data_9GO2
# 
_entry.id   9GO2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9GO2         pdb_00009go2 10.2210/pdb9go2/pdb 
WWPDB D_1292141216 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GO2 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              joerg.standfuss@psi.ch 
_pdbx_contact_author.name_first         Joerg 
_pdbx_contact_author.name_last          Standfuss 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8825-386X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mulder, M.'     1 0009-0003-2988-2780 
'Weinert, T.'    2 0000-0002-0339-3722 
'Skopintsev, P.' 3 ?                   
'Bruenle, S.'    4 ?                   
'Broser, M.'     5 ?                   
'Hegemann, P.'   6 ?                   
'Standfuss, J.'  7 ?                   
# 
_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            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                1282 
_citation.page_last                 1290 
_citation.title                     'Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c15402 
_citation.pdbx_database_id_PubMed   39680650 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mulder, M.'       1  ?                   
primary 'Hwang, S.'        2  0000-0003-4323-1450 
primary 'Broser, M.'       3  0000-0002-7133-4548 
primary 'Brunle, S.'       4  ?                   
primary 'Skopintsev, P.'   5  ?                   
primary 'Schattenberg, C.' 6  0009-0005-1509-0445 
primary 'Schnick, C.'      7  ?                   
primary 'Hartmann, S.'     8  ?                   
primary 'Church, J.'       9  0000-0001-5986-1305 
primary 'Schapiro, I.'     10 0000-0001-8536-6869 
primary 'Dworkowski, F.'   11 ?                   
primary 'Weinert, T.'      12 ?                   
primary 'Hegemann, P.'     13 0000-0003-3589-6452 
primary 'Sun, H.'          14 0000-0002-1655-0838 
primary 'Standfuss, J.'    15 ?                   
# 
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 'Archaeal-type opsin 1,Archaeal-type opsin 2'    37441.984 1 ? ? ? ? 
2 non-polymer nat '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 356.540   9 ? ? ? ? 
3 non-polymer syn RETINAL                                          284.436   1 ? ? ? ? 
4 water       nat water                                            18.015    7 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Channelopsin-1,Retinal binding protein,Sensory opsin B' 
# 
_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       
;STGSDATVPVATQDGPDYVFHRAHERMLFQTSYTLENNGSVICIPNNGQCFCLAWLKSNGTNAEKLAANILQWITFALSA
LCLMFYGYQTWKSTCGWEEIYVATIEMIKFIIEYFHEFDEPAVIYSSNGNKTVWLRYAEWLLTCPVILIHLSNLTGLAND
YNKRTMGLLVSDIGTIVWGTTAALSKGYVRVIFFLMGLCYGIYTFFNAAKVYIEAYHTVPKGRCRQVVTGMAWLFFVSWG
MFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTKLNIGGTEIEVETLVEDEA
EAGAVSSEDLYFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STGSDATVPVATQDGPDYVFHRAHERMLFQTSYTLENNGSVICIPNNGQCFCLAWLKSNGTNAEKLAANILQWITFALSA
LCLMFYGYQTWKSTCGWEEIYVATIEMIKFIIEYFHEFDEPAVIYSSNGNKTVWLRYAEWLLTCPVILIHLSNLTGLAND
YNKRTMGLLVSDIGTIVWGTTAALSKGYVRVIFFLMGLCYGIYTFFNAAKVYIEAYHTVPKGRCRQVVTGMAWLFFVSWG
MFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTKLNIGGTEIEVETLVEDEA
EAGAVSSEDLYFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' OLC 
3 RETINAL                                          RET 
4 water                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   THR n 
1 3   GLY n 
1 4   SER n 
1 5   ASP n 
1 6   ALA n 
1 7   THR n 
1 8   VAL n 
1 9   PRO n 
1 10  VAL n 
1 11  ALA n 
1 12  THR n 
1 13  GLN n 
1 14  ASP n 
1 15  GLY n 
1 16  PRO n 
1 17  ASP n 
1 18  TYR n 
1 19  VAL n 
1 20  PHE n 
1 21  HIS n 
1 22  ARG n 
1 23  ALA n 
1 24  HIS n 
1 25  GLU n 
1 26  ARG n 
1 27  MET n 
1 28  LEU n 
1 29  PHE n 
1 30  GLN n 
1 31  THR n 
1 32  SER n 
1 33  TYR n 
1 34  THR n 
1 35  LEU n 
1 36  GLU n 
1 37  ASN n 
1 38  ASN n 
1 39  GLY n 
1 40  SER n 
1 41  VAL n 
1 42  ILE n 
1 43  CYS n 
1 44  ILE n 
1 45  PRO n 
1 46  ASN n 
1 47  ASN n 
1 48  GLY n 
1 49  GLN n 
1 50  CYS n 
1 51  PHE n 
1 52  CYS n 
1 53  LEU n 
1 54  ALA n 
1 55  TRP n 
1 56  LEU n 
1 57  LYS n 
1 58  SER n 
1 59  ASN n 
1 60  GLY n 
1 61  THR n 
1 62  ASN n 
1 63  ALA n 
1 64  GLU n 
1 65  LYS n 
1 66  LEU n 
1 67  ALA n 
1 68  ALA n 
1 69  ASN n 
1 70  ILE n 
1 71  LEU n 
1 72  GLN n 
1 73  TRP n 
1 74  ILE n 
1 75  THR n 
1 76  PHE n 
1 77  ALA n 
1 78  LEU n 
1 79  SER n 
1 80  ALA n 
1 81  LEU n 
1 82  CYS n 
1 83  LEU n 
1 84  MET n 
1 85  PHE n 
1 86  TYR n 
1 87  GLY n 
1 88  TYR n 
1 89  GLN n 
1 90  THR n 
1 91  TRP n 
1 92  LYS n 
1 93  SER n 
1 94  THR n 
1 95  CYS n 
1 96  GLY n 
1 97  TRP n 
1 98  GLU n 
1 99  GLU n 
1 100 ILE n 
1 101 TYR n 
1 102 VAL n 
1 103 ALA n 
1 104 THR n 
1 105 ILE n 
1 106 GLU n 
1 107 MET n 
1 108 ILE n 
1 109 LYS n 
1 110 PHE n 
1 111 ILE n 
1 112 ILE n 
1 113 GLU n 
1 114 TYR n 
1 115 PHE n 
1 116 HIS n 
1 117 GLU n 
1 118 PHE n 
1 119 ASP n 
1 120 GLU n 
1 121 PRO n 
1 122 ALA n 
1 123 VAL n 
1 124 ILE n 
1 125 TYR n 
1 126 SER n 
1 127 SER n 
1 128 ASN n 
1 129 GLY n 
1 130 ASN n 
1 131 LYS n 
1 132 THR n 
1 133 VAL n 
1 134 TRP n 
1 135 LEU n 
1 136 ARG n 
1 137 TYR n 
1 138 ALA n 
1 139 GLU n 
1 140 TRP n 
1 141 LEU n 
1 142 LEU n 
1 143 THR n 
1 144 CYS n 
1 145 PRO n 
1 146 VAL n 
1 147 ILE n 
1 148 LEU n 
1 149 ILE n 
1 150 HIS n 
1 151 LEU n 
1 152 SER n 
1 153 ASN n 
1 154 LEU n 
1 155 THR n 
1 156 GLY n 
1 157 LEU n 
1 158 ALA n 
1 159 ASN n 
1 160 ASP n 
1 161 TYR n 
1 162 ASN n 
1 163 LYS n 
1 164 ARG n 
1 165 THR n 
1 166 MET n 
1 167 GLY n 
1 168 LEU n 
1 169 LEU n 
1 170 VAL n 
1 171 SER n 
1 172 ASP n 
1 173 ILE n 
1 174 GLY n 
1 175 THR n 
1 176 ILE n 
1 177 VAL n 
1 178 TRP n 
1 179 GLY n 
1 180 THR n 
1 181 THR n 
1 182 ALA n 
1 183 ALA n 
1 184 LEU n 
1 185 SER n 
1 186 LYS n 
1 187 GLY n 
1 188 TYR n 
1 189 VAL n 
1 190 ARG n 
1 191 VAL n 
1 192 ILE n 
1 193 PHE n 
1 194 PHE n 
1 195 LEU n 
1 196 MET n 
1 197 GLY n 
1 198 LEU n 
1 199 CYS n 
1 200 TYR n 
1 201 GLY n 
1 202 ILE n 
1 203 TYR n 
1 204 THR n 
1 205 PHE n 
1 206 PHE n 
1 207 ASN n 
1 208 ALA n 
1 209 ALA n 
1 210 LYS n 
1 211 VAL n 
1 212 TYR n 
1 213 ILE n 
1 214 GLU n 
1 215 ALA n 
1 216 TYR n 
1 217 HIS n 
1 218 THR n 
1 219 VAL n 
1 220 PRO n 
1 221 LYS n 
1 222 GLY n 
1 223 ARG n 
1 224 CYS n 
1 225 ARG n 
1 226 GLN n 
1 227 VAL n 
1 228 VAL n 
1 229 THR n 
1 230 GLY n 
1 231 MET n 
1 232 ALA n 
1 233 TRP n 
1 234 LEU n 
1 235 PHE n 
1 236 PHE n 
1 237 VAL n 
1 238 SER n 
1 239 TRP n 
1 240 GLY n 
1 241 MET n 
1 242 PHE n 
1 243 PRO n 
1 244 ILE n 
1 245 LEU n 
1 246 PHE n 
1 247 ILE n 
1 248 LEU n 
1 249 GLY n 
1 250 PRO n 
1 251 GLU n 
1 252 GLY n 
1 253 PHE n 
1 254 GLY n 
1 255 VAL n 
1 256 LEU n 
1 257 SER n 
1 258 VAL n 
1 259 TYR n 
1 260 GLY n 
1 261 SER n 
1 262 THR n 
1 263 VAL n 
1 264 GLY n 
1 265 HIS n 
1 266 THR n 
1 267 ILE n 
1 268 ILE n 
1 269 ASP n 
1 270 LEU n 
1 271 MET n 
1 272 SER n 
1 273 LYS n 
1 274 ASN n 
1 275 CYS n 
1 276 TRP n 
1 277 GLY n 
1 278 LEU n 
1 279 LEU n 
1 280 GLY n 
1 281 HIS n 
1 282 TYR n 
1 283 LEU n 
1 284 ARG n 
1 285 VAL n 
1 286 LEU n 
1 287 ILE n 
1 288 HIS n 
1 289 GLU n 
1 290 HIS n 
1 291 ILE n 
1 292 LEU n 
1 293 ILE n 
1 294 HIS n 
1 295 GLY n 
1 296 ASP n 
1 297 ILE n 
1 298 ARG n 
1 299 LYS n 
1 300 THR n 
1 301 THR n 
1 302 LYS n 
1 303 LEU n 
1 304 ASN n 
1 305 ILE n 
1 306 GLY n 
1 307 GLY n 
1 308 THR n 
1 309 GLU n 
1 310 ILE n 
1 311 GLU n 
1 312 VAL n 
1 313 GLU n 
1 314 THR n 
1 315 LEU n 
1 316 VAL n 
1 317 GLU n 
1 318 ASP n 
1 319 GLU n 
1 320 ALA n 
1 321 GLU n 
1 322 ALA n 
1 323 GLY n 
1 324 ALA n 
1 325 VAL n 
1 326 SER n 
1 327 SER n 
1 328 GLU n 
1 329 ASP n 
1 330 LEU n 
1 331 TYR n 
1 332 PHE n 
1 333 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   222 'Chlamydomonas smithii' ? acop1                                  ? ? ? ? ? ? 
'Chlamydomonas reinhardtii' 3055 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 223 333 'Chlamydomonas smithii' ? 'cop4, acop2, CSOB, CHLRE_02g085257v5' ? ? ? ? ? ? 
'Chlamydomonas reinhardtii' 3055 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 1-Oleoyl-R-glycerol 'C21 H40 O4'     356.540 
PHE 'L-peptide linking' y PHENYLALANINE                                    ?                   'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                          ?                   'C5 H9 N O2'     115.130 
RET non-polymer         . RETINAL                                          ?                   'C20 H28 O'      284.436 
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   SER 1   331 ?   ?   ?   A . n 
A 1 2   THR 2   332 ?   ?   ?   A . n 
A 1 3   GLY 3   333 ?   ?   ?   A . n 
A 1 4   SER 4   334 ?   ?   ?   A . n 
A 1 5   ASP 5   335 ?   ?   ?   A . n 
A 1 6   ALA 6   336 ?   ?   ?   A . n 
A 1 7   THR 7   337 ?   ?   ?   A . n 
A 1 8   VAL 8   338 ?   ?   ?   A . n 
A 1 9   PRO 9   339 ?   ?   ?   A . n 
A 1 10  VAL 10  340 ?   ?   ?   A . n 
A 1 11  ALA 11  341 ?   ?   ?   A . n 
A 1 12  THR 12  342 ?   ?   ?   A . n 
A 1 13  GLN 13  343 ?   ?   ?   A . n 
A 1 14  ASP 14  344 ?   ?   ?   A . n 
A 1 15  GLY 15  345 ?   ?   ?   A . n 
A 1 16  PRO 16  346 ?   ?   ?   A . n 
A 1 17  ASP 17  347 ?   ?   ?   A . n 
A 1 18  TYR 18  348 ?   ?   ?   A . n 
A 1 19  VAL 19  349 ?   ?   ?   A . n 
A 1 20  PHE 20  350 ?   ?   ?   A . n 
A 1 21  HIS 21  351 ?   ?   ?   A . n 
A 1 22  ARG 22  352 ?   ?   ?   A . n 
A 1 23  ALA 23  353 ?   ?   ?   A . n 
A 1 24  HIS 24  354 ?   ?   ?   A . n 
A 1 25  GLU 25  355 ?   ?   ?   A . n 
A 1 26  ARG 26  356 ?   ?   ?   A . n 
A 1 27  MET 27  357 50  MET MET A . n 
A 1 28  LEU 28  358 51  LEU LEU A . n 
A 1 29  PHE 29  359 52  PHE PHE A . n 
A 1 30  GLN 30  360 53  GLN GLN A . n 
A 1 31  THR 31  361 54  THR THR A . n 
A 1 32  SER 32  362 55  SER SER A . n 
A 1 33  TYR 33  363 56  TYR TYR A . n 
A 1 34  THR 34  364 57  THR THR A . n 
A 1 35  LEU 35  365 58  LEU LEU A . n 
A 1 36  GLU 36  366 59  GLU GLU A . n 
A 1 37  ASN 37  367 60  ASN ASN A . n 
A 1 38  ASN 38  368 61  ASN ASN A . n 
A 1 39  GLY 39  369 62  GLY GLY A . n 
A 1 40  SER 40  370 63  SER SER A . n 
A 1 41  VAL 41  371 64  VAL VAL A . n 
A 1 42  ILE 42  372 65  ILE ILE A . n 
A 1 43  CYS 43  373 66  CYS CYS A . n 
A 1 44  ILE 44  374 67  ILE ILE A . n 
A 1 45  PRO 45  375 68  PRO PRO A . n 
A 1 46  ASN 46  376 69  ASN ASN A . n 
A 1 47  ASN 47  377 70  ASN ASN A . n 
A 1 48  GLY 48  378 71  GLY GLY A . n 
A 1 49  GLN 49  379 72  GLN GLN A . n 
A 1 50  CYS 50  380 73  CYS CYS A . n 
A 1 51  PHE 51  381 74  PHE PHE A . n 
A 1 52  CYS 52  382 75  CYS CYS A . n 
A 1 53  LEU 53  383 76  LEU LEU A . n 
A 1 54  ALA 54  384 77  ALA ALA A . n 
A 1 55  TRP 55  385 78  TRP TRP A . n 
A 1 56  LEU 56  386 79  LEU LEU A . n 
A 1 57  LYS 57  387 80  LYS LYS A . n 
A 1 58  SER 58  388 81  SER SER A . n 
A 1 59  ASN 59  389 82  ASN ASN A . n 
A 1 60  GLY 60  390 83  GLY GLY A . n 
A 1 61  THR 61  391 84  THR THR A . n 
A 1 62  ASN 62  392 85  ASN ASN A . n 
A 1 63  ALA 63  393 86  ALA ALA A . n 
A 1 64  GLU 64  394 87  GLU GLU A . n 
A 1 65  LYS 65  395 88  LYS LYS A . n 
A 1 66  LEU 66  396 89  LEU LEU A . n 
A 1 67  ALA 67  397 90  ALA ALA A . n 
A 1 68  ALA 68  398 91  ALA ALA A . n 
A 1 69  ASN 69  399 92  ASN ASN A . n 
A 1 70  ILE 70  400 93  ILE ILE A . n 
A 1 71  LEU 71  401 94  LEU LEU A . n 
A 1 72  GLN 72  402 95  GLN GLN A . n 
A 1 73  TRP 73  403 96  TRP TRP A . n 
A 1 74  ILE 74  404 97  ILE ILE A . n 
A 1 75  THR 75  405 98  THR THR A . n 
A 1 76  PHE 76  406 99  PHE PHE A . n 
A 1 77  ALA 77  407 100 ALA ALA A . n 
A 1 78  LEU 78  408 101 LEU LEU A . n 
A 1 79  SER 79  409 102 SER SER A . n 
A 1 80  ALA 80  410 103 ALA ALA A . n 
A 1 81  LEU 81  411 104 LEU LEU A . n 
A 1 82  CYS 82  412 105 CYS CYS A . n 
A 1 83  LEU 83  413 106 LEU LEU A . n 
A 1 84  MET 84  414 107 MET MET A . n 
A 1 85  PHE 85  415 108 PHE PHE A . n 
A 1 86  TYR 86  416 109 TYR TYR A . n 
A 1 87  GLY 87  417 110 GLY GLY A . n 
A 1 88  TYR 88  418 111 TYR TYR A . n 
A 1 89  GLN 89  419 ?   ?   ?   A . n 
A 1 90  THR 90  420 ?   ?   ?   A . n 
A 1 91  TRP 91  421 ?   ?   ?   A . n 
A 1 92  LYS 92  422 ?   ?   ?   A . n 
A 1 93  SER 93  423 ?   ?   ?   A . n 
A 1 94  THR 94  424 ?   ?   ?   A . n 
A 1 95  CYS 95  425 118 CYS CYS A . n 
A 1 96  GLY 96  426 119 GLY GLY A . n 
A 1 97  TRP 97  427 120 TRP TRP A . n 
A 1 98  GLU 98  428 121 GLU GLU A . n 
A 1 99  GLU 99  429 122 GLU GLU A . n 
A 1 100 ILE 100 430 123 ILE ILE A . n 
A 1 101 TYR 101 431 124 TYR TYR A . n 
A 1 102 VAL 102 432 125 VAL VAL A . n 
A 1 103 ALA 103 433 126 ALA ALA A . n 
A 1 104 THR 104 434 127 THR THR A . n 
A 1 105 ILE 105 435 128 ILE ILE A . n 
A 1 106 GLU 106 436 129 GLU GLU A . n 
A 1 107 MET 107 437 130 MET MET A . n 
A 1 108 ILE 108 438 131 ILE ILE A . n 
A 1 109 LYS 109 439 132 LYS LYS A . n 
A 1 110 PHE 110 440 133 PHE PHE A . n 
A 1 111 ILE 111 441 134 ILE ILE A . n 
A 1 112 ILE 112 442 135 ILE ILE A . n 
A 1 113 GLU 113 443 136 GLU GLU A . n 
A 1 114 TYR 114 444 137 TYR TYR A . n 
A 1 115 PHE 115 445 138 PHE PHE A . n 
A 1 116 HIS 116 446 139 HIS HIS A . n 
A 1 117 GLU 117 447 140 GLU GLU A . n 
A 1 118 PHE 118 448 141 PHE PHE A . n 
A 1 119 ASP 119 449 142 ASP ASP A . n 
A 1 120 GLU 120 450 143 GLU GLU A . n 
A 1 121 PRO 121 451 144 PRO PRO A . n 
A 1 122 ALA 122 452 145 ALA ALA A . n 
A 1 123 VAL 123 453 146 VAL VAL A . n 
A 1 124 ILE 124 454 147 ILE ILE A . n 
A 1 125 TYR 125 455 148 TYR TYR A . n 
A 1 126 SER 126 456 149 SER SER A . n 
A 1 127 SER 127 457 150 SER SER A . n 
A 1 128 ASN 128 458 151 ASN ASN A . n 
A 1 129 GLY 129 459 152 GLY GLY A . n 
A 1 130 ASN 130 460 153 ASN ASN A . n 
A 1 131 LYS 131 461 154 LYS LYS A . n 
A 1 132 THR 132 462 155 THR THR A . n 
A 1 133 VAL 133 463 156 VAL VAL A . n 
A 1 134 TRP 134 464 157 TRP TRP A . n 
A 1 135 LEU 135 465 158 LEU LEU A . n 
A 1 136 ARG 136 466 159 ARG ARG A . n 
A 1 137 TYR 137 467 160 TYR TYR A . n 
A 1 138 ALA 138 468 161 ALA ALA A . n 
A 1 139 GLU 139 469 162 GLU GLU A . n 
A 1 140 TRP 140 470 163 TRP TRP A . n 
A 1 141 LEU 141 471 164 LEU LEU A . n 
A 1 142 LEU 142 472 165 LEU LEU A . n 
A 1 143 THR 143 473 166 THR THR A . n 
A 1 144 CYS 144 474 167 CYS CYS A . n 
A 1 145 PRO 145 475 168 PRO PRO A . n 
A 1 146 VAL 146 476 169 VAL VAL A . n 
A 1 147 ILE 147 477 170 ILE ILE A . n 
A 1 148 LEU 148 478 171 LEU LEU A . n 
A 1 149 ILE 149 479 172 ILE ILE A . n 
A 1 150 HIS 150 480 173 HIS HIS A . n 
A 1 151 LEU 151 481 174 LEU LEU A . n 
A 1 152 SER 152 482 175 SER SER A . n 
A 1 153 ASN 153 483 176 ASN ASN A . n 
A 1 154 LEU 154 484 177 LEU LEU A . n 
A 1 155 THR 155 485 178 THR THR A . n 
A 1 156 GLY 156 486 179 GLY GLY A . n 
A 1 157 LEU 157 487 180 LEU LEU A . n 
A 1 158 ALA 158 488 181 ALA ALA A . n 
A 1 159 ASN 159 489 182 ASN ASN A . n 
A 1 160 ASP 160 490 183 ASP ASP A . n 
A 1 161 TYR 161 491 184 TYR TYR A . n 
A 1 162 ASN 162 492 185 ASN ASN A . n 
A 1 163 LYS 163 493 186 LYS LYS A . n 
A 1 164 ARG 164 494 187 ARG ARG A . n 
A 1 165 THR 165 495 188 THR THR A . n 
A 1 166 MET 166 496 189 MET MET A . n 
A 1 167 GLY 167 497 190 GLY GLY A . n 
A 1 168 LEU 168 498 191 LEU LEU A . n 
A 1 169 LEU 169 499 192 LEU LEU A . n 
A 1 170 VAL 170 500 193 VAL VAL A . n 
A 1 171 SER 171 501 194 SER SER A . n 
A 1 172 ASP 172 502 195 ASP ASP A . n 
A 1 173 ILE 173 503 196 ILE ILE A . n 
A 1 174 GLY 174 504 197 GLY GLY A . n 
A 1 175 THR 175 505 198 THR THR A . n 
A 1 176 ILE 176 506 199 ILE ILE A . n 
A 1 177 VAL 177 507 200 VAL VAL A . n 
A 1 178 TRP 178 508 201 TRP TRP A . n 
A 1 179 GLY 179 509 202 GLY GLY A . n 
A 1 180 THR 180 510 203 THR THR A . n 
A 1 181 THR 181 511 204 THR THR A . n 
A 1 182 ALA 182 512 205 ALA ALA A . n 
A 1 183 ALA 183 513 206 ALA ALA A . n 
A 1 184 LEU 184 514 207 LEU LEU A . n 
A 1 185 SER 185 515 208 SER SER A . n 
A 1 186 LYS 186 516 209 LYS LYS A . n 
A 1 187 GLY 187 517 210 GLY GLY A . n 
A 1 188 TYR 188 518 211 TYR TYR A . n 
A 1 189 VAL 189 519 212 VAL VAL A . n 
A 1 190 ARG 190 520 213 ARG ARG A . n 
A 1 191 VAL 191 521 214 VAL VAL A . n 
A 1 192 ILE 192 522 215 ILE ILE A . n 
A 1 193 PHE 193 523 216 PHE PHE A . n 
A 1 194 PHE 194 524 217 PHE PHE A . n 
A 1 195 LEU 195 525 218 LEU LEU A . n 
A 1 196 MET 196 526 219 MET MET A . n 
A 1 197 GLY 197 527 220 GLY GLY A . n 
A 1 198 LEU 198 528 221 LEU LEU A . n 
A 1 199 CYS 199 529 222 CYS CYS A . n 
A 1 200 TYR 200 530 223 TYR TYR A . n 
A 1 201 GLY 201 531 224 GLY GLY A . n 
A 1 202 ILE 202 532 225 ILE ILE A . n 
A 1 203 TYR 203 533 226 TYR TYR A . n 
A 1 204 THR 204 534 227 THR THR A . n 
A 1 205 PHE 205 535 228 PHE PHE A . n 
A 1 206 PHE 206 536 229 PHE PHE A . n 
A 1 207 ASN 207 537 230 ASN ASN A . n 
A 1 208 ALA 208 538 231 ALA ALA A . n 
A 1 209 ALA 209 539 232 ALA ALA A . n 
A 1 210 LYS 210 540 233 LYS LYS A . n 
A 1 211 VAL 211 541 234 VAL VAL A . n 
A 1 212 TYR 212 542 235 TYR TYR A . n 
A 1 213 ILE 213 543 236 ILE ILE A . n 
A 1 214 GLU 214 544 237 GLU GLU A . n 
A 1 215 ALA 215 545 238 ALA ALA A . n 
A 1 216 TYR 216 546 239 TYR TYR A . n 
A 1 217 HIS 217 547 240 HIS HIS A . n 
A 1 218 THR 218 548 241 THR THR A . n 
A 1 219 VAL 219 549 242 VAL VAL A . n 
A 1 220 PRO 220 550 243 PRO PRO A . n 
A 1 221 LYS 221 551 244 LYS LYS A . n 
A 1 222 GLY 222 552 245 GLY GLY A . n 
A 1 223 ARG 223 553 246 ARG ARG A . n 
A 1 224 CYS 224 554 247 CYS CYS A . n 
A 1 225 ARG 225 555 248 ARG ARG A . n 
A 1 226 GLN 226 556 249 GLN GLN A . n 
A 1 227 VAL 227 557 250 VAL VAL A . n 
A 1 228 VAL 228 558 251 VAL VAL A . n 
A 1 229 THR 229 559 252 THR THR A . n 
A 1 230 GLY 230 560 253 GLY GLY A . n 
A 1 231 MET 231 561 254 MET MET A . n 
A 1 232 ALA 232 562 255 ALA ALA A . n 
A 1 233 TRP 233 563 256 TRP TRP A . n 
A 1 234 LEU 234 564 257 LEU LEU A . n 
A 1 235 PHE 235 565 258 PHE PHE A . n 
A 1 236 PHE 236 566 259 PHE PHE A . n 
A 1 237 VAL 237 567 260 VAL VAL A . n 
A 1 238 SER 238 568 261 SER SER A . n 
A 1 239 TRP 239 569 262 TRP TRP A . n 
A 1 240 GLY 240 570 263 GLY GLY A . n 
A 1 241 MET 241 571 264 MET MET A . n 
A 1 242 PHE 242 572 265 PHE PHE A . n 
A 1 243 PRO 243 573 266 PRO PRO A . n 
A 1 244 ILE 244 574 267 ILE ILE A . n 
A 1 245 LEU 245 575 268 LEU LEU A . n 
A 1 246 PHE 246 576 269 PHE PHE A . n 
A 1 247 ILE 247 577 270 ILE ILE A . n 
A 1 248 LEU 248 578 271 LEU LEU A . n 
A 1 249 GLY 249 579 272 GLY GLY A . n 
A 1 250 PRO 250 580 273 PRO PRO A . n 
A 1 251 GLU 251 581 274 GLU GLU A . n 
A 1 252 GLY 252 582 275 GLY GLY A . n 
A 1 253 PHE 253 583 276 PHE PHE A . n 
A 1 254 GLY 254 584 277 GLY GLY A . n 
A 1 255 VAL 255 585 278 VAL VAL A . n 
A 1 256 LEU 256 586 279 LEU LEU A . n 
A 1 257 SER 257 587 280 SER SER A . n 
A 1 258 VAL 258 588 281 VAL VAL A . n 
A 1 259 TYR 259 589 282 TYR TYR A . n 
A 1 260 GLY 260 590 283 GLY GLY A . n 
A 1 261 SER 261 591 284 SER SER A . n 
A 1 262 THR 262 592 285 THR THR A . n 
A 1 263 VAL 263 593 286 VAL VAL A . n 
A 1 264 GLY 264 594 287 GLY GLY A . n 
A 1 265 HIS 265 595 288 HIS HIS A . n 
A 1 266 THR 266 596 289 THR THR A . n 
A 1 267 ILE 267 597 290 ILE ILE A . n 
A 1 268 ILE 268 598 291 ILE ILE A . n 
A 1 269 ASP 269 599 292 ASP ASP A . n 
A 1 270 LEU 270 600 293 LEU LEU A . n 
A 1 271 MET 271 601 294 MET MET A . n 
A 1 272 SER 272 602 295 SER SER A . n 
A 1 273 LYS 273 603 296 LYS LYR A . n 
A 1 274 ASN 274 604 297 ASN ASN A . n 
A 1 275 CYS 275 605 298 CYS CYS A . n 
A 1 276 TRP 276 606 299 TRP TRP A . n 
A 1 277 GLY 277 607 300 GLY GLY A . n 
A 1 278 LEU 278 608 301 LEU LEU A . n 
A 1 279 LEU 279 609 302 LEU LEU A . n 
A 1 280 GLY 280 610 303 GLY GLY A . n 
A 1 281 HIS 281 611 304 HIS HIS A . n 
A 1 282 TYR 282 612 305 TYR TYR A . n 
A 1 283 LEU 283 613 306 LEU LEU A . n 
A 1 284 ARG 284 614 307 ARG ARG A . n 
A 1 285 VAL 285 615 308 VAL VAL A . n 
A 1 286 LEU 286 616 309 LEU LEU A . n 
A 1 287 ILE 287 617 310 ILE ILE A . n 
A 1 288 HIS 288 618 311 HIS HIS A . n 
A 1 289 GLU 289 619 312 GLU GLU A . n 
A 1 290 HIS 290 620 313 HIS HIS A . n 
A 1 291 ILE 291 621 314 ILE ILE A . n 
A 1 292 LEU 292 622 315 LEU LEU A . n 
A 1 293 ILE 293 623 316 ILE ILE A . n 
A 1 294 HIS 294 624 317 HIS HIS A . n 
A 1 295 GLY 295 625 318 GLY GLY A . n 
A 1 296 ASP 296 626 319 ASP ASP A . n 
A 1 297 ILE 297 627 320 ILE ILE A . n 
A 1 298 ARG 298 628 321 ARG ARG A . n 
A 1 299 LYS 299 629 322 LYS LYS A . n 
A 1 300 THR 300 630 323 THR THR A . n 
A 1 301 THR 301 631 324 THR THR A . n 
A 1 302 LYS 302 632 325 LYS LYS A . n 
A 1 303 LEU 303 633 326 LEU LEU A . n 
A 1 304 ASN 304 634 327 ASN ASN A . n 
A 1 305 ILE 305 635 ?   ?   ?   A . n 
A 1 306 GLY 306 636 ?   ?   ?   A . n 
A 1 307 GLY 307 637 ?   ?   ?   A . n 
A 1 308 THR 308 638 331 THR THR A . n 
A 1 309 GLU 309 639 332 GLU GLU A . n 
A 1 310 ILE 310 640 333 ILE ILE A . n 
A 1 311 GLU 311 641 334 GLU GLU A . n 
A 1 312 VAL 312 642 335 VAL VAL A . n 
A 1 313 GLU 313 643 336 GLU GLU A . n 
A 1 314 THR 314 644 337 THR THR A . n 
A 1 315 LEU 315 645 338 LEU LEU A . n 
A 1 316 VAL 316 646 339 VAL VAL A . n 
A 1 317 GLU 317 647 340 GLU GLU A . n 
A 1 318 ASP 318 648 341 ASP ASP A . n 
A 1 319 GLU 319 649 342 GLU GLU A . n 
A 1 320 ALA 320 650 343 ALA ALA A . n 
A 1 321 GLU 321 651 344 GLU GLU A . n 
A 1 322 ALA 322 652 345 ALA ALA A . n 
A 1 323 GLY 323 653 346 GLY GLY A . n 
A 1 324 ALA 324 654 347 ALA ALA A . n 
A 1 325 VAL 325 655 348 VAL VAL A . n 
A 1 326 SER 326 656 349 SER SER A . n 
A 1 327 SER 327 657 350 SER SER A . n 
A 1 328 GLU 328 658 351 GLU GLU A . n 
A 1 329 ASP 329 659 352 ASP ASP A . n 
A 1 330 LEU 330 660 ?   ?   ?   A . n 
A 1 331 TYR 331 661 ?   ?   ?   A . n 
A 1 332 PHE 332 662 ?   ?   ?   A . n 
A 1 333 GLN 333 663 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        RET 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RET 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 OLC 1 701 402 OLC OLC A . 
C 2 OLC 1 702 403 OLC OLC A . 
D 2 OLC 1 703 404 OLC OLC A . 
E 2 OLC 1 704 405 OLC OLC A . 
F 2 OLC 1 705 406 OLC OLC A . 
G 2 OLC 1 706 407 OLC OLC A . 
H 2 OLC 1 707 408 OLC OLC A . 
I 2 OLC 1 708 409 OLC OLC A . 
J 2 OLC 1 709 410 OLC OLC A . 
K 3 RET 1 710 296 RET LYR A . 
L 4 HOH 1 801 2   HOH HOH A . 
L 4 HOH 2 802 3   HOH HOH A . 
L 4 HOH 3 803 4   HOH HOH A . 
L 4 HOH 4 804 6   HOH HOH A . 
L 4 HOH 5 805 14  HOH HOH A . 
L 4 HOH 6 806 9   HOH HOH A . 
L 4 HOH 7 807 10  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A MET 357 ? CG  ? A MET 27  CG  
2   1 Y 1 A MET 357 ? SD  ? A MET 27  SD  
3   1 Y 1 A MET 357 ? CE  ? A MET 27  CE  
4   1 Y 1 A CYS 425 ? SG  ? A CYS 95  SG  
5   1 Y 1 A LYS 493 ? CG  ? A LYS 163 CG  
6   1 Y 1 A LYS 493 ? CD  ? A LYS 163 CD  
7   1 Y 1 A LYS 493 ? CE  ? A LYS 163 CE  
8   1 Y 1 A LYS 493 ? NZ  ? A LYS 163 NZ  
9   1 Y 1 A LYS 551 ? CG  ? A LYS 221 CG  
10  1 Y 1 A LYS 551 ? CD  ? A LYS 221 CD  
11  1 Y 1 A LYS 551 ? CE  ? A LYS 221 CE  
12  1 Y 1 A LYS 551 ? NZ  ? A LYS 221 NZ  
13  1 Y 1 A ASN 634 ? CG  ? A ASN 304 CG  
14  1 Y 1 A ASN 634 ? OD1 ? A ASN 304 OD1 
15  1 Y 1 A ASN 634 ? ND2 ? A ASN 304 ND2 
16  1 Y 1 A THR 638 ? OG1 ? A THR 308 OG1 
17  1 Y 1 A THR 638 ? CG2 ? A THR 308 CG2 
18  1 Y 1 A GLU 639 ? CG  ? A GLU 309 CG  
19  1 Y 1 A GLU 639 ? CD  ? A GLU 309 CD  
20  1 Y 1 A GLU 639 ? OE1 ? A GLU 309 OE1 
21  1 Y 1 A GLU 639 ? OE2 ? A GLU 309 OE2 
22  1 Y 1 A GLU 649 ? CG  ? A GLU 319 CG  
23  1 Y 1 A GLU 649 ? CD  ? A GLU 319 CD  
24  1 Y 1 A GLU 649 ? OE1 ? A GLU 319 OE1 
25  1 Y 1 A GLU 649 ? OE2 ? A GLU 319 OE2 
26  1 N 1 A OLC 702 ? C18 ? C OLC 1   C18 
27  1 N 1 A OLC 702 ? C17 ? C OLC 1   C17 
28  1 N 1 A OLC 702 ? C24 ? C OLC 1   C24 
29  1 N 1 A OLC 702 ? C16 ? C OLC 1   C16 
30  1 N 1 A OLC 702 ? C15 ? C OLC 1   C15 
31  1 N 1 A OLC 702 ? C21 ? C OLC 1   C21 
32  1 N 1 A OLC 702 ? C22 ? C OLC 1   C22 
33  1 N 1 A OLC 702 ? O25 ? C OLC 1   O25 
34  1 N 1 A OLC 702 ? O23 ? C OLC 1   O23 
35  1 N 1 A OLC 703 ? C18 ? D OLC 1   C18 
36  1 N 1 A OLC 703 ? C10 ? D OLC 1   C10 
37  1 N 1 A OLC 703 ? C9  ? D OLC 1   C9  
38  1 N 1 A OLC 703 ? C17 ? D OLC 1   C17 
39  1 N 1 A OLC 703 ? C11 ? D OLC 1   C11 
40  1 N 1 A OLC 703 ? C8  ? D OLC 1   C8  
41  1 N 1 A OLC 703 ? C16 ? D OLC 1   C16 
42  1 N 1 A OLC 703 ? C12 ? D OLC 1   C12 
43  1 N 1 A OLC 703 ? C15 ? D OLC 1   C15 
44  1 N 1 A OLC 703 ? C13 ? D OLC 1   C13 
45  1 N 1 A OLC 703 ? C14 ? D OLC 1   C14 
46  1 N 1 A OLC 704 ? C18 ? E OLC 1   C18 
47  1 N 1 A OLC 704 ? C10 ? E OLC 1   C10 
48  1 N 1 A OLC 704 ? C17 ? E OLC 1   C17 
49  1 N 1 A OLC 704 ? C11 ? E OLC 1   C11 
50  1 N 1 A OLC 704 ? C16 ? E OLC 1   C16 
51  1 N 1 A OLC 704 ? C12 ? E OLC 1   C12 
52  1 N 1 A OLC 704 ? C15 ? E OLC 1   C15 
53  1 N 1 A OLC 704 ? C13 ? E OLC 1   C13 
54  1 N 1 A OLC 704 ? C14 ? E OLC 1   C14 
55  1 N 1 A OLC 705 ? C18 ? F OLC 1   C18 
56  1 N 1 A OLC 705 ? C17 ? F OLC 1   C17 
57  1 N 1 A OLC 705 ? C16 ? F OLC 1   C16 
58  1 N 1 A OLC 705 ? C12 ? F OLC 1   C12 
59  1 N 1 A OLC 705 ? C15 ? F OLC 1   C15 
60  1 N 1 A OLC 705 ? C13 ? F OLC 1   C13 
61  1 N 1 A OLC 705 ? C14 ? F OLC 1   C14 
62  1 N 1 A OLC 706 ? C18 ? G OLC 1   C18 
63  1 N 1 A OLC 706 ? C10 ? G OLC 1   C10 
64  1 N 1 A OLC 706 ? C9  ? G OLC 1   C9  
65  1 N 1 A OLC 706 ? C17 ? G OLC 1   C17 
66  1 N 1 A OLC 706 ? C11 ? G OLC 1   C11 
67  1 N 1 A OLC 706 ? C24 ? G OLC 1   C24 
68  1 N 1 A OLC 706 ? C16 ? G OLC 1   C16 
69  1 N 1 A OLC 706 ? C12 ? G OLC 1   C12 
70  1 N 1 A OLC 706 ? C15 ? G OLC 1   C15 
71  1 N 1 A OLC 706 ? C13 ? G OLC 1   C13 
72  1 N 1 A OLC 706 ? C14 ? G OLC 1   C14 
73  1 N 1 A OLC 706 ? C21 ? G OLC 1   C21 
74  1 N 1 A OLC 706 ? C22 ? G OLC 1   C22 
75  1 N 1 A OLC 706 ? O25 ? G OLC 1   O25 
76  1 N 1 A OLC 706 ? O23 ? G OLC 1   O23 
77  1 N 1 A OLC 707 ? C18 ? H OLC 1   C18 
78  1 N 1 A OLC 707 ? C10 ? H OLC 1   C10 
79  1 N 1 A OLC 707 ? C9  ? H OLC 1   C9  
80  1 N 1 A OLC 707 ? C17 ? H OLC 1   C17 
81  1 N 1 A OLC 707 ? C11 ? H OLC 1   C11 
82  1 N 1 A OLC 707 ? C24 ? H OLC 1   C24 
83  1 N 1 A OLC 707 ? C16 ? H OLC 1   C16 
84  1 N 1 A OLC 707 ? C12 ? H OLC 1   C12 
85  1 N 1 A OLC 707 ? C15 ? H OLC 1   C15 
86  1 N 1 A OLC 707 ? C13 ? H OLC 1   C13 
87  1 N 1 A OLC 707 ? C14 ? H OLC 1   C14 
88  1 N 1 A OLC 707 ? C21 ? H OLC 1   C21 
89  1 N 1 A OLC 707 ? C22 ? H OLC 1   C22 
90  1 N 1 A OLC 707 ? O25 ? H OLC 1   O25 
91  1 N 1 A OLC 707 ? O23 ? H OLC 1   O23 
92  1 N 1 A OLC 708 ? C18 ? I OLC 1   C18 
93  1 N 1 A OLC 708 ? C17 ? I OLC 1   C17 
94  1 N 1 A OLC 708 ? C11 ? I OLC 1   C11 
95  1 N 1 A OLC 708 ? C24 ? I OLC 1   C24 
96  1 N 1 A OLC 708 ? C16 ? I OLC 1   C16 
97  1 N 1 A OLC 708 ? C12 ? I OLC 1   C12 
98  1 N 1 A OLC 708 ? C15 ? I OLC 1   C15 
99  1 N 1 A OLC 708 ? C13 ? I OLC 1   C13 
100 1 N 1 A OLC 708 ? C14 ? I OLC 1   C14 
101 1 N 1 A OLC 708 ? C21 ? I OLC 1   C21 
102 1 N 1 A OLC 708 ? C1  ? I OLC 1   C1  
103 1 N 1 A OLC 708 ? C22 ? I OLC 1   C22 
104 1 N 1 A OLC 708 ? O19 ? I OLC 1   O19 
105 1 N 1 A OLC 708 ? O25 ? I OLC 1   O25 
106 1 N 1 A OLC 708 ? O23 ? I OLC 1   O23 
107 1 N 1 A OLC 708 ? O20 ? I OLC 1   O20 
108 1 N 1 A OLC 709 ? C18 ? J OLC 1   C18 
109 1 N 1 A OLC 709 ? C10 ? J OLC 1   C10 
110 1 N 1 A OLC 709 ? C17 ? J OLC 1   C17 
111 1 N 1 A OLC 709 ? C11 ? J OLC 1   C11 
112 1 N 1 A OLC 709 ? C24 ? J OLC 1   C24 
113 1 N 1 A OLC 709 ? C16 ? J OLC 1   C16 
114 1 N 1 A OLC 709 ? C12 ? J OLC 1   C12 
115 1 N 1 A OLC 709 ? C15 ? J OLC 1   C15 
116 1 N 1 A OLC 709 ? C13 ? J OLC 1   C13 
117 1 N 1 A OLC 709 ? C14 ? J OLC 1   C14 
118 1 N 1 A OLC 709 ? C21 ? J OLC 1   C21 
119 1 N 1 A OLC 709 ? C1  ? J OLC 1   C1  
120 1 N 1 A OLC 709 ? C22 ? J OLC 1   C22 
121 1 N 1 A OLC 709 ? O19 ? J OLC 1   O19 
122 1 N 1 A OLC 709 ? O25 ? J OLC 1   O25 
123 1 N 1 A OLC 709 ? O23 ? J OLC 1   O23 
124 1 N 1 A OLC 709 ? O20 ? J OLC 1   O20 
# 
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_4459 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.10.2    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.10.2    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20_4459 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GO2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.400 
_cell.length_a_esd                 ? 
_cell.length_b                     141.700 
_cell.length_b_esd                 ? 
_cell.length_c                     94.400 
_cell.length_c_esd                 ? 
_cell.volume                       821315.872 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GO2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GO2 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.66 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'100 mM sodium citrate (pH 6.0), 30% PEG500DME, 100 mM MgCl2, 100 mM NaCl, and 100 mM (NH4)2SO4.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-07-07 
_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                    Si-111 
_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   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GO2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.70 
_reflns.d_resolution_low                               70.85 
_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                                     7315 
_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                           62.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                348.47 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.98 
_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                                   ? 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   0.07 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.70 
_reflns_shell.d_res_low                                     2.79 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.16 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             72 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  0.755 
_reflns_shell.pdbx_R_split                                  0.85 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               58.23 
_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                                 9GO2 
_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                            2.70 
_refine.ls_d_res_low                             70.85 
_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                     7312 
_refine.ls_number_reflns_R_free                  729 
_refine.ls_number_reflns_R_work                  6583 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    62.89 
_refine.ls_percent_reflns_R_free                 9.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2399 
_refine.ls_R_factor_R_free                       0.2682 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2367 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.1086 
_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                            0.2580 
_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                       2.70 
_refine_hist.d_res_low                        70.85 
_refine_hist.number_atoms_solvent             7 
_refine_hist.number_atoms_total               2460 
_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        2322 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         131 
_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' ? 0.0038  ? 4882 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8098  ? 6608 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0494  ? 739  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0032  ? 823  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7481 ? 1715 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.70 2.91  . . 25  211  10.37  . . . . 0.4052 . . . . . . . . . . . 0.5518 
'X-RAY DIFFRACTION' 2.91 3.21  . . 59  593  28.61  . . . . 0.3188 . . . . . . . . . . . 0.4018 
'X-RAY DIFFRACTION' 3.21 3.67  . . 168 1503 72.84  . . . . 0.2646 . . . . . . . . . . . 0.3061 
'X-RAY DIFFRACTION' 3.67 4.62  . . 233 2087 100.00 . . . . 0.2156 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 4.63 70.85 . . 244 2189 99.84  . . . . 0.2335 . . . . . . . . . . . 0.2509 
# 
_struct.entry_id                     9GO2 
_struct.title                        'C1C2 Channelrhodopsin - SMX Light activated structure' 
_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        9GO2 
_struct_keywords.text            'channelrhodopsin, light-activated, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE 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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q93WP2_CHLRE Q93WP2 ? 1 
;STGSDATVPVATQDGPDYVFHRAHERMLFQTSYTLENNGSVICIPNNGQCFCLAWLKSNGTNAEKLAANILQWITFALSA
LCLMFYGYQTWKSTCGWEEIYVATIEMIKFIIEYFHEFDEPAVIYSSNGNKTVWLRYAEWLLTCPVILIHLSNLTGLAND
YNKRTMGLLVSDIGTIVWGTTAALSKGYVRVIFFLMGLCYGIYTFFNAAKVYIEAYHTVPKG
;
24  
2 UNP Q8RUT8_CHLRE Q8RUT8 ? 1 
;RCRQVVTGMAWLFFVSWGMFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTK
LNIGGTEIEVETLVEDEAEAGAV
;
207 
# 
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 9GO2 A 1   ? 222 ? Q93WP2 24  ? 245 ? 331 552 
2 2 9GO2 A 223 ? 325 ? Q8RUT8 207 ? 309 ? 553 655 
# 
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 
2 9GO2 SER A 326 ? UNP Q8RUT8 ? ? 'expression tag' 656 1 
2 9GO2 SER A 327 ? UNP Q8RUT8 ? ? 'expression tag' 657 2 
2 9GO2 GLU A 328 ? UNP Q8RUT8 ? ? 'expression tag' 658 3 
2 9GO2 ASP A 329 ? UNP Q8RUT8 ? ? 'expression tag' 659 4 
2 9GO2 LEU A 330 ? UNP Q8RUT8 ? ? 'expression tag' 660 5 
2 9GO2 TYR A 331 ? UNP Q8RUT8 ? ? 'expression tag' 661 6 
2 9GO2 PHE A 332 ? UNP Q8RUT8 ? ? 'expression tag' 662 7 
2 9GO2 GLN A 333 ? UNP Q8RUT8 ? ? 'expression tag' 663 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6260  ? 
1 MORE         -55   ? 
1 'SSA (A^2)'  26200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_555 -x,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 47.2000000000 
# 
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 LEU A 53  ? LYS A 57  ? LEU A 383 LYS A 387 5 ? 5  
HELX_P HELX_P2 AA2 THR A 61  ? GLY A 87  ? THR A 391 GLY A 417 1 ? 27 
HELX_P HELX_P3 AA3 GLY A 96  ? GLU A 117 ? GLY A 426 GLU A 447 1 ? 22 
HELX_P HELX_P4 AA4 VAL A 133 ? SER A 152 ? VAL A 463 SER A 482 1 ? 20 
HELX_P HELX_P5 AA5 ASN A 162 ? SER A 185 ? ASN A 492 SER A 515 1 ? 24 
HELX_P HELX_P6 AA6 LYS A 186 ? VAL A 219 ? LYS A 516 VAL A 549 1 ? 34 
HELX_P HELX_P7 AA7 GLY A 222 ? GLY A 249 ? GLY A 552 GLY A 579 1 ? 28 
HELX_P HELX_P8 AA8 SER A 257 ? LYS A 273 ? SER A 587 LYS A 603 1 ? 17 
HELX_P HELX_P9 AA9 LYS A 273 ? GLY A 295 ? LYS A 603 GLY A 625 1 ? 23 
# 
_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 
disulf1 disulf ?   ? A CYS 43  SG A ? ? 1_555 A CYS 43 SG  A ? A CYS 373 A CYS 373 3_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf2 disulf ?   ? A CYS 43  SG B ? ? 1_555 A CYS 43 SG  B ? A CYS 373 A CYS 373 3_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf3 disulf ?   ? A CYS 50  SG A ? ? 1_555 A CYS 52 SG  A ? A CYS 380 A CYS 382 3_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf4 disulf ?   ? A CYS 50  SG B ? ? 1_555 A CYS 52 SG  B ? A CYS 380 A CYS 382 3_555 ? ? ? ? ? ? ? 2.028 ? ? 
