? 279 ILE B CG2 1 
ATOM   4655 C  CD1 . ILE B 1 279 ? -65.570  8.577  32.063  1.00 81.49  ? 279 ILE B CD1 1 
ATOM   4656 N  N   . TYR B 1 280 ? -60.242  9.120  30.200  1.00 90.52  ? 280 TYR B N   1 
ATOM   4657 C  CA  . TYR B 1 280 ? -59.288  9.579  29.200  1.00 93.55  ? 280 TYR B CA  1 
ATOM   4658 C  C   . TYR B 1 280 ? -57.868  9.096  29.465  1.00 96.19  ? 280 TYR B C   1 
ATOM   4659 O  O   . TYR B 1 280 ? -56.956  9.471  28.719  1.00 97.24  ? 280 TYR B O   1 
ATOM   4660 C  CB  . TYR B 1 280 ? -59.312  11.107 29.111  1.00 93.55  ? 280 TYR B CB  1 
ATOM   4661 C  CG  . TYR B 1 280 ? -60.546  11.647 28.425  1.00 89.56  ? 280 TYR B CG  1 
ATOM   4662 C  CD1 . TYR B 1 280 ? -60.613  11.724 27.040  1.00 85.24  ? 280 TYR B CD1 1 
ATOM   4663 C  CD2 . TYR B 1 280 ? -61.646  12.075 29.159  1.00 86.39  ? 280 TYR B CD2 1 
ATOM   4664 C  CE1 . TYR B 1 280 ? -61.737  12.213 26.403  1.00 85.11  ? 280 TYR B CE1 1 
ATOM   4665 C  CE2 . TYR B 1 280 ? -62.776  12.566 28.531  1.00 88.11  ? 280 TYR B CE2 1 
ATOM   4666 C  CZ  . TYR B 1 280 ? -62.815  12.633 27.152  1.00 87.21  ? 280 TYR B CZ  1 
ATOM   4667 O  OH  . TYR B 1 280 ? -63.935  13.121 26.517  1.00 83.53  ? 280 TYR B OH  1 
ATOM   4668 N  N   . GLN B 1 281 ? -57.663  8.278  30.500  1.00 99.45  ? 281 GLN B N   1 
ATOM   4669 C  CA  . GLN B 1 281 ? -56.366  7.674  30.804  1.00 100.84 ? 281 GLN B CA  1 
ATOM   4670 C  C   . GLN B 1 281 ? -55.297  8.746  31.032  1.00 99.62  ? 281 GLN B C   1 
ATOM   4671 O  O   . GLN B 1 281 ? -54.249  8.770  30.383  1.00 100.13 ? 281 GLN B O   1 
ATOM   4672 C  CB  . GLN B 1 281 ? -55.939  6.703  29.699  1.00 103.19 ? 281 GLN B CB  1 
ATOM   4673 C  CG  . GLN B 1 281 ? -56.984  5.669  29.324  1.00 104.38 ? 281 GLN B CG  1 
ATOM   4674 C  CD  . GLN B 1 281 ? -56.669  4.996  28.002  1.00 114.48 ? 281 GLN B CD  1 
ATOM   4675 O  OE1 . GLN B 1 281 ? -55.598  5.205  27.429  1.00 114.52 ? 281 GLN B OE1 1 
ATOM   4676 N  NE2 . GLN B 1 281 ? -57.601  4.190  27.506  1.00 114.43 ? 281 GLN B NE2 1 
ATOM   4677 N  N   . LEU B 1 282 ? -55.586  9.642  31.970  1.00 99.48  ? 282 LEU B N   1 
ATOM   4678 C  CA  . LEU B 1 282 ? -54.635  10.681 32.336  1.00 104.27 ? 282 LEU B CA  1 
ATOM   4679 C  C   . LEU B 1 282 ? -53.518  10.089 33.186  1.00 105.98 ? 282 LEU B C   1 
ATOM   4680 O  O   . LEU B 1 282 ? -53.779  9.332  34.127  1.00 103.14 ? 282 LEU B O   1 
ATOM   4681 C  CB  . LEU B 1 282 ? -55.334  11.807 33.100  1.00 99.54  ? 282 LEU B CB  1 
ATOM   4682 C  CG  . LEU B 1 282 ? -56.370  12.657 32.364  1.00 98.05  ? 282 LEU B CG  1 
ATOM   4683 C  CD1 . LEU B 1 282 ? -56.873  13.771 33.271  1.00 95.56  ? 282 LEU B CD1 1 
ATOM   4684 C  CD2 . LEU B 1 282 ? -55.788  13.230 31.084  1.00 94.94  ? 282 LEU B CD2 1 
ATOM   4685 N  N   . ASP B 1 283 ? -52.275  10.431 32.855  1.00 103.17 ? 283 ASP B N   1 
ATOM   4686 C  CA  . ASP B 1 283 ? -51.144  10.047 33.687  1.00 103.11 ? 283 ASP B CA  1 
ATOM   4687 C  C   . ASP B 1 283 ? -51.069  11.001 34.879  1.00 101.47 ? 283 ASP B C   1 
ATOM   4688 O  O   . ASP B 1 283 ? -51.981  11.793 35.129  1.00 103.54 ? 283 ASP B O   1 
ATOM   4689 C  CB  . ASP B 1 283 ? -49.853  10.018 32.869  1.00 99.06  ? 283 ASP B CB  1 
ATOM   4690 C  CG  . ASP B 1 283 ? -49.518  11.360 32.243  1.00 101.43 ? 283 ASP B CG  1 
ATOM   4691 O  OD1 . ASP B 1 283 ? -49.309  12.340 32.988  1.00 104.08 ? 283 ASP B OD1 1 
ATOM   4692 O  OD2 . ASP B 1 283 ? -49.442  11.431 30.998  1.00 101.55 ? 283 ASP B OD2 1 
ATOM   4693 N  N   . THR B 1 284 ? -49.967  10.943 35.628  1.00 103.29 ? 284 THR B N   1 
ATOM   4694 C  CA  . THR B 1 284 ? -49.861  11.755 36.837  1.00 106.16 ? 284 THR B CA  1 
ATOM   4695 C  C   . THR B 1 284 ? -49.689  13.235 36.507  1.00 100.82 ? 284 THR B C   1 
ATOM   4696 O  O   . THR B 1 284 ? -50.264  14.096 37.183  1.00 98.54  ? 284 THR B O   1 
ATOM   4697 C  CB  . THR B 1 284 ? -48.706  11.257 37.705  1.00 103.14 ? 284 THR B CB  1 
ATOM   4698 O  OG1 . THR B 1 284 ? -47.578  10.955 36.874  1.00 107.29 ? 284 THR B OG1 1 
ATOM   4699 C  CG2 . THR B 1 284 ? -49.118  10.010 38.476  1.00 95.05  ? 284 THR B CG2 1 
ATOM   4700 N  N   . ALA B 1 285 ? -48.903  13.552 35.475  1.00 99.52  ? 285 ALA B N   1 
ATOM   4701 C  CA  . ALA B 1 285 ? -48.691  14.952 35.117  1.00 101.42 ? 285 ALA B CA  1 
ATOM   4702 C  C   . ALA B 1 285 ? -49.954  15.572 34.534  1.00 100.45 ? 285 ALA B C   1 
ATOM   4703 O  O   . ALA B 1 285 ? -50.292  16.720 34.850  1.00 94.40  ? 285 ALA B O   1 
ATOM   4704 C  CB  . ALA B 1 285 ? -47.529  15.073 34.132  1.00 98.79  ? 285 ALA B CB  1 
ATOM   4705 N  N   . GLU B 1 286 ? -50.663  14.829 33.680  1.00 100.93 ? 286 GLU B N   1 
ATOM   4706 C  CA  . GLU B 1 286 ? -51.912  15.330 33.118  1.00 93.82  ? 286 GLU B CA  1 
ATOM   4707 C  C   . GLU B 1 286 ? -52.974  15.515 34.192  1.00 96.09  ? 286 GLU B C   1 
ATOM   4708 O  O   . GLU B 1 286 ? -53.810  16.420 34.087  1.00 96.20  ? 286 GLU B O   1 
ATOM   4709 C  CB  . GLU B 1 286 ? -52.407  14.381 32.026  1.00 97.41  ? 286 GLU B CB  1 
ATOM   4710 C  CG  . GLU B 1 286 ? -51.564  14.410 30.758  1.00 94.52  ? 286 GLU B CG  1 
ATOM   4711 C  CD  . GLU B 1 286 ? -52.028  13.407 29.724  1.00 94.80  ? 286 GLU B CD  1 
ATOM   4712 O  OE1 . GLU B 1 286 ? -52.742  12.455 30.103  1.00 97.38  ? 286 GLU B OE1 1 
ATOM   4713 O  OE2 . GLU B 1 286 ? -51.682  13.570 28.534  1.00 94.22  ? 286 GLU B OE2 1 
ATOM   4714 N  N   . ARG B 1 287 ? -52.958  14.675 35.232  1.00 96.76  ? 287 ARG B N   1 
ATOM   4715 C  CA  . ARG B 1 287 ? -53.885  14.856 36.345  1.00 94.19  ? 287 ARG B CA  1 
ATOM   4716 C  C   . ARG B 1 287 ? -53.550  16.099 37.158  1.00 90.83  ? 287 ARG B C   1 
ATOM   4717 O  O   . ARG B 1 287 ? -54.457  16.761 37.675  1.00 88.63  ? 287 ARG B O   1 
ATOM   4718 C  CB  . ARG B 1 287 ? -53.884  13.619 37.245  1.00 97.06  ? 287 ARG B CB  1 
ATOM   4719 C  CG  . ARG B 1 287 ? -54.793  12.500 36.763  1.00 98.38  ? 287 ARG B CG  1 
ATOM   4720 C  CD  . ARG B 1 287 ? -54.864  11.356 37.768  1.00 104.23 ? 287 ARG B CD  1 
ATOM   4721 N  NE  . ARG B 1 287 ? -54.022  10.228 37.386  1.00 111.26 ? 287 ARG B NE  1 
ATOM   4722 C  CZ  . ARG B 1 287 ? -52.833  9.963  37.912  1.00 108.36 ? 287 ARG B CZ  1 
ATOM   4723 N  NH1 . ARG B 1 287 ? -52.315  10.720 38.864  1.00 109.90 ? 287 ARG B NH1 1 
ATOM   4724 N  NH2 . ARG B 1 287 ? -52.150  8.909  37.473  1.00 106.76 ? 287 ARG B NH2 1 
ATOM   4725 N  N   . GLU B 1 288 ? -52.262  16.429 37.286  1.00 92.78  ? 288 GLU B N   1 
ATOM   4726 C  CA  . GLU B 1 288 ? -51.881  17.652 37.985  1.00 88.23  ? 288 GLU B CA  1 
ATOM   4727 C  C   . GLU B 1 288 ? -52.176  18.881 37.137  1.00 90.83  ? 288 GLU B C   1 
ATOM   4728 O  O   . GLU B 1 288 ? -52.543  19.936 37.668  1.00 91.23  ? 288 GLU B O   1 
ATOM   4729 C  CB  . GLU B 1 288 ? -50.401  17.604 38.366  1.00 87.69  ? 288 GLU B CB  1 
ATOM   4730 N  N   . ALA B 1 289 ? -52.017  18.765 35.816  1.00 91.21  ? 289 ALA B N   1 
ATOM   4731 C  CA  . ALA B 1 289 ? -52.380  19.862 34.925  1.00 90.10  ? 289 ALA B CA  1 
ATOM   4732 C  C   . ALA B 1 289 ? -53.871  20.157 35.007  1.00 88.80  ? 289 ALA B C   1 
ATOM   4733 O  O   . ALA B 1 289 ? -54.282  21.319 35.112  1.00 87.94  ? 289 ALA B O   1 
ATOM   4734 C  CB  . ALA B 1 289 ? -51.973  19.529 33.490  1.00 88.97  ? 289 ALA B CB  1 
ATOM   4735 N  N   . LEU B 1 290 ? -54.700  19.109 34.959  1.00 88.75  ? 290 LEU B N   1 
ATOM   4736 C  CA  . LEU B 1 290 ? -56.141  19.286 35.104  1.00 86.92  ? 290 LEU B CA  1 
ATOM   4737 C  C   . LEU B 1 290 ? -56.499  19.900 36.451  1.00 87.75  ? 290 LEU B C   1 
ATOM   4738 O  O   . LEU B 1 290 ? -57.454  20.679 36.543  1.00 90.99  ? 290 LEU B O   1 
ATOM   4739 C  CB  . LEU B 1 290 ? -56.853  17.943 34.912  1.00 87.13  ? 290 LEU B CB  1 
ATOM   4740 C  CG  . LEU B 1 290 ? -58.315  17.786 35.346  1.00 84.86  ? 290 LEU B CG  1 
ATOM   4741 C  CD1 . LEU B 1 290 ? -59.043  16.856 34.402  1.00 89.49  ? 290 LEU B CD1 1 
ATOM   4742 C  CD2 . LEU B 1 290 ? -58.416  17.250 36.770  1.00 93.56  ? 290 LEU B CD2 1 
ATOM   4743 N  N   . GLU B 1 291 ? -55.752  19.564 37.506  1.00 86.26  ? 291 GLU B N   1 