covale1 covale one ? A LYS 273 NZ A ? ? 1_555 K RET .  C15 A ? A LYS 603 A RET 710 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale2 covale one ? A LYS 273 NZ B ? ? 1_555 K RET .  C15 B ? A LYS 603 A RET 710 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 RET K .  A LYS A 273 A RET A 710 ? 1_555 LYS A 603 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like   
2 RET K .  B LYS A 273 B RET A 710 ? 1_555 LYS A 603 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like   
3 CYS A 43 A CYS A 43  A CYS A 373 ? 1_555 CYS A 373 ? 3_555 SG  SG .   . .   None          'Disulfide bridge' 
4 CYS A 43 B CYS A 43  B CYS A 373 ? 1_555 CYS A 373 ? 3_555 SG  SG .   . .   None          'Disulfide bridge' 
5 CYS A 50 A CYS A 52  A CYS A 380 ? 1_555 CYS A 382 ? 3_555 SG  SG .   . .   None          'Disulfide bridge' 
6 CYS A 50 B CYS A 52  B CYS A 380 ? 1_555 CYS A 382 ? 3_555 SG  SG .   . .   None          'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 120 A . ? GLU 450 A PRO 121 A ? PRO 451 A 1 4.02 
2 GLU 120 A . ? GLU 450 A PRO 121 A ? PRO 451 A 1 3.83 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 34  ? GLU A 36  ? THR A 364 GLU A 366 
AA1 2 VAL A 41  ? CYS A 43  ? VAL A 371 CYS A 373 
AA2 1 ILE A 124 ? TYR A 125 ? ILE A 454 TYR A 455 
AA2 2 LYS A 131 ? THR A 132 ? LYS A 461 THR A 462 
AA3 1 ILE A 310 ? VAL A 316 ? ILE A 640 VAL A 646 
AA3 2 ILE A 297 ? ASN A 304 ? ILE A 627 ASN A 634 
AA3 3 ALA A 324 ? GLU A 328 ? ALA A 654 GLU A 658 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 36  ? N GLU A 366 O VAL A 41  ? O VAL A 371 
AA2 1 2 N ILE A 124 ? N ILE A 454 O THR A 132 ? O THR A 462 
AA3 1 2 O ILE A 310 ? O ILE A 640 N LEU A 303 ? N LEU A 633 
AA3 2 3 N THR A 300 ? N THR A 630 O VAL A 325 ? O VAL A 655 
# 
_pdbx_entry_details.entry_id                   9GO2 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   CZ 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   PHE 
_pdbx_validate_close_contact.auth_seq_id_1    583 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O20 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   OLC 
_pdbx_validate_close_contact.auth_seq_id_2    701 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.98 
# 
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 HIS A 446 ? A -142.60 37.31  
2 1 HIS A 446 ? B -142.47 37.02  
3 1 VAL A 585 ? B -121.95 -55.57 
4 1 LYS A 603 ? A -113.47 -75.95 
5 1 LYS A 603 ? B -93.31  -71.33 
6 1 ALA A 652 ? A -155.26 29.06  
7 1 ALA A 652 ? B -155.86 27.56  
8 1 SER A 657 ? A -167.80 113.84 
# 
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 SER 331 ? A SER 1   
2  1 Y 1 A THR 332 ? A THR 2   
3  1 Y 1 A GLY 333 ? A GLY 3   
4  1 Y 1 A SER 334 ? A SER 4   
5  1 Y 1 A ASP 335 ? A ASP 5   
6  1 Y 1 A ALA 336 ? A ALA 6   
7  1 Y 1 A THR 337 ? A THR 7   
8  1 Y 1 A VAL 338 ? A VAL 8   
9  1 Y 1 A PRO 339 ? A PRO 9   
10 1 Y 1 A VAL 340 ? A VAL 10  
11 1 Y 1 A ALA 341 ? A ALA 11  
12 1 Y 1 A THR 342 ? A THR 12  
13 1 Y 1 A GLN 343 ? A GLN 13  
14 1 Y 1 A ASP 344 ? A ASP 14  
15 1 Y 1 A GLY 345 ? A GLY 15  
16 1 Y 1 A PRO 346 ? A PRO 16  
17 1 Y 1 A ASP 347 ? A ASP 17  
18 1 Y 1 A TYR 348 ? A TYR 18  
19 1 Y 1 A VAL 349 ? A VAL 19  
20 1 Y 1 A PHE 350 ? A PHE 20  
21 1 Y 1 A HIS 351 ? A HIS 21  
22 1 Y 1 A ARG 352 ? A ARG 22  
23 1 Y 1 A ALA 353 ? A ALA 23  
24 1 Y 1 A HIS 354 ? A HIS 24  
25 1 Y 1 A GLU 355 ? A GLU 25  
26 1 Y 1 A ARG 356 ? A ARG 26  
27 1 Y 1 A GLN 419 ? A GLN 89  
28 1 Y 1 A THR 420 ? A THR 90  
29 1 Y 1 A TRP 421 ? A TRP 91  
30 1 Y 1 A LYS 422 ? A LYS 92  
31 1 Y 1 A SER 423 ? A SER 93  
32 1 Y 1 A THR 424 ? A THR 94  
33 1 Y 1 A ILE 635 ? A ILE 305 
34 1 Y 1 A GLY 636 ? A GLY 306 
35 1 Y 1 A GLY 637 ? A GLY 307 
36 1 Y 1 A LEU 660 ? A LEU 330 
37 1 Y 1 A TYR 661 ? A TYR 331 
38 1 Y 1 A PHE 662 ? A PHE 332 
39 1 Y 1 A GLN 663 ? A GLN 333 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
OLC C18  C N N 250 
OLC C10  C N N 251 
OLC C9   C N N 252 
OLC C17  C N N 253 
OLC C11  C N N 254 
OLC C8   C N N 255 
OLC C24  C N N 256 
OLC C16  C N N 257 
OLC C12  C N N 258 
OLC C7   C N N 259 
OLC C15  C N N 260 
OLC C13  C N N 261 
OLC C6   C N N 262 
OLC C14  C N N 263 
OLC C5   C N N 264 
OLC C4   C N N 265 
OLC C3   C N N 266 
OLC C2   C N N 267 
OLC C21  C N N 268 
OLC C1   C N N 269 
OLC C22  C N R 270 
OLC O19  O N N 271 
OLC O25  O N N 272 
OLC O23  O N N 273 
OLC O20  O N N 274 
OLC H18  H N N 275 
OLC H18A H N N 276 
OLC H18B H N N 277 
OLC H10  H N N 278 
OLC H9   H N N 279 
OLC H17  H N N 280 
OLC H17A H N N 281 
OLC H11  H N N 282 
OLC H11A H N N 283 
OLC H8   H N N 284 
OLC H8A  H N N 285 
OLC H24  H N N 286 
OLC H24A H N N 287 
OLC H16  H N N 288 
OLC H16A H N N 289 
OLC H12  H N N 290 
OLC H12A H N N 291 
OLC H7   H N N 292 
OLC H7A  H N N 293 
OLC H15  H N N 294 
OLC H15A H N N 295 
OLC H13  H N N 296 
OLC H13A H N N 297 
OLC H6   H N N 298 
OLC H6A  H N N 299 
OLC H14  H N N 300 
OLC H14A H N N 301 
OLC H5   H N N 302 
OLC H5A  H N N 303 
OLC H4   H N N 304 
OLC H4A  H N N 305 
OLC H3   H N N 306 
OLC H3A  H N N 307 
OLC H2   H N N 308 
OLC H2A  H N N 309 
OLC H21  H N N 310 
OLC H21A H N N 311 
OLC H22  H N N 312 
OLC HO25 H N N 313 
OLC HO23 H N N 314 
PHE N    N N N 315 
PHE CA   C N S 316 
PHE C    C N N 317 
PHE O    O N N 318 
PHE CB   C N N 319 
PHE CG   C Y N 320 
PHE CD1  C Y N 321 
PHE CD2  C Y N 322 
PHE CE1  C Y N 323 
PHE CE2  C Y N 324 
PHE CZ   C Y N 325 
PHE OXT  O N N 326 
PHE H    H N N 327 
PHE H2   H N N 328 
PHE HA   H N N 329 
PHE HB2  H N N 330 
PHE HB3  H N N 331 
PHE HD1  H N N 332 
PHE HD2  H N N 333 
PHE HE1  H N N 334 
PHE HE2  H N N 335 
PHE HZ   H N N 336 
PHE HXT  H N N 337 
PRO N    N N N 338 
PRO CA   C N S 339 
PRO C    C N N 340 
PRO O    O N N 341 
PRO CB   C N N 342 
PRO CG   C N N 343 
PRO CD   C N N 344 
PRO OXT  O N N 345 
PRO H    H N N 346 
PRO HA   H N N 347 
PRO HB2  H N N 348 
PRO HB3  H N N 349 
PRO HG2  H N N 350 
PRO HG3  H N N 351 
PRO HD2  H N N 352 
PRO HD3  H N N 353 
PRO HXT  H N N 354 
RET C1   C N N 355 
RET C2   C N N 356 
RET C3   C N N 357 
RET C4   C N N 358 
RET C5   C N N 359 
RET C6   C N N 360 
RET C7   C N N 361 
RET C8   C N N 362 
RET C9   C N N 363 
RET C10  C N N 364 
RET C11  C N N 365 
RET C12  C N N 366 
RET C13  C N N 367 
RET C14  C N N 368 
RET C15  C N N 369 
RET O1   O N N 370 
RET C16  C N N 371 
RET C17  C N N 372 
RET C18  C N N 373 
RET C19  C N N 374 
RET C20  C N N 375 
RET H21  H N N 376 
RET H22  H N N 377 
RET H31  H N N 378 
RET H32  H N N 379 
RET H41  H N N 380 
RET H42  H N N 381 
RET H7   H N N 382 
RET H8   H N N 383 
RET H10  H N N 384 
RET H11  H N N 385 
RET H12  H N N 386 
RET H14  H N N 387 
RET H15  H N N 388 
RET H161 H N N 389 
RET H162 H N N 390 
RET H163 H N N 391 
RET H171 H N N 392 
RET H172 H N N 393 
RET H173 H N N 394 
RET H181 H N N 395 
RET H182 H N N 396 
RET H183 H N N 397 
RET H191 H N N 398 
RET H192 H N N 399 
RET H193 H N N 400 
RET H201 H N N 401 
RET H202 H N N 402 
RET H203 H N N 403 
SER N    N N N 404 
SER CA   C N S 405 
SER C    C N N 406 
SER O    O N N 407 
SER CB   C N N 408 
SER OG   O N N 409 
SER OXT  O N N 410 
SER H    H N N 411 
SER H2   H N N 412 
SER HA   H N N 413 
SER HB2  H N N 414 
SER HB3  H N N 415 
SER HG   H N N 416 
SER HXT  H N N 417 
THR N    N N N 418 
THR CA   C N S 419 
THR C    C N N 420 
THR O    O N N 421 
THR CB   C N R 422 
THR OG1  O N N 423 
THR CG2  C N N 424 
THR OXT  O N N 425 
THR H    H N N 426 
THR H2   H N N 427 
THR HA   H N N 428 
THR HB   H N N 429 
THR HG1  H N N 430 
THR HG21 H N N 431 
THR HG22 H N N 432 
THR HG23 H N N 433 
THR HXT  H N N 434 
TRP N    N N N 435 
TRP CA   C N S 436 
TRP C    C N N 437 
TRP O    O N N 438 
TRP CB   C N N 439 
TRP CG   C Y N 440 
TRP CD1  C Y N 441 
TRP CD2  C Y N 442 
TRP NE1  N Y N 443 
TRP CE2  C Y N 444 
TRP CE3  C Y N 445 
TRP CZ2  C Y N 446 
TRP CZ3  C Y N 447 
TRP CH2  C Y N 448 
TRP OXT  O N N 449 
TRP H    H N N 450 
TRP H2   H N N 451 
TRP HA   H N N 452 
TRP HB2  H N N 453 
TRP HB3  H N N 454 
TRP HD1  H N N 455 
TRP HE1  H N N 456 
TRP HE3  H N N 457 
TRP HZ2  H N N 458 
TRP HZ3  H N N 459 
TRP HH2  H N N 460 
TRP HXT  H N N 461 
TYR N    N N N 462 
TYR CA   C N S 463 
TYR C    C N N 464 
TYR O    O N N 465 
TYR CB   C N N 466 
TYR CG   C Y N 467 
TYR CD1  C Y N 468 
TYR CD2  C Y N 469 
TYR CE1  C Y N 470 
TYR CE2  C Y N 471 
TYR CZ   C Y N 472 
TYR OH   O N N 473 
TYR OXT  O N N 474 
TYR H    H N N 475 
TYR H2   H N N 476 
TYR HA   H N N 477 
TYR HB2  H N N 478 
TYR HB3  H N N 479 
TYR HD1  H N N 480 
TYR HD2  H N N 481 
TYR HE1  H N N 482 
TYR HE2  H N N 483 
TYR HH   H N N 484 
TYR HXT  H N N 485 
VAL N    N N N 486 
VAL CA   C N S 487 
VAL C    C N N 488 
VAL O    O N N 489 
VAL CB   C N N 490 
VAL CG1  C N N 491 
VAL CG2  C N N 492 
VAL OXT  O N N 493 
VAL H    H N N 494 
VAL H2   H N N 495 
VAL HA   H N N 496 
VAL HB   H N N 497 
VAL HG11 H N N 498 
VAL HG12 H N N 499 
VAL HG13 H N N 500 
VAL HG21 H N N 501 
VAL HG22 H N N 502 
VAL HG23 H N N 503 
VAL HXT  H N N 504 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
OLC C18 C17  sing N N 237 
OLC C10 C9   doub N N 238 
OLC C10 C11  sing N N 239 
OLC C9  C8   sing N N 240 
OLC C17 C16  sing N Z 241 
OLC C11 C12  sing N N 242 
OLC C8  C7   sing N N 243 
OLC C24 C22  sing N N 244 
OLC C24 O25  sing N N 245 
OLC C16 C15  sing N N 246 
OLC C12 C13  sing N N 247 
OLC C7  C6   sing N N 248 
OLC C15 C14  sing N N 249 
OLC C13 C14  sing N N 250 
OLC C6  C5   sing N N 251 
OLC C5  C4   sing N N 252 
OLC C4  C3   sing N N 253 
OLC C3  C2   sing N N 254 
OLC C2  C1   sing N N 255 
OLC C21 C22  sing N N 256 
OLC C21 O20  sing N N 257 
OLC C1  O19  doub N N 258 
OLC C1  O20  sing N N 259 
OLC C22 O23  sing N N 260 
OLC C18 H18  sing N N 261 
OLC C18 H18A sing N N 262 
OLC C18 H18B sing N N 263 
OLC C10 H10  sing N N 264 
OLC C9  H9   sing N N 265 
OLC C17 H17  sing N N 266 
OLC C17 H17A sing N N 267 
OLC C11 H11  sing N N 268 
OLC C11 H11A sing N N 269 
OLC C8  H8   sing N N 270 
OLC C8  H8A  sing N N 271 
OLC C24 H24  sing N N 272 
OLC C24 H24A sing N N 273 
OLC C16 H16  sing N N 274 
OLC C16 H16A sing N N 275 
OLC C12 H12  sing N N 276 
OLC C12 H12A sing N N 277 
OLC C7  H7   sing N N 278 
OLC C7  H7A  sing N N 279 
OLC C15 H15  sing N N 280 
OLC C15 H15A sing N N 281 
OLC C13 H13  sing N N 282 
OLC C13 H13A sing N N 283 
OLC C6  H6   sing N N 284 
OLC C6  H6A  sing N N 285 
OLC C14 H14  sing N N 286 
OLC C14 H14A sing N N 287 
OLC C5  H5   sing N N 288 
OLC C5  H5A  sing N N 289 
OLC C4  H4   sing N N 290 
OLC C4  H4A  sing N N 291 
OLC C3  H3   sing N N 292 
OLC C3  H3A  sing N N 293 
OLC C2  H2   sing N N 294 
OLC C2  H2A  sing N N 295 
OLC C21 H21  sing N N 296 
OLC C21 H21A sing N N 297 
OLC C22 H22  sing N N 298 
OLC O25 HO25 sing N N 299 
OLC O23 HO23 sing N N 300 
PHE N   CA   sing N N 301 
PHE N   H    sing N N 302 
PHE N   H2   sing N N 303 
PHE CA  C    sing N N 304 
PHE CA  CB   sing N N 305 
PHE CA  HA   sing N N 306 
PHE C   O    doub N N 307 
PHE C   OXT  sing N N 308 
PHE CB  CG   sing N N 309 
PHE CB  HB2  sing N N 310 
PHE CB  HB3  sing N N 311 
PHE CG  CD1  doub Y N 312 
PHE CG  CD2  sing Y N 313 
PHE CD1 CE1  sing Y N 314 
PHE CD1 HD1  sing N N 315 
PHE CD2 CE2  doub Y N 316 
PHE CD2 HD2  sing N N 317 
PHE CE1 CZ   doub Y N 318 
PHE CE1 HE1  sing N N 319 
PHE CE2 CZ   sing Y N 320 
PHE CE2 HE2  sing N N 321 
PHE CZ  HZ   sing N N 322 
PHE OXT HXT  sing N N 323 
PRO N   CA   sing N N 324 
PRO N   CD   sing N N 325 
PRO N   H    sing N N 326 
PRO CA  C    sing N N 327 
PRO CA  CB   sing N N 328 
PRO CA  HA   sing N N 329 
PRO C   O    doub N N 330 
PRO C   OXT  sing N N 331 
PRO CB  CG   sing N N 332 
PRO CB  HB2  sing N N 333 
PRO CB  HB3  sing N N 334 
PRO CG  CD   sing N N 335 
PRO CG  HG2  sing N N 336 
PRO CG  HG3  sing N N 337 
PRO CD  HD2  sing N N 338 
PRO CD  HD3  sing N N 339 
PRO OXT HXT  sing N N 340 
RET C1  C2   sing N N 341 
RET C1  C6   sing N N 342 
RET C1  C16  sing N N 343 
RET C1  C17  sing N N 344 
RET C2  C3   sing N N 345 
RET C2  H21  sing N N 346 
RET C2  H22  sing N N 347 
RET C3  C4   sing N N 348 
RET C3  H31  sing N N 349 
RET C3  H32  sing N N 350 
RET C4  C5   sing N N 351 
RET C4  H41  sing N N 352 
RET C4  H42  sing N N 353 
RET C5  C6   doub N N 354 
RET C5  C18  sing N N 355 
RET C6  C7   sing N N 356 
RET C7  C8   doub N E 357 
RET C7  H7   sing N N 358 
RET C8  C9   sing N N 359 
RET C8  H8   sing N N 360 
RET C9  C10  doub N E 361 
RET C9  C19  sing N N 362 
RET C10 C11  sing N N 363 
RET C10 H10  sing N N 364 
RET C11 C12  doub N E 365 
RET C11 H11  sing N N 366 
RET C12 C13  sing N N 367 
RET C12 H12  sing N N 368 
RET C13 C14  doub N E 369 
RET C13 C20  sing N N 370 
RET C14 C15  sing N N 371 
RET C14 H14  sing N N 372 
RET C15 O1   doub N N 373 
RET C15 H15  sing N N 374 
RET C16 H161 sing N N 375 
RET C16 H162 sing N N 376 
RET C16 H163 sing N N 377 
RET C17 H171 sing N N 378 
RET C17 H172 sing N N 379 
RET C17 H173 sing N N 380 
RET C18 H181 sing N N 381 
RET C18 H182 sing N N 382 
RET C18 H183 sing N N 383 
RET C19 H191 sing N N 384 
RET C19 H192 sing N N 385 
RET C19 H193 sing N N 386 
RET C20 H201 sing N N 387 
RET C20 H202 sing N N 388 
RET C20 H203 sing N N 389 
SER N   CA   sing N N 390 
SER N   H    sing N N 391 
SER N   H2   sing N N 392 
SER CA  C    sing N N 393 
SER CA  CB   sing N N 394 
SER CA  HA   sing N N 395 
SER C   O    doub N N 396 
SER C   OXT  sing N N 397 
SER CB  OG   sing N N 398 
SER CB  HB2  sing N N 399 
SER CB  HB3  sing N N 400 
SER OG  HG   sing N N 401 
SER OXT HXT  sing N N 402 
THR N   CA   sing N N 403 
THR N   H    sing N N 404 
THR N   H2   sing N N 405 
THR CA  C    sing N N 406 
THR CA  CB   sing N N 407 
THR CA  HA   sing N N 408 
THR C   O    doub N N 409 
THR C   OXT  sing N N 410 
THR CB  OG1  sing N N 411 
THR CB  CG2  sing N N 412 
THR CB  HB   sing N N 413 
THR OG1 HG1  sing N N 414 
THR CG2 HG21 sing N N 415 
THR CG2 HG22 sing N N 416 
THR CG2 HG23 sing N N 417 
THR OXT HXT  sing N N 418 
TRP N   CA   sing N N 419 
TRP N   H    sing N N 420 
TRP N   H2   sing N N 421 
TRP CA  C    sing N N 422 
TRP CA  CB   sing N N 423 
TRP CA  HA   sing N N 424 
TRP C   O    doub N N 425 
TRP C   OXT  sing N N 426 
TRP CB  CG   sing N N 427 
TRP CB  HB2  sing N N 428 
TRP CB  HB3  sing N N 429 
TRP CG  CD1  doub Y N 430 
TRP CG  CD2  sing Y N 431 
TRP CD1 NE1  sing Y N 432 
TRP CD1 HD1  sing N N 433 
TRP CD2 CE2  doub Y N 434 
TRP CD2 CE3  sing Y N 435 
TRP NE1 CE2  sing Y N 436 
TRP NE1 HE1  sing N N 437 
TRP CE2 CZ2  sing Y N 438 
TRP CE3 CZ3  doub Y N 439 
TRP CE3 HE3  sing N N 440 
TRP CZ2 CH2  doub Y N 441 
TRP CZ2 HZ2  sing N N 442 
TRP CZ3 CH2  sing Y N 443 
TRP CZ3 HZ3  sing N N 444 
TRP CH2 HH2  sing N N 445 
TRP OXT HXT  sing N N 446 
TYR N   CA   sing N N 447 
TYR N   H    sing N N 448 
TYR N   H2   sing N N 449 
TYR CA  C    sing N N 450 
TYR CA  CB   sing N N 451 
TYR CA  HA   sing N N 452 
TYR C   O    doub N N 453 
TYR C   OXT  sing N N 454 
TYR CB  CG   sing N N 455 
TYR CB  HB2  sing N N 456 
TYR CB  HB3  sing N N 457 
TYR CG  CD1  doub Y N 458 
TYR CG  CD2  sing Y N 459 
TYR CD1 CE1  sing Y N 460 
TYR CD1 HD1  sing N N 461 
TYR CD2 CE2  doub Y N 462 
TYR CD2 HD2  sing N N 463 
TYR CE1 CZ   doub Y N 464 
TYR CE1 HE1  sing N N 465 
TYR CE2 CZ   sing Y N 466 
TYR CE2 HE2  sing N N 467 
TYR CZ  OH   sing N N 468 
TYR OH  HH   sing N N 469 
TYR OXT HXT  sing N N 470 
VAL N   CA   sing N N 471 
VAL N   H    sing N N 472 
VAL N   H2   sing N N 473 
VAL CA  C    sing N N 474 
VAL CA  CB   sing N N 475 
VAL CA  HA   sing N N 476 
VAL C   O    doub N N 477 
VAL C   OXT  sing N N 478 
VAL CB  CG1  sing N N 479 
VAL CB  CG2  sing N N 480 
VAL CB  HB   sing N N 481 
VAL CG1 HG11 sing N N 482 
VAL CG1 HG12 sing N N 483 
VAL CG1 HG13 sing N N 484 
VAL CG2 HG21 sing N N 485 
VAL CG2 HG22 sing N N 486 
VAL CG2 HG23 sing N N 487 
VAL OXT HXT  sing N N 488 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland      310030_197674   1 
'Swiss National Science Foundation' Switzerland      310030_207462   2 
Innosuisse                          'European Union' '42711.1 IP-LS' 3 
# 
_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   7C86 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_atom_sites.entry_id                    9GO2 
_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]   0.016287 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007057 
_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]   0.010593 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   A MET A 1 27  ? 13.85700  11.09800  22.43700 0.700 43.16982  ? 357 MET A N   1 
ATOM   2    C CA  A MET A 1 27  ? 12.49000  11.50300  22.75200 0.700 79.12767  ? 357 MET A CA  1 
ATOM   3    C C   A MET A 1 27  ? 12.11900  11.14800  24.19300 0.700 82.55494  ? 357 MET A C   1 
ATOM   4    O O   A MET A 1 27  ? 12.57900  10.14000  24.73200 0.700 75.74942  ? 357 MET A O   1 
ATOM   5    C CB  A MET A 1 27  ? 11.50500  10.84700  21.78100 0.700 43.90758  ? 357 MET A CB  1 
ATOM   6    N N   A LEU A 1 28  ? 11.27300  11.97800  24.81000 0.700 74.87087  ? 358 LEU A N   1 
ATOM   7    N N   B LEU A 1 28  ? 11.21000  12.09400  24.53700 0.300 73.97600  ? 358 LEU A N   1 
ATOM   8    C CA  A LEU A 1 28  ? 10.65100  11.66500  26.09200 0.700 62.31253  ? 358 LEU A CA  1 
ATOM   9    C CA  B LEU A 1 28  ? 10.74900  11.84600  25.89700 0.300 65.16389  ? 358 LEU A CA  1 
ATOM   10   C C   A LEU A 1 28  ? 9.17900   11.28300  25.94400 0.700 67.48213  ? 358 LEU A C   1 
ATOM   11   C C   B LEU A 1 28  ? 9.26600   11.48300  25.89400 0.300 67.75451  ? 358 LEU A C   1 
ATOM   12   O O   A LEU A 1 28  ? 8.38500   11.48000  26.86800 0.700 64.82908  ? 358 LEU A O   1 
ATOM   13   O O   B LEU A 1 28  ? 8.55300   11.71400  26.87100 0.300 65.98967  ? 358 LEU A O   1 
ATOM   14   C CB  A LEU A 1 28  ? 10.79900  12.84000  27.05700 0.700 67.90856  ? 358 LEU A CB  1 
ATOM   15   C CB  B LEU A 1 28  ? 11.00100  13.07000  26.78000 0.300 67.82279  ? 358 LEU A CB  1 
ATOM   16   C CG  B LEU A 1 28  ? 12.06300  12.91300  27.87100 0.300 60.63184  ? 358 LEU A CG  1 
ATOM   17   C CD1 B LEU A 1 28  ? 12.34200  14.24900  28.54200 0.300 47.11540  ? 358 LEU A CD1 1 
ATOM   18   C CD2 B LEU A 1 28  ? 11.64100  11.87100  28.89400 0.300 50.98660  ? 358 LEU A CD2 1 
ATOM   19   N N   A PHE A 1 29  ? 8.80000   10.74100  24.79000 0.700 69.93203  ? 359 PHE A N   1 
ATOM   20   N N   B PHE A 1 29  ? 8.81600   10.91100  24.78200 0.300 69.02943  ? 359 PHE A N   1 
ATOM   21   C CA  A PHE A 1 29  ? 7.61500   9.90700   24.65100 0.700 63.05461  ? 359 PHE A CA  1 
ATOM   22   C CA  B PHE A 1 29  ? 7.62400   10.08000  24.72100 0.300 62.81566  ? 359 PHE A CA  1 
ATOM   23   C C   A PHE A 1 29  ? 8.02700   8.50400   24.22000 0.700 61.02123  ? 359 PHE A C   1 
ATOM   24   C C   B PHE A 1 29  ? 8.01000   8.66600   24.30500 0.300 61.02140  ? 359 PHE A C   1 
ATOM   25   O O   A PHE A 1 29  ? 9.19200   8.23400   23.91600 0.700 61.75521  ? 359 PHE A O   1 
ATOM   26   O O   B PHE A 1 29  ? 9.15900   8.39000   23.94800 0.300 62.04853  ? 359 PHE A O   1 
ATOM   27   C CB  A PHE A 1 29  ? 6.60400   10.50300  23.65400 0.700 57.56725  ? 359 PHE A CB  1 
ATOM   28   C CB  B PHE A 1 29  ? 6.58200   10.66600  23.75700 0.300 57.74912  ? 359 PHE A CB  1 
ATOM   29   C CG  A PHE A 1 29  ? 7.22800   11.06700  22.40500 0.700 58.05724  ? 359 PHE A CG  1 
ATOM   30   C CG  B PHE A 1 29  ? 7.16200   11.19700  22.47600 0.300 58.05640  ? 359 PHE A CG  1 
ATOM   31   C CD1 A PHE A 1 29  ? 7.69300   10.22800  21.40300 0.700 59.83057  ? 359 PHE A CD1 1 
ATOM   32   C CD1 B PHE A 1 29  ? 7.57700   10.33600  21.47400 0.300 59.56564  ? 359 PHE A CD1 1 
ATOM   33   C CD2 A PHE A 1 29  ? 7.32900   12.43900  22.22500 0.700 58.03328  ? 359 PHE A CD2 1 
ATOM   34   C CD2 B PHE A 1 29  ? 7.28100   12.56100  22.27100 0.300 57.55082  ? 359 PHE A CD2 1 
ATOM   35   C CE1 A PHE A 1 29  ? 8.26500   10.74600  20.25400 0.700 62.67155  ? 359 PHE A CE1 1 
ATOM   36   C CE1 B PHE A 1 29  ? 8.10700   10.82600  20.29500 0.300 62.12589  ? 359 PHE A CE1 1 
ATOM   37   C CE2 A PHE A 1 29  ? 7.89600   12.96200  21.07800 0.700 58.01579  ? 359 PHE A CE2 1 
ATOM   38   C CE2 B PHE A 1 29  ? 7.80900   13.05700  21.09400 0.300 57.59888  ? 359 PHE A CE2 1 
ATOM   39   C CZ  A PHE A 1 29  ? 8.36500   12.11400  20.09000 0.700 59.40948  ? 359 PHE A CZ  1 
ATOM   40   C CZ  B PHE A 1 29  ? 8.22200   12.18800  20.10500 0.300 59.07972  ? 359 PHE A CZ  1 
ATOM   41   N N   A GLN A 1 30  ? 7.05000   7.60000   24.21400 0.700 60.33279  ? 360 GLN A N   1 
ATOM   42   N N   B GLN A 1 30  ? 7.03600   7.76000   24.36100 0.300 59.62877  ? 360 GLN A N   1 
ATOM   43   C CA  A GLN A 1 30  ? 7.32000   6.21400   23.86500 0.700 56.77556  ? 360 GLN A CA  1 
ATOM   44   C CA  B GLN A 1 30  ? 7.30500   6.36700   24.03300 0.300 57.39928  ? 360 GLN A CA  1 
ATOM   45   C C   A GLN A 1 30  ? 7.67000   6.09600   22.38600 0.700 59.51921  ? 360 GLN A C   1 
ATOM   46   C C   B GLN A 1 30  ? 7.60400   6.22600   22.54500 0.300 59.46373  ? 360 GLN A C   1 
ATOM   47   O O   A GLN A 1 30  ? 6.94500   6.59400   21.51800 0.700 57.19078  ? 360 GLN A O   1 
ATOM   48   O O   B GLN A 1 30  ? 6.84400   6.69900   21.69500 0.300 57.61476  ? 360 GLN A O   1 
ATOM   49   C CB  A GLN A 1 30  ? 6.10800   5.34400   24.19900 0.700 52.61229  ? 360 GLN A CB  1 
ATOM   50   C CB  B GLN A 1 30  ? 6.11400   5.49100   24.42000 0.300 54.08404  ? 360 GLN A CB  1 
ATOM   51   C CG  A GLN A 1 30  ? 6.36000   3.85200   24.09400 0.700 52.05898  ? 360 GLN A CG  1 
ATOM   52   C CG  B GLN A 1 30  ? 6.37900   3.99600   24.34100 0.300 52.78883  ? 360 GLN A CG  1 
ATOM   53   C CD  A GLN A 1 30  ? 7.56900   3.41100   24.89100 0.700 53.35252  ? 360 GLN A CD  1 
ATOM   54   C CD  B GLN A 1 30  ? 7.61300   3.58000   25.11600 0.300 55.08753  ? 360 GLN A CD  1 
ATOM   55   O OE1 A GLN A 1 30  ? 7.65300   3.64400   26.09800 0.700 56.28118  ? 360 GLN A OE1 1 
ATOM   56   O OE1 B GLN A 1 30  ? 7.72300   3.83800   26.31500 0.300 59.18686  ? 360 GLN A OE1 1 
ATOM   57   N NE2 A GLN A 1 30  ? 8.51200   2.75900   24.21900 0.700 54.81499  ? 360 GLN A NE2 1 
ATOM   58   N NE2 B GLN A 1 30  ? 8.54900   2.93000   24.43500 0.300 55.80874  ? 360 GLN A NE2 1 
ATOM   59   N N   A THR A 1 31  ? 8.79400   5.43700   22.10500 0.700 62.01335  ? 361 THR A N   1 
ATOM   60   N N   B THR A 1 31  ? 8.72400   5.56900   22.24000 0.300 61.38102  ? 361 THR A N   1 
ATOM   61   C CA  A THR A 1 31  ? 9.26100   5.21800   20.74500 0.700 57.09072  ? 361 THR A CA  1 
ATOM   62   C CA  B THR A 1 31  ? 9.16600   5.32700   20.87400 0.300 57.50250  ? 361 THR A CA  1 
ATOM   63   C C   A THR A 1 31  ? 9.39100   3.75000   20.37300 0.700 67.34995  ? 361 THR A C   1 
ATOM   64   C C   B THR A 1 31  ? 9.29600   3.85300   20.52100 0.300 66.26258  ? 361 THR A C   1 
ATOM   65   O O   A THR A 1 31  ? 9.47800   3.44200   19.17900 0.700 71.12218  ? 361 THR A O   1 
ATOM   66   O O   B THR A 1 31  ? 9.36300   3.52800   19.33100 0.300 70.06434  ? 361 THR A O   1 
ATOM   67   C CB  A THR A 1 31  ? 10.62000  5.90400   20.52600 0.700 56.21266  ? 361 THR A CB  1 
ATOM   68   C CB  B THR A 1 31  ? 10.51600  6.01600   20.61400 0.300 56.46373  ? 361 THR A CB  1 
ATOM   69   O OG1 A THR A 1 31  ? 11.56700  5.40300   21.47900 0.700 55.94689  ? 361 THR A OG1 1 
ATOM   70   O OG1 B THR A 1 31  ? 11.00300  5.64500   19.31800 0.300 63.03342  ? 361 THR A OG1 1 
ATOM   71   C CG2 A THR A 1 31  ? 10.49000  7.40900   20.68500 0.700 56.43787  ? 361 THR A CG2 1 
ATOM   72   C CG2 B THR A 1 31  ? 11.53400  5.61300   21.66900 0.300 57.80938  ? 361 THR A CG2 1 
ATOM   73   N N   A SER A 1 32  ? 9.41200   2.84600   21.34800 0.700 60.80005  ? 362 SER A N   1 
ATOM   74   N N   B SER A 1 32  ? 9.33100   2.96200   21.50700 0.300 60.63038  ? 362 SER A N   1 
ATOM   75   C CA  A SER A 1 32  ? 9.50100   1.41300   21.10200 0.700 59.28052  ? 362 SER A CA  1 
ATOM   76   C CA  B SER A 1 32  ? 9.43000   1.52800   21.27800 0.300 58.65556  ? 362 SER A CA  1 
ATOM   77   C C   A SER A 1 32  ? 8.12100   0.79100   21.27100 0.700 58.01101  ? 362 SER A C   1 
ATOM   78   C C   B SER A 1 32  ? 8.05900   0.88900   21.45000 0.300 56.98595  ? 362 SER A C   1 
ATOM   79   O O   A SER A 1 32  ? 7.45800   1.00600   22.29200 0.700 45.61716  ? 362 SER A O   1 
ATOM   80   O O   B SER A 1 32  ? 7.38900   1.10400   22.46600 0.300 46.09732  ? 362 SER A O   1 
ATOM   81   C CB  A SER A 1 32  ? 10.50800  0.75600   22.04800 0.700 55.27844  ? 362 SER A CB  1 
ATOM   82   C CB  B SER A 1 32  ? 10.43300  0.89100   22.24200 0.300 55.71844  ? 362 SER A CB  1 
ATOM   83   O OG  A SER A 1 32  ? 9.95500   0.58100   23.34100 0.700 54.95779  ? 362 SER A OG  1 
ATOM   84   O OG  B SER A 1 32  ? 11.67200  1.57800   22.21600 0.300 53.88587  ? 362 SER A OG  1 
ATOM   85   N N   A TYR A 1 33  ? 7.69400   0.02700   20.26900 0.700 60.99667  ? 363 TYR A N   1 
ATOM   86   N N   B TYR A 1 33  ? 7.64800   0.10600   20.45500 0.300 60.67938  ? 363 TYR A N   1 
ATOM   87   C CA  A TYR A 1 33  ? 6.41700   -0.66900  20.31900 0.700 56.43461  ? 363 TYR A CA  1 
ATOM   88   C CA  B TYR A 1 33  ? 6.38200   -0.60600  20.50800 0.300 56.39761  ? 363 TYR A CA  1 
ATOM   89   C C   A TYR A 1 33  ? 6.49600   -1.92600  19.46500 0.700 59.74046  ? 363 TYR A C   1 
ATOM   90   C C   B TYR A 1 33  ? 6.48600   -1.87500  19.67400 0.300 59.31686  ? 363 TYR A C   1 
ATOM   91   O O   A TYR A 1 33  ? 7.41400   -2.09900  18.66000 0.700 69.38649  ? 363 TYR A O   1 
ATOM   92   O O   B TYR A 1 33  ? 7.41400   -2.05200  18.88100 0.300 68.08769  ? 363 TYR A O   1 
ATOM   93   C CB  A TYR A 1 33  ? 5.27700   0.24000   19.85400 0.700 50.80299  ? 363 TYR A CB  1 
ATOM   94   C CB  B TYR A 1 33  ? 5.23100   0.27600   20.00900 0.300 51.05324  ? 363 TYR A CB  1 
ATOM   95   C CG  A TYR A 1 33  ? 5.42900   0.71100   18.42600 0.700 45.88215  ? 363 TYR A CG  1 
ATOM   96   C CG  B TYR A 1 33  ? 5.38000   0.71800   18.56900 0.300 46.75691  ? 363 TYR A CG  1 
ATOM   97   C CD1 A TYR A 1 33  ? 6.24000   1.79600   18.11600 0.700 51.29582  ? 363 TYR A CD1 1 
ATOM   98   C CD1 B TYR A 1 33  ? 6.17600   1.80600   18.23600 0.300 51.54778  ? 363 TYR A CD1 1 
ATOM   99   C CD2 A TYR A 1 33  ? 4.78200   0.05800   17.38500 0.700 50.88208  ? 363 TYR A CD2 1 
ATOM   100  C CD2 B TYR A 1 33  ? 4.72300   0.04900   17.54400 0.300 51.31818  ? 363 TYR A CD2 1 
ATOM   101  C CE1 A TYR A 1 33  ? 6.39000   2.22800   16.81000 0.700 61.94431  ? 363 TYR A CE1 1 
ATOM   102  C CE1 B TYR A 1 33  ? 6.31700   2.21400   16.92400 0.300 61.38742  ? 363 TYR A CE1 1 
ATOM   103  C CE2 A TYR A 1 33  ? 4.92700   0.48100   16.07600 0.700 60.19764  ? 363 TYR A CE2 1 
ATOM   104  C CE2 B TYR A 1 33  ? 4.85800   0.45100   16.22700 0.300 59.61039  ? 363 TYR A CE2 1 
ATOM   105  C CZ  A TYR A 1 33  ? 5.73300   1.56600   15.79400 0.700 64.31921  ? 363 TYR A CZ  1 
ATOM   106  C CZ  B TYR A 1 33  ? 5.65600   1.53400   15.92300 0.300 63.70360  ? 363 TYR A CZ  1 
ATOM   107  O OH  A TYR A 1 33  ? 5.87700   1.99100   14.49300 0.700 60.38672  ? 363 TYR A OH  1 
ATOM   108  O OH  B TYR A 1 33  ? 5.79400   1.93900   14.61500 0.300 60.31249  ? 363 TYR A OH  1 
ATOM   109  N N   A THR A 1 34  ? 5.51200   -2.80600  19.64600 0.700 59.55245  ? 364 THR A N   1 
ATOM   110  N N   B THR A 1 34  ? 5.51400   -2.76300  19.87000 0.300 59.81315  ? 364 THR A N   1 
ATOM   111  C CA  A THR A 1 34  ? 5.32500   -3.97600  18.79800 0.700 64.87580  ? 364 THR A CA  1 
ATOM   112  C CA  B THR A 1 34  ? 5.33700   -3.95100  19.04800 0.300 64.82550  ? 364 THR A CA  1 
ATOM   113  C C   A THR A 1 34  ? 3.93400   -3.94400  18.18000 0.700 57.20011  ? 364 THR A C   1 
ATOM   114  C C   B THR A 1 34  ? 3.94500   -3.95500  18.43300 0.300 58.69624  ? 364 THR A C   1 
ATOM   115  O O   A THR A 1 34  ? 2.95200   -3.60200  18.85000 0.700 57.28265  ? 364 THR A O   1 
ATOM   116  O O   B THR A 1 34  ? 2.95700   -3.63800  19.10300 0.300 58.14730  ? 364 THR A O   1 
ATOM   117  C CB  A THR A 1 34  ? 5.50400   -5.28500  19.58700 0.700 65.15582  ? 364 THR A CB  1 
ATOM   118  C CB  B THR A 1 34  ? 5.54100   -5.23200  19.86600 0.300 64.30872  ? 364 THR A CB  1 
ATOM   119  O OG1 A THR A 1 34  ? 4.41300   -5.45300  20.50000 0.700 63.45992  ? 364 THR A OG1 1 
ATOM   120  O OG1 B THR A 1 34  ? 4.45800   -5.38700  20.79200 0.300 63.89119  ? 364 THR A OG1 1 
ATOM   121  C CG2 A THR A 1 34  ? 6.80700   -5.26000  20.37800 0.700 50.20002  ? 364 THR A CG2 1 
ATOM   122  C CG2 B THR A 1 34  ? 6.85600   -5.17900  20.63000 0.300 51.88962  ? 364 THR A CG2 1 
ATOM   123  N N   A LEU A 1 35  ? 3.85800   -4.27800  16.89400 0.700 53.85889  ? 365 LEU A N   1 
ATOM   124  N N   B LEU A 1 35  ? 3.87300   -4.31900  17.15500 0.300 56.07780  ? 365 LEU A N   1 
ATOM   125  C CA  A LEU A 1 35  ? 2.58700   -4.60400  16.26300 0.700 61.58781  ? 365 LEU A CA  1 
ATOM   126  C CA  B LEU A 1 35  ? 2.60500   -4.68100  16.53700 0.300 61.14858  ? 365 LEU A CA  1 
ATOM   127  C C   A LEU A 1 35  ? 2.21000   -6.05000  16.56700 0.700 62.68523  ? 365 LEU A C   1 
ATOM   128  C C   B LEU A 1 35  ? 2.25800   -6.12400  16.88200 0.300 62.68929  ? 365 LEU A C   1 
ATOM   129  O O   A LEU A 1 35  ? 3.04200   -6.95500  16.44600 0.700 66.94501  ? 365 LEU A O   1 
ATOM   130  O O   B LEU A 1 35  ? 3.10600   -7.01600  16.78500 0.300 66.78579  ? 365 LEU A O   1 
ATOM   131  C CB  A LEU A 1 35  ? 2.67000   -4.39400  14.75000 0.700 60.02750  ? 365 LEU A CB  1 
ATOM   132  C CB  B LEU A 1 35  ? 2.67600   -4.49700  15.02200 0.300 59.53272  ? 365 LEU A CB  1 
ATOM   133  C CG  A LEU A 1 35  ? 2.88200   -2.98300  14.19500 0.700 55.72914  ? 365 LEU A CG  1 
ATOM   134  C CG  B LEU A 1 35  ? 2.85600   -3.06100  14.52700 0.300 57.15047  ? 365 LEU A CG  1 
ATOM   135  C CD1 A LEU A 1 35  ? 2.31100   -2.85700  12.79300 0.700 58.07507  ? 365 LEU A CD1 1 
ATOM   136  C CD1 B LEU A 1 35  ? 3.53700   -3.03900  13.16700 0.300 55.09107  ? 365 LEU A CD1 1 
ATOM   137  C CD2 A LEU A 1 35  ? 2.26600   -1.95200  15.09500 0.700 53.22484  ? 365 LEU A CD2 1 
ATOM   138  C CD2 B LEU A 1 35  ? 1.51700   -2.34700  14.47200 0.300 53.03627  ? 365 LEU A CD2 1 
ATOM   139  N N   A GLU A 1 36  ? 0.95700   -6.26700  16.95900 0.700 57.79371  ? 366 GLU A N   1 
ATOM   140  N N   B GLU A 1 36  ? 1.01000   -6.35200  17.28500 0.300 59.83644  ? 366 GLU A N   1 
ATOM   141  C CA  A GLU A 1 36  ? 0.43500   -7.60700  17.17800 0.700 62.61947  ? 366 GLU A CA  1 
ATOM   142  C CA  B GLU A 1 36  ? 0.50700   -7.69000  17.55200 0.300 62.56185  ? 366 GLU A CA  1 
ATOM   143  C C   A GLU A 1 36  ? -0.83500  -7.79200  16.35700 0.700 62.83313  ? 366 GLU A C   1 
ATOM   144  C C   B GLU A 1 36  ? -0.76100  -7.93400  16.74400 0.300 62.96186  ? 366 GLU A C   1 
ATOM   145  O O   A GLU A 1 36  ? -1.40000  -6.83300  15.82300 0.700 65.23755  ? 366 GLU A O   1 
ATOM   146  O O   B GLU A 1 36  ? -1.34400  -7.01300  16.16600 0.300 63.36489  ? 366 GLU A O   1 
ATOM   147  C CB  A GLU A 1 36  ? 0.14900   -7.85900  18.66600 0.700 58.17697  ? 366 GLU A CB  1 
ATOM   148  C CB  B GLU A 1 36  ? 0.22900   -7.88900  19.05100 0.300 58.63597  ? 366 GLU A CB  1 
ATOM   149  C CG  A GLU A 1 36  ? 1.35900   -7.69100  19.57400 0.700 54.09070  ? 366 GLU A CG  1 
ATOM   150  C CG  B GLU A 1 36  ? 1.43400   -7.66900  19.97000 0.300 56.06793  ? 366 GLU A CG  1 
ATOM   151  C CD  A GLU A 1 36  ? 2.40500   -8.77000  19.36300 0.700 65.73186  ? 366 GLU A CD  1 
ATOM   152  C CD  B GLU A 1 36  ? 2.52000   -8.72900  19.83800 0.300 64.55664  ? 366 GLU A CD  1 
ATOM   153  O OE1 A GLU A 1 36  ? 2.03000   -9.90300  18.99200 0.700 66.17745  ? 366 GLU A OE1 1 
ATOM   154  O OE1 B GLU A 1 36  ? 2.43100   -9.59800  18.94500 0.300 65.11416  ? 366 GLU A OE1 1 
ATOM   155  O OE2 A GLU A 1 36  ? 3.60300   -8.48300  19.57100 0.700 75.70139  ? 366 GLU A OE2 1 
ATOM   156  O OE2 B GLU A 1 36  ? 3.47700   -8.68700  20.64000 0.300 66.20600  ? 366 GLU A OE2 1 
ATOM   157  N N   A ASN A 1 37  ? -1.28800  -9.04700  16.28300 0.700 64.59225  ? 367 ASN A N   1 
ATOM   158  N N   B ASN A 1 37  ? -1.18700  -9.19900  16.73100 0.300 64.25230  ? 367 ASN A N   1 
ATOM   159  C CA  A ASN A 1 37  ? -2.56500  -9.40500  15.66200 0.700 62.27110  ? 367 ASN A CA  1 
ATOM   160  C CA  B ASN A 1 37  ? -2.45600  -9.62000  16.13300 0.300 63.08002  ? 367 ASN A CA  1 
ATOM   161  C C   A ASN A 1 37  ? -2.69200  -8.80500  14.26200 0.700 67.78535  ? 367 ASN A C   1 
ATOM   162  C C   B ASN A 1 37  ? -2.60600  -9.09900  14.70400 0.300 66.30685  ? 367 ASN A C   1 
ATOM   163  O O   A ASN A 1 37  ? -3.68700  -8.15700  13.92500 0.700 59.56582  ? 367 ASN A O   1 
ATOM   164  O O   B ASN A 1 37  ? -3.61800  -8.49600  14.33800 0.300 62.87191  ? 367 ASN A O   1 
ATOM   165  C CB  A ASN A 1 37  ? -3.73700  -8.98100  16.54900 0.700 60.58402  ? 367 ASN A CB  1 
ATOM   166  C CB  B ASN A 1 37  ? -3.63600  -9.17900  17.00100 0.300 62.66345  ? 367 ASN A CB  1 
ATOM   167  C CG  A ASN A 1 37  ? -3.81800  -9.78600  17.83100 0.700 68.73633  ? 367 ASN A CG  1 
ATOM   168  C CG  B ASN A 1 37  ? -3.69500  -9.91800  18.32300 0.300 67.51124  ? 367 ASN A CG  1 
ATOM   169  O OD1 A ASN A 1 37  ? -2.92600  -10.57900 18.13500 0.700 73.77340  ? 367 ASN A OD1 1 
ATOM   170  O OD1 B ASN A 1 37  ? -3.54300  -9.32200  19.38900 0.300 60.71136  ? 367 ASN A OD1 1 
ATOM   171  N ND2 A ASN A 1 37  ? -4.88800  -9.58400  18.59300 0.700 65.82132  ? 367 ASN A ND2 1 
ATOM   172  N ND2 B ASN A 1 37  ? -3.91700  -11.22600 18.25800 0.300 69.55464  ? 367 ASN A ND2 1 
ATOM   173  N N   A ASN A 1 38  ? -1.65400  -9.01400  13.44300 0.700 69.69811  ? 368 ASN A N   1 
ATOM   174  N N   B ASN A 1 38  ? -1.56700  -9.32500  13.89600 0.300 67.64090  ? 368 ASN A N   1 
ATOM   175  C CA  A ASN A 1 38  ? -1.66100  -8.57900  12.04300 0.700 72.43976  ? 368 ASN A CA  1 
ATOM   176  C CA  B ASN A 1 38  ? -1.57900  -8.98200  12.47200 0.300 68.88721  ? 368 ASN A CA  1 
ATOM   177  C C   A ASN A 1 38  ? -1.74400  -7.05600  11.96700 0.700 68.71061  ? 368 ASN A C   1 
ATOM   178  C C   B ASN A 1 38  ? -1.71100  -7.47200  12.28200 0.300 67.73715  ? 368 ASN A C   1 
ATOM   179  O O   A ASN A 1 38  ? -2.48800  -6.48900  11.16400 0.700 62.39316  ? 368 ASN A O   1 
ATOM   180  O O   B ASN A 1 38  ? -2.46400  -6.99200  11.43200 0.300 65.49537  ? 368 ASN A O   1 
ATOM   181  C CB  A ASN A 1 38  ? -2.79300  -9.23800  11.24700 0.700 75.25825  ? 368 ASN A CB  1 
ATOM   182  C CB  B ASN A 1 38  ? -2.68200  -9.73900  11.72300 0.300 69.62277  ? 368 ASN A CB  1 
ATOM   183  C CG  A ASN A 1 38  ? -2.62800  -9.07400  9.74200  0.700 80.15983  ? 368 ASN A CG  1 
ATOM   184  C CG  B ASN A 1 38  ? -2.51800  -9.67400  10.21300 0.300 75.69163  ? 368 ASN A CG  1 
ATOM   185  O OD1 A ASN A 1 38  ? -1.53400  -8.79300  9.25100  0.700 82.26763  ? 368 ASN A OD1 1 
ATOM   186  O OD1 B ASN A 1 38  ? -2.11900  -10.65200 9.58000  0.300 73.10492  ? 368 ASN A OD1 1 
ATOM   187  N ND2 A ASN A 1 38  ? -3.72200  -9.24200  9.00500  0.700 70.91805  ? 368 ASN A ND2 1 
ATOM   188  N ND2 B ASN A 1 38  ? -2.83600  -8.52400  9.63000  0.300 76.99379  ? 368 ASN A ND2 1 
ATOM   189  N N   A GLY A 1 39  ? -0.97400  -6.38800  12.82400 0.700 68.25886  ? 369 GLY A N   1 
ATOM   190  N N   B GLY A 1 39  ? -0.97300  -6.71600  13.09100 0.300 66.73542  ? 369 GLY A N   1 
ATOM   191  C CA  A GLY A 1 39  ? -0.87900  -4.94600  12.78500 0.700 61.62804  ? 369 GLY A CA  1 
ATOM   192  C CA  B GLY A 1 39  ? -0.91000  -5.27600  12.95900 0.300 62.77092  ? 369 GLY A CA  1 
ATOM   193  C C   A GLY A 1 39  ? -2.05600  -4.21000  13.38100 0.700 60.50900  ? 369 GLY A C   1 
ATOM   194  C C   B GLY A 1 39  ? -2.11100  -4.52500  13.48500 0.300 61.31363  ? 369 GLY A C   1 
ATOM   195  O O   A GLY A 1 39  ? -2.17600  -2.99700  13.17200 0.700 65.78235  ? 369 GLY A O   1 
ATOM   196  O O   B GLY A 1 39  ? -2.24800  -3.33100  13.19600 0.300 63.81276  ? 369 GLY A O   1 
ATOM   197  N N   A SER A 1 40  ? -2.92800  -4.89800  14.12100 0.700 58.76513  ? 370 SER A N   1 
ATOM   198  N N   B SER A 1 40  ? -2.98500  -5.18000  14.24900 0.300 59.44253  ? 370 SER A N   1 
ATOM   199  C CA  A SER A 1 40  ? -4.12900  -4.27800  14.65500 0.700 51.30234  ? 370 SER A CA  1 
ATOM   200  C CA  B SER A 1 40  ? -4.21100  -4.56200  14.73500 0.300 53.86068  ? 370 SER A CA  1 
ATOM   201  C C   A SER A 1 40  ? -3.99300  -3.87600  16.12300 0.700 50.39741  ? 370 SER A C   1 
ATOM   202  C C   B SER A 1 40  ? -4.10100  -4.09300  16.17900 0.300 51.11955  ? 370 SER A C   1 
ATOM   203  O O   A SER A 1 40  ? -4.87500  -3.17300  16.63200 0.700 57.34745  ? 370 SER A O   1 
ATOM   204  O O   B SER A 1 40  ? -4.99100  -3.37900  16.65300 0.300 55.80861  ? 370 SER A O   1 
ATOM   205  C CB  A SER A 1 40  ? -5.33200  -5.22800  14.48800 0.700 53.14117  ? 370 SER A CB  1 
ATOM   206  C CB  B SER A 1 40  ? -5.38800  -5.53700  14.60400 0.300 55.42420  ? 370 SER A CB  1 
ATOM   207  O OG  A SER A 1 40  ? -5.17900  -6.40500  15.26500 0.700 61.35194  ? 370 SER A OG  1 
ATOM   208  O OG  B SER A 1 40  ? -5.21500  -6.66400  15.44400 0.300 62.16549  ? 370 SER A OG  1 
ATOM   209  N N   A VAL A 1 41  ? -2.93000  -4.30600  16.81500 0.700 45.08567  ? 371 VAL A N   1 
ATOM   210  N N   B VAL A 1 41  ? -3.03500  -4.47300  16.88000 0.300 46.43640  ? 371 VAL A N   1 
ATOM   211  C CA  A VAL A 1 41  ? -2.71800  -3.98300  18.22300 0.700 45.45013  ? 371 VAL A CA  1 
ATOM   212  C CA  B VAL A 1 41  ? -2.81600  -4.11200  18.27400 0.300 45.97841  ? 371 VAL A CA  1 
ATOM   213  C C   A VAL A 1 41  ? -1.28400  -3.50000  18.38700 0.700 50.42985  ? 371 VAL A C   1 
ATOM   214  C C   B VAL A 1 41  ? -1.39300  -3.59100  18.40700 0.300 50.42389  ? 371 VAL A C   1 
ATOM   215  O O   A VAL A 1 41  ? -0.35300  -4.09600  17.82200 0.700 56.11424  ? 371 VAL A O   1 
ATOM   216  O O   B VAL A 1 41  ? -0.45500  -4.17700  17.85500 0.300 55.78339  ? 371 VAL A O   1 
ATOM   217  C CB  A VAL A 1 41  ? -2.98200  -5.20200  19.12800 0.700 52.28412  ? 371 VAL A CB  1 
ATOM   218  C CB  B VAL A 1 41  ? -3.04700  -5.31000  19.22100 0.300 52.56041  ? 371 VAL A CB  1 
ATOM   219  C CG1 A VAL A 1 41  ? -2.65600  -4.87600  20.56300 0.700 54.17723  ? 371 VAL A CG1 1 
ATOM   220  C CG1 B VAL A 1 41  ? -2.70700  -4.93300  20.65200 0.300 54.30082  ? 371 VAL A CG1 1 
ATOM   221  C CG2 A VAL A 1 41  ? -4.40700  -5.68600  18.99500 0.700 51.17803  ? 371 VAL A CG2 1 
ATOM   222  C CG2 B VAL A 1 41  ? -4.48100  -5.79700  19.12900 0.300 51.75665  ? 371 VAL A CG2 1 
ATOM   223  N N   A ILE A 1 42  ? -1.11400  -2.40200  19.13200 0.700 49.70167  ? 372 ILE A N   1 
ATOM   224  N N   B ILE A 1 42  ? -1.23200  -2.49100  19.13700 0.300 49.64802  ? 372 ILE A N   1 
ATOM   225  C CA  A ILE A 1 42  ? 0.19800   -1.91100  19.52200 0.700 53.75690  ? 372 ILE A CA  1 
ATOM   226  C CA  B ILE A 1 42  ? 0.08100   -1.96900  19.49800 0.300 53.36266  ? 372 ILE A CA  1 
ATOM   227  C C   A ILE A 1 42  ? 0.34200   -2.07400  21.04200 0.700 49.08609  ? 372 ILE A C   1 
ATOM   228  C C   B ILE A 1 42  ? 0.28100   -2.15800  20.99400 0.300 49.71361  ? 372 ILE A C   1 
ATOM   229  O O   A ILE A 1 42  ? -0.55600  -1.69500  21.80600 0.700 52.88754  ? 372 ILE A O   1 
ATOM   230  O O   B ILE A 1 42  ? -0.57600  -1.76900  21.79700 0.300 52.54789  ? 372 ILE A O   1 
ATOM   231  C CB  A ILE A 1 42  ? 0.41000   -0.46700  19.04000 0.700 39.18092  ? 372 ILE A CB  1 
ATOM   232  C CB  B ILE A 1 42  ? 0.22700   -0.49100  19.09900 0.300 40.20366  ? 372 ILE A CB  1 
ATOM   233  C CG1 A ILE A 1 42  ? 0.31400   -0.38700  17.48400 0.700 43.57674  ? 372 ILE A CG1 1 
ATOM   234  C CG1 B ILE A 1 42  ? 0.15500   -0.35700  17.57700 0.300 43.62651  ? 372 ILE A CG1 1 
ATOM   235  C CG2 A ILE A 1 42  ? 1.76400   0.08000   19.59900 0.700 44.98817  ? 372 ILE A CG2 1 
ATOM   236  C CG2 B ILE A 1 42  ? 1.52700   0.08500   19.64700 0.300 44.81240  ? 372 ILE A CG2 1 
ATOM   237  C CD1 A ILE A 1 42  ? 0.43200   1.03700   16.98600 0.700 43.11240  ? 372 ILE A CD1 1 
ATOM   238  C CD1 B ILE A 1 42  ? 0.81700   0.87900   17.03400 0.300 44.01776  ? 372 ILE A CD1 1 
ATOM   239  N N   A CYS A 1 43  ? 1.45400   -2.67000  21.46100 0.700 37.47849  ? 373 CYS A N   1 
ATOM   240  N N   B CYS A 1 43  ? 1.41600   -2.74300  21.36200 0.300 39.92718  ? 373 CYS A N   1 
ATOM   241  C CA  A CYS A 1 43  ? 1.85200   -2.88300  22.84700 0.700 46.96933  ? 373 CYS A CA  1 
ATOM   242  C CA  B CYS A 1 43  ? 1.81700   -2.93100  22.74900 0.300 47.58016  ? 373 CYS A CA  1 
ATOM   243  C C   A CYS A 1 43  ? 3.11000   -2.09700  23.18600 0.700 46.40896  ? 373 CYS A C   1 
ATOM   244  C C   B CYS A 1 43  ? 3.06500   -2.11200  23.05300 0.300 46.87401  ? 373 CYS A C   1 
ATOM   245  O O   A CYS A 1 43  ? 4.04400   -2.03400  22.38000 0.700 49.98342  ? 373 CYS A O   1 
ATOM   246  O O   B CYS A 1 43  ? 3.99200   -2.04600  22.23900 0.300 49.48977  ? 373 CYS A O   1 
ATOM   247  C CB  A CYS A 1 43  ? 2.07200   -4.37100  23.09900 0.700 57.38506  ? 373 CYS A CB  1 
ATOM   248  C CB  B CYS A 1 43  ? 2.05600   -4.41100  23.06300 0.300 57.25925  ? 373 CYS A CB  1 
ATOM   249  S SG  A CYS A 1 43  ? 0.61500   -5.40800  22.78100 0.700 50.84122  ? 373 CYS A SG  1 
ATOM   250  S SG  B CYS A 1 43  ? 0.61100   -5.47000  22.78600 0.300 55.66692  ? 373 CYS A SG  1 
ATOM   251  N N   A ILE A 1 44  ? 3.13300   -1.52600  24.39000 0.700 47.80820  ? 374 ILE A N   1 
ATOM   252  N N   B ILE A 1 44  ? 3.08000   -1.49600  24.23000 0.300 47.79025  ? 374 ILE A N   1 
ATOM   253  C CA  A ILE A 1 44  ? 4.22800   -0.65900  24.81100 0.700 51.70402  ? 374 ILE A CA  1 
ATOM   254  C CA  B ILE A 1 44  ? 4.15400   -0.59200  24.64100 0.300 51.54178  ? 374 ILE A CA  1 
ATOM   255  C C   A ILE A 1 44  ? 4.60800   -1.04200  26.24200 0.700 39.56207  ? 374 ILE A C   1 
ATOM   256  C C   B ILE A 1 44  ? 4.52400   -0.89600  26.08400 0.300 40.58702  ? 374 ILE A C   1 
ATOM   257  O O   A ILE A 1 44  ? 3.81800   -1.63700  26.97400 0.700 42.53167  ? 374 ILE A O   1 
ATOM   258  O O   B ILE A 1 44  ? 3.73000   -1.47300  26.83800 0.300 43.23009  ? 374 ILE A O   1 
ATOM   259  C CB  A ILE A 1 44  ? 3.82800   0.83700   24.79600 0.700 54.78670  ? 374 ILE A CB  1 
ATOM   260  C CB  B ILE A 1 44  ? 3.74100   0.88900   24.50600 0.300 52.62935  ? 374 ILE A CB  1 
ATOM   261  C CG1 A ILE A 1 44  ? 2.47900   1.07300   25.48300 0.700 48.80666  ? 374 ILE A CG1 1 
ATOM   262  C CG1 B ILE A 1 44  ? 2.33600   1.10800   25.07000 0.300 49.42858  ? 374 ILE A CG1 1 
ATOM   263  C CG2 A ILE A 1 44  ? 3.70000   1.35600   23.37100 0.700 43.63541  ? 374 ILE A CG2 1 
ATOM   264  C CG2 B ILE A 1 44  ? 3.80100   1.33500   23.05900 0.300 45.88956  ? 374 ILE A CG2 1 
ATOM   265  C CD1 A ILE A 1 44  ? 2.38600   2.44600   26.11600 0.700 58.89158  ? 374 ILE A CD1 1 
ATOM   266  C CD1 B ILE A 1 44  ? 2.10900   2.50300   25.61300 0.300 55.86017  ? 374 ILE A CD1 1 
ATOM   267  N N   A PRO A 1 45  ? 5.84100   -0.71600  26.63100 0.700 31.29362  ? 375 PRO A N   1 
ATOM   268  N N   B PRO A 1 45  ? 5.74000   -0.52800  26.49300 0.300 33.31486  ? 375 PRO A N   1 
ATOM   269  C CA  A PRO A 1 45  ? 6.19500   -0.85300  28.04500 0.700 44.04929  ? 375 PRO A CA  1 
ATOM   270  C CA  B PRO A 1 45  ? 6.08200   -0.61300  27.91800 0.300 44.31228  ? 375 PRO A CA  1 
ATOM   271  C C   A PRO A 1 45  ? 5.28100   0.05500   28.85200 0.700 41.69644  ? 375 PRO A C   1 
ATOM   272  C C   B PRO A 1 45  ? 5.16600   0.26500   28.75600 0.300 43.56487  ? 375 PRO A C   1 
ATOM   273  O O   A PRO A 1 45  ? 5.01900   1.20200   28.48200 0.700 52.59149  ? 375 PRO A O   1 
ATOM   274  O O   B PRO A 1 45  ? 4.87500   1.41100   28.40500 0.300 53.74012  ? 375 PRO A O   1 
ATOM   275  C CB  A PRO A 1 45  ? 7.66300   -0.40400  28.09700 0.700 52.07317  ? 375 PRO A CB  1 
ATOM   276  C CB  B PRO A 1 45  ? 7.53800   -0.13200  27.97300 0.300 51.52000  ? 375 PRO A CB  1 
ATOM   277  C CG  A PRO A 1 45  ? 8.15200   -0.45700  26.70000 0.700 49.99461  ? 375 PRO A CG  1 
ATOM   278  C CG  B PRO A 1 45  ? 8.04200   -0.21300  26.57400 0.300 50.28624  ? 375 PRO A CG  1 
ATOM   279  C CD  A PRO A 1 45  ? 6.96500   -0.23400  25.81800 0.700 42.67073  ? 375 PRO A CD  1 
ATOM   280  C CD  B PRO A 1 45  ? 6.86400   -0.04100  25.67600 0.300 43.30956  ? 375 PRO A CD  1 
ATOM   281  N N   A ASN A 1 46  ? 4.78900   -0.47700  29.97000 0.700 46.16658  ? 376 ASN A N   1 
ATOM   282  N N   B ASN A 1 46  ? 4.70900   -0.29200  29.87800 0.300 45.92339  ? 376 ASN A N   1 
ATOM   283  C CA  A ASN A 1 46  ? 4.02300   0.29800   30.94700 0.700 34.70086  ? 376 ASN A CA  1 
ATOM   284  C CA  B ASN A 1 46  ? 3.96000   0.46100   30.88400 0.300 35.83355  ? 376 ASN A CA  1 
ATOM   285  C C   A ASN A 1 46  ? 4.95000   1.09700   31.86100 0.700 46.30567  ? 376 ASN A C   1 
ATOM   286  C C   B ASN A 1 46  ? 4.93300   1.23700   31.77400 0.300 46.58107  ? 376 ASN A C   1 
ATOM   287  O O   A ASN A 1 46  ? 5.07800   0.84400   33.06000 0.700 48.53744  ? 376 ASN A O   1 
ATOM   288  O O   B ASN A 1 46  ? 5.11600   0.95800   32.96000 0.300 48.44795  ? 376 ASN A O   1 
ATOM   289  C CB  A ASN A 1 46  ? 3.11300   -0.61700  31.75100 0.700 51.45002  ? 376 ASN A CB  1 
ATOM   290  C CB  B ASN A 1 46  ? 3.07800   -0.47300  31.70000 0.300 50.77966  ? 376 ASN A CB  1 
ATOM   291  C CG  A ASN A 1 46  ? 2.06700   0.15200   32.53400 0.700 53.23860  ? 376 ASN A CG  1 
ATOM   292  C CG  B ASN A 1 46  ? 2.04000   0.27100   32.52000 0.300 53.52066  ? 376 ASN A CG  1 
ATOM   293  O OD1 A ASN A 1 46  ? 2.05300   1.38400   32.52900 0.700 64.42971  ? 376 ASN A OD1 1 
ATOM   294  O OD1 B ASN A 1 46  ? 2.00600   1.50100   32.53400 0.300 63.80056  ? 376 ASN A OD1 1 
ATOM   295  N ND2 A ASN A 1 46  ? 1.18300   -0.57200  33.21400 0.700 58.46334  ? 376 ASN A ND2 1 
ATOM   296  N ND2 B ASN A 1 46  ? 1.18800   -0.47600  33.21100 0.300 58.45340  ? 376 ASN A ND2 1 
ATOM   297  N N   A ASN A 1 47  ? 5.58600   2.10400   31.26400 0.700 56.57740  ? 377 ASN A N   1 
ATOM   298  N N   B ASN A 1 47  ? 5.56600   2.23900   31.16600 0.300 56.52543  ? 377 ASN A N   1 
ATOM   299  C CA  A ASN A 1 47  ? 6.58400   2.92100   31.94000 0.700 51.25556  ? 377 ASN A CA  1 
ATOM   300  C CA  B ASN A 1 47  ? 6.60000   3.02500   31.82400 0.300 51.65820  ? 377 ASN A CA  1 
ATOM   301  C C   A ASN A 1 47  ? 6.09300   4.34400   32.19100 0.700 48.66352  ? 377 ASN A C   1 
ATOM   302  C C   B ASN A 1 47  ? 6.14800   4.45300   32.10000 0.300 48.44070  ? 377 ASN A C   1 
ATOM   303  O O   A ASN A 1 47  ? 6.89300   5.21600   32.54800 0.700 45.77569  ? 377 ASN A O   1 
ATOM   304  O O   B ASN A 1 47  ? 6.97600   5.30400   32.44300 0.300 45.95281  ? 377 ASN A O   1 
ATOM   305  C CB  A ASN A 1 47  ? 7.88600   2.93500   31.13300 0.700 53.33155  ? 377 ASN A CB  1 
ATOM   306  C CB  B ASN A 1 47  ? 7.88100   3.01700   30.98400 0.300 53.40067  ? 377 ASN A CB  1 
ATOM   307  C CG  A ASN A 1 47  ? 7.69300   3.43900   29.71300 0.700 58.63848  ? 377 ASN A CG  1 
ATOM   308  C CG  B ASN A 1 47  ? 7.66200   3.54100   29.57400 0.300 58.18513  ? 377 ASN A CG  1 
ATOM   309  O OD1 A ASN A 1 47  ? 6.58200   3.78500   29.30500 0.700 56.48123  ? 377 ASN A OD1 1 
ATOM   310  O OD1 B ASN A 1 47  ? 6.55000   3.91600   29.20100 0.300 55.70639  ? 377 ASN A OD1 1 
ATOM   311  N ND2 A ASN A 1 47  ? 8.78000   3.47500   28.94800 0.700 59.06184  ? 377 ASN A ND2 1 
ATOM   312  N ND2 B ASN A 1 47  ? 8.72700   3.55800   28.78000 0.300 58.99965  ? 377 ASN A ND2 1 
ATOM   313  N N   A GLY A 1 48  ? 4.79300   4.59300   32.01300 0.700 48.31542  ? 378 GLY A N   1 
ATOM   314  N N   B GLY A 1 48  ? 4.85200   4.73200   31.95400 0.300 48.07542  ? 378 GLY A N   1 