ATOM   4744 C  CA  . GLU B 1 291 ? -56.025  20.157 38.810  1.00 86.47  ? 291 GLU B CA  1 
ATOM   4745 C  C   . GLU B 1 291 ? -55.662  21.637 38.839  1.00 87.31  ? 291 GLU B C   1 
ATOM   4746 O  O   . GLU B 1 291 ? -56.342  22.428 39.503  1.00 90.01  ? 291 GLU B O   1 
ATOM   4747 C  CB  . GLU B 1 291 ? -55.275  19.395 39.903  1.00 83.30  ? 291 GLU B CB  1 
ATOM   4748 C  CG  . GLU B 1 291 ? -55.501  19.925 41.314  1.00 86.09  ? 291 GLU B CG  1 
ATOM   4749 C  CD  . GLU B 1 291 ? -56.916  19.696 41.821  1.00 90.52  ? 291 GLU B CD  1 
ATOM   4750 O  OE1 . GLU B 1 291 ? -57.651  18.890 41.213  1.00 91.29  ? 291 GLU B OE1 1 
ATOM   4751 O  OE2 . GLU B 1 291 ? -57.293  20.325 42.835  1.00 86.68  ? 291 GLU B OE2 1 
ATOM   4752 N  N   . ARG B 1 292 ? -54.603  22.034 38.130  1.00 85.83  ? 292 ARG B N   1 
ATOM   4753 C  CA  . ARG B 1 292 ? -54.290  23.455 38.022  1.00 91.33  ? 292 ARG B CA  1 
ATOM   4754 C  C   . ARG B 1 292 ? -55.355  24.191 37.219  1.00 89.74  ? 292 ARG B C   1 
ATOM   4755 O  O   . ARG B 1 292 ? -55.731  25.318 37.563  1.00 92.81  ? 292 ARG B O   1 
ATOM   4756 C  CB  . ARG B 1 292 ? -52.915  23.653 37.387  1.00 92.09  ? 292 ARG B CB  1 
ATOM   4757 C  CG  . ARG B 1 292 ? -51.749  23.288 38.286  1.00 90.14  ? 292 ARG B CG  1 
ATOM   4758 C  CD  . ARG B 1 292 ? -50.552  24.176 37.992  1.00 89.18  ? 292 ARG B CD  1 
ATOM   4759 N  NE  . ARG B 1 292 ? -50.795  25.559 38.384  1.00 86.91  ? 292 ARG B NE  1 
ATOM   4760 C  CZ  . ARG B 1 292 ? -50.009  26.579 38.066  1.00 92.83  ? 292 ARG B CZ  1 
ATOM   4761 N  NH1 . ARG B 1 292 ? -48.923  26.410 37.328  1.00 93.49  ? 292 ARG B NH1 1 
ATOM   4762 N  NH2 . ARG B 1 292 ? -50.322  27.798 38.494  1.00 87.31  ? 292 ARG B NH2 1 
ATOM   4763 N  N   . TYR B 1 293 ? -55.850  23.569 36.147  1.00 83.51  ? 293 TYR B N   1 
ATOM   4764 C  CA  . TYR B 1 293 ? -56.894  24.194 35.343  1.00 83.56  ? 293 TYR B CA  1 
ATOM   4765 C  C   . TYR B 1 293 ? -58.148  24.448 36.170  1.00 83.62  ? 293 TYR B C   1 
ATOM   4766 O  O   . TYR B 1 293 ? -58.832  25.461 35.985  1.00 80.20  ? 293 TYR B O   1 
ATOM   4767 C  CB  . TYR B 1 293 ? -57.213  23.311 34.136  1.00 83.91  ? 293 TYR B CB  1 
ATOM   4768 C  CG  . TYR B 1 293 ? -57.981  24.010 33.036  1.00 87.71  ? 293 TYR B CG  1 
ATOM   4769 C  CD1 . TYR B 1 293 ? -57.385  25.008 32.277  1.00 81.92  ? 293 TYR B CD1 1 
ATOM   4770 C  CD2 . TYR B 1 293 ? -59.296  23.660 32.746  1.00 81.43  ? 293 TYR B CD2 1 
ATOM   4771 C  CE1 . TYR B 1 293 ? -58.076  25.647 31.271  1.00 86.00  ? 293 TYR B CE1 1 
ATOM   4772 C  CE2 . TYR B 1 293 ? -59.996  24.296 31.738  1.00 82.98  ? 293 TYR B CE2 1 
ATOM   4773 C  CZ  . TYR B 1 293 ? -59.380  25.288 31.003  1.00 87.40  ? 293 TYR B CZ  1 
ATOM   4774 O  OH  . TYR B 1 293 ? -60.067  25.928 29.997  1.00 81.32  ? 293 TYR B OH  1 
ATOM   4775 N  N   . ARG B 1 294 ? -58.454  23.547 37.104  1.00 84.18  ? 294 ARG B N   1 
ATOM   4776 C  CA  . ARG B 1 294 ? -59.683  23.660 37.880  1.00 83.07  ? 294 ARG B CA  1 
ATOM   4777 C  C   . ARG B 1 294 ? -59.581  24.741 38.951  1.00 85.77  ? 294 ARG B C   1 
ATOM   4778 O  O   . ARG B 1 294 ? -60.550  25.469 39.196  1.00 82.03  ? 294 ARG B O   1 
ATOM   4779 C  CB  . ARG B 1 294 ? -60.018  22.311 38.515  1.00 80.55  ? 294 ARG B CB  1 
ATOM   4780 C  CG  . ARG B 1 294 ? -61.319  22.292 39.290  1.00 82.28  ? 294 ARG B CG  1 
ATOM   4781 C  CD  . ARG B 1 294 ? -61.468  20.995 40.060  1.00 85.52  ? 294 ARG B CD  1 
ATOM   4782 N  NE  . ARG B 1 294 ? -60.434  20.844 41.076  1.00 87.05  ? 294 ARG B NE  1 
ATOM   4783 C  CZ  . ARG B 1 294 ? -60.590  21.168 42.352  1.00 89.81  ? 294 ARG B CZ  1 
ATOM   4784 N  NH1 . ARG B 1 294 ? -61.732  21.657 42.804  1.00 86.95  ? 294 ARG B NH1 1 
ATOM   4785 N  NH2 . ARG B 1 294 ? -59.575  20.995 43.194  1.00 86.13  ? 294 ARG B NH2 1 
ATOM   4786 N  N   . THR B 1 295 ? -58.424  24.866 39.595  1.00 84.67  ? 295 THR B N   1 
ATOM   4787 C  CA  . THR B 1 295 ? -58.296  25.797 40.706  1.00 86.64  ? 295 THR B CA  1 
ATOM   4788 C  C   . THR B 1 295 ? -57.731  27.148 40.289  1.00 84.53  ? 295 THR B C   1 
ATOM   4789 O  O   . THR B 1 295 ? -58.093  28.169 40.885  1.00 88.52  ? 295 THR B O   1 
ATOM   4790 C  CB  . THR B 1 295 ? -57.412  25.192 41.802  1.00 91.44  ? 295 THR B CB  1 
ATOM   4791 O  OG1 . THR B 1 295 ? -56.094  24.965 41.289  1.00 95.51  ? 295 THR B OG1 1 
ATOM   4792 C  CG2 . THR B 1 295 ? -57.995  23.871 42.284  1.00 83.64  ? 295 THR B CG2 1 
ATOM   4793 N  N   . ASP B 1 296 ? -56.857  27.185 39.282  1.00 81.64  ? 296 ASP B N   1 
ATOM   4794 C  CA  . ASP B 1 296 ? -56.210  28.428 38.884  1.00 87.52  ? 296 ASP B CA  1 
ATOM   4795 C  C   . ASP B 1 296 ? -56.845  29.088 37.667  1.00 86.49  ? 296 ASP B C   1 
ATOM   4796 O  O   . ASP B 1 296 ? -56.587  30.272 37.425  1.00 84.00  ? 296 ASP B O   1 
ATOM   4797 C  CB  . ASP B 1 296 ? -54.721  28.190 38.600  1.00 87.45  ? 296 ASP B CB  1 
ATOM   4798 C  CG  . ASP B 1 296 ? -53.937  27.837 39.851  1.00 92.26  ? 296 ASP B CG  1 
ATOM   4799 O  OD1 . ASP B 1 296 ? -54.372  28.221 40.958  1.00 89.45  ? 296 ASP B OD1 1 
ATOM   4800 O  OD2 . ASP B 1 296 ? -52.882  27.179 39.725  1.00 93.94  ? 296 ASP B OD2 1 
ATOM   4801 N  N   . ALA B 1 297 ? -57.663  28.366 36.902  1.00 86.59  ? 297 ALA B N   1 
ATOM   4802 C  CA  . ALA B 1 297 ? -58.312  28.923 35.722  1.00 81.15  ? 297 ALA B CA  1 
ATOM   4803 C  C   . ALA B 1 297 ? -59.827  28.989 35.872  1.00 77.71  ? 297 ALA B C   1 
ATOM   4804 O  O   . ALA B 1 297 ? -60.410  30.073 35.782  1.00 80.18  ? 297 ALA B O   1 
ATOM   4805 C  CB  . ALA B 1 297 ? -57.933  28.107 34.477  1.00 79.67  ? 297 ALA B CB  1 
ATOM   4806 N  N   . VAL B 1 298 ? -60.484  27.854 36.112  1.00 72.70  ? 298 VAL B N   1 
ATOM   4807 C  CA  . VAL B 1 298 ? -61.943  27.821 36.083  1.00 74.20  ? 298 VAL B CA  1 
ATOM   4808 C  C   . VAL B 1 298 ? -62.536  28.391 37.369  1.00 78.62  ? 298 VAL B C   1 
ATOM   4809 O  O   . VAL B 1 298 ? -63.537  29.114 37.334  1.00 78.87  ? 298 VAL B O   1 
ATOM   4810 C  CB  . VAL B 1 298 ? -62.428  26.386 35.816  1.00 74.38  ? 298 VAL B CB  1 
ATOM   4811 C  CG1 . VAL B 1 298 ? -63.943  26.348 35.709  1.00 73.18  ? 298 VAL B CG1 1 
ATOM   4812 C  CG2 . VAL B 1 298 ? -61.787  25.842 34.547  1.00 76.26  ? 298 VAL B CG2 1 
ATOM   4813 N  N   . ARG B 1 299 ? -61.942  28.076 38.522  1.00 80.27  ? 299 ARG B N   1 
ATOM   4814 C  CA  . ARG B 1 299 ? -62.462  28.610 39.777  1.00 73.02  ? 299 ARG B CA  1 
ATOM   4815 C  C   . ARG B 1 299 ? -62.188  30.103 39.902  1.00 76.97  ? 299 ARG B C   1 
ATOM   4816 O  O   . ARG B 1 299 ? -63.049  30.862 40.362  1.00 73.65  ? 299 ARG B O   1 
ATOM   4817 C  CB  . ARG B 1 299 ? -61.859  27.854 40.958  1.00 78.36  ? 299 ARG B CB  1 
ATOM   4818 C  CG  . ARG B 1 299 ? -62.691  26.673 41.408  1.00 80.18  ? 299 ARG B CG  1 
ATOM   4819 C  CD  . ARG B 1 299 ? -61.874  25.703 42.237  1.00 82.61  ? 299 ARG B CD  1 
ATOM   4820 N  NE  . ARG B 1 299 ? -62.732  24.741 42.913  1.00 81.35  ? 299 ARG B NE  1 
ATOM   4821 C  CZ  . ARG B 1 299 ? -63.072  24.819 44.191  1.00 73.30  ? 299 ARG B CZ  1 
ATOM   4822 N  NH1 . ARG B 1 299 ? -62.596  25.774 44.972  1.00 79.81  ? 299 ARG B NH1 1 
ATOM   4823 N  NH2 . ARG B 1 299 ? -63.910  23.920 44.696  1.00 64.66  ? 299 ARG B NH2 1 
ATOM   4824 N  N   . THR B 1 300 ? -60.998  30.543 39.489  1.00 79.46  ? 300 THR B N   1 
ATOM   4825 C  CA  . THR B 1 300 ? -60.644  31.951 39.623  1.00 78.53  ? 300 THR B CA  1 
ATOM   4826 C  C   . THR B 1 300 ? -61.464  32.840 38.695  1.00 77.15  ? 300 THR B C   1 
ATOM   4827 O  O   . THR B 1 300 ? -61.761  33.986 39.050  1.00 81.50  ? 300 THR B O   1 
ATOM   4828 C  CB  . THR B 1 300 ? -59.154  32.147 39.353  1.00 80.51  ? 300 THR B CB  1 
ATOM   4829 O  OG1 . THR B 1 300 ? -58.829  31.614 38.064  1.00 81.73  ? 300 THR B OG1 1 
ATOM   4830 C  CG2 . THR B 1 300 ? -58.326  31.441 40.413  1.00 78.74  ? 300 THR B CG2 1 
ATOM   4831 N  N   . VAL B 1 301 ? -61.839  32.346 37.512  1.00 74.63  ? 301 VAL B N   1 
ATOM   4832 C  CA  . VAL B 1 301 ? -62.622  33.184 36.607  1.00 74.33  ? 301 VAL B CA  1 