ATOM   315  C CA  A GLY A 1 48  ? 4.19400   5.89700   32.21200 0.700 47.95390  ? 378 GLY A CA  1 
ATOM   316  C CA  B GLY A 1 48  ? 4.29300   6.04700   32.17500 0.300 48.23035  ? 378 GLY A CA  1 
ATOM   317  C C   A GLY A 1 48  ? 4.25200   6.85200   31.04100 0.700 48.75148  ? 378 GLY A C   1 
ATOM   318  C C   B GLY A 1 48  ? 4.36200   6.99300   30.99600 0.300 49.02115  ? 378 GLY A C   1 
ATOM   319  O O   A GLY A 1 48  ? 3.57000   7.88500   31.07500 0.700 55.20552  ? 378 GLY A O   1 
ATOM   320  O O   B GLY A 1 48  ? 3.73500   8.05900   31.04400 0.300 54.42470  ? 378 GLY A O   1 
ATOM   321  N N   A GLN A 1 49  ? 5.02000   6.53900   30.00100 0.700 52.81100  ? 379 GLN A N   1 
ATOM   322  N N   B GLN A 1 49  ? 5.10300   6.65000   29.94700 0.300 52.50074  ? 379 GLN A N   1 
ATOM   323  C CA  A GLN A 1 49  ? 5.16700   7.44200   28.86600 0.700 42.30218  ? 379 GLN A CA  1 
ATOM   324  C CA  B GLN A 1 49  ? 5.25200   7.54600   28.81000 0.300 43.44959  ? 379 GLN A CA  1 
ATOM   325  C C   A GLN A 1 49  ? 3.96600   7.35700   27.93000 0.700 47.23120  ? 379 GLN A C   1 
ATOM   326  C C   B GLN A 1 49  ? 4.03400   7.49200   27.89500 0.300 47.40386  ? 379 GLN A C   1 
ATOM   327  O O   A GLN A 1 49  ? 3.35800   6.29500   27.75600 0.700 56.72836  ? 379 GLN A O   1 
ATOM   328  O O   B GLN A 1 49  ? 3.39000   6.45100   27.73800 0.300 55.90555  ? 379 GLN A O   1 
ATOM   329  C CB  A GLN A 1 49  ? 6.45000   7.13800   28.09800 0.700 45.22827  ? 379 GLN A CB  1 
ATOM   330  C CB  B GLN A 1 49  ? 6.51500   7.19500   28.02200 0.300 46.54363  ? 379 GLN A CB  1 
ATOM   331  C CG  A GLN A 1 49  ? 7.71300   7.43000   28.88900 0.700 54.67764  ? 379 GLN A CG  1 
ATOM   332  C CG  B GLN A 1 49  ? 7.80300   7.44500   28.79100 0.300 54.87599  ? 379 GLN A CG  1 
ATOM   333  C CD  A GLN A 1 49  ? 8.96500   7.35400   28.04000 0.700 64.18468  ? 379 GLN A CD  1 
ATOM   334  C CD  B GLN A 1 49  ? 9.03900   7.32400   27.92200 0.300 63.97703  ? 379 GLN A CD  1 
ATOM   335  O OE1 A GLN A 1 49  ? 8.90200   7.04800   26.84900 0.700 69.88343  ? 379 GLN A OE1 1 
ATOM   336  O OE1 B GLN A 1 49  ? 8.97400   6.83300   26.79600 0.300 69.58509  ? 379 GLN A OE1 1 
ATOM   337  N NE2 A GLN A 1 49  ? 10.11400  7.61800   28.65100 0.700 71.72089  ? 379 GLN A NE2 1 
ATOM   338  N NE2 B GLN A 1 49  ? 10.17500  7.77100   28.44400 0.300 71.46001  ? 379 GLN A NE2 1 
ATOM   339  N N   A CYS A 1 50  ? 3.63600   8.49400   27.31700 0.700 50.26707  ? 380 CYS A N   1 
ATOM   340  N N   B CYS A 1 50  ? 3.72200   8.63600   27.29000 0.300 49.84754  ? 380 CYS A N   1 
ATOM   341  C CA  A CYS A 1 50  ? 2.62000   8.57700   26.28100 0.700 40.51125  ? 380 CYS A CA  1 
ATOM   342  C CA  B CYS A 1 50  ? 2.69300   8.71300   26.26600 0.300 41.23014  ? 380 CYS A CA  1 
ATOM   343  C C   A CYS A 1 50  ? 3.16700   8.03200   24.96000 0.700 42.90904  ? 380 CYS A C   1 
ATOM   344  C C   B CYS A 1 50  ? 3.21900   8.16200   24.94200 0.300 43.94732  ? 380 CYS A C   1 
ATOM   345  O O   A CYS A 1 50  ? 4.37900   8.02700   24.71000 0.700 53.39531  ? 380 CYS A O   1 
ATOM   346  O O   B CYS A 1 50  ? 4.42500   8.13200   24.68800 0.300 54.22927  ? 380 CYS A O   1 
ATOM   347  C CB  A CYS A 1 50  ? 2.17300   10.02700  26.10700 0.700 42.84173  ? 380 CYS A CB  1 
ATOM   348  C CB  B CYS A 1 50  ? 2.21100   10.15300  26.08100 0.300 43.76733  ? 380 CYS A CB  1 
ATOM   349  S SG  A CYS A 1 50  ? 1.65000   10.79800  27.66300 0.700 40.75541  ? 380 CYS A SG  1 
ATOM   350  S SG  B CYS A 1 50  ? 1.69600   10.98500  27.60100 0.300 36.76894  ? 380 CYS A SG  1 
ATOM   351  N N   A PHE A 1 51  ? 2.25400   7.60400   24.08800 0.700 39.37332  ? 381 PHE A N   1 
ATOM   352  N N   B PHE A 1 51  ? 2.29200   7.73500   24.08700 0.300 40.73540  ? 381 PHE A N   1 
ATOM   353  C CA  A PHE A 1 51  ? 2.62700   6.98700   22.82100 0.700 44.56855  ? 381 PHE A CA  1 
ATOM   354  C CA  B PHE A 1 51  ? 2.64700   7.11900   22.81700 0.300 45.07351  ? 381 PHE A CA  1 
ATOM   355  C C   A PHE A 1 51  ? 1.66600   7.45000   21.73600 0.700 43.60375  ? 381 PHE A C   1 
ATOM   356  C C   B PHE A 1 51  ? 1.66400   7.58800   21.75600 0.300 44.28105  ? 381 PHE A C   1 
ATOM   357  O O   A PHE A 1 51  ? 0.45900   7.58100   21.97400 0.700 39.32787  ? 381 PHE A O   1 
ATOM   358  O O   B PHE A 1 51  ? 0.46200   7.69100   22.01600 0.300 40.30905  ? 381 PHE A O   1 
ATOM   359  C CB  A PHE A 1 51  ? 2.63000   5.45100   22.90300 0.700 50.63498  ? 381 PHE A CB  1 
ATOM   360  C CB  B PHE A 1 51  ? 2.64000   5.58600   22.90500 0.300 50.34795  ? 381 PHE A CB  1 
ATOM   361  C CG  A PHE A 1 51  ? 2.72500   4.77000   21.55800 0.700 48.99156  ? 381 PHE A CG  1 
ATOM   362  C CG  B PHE A 1 51  ? 2.72000   4.90100   21.56800 0.300 49.30731  ? 381 PHE A CG  1 
ATOM   363  C CD1 A PHE A 1 51  ? 3.95700   4.59000   20.94200 0.700 40.34051  ? 381 PHE A CD1 1 
ATOM   364  C CD1 B PHE A 1 51  ? 3.94300   4.70900   20.94900 0.300 41.59438  ? 381 PHE A CD1 1 
ATOM   365  C CD2 A PHE A 1 51  ? 1.58800   4.29500   20.92300 0.700 36.61441  ? 381 PHE A CD2 1 
ATOM   366  C CD2 B PHE A 1 51  ? 1.57500   4.44200   20.93400 0.300 38.21398  ? 381 PHE A CD2 1 
ATOM   367  C CE1 A PHE A 1 51  ? 4.04500   3.96600   19.71100 0.700 42.03713  ? 381 PHE A CE1 1 
ATOM   368  C CE1 B PHE A 1 51  ? 4.02500   4.08100   19.72100 0.300 42.99485  ? 381 PHE A CE1 1 
ATOM   369  C CE2 A PHE A 1 51  ? 1.67000   3.66600   19.69900 0.700 34.72126  ? 381 PHE A CE2 1 
ATOM   370  C CE2 B PHE A 1 51  ? 1.65100   3.81300   19.70500 0.300 36.30017  ? 381 PHE A CE2 1 
ATOM   371  C CZ  A PHE A 1 51  ? 2.89700   3.50100   19.09000 0.700 45.13023  ? 381 PHE A CZ  1 
ATOM   372  C CZ  B PHE A 1 51  ? 2.87800   3.63200   19.09900 0.300 45.53665  ? 381 PHE A CZ  1 
ATOM   373  N N   A CYS A 1 52  ? 2.21700   7.70600   20.55000 0.700 42.96550  ? 382 CYS A N   1 
ATOM   374  N N   B CYS A 1 52  ? 2.18400   7.86400   20.56100 0.300 42.35130  ? 382 CYS A N   1 
ATOM   375  C CA  A CYS A 1 52  ? 1.41000   7.94300   19.36600 0.700 41.31031  ? 382 CYS A CA  1 
ATOM   376  C CA  B CYS A 1 52  ? 1.35200   8.11000   19.39200 0.300 41.41751  ? 382 CYS A CA  1 
ATOM   377  C C   A CYS A 1 52  ? 2.27900   7.82200   18.12400 0.700 40.10584  ? 382 CYS A C   1 
ATOM   378  C C   B CYS A 1 52  ? 2.19400   8.02300   18.12900 0.300 41.03031  ? 382 CYS A C   1 
ATOM   379  O O   A CYS A 1 52  ? 3.41300   8.31500   18.09900 0.700 39.29336  ? 382 CYS A O   1 
ATOM   380  O O   B CYS A 1 52  ? 3.31500   8.53700   18.09000 0.300 40.79242  ? 382 CYS A O   1 
ATOM   381  C CB  A CYS A 1 52  ? 0.75800   9.32700   19.39700 0.700 39.87475  ? 382 CYS A CB  1 
ATOM   382  C CB  B CYS A 1 52  ? 0.67000   9.48100   19.46000 0.300 40.73201  ? 382 CYS A CB  1 
ATOM   383  S SG  A CYS A 1 52  ? -0.68700  9.48500   18.32500 0.700 39.05456  ? 382 CYS A SG  1 
ATOM   384  S SG  B CYS A 1 52  ? -0.79700  9.60600   18.41500 0.300 36.11539  ? 382 CYS A SG  1 
ATOM   385  N N   A LEU A 1 53  ? 1.74600   7.14600   17.10500 0.700 46.01534  ? 383 LEU A N   1 
ATOM   386  N N   B LEU A 1 53  ? 1.65100   7.35900   17.10600 0.300 46.44231  ? 383 LEU A N   1 
ATOM   387  C CA  A LEU A 1 53  ? 2.51100   6.93200   15.88400 0.700 49.53521  ? 383 LEU A CA  1 
ATOM   388  C CA  B LEU A 1 53  ? 2.39900   7.18200   15.86600 0.300 49.25063  ? 383 LEU A CA  1 
ATOM   389  C C   A LEU A 1 53  ? 2.77600   8.26300   15.19300 0.700 48.19117  ? 383 LEU A C   1 
ATOM   390  C C   B LEU A 1 53  ? 2.63400   8.52900   15.19800 0.300 48.62252  ? 383 LEU A C   1 
ATOM   391  O O   A LEU A 1 53  ? 3.86800   8.48400   14.65600 0.700 52.81462  ? 383 LEU A O   1 
ATOM   392  O O   B LEU A 1 53  ? 3.71200   8.77300   14.64100 0.300 53.30080  ? 383 LEU A O   1 
ATOM   393  C CB  A LEU A 1 53  ? 1.75500   5.97300   14.96600 0.700 50.13052  ? 383 LEU A CB  1 
ATOM   394  C CB  B LEU A 1 53  ? 1.65600   6.23600   14.92600 0.300 49.35980  ? 383 LEU A CB  1 
ATOM   395  C CG  A LEU A 1 53  ? 1.89700   4.48900   15.29700 0.700 39.15791  ? 383 LEU A CG  1 
ATOM   396  C CG  B LEU A 1 53  ? 1.83900   4.74900   15.22400 0.300 41.53050  ? 383 LEU A CG  1 
ATOM   397  C CD1 A LEU A 1 53  ? 1.03700   3.65900   14.35700 0.700 53.24245  ? 383 LEU A CD1 1 
ATOM   398  C CD1 B LEU A 1 53  ? 0.68300   4.26400   16.07500 0.300 38.87785  ? 383 LEU A CD1 1 
ATOM   399  C CD2 A LEU A 1 53  ? 3.35500   4.05600   15.22500 0.700 38.17304  ? 383 LEU A CD2 1 
ATOM   400  C CD2 B LEU A 1 53  ? 1.94800   3.93900   13.94100 0.300 52.36172  ? 383 LEU A CD2 1 
ATOM   401  N N   A ALA A 1 54  ? 1.77100   9.14900   15.18000 0.700 52.07265  ? 384 ALA A N   1 
ATOM   402  N N   B ALA A 1 54  ? 1.62000   9.40200   15.22200 0.300 51.18988  ? 384 ALA A N   1 
ATOM   403  C CA  A ALA A 1 54  ? 1.87700   10.41800  14.46700 0.700 45.44831  ? 384 ALA A CA  1 
ATOM   404  C CA  B ALA A 1 54  ? 1.70100   10.68400  14.52800 0.300 47.19885  ? 384 ALA A CA  1 
ATOM   405  C C   A ALA A 1 54  ? 3.09500   11.20300  14.93000 0.700 44.48140  ? 384 ALA A C   1 
ATOM   406  C C   B ALA A 1 54  ? 2.92600   11.46900  14.97600 0.300 46.85497  ? 384 ALA A C   1 
ATOM   407  O O   A ALA A 1 54  ? 3.72500   11.90800  14.13200 0.700 56.52118  ? 384 ALA A O   1 
ATOM   408  O O   B ALA A 1 54  ? 3.53100   12.19100  14.17500 0.300 56.42587  ? 384 ALA A O   1 
ATOM   409  C CB  A ALA A 1 54  ? 0.60600   11.24300  14.65700 0.700 38.66015  ? 384 ALA A CB  1 
ATOM   410  C CB  B ALA A 1 54  ? 0.42800   11.49400  14.76400 0.300 42.14247  ? 384 ALA A CB  1 
ATOM   411  N N   A TRP A 1 55  ? 3.43600   11.09700  16.21900 0.700 42.29721  ? 385 TRP A N   1 
ATOM   412  N N   B TRP A 1 55  ? 3.29900   11.34200  16.25300 0.300 43.11898  ? 385 TRP A N   1 
ATOM   413  C CA  A TRP A 1 55  ? 4.57000   11.82900  16.76700 0.700 45.93591  ? 385 TRP A CA  1 
ATOM   414  C CA  B TRP A 1 55  ? 4.44100   12.07100  16.78800 0.300 46.72768  ? 385 TRP A CA  1 
ATOM   415  C C   A TRP A 1 55  ? 5.89200   11.34100  16.19900 0.700 53.55031  ? 385 TRP A C   1 
ATOM   416  C C   B TRP A 1 55  ? 5.74900   11.59300  16.17800 0.300 53.79426  ? 385 TRP A C   1 
ATOM   417  O O   A TRP A 1 55  ? 6.87700   12.08700  16.22800 0.700 58.18361  ? 385 TRP A O   1 
ATOM   418  O O   B TRP A 1 55  ? 6.73100   12.34400  16.18100 0.300 57.56187  ? 385 TRP A O   1 
ATOM   419  C CB  A TRP A 1 55  ? 4.61100   11.72800  18.29500 0.700 40.38469  ? 385 TRP A CB  1 
ATOM   420  C CB  B TRP A 1 55  ? 4.51400   11.92800  18.31000 0.300 41.67802  ? 385 TRP A CB  1 
ATOM   421  C CG  A TRP A 1 55  ? 3.41300   12.27500  18.99600 0.700 40.74497  ? 385 TRP A CG  1 
ATOM   422  C CG  B TRP A 1 55  ? 3.32000   12.44600  19.04600 0.300 41.65126  ? 385 TRP A CG  1 
ATOM   423  C CD1 A TRP A 1 55  ? 2.54100   13.21600  18.52500 0.700 42.28940  ? 385 TRP A CD1 1 
ATOM   424  C CD1 B TRP A 1 55  ? 2.43100   13.38600  18.61300 0.300 42.48114  ? 385 TRP A CD1 1 
ATOM   425  C CD2 A TRP A 1 55  ? 2.96900   11.94000  20.31500 0.700 43.23924  ? 385 TRP A CD2 1 
ATOM   426  C CD2 B TRP A 1 55  ? 2.89400   12.06500  20.35900 0.300 43.67203  ? 385 TRP A CD2 1 
ATOM   427  N NE1 A TRP A 1 55  ? 1.57100   13.47600  19.46700 0.700 41.38048  ? 385 TRP A NE1 1 
ATOM   428  N NE1 B TRP A 1 55  ? 1.47100   13.60700  19.57200 0.300 40.67113  ? 385 TRP A NE1 1 
ATOM   429  C CE2 A TRP A 1 55  ? 1.81200   12.70300  20.57500 0.700 39.86252  ? 385 TRP A CE2 1 
ATOM   430  C CE2 B TRP A 1 55  ? 1.73400   12.80800  20.65400 0.300 40.58012  ? 385 TRP A CE2 1 
ATOM   431  C CE3 A TRP A 1 55  ? 3.43300   11.06000  21.30000 0.700 47.04946  ? 385 TRP A CE3 1 
ATOM   432  C CE3 B TRP A 1 55  ? 3.37800   11.16400  21.31200 0.300 47.45069  ? 385 TRP A CE3 1 
ATOM   433  C CZ2 A TRP A 1 55  ? 1.11100   12.61300  21.78100 0.700 38.76545  ? 385 TRP A CZ2 1 
ATOM   434  C CZ2 B TRP A 1 55  ? 1.05100   12.67800  21.86200 0.300 39.37747  ? 385 TRP A CZ2 1 
ATOM   435  C CZ3 A TRP A 1 55  ? 2.73500   10.97400  22.49800 0.700 45.50162  ? 385 TRP A CZ3 1 
ATOM   436  C CZ3 B TRP A 1 55  ? 2.69900   11.03600  22.51000 0.300 45.16126  ? 385 TRP A CZ3 1 
ATOM   437  C CH2 A TRP A 1 55  ? 1.58900   11.74800  22.72700 0.700 33.84847  ? 385 TRP A CH2 1 
ATOM   438  C CH2 B TRP A 1 55  ? 1.54900   11.78900  22.77500 0.300 37.67331  ? 385 TRP A CH2 1 
ATOM   439  N N   A LEU A 1 56  ? 5.94900   10.10900  15.69800 0.700 58.07694  ? 386 LEU A N   1 
ATOM   440  N N   B LEU A 1 56  ? 5.79000   10.36700  15.66200 0.300 56.31982  ? 386 LEU A N   1 
ATOM   441  C CA  A LEU A 1 56  ? 7.22400   9.53500   15.30200 0.700 61.29056  ? 386 LEU A CA  1 
ATOM   442  C CA  B LEU A 1 56  ? 7.03800   9.76900   15.21200 0.300 60.06645  ? 386 LEU A CA  1 
ATOM   443  C C   A LEU A 1 56  ? 7.53900   9.77500   13.83000 0.700 58.63872  ? 386 LEU A C   1 
ATOM   444  C C   B LEU A 1 56  ? 7.29900   10.01000  13.73300 0.300 57.51419  ? 386 LEU A C   1 
ATOM   445  O O   A LEU A 1 56  ? 8.60100   9.34700   13.36800 0.700 58.27508  ? 386 LEU A O   1 
ATOM   446  O O   B LEU A 1 56  ? 8.33700   9.56800   13.22600 0.300 57.95100  ? 386 LEU A O   1 
ATOM   447  C CB  A LEU A 1 56  ? 7.24500   8.03200   15.60400 0.700 51.17509  ? 386 LEU A CB  1 
ATOM   448  C CB  B LEU A 1 56  ? 7.04100   8.26500   15.50100 0.300 52.16889  ? 386 LEU A CB  1 
ATOM   449  C CG  A LEU A 1 56  ? 6.81300   7.61900   17.01500 0.700 46.93726  ? 386 LEU A CG  1 
ATOM   450  C CG  B LEU A 1 56  ? 6.66000   7.85700   16.92500 0.300 48.72407  ? 386 LEU A CG  1 
ATOM   451  C CD1 A LEU A 1 56  ? 6.47800   6.13700   17.06000 0.700 54.38833  ? 386 LEU A CD1 1 
ATOM   452  C CD1 B LEU A 1 56  ? 6.29200   6.38300   16.98300 0.300 54.16124  ? 386 LEU A CD1 1 
ATOM   453  C CD2 A LEU A 1 56  ? 7.87300   7.97100   18.05400 0.700 50.27199  ? 386 LEU A CD2 1 
ATOM   454  C CD2 B LEU A 1 56  ? 7.79500   8.16800   17.88700 0.300 51.06680  ? 386 LEU A CD2 1 
ATOM   455  N N   A LYS A 1 57  ? 6.62900   10.40300  13.08100 0.700 47.27400  ? 387 LYS A N   1 
ATOM   456  N N   B LYS A 1 57  ? 6.37300   10.66200  13.02700 0.300 48.96827  ? 387 LYS A N   1 
ATOM   457  C CA  A LYS A 1 57  ? 6.92300   10.79000  11.70900 0.700 48.41364  ? 387 LYS A CA  1 
ATOM   458  C CA  B LYS A 1 57  ? 6.61500   11.05100  11.64400 0.300 50.72229  ? 387 LYS A CA  1 
ATOM   459  C C   A LYS A 1 57  ? 8.20400   11.61300  11.69000 0.700 56.80662  ? 387 LYS A C   1 
ATOM   460  C C   B LYS A 1 57  ? 7.91800   11.83400  11.58100 0.300 57.01112  ? 387 LYS A C   1 
ATOM   461  O O   A LYS A 1 57  ? 8.45300   12.40800  12.60100 0.700 59.30807  ? 387 LYS A O   1 
ATOM   462  O O   B LYS A 1 57  ? 8.24300   12.58900  12.50100 0.300 59.19890  ? 387 LYS A O   1 
ATOM   463  C CB  A LYS A 1 57  ? 5.75600   11.57300  11.11000 0.700 47.96791  ? 387 LYS A CB  1 
ATOM   464  C CB  B LYS A 1 57  ? 5.45500   11.89500  11.11100 0.300 50.57496  ? 387 LYS A CB  1 
ATOM   465  C CG  A LYS A 1 57  ? 4.57200   10.68100  10.77800 0.700 45.45727  ? 387 LYS A CG  1 
ATOM   466  C CG  B LYS A 1 57  ? 4.18600   11.11000  10.82200 0.300 48.55230  ? 387 LYS A CG  1 
ATOM   467  C CD  A LYS A 1 57  ? 3.45200   11.43900  10.08700 0.700 49.19049  ? 387 LYS A CD  1 
ATOM   468  C CD  B LYS A 1 57  ? 3.12500   12.00200  10.19500 0.300 52.13584  ? 387 LYS A CD  1 
ATOM   469  C CE  A LYS A 1 57  ? 3.02000   12.64800  10.89800 0.700 60.97945  ? 387 LYS A CE  1 
ATOM   470  C CE  B LYS A 1 57  ? 1.73500   11.65700  10.70700 0.300 49.87155  ? 387 LYS A CE  1 
ATOM   471  N NZ  A LYS A 1 57  ? 1.54200   12.66900  11.09300 0.700 62.09751  ? 387 LYS A NZ  1 
ATOM   472  N NZ  B LYS A 1 57  ? 0.79000   12.79500  10.53900 0.300 51.33706  ? 387 LYS A NZ  1 
ATOM   473  N N   A SER A 1 58  ? 9.01000   11.44400  10.64300 0.700 62.78638  ? 388 SER A N   1 
ATOM   474  N N   B SER A 1 58  ? 8.67600   11.65300  10.50300 0.300 60.39998  ? 388 SER A N   1 
ATOM   475  C CA  A SER A 1 58  ? 10.26800  12.17500  10.58500 0.700 59.92159  ? 388 SER A CA  1 
ATOM   476  C CA  B SER A 1 58  ? 9.94600   12.35800  10.41800 0.300 60.40691  ? 388 SER A CA  1 
ATOM   477  C C   A SER A 1 58  ? 10.02500  13.67800  10.50100 0.700 60.90515  ? 388 SER A C   1 
ATOM   478  C C   B SER A 1 58  ? 9.72300   13.86500  10.36100 0.300 60.98269  ? 388 SER A C   1 
ATOM   479  O O   A SER A 1 58  ? 9.02300   14.14500  9.95100  0.700 61.40634  ? 388 SER A O   1 
ATOM   480  O O   B SER A 1 58  ? 8.72200   14.35400  9.83100  0.300 62.65639  ? 388 SER A O   1 
ATOM   481  C CB  A SER A 1 58  ? 11.10000  11.71500  9.38800  0.700 64.03290  ? 388 SER A CB  1 
ATOM   482  C CB  B SER A 1 58  ? 10.72800  11.89900  9.18800  0.300 63.26183  ? 388 SER A CB  1 
ATOM   483  O OG  A SER A 1 58  ? 10.48900  12.08900  8.16400  0.700 63.40129  ? 388 SER A OG  1 
ATOM   484  O OG  B SER A 1 58  ? 11.36100  10.65300  9.42100  0.300 60.06964  ? 388 SER A OG  1 
ATOM   485  N N   A ASN A 1 59  ? 10.96400  14.43500  11.06800 0.700 59.48942  ? 389 ASN A N   1 
ATOM   486  N N   B ASN A 1 59  ? 10.68200  14.60200  10.92000 0.300 59.09085  ? 389 ASN A N   1 
ATOM   487  C CA  A ASN A 1 59  ? 10.99400  15.88500  10.94900 0.700 56.54490  ? 389 ASN A CA  1 
ATOM   488  C CA  B ASN A 1 59  ? 10.72000  16.05300  10.81400 0.300 57.16257  ? 389 ASN A CA  1 
ATOM   489  C C   A ASN A 1 59  ? 11.61000  16.35300  9.63800  0.700 59.33303  ? 389 ASN A C   1 
ATOM   490  C C   B ASN A 1 59  ? 11.32500  16.53000  9.50300  0.300 59.74914  ? 389 ASN A C   1 
ATOM   491  O O   A ASN A 1 59  ? 11.49800  17.54000  9.31000  0.700 63.02872  ? 389 ASN A O   1 
ATOM   492  O O   B ASN A 1 59  ? 11.22000  17.72000  9.18700  0.300 62.19625  ? 389 ASN A O   1 
ATOM   493  C CB  A ASN A 1 59  ? 11.75800  16.49700  12.12800 0.700 63.10069  ? 389 ASN A CB  1 
ATOM   494  C CB  B ASN A 1 59  ? 11.49300  16.64700  11.99400 0.300 62.23119  ? 389 ASN A CB  1 
ATOM   495  C CG  A ASN A 1 59  ? 11.08100  16.23600  13.46300 0.700 54.80956  ? 389 ASN A CG  1 
ATOM   496  C CG  B ASN A 1 59  ? 10.82200  16.37500  13.32500 0.300 57.78175  ? 389 ASN A CG  1 
ATOM   497  O OD1 A ASN A 1 59  ? 9.85300   16.23400  13.56300 0.700 47.94104  ? 389 ASN A OD1 1 
ATOM   498  O OD1 B ASN A 1 59  ? 9.59500   16.38000  13.42800 0.300 53.33071  ? 389 ASN A OD1 1 
ATOM   499  N ND2 A ASN A 1 59  ? 11.88600  16.01200  14.49900 0.700 48.21089  ? 389 ASN A ND2 1 
ATOM   500  N ND2 B ASN A 1 59  ? 11.62600  16.14000  14.35600 0.300 53.65886  ? 389 ASN A ND2 1 
ATOM   501  N N   A GLY A 1 60  ? 12.24300  15.45800  8.88300  0.700 63.99961  ? 390 GLY A N   1 
ATOM   502  N N   B GLY A 1 60  ? 11.94500  15.64000  8.74000  0.300 63.12780  ? 390 GLY A N   1 
ATOM   503  C CA  A GLY A 1 60  ? 12.74500  15.77100  7.56700  0.700 66.01351  ? 390 GLY A CA  1 
ATOM   504  C CA  B GLY A 1 60  ? 12.44600  15.94300  7.42100  0.300 66.49717  ? 390 GLY A CA  1 
ATOM   505  C C   A GLY A 1 60  ? 14.10400  15.15000  7.32300  0.700 59.19575  ? 390 GLY A C   1 
ATOM   506  C C   B GLY A 1 60  ? 13.79800  15.29900  7.20200  0.300 61.98998  ? 390 GLY A C   1 
ATOM   507  O O   A GLY A 1 60  ? 14.62800  14.39200  8.13800  0.700 65.22966  ? 390 GLY A O   1 
ATOM   508  O O   B GLY A 1 60  ? 14.29400  14.53700  8.03000  0.300 64.68304  ? 390 GLY A O   1 
ATOM   509  N N   A THR A 1 61  ? 14.66900  15.50000  6.17100  0.700 58.52445  ? 391 THR A N   1 
ATOM   510  N N   B THR A 1 61  ? 14.39200  15.62100  6.05700  0.300 61.13156  ? 391 THR A N   1 
ATOM   511  C CA  A THR A 1 61  ? 15.96000  15.01200  5.71100  0.700 64.13716  ? 391 THR A CA  1 
ATOM   512  C CA  B THR A 1 61  ? 15.68700  15.09200  5.65400  0.300 64.62962  ? 391 THR A CA  1 
ATOM   513  C C   A THR A 1 61  ? 17.12700  15.62100  6.48800  0.700 68.69278  ? 391 THR A C   1 
ATOM   514  C C   B THR A 1 61  ? 16.82000  15.71400  6.47500  0.300 68.95219  ? 391 THR A C   1 
ATOM   515  O O   A THR A 1 61  ? 16.99800  16.63400  7.18200  0.700 65.83636  ? 391 THR A O   1 
ATOM   516  O O   B THR A 1 61  ? 16.66300  16.75700  7.11700  0.300 67.37420  ? 391 THR A O   1 
ATOM   517  C CB  A THR A 1 61  ? 16.13400  15.30300  4.21800  0.700 69.83436  ? 391 THR A CB  1 
ATOM   518  C CB  B THR A 1 61  ? 15.91000  15.34600  4.15900  0.300 69.44996  ? 391 THR A CB  1 
ATOM   519  O OG1 A THR A 1 61  ? 16.59000  16.65100  4.03700  0.700 64.55753  ? 391 THR A OG1 1 
ATOM   520  O OG1 B THR A 1 61  ? 14.68900  15.10200  3.45100  0.300 67.81368  ? 391 THR A OG1 1 
ATOM   521  C CG2 A THR A 1 61  ? 14.81300  15.11700  3.48400  0.700 68.02577  ? 391 THR A CG2 1 
ATOM   522  C CG2 B THR A 1 61  ? 16.98000  14.41800  3.59500  0.300 68.24966  ? 391 THR A CG2 1 
ATOM   523  N N   A ASN A 1 62  ? 18.28300  14.95700  6.36900  0.700 72.63048  ? 392 ASN A N   1 
ATOM   524  N N   B ASN A 1 62  ? 17.97800  15.04400  6.44600  0.300 71.75328  ? 392 ASN A N   1 
ATOM   525  C CA  A ASN A 1 62  ? 19.50800  15.43300  7.00400  0.700 70.94607  ? 392 ASN A CA  1 
ATOM   526  C CA  B ASN A 1 62  ? 19.16200  15.54200  7.14100  0.300 70.20203  ? 392 ASN A CA  1 
ATOM   527  C C   A ASN A 1 62  ? 19.93700  16.76500  6.40300  0.700 70.85219  ? 392 ASN A C   1 
ATOM   528  C C   B ASN A 1 62  ? 19.63300  16.85500  6.53300  0.300 70.64767  ? 392 ASN A C   1 
ATOM   529  O O   A ASN A 1 62  ? 20.52400  17.60300  7.09800  0.700 69.10211  ? 392 ASN A O   1 
ATOM   530  O O   B ASN A 1 62  ? 20.19200  17.70400  7.23700  0.300 69.91436  ? 392 ASN A O   1 
ATOM   531  C CB  A ASN A 1 62  ? 20.62100  14.39300  6.85800  0.700 75.61447  ? 392 ASN A CB  1 
ATOM   532  C CB  B ASN A 1 62  ? 20.27800  14.49800  7.10400  0.300 72.62337  ? 392 ASN A CB  1 
ATOM   533  C CG  A ASN A 1 62  ? 20.47300  13.23400  7.83100  0.700 79.47719  ? 392 ASN A CG  1 
ATOM   534  C CG  B ASN A 1 62  ? 21.17200  14.56000  8.32700  0.300 67.76800  ? 392 ASN A CG  1 
ATOM   535  O OD1 A ASN A 1 62  ? 21.46400  12.63700  8.25500  0.700 96.88947  ? 392 ASN A OD1 1 
ATOM   536  O OD1 B ASN A 1 62  ? 20.97800  13.81900  9.29100  0.300 69.12455  ? 392 ASN A OD1 1 
ATOM   537  N ND2 A ASN A 1 62  ? 19.23600  12.90900  8.18800  0.700 73.93794  ? 392 ASN A ND2 1 
ATOM   538  N ND2 B ASN A 1 62  ? 22.16000  15.44700  8.29500  0.300 54.40028  ? 392 ASN A ND2 1 
ATOM   539  N N   A ALA A 1 63  ? 19.64000  16.97400  5.11800  0.700 68.72730  ? 393 ALA A N   1 
ATOM   540  N N   B ALA A 1 63  ? 19.42100  17.03200  5.22700  0.300 68.96521  ? 393 ALA A N   1 
ATOM   541  C CA  A ALA A 1 63  ? 19.97800  18.22500  4.44700  0.700 74.31901  ? 393 ALA A CA  1 
ATOM   542  C CA  B ALA A 1 63  ? 19.81000  18.26900  4.56000  0.300 74.05462  ? 393 ALA A CA  1 
ATOM   543  C C   A ALA A 1 63  ? 19.18600  19.36400  5.07000  0.700 77.07009  ? 393 ALA A C   1 
ATOM   544  C C   B ALA A 1 63  ? 18.98200  19.42400  5.10500  0.300 76.12053  ? 393 ALA A C   1 
ATOM   545  O O   A ALA A 1 63  ? 19.72500  20.44900  5.32000  0.700 73.97324  ? 393 ALA A O   1 
ATOM   546  O O   B ALA A 1 63  ? 19.51200  20.50800  5.37900  0.300 73.94507  ? 393 ALA A O   1 
ATOM   547  C CB  A ALA A 1 63  ? 19.70300  18.11800  2.94700  0.700 70.34539  ? 393 ALA A CB  1 
ATOM   548  C CB  B ALA A 1 63  ? 19.63900  18.13700  3.04800  0.300 70.32201  ? 393 ALA A CB  1 
ATOM   549  N N   A GLU A 1 64  ? 17.89600  19.12900  5.30800  0.700 78.36392  ? 394 GLU A N   1 
ATOM   550  N N   B GLU A 1 64  ? 17.67500  19.20200  5.25300  0.300 75.76657  ? 394 GLU A N   1 
ATOM   551  C CA  A GLU A 1 64  ? 17.05100  20.10400  5.98500  0.700 61.57973  ? 394 GLU A CA  1 
ATOM   552  C CA  B GLU A 1 64  ? 16.79800  20.20200  5.84800  0.300 63.28315  ? 394 GLU A CA  1 
ATOM   553  C C   A GLU A 1 64  ? 17.59800  20.39400  7.38000  0.700 61.52006  ? 394 GLU A C   1 
ATOM   554  C C   B GLU A 1 64  ? 17.23800  20.51400  7.27400  0.300 63.95155  ? 394 GLU A C   1 
ATOM   555  O O   A GLU A 1 64  ? 17.64200  21.55300  7.80700  0.700 62.19197  ? 394 GLU A O   1 
ATOM   556  O O   B GLU A 1 64  ? 17.26200  21.68200  7.68100  0.300 64.11946  ? 394 GLU A O   1 
ATOM   557  C CB  A GLU A 1 64  ? 15.61600  19.58700  6.02300  0.700 52.30553  ? 394 GLU A CB  1 
ATOM   558  C CB  B GLU A 1 64  ? 15.35200  19.71100  5.81900  0.300 56.27175  ? 394 GLU A CB  1 
ATOM   559  C CG  A GLU A 1 64  ? 14.91300  19.71000  4.67800  0.700 51.08101  ? 394 GLU A CG  1 
ATOM   560  C CG  B GLU A 1 64  ? 14.69300  19.78800  4.45400  0.300 55.80469  ? 394 GLU A CG  1 
ATOM   561  C CD  A GLU A 1 64  ? 13.46400  19.27400  4.72300  0.700 60.84536  ? 394 GLU A CD  1 
ATOM   562  C CD  B GLU A 1 64  ? 13.23600  19.37400  4.48800  0.300 62.59061  ? 394 GLU A CD  1 
ATOM   563  O OE1 A GLU A 1 64  ? 13.15200  18.33600  5.48800  0.700 64.78010  ? 394 GLU A OE1 1 
ATOM   564  O OE1 B GLU A 1 64  ? 12.89000  18.47800  5.28700  0.300 64.57616  ? 394 GLU A OE1 1 
ATOM   565  O OE2 A GLU A 1 64  ? 12.63800  19.86600  3.99500  0.700 54.20103  ? 394 GLU A OE2 1 
ATOM   566  O OE2 B GLU A 1 64  ? 12.43600  19.94100  3.71400  0.300 55.50050  ? 394 GLU A OE2 1 
ATOM   567  N N   A LYS A 1 65  ? 18.01700  19.35200  8.10700  0.700 67.52932  ? 395 LYS A N   1 
ATOM   568  N N   B LYS A 1 65  ? 17.57600  19.48100  8.05400  0.300 66.48437  ? 395 LYS A N   1 
ATOM   569  C CA  A LYS A 1 65  ? 18.55600  19.55300  9.45000  0.700 69.13356  ? 395 LYS A CA  1 
ATOM   570  C CA  B LYS A 1 65  ? 18.00100  19.70200  9.43400  0.300 67.68543  ? 395 LYS A CA  1 
ATOM   571  C C   A LYS A 1 65  ? 19.81100  20.41200  9.39800  0.700 69.31423  ? 395 LYS A C   1 
ATOM   572  C C   B LYS A 1 65  ? 19.27700  20.53000  9.46800  0.300 68.50420  ? 395 LYS A C   1 
ATOM   573  O O   A LYS A 1 65  ? 19.97700  21.33200  10.20600 0.700 66.39250  ? 395 LYS A O   1 
ATOM   574  O O   B LYS A 1 65  ? 19.40200  21.46600  10.26700 0.300 68.87177  ? 395 LYS A O   1 
ATOM   575  C CB  A LYS A 1 65  ? 18.87600  18.20600  10.10000 0.700 73.76632  ? 395 LYS A CB  1 
ATOM   576  C CB  B LYS A 1 65  ? 18.22200  18.36400  10.14100 0.300 70.95363  ? 395 LYS A CB  1 
ATOM   577  C CG  A LYS A 1 65  ? 19.47800  18.31200  11.50000 0.700 78.86242  ? 395 LYS A CG  1 
ATOM   578  C CG  B LYS A 1 65  ? 17.87300  18.36000  11.62200 0.300 68.34760  ? 395 LYS A CG  1 
ATOM   579  C CD  A LYS A 1 65  ? 18.51500  18.58100  12.63400 0.700 78.57669  ? 395 LYS A CD  1 
ATOM   580  C CD  B LYS A 1 65  ? 18.87300  19.11300  12.48400 0.300 75.51595  ? 395 LYS A CD  1 
ATOM   581  C CE  A LYS A 1 65  ? 19.02500  17.87100  13.88800 0.700 85.93554  ? 395 LYS A CE  1 
ATOM   582  C CE  B LYS A 1 65  ? 18.61300  18.85200  13.96100 0.300 77.92114  ? 395 LYS A CE  1 
ATOM   583  N NZ  A LYS A 1 65  ? 19.05600  18.75500  15.09000 0.700 79.22180  ? 395 LYS A NZ  1 
ATOM   584  N NZ  B LYS A 1 65  ? 19.67100  19.42400  14.83800 0.300 77.69928  ? 395 LYS A NZ  1 
ATOM   585  N N   A LEU A 1 66  ? 20.71600  20.11800  8.46200  0.700 80.48834  ? 396 LEU A N   1 
ATOM   586  N N   B LEU A 1 66  ? 20.24600  20.18700  8.61600  0.300 75.06642  ? 396 LEU A N   1 
ATOM   587  C CA  A LEU A 1 66  ? 21.96800  20.86300  8.40500  0.700 87.85907  ? 396 LEU A CA  1 
ATOM   588  C CA  B LEU A 1 66  ? 21.52600  20.88800  8.63300  0.300 81.58354  ? 396 LEU A CA  1 
ATOM   589  C C   A LEU A 1 66  ? 21.67200  22.33500  8.14400  0.700 80.03553  ? 396 LEU A C   1 
ATOM   590  C C   B LEU A 1 66  ? 21.31000  22.36000  8.31200  0.300 78.36557  ? 396 LEU A C   1 
ATOM   591  O O   A LEU A 1 66  ? 22.21000  23.22300  8.81500  0.700 82.35533  ? 396 LEU A O   1 
ATOM   592  O O   B LEU A 1 66  ? 21.86300  23.24500  8.97700  0.300 80.39190  ? 396 LEU A O   1 
ATOM   593  C CB  A LEU A 1 66  ? 22.88100  20.27100  7.32900  0.700 87.38687  ? 396 LEU A CB  1 
ATOM   594  C CB  B LEU A 1 66  ? 22.49400  20.24300  7.64100  0.300 84.11314  ? 396 LEU A CB  1 
ATOM   595  C CG  A LEU A 1 66  ? 24.32300  20.77500  7.27700  0.700 85.99899  ? 396 LEU A CG  1 
ATOM   596  C CG  B LEU A 1 66  ? 23.94900  20.71100  7.69600  0.300 84.31657  ? 396 LEU A CG  1 
ATOM   597  C CD1 A LEU A 1 66  ? 25.07500  20.34400  8.52600  0.700 82.22117  ? 396 LEU A CD1 1 
ATOM   598  C CD1 B LEU A 1 66  ? 24.59600  20.29100  9.00600  0.300 76.90524  ? 396 LEU A CD1 1 
ATOM   599  C CD2 A LEU A 1 66  ? 25.01600  20.25600  6.02600  0.700 62.77221  ? 396 LEU A CD2 1 
ATOM   600  C CD2 B LEU A 1 66  ? 24.72900  20.16400  6.51100  0.300 71.10659  ? 396 LEU A CD2 1 
ATOM   601  N N   A ALA A 1 67  ? 20.79000  22.60100  7.17500  0.700 78.50081  ? 397 ALA A N   1 
ATOM   602  N N   B ALA A 1 67  ? 20.51300  22.63400  7.27500  0.300 77.24516  ? 397 ALA A N   1 
ATOM   603  C CA  A ALA A 1 67  ? 20.40000  23.96500  6.83100  0.700 71.76277  ? 397 ALA A CA  1 
ATOM   604  C CA  B ALA A 1 67  ? 20.21500  24.00700  6.88300  0.300 72.19084  ? 397 ALA A CA  1 
ATOM   605  C C   A ALA A 1 67  ? 19.83000  24.69600  8.04100  0.700 73.60633  ? 397 ALA A C   1 
ATOM   606  C C   B ALA A 1 67  ? 19.59300  24.77500  8.04300  0.300 73.72240  ? 397 ALA A C   1 
ATOM   607  O O   A ALA A 1 67  ? 20.11500  25.88000  8.25400  0.700 77.98635  ? 397 ALA A O   1 
ATOM   608  O O   B ALA A 1 67  ? 19.91700  25.94700  8.26900  0.300 76.94449  ? 397 ALA A O   1 
ATOM   609  C CB  A ALA A 1 67  ? 19.39200  23.95100  5.68300  0.700 66.85078  ? 397 ALA A CB  1 
ATOM   610  C CB  B ALA A 1 67  ? 19.29000  24.01900  5.66600  0.300 67.02460  ? 397 ALA A CB  1 
ATOM   611  N N   A ALA A 1 68  ? 19.01600  24.00400  8.84400  0.700 73.64196  ? 398 ALA A N   1 
ATOM   612  N N   B ALA A 1 68  ? 18.69000  24.12800  8.78600  0.300 72.87354  ? 398 ALA A N   1 
ATOM   613  C CA  A ALA A 1 68  ? 18.35500  24.65200  9.97300  0.700 69.84089  ? 398 ALA A CA  1 
ATOM   614  C CA  B ALA A 1 68  ? 17.98300  24.80700  9.86600  0.300 69.81466  ? 398 ALA A CA  1 
ATOM   615  C C   A ALA A 1 68  ? 19.36200  25.03900  11.04800 0.700 71.69278  ? 398 ALA A C   1 
ATOM   616  C C   B ALA A 1 68  ? 18.93200  25.13700  11.00900 0.300 72.67938  ? 398 ALA A C   1 
ATOM   617  O O   A ALA A 1 68  ? 19.26100  26.12300  11.63400 0.700 76.23447  ? 398 ALA A O   1 
ATOM   618  O O   B ALA A 1 68  ? 18.85100  26.22200  11.59600 0.300 73.82208  ? 398 ALA A O   1 
ATOM   619  C CB  A ALA A 1 68  ? 17.27700  23.73400  10.54900 0.700 70.33560  ? 398 ALA A CB  1 
ATOM   620  C CB  B ALA A 1 68  ? 16.82100  23.94600  10.36100 0.300 65.71324  ? 398 ALA A CB  1 
ATOM   621  N N   A ASN A 1 69  ? 20.34200  24.17400  11.31800 0.700 64.23390  ? 399 ASN A N   1 
ATOM   622  N N   B ASN A 1 69  ? 19.84000  24.21500  11.33700 0.300 68.10733  ? 399 ASN A N   1 
ATOM   623  C CA  A ASN A 1 69  ? 21.32600  24.48700  12.34900 0.700 73.16774  ? 399 ASN A CA  1 
ATOM   624  C CA  B ASN A 1 69  ? 20.76900  24.45600  12.43400 0.300 72.00678  ? 399 ASN A CA  1 
ATOM   625  C C   A ASN A 1 69  ? 22.20800  25.64700  11.90800 0.700 82.03765  ? 399 ASN A C   1 
ATOM   626  C C   B ASN A 1 69  ? 21.75200  25.56000  12.07000 0.300 79.15335  ? 399 ASN A C   1 
ATOM   627  O O   A ASN A 1 69  ? 22.63500  26.45400  12.74200 0.700 79.83982  ? 399 ASN A O   1 
ATOM   628  O O   B ASN A 1 69  ? 22.16800  26.33400  12.94000 0.300 78.64139  ? 399 ASN A O   1 
ATOM   629  C CB  A ASN A 1 69  ? 22.15400  23.25200  12.69800 0.700 80.76643  ? 399 ASN A CB  1 
ATOM   630  C CB  B ASN A 1 69  ? 21.51100  23.17000  12.79500 0.300 76.34897  ? 399 ASN A CB  1 
ATOM   631  C CG  A ASN A 1 69  ? 21.29600  22.09900  13.17800 0.700 85.92437  ? 399 ASN A CG  1 
ATOM   632  C CG  B ASN A 1 69  ? 21.60300  22.95200  14.29300 0.300 74.28407  ? 399 ASN A CG  1 
ATOM   633  O OD1 A ASN A 1 69  ? 20.09600  22.04500  12.90200 0.700 77.83339  ? 399 ASN A OD1 1 
ATOM   634  O OD1 B ASN A 1 69  ? 20.75700  23.42300  15.05300 0.300 68.75799  ? 399 ASN A OD1 1 
ATOM   635  N ND2 A ASN A 1 69  ? 21.90400  21.17700  13.91600 0.700 90.71396  ? 399 ASN A ND2 1 
ATOM   636  N ND2 B ASN A 1 69  ? 22.63500  22.23800  14.72500 0.300 70.83978  ? 399 ASN A ND2 1 
ATOM   637  N N   A ILE A 1 70  ? 22.47100  25.75800  10.60500 0.700 82.40218  ? 400 ILE A N   1 
ATOM   638  N N   B ILE A 1 70  ? 22.11800  25.65500  10.79100 0.300 80.25624  ? 400 ILE A N   1 
ATOM   639  C CA  A ILE A 1 70  ? 23.29100  26.85200  10.10200 0.700 76.64302  ? 400 ILE A CA  1 
ATOM   640  C CA  B ILE A 1 70  ? 23.04200  26.69100  10.34200 0.300 76.81167  ? 400 ILE A CA  1 
ATOM   641  C C   A ILE A 1 70  ? 22.53300  28.16300  10.25900 0.700 76.85330  ? 400 ILE A C   1 
ATOM   642  C C   B ILE A 1 70  ? 22.37200  28.05600  10.42600 0.300 76.29427  ? 400 ILE A C   1 
ATOM   643  O O   A ILE A 1 70  ? 23.05100  29.13400  10.82200 0.700 86.57107  ? 400 ILE A O   1 
ATOM   644  O O   B ILE A 1 70  ? 22.92200  29.00100  11.00300 0.300 82.26961  ? 400 ILE A O   1 
ATOM   645  C CB  A ILE A 1 70  ? 23.69800  26.59500  8.63800  0.700 78.99534  ? 400 ILE A CB  1 
ATOM   646  C CB  B ILE A 1 70  ? 23.54500  26.38900  8.91900  0.300 78.66610  ? 400 ILE A CB  1 
ATOM   647  C CG1 A ILE A 1 70  ? 24.68800  25.43100  8.55200  0.700 87.88021  ? 400 ILE A CG1 1 
ATOM   648  C CG1 B ILE A 1 70  ? 24.47000  25.17000  8.92700  0.300 84.17301  ? 400 ILE A CG1 1 
ATOM   649  C CG2 A ILE A 1 70  ? 24.28800  27.85500  8.00800  0.700 68.36998  ? 400 ILE A CG2 1 
ATOM   650  C CG2 B ILE A 1 70  ? 24.25600  27.60100  8.33700  0.300 71.25536  ? 400 ILE A CG2 1 
ATOM   651  C CD1 A ILE A 1 70  ? 25.75300  25.43800  9.63200  0.700 93.57327  ? 400 ILE A CD1 1 
ATOM   652  C CD1 B ILE A 1 70  ? 25.58100  25.25600  9.95200  0.300 89.17513  ? 400 ILE A CD1 1 
ATOM   653  N N   A LEU A 1 71  ? 21.29500  28.21400  9.76100  0.700 71.37811  ? 401 LEU A N   1 
ATOM   654  N N   B LEU A 1 71  ? 21.18000  28.18100  9.83600  0.300 71.47586  ? 401 LEU A N   1 
ATOM   655  C CA  A LEU A 1 71  ? 20.52100  29.44500  9.86100  0.700 72.13466  ? 401 LEU A CA  1 
ATOM   656  C CA  B LEU A 1 71  ? 20.47500  29.45900  9.83700  0.300 72.21728  ? 401 LEU A CA  1 
ATOM   657  C C   A LEU A 1 71  ? 20.31500  29.85400  11.30900 0.700 71.64586  ? 401 LEU A C   1 
ATOM   658  C C   B LEU A 1 71  ? 20.18200  29.92100  11.25900 0.300 71.29917  ? 401 LEU A C   1 
ATOM   659  O O   A LEU A 1 71  ? 20.28000  31.05200  11.61600 0.700 70.85191  ? 401 LEU A O   1 
ATOM   660  O O   B LEU A 1 71  ? 20.17400  31.12800  11.53000 0.300 70.75656  ? 401 LEU A O   1 
ATOM   661  C CB  A LEU A 1 71  ? 19.15400  29.28200  9.19900  0.700 68.66845  ? 401 LEU A CB  1 
ATOM   662  C CB  B LEU A 1 71  ? 19.18300  29.35000  9.02800  0.300 68.34681  ? 401 LEU A CB  1 
ATOM   663  C CG  A LEU A 1 71  ? 18.98500  29.28800  7.68400  0.700 59.80782  ? 401 LEU A CG  1 
ATOM   664  C CG  B LEU A 1 71  ? 19.35400  29.32100  7.50800  0.300 62.10987  ? 401 LEU A CG  1 
ATOM   665  C CD1 A LEU A 1 71  ? 17.51400  29.10900  7.32000  0.700 61.48830  ? 401 LEU A CD1 1 
ATOM   666  C CD1 B LEU A 1 71  ? 18.00400  29.24800  6.81300  0.300 58.99508  ? 401 LEU A CD1 1 
ATOM   667  C CD2 A LEU A 1 71  ? 19.51100  30.61700  7.15900  0.700 68.24361  ? 401 LEU A CD2 1 
ATOM   668  C CD2 B LEU A 1 71  ? 20.14100  30.53300  7.03500  0.300 69.82008  ? 401 LEU A CD2 1 
ATOM   669  N N   A GLN A 1 72  ? 20.16700  28.87900  12.21200 0.700 65.77779  ? 402 GLN A N   1 
ATOM   670  N N   B GLN A 1 72  ? 19.93000  28.98200  12.17500 0.300 67.24927  ? 402 GLN A N   1 
ATOM   671  C CA  A GLN A 1 72  ? 20.01700  29.20400  13.62500 0.700 67.68995  ? 402 GLN A CA  1 
ATOM   672  C CA  B GLN A 1 72  ? 19.70300  29.35100  13.56900 0.300 69.38690  ? 402 GLN A CA  1 
ATOM   673  C C   A GLN A 1 72  ? 21.28700  29.83400  14.17900 0.700 68.01369  ? 402 GLN A C   1 
ATOM   674  C C   B GLN A 1 72  ? 20.97000  29.95300  14.16400 0.300 69.35247  ? 402 GLN A C   1 
ATOM   675  O O   A GLN A 1 72  ? 21.23500  30.87800  14.84000 0.700 70.23890  ? 402 GLN A O   1 
ATOM   676  O O   B GLN A 1 72  ? 20.92000  31.00000  14.82100 0.300 69.46639  ? 402 GLN A O   1 
ATOM   677  C CB  A GLN A 1 72  ? 19.63300  27.95000  14.41100 0.700 76.73421  ? 402 GLN A CB  1 
ATOM   678  C CB  B GLN A 1 72  ? 19.23000  28.13600  14.36700 0.300 74.75719  ? 402 GLN A CB  1 
ATOM   679  C CG  A GLN A 1 72  ? 18.17200  27.55100  14.24600 0.700 72.13237  ? 402 GLN A CG  1 
ATOM   680  C CG  B GLN A 1 72  ? 17.76900  27.78800  14.11700 0.300 69.55287  ? 402 GLN A CG  1 
ATOM   681  C CD  A GLN A 1 72  ? 17.87700  26.13900  14.72200 0.700 71.00966  ? 402 GLN A CD  1 
ATOM   682  C CD  B GLN A 1 72  ? 17.39700  26.40500  14.61300 0.300 69.27166  ? 402 GLN A CD  1 
ATOM   683  O OE1 A GLN A 1 72  ? 16.73000  25.79900  15.01100 0.700 74.02095  ? 402 GLN A OE1 1 
ATOM   684  O OE1 B GLN A 1 72  ? 18.15600  25.45000  14.45100 0.300 73.58582  ? 402 GLN A OE1 1 
ATOM   685  N NE2 A GLN A 1 72  ? 18.91100  25.30700  14.79400 0.700 82.06973  ? 402 GLN A NE2 1 
ATOM   686  N NE2 B GLN A 1 72  ? 16.21800  26.28900  15.21200 0.300 71.20376  ? 402 GLN A NE2 1 
ATOM   687  N N   A TRP A 1 73  ? 22.44000  29.20600  13.92600 0.700 67.19244  ? 403 TRP A N   1 
ATOM   688  N N   B TRP A 1 73  ? 22.11200  29.28600  13.96700 0.300 68.10881  ? 403 TRP A N   1 
ATOM   689  C CA  A TRP A 1 73  ? 23.71000  29.78400  14.35900 0.700 68.01613  ? 403 TRP A CA  1 
ATOM   690  C CA  B TRP A 1 73  ? 23.38600  29.83800  14.42200 0.300 69.25444  ? 403 TRP A CA  1 
ATOM   691  C C   A TRP A 1 73  ? 23.89000  31.19300  13.80800 0.700 67.21409  ? 403 TRP A C   1 
ATOM   692  C C   B TRP A 1 73  ? 23.58600  31.23000  13.83700 0.300 68.15312  ? 403 TRP A C   1 
ATOM   693  O O   A TRP A 1 73  ? 24.27300  32.11200  14.54200 0.700 72.92268  ? 403 TRP A O   1 
ATOM   694  O O   B TRP A 1 73  ? 23.99500  32.16300  14.53900 0.300 71.10371  ? 403 TRP A O   1 
ATOM   695  C CB  A TRP A 1 73  ? 24.87500  28.87300  13.97000 0.700 64.03334  ? 403 TRP A CB  1 
ATOM   696  C CB  B TRP A 1 73  ? 24.54400  28.91200  14.04500 0.300 65.91194  ? 403 TRP A CB  1 
ATOM   697  C CG  A TRP A 1 73  ? 25.06800  27.78600  14.97400 0.700 68.96427  ? 403 TRP A CG  1 
ATOM   698  C CG  B TRP A 1 73  ? 24.75100  27.78400  15.01200 0.300 70.13257  ? 403 TRP A CG  1 
ATOM   699  C CD1 A TRP A 1 73  ? 24.72300  26.47300  14.84700 0.700 80.14715  ? 403 TRP A CD1 1 
ATOM   700  C CD1 B TRP A 1 73  ? 24.40800  26.47600  14.83500 0.300 78.07295  ? 403 TRP A CD1 1 
ATOM   701  C CD2 A TRP A 1 73  ? 25.60000  27.93600  16.29500 0.700 64.87627  ? 403 TRP A CD2 1 
ATOM   702  C CD2 B TRP A 1 73  ? 25.33500  27.87100  16.31800 0.300 66.98263  ? 403 TRP A CD2 1 
ATOM   703  N NE1 A TRP A 1 73  ? 25.03600  25.78900  15.99700 0.700 75.06964  ? 403 TRP A NE1 1 
ATOM   704  N NE1 B TRP A 1 73  ? 24.75100  25.74100  15.94300 0.300 74.97569  ? 403 TRP A NE1 1 
ATOM   705  C CE2 A TRP A 1 73  ? 25.57400  26.66500  16.90200 0.700 71.18890  ? 403 TRP A CE2 1 
ATOM   706  C CE2 B TRP A 1 73  ? 25.32000  26.57400  16.86900 0.300 71.85526  ? 403 TRP A CE2 1 
ATOM   707  C CE3 A TRP A 1 73  ? 26.10900  29.02000  17.01900 0.700 75.54591  ? 403 TRP A CE3 1 
ATOM   708  C CE3 B TRP A 1 73  ? 25.87200  28.91800  17.07300 0.300 74.81160  ? 403 TRP A CE3 1 
ATOM   709  C CZ2 A TRP A 1 73  ? 26.03600  26.44800  18.19800 0.700 75.41455  ? 403 TRP A CZ2 1 
ATOM   710  C CZ2 B TRP A 1 73  ? 25.82100  26.29700  18.14000 0.300 74.82971  ? 403 TRP A CZ2 1 
ATOM   711  C CZ3 A TRP A 1 73  ? 26.56900  28.80300  18.30400 0.700 78.12168  ? 403 TRP A CZ3 1 
ATOM   712  C CZ3 B TRP A 1 73  ? 26.36900  28.64100  18.33400 0.300 77.83715  ? 403 TRP A CZ3 1 
ATOM   713  C CH2 A TRP A 1 73  ? 26.52900  27.52700  18.88100 0.700 78.65254  ? 403 TRP A CH2 1 
ATOM   714  C CH2 B TRP A 1 73  ? 26.34000  27.34100  18.85400 0.300 77.62807  ? 403 TRP A CH2 1 
ATOM   715  N N   A ILE A 1 74  ? 23.63000  31.37700  12.51100 0.700 63.79910  ? 404 ILE A N   1 
ATOM   716  N N   B ILE A 1 74  ? 23.32800  31.37100  12.53200 0.300 65.11002  ? 404 ILE A N   1 
ATOM   717  C CA  A ILE A 1 74  ? 23.72100  32.70600  11.91000 0.700 60.93383  ? 404 ILE A CA  1 
ATOM   718  C CA  B ILE A 1 74  ? 23.41900  32.66400  11.85600 0.300 62.76139  ? 404 ILE A CA  1 
ATOM   719  C C   A ILE A 1 74  ? 22.86900  33.67900  12.71100 0.700 64.27273  ? 404 ILE A C   1 
ATOM   720  C C   B ILE A 1 74  ? 22.57700  33.69000  12.60000 0.300 65.43615  ? 404 ILE A C   1 
ATOM   721  O O   A ILE A 1 74  ? 23.29800  34.79300  13.03600 0.700 64.35628  ? 404 ILE A O   1 
ATOM   722  O O   B ILE A 1 74  ? 23.00400  34.83000  12.82500 0.300 65.62285  ? 404 ILE A O   1 
ATOM   723  C CB  A ILE A 1 74  ? 23.30900  32.65700  10.42300 0.700 65.26870  ? 404 ILE A CB  1 
ATOM   724  C CB  B ILE A 1 74  ? 22.98800  32.53100  10.38300 0.300 66.25376  ? 404 ILE A CB  1 
ATOM   725  C CG1 A ILE A 1 74  ? 24.42100  32.02400  9.58700  0.700 61.27602  ? 404 ILE A CG1 1 
ATOM   726  C CG1 B ILE A 1 74  ? 24.08200  31.84000  9.56700  0.300 63.56292  ? 404 ILE A CG1 1 
ATOM   727  C CG2 A ILE A 1 74  ? 22.97600  34.04700  9.90800  0.700 53.30197  ? 404 ILE A CG2 1 
ATOM   728  C CG2 B ILE A 1 74  ? 22.66200  33.89400  9.79100  0.300 54.79550  ? 404 ILE A CG2 1 
ATOM   729  C CD1 A ILE A 1 74  ? 24.12800  31.99000  8.10300  0.700 54.30280  ? 404 ILE A CD1 1 
ATOM   730  C CD1 B ILE A 1 74  ? 23.76200  31.72500  8.09200  0.300 57.05371  ? 404 ILE A CD1 1 
ATOM   731  N N   A THR A 1 75  ? 21.65300  33.25300  13.05800 0.700 71.12299  ? 405 THR A N   1 
ATOM   732  N N   B THR A 1 75  ? 21.36700  33.29600  13.00400 0.300 70.34645  ? 405 THR A N   1 
ATOM   733  C CA  A THR A 1 75  ? 20.69100  34.12200  13.72000 0.700 71.95776  ? 405 THR A CA  1 
ATOM   734  C CA  B THR A 1 75  ? 20.43300  34.23600  13.61300 0.300 71.48369  ? 405 THR A CA  1 
ATOM   735  C C   A THR A 1 75  ? 21.09100  34.37000  15.16600 0.700 62.55333  ? 405 THR A C   1 
ATOM   736  C C   B THR A 1 75  ? 20.89600  34.59300  15.02000 0.300 63.73925  ? 405 THR A C   1 
ATOM   737  O O   A THR A 1 75  ? 20.95600  35.49100  15.66800 0.700 59.98782  ? 405 THR A O   1 
ATOM   738  O O   B THR A 1 75  ? 20.77700  35.74800  15.44500 0.300 61.83337  ? 405 THR A O   1 
ATOM   739  C CB  A THR A 1 75  ? 19.29400  33.50500  13.66400 0.700 72.92069  ? 405 THR A CB  1 
ATOM   740  C CB  B THR A 1 75  ? 19.02400  33.64300  13.63400 0.300 72.04000  ? 405 THR A CB  1 
ATOM   741  O OG1 A THR A 1 75  ? 18.91000  33.33500  12.30100 0.700 72.71112  ? 405 THR A OG1 1 
ATOM   742  O OG1 B THR A 1 75  ? 18.60500  33.35800  12.29400 0.300 71.18571  ? 405 THR A OG1 1 
ATOM   743  C CG2 A THR A 1 75  ? 18.27300  34.40700  14.34900 0.700 70.05440  ? 405 THR A CG2 1 
ATOM   744  C CG2 B THR A 1 75  ? 18.04100  34.61900  14.26500 0.300 69.27412  ? 405 THR A CG2 1 
ATOM   745  N N   A PHE A 1 76  ? 21.60500  33.33900  15.84800 0.700 63.57997  ? 406 PHE A N   1 
ATOM   746  N N   B PHE A 1 76  ? 21.42600  33.61100  15.75500 0.300 64.19929  ? 406 PHE A N   1 
ATOM   747  C CA  A PHE A 1 76  ? 22.03200  33.52700  17.22800 0.700 65.02163  ? 406 PHE A CA  1 
ATOM   748  C CA  B PHE A 1 76  ? 21.94900  33.88600  17.08800 0.300 65.18179  ? 406 PHE A CA  1 
ATOM   749  C C   A PHE A 1 76  ? 23.16400  34.53500  17.27800 0.700 63.68526  ? 406 PHE A C   1 
ATOM   750  C C   B PHE A 1 76  ? 23.11900  34.85200  16.99200 0.300 64.88457  ? 406 PHE A C   1 
ATOM   751  O O   A PHE A 1 76  ? 23.15100  35.48000  18.07700 0.700 55.70264  ? 406 PHE A O   1 
ATOM   752  O O   B PHE A 1 76  ? 23.22000  35.80200  17.77700 0.300 61.08388  ? 406 PHE A O   1 
ATOM   753  C CB  A PHE A 1 76  ? 22.57900  32.20700  17.77000 0.700 65.50879  ? 406 PHE A CB  1 
ATOM   754  C CB  B PHE A 1 76  ? 22.38100  32.59400  17.77500 0.300 66.50917  ? 406 PHE A CB  1 
ATOM   755  C CG  A PHE A 1 76  ? 23.24500  32.34200  19.11100 0.700 72.36971  ? 406 PHE A CG  1 
ATOM   756  C CG  B PHE A 1 76  ? 23.15300  32.81600  19.04400 0.300 69.62241  ? 406 PHE A CG  1 
ATOM   757  C CD1 A PHE A 1 76  ? 22.43500  32.59300  20.21300 0.700 65.27786  ? 406 PHE A CD1 1 
ATOM   758  C CD1 B PHE A 1 76  ? 22.53600  33.36600  20.15600 0.300 63.39270  ? 406 PHE A CD1 1 
ATOM   759  C CD2 A PHE A 1 76  ? 24.64500  32.34000  19.27200 0.700 74.92407  ? 406 PHE A CD2 1 
ATOM   760  C CD2 B PHE A 1 76  ? 24.49400  32.47800  19.12600 0.300 74.20589  ? 406 PHE A CD2 1 
ATOM   761  C CE1 A PHE A 1 76  ? 22.96000  32.74200  21.46000 0.700 68.50464  ? 406 PHE A CE1 1 
ATOM   762  C CE1 B PHE A 1 76  ? 23.24100  33.57300  21.32700 0.300 64.28134  ? 406 PHE A CE1 1 
ATOM   763  C CE2 A PHE A 1 76  ? 25.20300  32.51500  20.54600 0.700 74.96649  ? 406 PHE A CE2 1 
ATOM   764  C CE2 B PHE A 1 76  ? 25.20500  32.68400  20.29400 0.300 74.50376  ? 406 PHE A CE2 1 
ATOM   765  C CZ  A PHE A 1 76  ? 24.34100  32.72100  21.64300 0.700 63.93877  ? 406 PHE A CZ  1 
ATOM   766  C CZ  B PHE A 1 76  ? 24.57700  33.23200  21.39600 0.300 64.84696  ? 406 PHE A CZ  1 
ATOM   767  N N   A ALA A 1 77  ? 24.14800  34.33600  16.40000 0.700 71.12901  ? 407 ALA A N   1 
ATOM   768  N N   B ALA A 1 77  ? 24.02300  34.61000  16.03900 0.300 69.16914  ? 407 ALA A N   1 
ATOM   769  C CA  A ALA A 1 77  ? 25.32600  35.18900  16.32100 0.700 76.44572  ? 407 ALA A CA  1 
ATOM   770  C CA  B ALA A 1 77  ? 25.19300  35.46300  15.88000 0.300 70.40424  ? 407 ALA A CA  1 
ATOM   771  C C   A ALA A 1 77  ? 24.96500  36.60800  15.90800 0.700 67.94870  ? 407 ALA A C   1 
ATOM   772  C C   B ALA A 1 77  ? 24.74900  36.88000  15.54800 0.300 64.10544  ? 407 ALA A C   1 
ATOM   773  O O   A ALA A 1 77  ? 25.38000  37.58700  16.54000 0.700 64.73799  ? 407 ALA A O   1 
ATOM   774  O O   B ALA A 1 77  ? 25.22700  37.85100  16.14400 0.300 62.62373  ? 407 ALA A O   1 
ATOM   775  C CB  A ALA A 1 77  ? 26.32400  34.57700  15.33800 0.700 61.90635  ? 407 ALA A CB  1 
ATOM   776  C CB  B ALA A 1 77  ? 26.11400  34.90700  14.79300 0.300 60.46739  ? 407 ALA A CB  1 
ATOM   777  N N   A LEU A 1 78  ? 24.17300  36.73000  14.83900 0.700 59.15207  ? 408 LEU A N   1 
ATOM   778  N N   B LEU A 1 78  ? 23.82600  37.01300  14.59100 0.300 59.22813  ? 408 LEU A N   1 
ATOM   779  C CA  A LEU A 1 78  ? 23.83900  38.04600  14.30300 0.700 52.06383  ? 408 LEU A CA  1 
ATOM   780  C CA  B LEU A 1 78  ? 23.38300  38.33500  14.16600 0.300 57.67793  ? 408 LEU A CA  1 
ATOM   781  C C   A LEU A 1 78  ? 22.98700  38.81600  15.30400 0.700 55.56964  ? 408 LEU A C   1 
ATOM   782  C C   B LEU A 1 78  ? 22.65100  39.03400  15.30400 0.300 58.54085  ? 408 LEU A C   1 
ATOM   783  O O   A LEU A 1 78  ? 23.13200  40.03600  15.44700 0.700 63.90435  ? 408 LEU A O   1 
ATOM   784  O O   B LEU A 1 78  ? 22.77700  40.25200  15.47600 0.300 62.76679  ? 408 LEU A O   1 
ATOM   785  C CB  A LEU A 1 78  ? 23.15600  37.88900  12.93800 0.700 59.23270  ? 408 LEU A CB  1 
ATOM   786  C CB  B LEU A 1 78  ? 22.48400  38.22600  12.93400 0.300 57.27353  ? 408 LEU A CB  1 
ATOM   787  C CG  A LEU A 1 78  ? 22.71100  39.02400  12.00300 0.700 47.06886  ? 408 LEU A CG  1 
ATOM   788  C CG  B LEU A 1 78  ? 23.13100  38.36900  11.55400 0.300 52.39757  ? 408 LEU A CG  1 
ATOM   789  C CD1 A LEU A 1 78  ? 21.66000  39.95500  12.57600 0.700 46.17527  ? 408 LEU A CD1 1 
ATOM   790  C CD1 B LEU A 1 78  ? 23.39600  39.83400  11.24200 0.300 52.04707  ? 408 LEU A CD1 1 
ATOM   791  C CD2 A LEU A 1 78  ? 23.94200  39.80300  11.51400 0.700 53.47822  ? 408 LEU A CD2 1 
ATOM   792  C CD2 B LEU A 1 78  ? 24.41400  37.55500  11.44700 0.300 56.80872  ? 408 LEU A CD2 1 
ATOM   793  N N   A SER A 1 79  ? 22.10000  38.11600  16.01600 0.700 55.92718  ? 409 SER A N   1 
ATOM   794  N N   B SER A 1 79  ? 21.89300  38.27500  16.10200 0.300 56.72596  ? 409 SER A N   1 
ATOM   795  C CA  A SER A 1 79  ? 21.26900  38.77600  17.01500 0.700 53.86560  ? 409 SER A CA  1 