ATOM   4833 C  C   . VAL B 1 301 ? -64.036  33.375 37.144  1.00 76.36  ? 301 VAL B C   1 
ATOM   4834 O  O   . VAL B 1 301 ? -64.674  34.403 36.884  1.00 77.69  ? 301 VAL B O   1 
ATOM   4835 C  CB  . VAL B 1 301 ? -62.621  32.603 35.177  1.00 72.15  ? 301 VAL B CB  1 
ATOM   4836 C  CG1 . VAL B 1 301 ? -63.469  31.346 35.088  1.00 76.33  ? 301 VAL B CG1 1 
ATOM   4837 C  CG2 . VAL B 1 301 ? -63.107  33.641 34.178  1.00 71.64  ? 301 VAL B CG2 1 
ATOM   4838 N  N   . ILE B 1 302 ? -64.542  32.413 37.915  1.00 76.64  ? 302 ILE B N   1 
ATOM   4839 C  CA  . ILE B 1 302 ? -65.856  32.564 38.530  1.00 74.41  ? 302 ILE B CA  1 
ATOM   4840 C  C   . ILE B 1 302 ? -65.772  33.462 39.756  1.00 76.79  ? 302 ILE B C   1 
ATOM   4841 O  O   . ILE B 1 302 ? -66.464  34.482 39.852  1.00 81.92  ? 302 ILE B O   1 
ATOM   4842 C  CB  . ILE B 1 302 ? -66.446  31.188 38.885  1.00 75.48  ? 302 ILE B CB  1 
ATOM   4843 C  CG1 . ILE B 1 302 ? -66.727  30.383 37.616  1.00 72.09  ? 302 ILE B CG1 1 
ATOM   4844 C  CG2 . ILE B 1 302 ? -67.709  31.349 39.720  1.00 73.01  ? 302 ILE B CG2 1 
ATOM   4845 C  CD1 . ILE B 1 302 ? -67.243  28.987 37.883  1.00 77.70  ? 302 ILE B CD1 1 
ATOM   4846 N  N   . ARG B 1 303 ? -64.911  33.096 40.708  1.00 81.77  ? 303 ARG B N   1 
ATOM   4847 C  CA  . ARG B 1 303 ? -64.836  33.831 41.966  1.00 80.76  ? 303 ARG B CA  1 
ATOM   4848 C  C   . ARG B 1 303 ? -64.272  35.232 41.765  1.00 79.39  ? 303 ARG B C   1 
ATOM   4849 O  O   . ARG B 1 303 ? -64.736  36.189 42.396  1.00 78.11  ? 303 ARG B O   1 
ATOM   4850 C  CB  . ARG B 1 303 ? -63.992  33.053 42.975  1.00 76.13  ? 303 ARG B CB  1 
ATOM   4851 C  CG  . ARG B 1 303 ? -63.756  33.792 44.278  1.00 80.19  ? 303 ARG B CG  1 
ATOM   4852 C  CD  . ARG B 1 303 ? -65.049  33.978 45.050  1.00 78.12  ? 303 ARG B CD  1 
ATOM   4853 N  NE  . ARG B 1 303 ? -64.891  34.927 46.144  1.00 81.11  ? 303 ARG B NE  1 
ATOM   4854 C  CZ  . ARG B 1 303 ? -65.706  35.014 47.186  1.00 81.48  ? 303 ARG B CZ  1 
ATOM   4855 N  NH1 . ARG B 1 303 ? -66.738  34.197 47.327  1.00 82.41  ? 303 ARG B NH1 1 
ATOM   4856 N  NH2 . ARG B 1 303 ? -65.477  35.939 48.112  1.00 75.70  ? 303 ARG B NH2 1 
ATOM   4857 N  N   . GLY B 1 304 ? -63.274  35.373 40.889  1.00 76.36  ? 304 GLY B N   1 
ATOM   4858 C  CA  . GLY B 1 304 ? -62.648  36.672 40.697  1.00 76.06  ? 304 GLY B CA  1 
ATOM   4859 C  C   . GLY B 1 304 ? -63.607  37.718 40.161  1.00 78.42  ? 304 GLY B C   1 
ATOM   4860 O  O   . GLY B 1 304 ? -63.515  38.898 40.511  1.00 78.16  ? 304 GLY B O   1 
ATOM   4861 N  N   . SER B 1 305 ? -64.539  37.301 39.304  1.00 79.54  ? 305 SER B N   1 
ATOM   4862 C  CA  . SER B 1 305 ? -65.524  38.236 38.775  1.00 81.75  ? 305 SER B CA  1 
ATOM   4863 C  C   . SER B 1 305 ? -66.454  38.732 39.872  1.00 84.12  ? 305 SER B C   1 
ATOM   4864 O  O   . SER B 1 305 ? -66.866  39.898 39.867  1.00 86.64  ? 305 SER B O   1 
ATOM   4865 C  CB  . SER B 1 305 ? -66.322  37.570 37.656  1.00 82.31  ? 305 SER B CB  1 
ATOM   4866 O  OG  . SER B 1 305 ? -67.254  38.467 37.079  1.00 88.07  ? 305 SER B OG  1 
ATOM   4867 N  N   . TYR B 1 306 ? -66.790  37.860 40.825  1.00 84.94  ? 306 TYR B N   1 
ATOM   4868 C  CA  . TYR B 1 306 ? -67.706  38.239 41.895  1.00 81.58  ? 306 TYR B CA  1 
ATOM   4869 C  C   . TYR B 1 306 ? -67.062  39.238 42.848  1.00 84.34  ? 306 TYR B C   1 
ATOM   4870 O  O   . TYR B 1 306 ? -67.705  40.210 43.262  1.00 89.44  ? 306 TYR B O   1 
ATOM   4871 C  CB  . TYR B 1 306 ? -68.170  36.989 42.641  1.00 78.96  ? 306 TYR B CB  1 
ATOM   4872 C  CG  . TYR B 1 306 ? -68.957  37.261 43.902  1.00 83.95  ? 306 TYR B CG  1 
ATOM   4873 C  CD1 . TYR B 1 306 ? -70.273  37.701 43.844  1.00 82.35  ? 306 TYR B CD1 1 
ATOM   4874 C  CD2 . TYR B 1 306 ? -68.387  37.059 45.154  1.00 83.58  ? 306 TYR B CD2 1 
ATOM   4875 C  CE1 . TYR B 1 306 ? -70.997  37.941 44.997  1.00 84.54  ? 306 TYR B CE1 1 
ATOM   4876 C  CE2 . TYR B 1 306 ? -69.102  37.297 46.310  1.00 84.25  ? 306 TYR B CE2 1 