ATOM   796  C CA  B SER A 1 79  ? 21.17800  38.86800  17.22600 0.300 55.49467  ? 409 SER A CA  1 
ATOM   797  C C   A SER A 1 79  ? 22.13700  39.24900  18.17200 0.700 65.90374  ? 409 SER A C   1 
ATOM   798  C C   B SER A 1 79  ? 22.16600  39.35000  18.27900 0.300 65.33855  ? 409 SER A C   1 
ATOM   799  O O   A SER A 1 79  ? 21.89700  40.31600  18.74700 0.700 66.04932  ? 409 SER A O   1 
ATOM   800  O O   B SER A 1 79  ? 21.94900  40.38500  18.92000 0.300 65.93196  ? 409 SER A O   1 
ATOM   801  C CB  A SER A 1 79  ? 20.16700  37.83900  17.50400 0.700 53.74230  ? 409 SER A CB  1 
ATOM   802  C CB  B SER A 1 79  ? 20.19300  37.86300  17.82300 0.300 55.96303  ? 409 SER A CB  1 
ATOM   803  O OG  A SER A 1 79  ? 20.49600  37.27900  18.76200 0.700 61.78346  ? 409 SER A OG  1 
ATOM   804  O OG  B SER A 1 79  ? 19.24500  37.44400  16.85700 0.300 59.53558  ? 409 SER A OG  1 
ATOM   805  N N   A ALA A 1 80  ? 23.16000  38.46200  18.51600 0.700 64.42400  ? 410 ALA A N   1 
ATOM   806  N N   B ALA A 1 80  ? 23.25800  38.60500  18.47200 0.300 64.11792  ? 410 ALA A N   1 
ATOM   807  C CA  A ALA A 1 80  ? 24.08200  38.84700  19.57800 0.700 59.61900  ? 410 ALA A CA  1 
ATOM   808  C CA  B ALA A 1 80  ? 24.28300  39.02100  19.42200 0.300 62.26566  ? 410 ALA A CA  1 
ATOM   809  C C   A ALA A 1 80  ? 24.92500  40.02700  19.11900 0.700 66.05510  ? 410 ALA A C   1 
ATOM   810  C C   B ALA A 1 80  ? 25.01600  40.24500  18.89000 0.300 67.14831  ? 410 ALA A C   1 
ATOM   811  O O   A ALA A 1 80  ? 25.21500  40.93800  19.90200 0.700 71.05643  ? 410 ALA A O   1 
ATOM   812  O O   B ALA A 1 80  ? 25.35300  41.15800  19.65300 0.300 69.77235  ? 410 ALA A O   1 
ATOM   813  C CB  A ALA A 1 80  ? 24.96200  37.66400  19.97800 0.700 66.51978  ? 410 ALA A CB  1 
ATOM   814  C CB  B ALA A 1 80  ? 25.25600  37.87500  19.69200 0.300 64.35100  ? 410 ALA A CB  1 
ATOM   815  N N   A LEU A 1 81  ? 25.32800  40.02000  17.84600 0.700 69.84243  ? 411 LEU A N   1 
ATOM   816  N N   B LEU A 1 81  ? 25.27900  40.26900  17.58100 0.300 69.44552  ? 411 LEU A N   1 
ATOM   817  C CA  A LEU A 1 81  ? 26.05600  41.15100  17.27700 0.700 68.47239  ? 411 LEU A CA  1 
ATOM   818  C CA  B LEU A 1 81  ? 25.88600  41.44000  16.95600 0.300 68.85074  ? 411 LEU A CA  1 
ATOM   819  C C   A LEU A 1 81  ? 25.19400  42.40700  17.32600 0.700 73.37467  ? 411 LEU A C   1 
ATOM   820  C C   B LEU A 1 81  ? 24.96700  42.64500  17.10400 0.300 73.29901  ? 411 LEU A C   1 
ATOM   821  O O   A LEU A 1 81  ? 25.66200  43.47400  17.74100 0.700 76.67014  ? 411 LEU A O   1 
ATOM   822  O O   B LEU A 1 81  ? 25.41200  43.73800  17.47300 0.300 75.99596  ? 411 LEU A O   1 
ATOM   823  C CB  A LEU A 1 81  ? 26.48600  40.85100  15.84200 0.700 68.20563  ? 411 LEU A CB  1 
ATOM   824  C CB  B LEU A 1 81  ? 26.19800  41.16000  15.48600 0.300 65.01709  ? 411 LEU A CB  1 
ATOM   825  C CG  A LEU A 1 81  ? 27.53100  39.75600  15.60800 0.700 77.66195  ? 411 LEU A CG  1 
ATOM   826  C CG  B LEU A 1 81  ? 27.28500  40.11600  15.21100 0.300 73.61379  ? 411 LEU A CG  1 
ATOM   827  C CD1 A LEU A 1 81  ? 28.12700  39.88400  14.21500 0.700 74.91812  ? 411 LEU A CD1 1 
ATOM   828  C CD1 B LEU A 1 81  ? 27.78800  40.22700  13.78000 0.300 71.80756  ? 411 LEU A CD1 1 
ATOM   829  C CD2 A LEU A 1 81  ? 28.62500  39.81200  16.66300 0.700 70.62241  ? 411 LEU A CD2 1 
ATOM   830  C CD2 B LEU A 1 81  ? 28.43600  40.25100  16.20000 0.300 71.45851  ? 411 LEU A CD2 1 
ATOM   831  N N   A CYS A 1 82  ? 23.92600  42.29700  16.90200 0.700 73.87174  ? 412 CYS A N   1 
ATOM   832  N N   B CYS A 1 82  ? 23.67800  42.46600  16.79300 0.300 72.64302  ? 412 CYS A N   1 
ATOM   833  C CA  A CYS A 1 82  ? 23.01600  43.43900  16.95900 0.700 71.18024  ? 412 CYS A CA  1 
ATOM   834  C CA  B CYS A 1 82  ? 22.71400  43.54900  16.96300 0.300 71.14209  ? 412 CYS A CA  1 
ATOM   835  C C   A CYS A 1 82  ? 22.91000  43.99400  18.37000 0.700 66.55499  ? 412 CYS A C   1 
ATOM   836  C C   B CYS A 1 82  ? 22.72600  44.04100  18.40300 0.300 67.22222  ? 412 CYS A C   1 
ATOM   837  O O   A CYS A 1 82  ? 22.88500  45.21500  18.55400 0.700 69.58147  ? 412 CYS A O   1 
ATOM   838  O O   B CYS A 1 82  ? 22.67400  45.25100  18.65500 0.300 69.98481  ? 412 CYS A O   1 
ATOM   839  C CB  A CYS A 1 82  ? 21.62900  43.04600  16.43900 0.700 72.86387  ? 412 CYS A CB  1 
ATOM   840  C CB  B CYS A 1 82  ? 21.31300  43.09200  16.55800 0.300 72.41733  ? 412 CYS A CB  1 
ATOM   841  S SG  A CYS A 1 82  ? 21.55900  42.66100  14.68500 0.700 66.09277  ? 412 CYS A SG  1 
ATOM   842  S SG  B CYS A 1 82  ? 21.10500  42.74000  14.79600 0.300 69.28280  ? 412 CYS A SG  1 
ATOM   843  N N   A LEU A 1 83  ? 22.82700  43.12400  19.38200 0.700 66.07719  ? 413 LEU A N   1 
ATOM   844  N N   B LEU A 1 83  ? 22.79900  43.11500  19.36200 0.300 66.38583  ? 413 LEU A N   1 
ATOM   845  C CA  A LEU A 1 83  ? 22.67500  43.62400  20.74700 0.700 65.13853  ? 413 LEU A CA  1 
ATOM   846  C CA  B LEU A 1 83  ? 22.76800  43.48600  20.77200 0.300 65.50030  ? 413 LEU A CA  1 
ATOM   847  C C   A LEU A 1 83  ? 23.90900  44.44200  21.10800 0.700 76.26326  ? 413 LEU A C   1 
ATOM   848  C C   B LEU A 1 83  ? 23.98300  44.34400  21.09900 0.300 75.79650  ? 413 LEU A C   1 
ATOM   849  O O   A LEU A 1 83  ? 23.80800  45.61300  21.49900 0.700 83.39943  ? 413 LEU A O   1 
ATOM   850  O O   B LEU A 1 83  ? 23.85300  45.45400  21.62900 0.300 81.56873  ? 413 LEU A O   1 
ATOM   851  C CB  A LEU A 1 83  ? 22.48000  42.45300  21.71300 0.700 58.66238  ? 413 LEU A CB  1 
ATOM   852  C CB  B LEU A 1 83  ? 22.72000  42.23500  21.65100 0.300 61.25436  ? 413 LEU A CB  1 
ATOM   853  C CG  A LEU A 1 83  ? 21.76400  42.63200  23.05900 0.700 61.92558  ? 413 LEU A CG  1 
ATOM   854  C CG  B LEU A 1 83  ? 22.11800  42.42100  23.04700 0.300 63.22067  ? 413 LEU A CG  1 
ATOM   855  C CD1 A LEU A 1 83  ? 21.97000  41.39400  23.90800 0.700 63.63242  ? 413 LEU A CD1 1 
ATOM   856  C CD1 B LEU A 1 83  ? 21.01800  43.47300  23.02900 0.300 57.94650  ? 413 LEU A CD1 1 
ATOM   857  C CD2 A LEU A 1 83  ? 22.25500  43.85500  23.81800 0.700 63.72486  ? 413 LEU A CD2 1 
ATOM   858  C CD2 B LEU A 1 83  ? 21.58800  41.10200  23.58700 0.300 60.81535  ? 413 LEU A CD2 1 
ATOM   859  N N   A MET A 1 84  ? 25.09000  43.81800  21.01100 0.700 75.92631  ? 414 MET A N   1 
ATOM   860  N N   B MET A 1 84  ? 25.18100  43.82100  20.81700 0.300 75.43902  ? 414 MET A N   1 
ATOM   861  C CA  A MET A 1 84  ? 26.34200  44.52300  21.27400 0.700 75.70226  ? 414 MET A CA  1 
ATOM   862  C CA  B MET A 1 84  ? 26.40900  44.57200  21.06100 0.300 76.25036  ? 414 MET A CA  1 
ATOM   863  C C   A MET A 1 84  ? 26.42800  45.77000  20.40800 0.700 81.85731  ? 414 MET A C   1 
ATOM   864  C C   B MET A 1 84  ? 26.33100  45.93500  20.38700 0.300 81.88896  ? 414 MET A C   1 
ATOM   865  O O   A MET A 1 84  ? 26.84700  46.83100  20.87800 0.700 86.34478  ? 414 MET A O   1 
ATOM   866  O O   B MET A 1 84  ? 26.71500  46.95300  20.97300 0.300 86.08011  ? 414 MET A O   1 
ATOM   867  C CB  A MET A 1 84  ? 27.55900  43.61200  21.08000 0.700 82.34507  ? 414 MET A CB  1 
ATOM   868  C CB  B MET A 1 84  ? 27.61700  43.78800  20.54700 0.300 78.61693  ? 414 MET A CB  1 
ATOM   869  C CG  A MET A 1 84  ? 27.85700  42.70600  22.27300 0.700 76.05867  ? 414 MET A CG  1 
ATOM   870  C CG  B MET A 1 84  ? 28.92300  44.11800  21.24800 0.300 72.62285  ? 414 MET A CG  1 
ATOM   871  S SD  A MET A 1 84  ? 27.00200  41.12900  22.36000 0.700 93.47176  ? 414 MET A SD  1 
ATOM   872  S SD  B MET A 1 84  ? 30.26000  43.00000  20.78000 0.300 59.98241  ? 414 MET A SD  1 
ATOM   873  C CE  A MET A 1 84  ? 27.99600  40.27300  23.58200 0.700 80.51216  ? 414 MET A CE  1 
ATOM   874  C CE  B MET A 1 84  ? 29.82400  42.63900  19.08000 0.300 63.09783  ? 414 MET A CE  1 
ATOM   875  N N   A PHE A 1 85  ? 26.03900  45.64900  19.13200 0.700 80.71228  ? 415 PHE A N   1 
ATOM   876  N N   B PHE A 1 85  ? 25.83900  45.96600  19.14400 0.300 80.86442  ? 415 PHE A N   1 
ATOM   877  C CA  A PHE A 1 85  ? 26.15400  46.76500  18.19800 0.700 85.64824  ? 415 PHE A CA  1 
ATOM   878  C CA  B PHE A 1 85  ? 25.77000  47.21300  18.39100 0.300 82.92444  ? 415 PHE A CA  1 
ATOM   879  C C   A PHE A 1 85  ? 25.30000  47.94000  18.65000 0.700 81.02618  ? 415 PHE A C   1 
ATOM   880  C C   B PHE A 1 85  ? 24.83700  48.19700  19.08200 0.300 81.89688  ? 415 PHE A C   1 
ATOM   881  O O   A PHE A 1 85  ? 25.74300  49.09400  18.60000 0.700 82.98805  ? 415 PHE A O   1 
ATOM   882  O O   B PHE A 1 85  ? 25.15300  49.38700  19.20100 0.300 86.69253  ? 415 PHE A O   1 
ATOM   883  C CB  A PHE A 1 85  ? 25.68800  46.35000  16.80000 0.700 87.47689  ? 415 PHE A CB  1 
ATOM   884  C CB  B PHE A 1 85  ? 25.30300  46.95100  16.95900 0.300 82.91775  ? 415 PHE A CB  1 
ATOM   885  C CG  A PHE A 1 85  ? 25.58400  47.50200  15.84300 0.700 84.79575  ? 415 PHE A CG  1 
ATOM   886  C CG  B PHE A 1 85  ? 24.99200  48.20300  16.18600 0.300 77.76829  ? 415 PHE A CG  1 
ATOM   887  C CD1 A PHE A 1 85  ? 26.70500  48.27300  15.59200 0.700 88.50352  ? 415 PHE A CD1 1 
ATOM   888  C CD1 B PHE A 1 85  ? 25.94400  49.20000  16.04400 0.300 83.29140  ? 415 PHE A CD1 1 
ATOM   889  C CD2 A PHE A 1 85  ? 24.36400  47.87200  15.26600 0.700 77.01529  ? 415 PHE A CD2 1 
ATOM   890  C CD2 B PHE A 1 85  ? 23.74500  48.38800  15.61300 0.300 75.43394  ? 415 PHE A CD2 1 
ATOM   891  C CE1 A PHE A 1 85  ? 26.65400  49.34200  14.72900 0.700 86.37602  ? 415 PHE A CE1 1 
ATOM   892  C CE1 B PHE A 1 85  ? 25.66000  50.35400  15.33800 0.300 77.18295  ? 415 PHE A CE1 1 
ATOM   893  C CE2 A PHE A 1 85  ? 24.29600  48.96000  14.40500 0.700 82.74818  ? 415 PHE A CE2 1 
ATOM   894  C CE2 B PHE A 1 85  ? 23.45500  49.54100  14.90500 0.300 75.96649  ? 415 PHE A CE2 1 
ATOM   895  C CZ  A PHE A 1 85  ? 25.44600  49.69600  14.13800 0.700 82.07078  ? 415 PHE A CZ  1 
ATOM   896  C CZ  B PHE A 1 85  ? 24.41400  50.52500  14.76800 0.300 72.37666  ? 415 PHE A CZ  1 
ATOM   897  N N   A TYR A 1 86  ? 24.06300  47.66800  19.08300 0.700 80.91444  ? 416 TYR A N   1 
ATOM   898  N N   B TYR A 1 86  ? 23.68100  47.71700  19.55100 0.300 79.02712  ? 416 TYR A N   1 
ATOM   899  C CA  A TYR A 1 86  ? 23.19400  48.72200  19.59200 0.700 84.95812  ? 416 TYR A CA  1 
ATOM   900  C CA  B TYR A 1 86  ? 22.77100  48.59400  20.27300 0.300 78.71557  ? 416 TYR A CA  1 
ATOM   901  C C   A TYR A 1 86  ? 23.72100  49.26100  20.91100 0.700 86.62688  ? 416 TYR A C   1 
ATOM   902  C C   B TYR A 1 86  ? 23.35600  49.00800  21.61500 0.300 79.95000  ? 416 TYR A C   1 
ATOM   903  O O   A TYR A 1 86  ? 23.34200  50.36200  21.32700 0.700 86.31794  ? 416 TYR A O   1 
ATOM   904  O O   B TYR A 1 86  ? 22.91300  50.00600  22.19200 0.300 76.90250  ? 416 TYR A O   1 
ATOM   905  C CB  A TYR A 1 86  ? 21.77800  48.19100  19.81900 0.700 76.03196  ? 416 TYR A CB  1 
ATOM   906  C CB  B TYR A 1 86  ? 21.43200  47.89000  20.50300 0.300 71.35711  ? 416 TYR A CB  1 
ATOM   907  C CG  A TYR A 1 86  ? 21.06200  47.64100  18.60300 0.700 76.89260  ? 416 TYR A CG  1 
ATOM   908  C CG  B TYR A 1 86  ? 20.71100  47.47100  19.24500 0.300 71.59148  ? 416 TYR A CG  1 
ATOM   909  C CD1 A TYR A 1 86  ? 21.33300  48.11100  17.32300 0.700 75.50712  ? 416 TYR A CD1 1 
ATOM   910  C CD1 B TYR A 1 86  ? 20.87200  48.17200  18.05700 0.300 73.12874  ? 416 TYR A CD1 1 
ATOM   911  C CD2 A TYR A 1 86  ? 20.11700  46.63000  18.74200 0.700 73.70503  ? 416 TYR A CD2 1 
ATOM   912  C CD2 B TYR A 1 86  ? 19.88400  46.35500  19.24200 0.300 68.81091  ? 416 TYR A CD2 1 
ATOM   913  C CE1 A TYR A 1 86  ? 20.67100  47.59100  16.21800 0.700 68.75573  ? 416 TYR A CE1 1 
ATOM   914  C CE1 B TYR A 1 86  ? 20.21800  47.78000  16.90600 0.300 67.86366  ? 416 TYR A CE1 1 
ATOM   915  C CE2 A TYR A 1 86  ? 19.45800  46.10600  17.65000 0.700 75.90801  ? 416 TYR A CE2 1 
ATOM   916  C CE2 B TYR A 1 86  ? 19.23100  45.95400  18.09700 0.300 71.39595  ? 416 TYR A CE2 1 
ATOM   917  C CZ  A TYR A 1 86  ? 19.73600  46.58900  16.39200 0.700 68.54766  ? 416 TYR A CZ  1 
ATOM   918  C CZ  B TYR A 1 86  ? 19.39800  46.67100  16.93400 0.300 68.44816  ? 416 TYR A CZ  1 
ATOM   919  O OH  A TYR A 1 86  ? 19.06600  46.06200  15.31200 0.700 55.46090  ? 416 TYR A OH  1 
ATOM   920  O OH  B TYR A 1 86  ? 18.73700  46.27000  15.79900 0.300 59.79342  ? 416 TYR A OH  1 
ATOM   921  N N   A GLY A 1 87  ? 24.57500  48.48100  21.57300 0.700 86.01302  ? 417 GLY A N   1 
ATOM   922  N N   B GLY A 1 87  ? 24.33500  48.25500  22.12000 0.300 82.13122  ? 417 GLY A N   1 
ATOM   923  C CA  A GLY A 1 87  ? 25.17300  48.70500  22.87400 0.700 87.04091  ? 417 GLY A CA  1 
ATOM   924  C CA  B GLY A 1 87  ? 24.93700  48.48100  23.42400 0.300 82.57480  ? 417 GLY A CA  1 
ATOM   925  C C   A GLY A 1 87  ? 26.24300  49.77200  22.87700 0.700 100.31627 ? 417 GLY A C   1 
ATOM   926  C C   B GLY A 1 87  ? 25.84800  49.68800  23.47000 0.300 94.88019  ? 417 GLY A C   1 
ATOM   927  O O   A GLY A 1 87  ? 26.63500  50.23400  23.95400 0.700 104.22934 ? 417 GLY A O   1 
ATOM   928  O O   B GLY A 1 87  ? 26.19800  50.14700  24.56400 0.300 97.40425  ? 417 GLY A O   1 
ATOM   929  N N   A TYR A 1 88  ? 26.71800  50.16700  21.69800 0.700 99.98382  ? 418 TYR A N   1 
ATOM   930  N N   B TYR A 1 88  ? 26.23700  50.19800  22.30300 0.300 96.20720  ? 418 TYR A N   1 
ATOM   931  C CA  A TYR A 1 88  ? 27.77600  51.15800  21.55200 0.700 92.36984  ? 418 TYR A CA  1 
ATOM   932  C CA  B TYR A 1 88  ? 27.12700  51.33800  22.15000 0.300 93.08292  ? 418 TYR A CA  1 
ATOM   933  C C   A TYR A 1 88  ? 27.31200  52.50200  22.09200 0.700 98.34448  ? 418 TYR A C   1 
ATOM   934  C C   B TYR A 1 88  ? 26.49000  52.60700  22.71000 0.300 97.42339  ? 418 TYR A C   1 
ATOM   935  O O   A TYR A 1 88  ? 26.11300  52.75800  22.20300 0.700 103.87282 ? 418 TYR A O   1 
ATOM   936  O O   B TYR A 1 88  ? 27.16900  53.60500  22.95400 0.300 97.79543  ? 418 TYR A O   1 
ATOM   937  C CB  A TYR A 1 88  ? 28.13200  51.34100  20.06800 0.700 94.02217  ? 418 TYR A CB  1 
ATOM   938  C CB  B TYR A 1 88  ? 27.45700  51.53800  20.66200 0.300 91.31495  ? 418 TYR A CB  1 
ATOM   939  C CG  A TYR A 1 88  ? 28.82300  50.18300  19.37500 0.700 106.86334 ? 418 TYR A CG  1 
ATOM   940  C CG  B TYR A 1 88  ? 28.32400  50.45500  20.04400 0.300 97.54703  ? 418 TYR A CG  1 
ATOM   941  C CD1 A TYR A 1 88  ? 28.92000  48.93500  19.97200 0.700 104.73586 ? 418 TYR A CD1 1 
ATOM   942  C CD1 B TYR A 1 88  ? 28.68900  49.32400  20.76600 0.300 96.61336  ? 418 TYR A CD1 1 
ATOM   943  C CD2 A TYR A 1 88  ? 29.33500  50.33400  18.08700 0.700 104.45703 ? 418 TYR A CD2 1 
ATOM   944  C CD2 B TYR A 1 88  ? 28.75800  50.56000  18.72900 0.300 100.69799 ? 418 TYR A CD2 1 
ATOM   945  C CE1 A TYR A 1 88  ? 29.52400  47.87400  19.32300 0.700 102.82614 ? 418 TYR A CE1 1 
ATOM   946  C CE1 B TYR A 1 88  ? 29.47200  48.33600  20.20100 0.300 97.56736  ? 418 TYR A CE1 1 
ATOM   947  C CE2 A TYR A 1 88  ? 29.94600  49.27800  17.43000 0.700 96.45381  ? 418 TYR A CE2 1 
ATOM   948  C CE2 B TYR A 1 88  ? 29.54400  49.57700  18.15500 0.300 100.18775 ? 418 TYR A CE2 1 
ATOM   949  C CZ  A TYR A 1 88  ? 30.03700  48.05100  18.05400 0.700 98.18083  ? 418 TYR A CZ  1 
ATOM   950  C CZ  B TYR A 1 88  ? 29.89600  48.46700  18.89700 0.300 99.20469  ? 418 TYR A CZ  1 
ATOM   951  O OH  A TYR A 1 88  ? 30.64100  46.99200  17.41700 0.700 100.92429 ? 418 TYR A OH  1 
ATOM   952  O OH  B TYR A 1 88  ? 30.68100  47.48800  18.33200 0.300 98.47628  ? 418 TYR A OH  1 
ATOM   953  N N   A CYS A 1 95  ? 14.37100  54.76000  25.65000 0.700 55.25973  ? 425 CYS A N   1 
ATOM   954  N N   B CYS A 1 95  ? 14.39300  55.01900  25.26500 0.300 60.30610  ? 425 CYS A N   1 
ATOM   955  C CA  A CYS A 1 95  ? 14.65800  54.97800  24.23500 0.700 72.59629  ? 425 CYS A CA  1 
ATOM   956  C CA  B CYS A 1 95  ? 14.72000  55.12300  23.84800 0.300 71.09651  ? 425 CYS A CA  1 
ATOM   957  C C   A CYS A 1 95  ? 15.64800  53.93300  23.72300 0.700 78.53015  ? 425 CYS A C   1 
ATOM   958  C C   B CYS A 1 95  ? 15.70300  54.03200  23.43600 0.300 77.12412  ? 425 CYS A C   1 
ATOM   959  O O   A CYS A 1 95  ? 16.65000  53.65400  24.37900 0.700 75.47697  ? 425 CYS A O   1 
ATOM   960  O O   B CYS A 1 95  ? 16.69000  53.77900  24.12700 0.300 74.69463  ? 425 CYS A O   1 
ATOM   961  C CB  A CYS A 1 95  ? 15.20700  56.39000  24.00900 0.700 62.29741  ? 425 CYS A CB  1 
ATOM   962  C CB  B CYS A 1 95  ? 15.29700  56.50400  23.53000 0.300 63.31959  ? 425 CYS A CB  1 
ATOM   963  N N   A GLY A 1 96  ? 15.37100  53.35900  22.55100 0.700 80.66326  ? 426 GLY A N   1 
ATOM   964  N N   B GLY A 1 96  ? 15.42700  53.39000  22.30200 0.300 78.59116  ? 426 GLY A N   1 
ATOM   965  C CA  A GLY A 1 96  ? 16.16900  52.25800  22.04900 0.700 63.08614  ? 426 GLY A CA  1 
ATOM   966  C CA  B GLY A 1 96  ? 16.19600  52.24400  21.86900 0.300 63.04626  ? 426 GLY A CA  1 
ATOM   967  C C   A GLY A 1 96  ? 15.84100  50.90000  22.63400 0.700 62.11790  ? 426 GLY A C   1 
ATOM   968  C C   B GLY A 1 96  ? 15.83000  50.93500  22.53300 0.300 62.25756  ? 426 GLY A C   1 
ATOM   969  O O   A GLY A 1 96  ? 16.48400  49.91400  22.25900 0.700 51.77949  ? 426 GLY A O   1 
ATOM   970  O O   B GLY A 1 96  ? 16.45100  49.91000  22.22500 0.300 52.30812  ? 426 GLY A O   1 
ATOM   971  N N   A TRP A 1 97  ? 14.85800  50.81800  23.53300 0.700 63.81327  ? 427 TRP A N   1 
ATOM   972  N N   B TRP A 1 97  ? 14.84700  50.93400  23.43800 0.300 63.02757  ? 427 TRP A N   1 
ATOM   973  C CA  A TRP A 1 97  ? 14.57100  49.57800  24.24900 0.700 48.34119  ? 427 TRP A CA  1 
ATOM   974  C CA  B TRP A 1 97  ? 14.54400  49.73200  24.20800 0.300 49.23602  ? 427 TRP A CA  1 
ATOM   975  C C   A TRP A 1 97  ? 13.95600  48.51600  23.34500 0.700 51.46579  ? 427 TRP A C   1 
ATOM   976  C C   B TRP A 1 97  ? 13.89200  48.65500  23.34900 0.300 51.52287  ? 427 TRP A C   1 
ATOM   977  O O   A TRP A 1 97  ? 14.09200  47.31800  23.62200 0.700 55.44656  ? 427 TRP A O   1 
ATOM   978  O O   B TRP A 1 97  ? 14.01500  47.46400  23.65700 0.300 54.62318  ? 427 TRP A O   1 
ATOM   979  C CB  A TRP A 1 97  ? 13.66000  49.86900  25.44500 0.700 51.60944  ? 427 TRP A CB  1 
ATOM   980  C CB  B TRP A 1 97  ? 13.66000  50.08400  25.40700 0.300 52.13791  ? 427 TRP A CB  1 
ATOM   981  C CG  A TRP A 1 97  ? 12.24300  50.22100  25.08100 0.700 46.50939  ? 427 TRP A CG  1 
ATOM   982  C CG  B TRP A 1 97  ? 12.25000  50.44900  25.06000 0.300 47.04583  ? 427 TRP A CG  1 
ATOM   983  C CD1 A TRP A 1 97  ? 11.72600  51.47600  24.91900 0.700 44.22886  ? 427 TRP A CD1 1 
ATOM   984  C CD1 B TRP A 1 97  ? 11.75400  51.70500  24.86400 0.300 45.08503  ? 427 TRP A CD1 1 
ATOM   985  C CD2 A TRP A 1 97  ? 11.15400  49.31000  24.87800 0.700 48.04412  ? 427 TRP A CD2 1 
ATOM   986  C CD2 B TRP A 1 97  ? 11.14200  49.55300  24.90900 0.300 48.36742  ? 427 TRP A CD2 1 
ATOM   987  N NE1 A TRP A 1 97  ? 10.38900  51.40100  24.60700 0.700 36.94109  ? 427 TRP A NE1 1 
ATOM   988  N NE1 B TRP A 1 97  ? 10.41200  51.64500  24.57900 0.300 37.74909  ? 427 TRP A NE1 1 
ATOM   989  C CE2 A TRP A 1 97  ? 10.01200  50.08300  24.57700 0.700 47.65851  ? 427 TRP A CE2 1 
ATOM   990  C CE2 B TRP A 1 97  ? 10.01100  50.33500  24.60200 0.300 47.49668  ? 427 TRP A CE2 1 
ATOM   991  C CE3 A TRP A 1 97  ? 11.03600  47.91600  24.91100 0.700 39.76941  ? 427 TRP A CE3 1 
ATOM   992  C CE3 B TRP A 1 97  ? 10.99800  48.16400  24.99300 0.300 41.52436  ? 427 TRP A CE3 1 
ATOM   993  C CZ2 A TRP A 1 97  ? 8.76800   49.50900  24.31100 0.700 43.02831  ? 427 TRP A CZ2 1 
ATOM   994  C CZ2 B TRP A 1 97  ? 8.75400   49.77600  24.37900 0.300 43.92842  ? 427 TRP A CZ2 1 
ATOM   995  C CZ3 A TRP A 1 97  ? 9.80100   47.34800  24.64500 0.700 40.14101  ? 427 TRP A CZ3 1 
ATOM   996  C CZ3 B TRP A 1 97  ? 9.75000   47.61100  24.77100 0.300 41.73841  ? 427 TRP A CZ3 1 
ATOM   997  C CH2 A TRP A 1 97  ? 8.68200   48.14500  24.34900 0.700 41.65615  ? 427 TRP A CH2 1 
ATOM   998  C CH2 B TRP A 1 97  ? 8.64400   48.41600  24.46800 0.300 42.15349  ? 427 TRP A CH2 1 
ATOM   999  N N   A GLU A 1 98  ? 13.27500  48.92600  22.27200 0.700 57.76001  ? 428 GLU A N   1 
ATOM   1000 N N   B GLU A 1 98  ? 13.19600  49.04600  22.27700 0.300 57.19046  ? 428 GLU A N   1 
ATOM   1001 C CA  A GLU A 1 98  ? 12.59700  47.96100  21.40900 0.700 54.03020  ? 428 GLU A CA  1 
ATOM   1002 C CA  B GLU A 1 98  ? 12.49700  48.06300  21.45400 0.300 53.27100  ? 428 GLU A CA  1 
ATOM   1003 C C   A GLU A 1 98  ? 13.58300  47.09200  20.63300 0.700 47.70494  ? 428 GLU A C   1 
ATOM   1004 C C   B GLU A 1 98  ? 13.48000  47.18500  20.69200 0.300 48.05219  ? 428 GLU A C   1 
ATOM   1005 O O   A GLU A 1 98  ? 13.38600  45.87500  20.53100 0.700 51.84712  ? 428 GLU A O   1 
ATOM   1006 O O   B GLU A 1 98  ? 13.31200  45.96100  20.63600 0.300 51.65050  ? 428 GLU A O   1 
ATOM   1007 C CB  A GLU A 1 98  ? 11.65500  48.68300  20.44200 0.700 44.90846  ? 428 GLU A CB  1 
ATOM   1008 C CB  B GLU A 1 98  ? 11.54600  48.76300  20.48500 0.300 45.08989  ? 428 GLU A CB  1 
ATOM   1009 C CG  A GLU A 1 98  ? 10.74000  49.70600  21.08800 0.700 35.97346  ? 428 GLU A CG  1 
ATOM   1010 C CG  B GLU A 1 98  ? 10.57500  49.72300  21.14600 0.300 37.66151  ? 428 GLU A CG  1 
ATOM   1011 C CD  A GLU A 1 98  ? 11.12400  51.12400  20.73000 0.700 44.73760  ? 428 GLU A CD  1 
ATOM   1012 C CD  B GLU A 1 98  ? 10.86900  51.16800  20.80300 0.300 45.41545  ? 428 GLU A CD  1 
ATOM   1013 O OE1 A GLU A 1 98  ? 12.34000  51.41100  20.70000 0.700 47.83795  ? 428 GLU A OE1 1 
ATOM   1014 O OE1 B GLU A 1 98  ? 12.06100  51.53100  20.72200 0.300 50.37989  ? 428 GLU A OE1 1 
ATOM   1015 O OE2 A GLU A 1 98  ? 10.21600  51.95300  20.48600 0.700 45.22526  ? 428 GLU A OE2 1 
ATOM   1016 O OE2 B GLU A 1 98  ? 9.90600   51.94100  20.61000 0.300 47.21436  ? 428 GLU A OE2 1 
ATOM   1017 N N   A GLU A 1 99  ? 14.63500  47.68400  20.05900 0.700 51.49884  ? 429 GLU A N   1 
ATOM   1018 N N   B GLU A 1 99  ? 14.50800  47.79100  20.09200 0.300 51.69386  ? 429 GLU A N   1 
ATOM   1019 C CA  A GLU A 1 99  ? 15.62400  46.86500  19.36200 0.700 51.21077  ? 429 GLU A CA  1 
ATOM   1020 C CA  B GLU A 1 99  ? 15.52800  47.00300  19.40800 0.300 51.70729  ? 429 GLU A CA  1 
ATOM   1021 C C   A GLU A 1 99  ? 16.27600  45.84700  20.29800 0.700 54.76176  ? 429 GLU A C   1 
ATOM   1022 C C   B GLU A 1 99  ? 16.21500  46.05300  20.38100 0.300 54.38950  ? 429 GLU A C   1 
ATOM   1023 O O   A GLU A 1 99  ? 16.52500  44.70300  19.90200 0.700 62.69171  ? 429 GLU A O   1 
ATOM   1024 O O   B GLU A 1 99  ? 16.53700  44.91300  20.02800 0.300 60.31313  ? 429 GLU A O   1 
ATOM   1025 C CB  A GLU A 1 99  ? 16.67200  47.75500  18.69200 0.700 59.06416  ? 429 GLU A CB  1 
ATOM   1026 C CB  B GLU A 1 99  ? 16.54400  47.92400  18.73200 0.300 58.98425  ? 429 GLU A CB  1 
ATOM   1027 C CG  A GLU A 1 99  ? 16.09500  48.84300  17.78300 0.700 58.33862  ? 429 GLU A CG  1 
ATOM   1028 C CG  B GLU A 1 99  ? 15.93100  48.97300  17.81400 0.300 57.97790  ? 429 GLU A CG  1 
ATOM   1029 C CD  A GLU A 1 99  ? 15.85900  50.15300  18.50800 0.700 61.24554  ? 429 GLU A CD  1 
ATOM   1030 C CD  B GLU A 1 99  ? 15.64300  50.28100  18.52200 0.300 61.55281  ? 429 GLU A CD  1 
ATOM   1031 O OE1 A GLU A 1 99  ? 14.78700  50.29900  19.13400 0.700 67.60036  ? 429 GLU A OE1 1 
ATOM   1032 O OE1 B GLU A 1 99  ? 14.86700  50.27300  19.50000 0.300 65.03765  ? 429 GLU A OE1 1 
ATOM   1033 O OE2 A GLU A 1 99  ? 16.74500  51.03600  18.45100 0.700 61.58048  ? 429 GLU A OE2 1 
ATOM   1034 O OE2 B GLU A 1 99  ? 16.19100  51.32000  18.09600 0.300 58.73141  ? 429 GLU A OE2 1 
ATOM   1035 N N   A ILE A 1 100 ? 16.55500  46.23900  21.54300 0.700 49.12248  ? 430 ILE A N   1 
ATOM   1036 N N   B ILE A 1 100 ? 16.44600  46.50900  21.61400 0.300 51.65878  ? 430 ILE A N   1 
ATOM   1037 C CA  A ILE A 1 100 ? 17.25900  45.35000  22.46900 0.700 48.02617  ? 430 ILE A CA  1 
ATOM   1038 C CA  B ILE A 1 100 ? 17.18200  45.71100  22.58800 0.300 50.63133  ? 430 ILE A CA  1 
ATOM   1039 C C   A ILE A 1 100 ? 16.34500  44.22700  22.94100 0.700 56.55801  ? 430 ILE A C   1 
ATOM   1040 C C   B ILE A 1 100 ? 16.32300  44.54900  23.07400 0.300 55.65885  ? 430 ILE A C   1 
ATOM   1041 O O   A ILE A 1 100 ? 16.75200  43.05900  22.99200 0.700 56.35565  ? 430 ILE A O   1 
ATOM   1042 O O   B ILE A 1 100 ? 16.80100  43.41500  23.20000 0.300 56.28792  ? 430 ILE A O   1 
ATOM   1043 C CB  A ILE A 1 100 ? 17.89200  46.12300  23.64800 0.700 53.22347  ? 430 ILE A CB  1 
ATOM   1044 C CB  B ILE A 1 100 ? 17.66100  46.59800  23.75200 0.300 55.06318  ? 430 ILE A CB  1 
ATOM   1045 C CG1 A ILE A 1 100 ? 19.11000  46.95300  23.18200 0.700 55.84043  ? 430 ILE A CG1 1 
ATOM   1046 C CG1 B ILE A 1 100 ? 18.74800  47.56300  23.27200 0.300 54.40868  ? 430 ILE A CG1 1 
ATOM   1047 C CG2 A ILE A 1 100 ? 18.18600  45.19200  24.85700 0.700 57.97465  ? 430 ILE A CG2 1 
ATOM   1048 C CG2 B ILE A 1 100 ? 18.17500  45.74500  24.90100 0.300 55.70607  ? 430 ILE A CG2 1 
ATOM   1049 C CD1 A ILE A 1 100 ? 18.83100  48.10200  22.18700 0.700 63.21282  ? 430 ILE A CD1 1 
ATOM   1050 C CD1 B ILE A 1 100 ? 19.11600  48.62500  24.28500 0.300 43.06832  ? 430 ILE A CD1 1 
ATOM   1051 N N   A TYR A 1 101 ? 15.09400  44.55200  23.27800 0.700 52.36748  ? 431 TYR A N   1 
ATOM   1052 N N   B TYR A 1 101 ? 15.04500  44.81500  23.36300 0.300 52.20729  ? 431 TYR A N   1 
ATOM   1053 C CA  A TYR A 1 101 ? 14.19700  43.52400  23.79400 0.700 49.17679  ? 431 TYR A CA  1 
ATOM   1054 C CA  B TYR A 1 101 ? 14.15300  43.77800  23.87700 0.300 50.00422  ? 431 TYR A CA  1 
ATOM   1055 C C   A TYR A 1 101 ? 14.03300  42.39700  22.77900 0.700 50.55122  ? 431 TYR A C   1 
ATOM   1056 C C   B TYR A 1 101 ? 14.04200  42.62600  22.88500 0.300 50.72939  ? 431 TYR A C   1 
ATOM   1057 O O   A TYR A 1 101 ? 14.13300  41.21600  23.13000 0.700 54.14362  ? 431 TYR A O   1 
ATOM   1058 O O   B TYR A 1 101 ? 14.13100  41.45300  23.26400 0.300 52.25012  ? 431 TYR A O   1 
ATOM   1059 C CB  A TYR A 1 101 ? 12.84500  44.13700  24.16300 0.700 51.68867  ? 431 TYR A CB  1 
ATOM   1060 C CB  B TYR A 1 101 ? 12.77700  44.36900  24.18300 0.300 51.39399  ? 431 TYR A CB  1 
ATOM   1061 C CG  A TYR A 1 101 ? 11.90600  43.16500  24.84200 0.700 50.10753  ? 431 TYR A CG  1 
ATOM   1062 C CG  B TYR A 1 101 ? 11.82800  43.40000  24.85400 0.300 50.01220  ? 431 TYR A CG  1 
ATOM   1063 C CD1 A TYR A 1 101 ? 12.04400  42.87600  26.19400 0.700 54.81607  ? 431 TYR A CD1 1 
ATOM   1064 C CD1 B TYR A 1 101 ? 11.91500  43.14900  26.21700 0.300 54.12282  ? 431 TYR A CD1 1 
ATOM   1065 C CD2 A TYR A 1 101 ? 10.87800  42.55000  24.14400 0.700 42.09535  ? 431 TYR A CD2 1 
ATOM   1066 C CD2 B TYR A 1 101 ? 10.84200  42.74400  24.12900 0.300 42.74372  ? 431 TYR A CD2 1 
ATOM   1067 C CE1 A TYR A 1 101 ? 11.20600  41.98200  26.82500 0.700 49.92539  ? 431 TYR A CE1 1 
ATOM   1068 C CE1 B TYR A 1 101 ? 11.06200  42.25600  26.83600 0.300 50.09666  ? 431 TYR A CE1 1 
ATOM   1069 C CE2 A TYR A 1 101 ? 10.02300  41.66300  24.77100 0.700 45.53661  ? 431 TYR A CE2 1 
ATOM   1070 C CE2 B TYR A 1 101 ? 9.97400   41.85900  24.74200 0.300 45.55862  ? 431 TYR A CE2 1 
ATOM   1071 C CZ  A TYR A 1 101 ? 10.19600  41.38300  26.11200 0.700 47.21512  ? 431 TYR A CZ  1 
ATOM   1072 C CZ  B TYR A 1 101 ? 10.09100  41.61600  26.09500 0.300 47.39320  ? 431 TYR A CZ  1 
ATOM   1073 O OH  A TYR A 1 101 ? 9.34300   40.51200  26.74800 0.700 45.47830  ? 431 TYR A OH  1 
ATOM   1074 O OH  B TYR A 1 101 ? 9.22000   40.74700  26.71100 0.300 46.02822  ? 431 TYR A OH  1 
ATOM   1075 N N   A VAL A 1 102 ? 13.79500  42.74400  21.50900 0.700 44.38504  ? 432 VAL A N   1 
ATOM   1076 N N   B VAL A 1 102 ? 13.84400  42.94800  21.60400 0.300 45.89769  ? 432 VAL A N   1 
ATOM   1077 C CA  A VAL A 1 102 ? 13.59400  41.72200  20.48100 0.700 43.00379  ? 432 VAL A CA  1 
ATOM   1078 C CA  B VAL A 1 102 ? 13.68500  41.91700  20.58100 0.300 44.02367  ? 432 VAL A CA  1 
ATOM   1079 C C   A VAL A 1 102 ? 14.87100  40.91200  20.28500 0.700 45.69538  ? 432 VAL A C   1 
ATOM   1080 C C   B VAL A 1 102 ? 14.97000  41.11000  20.46100 0.300 46.05029  ? 432 VAL A C   1 
ATOM   1081 O O   A VAL A 1 102 ? 14.83800  39.68000  20.17000 0.700 51.09586  ? 432 VAL A O   1 
ATOM   1082 O O   B VAL A 1 102 ? 14.94300  39.87600  20.36000 0.300 49.69338  ? 432 VAL A O   1 
ATOM   1083 C CB  A VAL A 1 102 ? 13.13600  42.36800  19.16100 0.700 45.33008  ? 432 VAL A CB  1 
ATOM   1084 C CB  B VAL A 1 102 ? 13.27600  42.54700  19.23700 0.300 45.47966  ? 432 VAL A CB  1 
ATOM   1085 C CG1 A VAL A 1 102 ? 12.93400  41.29600  18.08900 0.700 40.77056  ? 432 VAL A CG1 1 
ATOM   1086 C CG1 B VAL A 1 102 ? 13.12300  41.47200  18.17400 0.300 41.81738  ? 432 VAL A CG1 1 
ATOM   1087 C CG2 A VAL A 1 102 ? 11.87700  43.19300  19.37700 0.700 32.23380  ? 432 VAL A CG2 1 
ATOM   1088 C CG2 B VAL A 1 102 ? 11.97800  43.32300  19.39200 0.300 33.54280  ? 432 VAL A CG2 1 
ATOM   1089 N N   A ALA A 1 103 ? 16.01400  41.59900  20.22300 0.700 48.01540  ? 433 ALA A N   1 
ATOM   1090 N N   B ALA A 1 103 ? 16.11500  41.79500  20.46300 0.300 48.51293  ? 433 ALA A N   1 
ATOM   1091 C CA  A ALA A 1 103 ? 17.29000  40.93000  19.98800 0.700 46.85161  ? 433 ALA A CA  1 
ATOM   1092 C CA  B ALA A 1 103 ? 17.39800  41.11900  20.31100 0.300 48.92230  ? 433 ALA A CA  1 
ATOM   1093 C C   A ALA A 1 103 ? 17.65900  40.03000  21.16000 0.700 45.79306  ? 433 ALA A C   1 
ATOM   1094 C C   B ALA A 1 103 ? 17.67200  40.21900  21.50800 0.300 49.27804  ? 433 ALA A C   1 
ATOM   1095 O O   A ALA A 1 103 ? 18.21000  38.94000  20.96300 0.700 46.42585  ? 433 ALA A O   1 
ATOM   1096 O O   B ALA A 1 103 ? 18.23800  39.12900  21.35700 0.300 48.93852  ? 433 ALA A O   1 
ATOM   1097 C CB  A ALA A 1 103 ? 18.39000  41.95900  19.72400 0.700 52.38423  ? 433 ALA A CB  1 
ATOM   1098 C CB  B ALA A 1 103 ? 18.51900  42.14300  20.13400 0.300 53.13097  ? 433 ALA A CB  1 
ATOM   1099 N N   A THR A 1 104 ? 17.35400  40.46700  22.38500 0.700 51.65471  ? 434 THR A N   1 
ATOM   1100 N N   B THR A 1 104 ? 17.28400  40.66200  22.70700 0.300 51.59154  ? 434 THR A N   1 
ATOM   1101 C CA  A THR A 1 104 ? 17.53300  39.60600  23.55000 0.700 47.06972  ? 434 THR A CA  1 
ATOM   1102 C CA  B THR A 1 104 ? 17.35900  39.79100  23.87700 0.300 47.32936  ? 434 THR A CA  1 
ATOM   1103 C C   A THR A 1 104 ? 16.69500  38.34200  23.43400 0.700 43.45647  ? 434 THR A C   1 
ATOM   1104 C C   B THR A 1 104 ? 16.49400  38.55400  23.67200 0.300 43.61277  ? 434 THR A C   1 
ATOM   1105 O O   A THR A 1 104 ? 17.20000  37.23200  23.64000 0.700 43.77734  ? 434 THR A O   1 
ATOM   1106 O O   B THR A 1 104 ? 16.94500  37.42500  23.89500 0.300 44.87263  ? 434 THR A O   1 
ATOM   1107 C CB  A THR A 1 104 ? 17.17200  40.36300  24.82900 0.700 45.40914  ? 434 THR A CB  1 
ATOM   1108 C CB  B THR A 1 104 ? 16.92700  40.55100  25.13100 0.300 48.65406  ? 434 THR A CB  1 
ATOM   1109 O OG1 A THR A 1 104 ? 17.89600  41.59800  24.88100 0.700 55.99406  ? 434 THR A OG1 1 
ATOM   1110 O OG1 B THR A 1 104 ? 17.67600  41.76900  25.23700 0.300 56.75021  ? 434 THR A OG1 1 
ATOM   1111 C CG2 A THR A 1 104 ? 17.49300  39.52600  26.05400 0.700 44.77320  ? 434 THR A CG2 1 
ATOM   1112 C CG2 B THR A 1 104 ? 17.16300  39.70300  26.37100 0.300 48.88908  ? 434 THR A CG2 1 
ATOM   1113 N N   A ILE A 1 105 ? 15.40400  38.48400  23.12400 0.700 38.26932  ? 435 ILE A N   1 
ATOM   1114 N N   B ILE A 1 105 ? 15.23600  38.74900  23.26400 0.300 40.02918  ? 435 ILE A N   1 
ATOM   1115 C CA  A ILE A 1 105 ? 14.54800  37.30400  23.08400 0.700 32.82166  ? 435 ILE A CA  1 
ATOM   1116 C CA  B ILE A 1 105 ? 14.33000  37.61400  23.10900 0.300 35.48735  ? 435 ILE A CA  1 
ATOM   1117 C C   A ILE A 1 105 ? 15.03400  36.34000  22.00500 0.700 42.02696  ? 435 ILE A C   1 
ATOM   1118 C C   B ILE A 1 105 ? 14.87200  36.67600  22.04000 0.300 42.81461  ? 435 ILE A C   1 
ATOM   1119 O O   A ILE A 1 105 ? 15.09100  35.12300  22.22600 0.700 48.48454  ? 435 ILE A O   1 
ATOM   1120 O O   B ILE A 1 105 ? 14.81000  35.44800  22.18000 0.300 45.77591  ? 435 ILE A O   1 
ATOM   1121 C CB  A ILE A 1 105 ? 13.07900  37.71600  22.86600 0.700 31.11588  ? 435 ILE A CB  1 
ATOM   1122 C CB  B ILE A 1 105 ? 12.90100  38.09000  22.78900 0.300 37.13341  ? 435 ILE A CB  1 
ATOM   1123 C CG1 A ILE A 1 105 ? 12.59100  38.58400  24.02800 0.700 45.02284  ? 435 ILE A CG1 1 
ATOM   1124 C CG1 B ILE A 1 105 ? 12.35300  38.93400  23.94100 0.300 47.89381  ? 435 ILE A CG1 1 
ATOM   1125 C CG2 A ILE A 1 105 ? 12.19400  36.49000  22.72100 0.700 31.90894  ? 435 ILE A CG2 1 
ATOM   1126 C CG2 B ILE A 1 105 ? 11.98700  36.89900  22.53700 0.300 34.56410  ? 435 ILE A CG2 1 
ATOM   1127 C CD1 A ILE A 1 105 ? 12.55300  37.86000  25.35300 0.700 52.01696  ? 435 ILE A CD1 1 
ATOM   1128 C CD1 B ILE A 1 105 ? 12.18100  38.16700  25.23500 0.300 50.20532  ? 435 ILE A CD1 1 
ATOM   1129 N N   A GLU A 1 106 ? 15.40800  36.86900  20.82800 0.700 44.39300  ? 436 GLU A N   1 
ATOM   1130 N N   B GLU A 1 106 ? 15.39100  37.24400  20.94300 0.300 45.98103  ? 436 GLU A N   1 
ATOM   1131 C CA  A GLU A 1 106 ? 15.88500  36.00800  19.74500 0.700 45.90751  ? 436 GLU A CA  1 
ATOM   1132 C CA  B GLU A 1 106 ? 15.93900  36.42700  19.86400 0.300 47.19767  ? 436 GLU A CA  1 
ATOM   1133 C C   A GLU A 1 106 ? 17.07300  35.17300  20.20500 0.700 50.23458  ? 436 GLU A C   1 
ATOM   1134 C C   B GLU A 1 106 ? 17.01300  35.49700  20.41200 0.300 49.75615  ? 436 GLU A C   1 
ATOM   1135 O O   A GLU A 1 106 ? 17.18900  33.99100  19.85500 0.700 59.03050  ? 436 GLU A O   1 
ATOM   1136 O O   B GLU A 1 106 ? 17.13200  34.34100  19.99000 0.300 55.02601  ? 436 GLU A O   1 
ATOM   1137 C CB  A GLU A 1 106 ? 16.26100  36.83900  18.52200 0.700 44.97106  ? 436 GLU A CB  1 
ATOM   1138 C CB  B GLU A 1 106 ? 16.54000  37.33500  18.78900 0.300 47.67416  ? 436 GLU A CB  1 
ATOM   1139 C CG  A GLU A 1 106 ? 15.17500  36.93900  17.47800 0.700 54.33843  ? 436 GLU A CG  1 
ATOM   1140 C CG  B GLU A 1 106 ? 15.65200  37.67000  17.60600 0.300 53.26428  ? 436 GLU A CG  1 
ATOM   1141 C CD  A GLU A 1 106 ? 15.74300  37.33000  16.14000 0.700 69.51449  ? 436 GLU A CD  1 
ATOM   1142 C CD  B GLU A 1 106 ? 15.01100  36.45900  16.97800 0.300 59.98916  ? 436 GLU A CD  1 
ATOM   1143 O OE1 A GLU A 1 106 ? 16.34100  38.42100  16.05600 0.700 64.07730  ? 436 GLU A OE1 1 
ATOM   1144 O OE1 B GLU A 1 106 ? 15.74200  35.56400  16.50700 0.300 63.48160  ? 436 GLU A OE1 1 
ATOM   1145 O OE2 A GLU A 1 106 ? 15.60400  36.54100  15.18000 0.700 81.04912  ? 436 GLU A OE2 1 
ATOM   1146 O OE2 B GLU A 1 106 ? 13.76800  36.42200  16.93300 0.300 58.60064  ? 436 GLU A OE2 1 
ATOM   1147 N N   A MET A 1 107 ? 17.95200  35.77200  21.01700 0.700 45.79609  ? 437 MET A N   1 
ATOM   1148 N N   B MET A 1 107 ? 17.80600  36.00400  21.35900 0.300 47.02694  ? 437 MET A N   1 
ATOM   1149 C CA  A MET A 1 107 ? 19.14600  35.08100  21.49400 0.700 45.85705  ? 437 MET A CA  1 
ATOM   1150 C CA  B MET A 1 107 ? 18.90200  35.24500  21.95200 0.300 46.78685  ? 437 MET A CA  1 
ATOM   1151 C C   A MET A 1 107 ? 18.73800  33.97400  22.44300 0.700 45.55763  ? 437 MET A C   1 
ATOM   1152 C C   B MET A 1 107 ? 18.36700  34.10300  22.80600 0.300 46.72076  ? 437 MET A C   1 
ATOM   1153 O O   A MET A 1 107 ? 19.15200  32.81800  22.29300 0.700 49.85582  ? 437 MET A O   1 
ATOM   1154 O O   B MET A 1 107 ? 18.75800  32.94300  22.62800 0.300 48.93046  ? 437 MET A O   1 
ATOM   1155 C CB  A MET A 1 107 ? 20.11200  36.04100  22.18100 0.700 46.51675  ? 437 MET A CB  1 
ATOM   1156 C CB  B MET A 1 107 ? 19.80500  36.16500  22.77200 0.300 49.34732  ? 437 MET A CB  1 
ATOM   1157 C CG  A MET A 1 107 ? 21.52900  35.50100  22.21800 0.700 60.30277  ? 437 MET A CG  1 
ATOM   1158 C CG  B MET A 1 107 ? 20.82200  36.93000  21.93900 0.300 50.48075  ? 437 MET A CG  1 
ATOM   1159 S SD  A MET A 1 107 ? 22.64800  36.48700  23.21600 0.700 69.90094  ? 437 MET A SD  1 
ATOM   1160 S SD  B MET A 1 107 ? 22.19600  37.57100  22.91600 0.300 66.43587  ? 437 MET A SD  1 
ATOM   1161 C CE  A MET A 1 107 ? 21.78700  38.05200  23.18900 0.700 64.32249  ? 437 MET A CE  1 
ATOM   1162 C CE  B MET A 1 107 ? 22.18700  36.43500  24.30100 0.300 63.99639  ? 437 MET A CE  1 
ATOM   1163 N N   A ILE A 1 108 ? 17.96200  34.34400  23.46500 0.700 42.27157  ? 438 ILE A N   1 
ATOM   1164 N N   B ILE A 1 108 ? 17.49100  34.43100  23.76300 0.300 45.62446  ? 438 ILE A N   1 
ATOM   1165 C CA  A ILE A 1 108 ? 17.39100  33.38300  24.40300 0.700 47.90799  ? 438 ILE A CA  1 
ATOM   1166 C CA  B ILE A 1 108 ? 16.83400  33.42000  24.59200 0.300 47.57896  ? 438 ILE A CA  1 
ATOM   1167 C C   A ILE A 1 108 ? 16.71500  32.25600  23.63600 0.700 48.77391  ? 438 ILE A C   1 
ATOM   1168 C C   B ILE A 1 108 ? 16.23000  32.32700  23.72100 0.300 49.47653  ? 438 ILE A C   1 
ATOM   1169 O O   A ILE A 1 108 ? 16.75800  31.09400  24.05100 0.700 52.17830  ? 438 ILE A O   1 
ATOM   1170 O O   B ILE A 1 108 ? 16.26700  31.14300  24.07600 0.300 51.42040  ? 438 ILE A O   1 
ATOM   1171 C CB  A ILE A 1 108 ? 16.42500  34.08400  25.37600 0.700 37.69258  ? 438 ILE A CB  1 
ATOM   1172 C CB  B ILE A 1 108 ? 15.77100  34.08300  25.48900 0.300 39.06944  ? 438 ILE A CB  1 
ATOM   1173 C CG1 A ILE A 1 108 ? 17.15900  35.16800  26.17000 0.700 35.80756  ? 438 ILE A CG1 1 
ATOM   1174 C CG1 B ILE A 1 108 ? 16.42000  35.13300  26.39100 0.300 39.16543  ? 438 ILE A CG1 1 
ATOM   1175 C CG2 A ILE A 1 108 ? 15.76100  33.07600  26.30600 0.700 44.63872  ? 438 ILE A CG2 1 
ATOM   1176 C CG2 B ILE A 1 108 ? 15.04700  33.04000  26.32700 0.300 42.12479  ? 438 ILE A CG2 1 
ATOM   1177 C CD1 A ILE A 1 108 ? 16.23900  36.23200  26.72000 0.700 45.61313  ? 438 ILE A CD1 1 
ATOM   1178 C CD1 B ILE A 1 108 ? 15.45900  36.18800  26.88900 0.300 41.12270  ? 438 ILE A CD1 1 
ATOM   1179 N N   A LYS A 1 109 ? 16.05000  32.58700  22.52400 0.700 44.20938  ? 439 LYS A N   1 
ATOM   1180 N N   B LYS A 1 109 ? 15.63500  32.70200  22.58800 0.300 46.47972  ? 439 LYS A N   1 
ATOM   1181 C CA  A LYS A 1 109 ? 15.31000  31.58100  21.76900 0.700 45.03438  ? 439 LYS A CA  1 
ATOM   1182 C CA  B LYS A 1 109 ? 14.98000  31.70200  21.75200 0.300 47.13870  ? 439 LYS A CA  1 
ATOM   1183 C C   A LYS A 1 109 ? 16.26100  30.48200  21.31000 0.700 50.07841  ? 439 LYS A C   1 
ATOM   1184 C C   B LYS A 1 109 ? 16.00100  30.67100  21.28400 0.300 51.35477  ? 439 LYS A C   1 
ATOM   1185 O O   A LYS A 1 109 ? 15.93000  29.29200  21.38700 0.700 45.15638  ? 439 LYS A O   1 
ATOM   1186 O O   B LYS A 1 109 ? 15.74900  29.46100  21.32400 0.300 46.43748  ? 439 LYS A O   1 
ATOM   1187 C CB  A LYS A 1 109 ? 14.60100  32.23100  20.58300 0.700 49.58210  ? 439 LYS A CB  1 
ATOM   1188 C CB  B LYS A 1 109 ? 14.28700  32.37000  20.56500 0.300 51.14305  ? 439 LYS A CB  1 
ATOM   1189 C CG  A LYS A 1 109 ? 13.95900  31.25700  19.60800 0.700 46.97847  ? 439 LYS A CG  1 
ATOM   1190 C CG  B LYS A 1 109 ? 13.75000  31.38900  19.53400 0.300 48.00454  ? 439 LYS A CG  1 
ATOM   1191 C CD  A LYS A 1 109 ? 14.06000  31.78000  18.18300 0.700 52.06025  ? 439 LYS A CD  1 
ATOM   1192 C CD  B LYS A 1 109 ? 13.86300  31.93500  18.11900 0.300 53.25434  ? 439 LYS A CD  1 
ATOM   1193 C CE  A LYS A 1 109 ? 13.23100  30.94300  17.23200 0.700 52.93799  ? 439 LYS A CE  1 
ATOM   1194 C CE  B LYS A 1 109 ? 15.19800  32.62000  17.88100 0.300 53.23501  ? 439 LYS A CE  1 
ATOM   1195 N NZ  A LYS A 1 109 ? 11.84200  30.79200  17.73700 0.700 56.49124  ? 439 LYS A NZ  1 
ATOM   1196 N NZ  B LYS A 1 109 ? 15.40700  32.93000  16.43900 0.300 54.47594  ? 439 LYS A NZ  1 
ATOM   1197 N N   A PHE A 1 110 ? 17.44100  30.86600  20.81000 0.700 57.73730  ? 440 PHE A N   1 
ATOM   1198 N N   B PHE A 1 110 ? 17.16900  31.14400  20.83600 0.300 57.57590  ? 440 PHE A N   1 
ATOM   1199 C CA  A PHE A 1 110 ? 18.37100  29.90100  20.23000 0.700 58.74822  ? 440 PHE A CA  1 
ATOM   1200 C CA  B PHE A 1 110 ? 18.16800  30.26600  20.23500 0.300 59.23822  ? 440 PHE A CA  1 
ATOM   1201 C C   A PHE A 1 110 ? 18.88300  28.94100  21.29100 0.700 59.86733  ? 440 PHE A C   1 
ATOM   1202 C C   B PHE A 1 110 ? 18.74000  29.29500  21.26100 0.300 59.66789  ? 440 PHE A C   1 
ATOM   1203 O O   A PHE A 1 110 ? 19.01300  27.74100  21.03000 0.700 63.11268  ? 440 PHE A O   1 
ATOM   1204 O O   B PHE A 1 110 ? 18.98000  28.12300  20.94700 0.300 62.05227  ? 440 PHE A O   1 
ATOM   1205 C CB  A PHE A 1 110 ? 19.54700  30.61000  19.54700 0.700 66.81446  ? 440 PHE A CB  1 
ATOM   1206 C CB  B PHE A 1 110 ? 19.29100  31.08200  19.59900 0.300 62.53403  ? 440 PHE A CB  1 
ATOM   1207 C CG  A PHE A 1 110 ? 20.67000  29.67300  19.10700 0.700 77.10957  ? 440 PHE A CG  1 
ATOM   1208 C CG  B PHE A 1 110 ? 20.44800  30.24700  19.12600 0.300 70.91436  ? 440 PHE A CG  1 
ATOM   1209 C CD1 A PHE A 1 110 ? 21.56600  29.13500  20.03700 0.700 72.16755  ? 440 PHE A CD1 1 
ATOM   1210 C CD1 B PHE A 1 110 ? 20.43200  29.67300  17.86500 0.300 69.88268  ? 440 PHE A CD1 1 
ATOM   1211 C CD2 A PHE A 1 110 ? 20.89200  29.41700  17.76100 0.700 71.28615  ? 440 PHE A CD2 1 
ATOM   1212 C CD2 B PHE A 1 110 ? 21.55300  30.03500  19.94000 0.300 68.68006  ? 440 PHE A CD2 1 
ATOM   1213 C CE1 A PHE A 1 110 ? 22.59900  28.30400  19.64300 0.700 65.16704  ? 440 PHE A CE1 1 
ATOM   1214 C CE1 B PHE A 1 110 ? 21.49200  28.90600  17.42400 0.300 69.51364  ? 440 PHE A CE1 1 
ATOM   1215 C CE2 A PHE A 1 110 ? 21.93400  28.58800  17.35900 0.700 70.38809  ? 440 PHE A CE2 1 
ATOM   1216 C CE2 B PHE A 1 110 ? 22.61500  29.26800  19.50300 0.300 69.49354  ? 440 PHE A CE2 1 
ATOM   1217 C CZ  A PHE A 1 110 ? 22.78800  28.03300  18.30400 0.700 75.39285  ? 440 PHE A CZ  1 
ATOM   1218 C CZ  B PHE A 1 110 ? 22.58500  28.70300  18.24400 0.300 71.95021  ? 440 PHE A CZ  1 
ATOM   1219 N N   A ILE A 1 111 ? 19.15900  29.44400  22.49900 0.700 56.71810  ? 441 ILE A N   1 
ATOM   1220 N N   B ILE A 1 111 ? 18.97700  29.76800  22.48900 0.300 57.33313  ? 441 ILE A N   1 
ATOM   1221 C CA  A ILE A 1 111 ? 19.68100  28.57000  23.54500 0.700 52.76430  ? 441 ILE A CA  1 
ATOM   1222 C CA  B ILE A 1 111 ? 19.54700  28.90500  23.52200 0.300 55.63139  ? 441 ILE A CA  1 
ATOM   1223 C C   A ILE A 1 111 ? 18.64200  27.51100  23.86700 0.700 62.38588  ? 441 ILE A C   1 
ATOM   1224 C C   B ILE A 1 111 ? 18.58100  27.77000  23.83000 0.300 62.09090  ? 441 ILE A C   1 
ATOM   1225 O O   A ILE A 1 111 ? 18.98900  26.36500  24.17900 0.700 69.45529  ? 441 ILE A O   1 
ATOM   1226 O O   B ILE A 1 111 ? 18.99700  26.64100  24.11600 0.300 67.53709  ? 441 ILE A O   1 
ATOM   1227 C CB  A ILE A 1 111 ? 20.12500  29.36500  24.79300 0.700 58.31711  ? 441 ILE A CB  1 
ATOM   1228 C CB  B ILE A 1 111 ? 19.92600  29.71800  24.77800 0.300 59.01955  ? 441 ILE A CB  1 
ATOM   1229 C CG1 A ILE A 1 111 ? 18.93800  29.82800  25.63700 0.700 60.46957  ? 441 ILE A CG1 1 
ATOM   1230 C CG1 B ILE A 1 111 ? 18.69800  30.09600  25.60800 0.300 59.74544  ? 441 ILE A CG1 1 
ATOM   1231 C CG2 A ILE A 1 111 ? 20.98300  30.55700  24.37900 0.700 54.85361  ? 441 ILE A CG2 1 
ATOM   1232 C CG2 B ILE A 1 111 ? 20.70700  30.96700  24.38900 0.300 54.27678  ? 441 ILE A CG2 1 
ATOM   1233 C CD1 A ILE A 1 111 ? 19.25200  29.92200  27.11600 0.700 62.46350  ? 441 ILE A CD1 1 
ATOM   1234 C CD1 B ILE A 1 111 ? 19.02700  30.84400  26.88200 0.300 53.51068  ? 441 ILE A CD1 1 
ATOM   1235 N N   A ILE A 1 112 ? 17.35700  27.86500  23.80600 0.700 66.93047  ? 442 ILE A N   1 
ATOM   1236 N N   B ILE A 1 112 ? 17.27900  28.05100  23.78000 0.300 65.12882  ? 442 ILE A N   1 
ATOM   1237 C CA  A ILE A 1 112 ? 16.32900  26.86600  24.05800 0.700 57.85896  ? 442 ILE A CA  1 
ATOM   1238 C CA  B ILE A 1 112 ? 16.29000  27.00800  24.01900 0.300 58.03059  ? 442 ILE A CA  1 
ATOM   1239 C C   A ILE A 1 112 ? 16.27100  25.90300  22.87700 0.700 55.19711  ? 442 ILE A C   1 
ATOM   1240 C C   B ILE A 1 112 ? 16.26000  26.06000  22.82700 0.300 55.71702  ? 442 ILE A C   1 
ATOM   1241 O O   A ILE A 1 112 ? 16.23100  24.68100  23.05800 0.700 60.24913  ? 442 ILE A O   1 
ATOM   1242 O O   B ILE A 1 112 ? 16.24900  24.83400  22.98700 0.300 59.85706  ? 442 ILE A O   1 
ATOM   1243 C CB  A ILE A 1 112 ? 14.97300  27.54200  24.31800 0.700 53.58355  ? 442 ILE A CB  1 
ATOM   1244 C CB  B ILE A 1 112 ? 14.90800  27.62600  24.29600 0.300 53.98373  ? 442 ILE A CB  1 
ATOM   1245 C CG1 A ILE A 1 112 ? 15.07700  28.49000  25.51400 0.700 48.92794  ? 442 ILE A CG1 1 
ATOM   1246 C CG1 B ILE A 1 112 ? 14.97700  28.55800  25.50800 0.300 50.02014  ? 442 ILE A CG1 1 
ATOM   1247 C CG2 A ILE A 1 112 ? 13.89700  26.50000  24.53400 0.700 54.68474  ? 442 ILE A CG2 1 
ATOM   1248 C CG2 B ILE A 1 112 ? 13.87200  26.53800  24.51600 0.300 54.76424  ? 442 ILE A CG2 1 
ATOM   1249 C CD1 A ILE A 1 112 ? 13.82900  29.31700  25.75100 0.700 53.92632  ? 442 ILE A CD1 1 
ATOM   1250 C CD1 B ILE A 1 112 ? 13.69800  29.32900  25.76200 0.300 53.78759  ? 442 ILE A CD1 1 
ATOM   1251 N N   A GLU A 1 113 ? 16.24400  26.44100  21.64800 0.700 60.25572  ? 443 GLU A N   1 
ATOM   1252 N N   B GLU A 1 113 ? 16.21900  26.62100  21.61200 0.300 60.47771  ? 443 GLU A N   1 
ATOM   1253 C CA  A GLU A 1 113 ? 16.30900  25.58800  20.46200 0.700 63.15451  ? 443 GLU A CA  1 
ATOM   1254 C CA  B GLU A 1 113 ? 16.28700  25.80700  20.40100 0.300 62.91309  ? 443 GLU A CA  1 
ATOM   1255 C C   A GLU A 1 113 ? 17.53100  24.68400  20.54800 0.700 66.83364  ? 443 GLU A C   1 
ATOM   1256 C C   B GLU A 1 113 ? 17.50800  24.89700  20.43300 0.300 66.55441  ? 443 GLU A C   1 
ATOM   1257 O O   A GLU A 1 113 ? 17.46300  23.48000  20.28600 0.700 69.32691  ? 443 GLU A O   1 
ATOM   1258 O O   B GLU A 1 113 ? 17.42500  23.70400  20.12600 0.300 67.79635  ? 443 GLU A O   1 
ATOM   1259 C CB  A GLU A 1 113 ? 16.37400  26.43200  19.18600 0.700 58.35859  ? 443 GLU A CB  1 
ATOM   1260 C CB  B GLU A 1 113 ? 16.34800  26.71000  19.16500 0.300 59.97823  ? 443 GLU A CB  1 
ATOM   1261 C CG  A GLU A 1 113 ? 15.11100  27.16100  18.83000 0.700 57.94904  ? 443 GLU A CG  1 
ATOM   1262 C CG  B GLU A 1 113 ? 15.07400  27.45500  18.84400 0.300 60.69718  ? 443 GLU A CG  1 
ATOM   1263 C CD  A GLU A 1 113 ? 15.17000  27.78300  17.44900 0.700 67.85574  ? 443 GLU A CD  1 
ATOM   1264 C CD  B GLU A 1 113 ? 15.12200  28.14400  17.49600 0.300 67.79160  ? 443 GLU A CD  1 
ATOM   1265 O OE1 A GLU A 1 113 ? 16.17400  28.46500  17.14700 0.700 69.66620  ? 443 GLU A OE1 1 
ATOM   1266 O OE1 B GLU A 1 113 ? 16.21600  28.59300  17.09600 0.300 69.14492  ? 443 GLU A OE1 1 
ATOM   1267 O OE2 A GLU A 1 113 ? 14.21200  27.59300  16.66900 0.700 69.31891  ? 443 GLU A OE2 1 
ATOM   1268 O OE2 B GLU A 1 113 ? 14.06400  28.23800  16.83700 0.300 67.17129  ? 443 GLU A OE2 1 
ATOM   1269 N N   A TYR A 1 114 ? 18.67000  25.27300  20.91200 0.700 66.57163  ? 444 TYR A N   1 
ATOM   1270 N N   B TYR A 1 114 ? 18.66000  25.45800  20.80500 0.300 66.14970  ? 444 TYR A N   1 
ATOM   1271 C CA  A TYR A 1 114 ? 19.93500  24.54800  20.91700 0.700 63.78947  ? 444 TYR A CA  1 
ATOM   1272 C CA  B TYR A 1 114 ? 19.91400  24.71500  20.74900 0.300 64.97077  ? 444 TYR A CA  1 
ATOM   1273 C C   A TYR A 1 114 ? 19.90100  23.37000  21.87800 0.700 72.52807  ? 444 TYR A C   1 
ATOM   1274 C C   B TYR A 1 114 ? 19.87600  23.49200  21.65800 0.300 71.65380  ? 444 TYR A C   1 
ATOM   1275 O O   A TYR A 1 114 ? 20.41600  22.29300  21.56500 0.700 72.62105  ? 444 TYR A O   1 
ATOM   1276 O O   B TYR A 1 114 ? 20.37600  22.42100  21.29500 0.300 71.80069  ? 444 TYR A O   1 
ATOM   1277 C CB  A TYR A 1 114 ? 21.08900  25.47900  21.27400 0.700 70.42841  ? 444 TYR A CB  1 
ATOM   1278 C CB  B TYR A 1 114 ? 21.08400  25.62700  21.11900 0.300 70.45940  ? 444 TYR A CB  1 
ATOM   1279 C CG  A TYR A 1 114 ? 22.41600  24.76500  21.39200 0.700 78.75905  ? 444 TYR A CG  1 
ATOM   1280 C CG  B TYR A 1 114 ? 22.41500  24.91500  21.15900 0.300 78.61843  ? 444 TYR A CG  1 
ATOM   1281 C CD1 A TYR A 1 114 ? 23.08000  24.27700  20.27300 0.700 78.55655  ? 444 TYR A CD1 1 
ATOM   1282 C CD1 B TYR A 1 114 ? 23.03200  24.49300  19.98900 0.300 77.98130  ? 444 TYR A CD1 1 
ATOM   1283 C CD2 A TYR A 1 114 ? 23.00000  24.57700  22.63800 0.700 78.16706  ? 444 TYR A CD2 1 
ATOM   1284 C CD2 B TYR A 1 114 ? 23.05600  24.66400  22.36500 0.300 78.20108  ? 444 TYR A CD2 1 
ATOM   1285 C CE1 A TYR A 1 114 ? 24.29700  23.62300  20.39900 0.700 81.49860  ? 444 TYR A CE1 1 
ATOM   1286 C CE1 B TYR A 1 114 ? 24.24900  23.84000  20.01700 0.300 79.40332  ? 444 TYR A CE1 1 
ATOM   1287 C CE2 A TYR A 1 114 ? 24.20700  23.93000  22.77300 0.700 84.06131  ? 444 TYR A CE2 1 
ATOM   1288 C CE2 B TYR A 1 114 ? 24.27400  24.01200  22.40400 0.300 83.86711  ? 444 TYR A CE2 1 
ATOM   1289 C CZ  A TYR A 1 114 ? 24.85400  23.45500  21.65400 0.700 93.76787  ? 444 TYR A CZ  1 
ATOM   1290 C CZ  B TYR A 1 114 ? 24.86500  23.60300  21.22700 0.300 89.61845  ? 444 TYR A CZ  1 
ATOM   1291 O OH  A TYR A 1 114 ? 26.06200  22.80900  21.79900 0.700 107.97639 ? 444 TYR A OH  1 
ATOM   1292 O OH  B TYR A 1 114 ? 26.07800  22.95300  21.26000 0.300 100.32576 ? 444 TYR A OH  1 
ATOM   1293 N N   A PHE A 1 115 ? 19.29100  23.54200  23.04100 0.700 67.97345  ? 445 PHE A N   1 
ATOM   1294 N N   B PHE A 1 115 ? 19.28400  23.63500  22.84300 0.300 67.91583  ? 445 PHE A N   1 
ATOM   1295 C CA  A PHE A 1 115 ? 19.31400  22.46500  24.01000 0.700 55.75098  ? 445 PHE A CA  1 
ATOM   1296 C CA  B PHE A 1 115 ? 19.25600  22.56900  23.83600 0.300 57.43938  ? 445 PHE A CA  1 
ATOM   1297 C C   A PHE A 1 115 ? 18.10500  21.55100  23.91900 0.700 59.09776  ? 445 PHE A C   1 
ATOM   1298 C C   B PHE A 1 115 ? 18.00100  21.70400  23.78500 0.300 59.86963  ? 445 PHE A C   1 
ATOM   1299 O O   A PHE A 1 115 ? 18.24400  20.34000  24.14400 0.700 72.10796  ? 445 PHE A O   1 
ATOM   1300 O O   B PHE A 1 115 ? 18.08600  20.50100  24.05900 0.300 70.32572  ? 445 PHE A O   1 
ATOM   1301 C CB  A PHE A 1 115 ? 19.33300  22.99600  25.44700 0.700 55.78968  ? 445 PHE A CB  1 
ATOM   1302 C CB  B PHE A 1 115 ? 19.37700  23.16700  25.24000 0.300 58.26570  ? 445 PHE A CB  1 
ATOM   1303 C CG  A PHE A 1 115 ? 20.61700  23.62700  25.88400 0.700 68.56897  ? 445 PHE A CG  1 
ATOM   1304 C CG  B PHE A 1 115 ? 20.74200  23.70300  25.56100 0.300 67.91817  ? 445 PHE A CG  1 
ATOM   1305 C CD1 A PHE A 1 115 ? 21.85800  23.02500  25.64700 0.700 68.11656  ? 445 PHE A CD1 1 
ATOM   1306 C CD1 B PHE A 1 115 ? 21.87700  22.94800  25.31800 0.300 67.66084  ? 445 PHE A CD1 1 
ATOM   1307 C CD2 A PHE A 1 115 ? 20.56100  24.80100  26.62500 0.700 63.41289  ? 445 PHE A CD2 1 
ATOM   1308 C CD2 B PHE A 1 115 ? 20.88800  24.96700  26.10800 0.300 65.89662  ? 445 PHE A CD2 1 
ATOM   1309 C CE1 A PHE A 1 115 ? 23.02600  23.63000  26.09800 0.700 67.08487  ? 445 PHE A CE1 1 
ATOM   1310 C CE1 B PHE A 1 115 ? 23.13300  23.44500  25.61600 0.300 65.46723  ? 445 PHE A CE1 1 
ATOM   1311 C CE2 A PHE A 1 115 ? 21.70100  25.41100  27.08400 0.700 69.41834  ? 445 PHE A CE2 1 
ATOM   1312 C CE2 B PHE A 1 115 ? 22.13900  25.46900  26.40700 0.300 70.41858  ? 445 PHE A CE2 1 
ATOM   1313 C CZ  A PHE A 1 115 ? 22.94500  24.83000  26.82300 0.700 76.23400  ? 445 PHE A CZ  1 
ATOM   1314 C CZ  B PHE A 1 115 ? 23.26300  24.70700  26.16000 0.300 72.08732  ? 445 PHE A CZ  1 
ATOM   1315 N N   A HIS A 1 116 ? 16.93500  22.08500  23.57400 0.700 58.36320  ? 446 HIS A N   1 
ATOM   1316 N N   B HIS A 1 116 ? 16.84200  22.26700  23.44700 0.300 59.58576  ? 446 HIS A N   1 
ATOM   1317 C CA  A HIS A 1 116 ? 15.68000  21.35000  23.71900 0.700 56.25191  ? 446 HIS A CA  1 
ATOM   1318 C CA  B HIS A 1 116 ? 15.57600  21.55800  23.63200 0.300 57.42562  ? 446 HIS A CA  1 
ATOM   1319 C C   A HIS A 1 116 ? 14.71100  21.62600  22.57100 0.700 53.11807  ? 446 HIS A C   1 
ATOM   1320 C C   B HIS A 1 116 ? 14.59800  21.83000  22.49600 0.300 54.90309  ? 446 HIS A C   1 
ATOM   1321 O O   A HIS A 1 116 ? 13.50000  21.73000  22.78900 0.700 55.11597  ? 446 HIS A O   1 
ATOM   1322 O O   B HIS A 1 116 ? 13.39000  21.95500  22.72500 0.300 55.89683  ? 446 HIS A O   1 
ATOM   1323 C CB  A HIS A 1 116 ? 15.00200  21.68300  25.04700 0.700 64.36357  ? 446 HIS A CB  1 
ATOM   1324 C CB  B HIS A 1 116 ? 14.92600  21.91300  24.97100 0.300 63.68827  ? 446 HIS A CB  1 
ATOM   1325 C CG  A HIS A 1 116 ? 15.87900  21.48400  26.24300 0.700 72.28689  ? 446 HIS A CG  1 
ATOM   1326 C CG  B HIS A 1 116 ? 15.81600  21.70600  26.15800 0.300 70.70479  ? 446 HIS A CG  1 
ATOM   1327 N ND1 A HIS A 1 116 ? 16.14600  20.24000  26.77300 0.700 73.32501  ? 446 HIS A ND1 1 
ATOM   1328 N ND1 B HIS A 1 116 ? 16.06400  20.46000  26.69300 0.300 73.08841  ? 446 HIS A ND1 1 
ATOM   1329 C CD2 A HIS A 1 116 ? 16.52500  22.37600  27.03100 0.700 64.51009  ? 446 HIS A CD2 1 
ATOM   1330 C CD2 B HIS A 1 116 ? 16.49400  22.58800  26.93000 0.300 64.52595  ? 446 HIS A CD2 1 
ATOM   1331 C CE1 A HIS A 1 116 ? 16.93400  20.37400  27.82500 0.700 74.42844  ? 446 HIS A CE1 1 
ATOM   1332 C CE1 B HIS A 1 116 ? 16.86900  20.58200  27.73300 0.300 73.95757  ? 446 HIS A CE1 1 
ATOM   1333 N NE2 A HIS A 1 116 ? 17.17900  21.65900  28.00300 0.700 72.58639  ? 446 HIS A NE2 1 
ATOM   1334 N NE2 B HIS A 1 116 ? 17.14500  21.86300  27.89800 0.300 72.64310  ? 446 HIS A NE2 1 
ATOM   1335 N N   A GLU A 1 117 ? 15.21900  21.77200  21.33900 0.700 61.40091  ? 447 GLU A N   1 
ATOM   1336 N N   B GLU A 1 117 ? 15.09800  21.94500  21.25800 0.300 62.12179  ? 447 GLU A N   1 
ATOM   1337 C CA  A GLU A 1 117 ? 14.37800  22.25800  20.24200 0.700 67.03373  ? 447 GLU A CA  1 
ATOM   1338 C CA  B GLU A 1 117 ? 14.25600  22.41800  20.15800 0.300 66.48435  ? 447 GLU A CA  1 
ATOM   1339 C C   A GLU A 1 117 ? 13.13000  21.40300  20.07800 0.700 68.72043  ? 447 GLU A C   1 
ATOM   1340 C C   B GLU A 1 117 ? 13.00200  21.56300  20.01900 0.300 67.56754  ? 447 GLU A C   1 
ATOM   1341 O O   A GLU A 1 117 ? 12.04100  21.92400  19.80800 0.700 70.28487  ? 447 GLU A O   1 
ATOM   1342 O O   B GLU A 1 117 ? 11.91000  22.08400  19.76600 0.300 68.11012  ? 447 GLU A O   1 
ATOM   1343 C CB  A GLU A 1 117 ? 15.16200  22.27300  18.93100 0.700 69.70700  ? 447 GLU A CB  1 
ATOM   1344 C CB  B GLU A 1 117 ? 15.04100  22.41400  18.84700 0.300 69.43156  ? 447 GLU A CB  1 
ATOM   1345 C CG  A GLU A 1 117 ? 14.46200  22.98800  17.78900 0.700 76.23681  ? 447 GLU A CG  1 
ATOM   1346 C CG  B GLU A 1 117 ? 14.33900  23.11600  17.69800 0.300 75.75077  ? 447 GLU A CG  1 
ATOM   1347 C CD  A GLU A 1 117 ? 15.29700  23.01200  16.52400 0.700 78.93336  ? 447 GLU A CD  1 
ATOM   1348 C CD  B GLU A 1 117 ? 15.16800  23.12900  16.42900 0.300 78.56365  ? 447 GLU A CD  1 
ATOM   1349 O OE1 A GLU A 1 117 ? 16.48800  22.63900  16.59000 0.700 87.33288  ? 447 GLU A OE1 1 
ATOM   1350 O OE1 B GLU A 1 117 ? 15.82800  22.11000  16.13500 0.300 75.64713  ? 447 GLU A OE1 1 
ATOM   1351 O OE2 A GLU A 1 117 ? 14.76000  23.39500  15.46300 0.700 78.52957  ? 447 GLU A OE2 1 
ATOM   1352 O OE2 B GLU A 1 117 ? 15.15700  24.15800  15.72200 0.300 69.79065  ? 447 GLU A OE2 1 
ATOM   1353 N N   A PHE A 1 118 ? 13.26800  20.08800  20.22300 0.700 56.17562  ? 448 PHE A N   1 
ATOM   1354 N N   B PHE A 1 118 ? 13.14000  20.24800  20.17900 0.300 57.46245  ? 448 PHE A N   1 
ATOM   1355 C CA  A PHE A 1 118 ? 12.18800  19.15300  19.94800 0.700 53.17282  ? 448 PHE A CA  1 
ATOM   1356 C CA  B PHE A 1 118 ? 12.05700  19.30600  19.93200 0.300 53.71099  ? 448 PHE A CA  1 
ATOM   1357 C C   A PHE A 1 118 ? 11.69700  18.49100  21.22500 0.700 48.14450  ? 448 PHE A C   1 
ATOM   1358 C C   B PHE A 1 118 ? 11.58400  18.65300  21.22200 0.300 48.88621  ? 448 PHE A C   1 
ATOM   1359 O O   A PHE A 1 118 ? 10.94800  17.51100  21.16800 0.700 45.58938  ? 448 PHE A O   1 
ATOM   1360 O O   B PHE A 1 118 ? 10.83700  17.67000  21.18200 0.300 45.91661  ? 448 PHE A O   1 
ATOM   1361 C CB  A PHE A 1 118 ? 12.63800  18.12500  18.91500 0.700 49.30132  ? 448 PHE A CB  1 
ATOM   1362 C CB  B PHE A 1 118 ? 12.48600  18.25600  18.90700 0.300 50.08345  ? 448 PHE A CB  1 
ATOM   1363 C CG  A PHE A 1 118 ? 12.85400  18.71800  17.55900 0.700 52.64922  ? 448 PHE A CG  1 
ATOM   1364 C CG  B PHE A 1 118 ? 12.67900  18.81600  17.53200 0.300 53.06074  ? 448 PHE A CG  1 
ATOM   1365 C CD1 A PHE A 1 118 ? 11.77300  19.08000  16.77500 0.700 51.35528  ? 448 PHE A CD1 1 
ATOM   1366 C CD1 B PHE A 1 118 ? 11.58500  19.16700  16.75800 0.300 52.15701  ? 448 PHE A CD1 1 
ATOM   1367 C CD2 A PHE A 1 118 ? 14.13200  18.95800  17.08500 0.700 65.43137  ? 448 PHE A CD2 1 
ATOM   1368 C CD2 B PHE A 1 118 ? 13.94800  19.01500  17.01900 0.300 64.75048  ? 448 PHE A CD2 1 
ATOM   1369 C CE1 A PHE A 1 118 ? 11.96100  19.64200  15.53200 0.700 65.29059  ? 448 PHE A CE1 1 
ATOM   1370 C CE1 B PHE A 1 118 ? 11.75300  19.69300  15.49500 0.300 65.28138  ? 448 PHE A CE1 1 
ATOM   1371 C CE2 A PHE A 1 118 ? 14.32700  19.52000  15.84200 0.700 63.42180  ? 448 PHE A CE2 1 
ATOM   1372 C CE2 B PHE A 1 118 ? 14.12200  19.54100  15.75400 0.300 64.38638  ? 448 PHE A CE2 1 
ATOM   1373 C CZ  A PHE A 1 118 ? 13.23800  19.86500  15.06600 0.700 69.90611  ? 448 PHE A CZ  1 
ATOM   1374 C CZ  B PHE A 1 118 ? 13.02100  19.88200  14.99400 0.300 70.07585  ? 448 PHE A CZ  1 
ATOM   1375 N N   A ASP A 1 119 ? 12.10900  19.02100  22.37000 0.700 53.48931  ? 449 ASP A N   1 
ATOM   1376 N N   B ASP A 1 119 ? 12.00900  19.18800  22.36200 0.300 53.52506  ? 449 ASP A N   1 
ATOM   1377 C CA  A ASP A 1 119 ? 11.61900  18.62500  23.68000 0.700 53.24089  ? 449 ASP A CA  1 
ATOM   1378 C CA  B ASP A 1 119 ? 11.53100  18.78700  23.67500 0.300 53.34249  ? 449 ASP A CA  1 
ATOM   1379 C C   A ASP A 1 119 ? 10.36300  19.42300  24.01000 0.700 48.41442  ? 449 ASP A C   1 
ATOM   1380 C C   B ASP A 1 119 ? 10.27700  19.57300  24.02900 0.300 48.86737  ? 449 ASP A C   1 
ATOM   1381 O O   A ASP A 1 119 ? 10.26300  20.61100  23.69000 0.700 49.57939  ? 449 ASP A O   1 
ATOM   1382 O O   B ASP A 1 119 ? 10.17000  20.76500  23.73000 0.300 49.61681  ? 449 ASP A O   1 
ATOM   1383 C CB  A ASP A 1 119 ? 12.69200  18.83900  24.75000 0.700 54.58150  ? 449 ASP A CB  1 
ATOM   1384 C CB  B ASP A 1 119 ? 12.60700  19.00100  24.73900 0.300 55.17242  ? 449 ASP A CB  1 
ATOM   1385 C CG  A ASP A 1 119 ? 13.93600  18.00100  24.50400 0.700 57.82367  ? 449 ASP A CG  1 
ATOM   1386 C CG  B ASP A 1 119 ? 13.84700  18.17100  24.48500 0.300 57.85661  ? 449 ASP A CG  1 
ATOM   1387 O OD1 A ASP A 1 119 ? 13.82600  16.94200  23.84900 0.700 57.79999  ? 449 ASP A OD1 1 
ATOM   1388 O OD1 B ASP A 1 119 ? 13.73200  17.11700  23.82500 0.300 57.99085  ? 449 ASP A OD1 1 
ATOM   1389 O OD2 A ASP A 1 119 ? 15.02600  18.39800  24.96800 0.700 62.45700  ? 449 ASP A OD2 1 
ATOM   1390 O OD2 B ASP A 1 119 ? 14.93500  18.57200  24.94800 0.300 62.27781  ? 449 ASP A OD2 1 
ATOM   1391 N N   A GLU A 1 120 ? 9.40200   18.75900  24.62800 0.700 50.44385  ? 450 GLU A N   1 
ATOM   1392 N N   B GLU A 1 120 ? 9.33000   18.89500  24.65300 0.300 50.54304  ? 450 GLU A N   1 
ATOM   1393 C CA  A GLU A 1 120 ? 8.21700   19.44700  25.12400 0.700 49.14308  ? 450 GLU A CA  1 
ATOM   1394 C CA  B GLU A 1 120 ? 8.15000   19.57400  25.17000 0.300 49.40005  ? 450 GLU A CA  1 
ATOM   1395 C C   A GLU A 1 120 ? 8.59000   20.39400  26.26000 0.700 59.80295  ? 450 GLU A C   1 
ATOM   1396 C C   B GLU A 1 120 ? 8.53200   20.51000  26.31200 0.300 59.47354  ? 450 GLU A C   1 
ATOM   1397 O O   A GLU A 1 120 ? 9.34600   20.01000  27.16200 0.700 66.41657  ? 450 GLU A O   1 
ATOM   1398 O O   B GLU A 1 120 ? 9.29200   20.11700  27.20600 0.300 65.73373  ? 450 GLU A O   1 
ATOM   1399 C CB  A GLU A 1 120 ? 7.18100   18.44000  25.60700 0.700 46.36430  ? 450 GLU A CB  1 
ATOM   1400 C CB  B GLU A 1 120 ? 7.11800   18.56300  25.65600 0.300 46.61853  ? 450 GLU A CB  1 
ATOM   1401 C CG  A GLU A 1 120 ? 6.37700   17.80500  24.50100 0.700 46.74275  ? 450 GLU A CG  1 
ATOM   1402 C CG  B GLU A 1 120 ? 6.44000   17.77600  24.55900 0.300 46.71706  ? 450 GLU A CG  1 
ATOM   1403 C CD  A GLU A 1 120 ? 4.89500   17.85300  24.78100 0.700 40.35806  ? 450 GLU A CD  1 
ATOM   1404 C CD  B GLU A 1 120 ? 4.93400   17.83200  24.68200 0.300 41.08123  ? 450 GLU A CD  1 
ATOM   1405 O OE1 A GLU A 1 120 ? 4.49700   18.56800  25.72500 0.700 40.94643  ? 450 GLU A OE1 1 
ATOM   1406 O OE1 B GLU A 1 120 ? 4.45000   18.52400  25.60100 0.300 41.75778  ? 450 GLU A OE1 1 
ATOM   1407 O OE2 A GLU A 1 120 ? 4.12800   17.17600  24.06200 0.700 48.40712  ? 450 GLU A OE2 1 
ATOM   1408 O OE2 B GLU A 1 120 ? 4.23900   17.17400  23.88000 0.300 47.40144  ? 450 GLU A OE2 1 
ATOM   1409 N N   A PRO A 1 121 ? 8.09500   21.64000  26.24400 0.700 59.61822  ? 451 PRO A N   1 
ATOM   1410 N N   B PRO A 1 121 ? 8.03700   21.75700  26.30900 0.300 58.87838  ? 451 PRO A N   1 
ATOM   1411 C CA  A PRO A 1 121 ? 7.14600   22.20400  25.28300 0.700 51.49618  ? 451 PRO A CA  1 
ATOM   1412 C CA  B PRO A 1 121 ? 7.08500   22.31400  25.34800 0.300 51.28959  ? 451 PRO A CA  1 
ATOM   1413 C C   A PRO A 1 121 ? 7.70400   23.15100  24.22700 0.700 54.66786  ? 451 PRO A C   1 
ATOM   1414 C C   B PRO A 1 121 ? 7.63100   23.26700  24.28600 0.300 54.10793  ? 451 PRO A C   1 
ATOM   1415 O O   A PRO A 1 121 ? 6.96800   24.03400  23.79100 0.700 57.83657  ? 451 PRO A O   1 
ATOM   1416 O O   B PRO A 1 121 ? 6.88300   24.13800  23.85200 0.300 56.60116  ? 451 PRO A O   1 
ATOM   1417 C CB  A PRO A 1 121 ? 6.19800   22.94200  26.22200 0.700 49.00161  ? 451 PRO A CB  1 
ATOM   1418 C CB  B PRO A 1 121 ? 6.13000   23.04500  26.28300 0.300 49.15406  ? 451 PRO A CB  1 
ATOM   1419 C CG  A PRO A 1 121 ? 7.18400   23.60700  27.19000 0.700 48.70930  ? 451 PRO A CG  1 
ATOM   1420 C CG  B PRO A 1 121 ? 7.09300   23.69900  27.27700 0.300 48.64492  ? 451 PRO A CG  1 
ATOM   1421 C CD  A PRO A 1 121 ? 8.36300   22.62200  27.31000 0.700 55.80137  ? 451 PRO A CD  1 
ATOM   1422 C CD  B PRO A 1 121 ? 8.28600   22.73200  27.38700 0.300 55.25626  ? 451 PRO A CD  1 
ATOM   1423 N N   A ALA A 1 122 ? 8.96500   23.04500  23.79800 0.700 53.83904  ? 452 ALA A N   1 
ATOM   1424 N N   B ALA A 1 122 ? 8.88800   23.17500  23.84500 0.300 53.37247  ? 452 ALA A N   1 
ATOM   1425 C CA  A ALA A 1 122 ? 9.37200   23.76600  22.59600 0.700 44.47863  ? 452 ALA A CA  1 
ATOM   1426 C CA  B ALA A 1 122 ? 9.27900   23.90300  22.64100 0.300 44.71603  ? 452 ALA A CA  1 
ATOM   1427 C C   A ALA A 1 122 ? 8.58400   23.28900  21.38100 0.700 39.72395  ? 452 ALA A C   1 
ATOM   1428 C C   B ALA A 1 122 ? 8.48800   23.42300  21.42900 0.300 39.52732  ? 452 ALA A C   1 
ATOM   1429 O O   A ALA A 1 122 ? 8.15100   24.09700  20.54900 0.700 37.24648  ? 452 ALA A O   1 
ATOM   1430 O O   B ALA A 1 122 ? 8.07500   24.22800  20.58500 0.300 37.43522  ? 452 ALA A O   1 
ATOM   1431 C CB  A ALA A 1 122 ? 10.87300  23.60000  22.36800 0.700 42.81365  ? 452 ALA A CB  1 
ATOM   1432 C CB  B ALA A 1 122 ? 10.77900  23.75500  22.39700 0.300 43.72434  ? 452 ALA A CB  1 
ATOM   1433 N N   A VAL A 1 123 ? 8.36000   21.98000  21.28500 0.700 43.07922  ? 453 VAL A N   1 
ATOM   1434 N N   B VAL A 1 123 ? 8.27400   22.11400  21.32800 0.300 44.69687  ? 453 VAL A N   1 
ATOM   1435 C CA  A VAL A 1 123 ? 7.37300   21.38700  20.39100 0.700 36.58853  ? 453 VAL A CA  1 
ATOM   1436 C CA  B VAL A 1 123 ? 7.28800   21.51400  20.43700 0.300 37.61832  ? 453 VAL A CA  1 
ATOM   1437 C C   A VAL A 1 123 ? 6.35000   20.67500  21.25800 0.700 39.01579  ? 453 VAL A C   1 
ATOM   1438 C C   B VAL A 1 123 ? 6.27000   20.78500  21.30000 0.300 40.10478  ? 453 VAL A C   1 
ATOM   1439 O O   A VAL A 1 123 ? 6.71700   19.85900  22.11100 0.700 46.52434  ? 453 VAL A O   1 
ATOM   1440 O O   B VAL A 1 123 ? 6.64700   19.97900  22.15900 0.300 46.26797  ? 453 VAL A O   1 
ATOM   1441 C CB  A VAL A 1 123 ? 8.01200   20.40300  19.39500 0.700 45.72956  ? 453 VAL A CB  1 
ATOM   1442 C CB  B VAL A 1 123 ? 7.94000   20.55500  19.42400 0.300 44.69459  ? 453 VAL A CB  1 
ATOM   1443 C CG1 A VAL A 1 123 ? 6.93300   19.76400  18.52200 0.700 43.49855  ? 453 VAL A CG1 1 
ATOM   1444 C CG1 B VAL A 1 123 ? 6.88000   19.90000  18.55300 0.300 43.31562  ? 453 VAL A CG1 1 
ATOM   1445 C CG2 A VAL A 1 123 ? 9.08200   21.09900  18.55100 0.700 40.51215  ? 453 VAL A CG2 1 
ATOM   1446 C CG2 B VAL A 1 123 ? 8.95300   21.29600  18.56800 0.300 41.10145  ? 453 VAL A CG2 1 
ATOM   1447 N N   A ILE A 1 124 ? 5.07600   20.96300  21.03600 0.700 33.72244  ? 454 ILE A N   1 
ATOM   1448 N N   B ILE A 1 124 ? 4.99000   21.06000  21.07700 0.300 34.64540  ? 454 ILE A N   1 
ATOM   1449 C CA  A ILE A 1 124 ? 4.01100   20.25300  21.72900 0.700 30.47284  ? 454 ILE A CA  1 
ATOM   1450 C CA  B ILE A 1 124 ? 3.92500   20.33400  21.75900 0.300 30.17572  ? 454 ILE A CA  1 
ATOM   1451 C C   A ILE A 1 124 ? 3.56000   19.07500  20.88000 0.700 43.14195  ? 454 ILE A C   1 
ATOM   1452 C C   B ILE A 1 124 ? 3.49300   19.15800  20.89300 0.300 42.69889  ? 454 ILE A C   1 
ATOM   1453 O O   A ILE A 1 124 ? 3.11500   19.24900  19.74000 0.700 40.39353  ? 454 ILE A O   1 
ATOM   1454 O O   B ILE A 1 124 ? 3.04700   19.34000  19.75500 0.300 40.72159  ? 454 ILE A O   1 
ATOM   1455 C CB  A ILE A 1 124 ? 2.83200   21.18200  22.05000 0.700 29.91669  ? 454 ILE A CB  1 
ATOM   1456 C CB  B ILE A 1 124 ? 2.73200   21.25000  22.07100 0.300 30.22678  ? 454 ILE A CB  1 
ATOM   1457 C CG1 A ILE A 1 124 ? 3.29900   22.35100  22.92000 0.700 30.91927  ? 454 ILE A CG1 1 
ATOM   1458 C CG1 B ILE A 1 124 ? 3.16900   22.42700  22.94500 0.300 32.02193  ? 454 ILE A CG1 1 
ATOM   1459 C CG2 A ILE A 1 124 ? 1.71500   20.39700  22.73200 0.700 33.72828  ? 454 ILE A CG2 1 
ATOM   1460 C CG2 B ILE A 1 124 ? 1.62400   20.46300  22.75000 0.300 33.99209  ? 454 ILE A CG2 1 
ATOM   1461 C CD1 A ILE A 1 124 ? 2.25700   23.43700  23.08900 0.700 29.42302  ? 454 ILE A CD1 1 
ATOM   1462 C CD1 B ILE A 1 124 ? 2.10400   23.49100  23.09900 0.300 30.28198  ? 454 ILE A CD1 1 
ATOM   1463 N N   A TYR A 1 125 ? 3.68500   17.87400  21.43900 0.700 47.14031  ? 455 TYR A N   1 
ATOM   1464 N N   B TYR A 1 125 ? 3.62700   17.95000  21.43600 0.300 47.64583  ? 455 TYR A N   1 
ATOM   1465 C CA  A TYR A 1 125 ? 3.12700   16.66100  20.85600 0.700 35.45995  ? 455 TYR A CA  1 
ATOM   1466 C CA  B TYR A 1 125 ? 3.09000   16.73800  20.83000 0.300 35.32627  ? 455 TYR A CA  1 
ATOM   1467 C C   A TYR A 1 125 ? 1.81900   16.37000  21.58400 0.700 36.25165  ? 455 TYR A C   1 
ATOM   1468 C C   B TYR A 1 125 ? 1.78200   16.42400  21.54700 0.300 34.65357  ? 455 TYR A C   1 
ATOM   1469 O O   A TYR A 1 125 ? 1.83100   15.95500  22.74800 0.700 51.56098  ? 455 TYR A O   1 
ATOM   1470 O O   B TYR A 1 125 ? 1.79200   15.98600  22.70200 0.300 50.56049  ? 455 TYR A O   1 
ATOM   1471 C CB  A TYR A 1 125 ? 4.09500   15.48500  20.97400 0.700 44.92724  ? 455 TYR A CB  1 
ATOM   1472 C CB  B TYR A 1 125 ? 4.07700   15.57800  20.95000 0.300 44.68130  ? 455 TYR A CB  1 
ATOM   1473 C CG  A TYR A 1 125 ? 5.49100   15.77000  20.47300 0.700 40.85446  ? 455 TYR A CG  1 
ATOM   1474 C CG  B TYR A 1 125 ? 5.47400   15.90200  20.47100 0.300 42.33890  ? 455 TYR A CG  1 
ATOM   1475 C CD1 A TYR A 1 125 ? 6.43000   16.39800  21.28200 0.700 47.55425  ? 455 TYR A CD1 1 
ATOM   1476 C CD1 B TYR A 1 125 ? 5.81700   15.78800  19.13100 0.300 44.80252  ? 455 TYR A CD1 1 
ATOM   1477 C CD2 A TYR A 1 125 ? 5.86400   15.42600  19.18000 0.700 40.24319  ? 455 TYR A CD2 1 
ATOM   1478 C CD2 B TYR A 1 125 ? 6.45300   16.31800  21.36400 0.300 47.96645  ? 455 TYR A CD2 1 
ATOM   1479 C CE1 A TYR A 1 125 ? 7.71000   16.65500  20.82500 0.700 50.68863  ? 455 TYR A CE1 1 
ATOM   1480 C CE1 B TYR A 1 125 ? 7.09300   16.09100  18.69200 0.300 46.38881  ? 455 TYR A CE1 1 
ATOM   1481 C CE2 A TYR A 1 125 ? 7.13700   15.68600  18.71200 0.700 43.39336  ? 455 TYR A CE2 1 
ATOM   1482 C CE2 B TYR A 1 125 ? 7.73200   16.61700  20.93600 0.300 51.37978  ? 455 TYR A CE2 1 
ATOM   1483 C CZ  A TYR A 1 125 ? 8.05800   16.29800  19.53900 0.700 48.86459  ? 455 TYR A CZ  1 
ATOM   1484 C CZ  B TYR A 1 125 ? 8.04600   16.50300  19.59900 0.300 48.90721  ? 455 TYR A CZ  1 
ATOM   1485 O OH  A TYR A 1 125 ? 9.32500   16.56300  19.07100 0.700 51.93544  ? 455 TYR A OH  1 
ATOM   1486 O OH  B TYR A 1 125 ? 9.32100   16.79100  19.16900 0.300 52.71400  ? 455 TYR A OH  1 
ATOM   1487 N N   A SER A 1 126 ? 0.69700   16.58900  20.90600 0.700 28.31666  ? 456 SER A N   1 
ATOM   1488 N N   B SER A 1 126 ? 0.66200   16.64200  20.86900 0.300 28.58737  ? 456 SER A N   1 
ATOM   1489 C CA  A SER A 1 126 ? -0.60700  16.60400  21.55000 0.700 40.10129  ? 456 SER A CA  1 
ATOM   1490 C CA  B SER A 1 126 ? -0.64100  16.63500  21.51700 0.300 40.01214  ? 456 SER A CA  1 
ATOM   1491 C C   A SER A 1 126 ? -1.38200  15.34100  21.19300 0.700 42.00627  ? 456 SER A C   1 
ATOM   1492 C C   B SER A 1 126 ? -1.42100  15.37800  21.15300 0.300 41.58632  ? 456 SER A C   1 
ATOM   1493 O O   A SER A 1 126 ? -1.00200  14.58100  20.29500 0.700 47.03522  ? 456 SER A O   1 
ATOM   1494 O O   B SER A 1 126 ? -1.06700  14.63500  20.23300 0.300 46.75203  ? 456 SER A O   1 
ATOM   1495 C CB  A SER A 1 126 ? -1.39300  17.86300  21.16000 0.700 38.50825  ? 456 SER A CB  1 
ATOM   1496 C CB  B SER A 1 126 ? -1.43600  17.88800  21.13400 0.300 38.17398  ? 456 SER A CB  1 
ATOM   1497 O OG  A SER A 1 126 ? -1.58200  17.94700  19.75900 0.700 46.49469  ? 456 SER A OG  1 
ATOM   1498 O OG  B SER A 1 126 ? -1.62100  17.97000  19.73100 0.300 46.19008  ? 456 SER A OG  1 
ATOM   1499 N N   A SER A 1 127 ? -2.47600  15.11200  21.93100 0.700 41.15216  ? 457 SER A N   1 
ATOM   1500 N N   B SER A 1 127 ? -2.50300  15.14700  21.90400 0.300 40.29383  ? 457 SER A N   1 
ATOM   1501 C CA  A SER A 1 127 ? -3.18600  13.83900  21.84100 0.700 34.67903  ? 457 SER A CA  1 
ATOM   1502 C CA  B SER A 1 127 ? -3.23200  13.88600  21.81700 0.300 35.01128  ? 457 SER A CA  1 
ATOM   1503 C C   A SER A 1 127 ? -3.84800  13.65000  20.48600 0.700 37.99668  ? 457 SER A C   1 
ATOM   1504 C C   B SER A 1 127 ? -3.93300  13.71500  20.47700 0.300 38.41961  ? 457 SER A C   1 
ATOM   1505 O O   A SER A 1 127 ? -4.12100  12.51100  20.09400 0.700 48.58534  ? 457 SER A O   1 
ATOM   1506 O O   B SER A 1 127 ? -4.25200  12.58400  20.09700 0.300 48.21069  ? 457 SER A O   1 
ATOM   1507 C CB  A SER A 1 127 ? -4.24100  13.72800  22.94500 0.700 36.83280  ? 457 SER A CB  1 
ATOM   1508 C CB  B SER A 1 127 ? -4.24700  13.77400  22.95700 0.300 36.50837  ? 457 SER A CB  1 
ATOM   1509 O OG  A SER A 1 127 ? -5.08000  14.86900  22.97500 0.700 50.05419  ? 457 SER A OG  1 
ATOM   1510 O OG  B SER A 1 127 ? -5.06400  14.92500  23.03800 0.300 49.87179  ? 457 SER A OG  1 
ATOM   1511 N N   A ASN A 1 128 ? -4.11100  14.73400  19.76800 0.700 41.58545  ? 458 ASN A N   1 
ATOM   1512 N N   B ASN A 1 128 ? -4.20000  14.80800  19.76700 0.300 41.70991  ? 458 ASN A N   1 
ATOM   1513 C CA  A ASN A 1 128 ? -4.67200  14.64700  18.42900 0.700 42.83318  ? 458 ASN A CA  1 
ATOM   1514 C CA  B ASN A 1 128 ? -4.79800  14.73800  18.44200 0.300 42.45501  ? 458 ASN A CA  1 
ATOM   1515 C C   A ASN A 1 128 ? -3.60900  14.40000  17.36400 0.700 31.31868  ? 458 ASN A C   1 
ATOM   1516 C C   B ASN A 1 128 ? -3.76700  14.48100  17.35300 0.300 32.31968  ? 458 ASN A C   1 
ATOM   1517 O O   A ASN A 1 128 ? -3.94600  14.35100  16.18000 0.700 30.35726  ? 458 ASN A O   1 
ATOM   1518 O O   B ASN A 1 128 ? -4.13000  14.44500  16.17200 0.300 30.42258  ? 458 ASN A O   1 
ATOM   1519 C CB  A ASN A 1 128 ? -5.49500  15.90600  18.11500 0.700 40.98569  ? 458 ASN A CB  1 
ATOM   1520 C CB  B ASN A 1 128 ? -5.55900  16.03100  18.13600 0.300 41.13262  ? 458 ASN A CB  1 
ATOM   1521 C CG  A ASN A 1 128 ? -4.64500  17.16100  17.97100 0.700 37.58407  ? 458 ASN A CG  1 
ATOM   1522 C CG  B ASN A 1 128 ? -4.63700  17.21900  17.94900 0.300 39.12404  ? 458 ASN A CG  1 
ATOM   1523 O OD1 A ASN A 1 128 ? -3.41500  17.10900  17.92800 0.700 40.72537  ? 458 ASN A OD1 1 
ATOM   1524 O OD1 B ASN A 1 128 ? -3.61000  17.33300  18.61600 0.300 44.45097  ? 458 ASN A OD1 1 
ATOM   1525 N ND2 A ASN A 1 128 ? -5.31300  18.30400  17.89100 0.700 35.71178  ? 458 ASN A ND2 1 
ATOM   1526 N ND2 B ASN A 1 128 ? -5.00000  18.11100  17.03500 0.300 38.69715  ? 458 ASN A ND2 1 
ATOM   1527 N N   A GLY A 1 129 ? -2.34500  14.23900  17.75600 0.700 24.66663  ? 459 GLY A N   1 
ATOM   1528 N N   B GLY A 1 129 ? -2.49800  14.30300  17.71800 0.300 29.02888  ? 459 GLY A N   1 
ATOM   1529 C CA  A GLY A 1 129 ? -1.28300  13.86900  16.84400 0.700 29.42561  ? 459 GLY A CA  1 
ATOM   1530 C CA  B GLY A 1 129 ? -1.46700  13.92200  16.78000 0.300 30.08393  ? 459 GLY A CA  1 
ATOM   1531 C C   A GLY A 1 129 ? -0.47000  15.03000  16.31000 0.700 42.03552  ? 459 GLY A C   1 
ATOM   1532 C C   B GLY A 1 129 ? -0.66900  15.08400  16.23500 0.300 42.29356  ? 459 GLY A C   1 
ATOM   1533 O O   A GLY A 1 129 ? 0.56800   14.79900  15.67600 0.700 45.98436  ? 459 GLY A O   1 
ATOM   1534 O O   B GLY A 1 129 ? 0.35200   14.85800  15.57200 0.300 45.36896  ? 459 GLY A O   1 
ATOM   1535 N N   A ASN A 1 130 ? -0.90600  16.26400  16.54800 0.700 50.06862  ? 460 ASN A N   1 
ATOM   1536 N N   B ASN A 1 130 ? -1.10200  16.31400  16.49700 0.300 50.03091  ? 460 ASN A N   1 
ATOM   1537 C CA  A ASN A 1 130 ? -0.20200  17.43200  16.03800 0.700 45.44682  ? 460 ASN A CA  1 
ATOM   1538 C CA  B ASN A 1 130 ? -0.41900  17.48600  15.97500 0.300 45.42289  ? 460 ASN A CA  1 
ATOM   1539 C C   A ASN A 1 130 ? 1.14700   17.61300  16.72300 0.700 35.27297  ? 460 ASN A C   1 
ATOM   1540 C C   B ASN A 1 130 ? 0.95000   17.65700  16.62100 0.300 36.30348  ? 460 ASN A C   1 
ATOM   1541 O O   A ASN A 1 130 ? 1.33700   17.24900  17.88800 0.700 39.61252  ? 460 ASN A O   1 
ATOM   1542 O O   B ASN A 1 130 ? 1.16800   17.31000  17.78500 0.300 39.31021  ? 460 ASN A O   1 
ATOM   1543 C CB  A ASN A 1 130 ? -1.04200  18.69500  16.23500 0.700 41.02631  ? 460 ASN A CB  1 
ATOM   1544 C CB  B ASN A 1 130 ? -1.25800  18.74200  16.20500 0.300 41.66867  ? 460 ASN A CB  1 
ATOM   1545 C CG  A ASN A 1 130 ? -2.16800  18.80500  15.23600 0.700 45.09228  ? 460 ASN A CG  1 
ATOM   1546 C CG  B ASN A 1 130 ? -2.42100  18.84600  15.24500 0.300 45.92115  ? 460 ASN A CG  1 
ATOM   1547 O OD1 A ASN A 1 130 ? -2.30700  17.96200  14.35200 0.700 47.69776  ? 460 ASN A OD1 1 
ATOM   1548 O OD1 B ASN A 1 130 ? -2.59000  18.00100  14.36700 0.300 48.51182  ? 460 ASN A OD1 1 
ATOM   1549 N ND2 A ASN A 1 130 ? -2.98900  19.84300  15.37800 0.700 51.67957  ? 460 ASN A ND2 1 
ATOM   1550 N ND2 B ASN A 1 130 ? -3.23100  19.88600  15.40300 0.300 50.62424  ? 460 ASN A ND2 1 
ATOM   1551 N N   A LYS A 1 131 ? 2.09800   18.15600  15.96500 0.700 39.20102  ? 461 LYS A N   1 
ATOM   1552 N N   B LYS A 1 131 ? 1.87600   18.20300  15.84100 0.300 40.19488  ? 461 LYS A N   1 
ATOM   1553 C CA  A LYS A 1 131 ? 3.31900   18.74300  16.50800 0.700 41.72608  ? 461 LYS A CA  1 
ATOM   1554 C CA  B LYS A 1 131 ? 3.11900   18.76900  16.34600 0.300 42.60591  ? 461 LYS A CA  1 
ATOM   1555 C C   A LYS A 1 131 ? 3.17400   20.25400  16.36600 0.700 44.47370  ? 461 LYS A C   1 
ATOM   1556 C C   B LYS A 1 131 ? 2.97900   20.28200  16.23400 0.300 42.92297  ? 461 LYS A C   1 
ATOM   1557 O O   A LYS A 1 131 ? 3.10500   20.77300  15.24600 0.700 37.50433  ? 461 LYS A O   1 
ATOM   1558 O O   B LYS A 1 131 ? 2.89900   20.81900  15.12400 0.300 35.43868  ? 461 LYS A O   1 
ATOM   1559 C CB  A LYS A 1 131 ? 4.55400   18.24600  15.76300 0.700 32.23117  ? 461 LYS A CB  1 
ATOM   1560 C CB  B LYS A 1 131 ? 4.29100   18.25700  15.51300 0.300 36.49667  ? 461 LYS A CB  1 
ATOM   1561 C CG  A LYS A 1 131 ? 4.86900   16.77100  15.94100 0.700 30.56216  ? 461 LYS A CG  1 
ATOM   1562 C CG  B LYS A 1 131 ? 4.54800   16.76500  15.65900 0.300 34.76659  ? 461 LYS A CG  1 
ATOM   1563 C CD  A LYS A 1 131 ? 6.00600   16.37600  15.01000 0.700 35.89032  ? 461 LYS A CD  1 
ATOM   1564 C CD  B LYS A 1 131 ? 5.59200   16.28300  14.66100 0.300 37.13415  ? 461 LYS A CD  1 
ATOM   1565 C CE  A LYS A 1 131 ? 6.28300   14.89000  15.04600 0.700 48.96679  ? 461 LYS A CE  1 
ATOM   1566 C CE  B LYS A 1 131 ? 6.66200   15.43500  15.31200 0.300 47.16897  ? 461 LYS A CE  1 
ATOM   1567 N NZ  A LYS A 1 131 ? 7.29800   14.49500  14.02400 0.700 46.87121  ? 461 LYS A NZ  1 
ATOM   1568 N NZ  B LYS A 1 131 ? 7.58400   14.85300  14.29700 0.300 48.51370  ? 461 LYS A NZ  1 
ATOM   1569 N N   A THR A 1 132 ? 3.10400   20.96000  17.48900 0.700 39.98666  ? 462 THR A N   1 
ATOM   1570 N N   B THR A 1 132 ? 2.94900   20.97100  17.37300 0.300 40.06558  ? 462 THR A N   1 
ATOM   1571 C CA  A THR A 1 132 ? 2.91700   22.40500  17.47800 0.700 33.57664  ? 462 THR A CA  1 
ATOM   1572 C CA  B THR A 1 132 ? 2.76900   22.41700  17.39000 0.300 34.35973  ? 462 THR A CA  1 
ATOM   1573 C C   A THR A 1 132 ? 4.14100   23.07200  18.08600 0.700 28.48281  ? 462 THR A C   1 
ATOM   1574 C C   B THR A 1 132 ? 4.00500   23.08800  17.96800 0.300 29.98744  ? 462 THR A C   1 
ATOM   1575 O O   A THR A 1 132 ? 4.54800   22.73100  19.20300 0.700 30.06005  ? 462 THR A O   1 
ATOM   1576 O O   B THR A 1 132 ? 4.41900   22.77400  19.08900 0.300 30.58428  ? 462 THR A O   1 
ATOM   1577 C CB  A THR A 1 132 ? 1.64800   22.80200  18.22800 0.700 31.95545  ? 462 THR A CB  1 
ATOM   1578 C CB  B THR A 1 132 ? 1.53400   22.80500  18.20500 0.300 31.14690  ? 462 THR A CB  1 
ATOM   1579 O OG1 A THR A 1 132 ? 0.51400   22.18700  17.60000 0.700 33.18016  ? 462 THR A OG1 1 
ATOM   1580 O OG1 B THR A 1 132 ? 0.36700   22.20500  17.62900 0.300 34.57924  ? 462 THR A OG1 1 
ATOM   1581 C CG2 A THR A 1 132 ? 1.47600   24.31100  18.20400 0.700 34.84924  ? 462 THR A CG2 1 
ATOM   1582 C CG2 B THR A 1 132 ? 1.36600   24.31900  18.22200 0.300 34.67106  ? 462 THR A CG2 1 
ATOM   1583 N N   A VAL A 1 133 ? 4.74300   23.99200  17.33600 0.700 29.43052  ? 463 VAL A N   1 
ATOM   1584 N N   B VAL A 1 133 ? 4.58800   24.01100  17.20500 0.300 29.79592  ? 463 VAL A N   1 
ATOM   1585 C CA  A VAL A 1 133 ? 5.98100   24.64900  17.73800 0.700 36.68035  ? 463 VAL A CA  1 
ATOM   1586 C CA  B VAL A 1 133 ? 5.82800   24.66100  17.61100 0.300 37.14784  ? 463 VAL A CA  1 
ATOM   1587 C C   A VAL A 1 133 ? 5.63000   25.80800  18.66300 0.700 35.75587  ? 463 VAL A C   1 
ATOM   1588 C C   B VAL A 1 133 ? 5.47900   25.82000  18.53400 0.300 35.71265  ? 463 VAL A C   1 
ATOM   1589 O O   A VAL A 1 133 ? 5.59400   26.96700  18.23100 0.700 29.23426  ? 463 VAL A O   1 
ATOM   1590 O O   B VAL A 1 133 ? 5.43000   26.97600  18.09800 0.300 29.23669  ? 463 VAL A O   1 
ATOM   1591 C CB  A VAL A 1 133 ? 6.77400   25.13100  16.50800 0.700 33.00438  ? 463 VAL A CB  1 
ATOM   1592 C CB  B VAL A 1 133 ? 6.64500   25.13700  16.39500 0.300 33.36469  ? 463 VAL A CB  1 
ATOM   1593 C CG1 A VAL A 1 133 ? 8.17700   25.58800  16.90600 0.700 23.29510  ? 463 VAL A CG1 1 
ATOM   1594 C CG1 B VAL A 1 133 ? 8.03300   25.58300  16.83100 0.300 25.85488  ? 463 VAL A CG1 1 
ATOM   1595 C CG2 A VAL A 1 133 ? 6.83100   24.03900  15.44800 0.700 35.89730  ? 463 VAL A CG2 1 
ATOM   1596 C CG2 B VAL A 1 133 ? 6.74000   24.03200  15.35700 0.300 36.35180  ? 463 VAL A CG2 1 
ATOM   1597 N N   A TRP A 1 134 ? 5.37200   25.51100  19.94200 0.700 33.26946  ? 464 TRP A N   1 
ATOM   1598 N N   B TRP A 1 134 ? 5.20700   25.52200  19.80900 0.300 33.39428  ? 464 TRP A N   1 
ATOM   1599 C CA  A TRP A 1 134 ? 4.98900   26.57300  20.87100 0.700 35.90156  ? 464 TRP A CA  1 
ATOM   1600 C CA  B TRP A 1 134 ? 4.83900   26.58300  20.74300 0.300 35.63504  ? 464 TRP A CA  1 
ATOM   1601 C C   A TRP A 1 134 ? 6.06500   27.64200  20.98200 0.700 40.52899  ? 464 TRP A C   1 
ATOM   1602 C C   B TRP A 1 134 ? 5.94400   27.62100  20.87000 0.300 39.96135  ? 464 TRP A C   1 
ATOM   1603 O O   A TRP A 1 134 ? 5.74500   28.82400  21.16700 0.700 41.66551  ? 464 TRP A O   1 
ATOM   1604 O O   B TRP A 1 134 ? 5.66300   28.80600  21.08900 0.300 41.38210  ? 464 TRP A O   1 
ATOM   1605 C CB  A TRP A 1 134 ? 4.67100   25.98600  22.24700 0.700 38.50297  ? 464 TRP A CB  1 
ATOM   1606 C CB  B TRP A 1 134 ? 4.49700   25.99400  22.10900 0.300 38.48498  ? 464 TRP A CB  1 
ATOM   1607 C CG  A TRP A 1 134 ? 4.56200   27.01900  23.31100 0.700 28.12662  ? 464 TRP A CG  1 
ATOM   1608 C CG  B TRP A 1 134 ? 4.41100   27.03100  23.17200 0.300 29.10933  ? 464 TRP A CG  1 
ATOM   1609 C CD1 A TRP A 1 134 ? 5.39400   27.19900  24.37900 0.700 23.88799  ? 464 TRP A CD1 1 
ATOM   1610 C CD1 B TRP A 1 134 ? 5.24900   27.17800  24.23400 0.300 24.96265  ? 464 TRP A CD1 1 
ATOM   1611 C CD2 A TRP A 1 134 ? 3.59400   28.06900  23.37400 0.700 35.70836  ? 464 TRP A CD2 1 
ATOM   1612 C CD2 B TRP A 1 134 ? 3.46400   28.10400  23.25500 0.300 35.43825  ? 464 TRP A CD2 1 
ATOM   1613 N NE1 A TRP A 1 134 ? 4.97700   28.27500  25.12700 0.700 37.85806  ? 464 TRP A NE1 1 
ATOM   1614 N NE1 B TRP A 1 134 ? 4.87000   28.25900  24.98900 0.300 37.11209  ? 464 TRP A NE1 1 
ATOM   1615 C CE2 A TRP A 1 134 ? 3.87600   28.83100  24.52700 0.700 39.36315  ? 464 TRP A CE2 1 
ATOM   1616 C CE2 B TRP A 1 134 ? 3.77700   28.84700  24.40900 0.300 39.14951  ? 464 TRP A CE2 1 
ATOM   1617 C CE3 A TRP A 1 134 ? 2.50400   28.43000  22.57500 0.700 33.31240  ? 464 TRP A CE3 1 
ATOM   1618 C CE3 B TRP A 1 134 ? 2.37500   28.50200  22.47300 0.300 33.88732  ? 464 TRP A CE3 1 
ATOM   1619 C CZ2 A TRP A 1 134 ? 3.10800   29.93200  24.89900 0.700 35.77154  ? 464 TRP A CZ2 1 
ATOM   1620 C CZ2 B TRP A 1 134 ? 3.04400   29.96400  24.80200 0.300 35.87247  ? 464 TRP A CZ2 1 
ATOM   1621 C CZ3 A TRP A 1 134 ? 1.74600   29.52200  22.94300 0.700 29.82478  ? 464 TRP A CZ3 1 
ATOM   1622 C CZ3 B TRP A 1 134 ? 1.64700   29.61200  22.86400 0.300 31.15499  ? 464 TRP A CZ3 1 
ATOM   1623 C CH2 A TRP A 1 134 ? 2.05000   30.26300  24.09600 0.700 34.61247  ? 464 TRP A CH2 1 
ATOM   1624 C CH2 B TRP A 1 134 ? 1.98500   30.33000  24.01800 0.300 34.90449  ? 464 TRP A CH2 1 
ATOM   1625 N N   A LEU A 1 135 ? 7.33900   27.24700  20.86400 0.700 39.00334  ? 465 LEU A N   1 
ATOM   1626 N N   B LEU A 1 135 ? 7.20000   27.18800  20.74600 0.300 38.61634  ? 465 LEU A N   1 
ATOM   1627 C CA  A LEU A 1 135 ? 8.43900   28.20400  20.95600 0.700 31.02684  ? 465 LEU A CA  1 
ATOM   1628 C CA  B LEU A 1 135 ? 8.34100   28.09100  20.85300 0.300 32.07758  ? 465 LEU A CA  1 
ATOM   1629 C C   A LEU A 1 135 ? 8.24600   29.33800  19.96100 0.700 33.63933  ? 465 LEU A C   1 
ATOM   1630 C C   B LEU A 1 135 ? 8.20200   29.25500  19.87900 0.300 34.09737  ? 465 LEU A C   1 
ATOM   1631 O O   A LEU A 1 135 ? 8.45100   30.51100  20.29300 0.700 42.69986  ? 465 LEU A O   1 
ATOM   1632 O O   B LEU A 1 135 ? 8.50000   30.40600  20.22100 0.300 42.19233  ? 465 LEU A O   1 
ATOM   1633 C CB  A LEU A 1 135 ? 9.78200   27.50600  20.75800 0.700 36.09006  ? 465 LEU A CB  1 
ATOM   1634 C CB  B LEU A 1 135 ? 9.63300   27.31300  20.62400 0.300 36.58189  ? 465 LEU A CB  1 
ATOM   1635 C CG  A LEU A 1 135 ? 10.96200  28.47300  20.88600 0.700 48.09195  ? 465 LEU A CG  1 
ATOM   1636 C CG  B LEU A 1 135 ? 10.94700  28.07200  20.73900 0.300 46.04505  ? 465 LEU A CG  1 
ATOM   1637 C CD1 A LEU A 1 135 ? 11.06500  29.01800  22.28700 0.700 48.07182  ? 465 LEU A CD1 1 
ATOM   1638 C CD1 B LEU A 1 135 ? 11.16100  28.54500  22.16200 0.300 46.75002  ? 465 LEU A CD1 1 
ATOM   1639 C CD2 A LEU A 1 135 ? 12.26000  27.76800  20.54300 0.700 48.54765  ? 465 LEU A CD2 1 
ATOM   1640 C CD2 B LEU A 1 135 ? 12.04500  27.12700  20.34500 0.300 41.92527  ? 465 LEU A CD2 1 
ATOM   1641 N N   A ARG A 1 136 ? 7.82600   29.00300  18.74000 0.700 39.04776  ? 466 ARG A N   1 
ATOM   1642 N N   B ARG A 1 136 ? 7.76000   28.96600  18.65300 0.300 38.94999  ? 466 ARG A N   1 
ATOM   1643 C CA  A ARG A 1 136 ? 7.65800   30.01300  17.70200 0.700 37.56185  ? 466 ARG A CA  1 
ATOM   1644 C CA  B ARG A 1 136 ? 7.63900   29.99200  17.62300 0.300 37.46159  ? 466 ARG A CA  1 
ATOM   1645 C C   A ARG A 1 136 ? 6.53300   30.96800  18.07600 0.700 28.21576  ? 466 ARG A C   1 
ATOM   1646 C C   B ARG A 1 136 ? 6.56400   31.00400  18.00400 0.300 32.44840  ? 466 ARG A C   1 
ATOM   1647 O O   A ARG A 1 136 ? 6.70300   32.19300  18.04000 0.700 38.34763  ? 466 ARG A O   1 
ATOM   1648 O O   B ARG A 1 136 ? 6.80000   32.21700  17.97600 0.300 38.42124  ? 466 ARG A O   1 
ATOM   1649 C CB  A ARG A 1 136 ? 7.38900   29.32800  16.36100 0.700 31.42899  ? 466 ARG A CB  1 
ATOM   1650 C CB  B ARG A 1 136 ? 7.31300   29.32800  16.28500 0.300 30.88617  ? 466 ARG A CB  1 
ATOM   1651 C CG  A ARG A 1 136 ? 7.09900   30.26100  15.20000 0.700 39.22023  ? 466 ARG A CG  1 
ATOM   1652 C CG  B ARG A 1 136 ? 7.06800   30.27600  15.13200 0.300 38.59634  ? 466 ARG A CG  1 
ATOM   1653 C CD  A ARG A 1 136 ? 6.69300   29.43700  13.98300 0.700 35.73237  ? 466 ARG A CD  1 
ATOM   1654 C CD  B ARG A 1 136 ? 6.59300   29.50000  13.91400 0.300 36.92921  ? 466 ARG A CD  1 
ATOM   1655 N NE  A ARG A 1 136 ? 7.67800   28.39600  13.71900 0.700 32.69402  ? 466 ARG A NE  1 
ATOM   1656 N NE  B ARG A 1 136 ? 7.47400   28.38400  13.59400 0.300 34.26762  ? 466 ARG A NE  1 
ATOM   1657 C CZ  A ARG A 1 136 ? 7.42000   27.24000  13.12100 0.700 40.97348  ? 466 ARG A CZ  1 
ATOM   1658 C CZ  B ARG A 1 136 ? 7.08400   27.27900  12.97300 0.300 42.83567  ? 466 ARG A CZ  1 
ATOM   1659 N NH1 A ARG A 1 136 ? 6.20800   26.94900  12.66800 0.700 36.65089  ? 466 ARG A NH1 1 
ATOM   1660 N NH1 B ARG A 1 136 ? 5.83800   27.12300  12.55700 0.300 40.80763  ? 466 ARG A NH1 1 
ATOM   1661 N NH2 A ARG A 1 136 ? 8.40700   26.36100  12.95600 0.700 41.96556  ? 466 ARG A NH2 1 
ATOM   1662 N NH2 B ARG A 1 136 ? 7.96900   26.31000  12.75500 0.300 45.26297  ? 466 ARG A NH2 1 
ATOM   1663 N N   A TYR A 1 137 ? 5.36700   30.42500  18.42700 0.700 31.36232  ? 467 TYR A N   1 
ATOM   1664 N N   B TYR A 1 137 ? 5.37000   30.51900  18.35400 0.300 31.35183  ? 467 TYR A N   1 
ATOM   1665 C CA  A TYR A 1 137 ? 4.21300   31.28100  18.66500 0.700 27.98008  ? 467 TYR A CA  1 
ATOM   1666 C CA  B TYR A 1 137 ? 4.23700   31.40600  18.60200 0.300 29.31881  ? 467 TYR A CA  1 
ATOM   1667 C C   A TYR A 1 137 ? 4.43800   32.10000  19.92700 0.700 34.53097  ? 467 TYR A C   1 
ATOM   1668 C C   B TYR A 1 137 ? 4.46300   32.22100  19.86900 0.300 35.16203  ? 467 TYR A C   1 
ATOM   1669 O O   A TYR A 1 137 ? 4.09100   33.28600  19.97900 0.700 43.90692  ? 467 TYR A O   1 
ATOM   1670 O O   B TYR A 1 137 ? 4.11700   33.40700  19.92500 0.300 43.85901  ? 467 TYR A O   1 
ATOM   1671 C CB  A TYR A 1 137 ? 2.94100   30.43800  18.74900 0.700 34.58893  ? 467 TYR A CB  1 
ATOM   1672 C CB  B TYR A 1 137 ? 2.94400   30.59700  18.68000 0.300 34.78840  ? 467 TYR A CB  1 
ATOM   1673 C CG  A TYR A 1 137 ? 2.74900   29.58500  17.51400 0.700 34.97925  ? 467 TYR A CG  1 
ATOM   1674 C CG  B TYR A 1 137 ? 2.70400   29.76500  17.44200 0.300 35.52843  ? 467 TYR A CG  1 
ATOM   1675 C CD1 A TYR A 1 137 ? 2.64500   30.16300  16.25500 0.700 39.56599  ? 467 TYR A CD1 1 
ATOM   1676 C CD1 B TYR A 1 137 ? 2.59700   30.36700  16.19600 0.300 39.13286  ? 467 TYR A CD1 1 
ATOM   1677 C CD2 A TYR A 1 137 ? 2.70500   28.20300  17.60400 0.700 36.50026  ? 467 TYR A CD2 1 
ATOM   1678 C CD2 B TYR A 1 137 ? 2.60000   28.38200  17.51300 0.300 36.96263  ? 467 TYR A CD2 1 
ATOM   1679 C CE1 A TYR A 1 137 ? 2.48400   29.38800  15.12200 0.700 45.15485  ? 467 TYR A CE1 1 
ATOM   1680 C CE1 B TYR A 1 137 ? 2.38600   29.62000  15.05500 0.300 45.78576  ? 467 TYR A CE1 1 
ATOM   1681 C CE2 A TYR A 1 137 ? 2.54300   27.41800  16.47600 0.700 42.13776  ? 467 TYR A CE2 1 
ATOM   1682 C CE2 B TYR A 1 137 ? 2.38700   27.62500  16.37600 0.300 41.24976  ? 467 TYR A CE2 1 
ATOM   1683 C CZ  A TYR A 1 137 ? 2.43400   28.01600  15.23800 0.700 40.54991  ? 467 TYR A CZ  1 
ATOM   1684 C CZ  B TYR A 1 137 ? 2.28100   28.25000  15.15000 0.300 41.02978  ? 467 TYR A CZ  1 
ATOM   1685 O OH  A TYR A 1 137 ? 2.27200   27.23700  14.11300 0.700 50.79206  ? 467 TYR A OH  1 
ATOM   1686 O OH  B TYR A 1 137 ? 2.06900   27.50500  14.01300 0.300 50.87376  ? 467 TYR A OH  1 
ATOM   1687 N N   A ALA A 1 138 ? 5.02600   31.47500  20.95200 0.700 35.79907  ? 468 ALA A N   1 
ATOM   1688 N N   B ALA A 1 138 ? 5.03200   31.59000  20.89800 0.300 35.99877  ? 468 ALA A N   1 
ATOM   1689 C CA  A ALA A 1 138 ? 5.40200   32.20100  22.16100 0.700 32.06920  ? 468 ALA A CA  1 
ATOM   1690 C CA  B ALA A 1 138 ? 5.40800   32.30400  22.11500 0.300 32.02125  ? 468 ALA A CA  1 
ATOM   1691 C C   A ALA A 1 138 ? 6.37200   33.32700  21.83400 0.700 32.09170  ? 468 ALA A C   1 
ATOM   1692 C C   B ALA A 1 138 ? 6.38500   33.42700  21.79200 0.300 31.55251  ? 468 ALA A C   1 
ATOM   1693 O O   A ALA A 1 138 ? 6.21100   34.46000  22.30400 0.700 29.54448  ? 468 ALA A O   1 
ATOM   1694 O O   B ALA A 1 138 ? 6.24600   34.55000  22.28800 0.300 30.28866  ? 468 ALA A O   1 
ATOM   1695 C CB  A ALA A 1 138 ? 6.01900   31.24400  23.18000 0.700 24.95664  ? 468 ALA A CB  1 
ATOM   1696 C CB  B ALA A 1 138 ? 6.01100   31.33500  23.13200 0.300 25.36062  ? 468 ALA A CB  1 
ATOM   1697 N N   A GLU A 1 139 ? 7.39700   33.02600  21.03000 0.700 35.06987  ? 469 GLU A N   1 
ATOM   1698 N N   B GLU A 1 139 ? 7.39700   33.12800  20.97300 0.300 35.09832  ? 469 GLU A N   1 
ATOM   1699 C CA  A GLU A 1 139 ? 8.33400   34.05600  20.58600 0.700 43.97079  ? 469 GLU A CA  1 
ATOM   1700 C CA  B GLU A 1 139 ? 8.33500   34.15600  20.53500 0.300 38.74627  ? 469 GLU A CA  1 
ATOM   1701 C C   A GLU A 1 139 ? 7.60200   35.18300  19.86300 0.700 35.61832  ? 469 GLU A C   1 
ATOM   1702 C C   B GLU A 1 139 ? 7.61200   35.31200  19.85100 0.300 36.17359  ? 469 GLU A C   1 
ATOM   1703 O O   A GLU A 1 139 ? 7.90500   36.36200  20.08500 0.700 40.68872  ? 469 GLU A O   1 
ATOM   1704 O O   B GLU A 1 139 ? 7.92200   36.48100  20.10700 0.300 40.66568  ? 469 GLU A O   1 
ATOM   1705 C CB  A GLU A 1 139 ? 9.42800   33.42400  19.72300 0.700 33.30418  ? 469 GLU A CB  1 
ATOM   1706 C CB  B GLU A 1 139 ? 9.35700   33.52700  19.59100 0.300 33.97345  ? 469 GLU A CB  1 
ATOM   1707 C CG  A GLU A 1 139 ? 10.52100  34.36300  19.24200 0.700 35.17997  ? 469 GLU A CG  1 
ATOM   1708 C CG  B GLU A 1 139 ? 10.44100  34.44700  19.08900 0.300 36.37502  ? 469 GLU A CG  1 
ATOM   1709 C CD  A GLU A 1 139 ? 10.51300  34.54200  17.74300 0.700 60.38951  ? 469 GLU A CD  1 
ATOM   1710 C CD  B GLU A 1 139 ? 11.01900  33.95400  17.77900 0.300 57.72551  ? 469 GLU A CD  1 
ATOM   1711 O OE1 A GLU A 1 139 ? 9.41900   34.49200  17.14600 0.700 64.28163  ? 469 GLU A OE1 1 
ATOM   1712 O OE1 B GLU A 1 139 ? 10.49700  32.95600  17.23900 0.300 52.93398  ? 469 GLU A OE1 1 
ATOM   1713 O OE2 A GLU A 1 139 ? 11.60600  34.71500  17.15900 0.700 58.23222  ? 469 GLU A OE2 1 
ATOM   1714 O OE2 B GLU A 1 139 ? 11.98900  34.55700  17.28600 0.300 58.76423  ? 469 GLU A OE2 1 
ATOM   1715 N N   A TRP A 1 140 ? 6.65200   34.84800  18.97700 0.700 39.90745  ? 470 TRP A N   1 
ATOM   1716 N N   B TRP A 1 140 ? 6.65700   35.00700  18.96700 0.300 39.37394  ? 470 TRP A N   1 
ATOM   1717 C CA  A TRP A 1 140 ? 5.90100   35.89500  18.28300 0.700 27.07121  ? 470 TRP A CA  1 
ATOM   1718 C CA  B TRP A 1 140 ? 5.90300   36.06400  18.29400 0.300 29.48696  ? 470 TRP A CA  1 
ATOM   1719 C C   A TRP A 1 140 ? 5.18000   36.78700  19.28500 0.700 25.29588  ? 470 TRP A C   1 
ATOM   1720 C C   B TRP A 1 140 ? 5.17300   36.93900  19.30700 0.300 28.00043  ? 470 TRP A C   1 
ATOM   1721 O O   A TRP A 1 140 ? 5.13100   38.01200  19.12000 0.700 44.15037  ? 470 TRP A O   1 
ATOM   1722 O O   B TRP A 1 140 ? 5.14700   38.16800  19.17800 0.300 43.33959  ? 470 TRP A O   1 
ATOM   1723 C CB  A TRP A 1 140 ? 4.88600   35.30500  17.30100 0.700 32.34256  ? 470 TRP A CB  1 
ATOM   1724 C CB  B TRP A 1 140 ? 4.92400   35.46800  17.28100 0.300 33.45897  ? 470 TRP A CB  1 
ATOM   1725 C CG  A TRP A 1 140 ? 5.46000   34.53800  16.15400 0.700 29.35642  ? 470 TRP A CG  1 
ATOM   1726 C CG  B TRP A 1 140 ? 5.59200   34.74600  16.14800 0.300 31.22202  ? 470 TRP A CG  1 
ATOM   1727 C CD1 A TRP A 1 140 ? 6.77900   34.41100  15.82000 0.700 33.33552  ? 470 TRP A CD1 1 
ATOM   1728 C CD1 B TRP A 1 140 ? 6.93000   34.69100  15.88600 0.300 36.00482  ? 470 TRP A CD1 1 
ATOM   1729 C CD2 A TRP A 1 140 ? 4.72100   33.83900  15.14500 0.700 35.58954  ? 470 TRP A CD2 1 
ATOM   1730 C CD2 B TRP A 1 140 ? 4.94900   34.00400  15.10400 0.300 35.18815  ? 470 TRP A CD2 1 
ATOM   1731 N NE1 A TRP A 1 140 ? 6.90800   33.64800  14.68200 0.700 36.75810  ? 470 TRP A NE1 1 
ATOM   1732 N NE1 B TRP A 1 140 ? 7.16100   33.94700  14.75400 0.300 40.57635  ? 470 TRP A NE1 1 
ATOM   1733 C CE2 A TRP A 1 140 ? 5.65900   33.28600  14.24700 0.700 36.46492  ? 470 TRP A CE2 1 
ATOM   1734 C CE2 B TRP A 1 140 ? 5.96100   33.51500  14.25500 0.300 39.10367  ? 470 TRP A CE2 1 
ATOM   1735 C CE3 A TRP A 1 140 ? 3.35800   33.61500  14.92100 0.700 41.72571  ? 470 TRP A CE3 1 
ATOM   1736 C CE3 B TRP A 1 140 ? 3.61700   33.69800  14.81100 0.300 41.16269  ? 470 TRP A CE3 1 
ATOM   1737 C CZ2 A TRP A 1 140 ? 5.27700   32.52000  13.14300 0.700 35.83753  ? 470 TRP A CZ2 1 
ATOM   1738 C CZ2 B TRP A 1 140 ? 5.68200   32.73900  13.13300 0.300 40.77207  ? 470 TRP A CZ2 1 
ATOM   1739 C CZ3 A TRP A 1 140 ? 2.98000   32.85300  13.82300 0.700 33.72455  ? 470 TRP A CZ3 1 
ATOM   1740 C CZ3 B TRP A 1 140 ? 3.34200   32.92800  13.69500 0.300 39.09154  ? 470 TRP A CZ3 1 
ATOM   1741 C CH2 A TRP A 1 140 ? 3.93700   32.31700  12.94900 0.700 40.72298  ? 470 TRP A CH2 1 
ATOM   1742 C CH2 B TRP A 1 140 ? 4.37000   32.45700  12.87000 0.300 43.80598  ? 470 TRP A CH2 1 
ATOM   1743 N N   A LEU A 1 141 ? 4.59300   36.18000  20.31900 0.700 35.40526  ? 471 LEU A N   1 
ATOM   1744 N N   B LEU A 1 141 ? 4.58200   36.31600  20.32800 0.300 35.84249  ? 471 LEU A N   1 
ATOM   1745 C CA  A LEU A 1 141 ? 3.86500   36.93500  21.33200 0.700 38.26229  ? 471 LEU A CA  1 
ATOM   1746 C CA  B LEU A 1 141 ? 3.84200   37.05000  21.35000 0.300 38.53429  ? 471 LEU A CA  1 
ATOM   1747 C C   A LEU A 1 141 ? 4.79300   37.87500  22.09200 0.700 33.32876  ? 471 LEU A C   1 
ATOM   1748 C C   B LEU A 1 141 ? 4.75200   37.98900  22.12800 0.300 33.57901  ? 471 LEU A C   1 
ATOM   1749 O O   A LEU A 1 141 ? 4.37400   38.95400  22.52300 0.700 29.75058  ? 471 LEU A O   1 
ATOM   1750 O O   B LEU A 1 141 ? 4.31300   39.05200  22.58200 0.300 31.41201  ? 471 LEU A O   1 
ATOM   1751 C CB  A LEU A 1 141 ? 3.18000   35.96600  22.29500 0.700 32.15577  ? 471 LEU A CB  1 
ATOM   1752 C CB  B LEU A 1 141 ? 3.15400   36.06800  22.29700 0.300 30.87009  ? 471 LEU A CB  1 
ATOM   1753 C CG  A LEU A 1 141 ? 1.91100   35.29400  21.76300 0.700 35.38717  ? 471 LEU A CG  1 
ATOM   1754 C CG  B LEU A 1 141 ? 1.89000   35.39700  21.75900 0.300 34.36621  ? 471 LEU A CG  1 
ATOM   1755 C CD1 A LEU A 1 141 ? 1.53400   34.11000  22.63500 0.700 38.36795  ? 471 LEU A CD1 1 
ATOM   1756 C CD1 B LEU A 1 141 ? 1.51700   34.20400  22.62100 0.300 38.55650  ? 471 LEU A CD1 1 
ATOM   1757 C CD2 A LEU A 1 141 ? 0.75800   36.28500  21.67600 0.700 35.83911  ? 471 LEU A CD2 1 
ATOM   1758 C CD2 B LEU A 1 141 ? 0.74300   36.39400  21.68900 0.300 35.25385  ? 471 LEU A CD2 1 
ATOM   1759 N N   A LEU A 1 142 ? 6.05800   37.48600  22.25700 0.700 36.13654  ? 472 LEU A N   1 