ATOM   4877 C  CZ  . TYR B 1 306 ? -70.405  37.737 46.226  1.00 88.17  ? 306 TYR B CZ  1 
ATOM   4878 O  OH  . TYR B 1 306 ? -71.116  37.974 47.379  1.00 92.19  ? 306 TYR B OH  1 
ATOM   4879 N  N   . ASP B 1 307 ? -65.794  39.018 43.205  1.00 84.13  ? 307 ASP B N   1 
ATOM   4880 C  CA  . ASP B 1 307 ? -65.095  39.959 44.076  1.00 85.87  ? 307 ASP B CA  1 
ATOM   4881 C  C   . ASP B 1 307 ? -64.958  41.323 43.411  1.00 87.92  ? 307 ASP B C   1 
ATOM   4882 O  O   . ASP B 1 307 ? -65.212  42.361 44.032  1.00 90.81  ? 307 ASP B O   1 
ATOM   4883 C  CB  . ASP B 1 307 ? -63.716  39.408 44.447  1.00 87.69  ? 307 ASP B CB  1 
ATOM   4884 C  CG  . ASP B 1 307 ? -63.793  38.148 45.288  1.00 85.80  ? 307 ASP B CG  1 
ATOM   4885 O  OD1 . ASP B 1 307 ? -64.718  38.040 46.121  1.00 80.29  ? 307 ASP B OD1 1 
ATOM   4886 O  OD2 . ASP B 1 307 ? -62.923  37.267 45.117  1.00 87.74  ? 307 ASP B OD2 1 
ATOM   4887 N  N   . TRP B 1 308 ? -64.564  41.335 42.136  1.00 89.63  ? 308 TRP B N   1 
ATOM   4888 C  CA  . TRP B 1 308 ? -64.313  42.591 41.438  1.00 88.35  ? 308 TRP B CA  1 
ATOM   4889 C  C   . TRP B 1 308 ? -65.603  43.370 41.205  1.00 90.16  ? 308 TRP B C   1 
ATOM   4890 O  O   . TRP B 1 308 ? -65.606  44.605 41.262  1.00 95.00  ? 308 TRP B O   1 
ATOM   4891 C  CB  . TRP B 1 308 ? -63.598  42.304 40.119  1.00 84.29  ? 308 TRP B CB  1 
ATOM   4892 C  CG  . TRP B 1 308 ? -63.347  43.505 39.263  1.00 86.57  ? 308 TRP B CG  1 
ATOM   4893 C  CD1 . TRP B 1 308 ? -62.341  44.415 39.400  1.00 86.23  ? 308 TRP B CD1 1 
ATOM   4894 C  CD2 . TRP B 1 308 ? -64.102  43.911 38.115  1.00 84.14  ? 308 TRP B CD2 1 
ATOM   4895 N  NE1 . TRP B 1 308 ? -62.428  45.370 38.415  1.00 82.81  ? 308 TRP B NE1 1 
ATOM   4896 C  CE2 . TRP B 1 308 ? -63.502  45.083 37.613  1.00 86.48  ? 308 TRP B CE2 1 
ATOM   4897 C  CE3 . TRP B 1 308 ? -65.232  43.401 37.466  1.00 84.32  ? 308 TRP B CE3 1 
ATOM   4898 C  CZ2 . TRP B 1 308 ? -63.993  45.754 36.492  1.00 84.83  ? 308 TRP B CZ2 1 
ATOM   4899 C  CZ3 . TRP B 1 308 ? -65.717  44.067 36.353  1.00 82.59  ? 308 TRP B CZ3 1 
ATOM   4900 C  CH2 . TRP B 1 308 ? -65.098  45.230 35.878  1.00 81.46  ? 308 TRP B CH2 1 
ATOM   4901 N  N   . HIS B 1 309 ? -66.710  42.670 40.943  1.00 86.85  ? 309 HIS B N   1 
ATOM   4902 C  CA  . HIS B 1 309 ? -67.984  43.355 40.748  1.00 86.81  ? 309 HIS B CA  1 
ATOM   4903 C  C   . HIS B 1 309 ? -68.496  43.977 42.042  1.00 93.40  ? 309 HIS B C   1 
ATOM   4904 O  O   . HIS B 1 309 ? -69.180  45.005 42.003  1.00 97.13  ? 309 HIS B O   1 
ATOM   4905 C  CB  . HIS B 1 309 ? -69.022  42.389 40.173  1.00 86.62  ? 309 HIS B CB  1 
ATOM   4906 C  CG  . HIS B 1 309 ? -68.953  42.238 38.684  1.00 89.93  ? 309 HIS B CG  1 
ATOM   4907 N  ND1 . HIS B 1 309 ? -69.013  41.012 38.056  1.00 90.13  ? 309 HIS B ND1 1 
ATOM   4908 C  CD2 . HIS B 1 309 ? -68.842  43.159 37.698  1.00 86.60  ? 309 HIS B CD2 1 
ATOM   4909 C  CE1 . HIS B 1 309 ? -68.935  41.184 36.748  1.00 84.97  ? 309 HIS B CE1 1 
ATOM   4910 N  NE2 . HIS B 1 309 ? -68.830  42.478 36.504  1.00 85.95  ? 309 HIS B NE2 1 
ATOM   4911 N  N   . ARG B 1 310 ? -68.178  43.378 43.193  1.00 96.61  ? 310 ARG B N   1 
ATOM   4912 C  CA  . ARG B 1 310 ? -68.612  43.954 44.462  1.00 102.65 ? 310 ARG B CA  1 
ATOM   4913 C  C   . ARG B 1 310 ? -67.750  45.145 44.863  1.00 105.58 ? 310 ARG B C   1 
ATOM   4914 O  O   . ARG B 1 310 ? -68.253  46.103 45.461  1.00 113.05 ? 310 ARG B O   1 
ATOM   4915 C  CB  . ARG B 1 310 ? -68.592  42.893 45.567  1.00 96.14  ? 310 ARG B CB  1 
ATOM   4916 C  CG  . ARG B 1 310 ? -69.660  41.817 45.430  1.00 98.48  ? 310 ARG B CG  1 
ATOM   4917 C  CD  . ARG B 1 310 ? -70.230  41.418 46.788  1.00 100.81 ? 310 ARG B CD  1 
ATOM   4918 N  NE  . ARG B 1 310 ? -71.554  41.989 47.016  1.00 105.80 ? 310 ARG B NE  1 
ATOM   4919 C  CZ  . ARG B 1 310 ? -72.242  41.873 48.145  1.00 110.57 ? 310 ARG B CZ  1 
ATOM   4920 N  NH1 . ARG B 1 310 ? -71.752  41.225 49.191  1.00 105.96 ? 310 ARG B NH1 1 
ATOM   4921 N  NH2 . ARG B 1 310 ? -73.451  42.421 48.228  1.00 106.61 ? 310 ARG B NH2 1 
ATOM   4922 N  N   . SER B 1 311 ? -66.459  45.105 44.546  1.00 106.33 ? 311 SER B N   1 
ATOM   4923 C  CA  . SER B 1 311 ? -65.554  46.199 44.883  1.00 108.33 ? 311 SER B CA  1 
ATOM   4924 C  C   . SER B 1 311 ? -65.865  47.439 44.046  1.00 108.15 ? 311 SER B C   1 
ATOM   4925 O  O   . SER B 1 311 ? -66.363  48.441 44.561  1.00 103.70 ? 311 SER B O   1 
ATOM   4926 C  CB  . SER B 1 311 ? -64.097  45.777 44.679  1.00 104.37 ? 311 SER B CB  1 
ATOM   4927 O  OG  . SER B 1 311 ? -63.802  45.610 43.302  1.00 97.86  ? 311 SER B OG  1 
HETATM 4928 P  PA  . FDF C 2 .   ? -76.735  13.956 6.665   1.00 115.41 ? 401 FDF A PA  1 
HETATM 4929 P  PB  . FDF C 2 .   ? -77.413  11.433 5.528   1.00 117.15 ? 401 FDF A PB  1 
HETATM 4930 C  C1  . FDF C 2 .   ? -78.308  14.295 8.697   1.00 104.30 ? 401 FDF A C1  1 
HETATM 4931 O  O1  . FDF C 2 .   ? -77.366  13.446 8.055   1.00 103.51 ? 401 FDF A O1  1 
HETATM 4932 O  O1A . FDF C 2 .   ? -75.229  13.863 6.762   1.00 106.66 ? 401 FDF A O1A 1 
HETATM 4933 O  O1B . FDF C 2 .   ? -76.959  10.956 6.887   1.00 113.55 ? 401 FDF A O1B 1 
HETATM 4934 C  C2  . FDF C 2 .   ? -79.732  13.952 8.308   1.00 99.40  ? 401 FDF A C2  1 
HETATM 4935 O  O2A . FDF C 2 .   ? -77.154  15.393 6.447   1.00 109.76 ? 401 FDF A O2A 1 
HETATM 4936 O  O2B . FDF C 2 .   ? -76.550  10.801 4.459   1.00 118.11 ? 401 FDF A O2B 1 
HETATM 4937 C  C3  . FDF C 2 .   ? -80.769  14.705 8.733   1.00 93.39  ? 401 FDF A C3  1 
HETATM 4938 O  O3A . FDF C 2 .   ? -77.260  13.041 5.442   1.00 119.04 ? 401 FDF A O3A 1 
HETATM 4939 O  O3B . FDF C 2 .   ? -78.860  11.052 5.319   1.00 109.13 ? 401 FDF A O3B 1 
HETATM 4940 C  C4  . FDF C 2 .   ? -80.505  15.908 9.614   1.00 84.50  ? 401 FDF A C4  1 
HETATM 4941 C  C5  . FDF C 2 .   ? -82.169  14.295 8.305   1.00 83.86  ? 401 FDF A C5  1 
HETATM 4942 C  C6  . FDF C 2 .   ? -83.171  14.767 9.350   1.00 82.26  ? 401 FDF A C6  1 
HETATM 4943 C  C7  . FDF C 2 .   ? -83.265  13.841 10.546  1.00 85.79  ? 401 FDF A C7  1 
HETATM 4944 C  C8  . FDF C 2 .   ? -83.782  14.218 11.742  1.00 81.55  ? 401 FDF A C8  1 
HETATM 4945 C  C9  . FDF C 2 .   ? -83.786  13.134 12.810  1.00 85.30  ? 401 FDF A C9  1 
HETATM 4946 C  C10 . FDF C 2 .   ? -84.305  15.629 11.954  1.00 81.79  ? 401 FDF A C10 1 
HETATM 4947 C  C11 . FDF C 2 .   ? -82.830  11.976 12.543  1.00 87.27  ? 401 FDF A C11 1 
HETATM 4948 C  C12 . FDF C 2 .   ? -81.612  12.019 13.433  1.00 87.75  ? 401 FDF A C12 1 
HETATM 4949 C  C13 . FDF C 2 .   ? -80.396  11.773 12.911  1.00 92.63  ? 401 FDF A C13 1 
HETATM 4950 C  C14 . FDF C 2 .   ? -80.252  11.462 11.425  1.00 98.64  ? 401 FDF A C14 1 
HETATM 4951 C  C15 . FDF C 2 .   ? -79.224  11.834 13.870  1.00 98.05  ? 401 FDF A C15 1 
HETATM 4952 F  F1  . FDF C 2 .   ? -78.044  11.414 13.313  1.00 108.84 ? 401 FDF A F1  1 
HETATM 4953 F  F2  . FDF C 2 .   ? -79.017  10.990 11.069  1.00 104.63 ? 401 FDF A F2  1 
HETATM 4954 MG MG  . MG  D 3 .   ? -78.065  14.355 3.442   1.00 94.93  ? 402 MG  A MG  1 
HETATM 4955 MG MG  . MG  E 3 .   ? -77.296  17.849 4.792   1.00 100.73 ? 403 MG  A MG  1 
HETATM 4956 MG MG  . MG  F 3 .   ? -73.695  12.061 6.700   1.00 104.46 ? 404 MG  A MG  1 
HETATM 4957 O  O   . HOH G 4 .   ? -88.940  -2.667 11.991  1.00 85.47  ? 501 HOH A O   1 
HETATM 4958 O  O   . HOH G 4 .   ? -67.663  23.642 -2.550  1.00 98.82  ? 502 HOH A O   1 
HETATM 4959 O  O   . HOH G 4 .   ? -84.139  30.302 7.563   1.00 75.32  ? 503 HOH A O   1 
HETATM 4960 O  O   . HOH G 4 .   ? -89.666  31.137 12.282  1.00 73.75  ? 504 HOH A O   1 
HETATM 4961 O  O   . HOH G 4 .   ? -88.360  9.216  -1.818  1.00 67.49  ? 505 HOH A O   1 
HETATM 4962 O  O   . HOH G 4 .   ? -81.960  22.509 16.645  1.00 68.16  ? 506 HOH A O   1 
HETATM 4963 O  O   . HOH G 4 .   ? -68.650  17.727 24.458  1.00 78.93  ? 507 HOH A O   1 
HETATM 4964 O  O   . HOH G 4 .   ? -92.098  12.246 -4.897  1.00 75.59  ? 508 HOH A O   1 
HETATM 4965 O  O   . HOH G 4 .   ? -94.627  9.319  7.141   1.00 63.83  ? 509 HOH A O   1 
HETATM 4966 O  O   . HOH G 4 .   ? -79.810  22.135 26.837  1.00 73.37  ? 510 HOH A O   1 