ATOM   1760 N N   B LEU A 1 142 ? 6.02100   37.61700  22.28400 0.300 36.19737  ? 472 LEU A N   1 
ATOM   1761 C CA  A LEU A 1 142 ? 7.02100   38.31600  22.97100 0.700 31.16540  ? 472 LEU A CA  1 
ATOM   1762 C CA  B LEU A 1 142 ? 6.98600   38.43000  23.01500 0.300 31.60256  ? 472 LEU A CA  1 
ATOM   1763 C C   A LEU A 1 142 ? 7.52600   39.46000  22.09800 0.700 36.76685  ? 472 LEU A C   1 
ATOM   1764 C C   B LEU A 1 142 ? 7.47000   39.61000  22.18100 0.300 36.92022  ? 472 LEU A C   1 
ATOM   1765 O O   A LEU A 1 142 ? 7.73100   40.57600  22.59000 0.700 39.75111  ? 472 LEU A O   1 
ATOM   1766 O O   B LEU A 1 142 ? 7.67100   40.70700  22.71300 0.300 38.49567  ? 472 LEU A O   1 
ATOM   1767 C CB  A LEU A 1 142 ? 8.18500   37.46200  23.47100 0.700 39.09075  ? 472 LEU A CB  1 
ATOM   1768 C CB  B LEU A 1 142 ? 8.16800   37.56600  23.45400 0.300 38.40654  ? 472 LEU A CB  1 
ATOM   1769 C CG  A LEU A 1 142 ? 7.83600   36.50800  24.61500 0.700 35.06208  ? 472 LEU A CG  1 
ATOM   1770 C CG  B LEU A 1 142 ? 7.87800   36.54700  24.55800 0.300 34.80124  ? 472 LEU A CG  1 
ATOM   1771 C CD1 A LEU A 1 142 ? 9.02500   35.63600  24.97300 0.700 27.04650  ? 472 LEU A CD1 1 
ATOM   1772 C CD1 B LEU A 1 142 ? 9.10200   35.68700  24.82600 0.300 28.33814  ? 472 LEU A CD1 1 
ATOM   1773 C CD2 A LEU A 1 142 ? 7.34200   37.28300  25.82800 0.700 32.19914  ? 472 LEU A CD2 1 
ATOM   1774 C CD2 B LEU A 1 142 ? 7.41300   37.24300  25.82900 0.300 40.33545  ? 472 LEU A CD2 1 
ATOM   1775 N N   A THR A 1 143 ? 7.73800   39.20500  20.80900 0.700 38.55889  ? 473 THR A N   1 
ATOM   1776 N N   B THR A 1 143 ? 7.66100   39.40800  20.87900 0.300 38.24910  ? 473 THR A N   1 
ATOM   1777 C CA  A THR A 1 143 ? 8.49000   40.10500  19.94300 0.700 26.16403  ? 473 THR A CA  1 
ATOM   1778 C CA  B THR A 1 143 ? 8.38900   40.32800  20.01400 0.300 27.53157  ? 473 THR A CA  1 
ATOM   1779 C C   A THR A 1 143 ? 7.59100   40.95200  19.05000 0.700 26.34214  ? 473 THR A C   1 
ATOM   1780 C C   B THR A 1 143 ? 7.46700   41.19800  19.17300 0.300 28.56991  ? 473 THR A C   1 
ATOM   1781 O O   A THR A 1 143 ? 7.85900   42.14600  18.88300 0.700 35.13828  ? 473 THR A O   1 
ATOM   1782 O O   B THR A 1 143 ? 7.72400   42.39700  19.03000 0.300 35.69628  ? 473 THR A O   1 
ATOM   1783 C CB  A THR A 1 143 ? 9.47700   39.31200  19.08000 0.700 28.89054  ? 473 THR A CB  1 
ATOM   1784 C CB  B THR A 1 143 ? 9.33400   39.55800  19.08500 0.300 29.13427  ? 473 THR A CB  1 
ATOM   1785 O OG1 A THR A 1 143 ? 8.75500   38.43300  18.20700 0.700 36.75099  ? 473 THR A OG1 1 
ATOM   1786 O OG1 B THR A 1 143 ? 8.56900   38.72000  18.21000 0.300 36.55843  ? 473 THR A OG1 1 
ATOM   1787 C CG2 A THR A 1 143 ? 10.40600  38.49400  19.96600 0.700 35.60156  ? 473 THR A CG2 1 
ATOM   1788 C CG2 B THR A 1 143 ? 10.29700  38.70400  19.89100 0.300 35.28516  ? 473 THR A CG2 1 
ATOM   1789 N N   A CYS A 1 144 ? 6.55000   40.36900  18.44500 0.700 26.31565  ? 474 CYS A N   1 
ATOM   1790 N N   B CYS A 1 144 ? 6.40700   40.62000  18.60300 0.300 28.35711  ? 474 CYS A N   1 
ATOM   1791 C CA  A CYS A 1 144 ? 5.76200   41.12100  17.46600 0.700 30.64642  ? 474 CYS A CA  1 
ATOM   1792 C CA  B CYS A 1 144 ? 5.57600   41.35400  17.64900 0.300 34.22957  ? 474 CYS A CA  1 
ATOM   1793 C C   A CYS A 1 144 ? 5.13800   42.37800  18.05700 0.700 34.69379  ? 474 CYS A C   1 
ATOM   1794 C C   B CYS A 1 144 ? 4.96900   42.62000  18.24500 0.300 35.52917  ? 474 CYS A C   1 
ATOM   1795 O O   A CYS A 1 144 ? 5.22100   43.43700  17.41000 0.700 39.04686  ? 474 CYS A O   1 
ATOM   1796 O O   B CYS A 1 144 ? 5.02300   43.66900  17.57800 0.300 37.47429  ? 474 CYS A O   1 
ATOM   1797 C CB  A CYS A 1 144 ? 4.69500   40.22600  16.83100 0.700 36.56759  ? 474 CYS A CB  1 
ATOM   1798 C CB  B CYS A 1 144 ? 4.47900   40.42900  17.11400 0.300 39.11209  ? 474 CYS A CB  1 
ATOM   1799 S SG  A CYS A 1 144 ? 5.38400   38.87200  15.90400 0.700 42.10250  ? 474 CYS A SG  1 
ATOM   1800 S SG  B CYS A 1 144 ? 5.07800   39.00500  16.20000 0.300 42.64447  ? 474 CYS A SG  1 
ATOM   1801 N N   A PRO A 1 145 ? 4.49800   42.35200  19.23300 0.700 35.89265  ? 475 PRO A N   1 
ATOM   1802 N N   B PRO A 1 145 ? 4.36900   42.61000  19.44500 0.300 36.35177  ? 475 PRO A N   1 
ATOM   1803 C CA  A PRO A 1 145 ? 3.96100   43.61500  19.76500 0.700 36.30409  ? 475 PRO A CA  1 
ATOM   1804 C CA  B PRO A 1 145 ? 3.84300   43.87600  19.98700 0.300 37.99832  ? 475 PRO A CA  1 
ATOM   1805 C C   A PRO A 1 145 ? 5.03900   44.66900  19.93100 0.700 33.80636  ? 475 PRO A C   1 
ATOM   1806 C C   B PRO A 1 145 ? 4.91700   44.93800  20.12300 0.300 35.13601  ? 475 PRO A C   1 
ATOM   1807 O O   A PRO A 1 145 ? 4.77200   45.85600  19.70400 0.700 41.89762  ? 475 PRO A O   1 
ATOM   1808 O O   B PRO A 1 145 ? 4.63300   46.13000  19.95100 0.300 42.32581  ? 475 PRO A O   1 
ATOM   1809 C CB  A PRO A 1 145 ? 3.32900   43.21300  21.10800 0.700 41.11288  ? 475 PRO A CB  1 
ATOM   1810 C CB  B PRO A 1 145 ? 3.26400   43.47500  21.35100 0.300 41.77106  ? 475 PRO A CB  1 
ATOM   1811 C CG  A PRO A 1 145 ? 3.10700   41.74300  21.02100 0.700 23.22481  ? 475 PRO A CG  1 
ATOM   1812 C CG  B PRO A 1 145 ? 3.05400   42.01700  21.28400 0.300 27.83759  ? 475 PRO A CG  1 
ATOM   1813 C CD  A PRO A 1 145 ? 4.13600   41.19500  20.07700 0.700 32.72405  ? 475 PRO A CD  1 
ATOM   1814 C CD  B PRO A 1 145 ? 4.04600   41.46300  20.31500 0.300 33.60798  ? 475 PRO A CD  1 
ATOM   1815 N N   A VAL A 1 146 ? 6.26800   44.26200  20.26100 0.700 36.48684  ? 476 VAL A N   1 
ATOM   1816 N N   B VAL A 1 146 ? 6.15000   44.52900  20.42900 0.300 36.06276  ? 476 VAL A N   1 
ATOM   1817 C CA  A VAL A 1 146 ? 7.33600   45.23300  20.48300 0.700 34.48139  ? 476 VAL A CA  1 
ATOM   1818 C CA  B VAL A 1 146 ? 7.24000   45.47800  20.62600 0.300 34.54537  ? 476 VAL A CA  1 
ATOM   1819 C C   A VAL A 1 146 ? 7.77100   45.84200  19.15700 0.700 30.41435  ? 476 VAL A C   1 
ATOM   1820 C C   B VAL A 1 146 ? 7.67000   46.06700  19.28800 0.300 32.21467  ? 476 VAL A C   1 
ATOM   1821 O O   A VAL A 1 146 ? 8.04700   47.04600  19.07400 0.700 43.96673  ? 476 VAL A O   1 
ATOM   1822 O O   B VAL A 1 146 ? 7.97400   47.26200  19.18900 0.300 44.55258  ? 476 VAL A O   1 
ATOM   1823 C CB  A VAL A 1 146 ? 8.51700   44.58000  21.22400 0.700 31.25305  ? 476 VAL A CB  1 
ATOM   1824 C CB  B VAL A 1 146 ? 8.41200   44.79800  21.35900 0.300 32.24800  ? 476 VAL A CB  1 
ATOM   1825 C CG1 A VAL A 1 146 ? 9.67900   45.55600  21.33200 0.700 31.98723  ? 476 VAL A CG1 1 
ATOM   1826 C CG1 B VAL A 1 146 ? 9.60500   45.73500  21.45100 0.300 32.75002  ? 476 VAL A CG1 1 
ATOM   1827 C CG2 A VAL A 1 146 ? 8.08000   44.11700  22.60300 0.700 28.41245  ? 476 VAL A CG2 1 
ATOM   1828 C CG2 B VAL A 1 146 ? 7.97700   44.35000  22.74600 0.300 30.21182  ? 476 VAL A CG2 1 
ATOM   1829 N N   A ILE A 1 147 ? 7.84200   45.02200  18.10300 0.700 39.57676  ? 477 ILE A N   1 
ATOM   1830 N N   B ILE A 1 147 ? 7.70400   45.23700  18.24100 0.300 38.98584  ? 477 ILE A N   1 
ATOM   1831 C CA  A ILE A 1 147 ? 8.08300   45.54800  16.76100 0.700 39.31327  ? 477 ILE A CA  1 
ATOM   1832 C CA  B ILE A 1 147 ? 7.94700   45.74000  16.89100 0.300 39.34380  ? 477 ILE A CA  1 
ATOM   1833 C C   A ILE A 1 147 ? 7.01300   46.57000  16.40000 0.700 42.59504  ? 477 ILE A C   1 
ATOM   1834 C C   B ILE A 1 147 ? 6.91000   46.79400  16.52500 0.300 41.83784  ? 477 ILE A C   1 
ATOM   1835 O O   A ILE A 1 147 ? 7.30700   47.62800  15.82600 0.700 42.77749  ? 477 ILE A O   1 
ATOM   1836 O O   B ILE A 1 147 ? 7.24100   47.83800  15.94900 0.300 42.57932  ? 477 ILE A O   1 
ATOM   1837 C CB  A ILE A 1 147 ? 8.14100   44.40700  15.72900 0.700 32.30472  ? 477 ILE A CB  1 
ATOM   1838 C CB  B ILE A 1 147 ? 7.95100   44.57400  15.88200 0.300 33.62088  ? 477 ILE A CB  1 
ATOM   1839 C CG1 A ILE A 1 147 ? 9.48100   43.67300  15.80600 0.700 32.87044  ? 477 ILE A CG1 1 
ATOM   1840 C CG1 B ILE A 1 147 ? 9.26600   43.79600  15.96000 0.300 33.79580  ? 477 ILE A CG1 1 
ATOM   1841 C CG2 A ILE A 1 147 ? 7.91300   44.94800  14.32800 0.700 37.24317  ? 477 ILE A CG2 1 
ATOM   1842 C CG2 B ILE A 1 147 ? 7.71200   45.07900  14.46500 0.300 37.09816  ? 477 ILE A CG2 1 
ATOM   1843 C CD1 A ILE A 1 147 ? 9.42300   42.25500  15.27500 0.700 35.28606  ? 477 ILE A CD1 1 
ATOM   1844 C CD1 B ILE A 1 147 ? 9.15900   42.36900  15.46400 0.300 38.23405  ? 477 ILE A CD1 1 
ATOM   1845 N N   A LEU A 1 148 ? 5.75300   46.27500  16.73600 0.700 41.09798  ? 478 LEU A N   1 
ATOM   1846 N N   B LEU A 1 148 ? 5.64400   46.54900  16.86900 0.300 39.76405  ? 478 LEU A N   1 
ATOM   1847 C CA  A LEU A 1 148 ? 4.67800   47.19100  16.37700 0.700 39.02947  ? 478 LEU A CA  1 
ATOM   1848 C CA  B LEU A 1 148 ? 4.59200   47.49400  16.51300 0.300 39.45571  ? 478 LEU A CA  1 
ATOM   1849 C C   A LEU A 1 148 ? 4.73900   48.45600  17.22100 0.700 36.89852  ? 478 LEU A C   1 
ATOM   1850 C C   B LEU A 1 148 ? 4.68500   48.76300  17.34900 0.300 38.95357  ? 478 LEU A C   1 
ATOM   1851 O O   A LEU A 1 148 ? 4.40400   49.54300  16.73300 0.700 40.50149  ? 478 LEU A O   1 
ATOM   1852 O O   B LEU A 1 148 ? 4.33700   49.84700  16.86600 0.300 41.15140  ? 478 LEU A O   1 
ATOM   1853 C CB  A LEU A 1 148 ? 3.32800   46.49800  16.53400 0.700 41.60928  ? 478 LEU A CB  1 
ATOM   1854 C CB  B LEU A 1 148 ? 3.22000   46.84400  16.66600 0.300 43.41438  ? 478 LEU A CB  1 
ATOM   1855 C CG  A LEU A 1 148 ? 3.05700   45.41100  15.49300 0.700 36.89875  ? 478 LEU A CG  1 
ATOM   1856 C CG  B LEU A 1 148 ? 2.93000   45.77400  15.61400 0.300 41.04955  ? 478 LEU A CG  1 
ATOM   1857 C CD1 A LEU A 1 148 ? 1.67400   44.81800  15.69200 0.700 48.40755  ? 478 LEU A CD1 1 
ATOM   1858 C CD1 B LEU A 1 148 ? 1.53500   45.22300  15.80000 0.300 47.08697  ? 478 LEU A CD1 1 
ATOM   1859 C CD2 A LEU A 1 148 ? 3.22100   45.94800  14.07800 0.700 36.72933  ? 478 LEU A CD2 1 
ATOM   1860 C CD2 B LEU A 1 148 ? 3.11500   46.32800  14.20900 0.300 42.25444  ? 478 LEU A CD2 1 
ATOM   1861 N N   A ILE A 1 149 ? 5.19200   48.34200  18.47200 0.700 44.00108  ? 479 ILE A N   1 
ATOM   1862 N N   B ILE A 1 149 ? 5.14100   48.64800  18.59800 0.300 44.39667  ? 479 ILE A N   1 
ATOM   1863 C CA  A ILE A 1 149 ? 5.41000   49.53300  19.28700 0.700 38.67184  ? 479 ILE A CA  1 
ATOM   1864 C CA  B ILE A 1 149 ? 5.38500   49.83800  19.41000 0.300 38.62076  ? 479 ILE A CA  1 
ATOM   1865 C C   A ILE A 1 149 ? 6.50800   50.37900  18.65500 0.700 36.38155  ? 479 ILE A C   1 
ATOM   1866 C C   B ILE A 1 149 ? 6.49100   50.66800  18.77500 0.300 38.35334  ? 479 ILE A C   1 
ATOM   1867 O O   A ILE A 1 149 ? 6.39100   51.60600  18.54700 0.700 49.21705  ? 479 ILE A O   1 
ATOM   1868 O O   B ILE A 1 149 ? 6.38800   51.89600  18.66500 0.300 49.57377  ? 479 ILE A O   1 
ATOM   1869 C CB  A ILE A 1 149 ? 5.74000   49.14500  20.73800 0.700 30.90934  ? 479 ILE A CB  1 
ATOM   1870 C CB  B ILE A 1 149 ? 5.72200   49.44500  20.85900 0.300 32.71095  ? 479 ILE A CB  1 
ATOM   1871 C CG1 A ILE A 1 149 ? 4.50400   48.54800  21.41400 0.700 34.81329  ? 479 ILE A CG1 1 
ATOM   1872 C CG1 B ILE A 1 149 ? 4.48500   48.87000  21.55100 0.300 36.11706  ? 479 ILE A CG1 1 
ATOM   1873 C CG2 A ILE A 1 149 ? 6.22200   50.35200  21.51200 0.700 39.85201  ? 479 ILE A CG2 1 
ATOM   1874 C CG2 B ILE A 1 149 ? 6.26100   50.64000  21.63000 0.300 42.67073  ? 479 ILE A CG2 1 
ATOM   1875 C CD1 A ILE A 1 149 ? 4.81400   47.77700  22.68300 0.700 36.12031  ? 479 ILE A CD1 1 
ATOM   1876 C CD1 B ILE A 1 149 ? 4.79200   48.10000  22.81200 0.300 39.38166  ? 479 ILE A CD1 1 
ATOM   1877 N N   A HIS A 1 150 ? 7.60400   49.72700  18.24900 0.700 35.52491  ? 480 HIS A N   1 
ATOM   1878 N N   B HIS A 1 150 ? 7.57800   50.00600  18.36700 0.300 36.08318  ? 480 HIS A N   1 
ATOM   1879 C CA  A HIS A 1 150 ? 8.66700   50.39800  17.50600 0.700 37.73688  ? 480 HIS A CA  1 
ATOM   1880 C CA  B HIS A 1 150 ? 8.63500   50.68200  17.62300 0.300 39.59654  ? 480 HIS A CA  1 
ATOM   1881 C C   A HIS A 1 150 ? 8.08800   51.08800  16.27800 0.700 36.53539  ? 480 HIS A C   1 
ATOM   1882 C C   B HIS A 1 150 ? 8.04800   51.37700  16.40000 0.300 38.64244  ? 480 HIS A C   1 
ATOM   1883 O O   A HIS A 1 150 ? 8.36000   52.26700  16.02200 0.700 45.00131  ? 480 HIS A O   1 
ATOM   1884 O O   B HIS A 1 150 ? 8.32600   52.55300  16.14300 0.300 44.84755  ? 480 HIS A O   1 
ATOM   1885 C CB  A HIS A 1 150 ? 9.74100   49.38000  17.10500 0.700 39.68552  ? 480 HIS A CB  1 
ATOM   1886 C CB  B HIS A 1 150 ? 9.71200   49.67100  17.22100 0.300 40.21951  ? 480 HIS A CB  1 
ATOM   1887 C CG  A HIS A 1 150 ? 10.96900  49.98400  16.49400 0.700 36.10526  ? 480 HIS A CG  1 
ATOM   1888 C CG  B HIS A 1 150 ? 10.93400  50.28500  16.60900 0.300 38.68758  ? 480 HIS A CG  1 
ATOM   1889 N ND1 A HIS A 1 150 ? 11.06500  51.31800  16.15700 0.700 40.38100  ? 480 HIS A ND1 1 
ATOM   1890 N ND1 B HIS A 1 150 ? 11.05200  51.63600  16.36300 0.300 46.41756  ? 480 HIS A ND1 1 
ATOM   1891 C CD2 A HIS A 1 150 ? 12.16200  49.42900  16.16800 0.700 38.65702  ? 480 HIS A CD2 1 
ATOM   1892 C CD2 B HIS A 1 150 ? 12.09100  49.72400  16.18300 0.300 40.84537  ? 480 HIS A CD2 1 
ATOM   1893 C CE1 A HIS A 1 150 ? 12.26000  51.55700  15.64500 0.700 51.90957  ? 480 HIS A CE1 1 
ATOM   1894 C CE1 B HIS A 1 150 ? 12.22900  51.88100  15.81500 0.300 52.78661  ? 480 HIS A CE1 1 
ATOM   1895 N NE2 A HIS A 1 150 ? 12.94500  50.42700  15.64000 0.700 42.12261  ? 480 HIS A NE2 1 
ATOM   1896 N NE2 B HIS A 1 150 ? 12.88000  50.73800  15.69600 0.300 46.64429  ? 480 HIS A NE2 1 
ATOM   1897 N N   A LEU A 1 151 ? 7.28900   50.35000  15.50100 0.700 41.81395  ? 481 LEU A N   1 
ATOM   1898 N N   B LEU A 1 151 ? 7.24700   50.64200  15.62100 0.300 42.13887  ? 481 LEU A N   1 
ATOM   1899 C CA  A LEU A 1 151 ? 6.70800   50.89800  14.27900 0.700 42.87197  ? 481 LEU A CA  1 
ATOM   1900 C CA  B LEU A 1 151 ? 6.65600   51.19600  14.40400 0.300 43.33590  ? 481 LEU A CA  1 
ATOM   1901 C C   A LEU A 1 151 ? 5.91000   52.16100  14.57300 0.700 46.08967  ? 481 LEU A C   1 
ATOM   1902 C C   B LEU A 1 151 ? 5.84400   52.45000  14.70500 0.300 46.28013  ? 481 LEU A C   1 
ATOM   1903 O O   A LEU A 1 151 ? 5.95800   53.13100  13.80600 0.700 46.95970  ? 481 LEU A O   1 
ATOM   1904 O O   B LEU A 1 151 ? 5.86300   53.41400  13.93100 0.300 47.38423  ? 481 LEU A O   1 
ATOM   1905 C CB  A LEU A 1 151 ? 5.82000   49.84400  13.61700 0.700 39.37281  ? 481 LEU A CB  1 
ATOM   1906 C CB  B LEU A 1 151 ? 5.78200   50.14000  13.72700 0.300 41.38204  ? 481 LEU A CB  1 
ATOM   1907 C CG  A LEU A 1 151 ? 4.97100   50.29900  12.43000 0.700 43.65800  ? 481 LEU A CG  1 
ATOM   1908 C CG  B LEU A 1 151 ? 4.92800   50.58900  12.54100 0.300 46.11501  ? 481 LEU A CG  1 
ATOM   1909 C CD1 A LEU A 1 151 ? 5.84000   50.85800  11.31800 0.700 49.92237  ? 481 LEU A CD1 1 
ATOM   1910 C CD1 B LEU A 1 151 ? 5.79700   51.16200  11.44000 0.300 48.68132  ? 481 LEU A CD1 1 
ATOM   1911 C CD2 A LEU A 1 151 ? 4.10500   49.15200  11.92700 0.700 45.58145  ? 481 LEU A CD2 1 
ATOM   1912 C CD2 B LEU A 1 151 ? 4.08500   49.43400  12.01700 0.300 46.90781  ? 481 LEU A CD2 1 
ATOM   1913 N N   A SER A 1 152 ? 5.19200   52.17600  15.69700 0.700 42.98167  ? 482 SER A N   1 
ATOM   1914 N N   B SER A 1 152 ? 5.12300   52.45300  15.82800 0.300 44.03428  ? 482 SER A N   1 
ATOM   1915 C CA  A SER A 1 152 ? 4.37100   53.31600  16.08100 0.700 43.02160  ? 482 SER A CA  1 
ATOM   1916 C CA  B SER A 1 152 ? 4.28700   53.58300  16.21200 0.300 43.48404  ? 482 SER A CA  1 
ATOM   1917 C C   A SER A 1 152 ? 5.19800   54.52300  16.48900 0.700 37.42965  ? 482 SER A C   1 
ATOM   1918 C C   B SER A 1 152 ? 5.09900   54.80300  16.62900 0.300 41.16170  ? 482 SER A C   1 
ATOM   1919 O O   A SER A 1 152 ? 4.62800   55.59900  16.69600 0.700 55.42362  ? 482 SER A O   1 
ATOM   1920 O O   B SER A 1 152 ? 4.51900   55.87800  16.81100 0.300 56.93882  ? 482 SER A O   1 
ATOM   1921 C CB  A SER A 1 152 ? 3.43100   52.92600  17.21800 0.700 42.08107  ? 482 SER A CB  1 
ATOM   1922 C CB  B SER A 1 152 ? 3.34400   53.17300  17.34300 0.300 43.30596  ? 482 SER A CB  1 
ATOM   1923 O OG  A SER A 1 152 ? 2.66900   51.78400  16.86400 0.700 44.23464  ? 482 SER A OG  1 
ATOM   1924 O OG  B SER A 1 152 ? 2.59700   52.02400  16.98100 0.300 44.51138  ? 482 SER A OG  1 
ATOM   1925 N N   A ASN A 1 153 ? 6.51400   54.36800  16.63100 0.700 34.92621  ? 483 ASN A N   1 
ATOM   1926 N N   B ASN A 1 153 ? 6.41500   54.66100  16.78300 0.300 38.27166  ? 483 ASN A N   1 
ATOM   1927 C CA  A ASN A 1 153 ? 7.40300   55.47600  16.95800 0.700 42.15569  ? 483 ASN A CA  1 
ATOM   1928 C CA  B ASN A 1 153 ? 7.30600   55.76600  17.11600 0.300 44.28957  ? 483 ASN A CA  1 
ATOM   1929 C C   A ASN A 1 153 ? 8.72400   55.28300  16.20700 0.700 43.19589  ? 483 ASN A C   1 
ATOM   1930 C C   B ASN A 1 153 ? 8.62900   55.56400  16.37500 0.300 44.20978  ? 483 ASN A C   1 
ATOM   1931 O O   A ASN A 1 153 ? 9.80000   55.15200  16.78600 0.700 44.71290  ? 483 ASN A O   1 
ATOM   1932 O O   B ASN A 1 153 ? 9.69600   55.41500  16.96300 0.300 46.77744  ? 483 ASN A O   1 
ATOM   1933 C CB  A ASN A 1 153 ? 7.60600   55.57200  18.47100 0.700 45.79025  ? 483 ASN A CB  1 
ATOM   1934 C CB  B ASN A 1 153 ? 7.51200   55.86200  18.62600 0.300 46.60819  ? 483 ASN A CB  1 
ATOM   1935 C CG  A ASN A 1 153 ? 8.31900   56.84200  18.88700 0.700 47.58538  ? 483 ASN A CG  1 
ATOM   1936 C CG  B ASN A 1 153 ? 8.23100   57.12900  19.03600 0.300 49.79173  ? 483 ASN A CG  1 
ATOM   1937 O OD1 A ASN A 1 153 ? 8.30300   57.84000  18.16800 0.700 50.49617  ? 483 ASN A OD1 1 
ATOM   1938 O OD1 B ASN A 1 153 ? 8.21600   58.12500  18.31500 0.300 52.68848  ? 483 ASN A OD1 1 
ATOM   1939 N ND2 A ASN A 1 153 ? 8.94700   56.81200  20.05800 0.700 47.38793  ? 483 ASN A ND2 1 
ATOM   1940 N ND2 B ASN A 1 153 ? 8.86400   57.10000  20.20300 0.300 51.45246  ? 483 ASN A ND2 1 
ATOM   1941 N N   A LEU A 1 154 ? 8.62500   55.27000  14.87300 0.700 37.57351  ? 484 LEU A N   1 
ATOM   1942 N N   B LEU A 1 154 ? 8.54200   55.54300  15.04100 0.300 39.27922  ? 484 LEU A N   1 
ATOM   1943 C CA  A LEU A 1 154 ? 9.79100   55.01300  14.03000 0.700 38.37943  ? 484 LEU A CA  1 
ATOM   1944 C CA  B LEU A 1 154 ? 9.71500   55.27300  14.21600 0.300 40.77247  ? 484 LEU A CA  1 
ATOM   1945 C C   A LEU A 1 154 ? 10.86300  56.07800  14.23600 0.700 46.51442  ? 484 LEU A C   1 
ATOM   1946 C C   B LEU A 1 154 ? 10.79600  56.32800  14.41000 0.300 47.48099  ? 484 LEU A C   1 
ATOM   1947 O O   A LEU A 1 154 ? 12.06000  55.76700  14.26600 0.700 53.84715  ? 484 LEU A O   1 
ATOM   1948 O O   B LEU A 1 154 ? 11.98800  56.00500  14.45600 0.300 53.64291  ? 484 LEU A O   1 
ATOM   1949 C CB  A LEU A 1 154 ? 9.36300   54.94000  12.56500 0.700 43.57392  ? 484 LEU A CB  1 
ATOM   1950 C CB  B LEU A 1 154 ? 9.31300   55.18100  12.74700 0.300 44.55778  ? 484 LEU A CB  1 
ATOM   1951 C CG  A LEU A 1 154 ? 8.79800   53.59300  12.11000 0.700 45.79498  ? 484 LEU A CG  1 
ATOM   1952 C CG  B LEU A 1 154 ? 8.75600   53.80500  12.38600 0.300 46.24611  ? 484 LEU A CG  1 
ATOM   1953 C CD1 A LEU A 1 154 ? 8.32100   53.67600  10.67500 0.700 45.79842  ? 484 LEU A CD1 1 
ATOM   1954 C CD1 B LEU A 1 154 ? 8.27900   53.75600  10.93800 0.300 45.83121  ? 484 LEU A CD1 1 
ATOM   1955 C CD2 A LEU A 1 154 ? 9.85200   52.50500  12.25800 0.700 47.83998  ? 484 LEU A CD2 1 
ATOM   1956 C CD2 B LEU A 1 154 ? 9.75700   52.70800  12.70700 0.300 47.89144  ? 484 LEU A CD2 1 
ATOM   1957 N N   A THR A 1 155 ? 10.45400  57.34100  14.37100 0.700 50.38572  ? 485 THR A N   1 
ATOM   1958 N N   B THR A 1 155 ? 10.40100  57.59800  14.51700 0.300 50.62742  ? 485 THR A N   1 
ATOM   1959 C CA  A THR A 1 155 ? 11.41700  58.42100  14.55500 0.700 48.12613  ? 485 THR A CA  1 
ATOM   1960 C CA  B THR A 1 155 ? 11.37600  58.67000  14.67700 0.300 49.03878  ? 485 THR A CA  1 
ATOM   1961 C C   A THR A 1 155 ? 12.04200  58.37600  15.94200 0.700 52.34711  ? 485 THR A C   1 
ATOM   1962 C C   B THR A 1 155 ? 12.00800  58.66200  16.06100 0.300 52.89897  ? 485 THR A C   1 
ATOM   1963 O O   A THR A 1 155 ? 13.13700  58.91300  16.13600 0.700 55.37021  ? 485 THR A O   1 
ATOM   1964 O O   B THR A 1 155 ? 13.12300  59.17000  16.22500 0.300 55.32672  ? 485 THR A O   1 
ATOM   1965 C CB  A THR A 1 155 ? 10.75500  59.78200  14.33400 0.700 44.16861  ? 485 THR A CB  1 
ATOM   1966 C CB  B THR A 1 155 ? 10.72300  60.02900  14.41700 0.300 45.51627  ? 485 THR A CB  1 
ATOM   1967 O OG1 A THR A 1 155 ? 9.82100   60.03700  15.39100 0.700 47.07014  ? 485 THR A OG1 1 
ATOM   1968 O OG1 B THR A 1 155 ? 9.78400   60.31800  15.46100 0.300 50.37631  ? 485 THR A OG1 1 
ATOM   1969 C CG2 A THR A 1 155 ? 10.01800  59.80400  13.00200 0.700 46.05606  ? 485 THR A CG2 1 
ATOM   1970 C CG2 B THR A 1 155 ? 10.00000  60.02400  13.07800 0.300 46.56914  ? 485 THR A CG2 1 
ATOM   1971 N N   A GLY A 1 156 ? 11.35400  57.76900  16.90900 0.700 52.37957  ? 486 GLY A N   1 
ATOM   1972 N N   B GLY A 1 156 ? 11.32300  58.10000  17.05100 0.300 52.14226  ? 486 GLY A N   1 
ATOM   1973 C CA  A GLY A 1 156 ? 11.78200  57.74300  18.28900 0.700 47.51316  ? 486 GLY A CA  1 
ATOM   1974 C CA  B GLY A 1 156 ? 11.76800  58.12400  18.42500 0.300 51.31450  ? 486 GLY A CA  1 
ATOM   1975 C C   A GLY A 1 156 ? 11.54400  59.01900  19.06000 0.700 58.63902  ? 486 GLY A C   1 
ATOM   1976 C C   B GLY A 1 156 ? 11.55200  59.43500  19.14300 0.300 60.08458  ? 486 GLY A C   1 
ATOM   1977 O O   A GLY A 1 156 ? 11.88600  59.07400  20.24900 0.700 65.98368  ? 486 GLY A O   1 
ATOM   1978 O O   B GLY A 1 156 ? 11.93300  59.54800  20.31600 0.300 65.09690  ? 486 GLY A O   1 
ATOM   1979 N N   A LEU A 1 157 ? 10.93900  60.03200  18.44300 0.700 59.08462  ? 487 LEU A N   1 
ATOM   1980 N N   B LEU A 1 157 ? 10.95500  60.43000  18.48700 0.300 58.50520  ? 487 LEU A N   1 
ATOM   1981 C CA  A LEU A 1 157 ? 10.77200  61.31100  19.11600 0.700 59.64134  ? 487 LEU A CA  1 
ATOM   1982 C CA  B LEU A 1 157 ? 10.79400  61.73900  19.10100 0.300 58.88705  ? 487 LEU A CA  1 
ATOM   1983 C C   A LEU A 1 157 ? 9.48500   61.36500  19.91800 0.700 62.83327  ? 487 LEU A C   1 
ATOM   1984 C C   B LEU A 1 157 ? 9.49600   61.83000  19.88600 0.300 63.31192  ? 487 LEU A C   1 
ATOM   1985 O O   A LEU A 1 157 ? 9.43600   62.03400  20.95700 0.700 74.99697  ? 487 LEU A O   1 
ATOM   1986 O O   B LEU A 1 157 ? 9.43000   62.55500  20.88600 0.300 71.11685  ? 487 LEU A O   1 
ATOM   1987 C CB  A LEU A 1 157 ? 10.75800  62.44400  18.08700 0.700 54.48356  ? 487 LEU A CB  1 
ATOM   1988 C CB  B LEU A 1 157 ? 10.82800  62.83500  18.03300 0.300 55.58872  ? 487 LEU A CB  1 
ATOM   1989 C CG  A LEU A 1 157 ? 11.92200  62.51000  17.09900 0.700 58.83544  ? 487 LEU A CG  1 
ATOM   1990 C CG  B LEU A 1 157 ? 12.03000  62.83000  17.08600 0.300 59.48270  ? 487 LEU A CG  1 
ATOM   1991 C CD1 A LEU A 1 157 ? 11.71500  63.65500  16.11800 0.700 47.37299  ? 487 LEU A CD1 1 
ATOM   1992 C CD1 B LEU A 1 157 ? 11.89700  63.93700  16.05300 0.300 50.41779  ? 487 LEU A CD1 1 
ATOM   1993 C CD2 A LEU A 1 157 ? 13.24200  62.65400  17.83800 0.700 56.35556  ? 487 LEU A CD2 1 
ATOM   1994 C CD2 B LEU A 1 157 ? 13.33200  62.96600  17.86000 0.300 57.69169  ? 487 LEU A CD2 1 
ATOM   1995 N N   A ALA A 1 158 ? 8.44700   60.67400  19.45200 0.700 58.03034  ? 488 ALA A N   1 
ATOM   1996 N N   B ALA A 1 158 ? 8.46700   61.11600  19.43600 0.300 60.92436  ? 488 ALA A N   1 
ATOM   1997 C CA  A ALA A 1 158 ? 7.16200   60.69300  20.13200 0.700 63.92039  ? 488 ALA A CA  1 
ATOM   1998 C CA  B ALA A 1 158 ? 7.16700   61.15100  20.08800 0.300 64.18750  ? 488 ALA A CA  1 
ATOM   1999 C C   A ALA A 1 158 ? 7.28600   60.11400  21.53500 0.700 73.40183  ? 488 ALA A C   1 
ATOM   2000 C C   B ALA A 1 158 ? 7.27700   60.63400  21.51600 0.300 71.83371  ? 488 ALA A C   1 
ATOM   2001 O O   A ALA A 1 158 ? 8.04600   59.17100  21.77400 0.700 74.55861  ? 488 ALA A O   1 
ATOM   2002 O O   B ALA A 1 158 ? 8.04300   59.71100  21.80500 0.300 70.21650  ? 488 ALA A O   1 
ATOM   2003 C CB  A ALA A 1 158 ? 6.12200   59.91100  19.32900 0.700 62.17448  ? 488 ALA A CB  1 
ATOM   2004 C CB  B ALA A 1 158 ? 6.15000   60.32400  19.30100 0.300 60.41423  ? 488 ALA A CB  1 
ATOM   2005 N N   A ASN A 1 159 ? 6.53500   60.69200  22.46800 0.700 74.69026  ? 489 ASN A N   1 
ATOM   2006 N N   B ASN A 1 159 ? 6.50000   61.23500  22.41300 0.300 74.04789  ? 489 ASN A N   1 
ATOM   2007 C CA  A ASN A 1 159 ? 6.40500   60.15100  23.81100 0.700 73.52997  ? 489 ASN A CA  1 
ATOM   2008 C CA  B ASN A 1 159 ? 6.37000   60.74500  23.77500 0.300 75.49788  ? 489 ASN A CA  1 
ATOM   2009 C C   A ASN A 1 159 ? 5.04200   59.52400  24.04700 0.700 70.17415  ? 489 ASN A C   1 
ATOM   2010 C C   B ASN A 1 159 ? 5.02700   60.08400  24.03400 0.300 72.05562  ? 489 ASN A C   1 
ATOM   2011 O O   A ASN A 1 159 ? 4.84400   58.88100  25.08400 0.700 71.14048  ? 489 ASN A O   1 
ATOM   2012 O O   B ASN A 1 159 ? 4.84700   59.47700  25.09500 0.300 72.14966  ? 489 ASN A O   1 
ATOM   2013 C CB  A ASN A 1 159 ? 6.67400   61.22900  24.87200 0.700 88.04993  ? 489 ASN A CB  1 
ATOM   2014 C CB  B ASN A 1 159 ? 6.57700   61.89000  24.77900 0.300 80.45356  ? 489 ASN A CB  1 
ATOM   2015 C CG  A ASN A 1 159 ? 8.07600   61.80300  24.77600 0.700 87.71322  ? 489 ASN A CG  1 
ATOM   2016 C CG  B ASN A 1 159 ? 7.95000   62.52300  24.66700 0.300 82.07125  ? 489 ASN A CG  1 
ATOM   2017 O OD1 A ASN A 1 159 ? 8.30200   62.97700  25.07100 0.700 84.45622  ? 489 ASN A OD1 1 
ATOM   2018 O OD1 B ASN A 1 159 ? 8.41600   62.83200  23.57000 0.300 78.66777  ? 489 ASN A OD1 1 
ATOM   2019 N ND2 A ASN A 1 159 ? 9.03200   60.96800  24.37100 0.700 73.05142  ? 489 ASN A ND2 1 
ATOM   2020 N ND2 B ASN A 1 159 ? 8.60800   62.71600  25.80400 0.300 83.54607  ? 489 ASN A ND2 1 
ATOM   2021 N N   A ASP A 1 160 ? 4.10600   59.69900  23.11800 0.700 70.80892  ? 490 ASP A N   1 
ATOM   2022 N N   B ASP A 1 160 ? 4.08800   60.18600  23.09800 0.300 70.78394  ? 490 ASP A N   1 
ATOM   2023 C CA  A ASP A 1 160 ? 2.75600   59.18200  23.24400 0.700 84.37420  ? 490 ASP A CA  1 
ATOM   2024 C CA  B ASP A 1 160 ? 2.75300   59.63200  23.24100 0.300 80.77127  ? 490 ASP A CA  1 
ATOM   2025 C C   A ASP A 1 160 ? 2.42100   58.29300  22.05000 0.700 80.81711  ? 490 ASP A C   1 
ATOM   2026 C C   B ASP A 1 160 ? 2.43900   58.68400  22.08900 0.300 79.17887  ? 490 ASP A C   1 
ATOM   2027 O O   A ASP A 1 160 ? 3.10200   58.30600  21.02000 0.700 73.20879  ? 490 ASP A O   1 
ATOM   2028 O O   B ASP A 1 160 ? 3.12300   58.66600  21.06200 0.300 74.51937  ? 490 ASP A O   1 
ATOM   2029 C CB  A ASP A 1 160 ? 1.74600   60.33100  23.34700 0.700 83.63208  ? 490 ASP A CB  1 
ATOM   2030 C CB  B ASP A 1 160 ? 1.70100   60.74500  23.28700 0.300 81.33005  ? 490 ASP A CB  1 
ATOM   2031 C CG  A ASP A 1 160 ? 1.88500   61.11400  24.63900 0.700 87.29376  ? 490 ASP A CG  1 
ATOM   2032 C CG  B ASP A 1 160 ? 1.79900   61.58800  24.54100 0.300 84.61488  ? 490 ASP A CG  1 
ATOM   2033 O OD1 A ASP A 1 160 ? 2.89900   61.82600  24.79600 0.700 89.58944  ? 490 ASP A OD1 1 
ATOM   2034 O OD1 B ASP A 1 160 ? 2.08700   61.02500  25.61800 0.300 88.43578  ? 490 ASP A OD1 1 
ATOM   2035 O OD2 A ASP A 1 160 ? 0.98200   61.01800  25.49700 0.700 92.75948  ? 490 ASP A OD2 1 
ATOM   2036 O OD2 B ASP A 1 160 ? 1.58400   62.81600  24.45000 0.300 74.35277  ? 490 ASP A OD2 1 
ATOM   2037 N N   A TYR A 1 161 ? 1.35200   57.51400  22.20800 0.700 80.41091  ? 491 TYR A N   1 
ATOM   2038 N N   B TYR A 1 161 ? 1.38700   57.89100  22.28000 0.300 79.23426  ? 491 TYR A N   1 
ATOM   2039 C CA  A TYR A 1 161 ? 0.81600   56.65000  21.16500 0.700 77.75528  ? 491 TYR A CA  1 
ATOM   2040 C CA  B TYR A 1 161 ? 0.87900   56.98200  21.26400 0.300 75.75313  ? 491 TYR A CA  1 
ATOM   2041 C C   A TYR A 1 161 ? -0.68000  56.90200  21.04300 0.700 72.98489  ? 491 TYR A C   1 
ATOM   2042 C C   B TYR A 1 161 ? -0.61900  57.20900  21.12400 0.300 73.53040  ? 491 TYR A C   1 
ATOM   2043 O O   A TYR A 1 161 ? -1.37300  57.04200  22.05500 0.700 71.37957  ? 491 TYR A O   1 
ATOM   2044 O O   B TYR A 1 161 ? -1.32700  57.37300  22.12100 0.300 73.51558  ? 491 TYR A O   1 
ATOM   2045 C CB  A TYR A 1 161 ? 1.09500   55.17100  21.47700 0.700 71.17366  ? 491 TYR A CB  1 
ATOM   2046 C CB  B TYR A 1 161 ? 1.17800   55.51900  21.61500 0.300 70.03712  ? 491 TYR A CB  1 
ATOM   2047 C CG  A TYR A 1 161 ? 2.56800   54.85100  21.64800 0.700 54.79076  ? 491 TYR A CG  1 
ATOM   2048 C CG  B TYR A 1 161 ? 2.65100   55.22000  21.80100 0.300 60.09693  ? 491 TYR A CG  1 
ATOM   2049 C CD1 A TYR A 1 161 ? 3.19200   54.99300  22.88200 0.700 54.07607  ? 491 TYR A CD1 1 
ATOM   2050 C CD1 B TYR A 1 161 ? 3.27100   55.40100  23.03100 0.300 59.03502  ? 491 TYR A CD1 1 
ATOM   2051 C CD2 A TYR A 1 161 ? 3.33300   54.41100  20.57500 0.700 55.85776  ? 491 TYR A CD2 1 
ATOM   2052 C CD2 B TYR A 1 161 ? 3.41900   54.74600  20.74400 0.300 56.96466  ? 491 TYR A CD2 1 
ATOM   2053 C CE1 A TYR A 1 161 ? 4.53500   54.70200  23.04300 0.700 56.41519  ? 491 TYR A CE1 1 
ATOM   2054 C CE1 B TYR A 1 161 ? 4.61500   55.12100  23.20200 0.300 58.66846  ? 491 TYR A CE1 1 
ATOM   2055 C CE2 A TYR A 1 161 ? 4.67600   54.12000  20.72600 0.700 54.54874  ? 491 TYR A CE2 1 
ATOM   2056 C CE2 B TYR A 1 161 ? 4.76300   54.46700  20.90500 0.300 56.01613  ? 491 TYR A CE2 1 
ATOM   2057 C CZ  A TYR A 1 161 ? 5.27200   54.26600  21.96200 0.700 52.28578  ? 491 TYR A CZ  1 
ATOM   2058 C CZ  B TYR A 1 161 ? 5.35600   54.65500  22.13500 0.300 55.84556  ? 491 TYR A CZ  1 
ATOM   2059 O OH  A TYR A 1 161 ? 6.61200   53.98100  22.11400 0.700 41.62651  ? 491 TYR A OH  1 
ATOM   2060 O OH  B TYR A 1 161 ? 6.69600   54.38200  22.29700 0.300 48.55583  ? 491 TYR A OH  1 
ATOM   2061 N N   A ASN A 1 162 ? -1.18500  56.94600  19.81100 0.700 72.41635  ? 492 ASN A N   1 
ATOM   2062 N N   B ASN A 1 162 ? -1.09600  57.21200  19.88200 0.300 72.00550  ? 492 ASN A N   1 
ATOM   2063 C CA  A ASN A 1 162 ? -2.60100  57.22500  19.62500 0.700 75.62052  ? 492 ASN A CA  1 
ATOM   2064 C CA  B ASN A 1 162 ? -2.50000  57.46100  19.59700 0.300 74.26960  ? 492 ASN A CA  1 
ATOM   2065 C C   A ASN A 1 162 ? -3.45300  55.98700  19.92000 0.700 61.82185  ? 492 ASN A C   1 
ATOM   2066 C C   B ASN A 1 162 ? -3.36600  56.23100  19.86800 0.300 63.45679  ? 492 ASN A C   1 
ATOM   2067 O O   A ASN A 1 162 ? -2.94900  54.91200  20.25800 0.700 50.86346  ? 492 ASN A O   1 
ATOM   2068 O O   B ASN A 1 162 ? -2.89100  55.16400  20.26800 0.300 53.07907  ? 492 ASN A O   1 
ATOM   2069 C CB  A ASN A 1 162 ? -2.84400  57.75400  18.21100 0.700 71.17989  ? 492 ASN A CB  1 
ATOM   2070 C CB  B ASN A 1 162 ? -2.66300  57.92900  18.15200 0.300 69.86506  ? 492 ASN A CB  1 
ATOM   2071 C CG  A ASN A 1 162 ? -2.26800  56.84700  17.13600 0.700 59.54043  ? 492 ASN A CG  1 
ATOM   2072 C CG  B ASN A 1 162 ? -2.01300  56.98500  17.15500 0.300 61.72649  ? 492 ASN A CG  1 
ATOM   2073 O OD1 A ASN A 1 162 ? -1.88200  55.70900  17.40300 0.700 60.55313  ? 492 ASN A OD1 1 
ATOM   2074 O OD1 B ASN A 1 162 ? -1.63200  55.86500  17.49600 0.300 61.83570  ? 492 ASN A OD1 1 
ATOM   2075 N ND2 A ASN A 1 162 ? -2.20100  57.35500  15.91200 0.700 61.89352  ? 492 ASN A ND2 1 
ATOM   2076 N ND2 B ASN A 1 162 ? -1.88300  57.43800  15.91400 0.300 63.71839  ? 492 ASN A ND2 1 
ATOM   2077 N N   A LYS A 1 163 ? -4.77500  56.15200  19.80800 0.700 60.31002  ? 493 LYS A N   1 
ATOM   2078 N N   B LYS A 1 163 ? -4.67300  56.40700  19.64700 0.300 62.74387  ? 493 LYS A N   1 
ATOM   2079 C CA  A LYS A 1 163 ? -5.68100  55.01000  19.89700 0.700 53.28974  ? 493 LYS A CA  1 
ATOM   2080 C CA  B LYS A 1 163 ? -5.61500  55.29300  19.68200 0.300 56.18801  ? 493 LYS A CA  1 
ATOM   2081 C C   A LYS A 1 163 ? -5.39400  53.96700  18.82300 0.700 63.84544  ? 493 LYS A C   1 
ATOM   2082 C C   B LYS A 1 163 ? -5.24900  54.22200  18.66300 0.300 63.14235  ? 493 LYS A C   1 
ATOM   2083 O O   A LYS A 1 163 ? -5.50800  52.76200  19.07800 0.700 56.06388  ? 493 LYS A O   1 
ATOM   2084 O O   B LYS A 1 163 ? -5.44400  53.02600  18.91200 0.300 57.32012  ? 493 LYS A O   1 
ATOM   2085 C CB  A LYS A 1 163 ? -7.13300  55.48500  19.81200 0.700 50.95492  ? 493 LYS A CB  1 
ATOM   2086 C CB  B LYS A 1 163 ? -7.03600  55.80000  19.44100 0.300 53.20386  ? 493 LYS A CB  1 
ATOM   2087 N N   A ARG A 1 164 ? -5.02000  54.40500  17.61400 0.700 65.51696  ? 494 ARG A N   1 
ATOM   2088 N N   B ARG A 1 164 ? -4.73400  54.63400  17.50000 0.300 63.07217  ? 494 ARG A N   1 
ATOM   2089 C CA  A ARG A 1 164 ? -4.83100  53.44700  16.52500 0.700 68.78852  ? 494 ARG A CA  1 
ATOM   2090 C CA  B ARG A 1 164 ? -4.45300  53.67400  16.43700 0.300 65.11466  ? 494 ARG A CA  1 
ATOM   2091 C C   A ARG A 1 164 ? -3.69600  52.47700  16.84400 0.700 58.51200  ? 494 ARG A C   1 
ATOM   2092 C C   B ARG A 1 164 ? -3.40600  52.66300  16.87500 0.300 58.53315  ? 494 ARG A C   1 
ATOM   2093 O O   A ARG A 1 164 ? -3.75600  51.29900  16.46700 0.700 55.97677  ? 494 ARG A O   1 
ATOM   2094 O O   B ARG A 1 164 ? -3.46300  51.49100  16.48300 0.300 56.69321  ? 494 ARG A O   1 
ATOM   2095 C CB  A ARG A 1 164 ? -4.66300  54.17300  15.18400 0.700 68.16508  ? 494 ARG A CB  1 
ATOM   2096 C CB  B ARG A 1 164 ? -3.96300  54.39800  15.18600 0.300 63.34694  ? 494 ARG A CB  1 
ATOM   2097 C CG  A ARG A 1 164 ? -3.83100  53.47100  14.12100 0.700 63.03485  ? 494 ARG A CG  1 
ATOM   2098 C CG  B ARG A 1 164 ? -3.90500  53.51600  13.95300 0.300 62.60916  ? 494 ARG A CG  1 
ATOM   2099 C CD  A ARG A 1 164 ? -3.24800  54.48400  13.14800 0.700 61.09231  ? 494 ARG A CD  1 
ATOM   2100 C CD  B ARG A 1 164 ? -2.86200  54.02600  12.97900 0.300 57.97478  ? 494 ARG A CD  1 
ATOM   2101 N NE  A ARG A 1 164 ? -1.97200  55.06800  13.53400 0.700 76.24071  ? 494 ARG A NE  1 
ATOM   2102 N NE  B ARG A 1 164 ? -3.36800  55.10100  12.13800 0.300 58.31014  ? 494 ARG A NE  1 
ATOM   2103 C CZ  A ARG A 1 164 ? -1.20900  55.76000  12.70000 0.700 67.52325  ? 494 ARG A CZ  1 
ATOM   2104 C CZ  B ARG A 1 164 ? -2.86700  56.32900  12.12200 0.300 59.13107  ? 494 ARG A CZ  1 
ATOM   2105 N NH1 A ARG A 1 164 ? -1.57900  55.97500  11.44700 0.700 68.83106  ? 494 ARG A NH1 1 
ATOM   2106 N NH1 B ARG A 1 164 ? -1.83600  56.66400  12.88100 0.300 63.94476  ? 494 ARG A NH1 1 
ATOM   2107 N NH2 A ARG A 1 164 ? -0.05800  56.26400  13.13700 0.700 57.88283  ? 494 ARG A NH2 1 
ATOM   2108 N NH2 B ARG A 1 164 ? -3.41100  57.24100  11.32200 0.300 68.24554  ? 494 ARG A NH2 1 
ATOM   2109 N N   A THR A 1 165 ? -2.65000  52.95800  17.52600 0.700 53.40439  ? 495 THR A N   1 
ATOM   2110 N N   B THR A 1 165 ? -2.42500  53.10500  17.66600 0.300 54.58655  ? 495 THR A N   1 
ATOM   2111 C CA  A THR A 1 165 ? -1.56400  52.07700  17.95500 0.700 53.77284  ? 495 THR A CA  1 
ATOM   2112 C CA  B THR A 1 165 ? -1.42900  52.17900  18.19000 0.300 53.38588  ? 495 THR A CA  1 
ATOM   2113 C C   A THR A 1 165 ? -2.11000  50.90100  18.75400 0.700 49.13588  ? 495 THR A C   1 
ATOM   2114 C C   B THR A 1 165 ? -2.10300  51.02900  18.92200 0.300 49.25042  ? 495 THR A C   1 
ATOM   2115 O O   A THR A 1 165 ? -1.68900  49.75400  18.56200 0.700 43.84890  ? 495 THR A O   1 
ATOM   2116 O O   B THR A 1 165 ? -1.79800  49.86000  18.67000 0.300 43.60672  ? 495 THR A O   1 
ATOM   2117 C CB  A THR A 1 165 ? -0.55000  52.84900  18.80100 0.700 50.95818  ? 495 THR A CB  1 
ATOM   2118 C CB  B THR A 1 165 ? -0.45700  52.91100  19.11400 0.300 52.79770  ? 495 THR A CB  1 
ATOM   2119 O OG1 A THR A 1 165 ? -0.10400  54.01300  18.09300 0.700 58.52841  ? 495 THR A OG1 1 
ATOM   2120 O OG1 B THR A 1 165 ? 0.08900   54.04700  18.43300 0.300 58.56203  ? 495 THR A OG1 1 
ATOM   2121 C CG2 A THR A 1 165 ? 0.62300   51.96000  19.18000 0.700 37.39060  ? 495 THR A CG2 1 
ATOM   2122 C CG2 B THR A 1 165 ? 0.67300   51.98800  19.51400 0.300 41.93064  ? 495 THR A CG2 1 
ATOM   2123 N N   A MET A 1 166 ? -3.03800  51.17900  19.67100 0.700 49.34389  ? 496 MET A N   1 
ATOM   2124 N N   B MET A 1 166 ? -3.09900  51.34200  19.75400 0.300 49.94926  ? 496 MET A N   1 
ATOM   2125 C CA  A MET A 1 166 ? -3.54600  50.15300  20.57000 0.700 40.20503  ? 496 MET A CA  1 
ATOM   2126 C CA  B MET A 1 166 ? -3.72100  50.32600  20.59700 0.300 42.84712  ? 496 MET A CA  1 
ATOM   2127 C C   A MET A 1 166 ? -4.30800  49.09500  19.78400 0.700 43.57385  ? 496 MET A C   1 
ATOM   2128 C C   B MET A 1 166 ? -4.44200  49.29800  19.74200 0.300 44.47625  ? 496 MET A C   1 
ATOM   2129 O O   A MET A 1 166 ? -4.21000  47.89800  20.07800 0.700 55.80902  ? 496 MET A O   1 
ATOM   2130 O O   B MET A 1 166 ? -4.42300  48.09900  20.04500 0.300 51.80970  ? 496 MET A O   1 
ATOM   2131 C CB  A MET A 1 166 ? -4.41700  50.79400  21.65000 0.700 41.34355  ? 496 MET A CB  1 
ATOM   2132 C CB  B MET A 1 166 ? -4.67200  50.98400  21.59200 0.300 44.35325  ? 496 MET A CB  1 
ATOM   2133 C CG  A MET A 1 166 ? -3.59800  51.65200  22.59700 0.700 45.93625  ? 496 MET A CG  1 
ATOM   2134 C CG  B MET A 1 166 ? -3.93400  51.81100  22.61900 0.300 49.75100  ? 496 MET A CG  1 
ATOM   2135 S SD  A MET A 1 166 ? -2.00900  50.89000  22.98200 0.700 54.07677  ? 496 MET A SD  1 
ATOM   2136 S SD  B MET A 1 166 ? -2.42700  50.96600  23.12700 0.300 57.36098  ? 496 MET A SD  1 
ATOM   2137 C CE  A MET A 1 166 ? -1.97800  51.08000  24.76300 0.700 48.26333  ? 496 MET A CE  1 
ATOM   2138 C CE  B MET A 1 166 ? -1.82400  52.08700  24.37700 0.300 47.81310  ? 496 MET A CE  1 
ATOM   2139 N N   A GLY A 1 167 ? -5.06000  49.52300  18.77000 0.700 52.12148  ? 497 GLY A N   1 
ATOM   2140 N N   B GLY A 1 167 ? -5.08300  49.75500  18.66900 0.300 52.75092  ? 497 GLY A N   1 
ATOM   2141 C CA  A GLY A 1 167 ? -5.76100  48.57800  17.91700 0.700 46.16687  ? 497 GLY A CA  1 
ATOM   2142 C CA  B GLY A 1 167 ? -5.72900  48.83300  17.75700 0.300 48.16610  ? 497 GLY A CA  1 
ATOM   2143 C C   A GLY A 1 167 ? -4.79200  47.70300  17.14700 0.700 44.24048  ? 497 GLY A C   1 
ATOM   2144 C C   B GLY A 1 167 ? -4.72500  47.93000  17.06500 0.300 44.40654  ? 497 GLY A C   1 
ATOM   2145 O O   A GLY A 1 167 ? -5.03500  46.50800  16.95200 0.700 47.16988  ? 497 GLY A O   1 
ATOM   2146 O O   B GLY A 1 167 ? -4.99300  46.74600  16.84600 0.300 47.27760  ? 497 GLY A O   1 
ATOM   2147 N N   A LEU A 1 168 ? -3.68500  48.29200  16.68600 0.700 46.38150  ? 498 LEU A N   1 
ATOM   2148 N N   B LEU A 1 168 ? -3.56500  48.48200  16.69100 0.300 46.35888  ? 498 LEU A N   1 
ATOM   2149 C CA  A LEU A 1 168 ? -2.65400  47.51400  16.00700 0.700 41.64395  ? 498 LEU A CA  1 
ATOM   2150 C CA  B LEU A 1 168 ? -2.51700  47.66300  16.08500 0.300 42.37606  ? 498 LEU A CA  1 
ATOM   2151 C C   A LEU A 1 168 ? -2.18300  46.36700  16.89700 0.700 45.95299  ? 498 LEU A C   1 
ATOM   2152 C C   B LEU A 1 168 ? -2.13100  46.50000  16.99700 0.300 45.55423  ? 498 LEU A C   1 
ATOM   2153 O O   A LEU A 1 168 ? -2.01600  45.23600  16.42600 0.700 53.33242  ? 498 LEU A O   1 
ATOM   2154 O O   B LEU A 1 168 ? -1.99700  45.36100  16.53500 0.300 51.83085  ? 498 LEU A O   1 
ATOM   2155 C CB  A LEU A 1 168 ? -1.50700  48.44000  15.61100 0.700 43.81778  ? 498 LEU A CB  1 
ATOM   2156 C CB  B LEU A 1 168 ? -1.30700  48.54000  15.76200 0.300 45.38012  ? 498 LEU A CB  1 
ATOM   2157 C CG  A LEU A 1 168 ? -0.27300  47.87100  14.93200 0.700 59.16037  ? 498 LEU A CG  1 
ATOM   2158 C CG  B LEU A 1 168 ? -0.39500  48.09600  14.61900 0.300 57.78160  ? 498 LEU A CG  1 
ATOM   2159 C CD1 A LEU A 1 168 ? -0.48500  47.80900  13.42900 0.700 67.01898  ? 498 LEU A CD1 1 
ATOM   2160 C CD1 B LEU A 1 168 ? -1.21000  47.88100  13.35700 0.300 55.60327  ? 498 LEU A CD1 1 
ATOM   2161 C CD2 A LEU A 1 168 ? 0.90500   48.76900  15.26800 0.700 53.22339  ? 498 LEU A CD2 1 
ATOM   2162 C CD2 B LEU A 1 168 ? 0.69400   49.12900  14.38000 0.300 44.00608  ? 498 LEU A CD2 1 
ATOM   2163 N N   A LEU A 1 169 ? -1.95700  46.64100  18.18600 0.700 42.75366  ? 499 LEU A N   1 
ATOM   2164 N N   B LEU A 1 169 ? -1.94300  46.76000  18.29700 0.300 42.92939  ? 499 LEU A N   1 
ATOM   2165 C CA  A LEU A 1 169 ? -1.39300  45.63100  19.08000 0.700 35.42730  ? 499 LEU A CA  1 
ATOM   2166 C CA  B LEU A 1 169 ? -1.46000  45.69800  19.18300 0.300 36.67876  ? 499 LEU A CA  1 
ATOM   2167 C C   A LEU A 1 169 ? -2.42900  44.54500  19.35900 0.700 35.48940  ? 499 LEU A C   1 
ATOM   2168 C C   B LEU A 1 169 ? -2.55400  44.66600  19.42000 0.300 35.49820  ? 499 LEU A C   1 
ATOM   2169 O O   A LEU A 1 169 ? -2.11000  43.35000  19.36400 0.700 37.75589  ? 499 LEU A O   1 
ATOM   2170 O O   B LEU A 1 169 ? -2.28900  43.45900  19.40500 0.300 37.53947  ? 499 LEU A O   1 
ATOM   2171 C CB  A LEU A 1 169 ? -0.91900  46.27200  20.38300 0.700 35.74954  ? 499 LEU A CB  1 
ATOM   2172 C CB  B LEU A 1 169 ? -0.90100  46.22500  20.51000 0.300 36.73632  ? 499 LEU A CB  1 
ATOM   2173 C CG  A LEU A 1 169 ? 0.26300   47.23600  20.30900 0.700 34.41446  ? 499 LEU A CG  1 
ATOM   2174 C CG  B LEU A 1 169 ? 0.39300   47.05200  20.58600 0.300 37.00154  ? 499 LEU A CG  1 
ATOM   2175 C CD1 A LEU A 1 169 ? 0.56900   47.78500  21.68900 0.700 35.83957  ? 499 LEU A CD1 1 
ATOM   2176 C CD1 B LEU A 1 169 ? 0.28600   48.47100  20.11800 0.300 44.04970  ? 499 LEU A CD1 1 
ATOM   2177 C CD2 A LEU A 1 169 ? 1.48300   46.53100  19.73600 0.700 33.97408  ? 499 LEU A CD2 1 
ATOM   2178 C CD2 B LEU A 1 169 ? 0.95600   47.00500  22.00400 0.300 36.40118  ? 499 LEU A CD2 1 
ATOM   2179 N N   A VAL A 1 170 ? -3.68200  44.95300  19.58900 0.700 35.68291  ? 500 VAL A N   1 
ATOM   2180 N N   B VAL A 1 170 ? -3.79100  45.12200  19.62900 0.300 35.64057  ? 500 VAL A N   1 
ATOM   2181 C CA  A VAL A 1 170 ? -4.74300  44.02300  19.96700 0.700 36.55722  ? 500 VAL A CA  1 
ATOM   2182 C CA  B VAL A 1 170 ? -4.87400  44.20500  19.96600 0.300 36.87371  ? 500 VAL A CA  1 
ATOM   2183 C C   A VAL A 1 170 ? -5.08200  43.11500  18.79100 0.700 33.25791  ? 500 VAL A C   1 
ATOM   2184 C C   B VAL A 1 170 ? -5.19200  43.33300  18.76100 0.300 34.53998  ? 500 VAL A C   1 
ATOM   2185 O O   A VAL A 1 170 ? -5.31700  41.91200  18.96300 0.700 43.65317  ? 500 VAL A O   1 
ATOM   2186 O O   B VAL A 1 170 ? -5.44500  42.12900  18.89500 0.300 43.28277  ? 500 VAL A O   1 
ATOM   2187 C CB  A VAL A 1 170 ? -5.98000  44.79300  20.47000 0.700 40.94124  ? 500 VAL A CB  1 
ATOM   2188 C CB  B VAL A 1 170 ? -6.11000  44.98700  20.44700 0.300 41.49344  ? 500 VAL A CB  1 
ATOM   2189 C CG1 A VAL A 1 170 ? -7.15300  43.85000  20.68800 0.700 39.34189  ? 500 VAL A CG1 1 
ATOM   2190 C CG1 B VAL A 1 170 ? -7.30300  44.05500  20.61900 0.300 39.59709  ? 500 VAL A CG1 1 
ATOM   2191 C CG2 A VAL A 1 170 ? -5.65700  45.54000  21.75300 0.700 47.72169  ? 500 VAL A CG2 1 
ATOM   2192 C CG2 B VAL A 1 170 ? -5.80700  45.71800  21.74500 0.300 46.99274  ? 500 VAL A CG2 1 
ATOM   2193 N N   A SER A 1 171 ? -5.10800  43.67600  17.57700 0.700 40.35831  ? 501 SER A N   1 
ATOM   2194 N N   B SER A 1 171 ? -5.18700  43.92400  17.56500 0.300 41.24881  ? 501 SER A N   1 
ATOM   2195 C CA  A SER A 1 171 ? -5.36300  42.86200  16.39200 0.700 39.61544  ? 501 SER A CA  1 
ATOM   2196 C CA  B SER A 1 171 ? -5.40800  43.13900  16.35800 0.300 40.36806  ? 501 SER A CA  1 
ATOM   2197 C C   A SER A 1 171 ? -4.24200  41.85300  16.19800 0.700 35.98468  ? 501 SER A C   1 
ATOM   2198 C C   B SER A 1 171 ? -4.27100  42.14600  16.16000 0.300 36.17519  ? 501 SER A C   1 
ATOM   2199 O O   A SER A 1 171 ? -4.48600  40.71500  15.78200 0.700 43.92560  ? 501 SER A O   1 
ATOM   2200 O O   B SER A 1 171 ? -4.49300  41.01400  15.71500 0.300 40.85053  ? 501 SER A O   1 
ATOM   2201 C CB  A SER A 1 171 ? -5.50300  43.74300  15.15100 0.700 36.49404  ? 501 SER A CB  1 
ATOM   2202 C CB  B SER A 1 171 ? -5.53700  44.05500  15.14500 0.300 37.18179  ? 501 SER A CB  1 
ATOM   2203 O OG  A SER A 1 171 ? -4.29900  44.43900  14.87600 0.700 28.51970  ? 501 SER A OG  1 
ATOM   2204 O OG  B SER A 1 171 ? -5.23300  43.36100  13.94800 0.300 38.67837  ? 501 SER A OG  1 
ATOM   2205 N N   A ASP A 1 172 ? -3.00300  42.25100  16.49300 0.700 38.25888  ? 502 ASP A N   1 
ATOM   2206 N N   B ASP A 1 172 ? -3.04100  42.55700  16.47900 0.300 38.01991  ? 502 ASP A N   1 
ATOM   2207 C CA  A ASP A 1 172 ? -1.87400  41.37000  16.22000 0.700 31.23602  ? 502 ASP A CA  1 
ATOM   2208 C CA  B ASP A 1 172 ? -1.88900  41.70600  16.20600 0.300 33.46066  ? 502 ASP A CA  1 
ATOM   2209 C C   A ASP A 1 172 ? -1.83500  40.23300  17.22900 0.700 33.48558  ? 502 ASP A C   1 
ATOM   2210 C C   B ASP A 1 172 ? -1.83000  40.55400  17.19900 0.300 34.56358  ? 502 ASP A C   1 
ATOM   2211 O O   A ASP A 1 172 ? -1.52000  39.09200  16.87200 0.700 34.94809  ? 502 ASP A O   1 
ATOM   2212 O O   B ASP A 1 172 ? -1.48300  39.42600  16.83100 0.300 34.77642  ? 502 ASP A O   1 
ATOM   2213 C CB  A ASP A 1 172 ? -0.56200  42.14500  16.24500 0.700 27.46298  ? 502 ASP A CB  1 
ATOM   2214 C CB  B ASP A 1 172 ? -0.60300  42.52600  16.25600 0.300 31.02185  ? 502 ASP A CB  1 
ATOM   2215 C CG  A ASP A 1 172 ? 0.63700   41.24800  16.02200 0.700 36.69314  ? 502 ASP A CG  1 
ATOM   2216 C CG  B ASP A 1 172 ? 0.63300   41.68500  16.02700 0.300 39.43319  ? 502 ASP A CG  1 
ATOM   2217 O OD1 A ASP A 1 172 ? 0.73600   40.63200  14.93900 0.700 41.16348  ? 502 ASP A OD1 1 
ATOM   2218 O OD1 B ASP A 1 172 ? 0.75800   41.10200  14.93100 0.300 45.10738  ? 502 ASP A OD1 1 
ATOM   2219 O OD2 A ASP A 1 172 ? 1.48100   41.15100  16.93600 0.700 42.26572  ? 502 ASP A OD2 1 
ATOM   2220 O OD2 B ASP A 1 172 ? 1.48100   41.61100  16.94000 0.300 41.84619  ? 502 ASP A OD2 1 
ATOM   2221 N N   A ILE A 1 173 ? -2.14300  40.52800  18.49500 0.700 34.10501  ? 503 ILE A N   1 
ATOM   2222 N N   B ILE A 1 173 ? -2.14600  40.82600  18.46900 0.300 35.39805  ? 503 ILE A N   1 
ATOM   2223 C CA  A ILE A 1 173 ? -2.17600  39.47600  19.50800 0.700 25.96600  ? 503 ILE A CA  1 
ATOM   2224 C CA  B ILE A 1 173 ? -2.16800  39.76500  19.47100 0.300 27.15248  ? 503 ILE A CA  1 
ATOM   2225 C C   A ILE A 1 173 ? -3.22000  38.44200  19.12100 0.700 32.32560  ? 503 ILE A C   1 
ATOM   2226 C C   B ILE A 1 173 ? -3.20400  38.72300  19.08000 0.300 31.37652  ? 503 ILE A C   1 
ATOM   2227 O O   A ILE A 1 173 ? -2.97500  37.23000  19.19200 0.700 42.02858  ? 503 ILE A O   1 
ATOM   2228 O O   B ILE A 1 173 ? -2.95000  37.51400  19.14400 0.300 40.41571  ? 503 ILE A O   1 
ATOM   2229 C CB  A ILE A 1 173 ? -2.44900  40.05900  20.90600 0.700 23.86154  ? 503 ILE A CB  1 
ATOM   2230 C CB  B ILE A 1 173 ? -2.42700  40.33800  20.87700 0.300 25.31487  ? 503 ILE A CB  1 
ATOM   2231 C CG1 A ILE A 1 173 ? -1.27700  40.92100  21.36900 0.700 27.68948  ? 503 ILE A CG1 1 
ATOM   2232 C CG1 B ILE A 1 173 ? -1.24300  41.19500  21.32800 0.300 28.87135  ? 503 ILE A CG1 1 
ATOM   2233 C CG2 A ILE A 1 173 ? -2.69000  38.94000  21.90400 0.700 31.58265  ? 503 ILE A CG2 1 
ATOM   2234 C CG2 B ILE A 1 173 ? -2.67500  39.21700  21.87000 0.300 32.11320  ? 503 ILE A CG2 1 
ATOM   2235 C CD1 A ILE A 1 173 ? -1.67000  41.98600  22.37600 0.700 37.11154  ? 503 ILE A CD1 1 
ATOM   2236 C CD1 B ILE A 1 173 ? -1.60800  42.25400  22.34400 0.300 35.72788  ? 503 ILE A CD1 1 
ATOM   2237 N N   A GLY A 1 174 ? -4.39900  38.90700  18.69600 0.700 23.50687  ? 504 GLY A N   1 
ATOM   2238 N N   B GLY A 1 174 ? -4.38900  39.18100  18.66600 0.300 24.89564  ? 504 GLY A N   1 
ATOM   2239 C CA  A GLY A 1 174 ? -5.44800  37.98300  18.29700 0.700 29.62602  ? 504 GLY A CA  1 
ATOM   2240 C CA  B GLY A 1 174 ? -5.42900  38.25500  18.25600 0.300 29.49669  ? 504 GLY A CA  1 
ATOM   2241 C C   A GLY A 1 174 ? -4.99700  37.09700  17.15400 0.700 26.40374  ? 504 GLY A C   1 
ATOM   2242 C C   B GLY A 1 174 ? -4.97100  37.39700  17.09500 0.300 27.05315  ? 504 GLY A C   1 
ATOM   2243 O O   A GLY A 1 174 ? -5.25500  35.89100  17.15500 0.700 32.06763  ? 504 GLY A O   1 
ATOM   2244 O O   B GLY A 1 174 ? -5.23700  36.19300  17.05800 0.300 31.54800  ? 504 GLY A O   1 
ATOM   2245 N N   A THR A 1 175 ? -4.29200  37.68000  16.17700 0.700 28.84090  ? 505 THR A N   1 
ATOM   2246 N N   B THR A 1 175 ? -4.27500  38.00800  16.13000 0.300 30.62357  ? 505 THR A N   1 
ATOM   2247 C CA  A THR A 1 175 ? -3.79800  36.90500  15.04100 0.700 31.88879  ? 505 THR A CA  1 
ATOM   2248 C CA  B THR A 1 175 ? -3.77200  37.26700  14.97800 0.300 33.90814  ? 505 THR A CA  1 
ATOM   2249 C C   A THR A 1 175 ? -3.00300  35.70900  15.53600 0.700 32.19493  ? 505 THR A C   1 
ATOM   2250 C C   B THR A 1 175 ? -2.95400  36.07300  15.45100 0.300 31.98040  ? 505 THR A C   1 
ATOM   2251 O O   A THR A 1 175 ? -3.23400  34.56900  15.11800 0.700 34.24226  ? 505 THR A O   1 
ATOM   2252 O O   B THR A 1 175 ? -3.17500  34.93600  15.01700 0.300 33.95333  ? 505 THR A O   1 
ATOM   2253 C CB  A THR A 1 175 ? -2.92600  37.77600  14.13300 0.700 34.58529  ? 505 THR A CB  1 
ATOM   2254 C CB  B THR A 1 175 ? -2.92200  38.17900  14.08900 0.300 37.46765  ? 505 THR A CB  1 
ATOM   2255 O OG1 A THR A 1 175 ? -3.68400  38.88900  13.63900 0.700 38.76033  ? 505 THR A OG1 1 
ATOM   2256 O OG1 B THR A 1 175 ? -3.70700  39.28600  13.63200 0.300 39.74352  ? 505 THR A OG1 1 
ATOM   2257 C CG2 A THR A 1 175 ? -2.39600  36.95700  12.96600 0.700 34.86482  ? 505 THR A CG2 1 
ATOM   2258 C CG2 B THR A 1 175 ? -2.39800  37.41100  12.88700 0.300 36.18942  ? 505 THR A CG2 1 
ATOM   2259 N N   A ILE A 1 176 ? -2.04000  35.96300  16.42200 0.700 32.01075  ? 506 ILE A N   1 
ATOM   2260 N N   B ILE A 1 176 ? -1.99000  36.32400  16.33900 0.300 32.47202  ? 506 ILE A N   1 
ATOM   2261 C CA  A ILE A 1 176 ? -1.16000  34.90300  16.89700 0.700 29.52234  ? 506 ILE A CA  1 
ATOM   2262 C CA  B ILE A 1 176 ? -1.09200  35.27000  16.79600 0.300 30.86543  ? 506 ILE A CA  1 
ATOM   2263 C C   A ILE A 1 176 ? -1.96000  33.87300  17.68500 0.700 27.60155  ? 506 ILE A C   1 
ATOM   2264 C C   B ILE A 1 176 ? -1.88000  34.21900  17.57100 0.300 28.62122  ? 506 ILE A C   1 
ATOM   2265 O O   A ILE A 1 176 ? -1.73800  32.66100  17.55700 0.700 29.04097  ? 506 ILE A O   1 
ATOM   2266 O O   B ILE A 1 176 ? -1.65800  33.01300  17.41200 0.300 30.07076  ? 506 ILE A O   1 
ATOM   2267 C CB  A ILE A 1 176 ? -0.02500  35.51100  17.73500 0.700 28.64947  ? 506 ILE A CB  1 
ATOM   2268 C CB  B ILE A 1 176 ? 0.04500   35.87000  17.64400 0.300 30.97326  ? 506 ILE A CB  1 
ATOM   2269 C CG1 A ILE A 1 176 ? 0.77000   36.48500  16.86800 0.700 26.95892  ? 506 ILE A CG1 1 
ATOM   2270 C CG1 B ILE A 1 176 ? 0.85300   36.87700  16.82100 0.300 29.84014  ? 506 ILE A CG1 1 
ATOM   2271 C CG2 A ILE A 1 176 ? 0.86200   34.41000  18.30000 0.700 24.24704  ? 506 ILE A CG2 1 
ATOM   2272 C CG2 B ILE A 1 176 ? 0.95500   34.77400  18.17600 0.300 27.14073  ? 506 ILE A CG2 1 
ATOM   2273 C CD1 A ILE A 1 176 ? 1.52700   37.51300  17.64600 0.700 22.68596  ? 506 ILE A CD1 1 
ATOM   2274 C CD1 B ILE A 1 176 ? 1.41900   36.31100  15.54200 0.300 37.44875  ? 506 ILE A CD1 1 
ATOM   2275 N N   A VAL A 1 177 ? -2.89300  34.33900  18.52600 0.700 32.24040  ? 507 VAL A N   1 
ATOM   2276 N N   B VAL A 1 177 ? -2.81400  34.66400  18.41900 0.300 31.45567  ? 507 VAL A N   1 
ATOM   2277 C CA  A VAL A 1 177 ? -3.68600  33.42600  19.35100 0.700 29.04055  ? 507 VAL A CA  1 
ATOM   2278 C CA  B VAL A 1 177 ? -3.60100  33.74200  19.23700 0.300 30.35911  ? 507 VAL A CA  1 
ATOM   2279 C C   A VAL A 1 177 ? -4.54600  32.52600  18.47100 0.700 34.70180  ? 507 VAL A C   1 
ATOM   2280 C C   B VAL A 1 177 ? -4.45600  32.84600  18.34900 0.300 34.72139  ? 507 VAL A C   1 
ATOM   2281 O O   A VAL A 1 177 ? -4.64700  31.31400  18.70600 0.700 42.33077  ? 507 VAL A O   1 
ATOM   2282 O O   B VAL A 1 177 ? -4.52800  31.62900  18.55800 0.300 39.72226  ? 507 VAL A O   1 
ATOM   2283 C CB  A VAL A 1 177 ? -4.53900  34.21800  20.35800 0.700 20.66430  ? 507 VAL A CB  1 
ATOM   2284 C CB  B VAL A 1 177 ? -4.45600  34.52000  20.25400 0.300 22.24923  ? 507 VAL A CB  1 
ATOM   2285 C CG1 A VAL A 1 177 ? -5.49600  33.28900  21.07800 0.700 26.89083  ? 507 VAL A CG1 1 
ATOM   2286 C CG1 B VAL A 1 177 ? -5.41400  33.58300  20.97200 0.300 27.31535  ? 507 VAL A CG1 1 
ATOM   2287 C CG2 A VAL A 1 177 ? -3.64400  34.95000  21.35500 0.700 35.85494  ? 507 VAL A CG2 1 
ATOM   2288 C CG2 B VAL A 1 177 ? -3.56600  35.23600  21.25800 0.300 35.95764  ? 507 VAL A CG2 1 
ATOM   2289 N N   A TRP A 1 178 ? -5.19700  33.10700  17.45500 0.700 39.25288  ? 508 TRP A N   1 
ATOM   2290 N N   B TRP A 1 178 ? -5.10400  33.42800  17.33700 0.300 39.92623  ? 508 TRP A N   1 
ATOM   2291 C CA  A TRP A 1 178 ? -5.98000  32.30600  16.51600 0.700 29.84499  ? 508 TRP A CA  1 
ATOM   2292 C CA  B TRP A 1 178 ? -5.89100  32.62600  16.40200 0.300 32.03607  ? 508 TRP A CA  1 
ATOM   2293 C C   A TRP A 1 178 ? -5.07200  31.38300  15.71500 0.700 31.66770  ? 508 TRP A C   1 
ATOM   2294 C C   B TRP A 1 178 ? -4.99300  31.68700  15.60800 0.300 31.72623  ? 508 TRP A C   1 
ATOM   2295 O O   A TRP A 1 178 ? -5.39000  30.20200  15.52800 0.700 37.50962  ? 508 TRP A O   1 
ATOM   2296 O O   B TRP A 1 178 ? -5.33700  30.51700  15.40600 0.300 37.05679  ? 508 TRP A O   1 
ATOM   2297 C CB  A TRP A 1 178 ? -6.80300  33.20300  15.59000 0.700 34.23388  ? 508 TRP A CB  1 
ATOM   2298 C CB  B TRP A 1 178 ? -6.72500  33.52000  15.48200 0.300 35.29682  ? 508 TRP A CB  1 
ATOM   2299 C CG  A TRP A 1 178 ? -7.72400  34.13600  16.31600 0.700 32.47856  ? 508 TRP A CG  1 
ATOM   2300 C CG  B TRP A 1 178 ? -7.65600  34.45400  16.21700 0.300 34.77374  ? 508 TRP A CG  1 
ATOM   2301 C CD1 A TRP A 1 178 ? -7.93400  35.45800  16.04400 0.700 44.56729  ? 508 TRP A CD1 1 
ATOM   2302 C CD1 B TRP A 1 178 ? -7.87500  35.77200  15.94200 0.300 44.72045  ? 508 TRP A CD1 1 
ATOM   2303 C CD2 A TRP A 1 178 ? -8.58900  33.81000  17.41600 0.700 36.05215  ? 508 TRP A CD2 1 
ATOM   2304 C CD2 B TRP A 1 178 ? -8.51300  34.13000  17.32600 0.300 37.93540  ? 508 TRP A CD2 1 
ATOM   2305 N NE1 A TRP A 1 178 ? -8.85400  35.98100  16.92200 0.700 47.70271  ? 508 TRP A NE1 1 
ATOM   2306 N NE1 B TRP A 1 178 ? -8.79500  36.29300  16.81900 0.300 46.70498  ? 508 TRP A NE1 1 
ATOM   2307 C CE2 A TRP A 1 178 ? -9.27400  34.99000  17.77000 0.700 43.28047  ? 508 TRP A CE2 1 
ATOM   2308 C CE2 B TRP A 1 178 ? -9.20500  35.30600  17.67500 0.300 44.25942  ? 508 TRP A CE2 1 
ATOM   2309 C CE3 A TRP A 1 178 ? -8.84500  32.63900  18.13800 0.700 39.63597  ? 508 TRP A CE3 1 
ATOM   2310 C CE3 B TRP A 1 178 ? -8.75800  32.96200  18.05900 0.300 39.61601  ? 508 TRP A CE3 1 
ATOM   2311 C CZ2 A TRP A 1 178 ? -10.19700 35.03100  18.81200 0.700 44.33656  ? 508 TRP A CZ2 1 
ATOM   2312 C CZ2 B TRP A 1 178 ? -10.12200 35.35000  18.72400 0.300 45.04977  ? 508 TRP A CZ2 1 
ATOM   2313 C CZ3 A TRP A 1 178 ? -9.76100  32.68200  19.17100 0.700 43.70140  ? 508 TRP A CZ3 1 
ATOM   2314 C CZ3 B TRP A 1 178 ? -9.66700  33.00900  19.10000 0.300 43.44246  ? 508 TRP A CZ3 1 
ATOM   2315 C CH2 A TRP A 1 178 ? -10.42700 33.86900  19.49800 0.700 34.61994  ? 508 TRP A CH2 1 
ATOM   2316 C CH2 B TRP A 1 178 ? -10.33900 34.19400  19.42100 0.300 38.01230  ? 508 TRP A CH2 1 
ATOM   2317 N N   A GLY A 1 179 ? -3.93500  31.90600  15.23700 0.700 35.84684  ? 509 GLY A N   1 
ATOM   2318 N N   B GLY A 1 179 ? -3.84800  32.18400  15.13700 0.300 35.67128  ? 509 GLY A N   1 
ATOM   2319 C CA  A GLY A 1 179 ? -3.01900  31.07800  14.47100 0.700 33.62876  ? 509 GLY A CA  1 
ATOM   2320 C CA  B GLY A 1 179 ? -2.94400  31.33100  14.38400 0.300 34.51159  ? 509 GLY A CA  1 
ATOM   2321 C C   A GLY A 1 179 ? -2.49200  29.92500  15.30000 0.700 29.09324  ? 509 GLY A C   1 
ATOM   2322 C C   B GLY A 1 179 ? -2.45100  30.17100  15.22800 0.300 29.94519  ? 509 GLY A C   1 
ATOM   2323 O O   A GLY A 1 179 ? -2.41100  28.79000  14.82300 0.700 36.26443  ? 509 GLY A O   1 
ATOM   2324 O O   B GLY A 1 179 ? -2.35800  29.03800  14.74900 0.300 36.76532  ? 509 GLY A O   1 
ATOM   2325 N N   A THR A 1 180 ? -2.13700  30.19800  16.55900 0.700 32.89992  ? 510 THR A N   1 
ATOM   2326 N N   B THR A 1 180 ? -2.11500  30.44100  16.49200 0.300 33.57090  ? 510 THR A N   1 
ATOM   2327 C CA  A THR A 1 180 ? -1.64000  29.14000  17.43100 0.700 34.74990  ? 510 THR A CA  1 
ATOM   2328 C CA  B THR A 1 180 ? -1.64800  29.38200  17.38100 0.300 34.54966  ? 510 THR A CA  1 
ATOM   2329 C C   A THR A 1 180 ? -2.72400  28.09400  17.63200 0.700 36.70369  ? 510 THR A C   1 
ATOM   2330 C C   B THR A 1 180 ? -2.73900  28.33400  17.57000 0.300 35.84663  ? 510 THR A C   1 
ATOM   2331 O O   A THR A 1 180 ? -2.47100  26.88600  17.54500 0.700 48.58344  ? 510 THR A O   1 
ATOM   2332 O O   B THR A 1 180 ? -2.47600  27.12700  17.50900 0.300 45.66354  ? 510 THR A O   1 
ATOM   2333 C CB  A THR A 1 180 ? -1.21100  29.72300  18.77700 0.700 30.55909  ? 510 THR A CB  1 
ATOM   2334 C CB  B THR A 1 180 ? -1.22000  29.96900  18.72700 0.300 31.09373  ? 510 THR A CB  1 
ATOM   2335 O OG1 A THR A 1 180 ? -0.31400  30.82100  18.56300 0.700 35.42305  ? 510 THR A OG1 1 
ATOM   2336 O OG1 B THR A 1 180 ? -0.29800  31.04500  18.51200 0.300 35.55003  ? 510 THR A OG1 1 
ATOM   2337 C CG2 A THR A 1 180 ? -0.52700  28.66200  19.62400 0.700 28.73452  ? 510 THR A CG2 1 
ATOM   2338 C CG2 B THR A 1 180 ? -0.55400  28.90300  19.58700 0.300 29.01756  ? 510 THR A CG2 1 
ATOM   2339 N N   A THR A 1 181 ? -3.94600  28.55300  17.91600 0.700 31.12292  ? 511 THR A N   1 
ATOM   2340 N N   B THR A 1 181 ? -3.97500  28.78400  17.82200 0.300 31.87752  ? 511 THR A N   1 
ATOM   2341 C CA  A THR A 1 181 ? -5.06300  27.63700  18.11300 0.700 27.84108  ? 511 THR A CA  1 
ATOM   2342 C CA  B THR A 1 181 ? -5.08900  27.85600  18.00400 0.300 28.59989  ? 511 THR A CA  1 
ATOM   2343 C C   A THR A 1 181 ? -5.29200  26.80000  16.86300 0.700 39.19357  ? 511 THR A C   1 
ATOM   2344 C C   B THR A 1 181 ? -5.27600  26.99500  16.76300 0.300 38.92808  ? 511 THR A C   1 
ATOM   2345 O O   A THR A 1 181 ? -5.51300  25.58500  16.95000 0.700 41.31207  ? 511 THR A O   1 
ATOM   2346 O O   B THR A 1 181 ? -5.52500  25.78700  16.86300 0.300 41.23838  ? 511 THR A O   1 
ATOM   2347 C CB  A THR A 1 181 ? -6.32700  28.41100  18.48600 0.700 24.13289  ? 511 THR A CB  1 
ATOM   2348 C CB  B THR A 1 181 ? -6.38400  28.61400  18.30900 0.300 26.02101  ? 511 THR A CB  1 
ATOM   2349 O OG1 A THR A 1 181 ? -6.08100  29.19100  19.66500 0.700 25.32697  ? 511 THR A OG1 1 
ATOM   2350 O OG1 B THR A 1 181 ? -6.62200  29.58800  17.28700 0.300 45.01240  ? 511 THR A OG1 1 
ATOM   2351 C CG2 A THR A 1 181 ? -7.48400  27.45500  18.73700 0.700 19.04520  ? 511 THR A CG2 1 
ATOM   2352 C CG2 B THR A 1 181 ? -6.31000  29.30900  19.65200 0.300 25.42839  ? 511 THR A CG2 1 
ATOM   2353 N N   A ALA A 1 182 ? -5.21500  27.43700  15.68800 0.700 43.23563  ? 512 ALA A N   1 
ATOM   2354 N N   B ALA A 1 182 ? -5.17300  27.61100  15.58200 0.300 42.34442  ? 512 ALA A N   1 
ATOM   2355 C CA  A ALA A 1 182 ? -5.35100  26.71200  14.42800 0.700 38.17687  ? 512 ALA A CA  1 
ATOM   2356 C CA  B ALA A 1 182 ? -5.26400  26.86700  14.33000 0.300 37.85535  ? 512 ALA A CA  1 
ATOM   2357 C C   A ALA A 1 182 ? -4.28100  25.63900  14.30200 0.700 34.66534  ? 512 ALA A C   1 
ATOM   2358 C C   B ALA A 1 182 ? -4.17800  25.80300  14.24600 0.300 35.18283  ? 512 ALA A C   1 
ATOM   2359 O O   A ALA A 1 182 ? -4.57600  24.50100  13.91500 0.700 43.16907  ? 512 ALA A O   1 
ATOM   2360 O O   B ALA A 1 182 ? -4.44500  24.66600  13.84000 0.300 42.11441  ? 512 ALA A O   1 
ATOM   2361 C CB  A ALA A 1 182 ? -5.27500  27.68500  13.25200 0.700 34.23445  ? 512 ALA A CB  1 
ATOM   2362 C CB  B ALA A 1 182 ? -5.17500  27.82500  13.14300 0.300 34.70916  ? 512 ALA A CB  1 
ATOM   2363 N N   A ALA A 1 183 ? -3.03200  25.97800  14.63700 0.700 36.12535  ? 513 ALA A N   1 
ATOM   2364 N N   B ALA A 1 183 ? -2.94300  26.15700  14.61100 0.300 36.60726  ? 513 ALA A N   1 
ATOM   2365 C CA  A ALA A 1 183 ? -1.95200  25.00100  14.54800 0.700 32.84752  ? 513 ALA A CA  1 
ATOM   2366 C CA  B ALA A 1 183 ? -1.85800  25.18300  14.56000 0.300 34.22491  ? 513 ALA A CA  1 
ATOM   2367 C C   A ALA A 1 183 ? -2.20200  23.83600  15.49500 0.700 37.77423  ? 513 ALA A C   1 
ATOM   2368 C C   B ALA A 1 183 ? -2.12900  24.02500  15.51100 0.300 37.38380  ? 513 ALA A C   1 
ATOM   2369 O O   A ALA A 1 183 ? -1.90800  22.68000  15.16500 0.700 43.80510  ? 513 ALA A O   1 
ATOM   2370 O O   B ALA A 1 183 ? -1.80100  22.87100  15.20800 0.300 43.55080  ? 513 ALA A O   1 
ATOM   2371 C CB  A ALA A 1 183 ? -0.61100  25.66900  14.85400 0.700 40.05397  ? 513 ALA A CB  1 
ATOM   2372 C CB  B ALA A 1 183 ? -0.52900  25.85800  14.89800 0.300 40.46278  ? 513 ALA A CB  1 
ATOM   2373 N N   A LEU A 1 184 ? -2.77100  24.12000  16.66800 0.700 40.11464  ? 514 LEU A N   1 
ATOM   2374 N N   B LEU A 1 184 ? -2.73000  24.31300  16.66700 0.300 39.49432  ? 514 LEU A N   1 
ATOM   2375 C CA  A LEU A 1 184 ? -3.06000  23.07400  17.64300 0.700 39.37289  ? 514 LEU A CA  1 
ATOM   2376 C CA  B LEU A 1 184 ? -3.03500  23.26300  17.62900 0.300 39.38514  ? 514 LEU A CA  1 
ATOM   2377 C C   A LEU A 1 184 ? -4.24600  22.21400  17.21800 0.700 39.24157  ? 514 LEU A C   1 
ATOM   2378 C C   B LEU A 1 184 ? -4.20300  22.40200  17.17200 0.300 39.60403  ? 514 LEU A C   1 
ATOM   2379 O O   A LEU A 1 184 ? -4.38600  21.08500  17.70100 0.700 48.01278  ? 514 LEU A O   1 
ATOM   2380 O O   B LEU A 1 184 ? -4.33700  21.26100  17.62800 0.300 46.38192  ? 514 LEU A O   1 
ATOM   2381 C CB  A LEU A 1 184 ? -3.34800  23.71200  19.00200 0.700 35.09780  ? 514 LEU A CB  1 
ATOM   2382 C CB  B LEU A 1 184 ? -3.35800  23.88200  18.99000 0.300 35.44852  ? 514 LEU A CB  1 
ATOM   2383 C CG  A LEU A 1 184 ? -2.16800  24.29200  19.77900 0.700 29.53488  ? 514 LEU A CG  1 
ATOM   2384 C CG  B LEU A 1 184 ? -2.23900  24.47100  19.84800 0.300 29.73391  ? 514 LEU A CG  1 
ATOM   2385 C CD1 A LEU A 1 184 ? -2.67900  25.12600  20.94000 0.700 33.69044  ? 514 LEU A CD1 1 
ATOM   2386 C CD1 B LEU A 1 184 ? -2.83200  25.27000  20.99400 0.300 34.12562  ? 514 LEU A CD1 1 
ATOM   2387 C CD2 A LEU A 1 184 ? -1.27600  23.17100  20.28600 0.700 34.60209  ? 514 LEU A CD2 1 
ATOM   2388 C CD2 B LEU A 1 184 ? -1.36400  23.35600  20.38700 0.300 34.50120  ? 514 LEU A CD2 1 
ATOM   2389 N N   A SER A 1 185 ? -5.10800  22.73600  16.34600 0.700 42.29516  ? 515 SER A N   1 
ATOM   2390 N N   B SER A 1 185 ? -5.04700  22.92500  16.28600 0.300 42.57052  ? 515 SER A N   1 
ATOM   2391 C CA  A SER A 1 185 ? -6.34000  22.08500  15.93100 0.700 35.77299  ? 515 SER A CA  1 
ATOM   2392 C CA  B SER A 1 185 ? -6.25900  22.25600  15.84800 0.300 36.91010  ? 515 SER A CA  1 
ATOM   2393 C C   A SER A 1 185 ? -6.13100  21.25600  14.66400 0.700 46.10568  ? 515 SER A C   1 
ATOM   2394 C C   B SER A 1 185 ? -5.99700  21.44100  14.58300 0.300 44.92148  ? 515 SER A C   1 
ATOM   2395 O O   A SER A 1 185 ? -5.02600  21.14800  14.12400 0.700 40.95711  ? 515 SER A O   1 
ATOM   2396 O O   B SER A 1 185 ? -4.87500  21.36100  14.07800 0.300 41.08699  ? 515 SER A O   1 
ATOM   2397 C CB  A SER A 1 185 ? -7.44300  23.11800  15.70900 0.700 41.16504  ? 515 SER A CB  1 
ATOM   2398 C CB  B SER A 1 185 ? -7.37100  23.27700  15.60800 0.300 42.23429  ? 515 SER A CB  1 
ATOM   2399 O OG  A SER A 1 185 ? -7.73000  23.82000  16.90100 0.700 49.12144  ? 515 SER A OG  1 
ATOM   2400 O OG  B SER A 1 185 ? -7.69500  23.97900  16.79400 0.300 48.20901  ? 515 SER A OG  1 
ATOM   2401 N N   A LYS A 1 186 ? -7.22700  20.66900  14.18400 0.700 52.48416  ? 516 LYS A N   1 
ATOM   2402 N N   B LYS A 1 186 ? -7.05700  20.82300  14.07000 0.300 50.97829  ? 516 LYS A N   1 
ATOM   2403 C CA  A LYS A 1 186 ? -7.24800  19.85500  12.97700 0.700 49.33062  ? 516 LYS A CA  1 
ATOM   2404 C CA  B LYS A 1 186 ? -6.99900  20.02500  12.85600 0.300 50.72482  ? 516 LYS A CA  1 
ATOM   2405 C C   A LYS A 1 186 ? -8.53500  20.13900  12.21700 0.700 49.58819  ? 516 LYS A C   1 
ATOM   2406 C C   B LYS A 1 186 ? -8.28300  20.27300  12.07600 0.300 51.22687  ? 516 LYS A C   1 
ATOM   2407 O O   A LYS A 1 186 ? -9.49500  20.68300  12.76900 0.700 54.25820  ? 516 LYS A O   1 
ATOM   2408 O O   B LYS A 1 186 ? -9.26800  20.77600  12.62200 0.300 53.10113  ? 516 LYS A O   1 
ATOM   2409 C CB  A LYS A 1 186 ? -7.16700  18.35000  13.27300 0.700 47.94065  ? 516 LYS A CB  1 
ATOM   2410 C CB  B LYS A 1 186 ? -6.81800  18.53100  13.16100 0.300 49.46312  ? 516 LYS A CB  1 
ATOM   2411 C CG  A LYS A 1 186 ? -5.80200  17.82900  13.68000 0.700 53.20722  ? 516 LYS A CG  1 
ATOM   2412 C CG  B LYS A 1 186 ? -6.12100  17.74700  12.05700 0.300 53.80957  ? 516 LYS A CG  1 
ATOM   2413 C CD  A LYS A 1 186 ? -5.65100  16.38900  13.20200 0.700 50.25103  ? 516 LYS A CD  1 
ATOM   2414 C CD  B LYS A 1 186 ? -5.31700  16.58800  12.62600 0.300 51.03859  ? 516 LYS A CD  1 
ATOM   2415 C CE  A LYS A 1 186 ? -4.30700  15.79800  13.57900 0.700 54.61447  ? 516 LYS A CE  1 
ATOM   2416 C CE  B LYS A 1 186 ? -3.95400  16.48500  11.95900 0.300 48.47089  ? 516 LYS A CE  1 
ATOM   2417 N NZ  A LYS A 1 186 ? -3.36200  15.68500  12.42800 0.700 56.66391  ? 516 LYS A NZ  1 
ATOM   2418 N NZ  B LYS A 1 186 ? -3.36300  15.12700  12.10100 0.300 56.37569  ? 516 LYS A NZ  1 
ATOM   2419 N N   A GLY A 1 187 ? -8.55000  19.73300  10.94700 0.700 45.42210  ? 517 GLY A N   1 
ATOM   2420 N N   B GLY A 1 187 ? -8.26900  19.89600  10.79800 0.300 48.78265  ? 517 GLY A N   1 
ATOM   2421 C CA  A GLY A 1 187 ? -9.78700  19.73000  10.18500 0.700 47.67529  ? 517 GLY A CA  1 
ATOM   2422 C CA  B GLY A 1 187 ? -9.50000  19.86800  10.02200 0.300 48.88609  ? 517 GLY A CA  1 
ATOM   2423 C C   A GLY A 1 187 ? -10.42300 21.10400  10.15300 0.700 48.75341  ? 517 GLY A C   1 
ATOM   2424 C C   B GLY A 1 187 ? -10.17900 21.22400  10.01600 0.300 50.49855  ? 517 GLY A C   1 
ATOM   2425 O O   A GLY A 1 187 ? -9.75300  22.12600  9.96100  0.700 50.93287  ? 517 GLY A O   1 
ATOM   2426 O O   B GLY A 1 187 ? -9.53500  22.26900  9.87400  0.300 52.26541  ? 517 GLY A O   1 
ATOM   2427 N N   A TYR A 1 188 ? -11.74700 21.13200  10.32600 0.700 54.07672  ? 518 TYR A N   1 
ATOM   2428 N N   B TYR A 1 188 ? -11.50500 21.21200  10.17300 0.300 54.03796  ? 518 TYR A N   1 
ATOM   2429 C CA  A TYR A 1 188 ? -12.49500 22.36600  10.11800 0.700 53.68534  ? 518 TYR A CA  1 
ATOM   2430 C CA  B TYR A 1 188 ? -12.27900 22.43600  9.98500  0.300 53.44793  ? 518 TYR A CA  1 
ATOM   2431 C C   A TYR A 1 188 ? -12.22800 23.36700  11.23600 0.700 53.22823  ? 518 TYR A C   1 
ATOM   2432 C C   B TYR A 1 188 ? -12.05100 23.41700  11.12900 0.300 52.83502  ? 518 TYR A C   1 
ATOM   2433 O O   A TYR A 1 188 ? -12.30100 24.58200  11.01300 0.700 55.37175  ? 518 TYR A O   1 
ATOM   2434 O O   B TYR A 1 188 ? -12.16300 24.63300  10.93400 0.300 54.55533  ? 518 TYR A O   1 
ATOM   2435 C CB  A TYR A 1 188 ? -13.98800 22.05500  10.00000 0.700 53.38644  ? 518 TYR A CB  1 
ATOM   2436 C CB  B TYR A 1 188 ? -13.76400 22.09900  9.83200  0.300 53.63377  ? 518 TYR A CB  1 
ATOM   2437 C CG  A TYR A 1 188 ? -14.32600 21.21900  8.78000  0.700 63.73152  ? 518 TYR A CG  1 
ATOM   2438 C CG  B TYR A 1 188 ? -14.43100 21.58700  11.09000 0.300 46.78981  ? 518 TYR A CG  1 
ATOM   2439 C CD1 A TYR A 1 188 ? -14.18800 19.83600  8.80000  0.700 72.99202  ? 518 TYR A CD1 1 
ATOM   2440 C CD1 B TYR A 1 188 ? -15.01300 22.46000  12.00200 0.300 43.41884  ? 518 TYR A CD1 1 
ATOM   2441 C CD2 A TYR A 1 188 ? -14.77300 21.81600  7.60600  0.700 67.60877  ? 518 TYR A CD2 1 
ATOM   2442 C CD2 B TYR A 1 188 ? -14.50000 20.22500  11.35200 0.300 38.57654  ? 518 TYR A CD2 1 
ATOM   2443 C CE1 A TYR A 1 188 ? -14.48300 19.07100  7.68400  0.700 89.77916  ? 518 TYR A CE1 1 
ATOM   2444 C CE1 B TYR A 1 188 ? -15.62900 21.99000  13.14700 0.300 33.19208  ? 518 TYR A CE1 1 
ATOM   2445 C CE2 A TYR A 1 188 ? -15.07700 21.05800  6.48700  0.700 54.24713  ? 518 TYR A CE2 1 
ATOM   2446 C CE2 B TYR A 1 188 ? -15.12000 19.74600  12.48900 0.300 31.33996  ? 518 TYR A CE2 1 
ATOM   2447 C CZ  A TYR A 1 188 ? -14.92900 19.68600  6.53200  0.700 84.65121  ? 518 TYR A CZ  1 
ATOM   2448 C CZ  B TYR A 1 188 ? -15.68100 20.63300  13.38300 0.300 27.50785  ? 518 TYR A CZ  1 
ATOM   2449 O OH  A TYR A 1 188 ? -15.23500 18.92400  5.42600  0.700 80.07236  ? 518 TYR A OH  1 
ATOM   2450 O OH  B TYR A 1 188 ? -16.28800 20.15800  14.52300 0.300 30.90990  ? 518 TYR A OH  1 
ATOM   2451 N N   A VAL A 1 189 ? -11.91500 22.87600  12.43600 0.700 51.51296  ? 519 VAL A N   1 
ATOM   2452 N N   B VAL A 1 189 ? -11.74300 22.90700  12.32500 0.300 51.20207  ? 519 VAL A N   1 
ATOM   2453 C CA  A VAL A 1 189 ? -11.57900 23.75800  13.55000 0.700 44.72917  ? 519 VAL A CA  1 
ATOM   2454 C CA  B VAL A 1 189 ? -11.44300 23.76800  13.46700 0.300 45.15640  ? 519 VAL A CA  1 
ATOM   2455 C C   A VAL A 1 189 ? -10.32800 24.56100  13.22100 0.700 46.53876  ? 519 VAL A C   1 
ATOM   2456 C C   B VAL A 1 189 ? -10.20600 24.60600  13.17600 0.300 47.10740  ? 519 VAL A C   1 
ATOM   2457 O O   A VAL A 1 189 ? -10.26400 25.77300  13.46300 0.700 55.25956  ? 519 VAL A O   1 
ATOM   2458 O O   B VAL A 1 189 ? -10.16500 25.81000  13.46200 0.300 54.89855  ? 519 VAL A O   1 
ATOM   2459 C CB  A VAL A 1 189 ? -11.41100 22.94100  14.84400 0.700 48.36541  ? 519 VAL A CB  1 
ATOM   2460 C CB  B VAL A 1 189 ? -11.27100 22.92800  14.74500 0.300 48.40539  ? 519 VAL A CB  1 
ATOM   2461 C CG1 A VAL A 1 189 ? -11.08800 23.85800  16.01200 0.700 46.26600  ? 519 VAL A CG1 1 
ATOM   2462 C CG1 B VAL A 1 189 ? -10.98700 23.83100  15.93500 0.300 46.54421  ? 519 VAL A CG1 1 
ATOM   2463 C CG2 A VAL A 1 189 ? -12.66800 22.13900  15.12000 0.700 49.43762  ? 519 VAL A CG2 1 
ATOM   2464 C CG2 B VAL A 1 189 ? -12.50800 22.08100  14.99100 0.300 49.84714  ? 519 VAL A CG2 1 
ATOM   2465 N N   A ARG A 1 190 ? -9.31200  23.89300  12.66800 0.700 46.43850  ? 520 ARG A N   1 
ATOM   2466 N N   B ARG A 1 190 ? -9.17600  23.97300  12.61300 0.300 46.07592  ? 520 ARG A N   1 
ATOM   2467 C CA  A ARG A 1 190 ? -8.11200  24.58900  12.21600 0.700 42.33995  ? 520 ARG A CA  1 
ATOM   2468 C CA  B ARG A 1 190 ? -7.97700  24.68700  12.19000 0.300 42.58542  ? 520 ARG A CA  1 
ATOM   2469 C C   A ARG A 1 190 ? -8.45800  25.66400  11.19200 0.700 48.27325  ? 520 ARG A C   1 
ATOM   2470 C C   B ARG A 1 190 ? -8.33000  25.78900  11.19900 0.300 48.41937  ? 520 ARG A C   1 
ATOM   2471 O O   A ARG A 1 190 ? -7.91000  26.77200  11.23600 0.700 50.20361  ? 520 ARG A O   1 
ATOM   2472 O O   B ARG A 1 190 ? -7.80000  26.90400  11.28200 0.300 49.29524  ? 520 ARG A O   1 
ATOM   2473 C CB  A ARG A 1 190 ? -7.11000  23.58300  11.65100 0.700 44.81267  ? 520 ARG A CB  1 
ATOM   2474 C CB  B ARG A 1 190 ? -6.98900  23.68800  11.58800 0.300 44.63175  ? 520 ARG A CB  1 
ATOM   2475 C CG  A ARG A 1 190 ? -5.96000  24.20100  10.89000 0.700 41.39843  ? 520 ARG A CG  1 
ATOM   2476 C CG  B ARG A 1 190 ? -5.81100  24.26800  10.83900 0.300 42.12613  ? 520 ARG A CG  1 
ATOM   2477 C CD  A ARG A 1 190 ? -5.00400  23.12400  10.42500 0.700 52.38832  ? 520 ARG A CD  1 
ATOM   2478 C CD  B ARG A 1 190 ? -4.93100  23.12300  10.36400 0.300 52.80986  ? 520 ARG A CD  1 
ATOM   2479 N NE  A ARG A 1 190 ? -4.25400  22.57100  11.54800 0.700 43.61699  ? 520 ARG A NE  1 
ATOM   2480 N NE  B ARG A 1 190 ? -4.22200  22.49500  11.47400 0.300 44.34074  ? 520 ARG A NE  1 
ATOM   2481 C CZ  A ARG A 1 190 ? -3.35000  21.60700  11.44500 0.700 48.59356  ? 520 ARG A CZ  1 
ATOM   2482 C CZ  B ARG A 1 190 ? -3.39500  21.46600  11.35100 0.300 49.56837  ? 520 ARG A CZ  1 
ATOM   2483 N NH1 A ARG A 1 190 ? -3.04600  21.06800  10.27600 0.700 71.20005  ? 520 ARG A NH1 1 
ATOM   2484 N NH1 B ARG A 1 190 ? -3.13700  20.92300  10.17200 0.300 71.11324  ? 520 ARG A NH1 1 
ATOM   2485 N NH2 A ARG A 1 190 ? -2.73500  21.17300  12.54300 0.700 43.99278  ? 520 ARG A NH2 1 
ATOM   2486 N NH2 B ARG A 1 190 ? -2.80900  20.97200  12.43700 0.300 45.25299  ? 520 ARG A NH2 1 
ATOM   2487 N N   A VAL A 1 191 ? -9.34900  25.34800  10.24900 0.700 55.14393  ? 521 VAL A N   1 
ATOM   2488 N N   B VAL A 1 191 ? -9.22000  25.49100  10.25000 0.300 54.55686  ? 521 VAL A N   1 
ATOM   2489 C CA  A VAL A 1 191 ? -9.60000  26.26100  9.13900  0.700 51.61611  ? 521 VAL A CA  1 
ATOM   2490 C CA  B VAL A 1 191 ? -9.49900  26.41200  9.15200  0.300 51.66317  ? 521 VAL A CA  1 
ATOM   2491 C C   A VAL A 1 191 ? -10.25100 27.53700  9.65500  0.700 47.91216  ? 521 VAL A C   1 
ATOM   2492 C C   B VAL A 1 191 ? -10.16400 27.67600  9.68600  0.300 47.95179  ? 521 VAL A C   1 
ATOM   2493 O O   A VAL A 1 191 ? -9.89200  28.64800  9.24500  0.700 54.04698  ? 521 VAL A O   1 
ATOM   2494 O O   B VAL A 1 191 ? -9.82800  28.79400  9.27400  0.300 53.34378  ? 521 VAL A O   1 
ATOM   2495 C CB  A VAL A 1 191 ? -10.46900 25.58300  8.06500  0.700 45.38499  ? 521 VAL A CB  1 
ATOM   2496 C CB  B VAL A 1 191 ? -10.36300 25.72100  8.08100  0.300 45.96775  ? 521 VAL A CB  1 
ATOM   2497 C CG1 A VAL A 1 191 ? -10.87300 26.59400  7.00700  0.700 42.68228  ? 521 VAL A CG1 1 
ATOM   2498 C CG1 B VAL A 1 191 ? -10.81200 26.72300  7.02800  0.300 42.99930  ? 521 VAL A CG1 1 
ATOM   2499 C CG2 A VAL A 1 191 ? -9.73500  24.40900  7.44500  0.700 50.74286  ? 521 VAL A CG2 1 
ATOM   2500 C CG2 B VAL A 1 191 ? -9.59800  24.57400  7.44100  0.300 51.45933  ? 521 VAL A CG2 1 
ATOM   2501 N N   A ILE A 1 192 ? -11.22500 27.39500  10.55700 0.700 43.07944  ? 522 ILE A N   1 
ATOM   2502 N N   B ILE A 1 192 ? -11.12200 27.51900  10.60500 0.300 43.91815  ? 522 ILE A N   1 
ATOM   2503 C CA  A ILE A 1 192 ? -11.94900 28.55200  11.07800 0.700 49.91577  ? 522 ILE A CA  1 
ATOM   2504 C CA  B ILE A 1 192 ? -11.85800 28.66200  11.14200 0.300 49.30059  ? 522 ILE A CA  1 
ATOM   2505 C C   A ILE A 1 192 ? -10.99800 29.48400  11.81800 0.700 51.02599  ? 522 ILE A C   1 
ATOM   2506 C C   B ILE A 1 192 ? -10.90600 29.61600  11.85400 0.300 50.33481  ? 522 ILE A C   1 
ATOM   2507 O O   A ILE A 1 192 ? -10.94600 30.69000  11.54700 0.700 50.22191  ? 522 ILE A O   1 
ATOM   2508 O O   B ILE A 1 192 ? -10.90000 30.82500  11.59500 0.300 49.47011  ? 522 ILE A O   1 
ATOM   2509 C CB  A ILE A 1 192 ? -13.10100 28.09500  11.98800 0.700 39.92341  ? 522 ILE A CB  1 
ATOM   2510 C CB  B ILE A 1 192 ? -12.98300 28.18600  12.07900 0.300 40.37729  ? 522 ILE A CB  1 
ATOM   2511 C CG1 A ILE A 1 192 ? -14.13100 27.30800  11.17600 0.700 36.56145  ? 522 ILE A CG1 1 
ATOM   2512 C CG1 B ILE A 1 192 ? -14.02500 27.37500  11.30500 0.300 36.90010  ? 522 ILE A CG1 1 
ATOM   2513 C CG2 A ILE A 1 192 ? -13.74700 29.30600  12.63700 0.700 33.63488  ? 522 ILE A CG2 1 
ATOM   2514 C CG2 B ILE A 1 192 ? -13.63100 29.36900  12.78400 0.300 34.48224  ? 522 ILE A CG2 1 
ATOM   2515 C CD1 A ILE A 1 192 ? -15.17000 26.60500  12.01800 0.700 41.84841  ? 522 ILE A CD1 1 
ATOM   2516 C CD1 B ILE A 1 192 ? -15.03000 26.67100  12.19400 0.300 41.81897  ? 522 ILE A CD1 1 
ATOM   2517 N N   A PHE A 1 193 ? -10.22600 28.93600  12.76100 0.700 49.30851  ? 523 PHE A N   1 
ATOM   2518 N N   B PHE A 1 193 ? -10.09300 29.08500  12.77300 0.300 49.06143  ? 523 PHE A N   1 
ATOM   2519 C CA  A PHE A 1 193 ? -9.33100  29.77100  13.55700 0.700 45.48641  ? 523 PHE A CA  1 
ATOM   2520 C CA  B PHE A 1 193 ? -9.18400  29.93200  13.54000 0.300 45.08784  ? 523 PHE A CA  1 
ATOM   2521 C C   A PHE A 1 193 ? -8.27700  30.42900  12.68200 0.700 43.32432  ? 523 PHE A C   1 
ATOM   2522 C C   B PHE A 1 193 ? -8.17000  30.60500  12.62500 0.300 43.71834  ? 523 PHE A C   1 
ATOM   2523 O O   A PHE A 1 193 ? -7.89700  31.58300  12.91500 0.700 51.08800  ? 523 PHE A O   1 
ATOM   2524 O O   B PHE A 1 193 ? -7.77500  31.75300  12.86200 0.300 50.14888  ? 523 PHE A O   1 
ATOM   2525 C CB  A PHE A 1 193 ? -8.68800  28.95300  14.67400 0.700 35.55364  ? 523 PHE A CB  1 
ATOM   2526 C CB  B PHE A 1 193 ? -8.48000  29.11600  14.62400 0.300 37.48610  ? 523 PHE A CB  1 
ATOM   2527 C CG  A PHE A 1 193 ? -9.61600  28.67000  15.81900 0.700 35.58713  ? 523 PHE A CG  1 
ATOM   2528 C CG  B PHE A 1 193 ? -9.35400  28.79900  15.80300 0.300 38.19776  ? 523 PHE A CG  1 
ATOM   2529 C CD1 A PHE A 1 193 ? -10.07700 29.70600  16.61600 0.700 40.05232  ? 523 PHE A CD1 1 
ATOM   2530 C CD1 B PHE A 1 193 ? -9.80400  29.81000  16.63600 0.300 41.04286  ? 523 PHE A CD1 1 
ATOM   2531 C CD2 A PHE A 1 193 ? -10.01400 27.38000  16.11100 0.700 36.66078  ? 523 PHE A CD2 1 
ATOM   2532 C CD2 B PHE A 1 193 ? -9.72600  27.49600  16.07800 0.300 37.56858  ? 523 PHE A CD2 1 
ATOM   2533 C CE1 A PHE A 1 193 ? -10.92600 29.45900  17.67500 0.700 37.49292  ? 523 PHE A CE1 1 
ATOM   2534 C CE1 B PHE A 1 193 ? -10.60900 29.52600  17.72300 0.300 39.65570  ? 523 PHE A CE1 1 
ATOM   2535 C CE2 A PHE A 1 193 ? -10.86200 27.12500  17.17000 0.700 41.77263  ? 523 PHE A CE2 1 
ATOM   2536 C CE2 B PHE A 1 193 ? -10.53000 27.20600  17.16200 0.300 42.58580  ? 523 PHE A CE2 1 
ATOM   2537 C CZ  A PHE A 1 193 ? -11.31900 28.16500  17.95300 0.700 48.84011  ? 523 PHE A CZ  1 
ATOM   2538 C CZ  B PHE A 1 193 ? -10.97200 28.22200  17.98600 0.300 47.74820  ? 523 PHE A CZ  1 
ATOM   2539 N N   A PHE A 1 194 ? -7.80200  29.71700  11.66200 0.700 45.83379  ? 524 PHE A N   1 
ATOM   2540 N N   B PHE A 1 194 ? -7.72600  29.89800  11.58400 0.300 46.77535  ? 524 PHE A N   1 
ATOM   2541 C CA  A PHE A 1 194 ? -6.89700  30.32700  10.69600 0.700 46.76926  ? 524 PHE A CA  1 
ATOM   2542 C CA  B PHE A 1 194 ? -6.86500  30.51600  10.58100 0.300 47.67653  ? 524 PHE A CA  1 
ATOM   2543 C C   A PHE A 1 194 ? -7.54600  31.53500  10.03000 0.700 55.10734  ? 524 PHE A C   1 
ATOM   2544 C C   B PHE A 1 194 ? -7.56100  31.71400  9.94600  0.300 54.57421  ? 524 PHE A C   1 
ATOM   2545 O O   A PHE A 1 194 ? -6.92100  32.59400  9.89800  0.700 65.01681  ? 524 PHE A O   1 
ATOM   2546 O O   B PHE A 1 194 ? -6.95900  32.78200  9.78300  0.300 61.52619  ? 524 PHE A O   1 
ATOM   2547 C CB  A PHE A 1 194 ? -6.46000  29.30900  9.64500  0.700 48.97636  ? 524 PHE A CB  1 
ATOM   2548 C CB  B PHE A 1 194 ? -6.46400  29.49600  9.51600  0.300 49.48752  ? 524 PHE A CB  1 
ATOM   2549 C CG  A PHE A 1 194 ? -5.50900  29.87300  8.62600  0.700 53.47389  ? 524 PHE A CG  1 
ATOM   2550 C CG  B PHE A 1 194 ? -5.55700  30.05700  8.45700  0.300 54.29365  ? 524 PHE A CG  1 
ATOM   2551 C CD1 A PHE A 1 194 ? -4.15000  29.93900  8.89100  0.700 54.52994  ? 524 PHE A CD1 1 
ATOM   2552 C CD1 B PHE A 1 194 ? -4.18400  30.04800  8.63400  0.300 55.22172  ? 524 PHE A CD1 1 
ATOM   2553 C CD2 A PHE A 1 194 ? -5.97400  30.35700  7.41200  0.700 53.82513  ? 524 PHE A CD2 1 
ATOM   2554 C CD2 B PHE A 1 194 ? -6.07500  30.60000  7.29200  0.300 55.05119  ? 524 PHE A CD2 1 
ATOM   2555 C CE1 A PHE A 1 194 ? -3.27200  30.46600  7.96100  0.700 52.73651  ? 524 PHE A CE1 1 
ATOM   2556 C CE1 B PHE A 1 194 ? -3.34300  30.56800  7.67000  0.300 55.20495  ? 524 PHE A CE1 1 
ATOM   2557 C CE2 A PHE A 1 194 ? -5.10000  30.88700  6.47900  0.700 58.44225  ? 524 PHE A CE2 1 
ATOM   2558 C CE2 B PHE A 1 194 ? -5.23800  31.12200  6.32400  0.300 60.25726  ? 524 PHE A CE2 1 
ATOM   2559 C CZ  A PHE A 1 194 ? -3.74600  30.94000  6.75500  0.700 57.71571  ? 524 PHE A CZ  1 
ATOM   2560 C CZ  B PHE A 1 194 ? -3.87200  31.10700  6.51500  0.300 60.44997  ? 524 PHE A CZ  1 
ATOM   2561 N N   A LEU A 1 195 ? -8.80600  31.39800  9.60400  0.700 51.83983  ? 525 LEU A N   1 
ATOM   2562 N N   B LEU A 1 195 ? -8.83300  31.55000  9.57200  0.300 51.65664  ? 525 LEU A N   1 
ATOM   2563 C CA  A LEU A 1 195 ? -9.46100  32.50100  8.90800  0.700 49.12168  ? 525 LEU A CA  1 
ATOM   2564 C CA  B LEU A 1 195 ? -9.55300  32.63900  8.92200  0.300 49.05188  ? 525 LEU A CA  1 
ATOM   2565 C C   A LEU A 1 195 ? -9.66100  33.70400  9.82400  0.700 50.30613  ? 525 LEU A C   1 
ATOM   2566 C C   B LEU A 1 195 ? -9.74400  33.80600  9.88300  0.300 50.18488  ? 525 LEU A C   1 
ATOM   2567 O O   A LEU A 1 195 ? -9.48900  34.85000  9.38800  0.700 55.00831  ? 525 LEU A O   1 
ATOM   2568 O O   B LEU A 1 195 ? -9.64600  34.97000  9.47800  0.300 54.07692  ? 525 LEU A O   1 
ATOM   2569 C CB  A LEU A 1 195 ? -10.79300 32.03000  8.32900  0.700 55.56571  ? 525 LEU A CB  1 
ATOM   2570 C CB  B LEU A 1 195 ? -10.90000 32.14300  8.39800  0.300 55.10593  ? 525 LEU A CB  1 
ATOM   2571 C CG  A LEU A 1 195 ? -10.64900 31.06700  7.15100  0.700 57.21384  ? 525 LEU A CG  1 
ATOM   2572 C CG  B LEU A 1 195 ? -10.84300 31.19700  7.19700  0.300 57.36084  ? 525 LEU A CG  1 
ATOM   2573 C CD1 A LEU A 1 195 ? -12.01200 30.56900  6.69400  0.700 55.72010  ? 525 LEU A CD1 1 
ATOM   2574 C CD1 B LEU A 1 195 ? -12.23400 30.70200  6.83600  0.300 56.77775  ? 525 LEU A CD1 1 
ATOM   2575 C CD2 A LEU A 1 195 ? -9.88700  31.72600  6.01000  0.700 55.77543  ? 525 LEU A CD2 1 
ATOM   2576 C CD2 B LEU A 1 195 ? -10.18300 31.87500  6.00600  0.300 56.60336  ? 525 LEU A CD2 1 
ATOM   2577 N N   A MET A 1 196 ? -10.02900 33.48000  11.09100 0.700 46.80428  ? 526 MET A N   1 
ATOM   2578 N N   B MET A 1 196 ? -10.02800 33.51400  11.15600 0.300 46.98038  ? 526 MET A N   1 
ATOM   2579 C CA  A MET A 1 196 ? -10.09800 34.61400  12.01300 0.700 42.92305  ? 526 MET A CA  1 
ATOM   2580 C CA  B MET A 1 196 ? -10.10600 34.57800  12.15200 0.300 43.32266  ? 526 MET A CA  1 
ATOM   2581 C C   A MET A 1 196 ? -8.73200  35.26500  12.15000 0.700 43.15832  ? 526 MET A C   1 
ATOM   2582 C C   B MET A 1 196 ? -8.76800  35.29700  12.25300 0.300 43.30866  ? 526 MET A C   1 
ATOM   2583 O O   A MET A 1 196 ? -8.62600  36.49500  12.23500 0.700 46.24223  ? 526 MET A O   1 
ATOM   2584 O O   B MET A 1 196 ? -8.71900  36.52600  12.38200 0.300 46.47429  ? 526 MET A O   1 
ATOM   2585 C CB  A MET A 1 196 ? -10.67700 34.24500  13.36800 0.700 40.12043  ? 526 MET A CB  1 
ATOM   2586 C CB  B MET A 1 196 ? -10.53200 34.01100  13.50500 0.300 43.09289  ? 526 MET A CB  1 
ATOM   2587 C CG  A MET A 1 196 ? -11.63000 33.09800  13.37300 0.700 46.97135  ? 526 MET A CG  1 
ATOM   2588 C CG  B MET A 1 196 ? -11.97700 33.53900  13.54300 0.300 49.53763  ? 526 MET A CG  1 
ATOM   2589 S SD  A MET A 1 196 ? -12.08000 32.87200  15.09300 0.700 60.69889  ? 526 MET A SD  1 
ATOM   2590 S SD  B MET A 1 196 ? -12.42800 32.78100  15.11400 0.300 65.58691  ? 526 MET A SD  1 
ATOM   2591 C CE  A MET A 1 196 ? -12.95400 34.42200  15.37800 0.700 44.47123  ? 526 MET A CE  1 
ATOM   2592 C CE  B MET A 1 196 ? -12.32000 34.19700  16.20500 0.300 50.45054  ? 526 MET A CE  1 
ATOM   2593 N N   A GLY A 1 197 ? -7.67800  34.44800  12.19300 0.700 37.92284  ? 527 GLY A N   1 
ATOM   2594 N N   B GLY A 1 197 ? -7.67000  34.53700  12.20900 0.300 38.45989  ? 527 GLY A N   1 
ATOM   2595 C CA  A GLY A 1 197 ? -6.33800  35.00100  12.19500 0.700 35.90306  ? 527 GLY A CA  1 
ATOM   2596 C CA  B GLY A 1 197 ? -6.35300  35.14800  12.16300 0.300 37.29766  ? 527 GLY A CA  1 
ATOM   2597 C C   A GLY A 1 197 ? -6.13100  35.84700  10.95600 0.700 44.19499  ? 527 GLY A C   1 
ATOM   2598 C C   B GLY A 1 197 ? -6.20100  36.02500  10.93600 0.300 44.14046  ? 527 GLY A C   1 
ATOM   2599 O O   A GLY A 1 197 ? -5.53700  36.92700  11.02100 0.700 47.27052  ? 527 GLY A O   1 
ATOM   2600 O O   B GLY A 1 197 ? -5.64400  37.12400  11.00600 0.300 46.73778  ? 527 GLY A O   1 
ATOM   2601 N N   A LEU A 1 198 ? -6.60700  35.35900  9.80700  0.700 50.19371  ? 528 LEU A N   1 
ATOM   2602 N N   B LEU A 1 198 ? -6.68300  35.53800  9.78800  0.300 49.70462  ? 528 LEU A N   1 
ATOM   2603 C CA  A LEU A 1 198 ? -6.45400  36.10700  8.56700  0.700 47.23343  ? 528 LEU A CA  1 
ATOM   2604 C CA  B LEU A 1 198 ? -6.57400  36.28600  8.54100  0.300 47.47895  ? 528 LEU A CA  1 
ATOM   2605 C C   A LEU A 1 198 ? -7.20400  37.43100  8.65900  0.700 44.68330  ? 528 LEU A C   1 
ATOM   2606 C C   B LEU A 1 198 ? -7.34600  37.59700  8.63000  0.300 44.60701  ? 528 LEU A C   1 
ATOM   2607 O O   A LEU A 1 198 ? -6.70300  38.47000  8.21300  0.700 46.75074  ? 528 LEU A O   1 
ATOM   2608 O O   B LEU A 1 198 ? -6.87800  38.63400  8.14400  0.300 45.85591  ? 528 LEU A O   1 
ATOM   2609 C CB  A LEU A 1 198 ? -6.97200  35.28400  7.38800  0.700 45.56513  ? 528 LEU A CB  1 
ATOM   2610 C CB  B LEU A 1 198 ? -7.07400  35.43900  7.37100  0.300 45.88990  ? 528 LEU A CB  1 
ATOM   2611 C CG  A LEU A 1 198 ? -6.31100  35.51300  6.02900  0.700 53.64308  ? 528 LEU A CG  1 
ATOM   2612 C CG  B LEU A 1 198 ? -6.40100  35.72100  6.02700  0.300 53.62133  ? 528 LEU A CG  1 
ATOM   2613 C CD1 A LEU A 1 198 ? -4.86300  35.06100  6.03900  0.700 54.79493  ? 528 LEU A CD1 1 
ATOM   2614 C CD1 B LEU A 1 198 ? -4.93400  35.32300  6.07400  0.300 55.30756  ? 528 LEU A CD1 1 
ATOM   2615 C CD2 A LEU A 1 198 ? -7.10100  34.80100  4.93800  0.700 61.63133  ? 528 LEU A CD2 1 
ATOM   2616 C CD2 B LEU A 1 198 ? -7.12000  35.00000  4.89700  0.300 61.34480  ? 528 LEU A CD2 1 
ATOM   2617 N N   A CYS A 1 199 ? -8.41200  37.41500  9.23700  0.700 36.94623  ? 529 CYS A N   1 
ATOM   2618 N N   B CYS A 1 199 ? -8.53700  37.56900  9.23900  0.300 38.08066  ? 529 CYS A N   1 
ATOM   2619 C CA  A CYS A 1 199 ? -9.15400  38.66500  9.38800  0.700 38.06760  ? 529 CYS A CA  1 
ATOM   2620 C CA  B CYS A 1 199 ? -9.30900  38.79800  9.39200  0.300 39.04704  ? 529 CYS A CA  1 
ATOM   2621 C C   A CYS A 1 199 ? -8.43000  39.60400  10.34000 0.700 40.39071  ? 529 CYS A C   1 
ATOM   2622 C C   B CYS A 1 199 ? -8.56500  39.76900  10.29700 0.300 41.19341  ? 529 CYS A C   1 
ATOM   2623 O O   A CYS A 1 199 ? -8.29300  40.80000  10.05600 0.700 43.36234  ? 529 CYS A O   1 
ATOM   2624 O O   B CYS A 1 199 ? -8.49600  40.97000  10.01100 0.300 43.98280  ? 529 CYS A O   1 
ATOM   2625 C CB  A CYS A 1 199 ? -10.57600 38.40000  9.88200  0.700 48.99326  ? 529 CYS A CB  1 
ATOM   2626 C CB  B CYS A 1 199 ? -10.69900 38.48800  9.94700  0.300 48.50929  ? 529 CYS A CB  1 
ATOM   2627 S SG  A CYS A 1 199 ? -11.62000 37.41800  8.77900  0.700 59.53309  ? 529 CYS A SG  1 
ATOM   2628 S SG  B CYS A 1 199 ? -11.71200 37.43700  8.87900  0.300 58.30982  ? 529 CYS A SG  1 
ATOM   2629 N N   A TYR A 1 200 ? -7.94600  39.07700  11.46700 0.700 47.31836  ? 530 TYR A N   1 
ATOM   2630 N N   B TYR A 1 200 ? -8.01000  39.26500  11.40300 0.300 46.73573  ? 530 TYR A N   1 
ATOM   2631 C CA  A TYR A 1 200 ? -7.18900  39.91500  12.38500 0.700 41.26053  ? 530 TYR A CA  1 
ATOM   2632 C CA  B TYR A 1 200 ? -7.22300  40.11700  12.28600 0.300 41.92134  ? 530 TYR A CA  1 
ATOM   2633 C C   A TYR A 1 200 ? -5.93700  40.41800  11.68400 0.700 42.95154  ? 530 TYR A C   1 
ATOM   2634 C C   B TYR A 1 200 ? -6.01900  40.65100  11.52200 0.300 43.03416  ? 530 TYR A C   1 
ATOM   2635 O O   A TYR A 1 200 ? -5.54700  41.58400  11.83600 0.700 45.45098  ? 530 TYR A O   1 
ATOM   2636 O O   B TYR A 1 200 ? -5.64700  41.82300  11.65600 0.300 45.17387  ? 530 TYR A O   1 
ATOM   2637 C CB  A TYR A 1 200 ? -6.82000  39.13400  13.65100 0.700 35.53761  ? 530 TYR A CB  1 
ATOM   2638 C CB  B TYR A 1 200 ? -6.79500  39.33900  13.52900 0.300 36.75758  ? 530 TYR A CB  1 
ATOM   2639 C CG  A TYR A 1 200 ? -7.82500  39.20400  14.78300 0.700 40.95022  ? 530 TYR A CG  1 
ATOM   2640 C CG  B TYR A 1 200 ? -7.77400  39.42400  14.67800 0.300 40.89880  ? 530 TYR A CG  1 
ATOM   2641 C CD1 A TYR A 1 200 ? -9.08300  38.61600  14.67000 0.700 40.64772  ? 530 TYR A CD1 1 
ATOM   2642 C CD1 B TYR A 1 200 ? -9.03100  38.84200  14.58900 0.300 41.76674  ? 530 TYR A CD1 1 
ATOM   2643 C CD2 A TYR A 1 200 ? -7.50700  39.84800  15.97200 0.700 40.46434  ? 530 TYR A CD2 1 
ATOM   2644 C CD2 B TYR A 1 200 ? -7.43400  40.07300  15.85800 0.300 40.03182  ? 530 TYR A CD2 1 
ATOM   2645 C CE1 A TYR A 1 200 ? -9.99400  38.67400  15.71300 0.700 43.95687  ? 530 TYR A CE1 1 
ATOM   2646 C CE1 B TYR A 1 200 ? -9.92800  38.91900  15.63700 0.300 45.19708  ? 530 TYR A CE1 1 
ATOM   2647 C CE2 A TYR A 1 200 ? -8.40500  39.91200  17.01500 0.700 32.40940  ? 530 TYR A CE2 1 
ATOM   2648 C CE2 B TYR A 1 200 ? -8.32100  40.15100  16.91300 0.300 33.74448  ? 530 TYR A CE2 1 
ATOM   2649 C CZ  A TYR A 1 200 ? -9.64500  39.32800  16.88400 0.700 41.99876  ? 530 TYR A CZ  1 
ATOM   2650 C CZ  B TYR A 1 200 ? -9.56700  39.57100  16.79800 0.300 42.37985  ? 530 TYR A CZ  1 
ATOM   2651 O OH  A TYR A 1 200 ? -10.52800 39.39900  17.93800 0.700 51.89213  ? 530 TYR A OH  1 
ATOM   2652 O OH  B TYR A 1 200 ? -10.45500 39.64500  17.84500 0.300 51.11283  ? 530 TYR A OH  1 
ATOM   2653 N N   A GLY A 1 201 ? -5.28100  39.52700  10.93100 0.700 46.11026  ? 531 GLY A N   1 
ATOM   2654 N N   B GLY A 1 201 ? -5.39300  39.78200  10.72500 0.300 45.52760  ? 531 GLY A N   1 
ATOM   2655 C CA  A GLY A 1 201 ? -4.03300  39.87800  10.27900 0.700 42.41651  ? 531 GLY A CA  1 
ATOM   2656 C CA  B GLY A 1 201 ? -4.19900  40.15700  9.98700  0.300 43.29830  ? 531 GLY A CA  1 
ATOM   2657 C C   A GLY A 1 201 ? -4.18400  40.98400  9.26100  0.700 40.29536  ? 531 GLY A C   1 
ATOM   2658 C C   B GLY A 1 201 ? -4.47100  41.27700  9.00200  0.300 45.40094  ? 531 GLY A C   1 
ATOM   2659 O O   A GLY A 1 201 ? -3.39700  41.93300  9.24200  0.700 51.11654  ? 531 GLY A O   1 
ATOM   2660 O O   B GLY A 1 201 ? -3.67000  42.19800  8.85500  0.300 50.35131  ? 531 GLY A O   1 
ATOM   2661 N N   A ILE A 1 202 ? -5.21900  40.89700  8.43100  0.700 46.35558  ? 532 ILE A N   1 
ATOM   2662 N N   B ILE A 1 202 ? -5.58300  41.19100  8.27700  0.300 47.30825  ? 532 ILE A N   1 
ATOM   2663 C CA  A ILE A 1 202 ? -5.45900  41.94900  7.45700  0.700 47.61277  ? 532 ILE A CA  1 
ATOM   2664 C CA  B ILE A 1 202 ? -5.93600  42.26900  7.35700  0.300 47.91717  ? 532 ILE A CA  1 
ATOM   2665 C C   A ILE A 1 202 ? -5.62300  43.27900  8.16700  0.700 52.70434  ? 532 ILE A C   1 
ATOM   2666 C C   B ILE A 1 202 ? -6.04500  43.59100  8.11100  0.300 51.54839  ? 532 ILE A C   1 
ATOM   2667 O O   A ILE A 1 202 ? -5.06000  44.29700  7.74600  0.700 53.12355  ? 532 ILE A O   1 
ATOM   2668 O O   B ILE A 1 202 ? -5.52500  44.62200  7.66600  0.300 52.82394  ? 532 ILE A O   1 
ATOM   2669 C CB  A ILE A 1 202 ? -6.69000  41.62700  6.59700  0.700 46.44759  ? 532 ILE A CB  1 
ATOM   2670 C CB  B ILE A 1 202 ? -7.24100  41.93200  6.61300  0.300 46.45848  ? 532 ILE A CB  1 
ATOM   2671 C CG1 A ILE A 1 202 ? -6.40700  40.47700  5.60800  0.700 53.97662  ? 532 ILE A CG1 1 
ATOM   2672 C CG1 B ILE A 1 202 ? -6.99100  40.85000  5.56000  0.300 51.06467  ? 532 ILE A CG1 1 
ATOM   2673 C CG2 A ILE A 1 202 ? -7.11100  42.90100  5.78900  0.700 51.92608  ? 532 ILE A CG2 1 
ATOM   2674 C CG2 B ILE A 1 202 ? -7.83100  43.17800  5.97000  0.300 47.27314  ? 532 ILE A CG2 1 
ATOM   2675 C CD1 A ILE A 1 202 ? -7.65100  39.70500  5.22600  0.700 41.63627  ? 532 ILE A CD1 1 
ATOM   2676 C CD1 B ILE A 1 202 ? -8.19600  39.97700  5.28800  0.300 41.45270  ? 532 ILE A CD1 1 
ATOM   2677 N N   A TYR A 1 203 ? -6.41000  43.29200  9.24700  0.700 46.78596  ? 533 TYR A N   1 
ATOM   2678 N N   B TYR A 1 203 ? -6.73000  43.58600  9.25900  0.300 46.62835  ? 533 TYR A N   1 
ATOM   2679 C CA  A TYR A 1 203 ? -6.56800  44.51600  10.02000 0.700 38.81814  ? 533 TYR A CA  1 
ATOM   2680 C CA  B TYR A 1 203 ? -6.82900  44.80200  10.06500 0.300 41.70239  ? 533 TYR A CA  1 
ATOM   2681 C C   A TYR A 1 203 ? -5.21600  45.01200  10.51100 0.700 38.70992  ? 533 TYR A C   1 
ATOM   2682 C C   B TYR A 1 203 ? -5.45200  45.32500  10.47800 0.300 41.58661  ? 533 TYR A C   1 
ATOM   2683 O O   A TYR A 1 203 ? -4.96400  46.22100  10.52200 0.700 43.37429  ? 533 TYR A O   1 
ATOM   2684 O O   B TYR A 1 203 ? -5.22800  46.54100  10.49300 0.300 46.02563  ? 533 TYR A O   1 
ATOM   2685 C CB  A TYR A 1 203 ? -7.52600  44.28200  11.19300 0.700 40.24508  ? 533 TYR A CB  1 
ATOM   2686 C CB  B TYR A 1 203 ? -7.71000  44.56000  11.29300 0.300 42.82785  ? 533 TYR A CB  1 
ATOM   2687 C CG  A TYR A 1 203 ? -7.82800  45.51800  12.03100 0.700 49.92158  ? 533 TYR A CG  1 
ATOM   2688 C CG  B TYR A 1 203 ? -7.94300  45.79800  12.14000 0.300 50.36432  ? 533 TYR A CG  1 
ATOM   2689 C CD1 A TYR A 1 203 ? -6.94200  45.95900  13.01400 0.700 52.66333  ? 533 TYR A CD1 1 
ATOM   2690 C CD1 B TYR A 1 203 ? -6.99900  46.23700  13.06000 0.300 51.77839  ? 533 TYR A CD1 1 
ATOM   2691 C CD2 A TYR A 1 203 ? -9.00000  46.23600  11.84400 0.700 48.98566  ? 533 TYR A CD2 1 
ATOM   2692 C CD2 B TYR A 1 203 ? -9.11700  46.53100  12.01300 0.300 48.12573  ? 533 TYR A CD2 1 
ATOM   2693 C CE1 A TYR A 1 203 ? -7.21600  47.08300  13.77000 0.700 49.48567  ? 533 TYR A CE1 1 
ATOM   2694 C CE1 B TYR A 1 203 ? -7.21200  47.37200  13.81900 0.300 49.46849  ? 533 TYR A CE1 1 
ATOM   2695 C CE2 A TYR A 1 203 ? -9.28400  47.35300  12.60000 0.700 41.12820  ? 533 TYR A CE2 1 
ATOM   2696 C CE2 B TYR A 1 203 ? -9.34200  47.66100  12.77400 0.300 44.14786  ? 533 TYR A CE2 1 
ATOM   2697 C CZ  A TYR A 1 203 ? -8.38900  47.77500  13.55700 0.700 45.20195  ? 533 TYR A CZ  1 
ATOM   2698 C CZ  B TYR A 1 203 ? -8.38500  48.07900  13.67400 0.300 48.75627  ? 533 TYR A CZ  1 
ATOM   2699 O OH  A TYR A 1 203 ? -8.67100  48.88300  14.32200 0.700 57.58368  ? 533 TYR A OH  1 
ATOM   2700 O OH  B TYR A 1 203 ? -8.61100  49.19900  14.44000 0.300 58.83524  ? 533 TYR A OH  1 
ATOM   2701 N N   A THR A 1 204 ? -4.33100  44.09700  10.92100 0.700 38.27951  ? 534 THR A N   1 
ATOM   2702 N N   B THR A 1 204 ? -4.51500  44.43100  10.82200 0.300 39.61615  ? 534 THR A N   1 
ATOM   2703 C CA  A THR A 1 204 ? -2.99700  44.50600  11.36000 0.700 34.07677  ? 534 THR A CA  1 
ATOM   2704 C CA  B THR A 1 204 ? -3.17400  44.88900  11.19600 0.300 38.85169  ? 534 THR A CA  1 
ATOM   2705 C C   A THR A 1 204 ? -2.23100  45.11200  10.18700 0.700 42.66293  ? 534 THR A C   1 
ATOM   2706 C C   B THR A 1 204 ? -2.49700  45.54900  9.99600  0.300 45.01602  ? 534 THR A C   1 
ATOM   2707 O O   A THR A 1 204 ? -1.64300  46.19600  10.30200 0.700 47.57427  ? 534 THR A O   1 
ATOM   2708 O O   B THR A 1 204 ? -1.93500  46.64300  10.11900 0.300 48.11160  ? 534 THR A O   1 
ATOM   2709 C CB  A THR A 1 204 ? -2.23800  43.32000  11.95600 0.700 32.45258  ? 534 THR A CB  1 
ATOM   2710 C CB  B THR A 1 204 ? -2.32500  43.77400  11.84000 0.300 37.51638  ? 534 THR A CB  1 
ATOM   2711 O OG1 A THR A 1 204 ? -3.03800  42.71100  12.97900 0.700 27.99834  ? 534 THR A OG1 1 
ATOM   2712 O OG1 B THR A 1 204 ? -1.21900  44.37400  12.52700 0.300 39.97871  ? 534 THR A OG1 1 
ATOM   2713 C CG2 A THR A 1 204 ? -0.92800  43.78800  12.56500 0.700 32.15750  ? 534 THR A CG2 1 
ATOM   2714 C CG2 B THR A 1 204 ? -1.74600  42.79500  10.85400 0.300 44.69312  ? 534 THR A CG2 1 
ATOM   2715 N N   A PHE A 1 205 ? -2.21100  44.40200  9.05000  0.700 48.95030  ? 535 PHE A N   1 
ATOM   2716 N N   B PHE A 1 205 ? -2.52400  44.89100  8.82800  0.300 46.74586  ? 535 PHE A N   1 
ATOM   2717 C CA  A PHE A 1 205 ? -1.42900  44.84100  7.89600  0.700 46.28523  ? 535 PHE A CA  1 
ATOM   2718 C CA  B PHE A 1 205 ? -1.80900  45.41200  7.66600  0.300 47.63053  ? 535 PHE A CA  1 
ATOM   2719 C C   A PHE A 1 205 ? -1.93300  46.20000  7.43000  0.700 45.00205  ? 535 PHE A C   1 
ATOM   2720 C C   B PHE A 1 205 ? -2.34200  46.79200  7.31200  0.300 47.30309  ? 535 PHE A C   1 
ATOM   2721 O O   A PHE A 1 205 ? -1.14000  47.08900  7.09400  0.700 44.23356  ? 535 PHE A O   1 
ATOM   2722 O O   B PHE A 1 205 ? -1.56800  47.70200  6.98900  0.300 45.18086  ? 535 PHE A O   1 