HETATM 4967 O  O   . HOH G 4 .   ? -99.904  7.842  6.960   1.00 61.42  ? 511 HOH A O   1 
HETATM 4968 O  O   . HOH G 4 .   ? -84.746  30.152 9.886   1.00 72.16  ? 512 HOH A O   1 
HETATM 4969 O  O   . HOH G 4 .   ? -100.269 26.702 7.275   1.00 72.18  ? 513 HOH A O   1 
HETATM 4970 O  O   . HOH G 4 .   ? -95.593  20.299 39.721  1.00 78.01  ? 514 HOH A O   1 
HETATM 4971 O  O   . HOH G 4 .   ? -92.091  19.264 15.295  1.00 60.41  ? 515 HOH A O   1 
HETATM 4972 O  O   . HOH G 4 .   ? -89.721  1.442  8.490   1.00 61.14  ? 516 HOH A O   1 
HETATM 4973 O  O   . HOH G 4 .   ? -101.472 12.294 18.529  1.00 71.46  ? 517 HOH A O   1 
HETATM 4974 O  O   . HOH G 4 .   ? -79.883  19.047 16.656  1.00 74.38  ? 518 HOH A O   1 
HETATM 4975 O  O   . HOH G 4 .   ? -76.469  17.775 2.515   1.00 89.86  ? 519 HOH A O   1 
HETATM 4976 O  O   . HOH G 4 .   ? -99.666  24.986 22.795  1.00 69.88  ? 520 HOH A O   1 
HETATM 4977 O  O   . HOH G 4 .   ? -87.190  9.518  0.938   1.00 65.82  ? 521 HOH A O   1 
HETATM 4978 O  O   . HOH G 4 .   ? -95.785  5.745  -10.394 1.00 63.73  ? 522 HOH A O   1 
HETATM 4979 O  O   . HOH G 4 .   ? -72.231  16.967 7.518   1.00 83.30  ? 523 HOH A O   1 
HETATM 4980 O  O   . HOH G 4 .   ? -76.628  -2.938 25.699  1.00 83.82  ? 524 HOH A O   1 
HETATM 4981 O  O   . HOH G 4 .   ? -101.858 7.972  20.399  1.00 68.15  ? 525 HOH A O   1 
HETATM 4982 O  O   . HOH G 4 .   ? -103.859 24.330 16.349  1.00 81.69  ? 526 HOH A O   1 
HETATM 4983 O  O   . HOH G 4 .   ? -75.552  15.454 2.865   1.00 99.33  ? 527 HOH A O   1 
HETATM 4984 O  O   . HOH G 4 .   ? -85.845  26.516 40.957  1.00 69.94  ? 528 HOH A O   1 
HETATM 4985 O  O   . HOH G 4 .   ? -99.125  34.373 3.931   1.00 72.39  ? 529 HOH A O   1 
HETATM 4986 O  O   . HOH G 4 .   ? -66.995  25.749 9.041   1.00 89.11  ? 530 HOH A O   1 
HETATM 4987 O  O   . HOH G 4 .   ? -80.004  22.516 24.506  1.00 68.49  ? 531 HOH A O   1 
HETATM 4988 O  O   . HOH H 4 .   ? -68.123  51.027 27.656  1.00 81.16  ? 401 HOH B O   1 
HETATM 4989 O  O   . HOH H 4 .   ? -52.290  47.308 30.957  1.00 79.43  ? 402 HOH B O   1 
HETATM 4990 O  O   . HOH H 4 .   ? -66.686  33.348 26.448  1.00 67.17  ? 403 HOH B O   1 
HETATM 4991 O  O   . HOH H 4 .   ? -69.009  49.989 6.593   1.00 81.94  ? 404 HOH B O   1 
HETATM 4992 O  O   . HOH H 4 .   ? -57.593  27.348 24.218  1.00 78.23  ? 405 HOH B O   1 
HETATM 4993 O  O   . HOH H 4 .   ? -64.971  50.763 12.397  1.00 77.34  ? 406 HOH B O   1 
HETATM 4994 O  O   . HOH H 4 .   ? -67.116  55.532 32.054  1.00 83.31  ? 407 HOH B O   1 
HETATM 4995 O  O   . HOH H 4 .   ? -47.812  8.421  35.924  1.00 94.81  ? 408 HOH B O   1 
HETATM 4996 O  O   . HOH H 4 .   ? -73.194  44.658 29.754  1.00 88.32  ? 409 HOH B O   1 
HETATM 4997 O  O   . HOH H 4 .   ? -89.462  45.180 39.893  1.00 74.26  ? 410 HOH B O   1 
HETATM 4998 O  O   . HOH H 4 .   ? -85.012  30.612 26.771  1.00 69.66  ? 411 HOH B O   1 
HETATM 4999 O  O   . HOH H 4 .   ? -65.800  49.353 28.250  1.00 75.92  ? 412 HOH B O   1 
HETATM 5000 O  O   . HOH H 4 .   ? -44.755  29.554 20.768  1.00 82.58  ? 413 HOH B O   1 
HETATM 5001 O  O   . HOH H 4 .   ? -75.317  42.262 26.499  1.00 86.47  ? 414 HOH B O   1 
HETATM 5002 O  O   . HOH H 4 .   ? -61.362  33.725 50.355  1.00 79.23  ? 415 HOH B O   1 
HETATM 5003 O  O   . HOH H 4 .   ? -58.165  8.509  26.303  1.00 86.43  ? 416 HOH B O   1 
HETATM 5004 O  O   . HOH H 4 .   ? -47.075  24.937 27.593  1.00 85.93  ? 417 HOH B O   1 
HETATM 5005 O  O   . HOH H 4 .   ? -71.713  50.798 6.460   1.00 84.38  ? 418 HOH B O   1 
HETATM 5006 O  O   . HOH H 4 .   ? -65.785  49.537 34.184  1.00 72.13  ? 419 HOH B O   1 
HETATM 5007 O  O   . HOH H 4 .   ? -56.546  48.401 39.462  1.00 75.96  ? 420 HOH B O   1 
HETATM 5008 O  O   . HOH H 4 .   ? -84.894  28.443 38.840  1.00 77.69  ? 421 HOH B O   1 
HETATM 5009 O  O   . HOH H 4 .   ? -64.826  53.452 34.580  1.00 78.32  ? 422 HOH B O   1 
HETATM 5010 O  O   . HOH H 4 .   ? -71.424  53.461 6.549   1.00 79.48  ? 423 HOH B O   1 
# 