ATOM   2723 C CB  A PHE A 1 205 ? -1.49200  43.80300  6.77600  0.700 47.53617  ? 535 PHE A CB  1 
ATOM   2724 C CB  B PHE A 1 205 ? -1.95300  44.47200  6.46700  0.300 48.61026  ? 535 PHE A CB  1 
ATOM   2725 C CG  A PHE A 1 205 ? -0.54200  42.65000  6.96800  0.700 53.05321  ? 535 PHE A CG  1 
ATOM   2726 C CG  B PHE A 1 205 ? -1.01700  43.29700  6.48500  0.300 51.46140  ? 535 PHE A CG  1 
ATOM   2727 C CD1 A PHE A 1 205 ? -0.84900  41.61600  7.83800  0.700 63.28789  ? 535 PHE A CD1 1 
ATOM   2728 C CD1 B PHE A 1 205 ? 0.28800   43.43100  6.04300  0.300 52.16872  ? 535 PHE A CD1 1 
ATOM   2729 C CD2 A PHE A 1 205 ? 0.66200   42.60300  6.28400  0.700 58.11748  ? 535 PHE A CD2 1 
ATOM   2730 C CD2 B PHE A 1 205 ? -1.45200  42.05200  6.90300  0.300 55.92207  ? 535 PHE A CD2 1 
ATOM   2731 C CE1 A PHE A 1 205 ? 0.02000   40.55600  8.02600  0.700 66.64446  ? 535 PHE A CE1 1 
ATOM   2732 C CE1 B PHE A 1 205 ? 1.14700   42.35000  6.04500  0.300 59.03993  ? 535 PHE A CE1 1 
ATOM   2733 C CE2 A PHE A 1 205 ? 1.53900   41.54200  6.46600  0.700 70.76641  ? 535 PHE A CE2 1 
ATOM   2734 C CE2 B PHE A 1 205 ? -0.59800  40.96700  6.90900  0.300 62.05787  ? 535 PHE A CE2 1 
ATOM   2735 C CZ  A PHE A 1 205 ? 1.21600   40.51700  7.33700  0.700 66.25967  ? 535 PHE A CZ  1 
ATOM   2736 C CZ  B PHE A 1 205 ? 0.70100   41.11500  6.47700  0.300 65.02915  ? 535 PHE A CZ  1 
ATOM   2737 N N   A PHE A 1 206 ? -3.25700  46.36800  7.39500  0.700 45.91254  ? 536 PHE A N   1 
ATOM   2738 N N   B PHE A 1 206 ? -3.66700  46.95800  7.35100  0.300 48.09704  ? 536 PHE A N   1 
ATOM   2739 C CA  A PHE A 1 206 ? -3.85700  47.60300  6.90500  0.700 46.75541  ? 536 PHE A CA  1 
ATOM   2740 C CA  B PHE A 1 206 ? -4.27900  48.22300  6.96100  0.300 52.15858  ? 536 PHE A CA  1 
ATOM   2741 C C   A PHE A 1 206 ? -3.38200  48.77200  7.75300  0.700 49.96620  ? 536 PHE A C   1 
ATOM   2742 C C   B PHE A 1 206 ? -3.76600  49.34500  7.85400  0.300 53.00522  ? 536 PHE A C   1 
ATOM   2743 O O   A PHE A 1 206 ? -2.95100  49.80600  7.23000  0.700 56.39319  ? 536 PHE A O   1 
ATOM   2744 O O   B PHE A 1 206 ? -3.35300  50.40400  7.36800  0.300 56.35703  ? 536 PHE A O   1 
ATOM   2745 C CB  A PHE A 1 206 ? -5.38300  47.49700  6.93200  0.700 55.54423  ? 536 PHE A CB  1 
ATOM   2746 C CB  B PHE A 1 206 ? -5.80200  48.11800  7.04100  0.300 56.89337  ? 536 PHE A CB  1 
ATOM   2747 C CG  A PHE A 1 206 ? -6.08400  48.72200  6.41800  0.700 66.52247  ? 536 PHE A CG  1 
ATOM   2748 C CG  B PHE A 1 206 ? -6.51700  49.37200  6.63100  0.300 66.72270  ? 536 PHE A CG  1 
ATOM   2749 C CD1 A PHE A 1 206 ? -6.09800  49.01900  5.06500  0.700 81.98265  ? 536 PHE A CD1 1 
ATOM   2750 C CD1 B PHE A 1 206 ? -6.58100  49.74900  5.30100  0.300 77.96714  ? 536 PHE A CD1 1 
ATOM   2751 C CD2 A PHE A 1 206 ? -6.72200  49.58500  7.29700  0.700 66.36347  ? 536 PHE A CD2 1 
ATOM   2752 C CD2 B PHE A 1 206 ? -7.12800  50.17500  7.58100  0.300 66.84844  ? 536 PHE A CD2 1 
ATOM   2753 C CE1 A PHE A 1 206 ? -6.73900  50.15200  4.59800  0.700 84.11795  ? 536 PHE A CE1 1 
ATOM   2754 C CE1 B PHE A 1 206 ? -7.23900  50.90600  4.92600  0.300 79.06829  ? 536 PHE A CE1 1 
ATOM   2755 C CE2 A PHE A 1 206 ? -7.36400  50.71900  6.83600  0.700 76.87118  ? 536 PHE A CE2 1 
ATOM   2756 C CE2 B PHE A 1 206 ? -7.78900  51.33000  7.21200  0.300 69.79358  ? 536 PHE A CE2 1 
ATOM   2757 C CZ  A PHE A 1 206 ? -7.37200  51.00300  5.48500  0.700 80.89381  ? 536 PHE A CZ  1 
ATOM   2758 C CZ  B PHE A 1 206 ? -7.84400  51.69600  5.88300  0.300 76.00971  ? 536 PHE A CZ  1 
ATOM   2759 N N   A ASN A 1 207 ? -3.45000  48.61800  9.07700  0.700 52.27825  ? 537 ASN A N   1 
ATOM   2760 N N   B ASN A 1 207 ? -3.79000  49.12800  9.17100  0.300 48.72597  ? 537 ASN A N   1 
ATOM   2761 C CA  A ASN A 1 207 ? -3.10400  49.71300  9.97200  0.700 35.22509  ? 537 ASN A CA  1 
ATOM   2762 C CA  B ASN A 1 207 ? -3.40000  50.18600  10.09400 0.300 41.25627  ? 537 ASN A CA  1 
ATOM   2763 C C   A ASN A 1 207 ? -1.59800  49.93600  9.97400  0.700 32.88251  ? 537 ASN A C   1 
ATOM   2764 C C   B ASN A 1 207 ? -1.89100  50.38300  10.05300 0.300 39.02319  ? 537 ASN A C   1 
ATOM   2765 O O   A ASN A 1 207 ? -1.14200  51.07900  10.07900 0.700 34.48353  ? 537 ASN A O   1 
ATOM   2766 O O   B ASN A 1 207 ? -1.40300  51.51300  10.17400 0.300 45.07172  ? 537 ASN A O   1 
ATOM   2767 C CB  A ASN A 1 207 ? -3.62300  49.42700  11.38000 0.700 41.03648  ? 537 ASN A CB  1 
ATOM   2768 C CB  B ASN A 1 207 ? -3.86500  49.85100  11.51100 0.300 46.28368  ? 537 ASN A CB  1 
ATOM   2769 C CG  A ASN A 1 207 ? -5.11300  49.66600  11.50500 0.700 52.79146  ? 537 ASN A CG  1 
ATOM   2770 C CG  B ASN A 1 207 ? -5.34900  50.08800  11.71000 0.300 56.41661  ? 537 ASN A CG  1 
ATOM   2771 O OD1 A ASN A 1 207 ? -5.56100  50.80700  11.63800 0.700 63.30168  ? 537 ASN A OD1 1 
ATOM   2772 O OD1 B ASN A 1 207 ? -6.17200  49.67000  10.89500 0.300 51.89657  ? 537 ASN A OD1 1 
ATOM   2773 N ND2 A ASN A 1 207 ? -5.89300  48.59500  11.42800 0.700 45.58854  ? 537 ASN A ND2 1 
ATOM   2774 N ND2 B ASN A 1 207 ? -5.69900  50.76000  12.80000 0.300 57.81972  ? 537 ASN A ND2 1 
ATOM   2775 N N   A ALA A 1 208 ? -0.80700  48.85800  9.87500  0.700 42.12456  ? 538 ALA A N   1 
ATOM   2776 N N   B ALA A 1 208 ? -1.13800  49.28800  9.90100  0.300 42.59988  ? 538 ALA A N   1 
ATOM   2777 C CA  A ALA A 1 208 ? 0.63700   49.02500  9.71700  0.700 45.43527  ? 538 ALA A CA  1 
ATOM   2778 C CA  B ALA A 1 208 ? 0.30400   49.39700  9.70100  0.300 46.57981  ? 538 ALA A CA  1 
ATOM   2779 C C   A ALA A 1 208 ? 0.92300   49.89000  8.49600  0.700 45.58425  ? 538 ALA A C   1 
ATOM   2780 C C   B ALA A 1 208 ? 0.60600   50.26500  8.48600  0.300 48.83233  ? 538 ALA A C   1 
ATOM   2781 O O   A ALA A 1 208 ? 1.83400   50.72700  8.51000  0.700 47.73086  ? 538 ALA A O   1 
ATOM   2782 O O   B ALA A 1 208 ? 1.56000   51.05200  8.49400  0.300 50.32604  ? 538 ALA A O   1 
ATOM   2783 C CB  A ALA A 1 208 ? 1.32200   47.66600  9.59500  0.700 44.08076  ? 538 ALA A CB  1 
ATOM   2784 C CB  B ALA A 1 208 ? 0.92400   48.01000  9.54500  0.300 46.17557  ? 538 ALA A CB  1 
ATOM   2785 N N   A ALA A 1 209 ? 0.15200   49.68100  7.42300  0.700 52.91373  ? 539 ALA A N   1 
ATOM   2786 N N   B ALA A 1 209 ? -0.19500  50.11900  7.42600  0.300 52.43311  ? 539 ALA A N   1 
ATOM   2787 C CA  A ALA A 1 209 ? 0.35200   50.41400  6.17800  0.700 53.33618  ? 539 ALA A CA  1 
ATOM   2788 C CA  B ALA A 1 209 ? 0.04600   50.85100  6.18700  0.300 52.38788  ? 539 ALA A CA  1 
ATOM   2789 C C   A ALA A 1 209 ? 0.09100   51.89000  6.42500  0.700 47.90252  ? 539 ALA A C   1 
ATOM   2790 C C   B ALA A 1 209 ? -0.08900  52.34800  6.42200  0.300 48.85003  ? 539 ALA A C   1 
ATOM   2791 O O   A ALA A 1 209 ? 0.83100   52.76100  5.95100  0.700 47.30656  ? 539 ALA A O   1 
ATOM   2792 O O   B ALA A 1 209 ? 0.71900   53.14100  5.92600  0.300 50.41151  ? 539 ALA A O   1 
ATOM   2793 C CB  A ALA A 1 209 ? -0.55600  49.86700  5.08000  0.700 51.58252  ? 539 ALA A CB  1 
ATOM   2794 C CB  B ALA A 1 209 ? -0.91800  50.38300  5.09800  0.300 53.54712  ? 539 ALA A CB  1 
ATOM   2795 N N   A LYS A 1 210 ? -0.97400  52.17200  7.17800  0.700 45.69620  ? 540 LYS A N   1 
ATOM   2796 N N   B LYS A 1 210 ? -1.12400  52.74900  7.16700  0.300 45.03551  ? 540 LYS A N   1 
ATOM   2797 C CA  A LYS A 1 210 ? -1.33200  53.53100  7.56600  0.700 36.57706  ? 540 LYS A CA  1 
ATOM   2798 C CA  B LYS A 1 210 ? -1.30700  54.15500  7.51000  0.300 42.72909  ? 540 LYS A CA  1 
ATOM   2799 C C   A LYS A 1 210 ? -0.17000  54.19400  8.29800  0.700 42.01717  ? 540 LYS A C   1 
ATOM   2800 C C   B LYS A 1 210 ? -0.08800  54.69300  8.24600  0.300 48.00679  ? 540 LYS A C   1 
ATOM   2801 O O   A LYS A 1 210 ? 0.15000   55.36300  8.04900  0.700 51.39370  ? 540 LYS A O   1 
ATOM   2802 O O   B LYS A 1 210 ? 0.37300   55.80600  7.96400  0.300 55.19430  ? 540 LYS A O   1 
ATOM   2803 C CB  A LYS A 1 210 ? -2.55500  53.43100  8.47800  0.700 46.41905  ? 540 LYS A CB  1 
ATOM   2804 C CB  B LYS A 1 210 ? -2.57500  54.33200  8.34700  0.300 43.51200  ? 540 LYS A CB  1 
ATOM   2805 C CG  A LYS A 1 210 ? -3.84100  54.11900  8.09300  0.700 54.10825  ? 540 LYS A CG  1 
ATOM   2806 C CG  B LYS A 1 210 ? -3.83800  53.83100  7.66100  0.300 53.25594  ? 540 LYS A CG  1 
ATOM   2807 C CD  A LYS A 1 210 ? -4.62400  54.35200  9.38800  0.700 70.14630  ? 540 LYS A CD  1 
ATOM   2808 C CD  B LYS A 1 210 ? -4.94600  53.53300  8.66100  0.300 56.24844  ? 540 LYS A CD  1 
ATOM   2809 C CE  A LYS A 1 210 ? -5.50800  55.57900  9.37400  0.700 69.80192  ? 540 LYS A CE  1 
ATOM   2810 C CE  B LYS A 1 210 ? -5.38000  54.78800  9.40100  0.300 65.27780  ? 540 LYS A CE  1 
ATOM   2811 N NZ  A LYS A 1 210 ? -6.36200  55.59700  10.60200 0.700 59.49871  ? 540 LYS A NZ  1 
ATOM   2812 N NZ  B LYS A 1 210 ? -6.23500  54.47200  10.58000 0.300 55.19739  ? 540 LYS A NZ  1 
ATOM   2813 N N   A VAL A 1 211 ? 0.45100   53.46900  9.23400  0.700 53.63432  ? 541 VAL A N   1 
ATOM   2814 N N   B VAL A 1 211 ? 0.43900   53.92600  9.20600  0.300 50.86392  ? 541 VAL A N   1 
ATOM   2815 C CA  A VAL A 1 211 ? 1.54700   54.02500  10.02900 0.700 48.50615  ? 541 VAL A CA  1 
ATOM   2816 C CA  B VAL A 1 211 ? 1.56800   54.39900  10.00500 0.300 50.11137  ? 541 VAL A CA  1 
ATOM   2817 C C   A VAL A 1 211 ? 2.71100   54.41300  9.12300  0.700 42.30333  ? 541 VAL A C   1 
ATOM   2818 C C   B VAL A 1 211 ? 2.75900   54.68100  9.09700  0.300 43.94460  ? 541 VAL A C   1 
ATOM   2819 O O   A VAL A 1 211 ? 3.29100   55.49800  9.25100  0.700 45.43259  ? 541 VAL A O   1 
ATOM   2820 O O   B VAL A 1 211 ? 3.40300   55.73300  9.19600  0.300 47.24398  ? 541 VAL A O   1 
ATOM   2821 C CB  A VAL A 1 211 ? 1.98600   53.03100  11.11900 0.700 46.35656  ? 541 VAL A CB  1 
ATOM   2822 C CB  B VAL A 1 211 ? 1.91900   53.37700  11.10100 0.300 48.27532  ? 541 VAL A CB  1 
ATOM   2823 C CG1 A VAL A 1 211 ? 3.16100   53.59500  11.90100 0.700 46.78063  ? 541 VAL A CG1 1 
ATOM   2824 C CG1 B VAL A 1 211 ? 3.12900   53.84300  11.89700 0.300 46.54701  ? 541 VAL A CG1 1 
ATOM   2825 C CG2 A VAL A 1 211 ? 0.83100   52.72800  12.05500 0.700 43.97148  ? 541 VAL A CG2 1 
ATOM   2826 C CG2 B VAL A 1 211 ? 0.72600   53.15200  12.01800 0.300 45.51228  ? 541 VAL A CG2 1 
ATOM   2827 N N   A TYR A 1 212 ? 3.09600   53.50500  8.22100  0.700 43.58735  ? 542 TYR A N   1 
ATOM   2828 N N   B TYR A 1 212 ? 3.07700   53.73800  8.20300  0.300 44.92886  ? 542 TYR A N   1 
ATOM   2829 C CA  A TYR A 1 212 ? 4.22500   53.75100  7.32800  0.700 43.91946  ? 542 TYR A CA  1 
ATOM   2830 C CA  B TYR A 1 212 ? 4.21900   53.92000  7.31200  0.300 44.44025  ? 542 TYR A CA  1 
ATOM   2831 C C   A TYR A 1 212 ? 3.97100   54.94000  6.40900  0.700 50.89833  ? 542 TYR A C   1 
ATOM   2832 C C   B TYR A 1 212 ? 4.00200   55.12200  6.40300  0.300 50.58839  ? 542 TYR A C   1 
ATOM   2833 O O   A TYR A 1 212 ? 4.90000   55.69400  6.09000  0.700 53.74373  ? 542 TYR A O   1 
ATOM   2834 O O   B TYR A 1 212 ? 4.95100   55.84800  6.08000  0.300 53.39978  ? 542 TYR A O   1 
ATOM   2835 C CB  A TYR A 1 212 ? 4.51800   52.50700  6.49200  0.700 49.38420  ? 542 TYR A CB  1 
ATOM   2836 C CB  B TYR A 1 212 ? 4.46300   52.65700  6.48500  0.300 48.98922  ? 542 TYR A CB  1 
ATOM   2837 C CG  A TYR A 1 212 ? 5.34700   51.44800  7.17700  0.700 43.27935  ? 542 TYR A CG  1 
ATOM   2838 C CG  B TYR A 1 212 ? 5.24600   51.59000  7.21300  0.300 43.54008  ? 542 TYR A CG  1 
ATOM   2839 C CD1 A TYR A 1 212 ? 6.71200   51.62300  7.36500  0.700 42.75792  ? 542 TYR A CD1 1 
ATOM   2840 C CD1 B TYR A 1 212 ? 6.61100   51.73100  7.41800  0.300 42.93080  ? 542 TYR A CD1 1 
ATOM   2841 C CD2 A TYR A 1 212 ? 4.77100   50.26100  7.61300  0.700 41.87693  ? 542 TYR A CD2 1 
ATOM   2842 C CD2 B TYR A 1 212 ? 4.62700   50.43900  7.68200  0.300 43.39331  ? 542 TYR A CD2 1 
ATOM   2843 C CE1 A TYR A 1 212 ? 7.48000   50.65200  7.98500  0.700 46.49094  ? 542 TYR A CE1 1 
ATOM   2844 C CE1 B TYR A 1 212 ? 7.33700   50.76600  8.08300  0.300 46.70149  ? 542 TYR A CE1 1 
ATOM   2845 C CE2 A TYR A 1 212 ? 5.52900   49.28300  8.22800  0.700 43.34066  ? 542 TYR A CE2 1 
ATOM   2846 C CE2 B TYR A 1 212 ? 5.34700   49.46200  8.34400  0.300 43.73174  ? 542 TYR A CE2 1 
ATOM   2847 C CZ  A TYR A 1 212 ? 6.88200   49.48400  8.41300  0.700 43.97457  ? 542 TYR A CZ  1 
ATOM   2848 C CZ  B TYR A 1 212 ? 6.70300   49.63300  8.54200  0.300 43.80732  ? 542 TYR A CZ  1 
ATOM   2849 O OH  A TYR A 1 212 ? 7.64000   48.51100  9.02200  0.700 35.18284  ? 542 TYR A OH  1 
ATOM   2850 O OH  B TYR A 1 212 ? 7.43400   48.66900  9.19700  0.300 36.14484  ? 542 TYR A OH  1 
ATOM   2851 N N   A ILE A 1 213 ? 2.72600   55.11400  5.95700  0.700 50.53942  ? 543 ILE A N   1 
ATOM   2852 N N   B ILE A 1 213 ? 2.75700   55.34100  5.97400  0.300 50.08368  ? 543 ILE A N   1 
ATOM   2853 C CA  A ILE A 1 213 ? 2.38900   56.27400  5.13300  0.700 47.87348  ? 543 ILE A CA  1 
ATOM   2854 C CA  B ILE A 1 213 ? 2.43400   56.51800  5.17300  0.300 48.90988  ? 543 ILE A CA  1 
ATOM   2855 C C   A ILE A 1 213 ? 2.59900   57.56500  5.91800  0.700 57.65056  ? 543 ILE A C   1 
ATOM   2856 C C   B ILE A 1 213 ? 2.69400   57.78300  5.98100  0.300 57.18670  ? 543 ILE A C   1 
ATOM   2857 O O   A ILE A 1 213 ? 3.24000   58.50700  5.43400  0.700 55.86917  ? 543 ILE A O   1 
ATOM   2858 O O   B ILE A 1 213 ? 3.32800   58.73000  5.50100  0.300 56.25844  ? 543 ILE A O   1 
ATOM   2859 C CB  A ILE A 1 213 ? 0.94700   56.15900  4.60300  0.700 44.37337  ? 543 ILE A CB  1 
ATOM   2860 C CB  B ILE A 1 213 ? 0.97700   56.44700  4.67900  0.300 46.35910  ? 543 ILE A CB  1 
ATOM   2861 C CG1 A ILE A 1 213 ? 0.88800   55.18400  3.42500  0.700 49.10387  ? 543 ILE A CG1 1 
ATOM   2862 C CG1 B ILE A 1 213 ? 0.86300   55.48700  3.49300  0.300 49.74477  ? 543 ILE A CG1 1 
ATOM   2863 C CG2 A ILE A 1 213 ? 0.42000   57.52000  4.17800  0.700 47.44139  ? 543 ILE A CG2 1 
ATOM   2864 C CG2 B ILE A 1 213 ? 0.46900   57.83000  4.29600  0.300 49.33918  ? 543 ILE A CG2 1 
ATOM   2865 C CD1 A ILE A 1 213 ? -0.49600  54.61300  3.17400  0.700 46.34432  ? 543 ILE A CD1 1 
ATOM   2866 C CD1 B ILE A 1 213 ? -0.53700  54.95600  3.27100  0.300 48.09610  ? 543 ILE A CD1 1 
ATOM   2867 N N   A GLU A 1 214 ? 2.07300   57.62400  7.14700  0.700 60.78288  ? 544 GLU A N   1 
ATOM   2868 N N   B GLU A 1 214 ? 2.19500   57.82000  7.22100  0.300 58.83230  ? 544 GLU A N   1 
ATOM   2869 C CA  A GLU A 1 214 ? 2.34100   58.77600  8.00500  0.700 49.98613  ? 544 GLU A CA  1 
ATOM   2870 C CA  B GLU A 1 214 ? 2.50800   58.93500  8.11000  0.300 51.37834  ? 544 GLU A CA  1 
ATOM   2871 C C   A GLU A 1 214 ? 3.83600   58.94500  8.24400  0.700 50.26942  ? 544 GLU A C   1 
ATOM   2872 C C   B GLU A 1 214 ? 4.01200   59.05300  8.32100  0.300 51.75174  ? 544 GLU A C   1 
ATOM   2873 O O   A GLU A 1 214 ? 4.35300   60.06800  8.20300  0.700 63.70171  ? 544 GLU A O   1 
ATOM   2874 O O   B GLU A 1 214 ? 4.56100   60.16100  8.30400  0.300 63.03658  ? 544 GLU A O   1 
ATOM   2875 C CB  A GLU A 1 214 ? 1.58200   58.65100  9.32500  0.700 62.92219  ? 544 GLU A CB  1 
ATOM   2876 C CB  B GLU A 1 214 ? 1.78000   58.77300  9.44300  0.300 62.76445  ? 544 GLU A CB  1 
ATOM   2877 C CG  A GLU A 1 214 ? 0.07100   58.61900  9.14900  0.700 65.92492  ? 544 GLU A CG  1 
ATOM   2878 C CG  B GLU A 1 214 ? 0.26900   58.77000  9.31200  0.300 66.98180  ? 544 GLU A CG  1 
ATOM   2879 C CD  A GLU A 1 214 ? -0.67400  58.68700  10.46600 0.700 75.02830  ? 544 GLU A CD  1 
ATOM   2880 C CD  B GLU A 1 214 ? -0.43100  58.79800  10.65400 0.300 74.23473  ? 544 GLU A CD  1 
ATOM   2881 O OE1 A GLU A 1 214 ? -0.02700  58.92000  11.51100 0.700 71.54311  ? 544 GLU A OE1 1 
ATOM   2882 O OE1 B GLU A 1 214 ? 0.25400   58.98100  11.68200 0.300 70.88419  ? 544 GLU A OE1 1 
ATOM   2883 O OE2 A GLU A 1 214 ? -1.91200  58.50900  10.45500 0.700 76.00620  ? 544 GLU A OE2 1 
ATOM   2884 O OE2 B GLU A 1 214 ? -1.66800  58.63800  10.67900 0.300 74.75603  ? 544 GLU A OE2 1 
ATOM   2885 N N   A ALA A 1 215 ? 4.54700   57.84300  8.51100  0.700 49.67877  ? 545 ALA A N   1 
ATOM   2886 N N   B ALA A 1 215 ? 4.69200   57.92300  8.53800  0.300 49.72483  ? 545 ALA A N   1 
ATOM   2887 C CA  A ALA A 1 215 ? 5.96300   57.94400  8.85100  0.700 51.51617  ? 545 ALA A CA  1 
ATOM   2888 C CA  B ALA A 1 215 ? 6.11800   57.96600  8.84800  0.300 51.54224  ? 545 ALA A CA  1 
ATOM   2889 C C   A ALA A 1 215 ? 6.74200   58.53200  7.68300  0.700 54.03719  ? 545 ALA A C   1 
ATOM   2890 C C   B ALA A 1 215 ? 6.88900   58.56300  7.68000  0.300 53.88952  ? 545 ALA A C   1 
ATOM   2891 O O   A ALA A 1 215 ? 7.63000   59.37200  7.87500  0.700 52.60046  ? 545 ALA A O   1 
ATOM   2892 O O   B ALA A 1 215 ? 7.81300   59.36200  7.87400  0.300 53.47065  ? 545 ALA A O   1 
ATOM   2893 C CB  A ALA A 1 215 ? 6.51800   56.57200  9.23500  0.700 53.19850  ? 545 ALA A CB  1 
ATOM   2894 C CB  B ALA A 1 215 ? 6.63200   56.56700  9.18400  0.300 53.10801  ? 545 ALA A CB  1 
ATOM   2895 N N   A TYR A 1 216 ? 6.42300   58.08600  6.46600  0.700 58.09460  ? 546 TYR A N   1 
ATOM   2896 N N   B TYR A 1 216 ? 6.52900   58.16400  6.45700  0.300 57.75662  ? 546 TYR A N   1 
ATOM   2897 C CA  A TYR A 1 216 ? 7.15400   58.51300  5.27700  0.700 61.31663  ? 546 TYR A CA  1 
ATOM   2898 C CA  B TYR A 1 216 ? 7.24300   58.60500  5.26400  0.300 60.92285  ? 546 TYR A CA  1 
ATOM   2899 C C   A TYR A 1 216 ? 7.07800   60.03000  5.13400  0.700 59.30881  ? 546 TYR A C   1 
ATOM   2900 C C   B TYR A 1 216 ? 7.21200   60.12400  5.16200  0.300 59.17888  ? 546 TYR A C   1 
ATOM   2901 O O   A TYR A 1 216 ? 8.08800   60.69600  4.88100  0.700 60.94642  ? 546 TYR A O   1 
ATOM   2902 O O   B TYR A 1 216 ? 8.23400   60.76700  4.89400  0.300 60.48072  ? 546 TYR A O   1 
ATOM   2903 C CB  A TYR A 1 216 ? 6.60400   57.79800  4.03900  0.700 55.56087  ? 546 TYR A CB  1 
ATOM   2904 C CB  B TYR A 1 216 ? 6.62600   57.96100  4.02100  0.300 55.72374  ? 546 TYR A CB  1 
ATOM   2905 C CG  A TYR A 1 216 ? 7.28800   58.15900  2.73500  0.700 55.38726  ? 546 TYR A CG  1 
ATOM   2906 C CG  B TYR A 1 216 ? 7.28800   58.36000  2.72200  0.300 56.52282  ? 546 TYR A CG  1 
ATOM   2907 C CD1 A TYR A 1 216 ? 8.42000   57.47100  2.31200  0.700 55.81304  ? 546 TYR A CD1 1 
ATOM   2908 C CD1 B TYR A 1 216 ? 8.45000   57.73600  2.29100  0.300 57.91096  ? 546 TYR A CD1 1 
ATOM   2909 C CD2 A TYR A 1 216 ? 6.79200   59.16400  1.91600  0.700 60.35372  ? 546 TYR A CD2 1 
ATOM   2910 C CD2 B TYR A 1 216 ? 6.74300   59.35600  1.92200  0.300 60.57395  ? 546 TYR A CD2 1 
ATOM   2911 C CE1 A TYR A 1 216 ? 9.05300   57.79300  1.12300  0.700 63.37153  ? 546 TYR A CE1 1 
ATOM   2912 C CE1 B TYR A 1 216 ? 9.06000   58.10200  1.10700  0.300 64.29427  ? 546 TYR A CE1 1 
ATOM   2913 C CE2 A TYR A 1 216 ? 7.41100   59.48900  0.72100  0.700 61.82194  ? 546 TYR A CE2 1 
ATOM   2914 C CE2 B TYR A 1 216 ? 7.34200   59.72500  0.73300  0.300 62.41576  ? 546 TYR A CE2 1 
ATOM   2915 C CZ  A TYR A 1 216 ? 8.54300   58.80100  0.32900  0.700 66.63267  ? 546 TYR A CZ  1 
ATOM   2916 C CZ  B TYR A 1 216 ? 8.50100   59.09600  0.33200  0.300 67.15546  ? 546 TYR A CZ  1 
ATOM   2917 O OH  A TYR A 1 216 ? 9.15800   59.11700  -0.86400 0.700 61.23409  ? 546 TYR A OH  1 
ATOM   2918 O OH  B TYR A 1 216 ? 9.09700   59.45300  -0.85600 0.300 63.42678  ? 546 TYR A OH  1 
ATOM   2919 N N   A HIS A 1 217 ? 5.88200   60.59200  5.31100  0.700 59.45604  ? 547 HIS A N   1 
ATOM   2920 N N   B HIS A 1 217 ? 6.03600   60.71000  5.37500  0.300 59.25480  ? 547 HIS A N   1 
ATOM   2921 C CA  A HIS A 1 217 ? 5.64000   62.02400  5.17900  0.700 62.16451  ? 547 HIS A CA  1 
ATOM   2922 C CA  B HIS A 1 217 ? 5.81100   62.14500  5.29000  0.300 61.98657  ? 547 HIS A CA  1 
ATOM   2923 C C   A HIS A 1 217 ? 6.02800   62.80400  6.42900  0.700 58.58883  ? 547 HIS A C   1 
ATOM   2924 C C   B HIS A 1 217 ? 6.22600   62.87600  6.56000  0.300 59.09117  ? 547 HIS A C   1 
ATOM   2925 O O   A HIS A 1 217 ? 5.91300   64.03500  6.43500  0.700 52.90158  ? 547 HIS A O   1 
ATOM   2926 O O   B HIS A 1 217 ? 6.14800   64.10800  6.60000  0.300 55.78892  ? 547 HIS A O   1 
ATOM   2927 C CB  A HIS A 1 217 ? 4.16600   62.29300  4.85100  0.700 59.07434  ? 547 HIS A CB  1 
ATOM   2928 C CB  B HIS A 1 217 ? 4.33700   62.42800  4.98900  0.300 60.29624  ? 547 HIS A CB  1 
ATOM   2929 C CG  A HIS A 1 217 ? 3.72700   61.74900  3.52600  0.700 60.47465  ? 547 HIS A CG  1 
ATOM   2930 C CG  B HIS A 1 217 ? 3.88400   61.91700  3.65600  0.300 62.39180  ? 547 HIS A CG  1 
ATOM   2931 N ND1 A HIS A 1 217 ? 4.60900   61.23700  2.59900  0.700 65.51541  ? 547 HIS A ND1 1 
ATOM   2932 N ND1 B HIS A 1 217 ? 2.64800   61.33900  3.46200  0.300 68.53941  ? 547 HIS A ND1 1 
ATOM   2933 C CD2 A HIS A 1 217 ? 2.49600   61.64800  2.96900  0.700 70.83569  ? 547 HIS A CD2 1 
ATOM   2934 C CD2 B HIS A 1 217 ? 4.50200   61.89500  2.45200  0.300 64.74009  ? 547 HIS A CD2 1 
ATOM   2935 C CE1 A HIS A 1 217 ? 3.94100   60.83900  1.53100  0.700 75.83474  ? 547 HIS A CE1 1 
ATOM   2936 C CE1 B HIS A 1 217 ? 2.52400   60.98400  2.19600  0.300 77.59157  ? 547 HIS A CE1 1 
ATOM   2937 N NE2 A HIS A 1 217 ? 2.65700   61.07700  1.73000  0.700 82.82114  ? 547 HIS A NE2 1 
ATOM   2938 N NE2 B HIS A 1 217 ? 3.63500   61.31000  1.56100  0.300 74.65443  ? 547 HIS A NE2 1 
ATOM   2939 N N   A THR A 1 218 ? 6.45400   62.12200  7.49100  0.700 56.18425  ? 548 THR A N   1 
ATOM   2940 N N   B THR A 1 218 ? 6.65900   62.15100  7.59400  0.300 56.93993  ? 548 THR A N   1 
ATOM   2941 C CA  A THR A 1 218 ? 6.88500   62.77300  8.72400  0.700 57.43508  ? 548 THR A CA  1 
ATOM   2942 C CA  B THR A 1 218 ? 7.10700   62.76000  8.84000  0.300 58.00364  ? 548 THR A CA  1 
ATOM   2943 C C   A THR A 1 218 ? 8.38800   63.03300  8.73800  0.700 54.55126  ? 548 THR A C   1 
ATOM   2944 C C   B THR A 1 218 ? 8.60900   63.01100  8.82900  0.300 55.44609  ? 548 THR A C   1 
ATOM   2945 O O   A THR A 1 218 ? 8.83000   64.10300  9.17200  0.700 59.03239  ? 548 THR A O   1 
ATOM   2946 O O   B THR A 1 218 ? 9.06400   64.07900  9.25500  0.300 58.98546  ? 548 THR A O   1 
ATOM   2947 C CB  A THR A 1 218 ? 6.49200   61.92900  9.93800  0.700 57.53643  ? 548 THR A CB  1 
ATOM   2948 C CB  B THR A 1 218 ? 6.76200   61.85400  10.03000 0.300 58.74235  ? 548 THR A CB  1 
ATOM   2949 O OG1 A THR A 1 218 ? 5.06400   61.84700  10.02100 0.700 53.52728  ? 548 THR A OG1 1 
ATOM   2950 O OG1 B THR A 1 218 ? 5.34200   61.72400  10.15500 0.300 57.92724  ? 548 THR A OG1 1 
ATOM   2951 C CG2 A THR A 1 218 ? 7.03500   62.55100  11.21500 0.700 52.42622  ? 548 THR A CG2 1 
ATOM   2952 C CG2 B THR A 1 218 ? 7.32200   62.42800  11.32500 0.300 54.11107  ? 548 THR A CG2 1 
ATOM   2953 N N   A VAL A 1 219 ? 9.18000   62.06900  8.27700  0.700 56.79478  ? 549 VAL A N   1 
ATOM   2954 N N   B VAL A 1 219 ? 9.38200   62.05200  8.33200  0.300 57.02368  ? 549 VAL A N   1 
ATOM   2955 C CA  A VAL A 1 219 ? 10.63800  62.10400  8.37700  0.700 58.50298  ? 549 VAL A CA  1 
ATOM   2956 C CA  B VAL A 1 219 ? 10.83900  62.08800  8.40400  0.300 58.78437  ? 549 VAL A CA  1 
ATOM   2957 C C   A VAL A 1 219 ? 11.19500  63.05700  7.32300  0.700 61.00587  ? 549 VAL A C   1 
ATOM   2958 C C   B VAL A 1 219 ? 11.35900  63.05600  7.34500  0.300 60.85333  ? 549 VAL A C   1 
ATOM   2959 O O   A VAL A 1 219 ? 10.50900  63.34800  6.33200  0.700 64.35277  ? 549 VAL A O   1 
ATOM   2960 O O   B VAL A 1 219 ? 10.64900  63.33400  6.36700  0.300 63.71143  ? 549 VAL A O   1 
ATOM   2961 C CB  A VAL A 1 219 ? 11.22800  60.69200  8.22400  0.700 56.75485  ? 549 VAL A CB  1 
ATOM   2962 C CB  B VAL A 1 219 ? 11.42800  60.67900  8.22700  0.300 56.53996  ? 549 VAL A CB  1 
ATOM   2963 C CG1 A VAL A 1 219 ? 10.67300  59.76400  9.30000  0.700 53.63280  ? 549 VAL A CG1 1 
ATOM   2964 C CG1 B VAL A 1 219 ? 10.89800  59.74800  9.30600  0.300 53.95409  ? 549 VAL A CG1 1 
ATOM   2965 C CG2 A VAL A 1 219 ? 10.95000  60.14200  6.83100  0.700 57.53712  ? 549 VAL A CG2 1 
ATOM   2966 C CG2 B VAL A 1 219 ? 11.10000  60.13500  6.84600  0.300 57.36695  ? 549 VAL A CG2 1 
ATOM   2967 N N   A PRO A 1 220 ? 12.41600  63.60200  7.51200  0.700 57.48584  ? 550 PRO A N   1 
ATOM   2968 N N   B PRO A 1 220 ? 12.57600  63.61500  7.50700  0.300 57.72543  ? 550 PRO A N   1 
ATOM   2969 C CA  A PRO A 1 220 ? 13.02200  64.47900  6.49300  0.700 63.23029  ? 550 PRO A CA  1 
ATOM   2970 C CA  B PRO A 1 220 ? 13.13300  64.50300  6.47300  0.300 63.27377  ? 550 PRO A CA  1 
ATOM   2971 C C   A PRO A 1 220 ? 13.06600  63.89800  5.08500  0.700 64.40584  ? 550 PRO A C   1 
ATOM   2972 C C   B PRO A 1 220 ? 13.13500  63.90000  5.07500  0.300 64.37991  ? 550 PRO A C   1 
ATOM   2973 O O   A PRO A 1 220 ? 12.98200  62.68100  4.89000  0.700 65.84326  ? 550 PRO A O   1 
ATOM   2974 O O   B PRO A 1 220 ? 13.08300  62.67800  4.90900  0.300 65.90709  ? 550 PRO A O   1 
ATOM   2975 C CB  A PRO A 1 220 ? 14.44100  64.72200  7.02900  0.700 63.92221  ? 550 PRO A CB  1 
ATOM   2976 C CB  B PRO A 1 220 ? 14.56300  64.77100  6.96300  0.300 63.77122  ? 550 PRO A CB  1 
ATOM   2977 C CG  A PRO A 1 220 ? 14.37800  64.43100  8.47700  0.700 60.84888  ? 550 PRO A CG  1 
ATOM   2978 C CG  B PRO A 1 220 ? 14.54800  64.47600  8.41500  0.300 60.95245  ? 550 PRO A CG  1 
ATOM   2979 C CD  A PRO A 1 220 ? 13.26400  63.45600  8.70800  0.700 58.65217  ? 550 PRO A CD  1 
ATOM   2980 C CD  B PRO A 1 220 ? 13.46200  63.48400  8.67600  0.300 59.02706  ? 550 PRO A CD  1 
ATOM   2981 N N   A LYS A 1 221 ? 13.21300  64.78700  4.09600  0.700 64.65828  ? 551 LYS A N   1 
ATOM   2982 N N   B LYS A 1 221 ? 13.22500  64.76800  4.06400  0.300 64.51456  ? 551 LYS A N   1 
ATOM   2983 C CA  A LYS A 1 221 ? 12.97100  64.45200  2.69500  0.700 61.01683  ? 551 LYS A CA  1 
ATOM   2984 C CA  B LYS A 1 221 ? 12.93700  64.39400  2.68300  0.300 61.31642  ? 551 LYS A CA  1 
ATOM   2985 C C   A LYS A 1 221 ? 13.99500  63.48700  2.11200  0.700 72.52525  ? 551 LYS A C   1 
ATOM   2986 C C   B LYS A 1 221 ? 13.96400  63.43900  2.08500  0.300 72.36750  ? 551 LYS A C   1 
ATOM   2987 O O   A LYS A 1 221 ? 13.69700  62.82200  1.11400  0.700 83.87023  ? 551 LYS A O   1 
ATOM   2988 O O   B LYS A 1 221 ? 13.64900  62.74900  1.11000  0.300 82.89129  ? 551 LYS A O   1 
ATOM   2989 C CB  A LYS A 1 221 ? 12.93700  65.72700  1.85200  0.700 52.03029  ? 551 LYS A CB  1 
ATOM   2990 C CB  B LYS A 1 221 ? 12.83900  65.64900  1.81400  0.300 52.48698  ? 551 LYS A CB  1 
ATOM   2991 N N   A GLY A 1 222 ? 15.18100  63.38700  2.69900  0.700 58.85514  ? 552 GLY A N   1 
ATOM   2992 N N   B GLY A 1 222 ? 15.17400  63.37800  2.63500  0.300 59.52728  ? 552 GLY A N   1 
ATOM   2993 C CA  A GLY A 1 222 ? 16.24000  62.64100  2.05200  0.700 65.24340  ? 552 GLY A CA  1 
ATOM   2994 C CA  B GLY A 1 222 ? 16.25100  62.65200  1.98600  0.300 65.31991  ? 552 GLY A CA  1 
ATOM   2995 C C   A GLY A 1 222 ? 16.37200  61.17500  2.40800  0.700 61.37496  ? 552 GLY A C   1 
ATOM   2996 C C   B GLY A 1 222 ? 16.43600  61.19800  2.37000  0.300 61.86382  ? 552 GLY A C   1 
ATOM   2997 O O   A GLY A 1 222 ? 15.49800  60.35500  2.10600  0.700 58.95133  ? 552 GLY A O   1 
ATOM   2998 O O   B GLY A 1 222 ? 15.57200  60.36000  2.09200  0.300 59.51636  ? 552 GLY A O   1 
ATOM   2999 N N   A ARG A 1 223 ? 17.49800  60.84800  3.04200  0.700 69.21938  ? 553 ARG A N   1 
ATOM   3000 N N   B ARG A 1 223 ? 17.57300  60.88900  3.00000  0.300 69.12674  ? 553 ARG A N   1 
ATOM   3001 C CA  A ARG A 1 223 ? 17.81700  59.47300  3.41200  0.700 64.73180  ? 553 ARG A CA  1 
ATOM   3002 C CA  B ARG A 1 223 ? 17.88700  59.50900  3.36800  0.300 64.95330  ? 553 ARG A CA  1 
ATOM   3003 C C   A ARG A 1 223 ? 16.75000  58.86400  4.31500  0.700 63.64164  ? 553 ARG A C   1 
ATOM   3004 C C   B ARG A 1 223 ? 16.81900  58.90400  4.27200  0.300 63.90175  ? 553 ARG A C   1 
ATOM   3005 O O   A ARG A 1 223 ? 16.43000  57.67500  4.19200  0.700 54.77581  ? 553 ARG A O   1 
ATOM   3006 O O   B ARG A 1 223 ? 16.51500  57.71000  4.16400  0.300 55.35412  ? 553 ARG A O   1 
ATOM   3007 C CB  A ARG A 1 223 ? 19.17900  59.49300  4.09600  0.700 64.82833  ? 553 ARG A CB  1 
ATOM   3008 C CB  B ARG A 1 223 ? 19.25800  59.44400  4.04200  0.300 65.03584  ? 553 ARG A CB  1 
ATOM   3009 C CG  A ARG A 1 223 ? 20.26200  58.64800  3.50200  0.700 67.23672  ? 553 ARG A CG  1 
ATOM   3010 C CG  B ARG A 1 223 ? 19.79200  58.03000  4.21600  0.300 58.03046  ? 553 ARG A CG  1 
ATOM   3011 C CD  A ARG A 1 223 ? 21.42600  58.73800  4.45700  0.700 65.56226  ? 553 ARG A CD  1 
ATOM   3012 C CD  B ARG A 1 223 ? 19.97100  57.33700  2.87200  0.300 54.02485  ? 553 ARG A CD  1 
ATOM   3013 N NE  A ARG A 1 223 ? 21.94500  60.10200  4.38400  0.700 79.79223  ? 553 ARG A NE  1 
ATOM   3014 N NE  B ARG A 1 223 ? 21.36800  57.01700  2.60200  0.300 56.79136  ? 553 ARG A NE  1 
ATOM   3015 C CZ  A ARG A 1 223 ? 22.95400  60.57800  5.09600  0.700 92.07453  ? 553 ARG A CZ  1 
ATOM   3016 C CZ  B ARG A 1 223 ? 21.79800  56.39800  1.51100  0.300 57.61807  ? 553 ARG A CZ  1 
ATOM   3017 N NH1 A ARG A 1 223 ? 23.59300  59.82800  5.97700  0.700 71.08454  ? 553 ARG A NH1 1 
ATOM   3018 N NH1 B ARG A 1 223 ? 20.96100  56.00200  0.56500  0.300 55.59263  ? 553 ARG A NH1 1 
ATOM   3019 N NH2 A ARG A 1 223 ? 23.32700  61.84200  4.91900  0.700 76.52110  ? 553 ARG A NH2 1 
ATOM   3020 N NH2 B ARG A 1 223 ? 23.09900  56.16500  1.36700  0.300 52.53857  ? 553 ARG A NH2 1 
ATOM   3021 N N   A CYS A 1 224 ? 16.20100  59.66000  5.24000  0.700 69.99563  ? 554 CYS A N   1 
ATOM   3022 N N   B CYS A 1 224 ? 16.26200  59.70000  5.18800  0.300 69.61664  ? 554 CYS A N   1 
ATOM   3023 C CA  A CYS A 1 224 ? 15.21500  59.14600  6.18900  0.700 60.40485  ? 554 CYS A CA  1 
ATOM   3024 C CA  B CYS A 1 224 ? 15.28100  59.17500  6.13500  0.300 60.69101  ? 554 CYS A CA  1 
ATOM   3025 C C   A CYS A 1 224 ? 14.02500  58.52700  5.46400  0.700 55.12243  ? 554 CYS A C   1 
ATOM   3026 C C   B CYS A 1 224 ? 14.10500  58.51800  5.41900  0.300 55.62243  ? 554 CYS A C   1 
ATOM   3027 O O   A CYS A 1 224 ? 13.48500  57.50000  5.89600  0.700 57.75763  ? 554 CYS A O   1 
ATOM   3028 O O   B CYS A 1 224 ? 13.59400  57.48600  5.87000  0.300 58.17097  ? 554 CYS A O   1 
ATOM   3029 C CB  A CYS A 1 224 ? 14.75900  60.26600  7.12300  0.700 59.48517  ? 554 CYS A CB  1 
ATOM   3030 C CB  B CYS A 1 224 ? 14.80300  60.29000  7.06300  0.300 59.96158  ? 554 CYS A CB  1 
ATOM   3031 S SG  A CYS A 1 224 ? 16.02300  60.77300  8.31800  0.700 78.71917  ? 554 CYS A SG  1 
ATOM   3032 S SG  B CYS A 1 224 ? 16.04300  60.82600  8.26500  0.300 78.60735  ? 554 CYS A SG  1 
ATOM   3033 N N   A ARG A 1 225 ? 13.60200  59.14300  4.35700  0.700 59.82793  ? 555 ARG A N   1 
ATOM   3034 N N   B ARG A 1 225 ? 13.65900  59.09900  4.30100  0.300 60.09778  ? 555 ARG A N   1 
ATOM   3035 C CA  A ARG A 1 225 ? 12.50300  58.61000  3.56200  0.700 60.57960  ? 555 ARG A CA  1 
ATOM   3036 C CA  B ARG A 1 225 ? 12.57300  58.49500  3.53500  0.300 60.55019  ? 555 ARG A CA  1 
ATOM   3037 C C   A ARG A 1 225 ? 12.91000  57.36700  2.77500  0.700 64.22148  ? 555 ARG A C   1 
ATOM   3038 C C   B ARG A 1 225 ? 13.02500  57.24800  2.78800  0.300 63.45721  ? 555 ARG A C   1 
ATOM   3039 O O   A ARG A 1 225 ? 12.04100  56.55900  2.42900  0.700 61.20804  ? 555 ARG A O   1 
ATOM   3040 O O   B ARG A 1 225 ? 12.18800  56.40100  2.45900  0.300 60.73859  ? 555 ARG A O   1 
ATOM   3041 C CB  A ARG A 1 225 ? 11.98000  59.70200  2.62200  0.700 65.70345  ? 555 ARG A CB  1 
ATOM   3042 C CB  B ARG A 1 225 ? 11.95100  59.50500  2.56900  0.300 65.48586  ? 555 ARG A CB  1 
ATOM   3043 C CG  A ARG A 1 225 ? 10.75200  60.45700  3.13400  0.700 58.52672  ? 555 ARG A CG  1 
ATOM   3044 C CG  B ARG A 1 225 ? 11.39700  60.73400  3.26200  0.300 58.41709  ? 555 ARG A CG  1 
ATOM   3045 C CD  A ARG A 1 225 ? 10.12400  61.29800  2.02500  0.700 71.11289  ? 555 ARG A CD  1 
ATOM   3046 C CD  B ARG A 1 225 ? 10.52000  61.56600  2.34400  0.300 65.54891  ? 555 ARG A CD  1 
ATOM   3047 N NE  A ARG A 1 225 ? 8.92600   62.01600  2.45200  0.700 76.06215  ? 555 ARG A NE  1 
ATOM   3048 N NE  B ARG A 1 225 ? 9.97300   62.72700  3.03600  0.300 61.79695  ? 555 ARG A NE  1 
ATOM   3049 C CZ  A ARG A 1 225 ? 8.92300   63.15900  3.12400  0.700 61.24019  ? 555 ARG A CZ  1 
ATOM   3050 C CZ  B ARG A 1 225 ? 8.92400   63.42300  2.61900  0.300 63.09294  ? 555 ARG A CZ  1 
ATOM   3051 N NH1 A ARG A 1 225 ? 10.04500  63.73000  3.52200  0.700 57.17143  ? 555 ARG A NH1 1 
ATOM   3052 N NH1 B ARG A 1 225 ? 8.31200   63.13700  1.48200  0.300 65.41518  ? 555 ARG A NH1 1 
ATOM   3053 N NH2 A ARG A 1 225 ? 7.76200   63.74100  3.41100  0.700 60.10450  ? 555 ARG A NH2 1 
ATOM   3054 N NH2 B ARG A 1 225 ? 8.48800   64.44200  3.35400  0.300 59.71503  ? 555 ARG A NH2 1 
ATOM   3055 N N   A GLN A 1 226 ? 14.20500  57.19300  2.48900  0.700 65.44240  ? 556 GLN A N   1 
ATOM   3056 N N   B GLN A 1 226 ? 14.32400  57.11600  2.51300  0.300 64.67455  ? 556 GLN A N   1 
ATOM   3057 C CA  A GLN A 1 226 ? 14.67100  55.95700  1.86200  0.700 58.30083  ? 556 GLN A CA  1 
ATOM   3058 C CA  B GLN A 1 226 ? 14.82900  55.88100  1.92100  0.300 58.36249  ? 556 GLN A CA  1 
ATOM   3059 C C   A GLN A 1 226 ? 14.55200  54.78800  2.83100  0.700 60.95590  ? 556 GLN A C   1 
ATOM   3060 C C   B GLN A 1 226 ? 14.71300  54.73800  2.92100  0.300 60.72152  ? 556 GLN A C   1 
ATOM   3061 O O   A GLN A 1 226 ? 14.05100  53.71600  2.47000  0.700 61.56080  ? 556 GLN A O   1 
ATOM   3062 O O   B GLN A 1 226 ? 14.26000  53.64000  2.57600  0.300 60.91225  ? 556 GLN A O   1 
ATOM   3063 C CB  A GLN A 1 226 ? 16.11400  56.10200  1.37100  0.700 52.32479  ? 556 GLN A CB  1 
ATOM   3064 C CB  B GLN A 1 226 ? 16.27500  56.06100  1.45900  0.300 53.02481  ? 556 GLN A CB  1 
ATOM   3065 C CG  A GLN A 1 226 ? 16.27000  56.88200  0.07400  0.700 63.24970  ? 556 GLN A CG  1 
ATOM   3066 C CG  B GLN A 1 226 ? 16.69700  55.08400  0.37300  0.300 56.23929  ? 556 GLN A CG  1 
ATOM   3067 C CD  A GLN A 1 226 ? 17.66700  57.45000  -0.09500 0.700 77.05330  ? 556 GLN A CD  1 
ATOM   3068 C CD  B GLN A 1 226 ? 17.88000  55.58100  -0.43400 0.300 63.98670  ? 556 GLN A CD  1 
ATOM   3069 O OE1 A GLN A 1 226 ? 17.92900  58.60400  0.24300  0.700 75.17575  ? 556 GLN A OE1 1 
ATOM   3070 O OE1 B GLN A 1 226 ? 18.06900  56.78600  -0.60300 0.300 71.12669  ? 556 GLN A OE1 1 
ATOM   3071 N NE2 A GLN A 1 226 ? 18.57500  56.63300  -0.61900 0.700 72.13013  ? 556 GLN A NE2 1 
ATOM   3072 N NE2 B GLN A 1 226 ? 18.68200  54.65200  -0.94000 0.300 51.92747  ? 556 GLN A NE2 1 
ATOM   3073 N N   A VAL A 1 227 ? 15.00700  54.98600  4.07200  0.700 64.53037  ? 557 VAL A N   1 
ATOM   3074 N N   B VAL A 1 227 ? 15.13500  54.97700  4.16500  0.300 63.64377  ? 557 VAL A N   1 
ATOM   3075 C CA  A VAL A 1 227 ? 15.01500  53.91200  5.06600  0.700 51.17001  ? 557 VAL A CA  1 
ATOM   3076 C CA  B VAL A 1 227 ? 15.12400  53.92700  5.18000  0.300 51.10414  ? 557 VAL A CA  1 
ATOM   3077 C C   A VAL A 1 227 ? 13.58900  53.46000  5.35700  0.700 45.29108  ? 557 VAL A C   1 
ATOM   3078 C C   B VAL A 1 227 ? 13.69200  53.47400  5.44300  0.300 46.38259  ? 557 VAL A C   1 
ATOM   3079 O O   A VAL A 1 227 ? 13.30100  52.25800  5.41400  0.700 52.29763  ? 557 VAL A O   1 
ATOM   3080 O O   B VAL A 1 227 ? 13.40400  52.27400  5.51700  0.300 52.55686  ? 557 VAL A O   1 
ATOM   3081 C CB  A VAL A 1 227 ? 15.73500  54.37300  6.34700  0.700 49.10641  ? 557 VAL A CB  1 
ATOM   3082 C CB  B VAL A 1 227 ? 15.81000  54.41400  6.46900  0.300 49.10119  ? 557 VAL A CB  1 
ATOM   3083 C CG1 A VAL A 1 227 ? 15.62900  53.31900  7.43500  0.700 50.40289  ? 557 VAL A CG1 1 
ATOM   3084 C CG1 B VAL A 1 227 ? 15.67100  53.37300  7.57000  0.300 50.30563  ? 557 VAL A CG1 1 
ATOM   3085 C CG2 A VAL A 1 227 ? 17.19300  54.68300  6.06100  0.700 49.41675  ? 557 VAL A CG2 1 
ATOM   3086 C CG2 B VAL A 1 227 ? 17.27400  54.72500  6.20500  0.300 49.70227  ? 557 VAL A CG2 1 
ATOM   3087 N N   A VAL A 1 228 ? 12.68100  54.41900  5.55500  0.700 43.50673  ? 558 VAL A N   1 
ATOM   3088 N N   B VAL A 1 228 ? 12.77600  54.43600  5.59700  0.300 43.99470  ? 558 VAL A N   1 
ATOM   3089 C CA  A VAL A 1 228 ? 11.28000  54.10100  5.83300  0.700 44.88740  ? 558 VAL A CA  1 
ATOM   3090 C CA  B VAL A 1 228 ? 11.37300  54.11000  5.84800  0.300 44.93322  ? 558 VAL A CA  1 
ATOM   3091 C C   A VAL A 1 228 ? 10.69300  53.27200  4.69600  0.700 52.29109  ? 558 VAL A C   1 
ATOM   3092 C C   B VAL A 1 228 ? 10.81800  53.24900  4.71900  0.300 52.50531  ? 558 VAL A C   1 
ATOM   3093 O O   A VAL A 1 228 ? 9.97000   52.29400  4.92600  0.700 55.00869  ? 558 VAL A O   1 
ATOM   3094 O O   B VAL A 1 228 ? 10.10800  52.26500  4.96200  0.300 54.10532  ? 558 VAL A O   1 
ATOM   3095 C CB  A VAL A 1 228 ? 10.48000  55.39500  6.06700  0.700 45.42993  ? 558 VAL A CB  1 
ATOM   3096 C CB  B VAL A 1 228 ? 10.54900  55.40000  6.03000  0.300 45.63731  ? 558 VAL A CB  1 
ATOM   3097 C CG1 A VAL A 1 228 ? 8.98600   55.10600  6.05900  0.700 45.42784  ? 558 VAL A CG1 1 
ATOM   3098 C CG1 B VAL A 1 228 ? 9.05800   55.09600  5.98900  0.300 45.55883  ? 558 VAL A CG1 1 
ATOM   3099 C CG2 A VAL A 1 228 ? 10.91500  56.05800  7.36400  0.700 50.72018  ? 558 VAL A CG2 1 
ATOM   3100 C CG2 B VAL A 1 228 ? 10.92100  56.09400  7.32800  0.300 50.75963  ? 558 VAL A CG2 1 
ATOM   3101 N N   A THR A 1 229 ? 10.99000  53.65700  3.45300  0.700 61.90360  ? 559 THR A N   1 
ATOM   3102 N N   B THR A 1 229 ? 11.12600  53.60800  3.46900  0.300 60.97417  ? 559 THR A N   1 
ATOM   3103 C CA  A THR A 1 229 ? 10.53600  52.89100  2.29500  0.700 56.16425  ? 559 THR A CA  1 
ATOM   3104 C CA  B THR A 1 229 ? 10.68900  52.79300  2.33900  0.300 56.20483  ? 559 THR A CA  1 
ATOM   3105 C C   A THR A 1 229 ? 11.08600  51.46700  2.33700  0.700 55.93968  ? 559 THR A C   1 
ATOM   3106 C C   B THR A 1 229 ? 11.26900  51.38700  2.43000  0.300 55.28818  ? 559 THR A C   1 
ATOM   3107 O O   A THR A 1 229 ? 10.36200  50.50300  2.05600  0.700 50.12074  ? 559 THR A O   1 
ATOM   3108 O O   B THR A 1 229 ? 10.56000  50.40000  2.20000  0.300 51.81421  ? 559 THR A O   1 
ATOM   3109 C CB  A THR A 1 229 ? 10.94400  53.59300  0.99700  0.700 55.84978  ? 559 THR A CB  1 
ATOM   3110 C CB  B THR A 1 229 ? 11.07800  53.45300  1.01600  0.300 56.19275  ? 559 THR A CB  1 
ATOM   3111 O OG1 A THR A 1 229 ? 10.17400  54.78900  0.83400  0.700 58.25021  ? 559 THR A OG1 1 
ATOM   3112 O OG1 B THR A 1 229 ? 12.43500  53.90800  1.08300  0.300 51.70122  ? 559 THR A OG1 1 
ATOM   3113 C CG2 A THR A 1 229 ? 10.69300  52.68700  -0.19900 0.700 64.37005  ? 559 THR A CG2 1 
ATOM   3114 C CG2 B THR A 1 229 ? 10.15800  54.62700  0.71400  0.300 58.61454  ? 559 THR A CG2 1 
ATOM   3115 N N   A GLY A 1 230 ? 12.37100  51.32000  2.66800  0.700 54.13754  ? 560 GLY A N   1 
ATOM   3116 N N   B GLY A 1 230 ? 12.56200  51.27700  2.75000  0.300 53.74261  ? 560 GLY A N   1 
ATOM   3117 C CA  A GLY A 1 230 ? 12.95400  49.99200  2.80000  0.700 52.94373  ? 560 GLY A CA  1 
ATOM   3118 C CA  B GLY A 1 230 ? 13.15400  49.96100  2.93100  0.300 53.19566  ? 560 GLY A CA  1 
ATOM   3119 C C   A GLY A 1 230 ? 12.24500  49.15600  3.84900  0.700 55.27549  ? 560 GLY A C   1 
ATOM   3120 C C   B GLY A 1 230 ? 12.46400  49.18500  4.03500  0.300 54.55031  ? 560 GLY A C   1 
ATOM   3121 O O   A GLY A 1 230 ? 12.03300  47.95200  3.66400  0.700 55.39098  ? 560 GLY A O   1 
ATOM   3122 O O   B GLY A 1 230 ? 12.23100  47.98000  3.91000  0.300 53.80228  ? 560 GLY A O   1 
ATOM   3123 N N   A MET A 1 231 ? 11.87500  49.78100  4.96800  0.700 49.47546  ? 561 MET A N   1 
ATOM   3124 N N   B MET A 1 231 ? 12.13500  49.86400  5.13500  0.300 49.62594  ? 561 MET A N   1 
ATOM   3125 C CA  A MET A 1 231 ? 11.26900  49.04800  6.07200  0.700 44.65655  ? 561 MET A CA  1 
ATOM   3126 C CA  B MET A 1 231 ? 11.53800  49.18300  6.27800  0.300 46.52288  ? 561 MET A CA  1 
ATOM   3127 C C   A MET A 1 231 ? 9.88700   48.56100  5.69800  0.700 42.28070  ? 561 MET A C   1 
ATOM   3128 C C   B MET A 1 231 ? 10.12300  48.73600  5.94200  0.300 44.70048  ? 561 MET A C   1 
ATOM   3129 O O   A MET A 1 231 ? 9.49600   47.45000  6.07000  0.700 47.84525  ? 561 MET A O   1 
ATOM   3130 O O   B MET A 1 231 ? 9.67400   47.67400  6.38800  0.300 48.03800  ? 561 MET A O   1 
ATOM   3131 C CB  A MET A 1 231 ? 11.15100  49.95700  7.28000  0.700 41.94934  ? 561 MET A CB  1 
ATOM   3132 C CB  B MET A 1 231 ? 11.54600  50.09700  7.49800  0.300 46.33493  ? 561 MET A CB  1 
ATOM   3133 C CG  A MET A 1 231 ? 12.43400  50.34300  7.90800  0.700 43.14876  ? 561 MET A CG  1 
ATOM   3134 C CG  B MET A 1 231 ? 12.93200  50.37800  8.05100  0.300 47.70588  ? 561 MET A CG  1 
ATOM   3135 S SD  A MET A 1 231 ? 11.96600  51.26900  9.35900  0.700 39.91648  ? 561 MET A SD  1 
ATOM   3136 S SD  B MET A 1 231 ? 12.87900  51.35200  9.56400  0.300 39.26558  ? 561 MET A SD  1 
ATOM   3137 C CE  A MET A 1 231 ? 13.48300  51.15400  10.21100 0.700 37.98107  ? 561 MET A CE  1 
ATOM   3138 C CE  B MET A 1 231 ? 11.11100  51.49400  9.78700  0.300 45.10491  ? 561 MET A CE  1 
ATOM   3139 N N   A ALA A 1 232 ? 9.15700   49.36500  4.92700  0.700 38.73985  ? 562 ALA A N   1 
ATOM   3140 N N   B ALA A 1 232 ? 9.40700   49.54800  5.15800  0.300 42.92908  ? 562 ALA A N   1 
ATOM   3141 C CA  A ALA A 1 232 ? 7.82700   48.97200  4.48800  0.700 41.33395  ? 562 ALA A CA  1 
ATOM   3142 C CA  B ALA A 1 232 ? 8.05300   49.20500  4.73900  0.300 44.81465  ? 562 ALA A CA  1 
ATOM   3143 C C   A ALA A 1 232 ? 7.92500   47.72600  3.62500  0.700 45.14367  ? 562 ALA A C   1 
ATOM   3144 C C   B ALA A 1 232 ? 8.06700   47.94300  3.89000  0.300 46.32949  ? 562 ALA A C   1 
ATOM   3145 O O   A ALA A 1 232 ? 7.16600   46.76600  3.80900  0.700 44.48334  ? 562 ALA A O   1 
ATOM   3146 O O   B ALA A 1 232 ? 7.25200   47.03400  4.08800  0.300 45.90812  ? 562 ALA A O   1 
ATOM   3147 C CB  A ALA A 1 232 ? 7.16100   50.12300  3.73400  0.700 52.17509  ? 562 ALA A CB  1 
ATOM   3148 C CB  B ALA A 1 232 ? 7.42700   50.37100  3.97400  0.300 50.70448  ? 562 ALA A CB  1 
ATOM   3149 N N   A TRP A 1 233 ? 8.86300   47.72700  2.67700  0.700 53.10395  ? 563 TRP A N   1 
ATOM   3150 N N   B TRP A 1 233 ? 8.98600   47.87900  2.92300  0.300 51.99763  ? 563 TRP A N   1 
ATOM   3151 C CA  A TRP A 1 233 ? 9.04300   46.56600  1.81900  0.700 49.88399  ? 563 TRP A CA  1 
ATOM   3152 C CA  B TRP A 1 233 ? 9.09400   46.70200  2.06800  0.300 50.96979  ? 563 TRP A CA  1 
ATOM   3153 C C   A TRP A 1 233 ? 9.39000   45.35300  2.67600  0.700 49.09726  ? 563 TRP A C   1 
ATOM   3154 C C   B TRP A 1 233 ? 9.38300   45.47300  2.91800  0.300 49.43108  ? 563 TRP A C   1 
ATOM   3155 O O   A TRP A 1 233 ? 8.73300   44.30800  2.59100  0.700 53.40088  ? 563 TRP A O   1 
ATOM   3156 O O   B TRP A 1 233 ? 8.68700   44.45600  2.81400  0.300 51.72362  ? 563 TRP A O   1 
ATOM   3157 C CB  A TRP A 1 233 ? 10.15800  46.85400  0.81200  0.700 55.77914  ? 563 TRP A CB  1 
ATOM   3158 C CB  B TRP A 1 233 ? 10.18000  46.91500  1.01600  0.300 55.70929  ? 563 TRP A CB  1 
ATOM   3159 C CG  A TRP A 1 233 ? 9.70800   47.56900  -0.43400 0.700 67.57363  ? 563 TRP A CG  1 
ATOM   3160 C CG  B TRP A 1 233 ? 9.67300   47.60900  -0.20800 0.300 67.17936  ? 563 TRP A CG  1 
ATOM   3161 C CD1 A TRP A 1 233 ? 9.91200   48.88800  -0.72800 0.700 79.79983  ? 563 TRP A CD1 1 
ATOM   3162 C CD1 B TRP A 1 233 ? 9.88600   48.91100  -0.55700 0.300 78.22081  ? 563 TRP A CD1 1 
ATOM   3163 C CD2 A TRP A 1 233 ? 8.98600   47.02000  -1.54300 0.700 66.87983  ? 563 TRP A CD2 1 
ATOM   3164 C CD2 B TRP A 1 233 ? 8.83900   47.05100  -1.23100 0.300 66.92480  ? 563 TRP A CD2 1 
ATOM   3165 N NE1 A TRP A 1 233 ? 9.36400   49.19300  -1.94800 0.700 81.78110  ? 563 TRP A NE1 1 
ATOM   3166 N NE1 B TRP A 1 233 ? 9.25100   49.19400  -1.74200 0.300 80.64206  ? 563 TRP A NE1 1 
ATOM   3167 C CE2 A TRP A 1 233 ? 8.79000   48.06500  -2.47000 0.700 73.43550  ? 563 TRP A CE2 1 
ATOM   3168 C CE2 B TRP A 1 233 ? 8.60000   48.06900  -2.17500 0.300 72.29534  ? 563 TRP A CE2 1 
ATOM   3169 C CE3 A TRP A 1 233 ? 8.48800   45.74800  -1.84500 0.700 70.62829  ? 563 TRP A CE3 1 
ATOM   3170 C CE3 B TRP A 1 233 ? 8.27800   45.78800  -1.44300 0.300 69.43002  ? 563 TRP A CE3 1 
ATOM   3171 C CZ2 A TRP A 1 233 ? 8.11800   47.87700  -3.67500 0.700 88.11575  ? 563 TRP A CZ2 1 
ATOM   3172 C CZ2 B TRP A 1 233 ? 7.82400   47.86300  -3.31400 0.300 82.21425  ? 563 TRP A CZ2 1 
ATOM   3173 C CZ3 A TRP A 1 233 ? 7.82000   45.56500  -3.04300 0.700 75.81548  ? 563 TRP A CZ3 1 
ATOM   3174 C CZ3 B TRP A 1 233 ? 7.50800   45.58600  -2.57500 0.300 71.17674  ? 563 TRP A CZ3 1 
ATOM   3175 C CH2 A TRP A 1 233 ? 7.64200   46.62400  -3.94300 0.700 90.75732  ? 563 TRP A CH2 1 
ATOM   3176 C CH2 B TRP A 1 233 ? 7.28900   46.61800  -3.49500 0.300 81.55785  ? 563 TRP A CH2 1 
ATOM   3177 N N   A LEU A 1 234 ? 10.44300  45.47600  3.49500  0.700 50.21494  ? 564 LEU A N   1 
ATOM   3178 N N   B LEU A 1 234 ? 10.43400  45.54100  3.74100  0.300 50.12046  ? 564 LEU A N   1 
ATOM   3179 C CA  A LEU A 1 234 ? 10.83900  44.41100  4.41700  0.700 40.12042  ? 564 LEU A CA  1 
ATOM   3180 C CA  B LEU A 1 234 ? 10.76400  44.44700  4.65000  0.300 41.33447  ? 564 LEU A CA  1 
ATOM   3181 C C   A LEU A 1 234 ? 9.65900   43.92500  5.25000  0.700 40.97212  ? 564 LEU A C   1 
ATOM   3182 C C   B LEU A 1 234 ? 9.51700   44.02200  5.41700  0.300 42.19917  ? 564 LEU A C   1 
ATOM   3183 O O   A LEU A 1 234 ? 9.43300   42.71800  5.39200  0.700 40.81440  ? 564 LEU A O   1 
ATOM   3184 O O   B LEU A 1 234 ? 9.21600   42.83000  5.54100  0.300 42.50596  ? 564 LEU A O   1 
ATOM   3185 C CB  A LEU A 1 234 ? 11.95300  44.89900  5.34000  0.700 39.44114  ? 564 LEU A CB  1 
ATOM   3186 C CB  B LEU A 1 234 ? 11.87200  44.87400  5.61200  0.300 40.05839  ? 564 LEU A CB  1 
ATOM   3187 C CG  A LEU A 1 234 ? 13.37500  44.48000  4.99400  0.700 48.82144  ? 564 LEU A CG  1 
ATOM   3188 C CG  B LEU A 1 234 ? 13.28900  44.40500  5.28000  0.300 48.82433  ? 564 LEU A CG  1 
ATOM   3189 C CD1 A LEU A 1 234 ? 14.34100  45.01700  6.03900  0.700 51.66256  ? 564 LEU A CD1 1 
ATOM   3190 C CD1 B LEU A 1 234 ? 14.27300  44.86700  6.34500  0.300 51.64500  ? 564 LEU A CD1 1 
ATOM   3191 C CD2 A LEU A 1 234 ? 13.45400  42.96900  4.89700  0.700 43.50881  ? 564 LEU A CD2 1 
ATOM   3192 C CD2 B LEU A 1 234 ? 13.33500  42.90100  5.10900  0.300 44.11739  ? 564 LEU A CD2 1 
ATOM   3193 N N   A PHE A 1 235 ? 8.90800   44.87000  5.82600  0.700 46.25114  ? 565 PHE A N   1 
ATOM   3194 N N   B PHE A 1 235 ? 8.78500   45.00700  5.94300  0.300 46.16387  ? 565 PHE A N   1 
ATOM   3195 C CA  A PHE A 1 235 ? 7.86500   44.53700  6.79400  0.700 38.07391  ? 565 PHE A CA  1 
ATOM   3196 C CA  B PHE A 1 235 ? 7.66200   44.75400  6.84000  0.300 40.48173  ? 565 PHE A CA  1 
ATOM   3197 C C   A PHE A 1 235 ? 6.76500   43.71000  6.14400  0.700 44.01117  ? 565 PHE A C   1 
ATOM   3198 C C   B PHE A 1 235 ? 6.56800   43.97500  6.11900  0.300 44.84797  ? 565 PHE A C   1 
ATOM   3199 O O   A PHE A 1 235 ? 6.44200   42.60700  6.60400  0.700 49.37596  ? 565 PHE A O   1 
ATOM   3200 O O   B PHE A 1 235 ? 6.14400   42.90700  6.57300  0.300 48.61492  ? 565 PHE A O   1 
ATOM   3201 C CB  A PHE A 1 235 ? 7.29100   45.81900  7.40500  0.700 38.40997  ? 565 PHE A CB  1 
ATOM   3202 C CB  B PHE A 1 235 ? 7.13200   46.09600  7.34800  0.300 39.53319  ? 565 PHE A CB  1 
ATOM   3203 C CG  A PHE A 1 235 ? 6.20900   45.58200  8.42200  0.700 29.97878  ? 565 PHE A CG  1 
ATOM   3204 C CG  B PHE A 1 235 ? 5.97000   45.99500  8.29000  0.300 37.74263  ? 565 PHE A CG  1 
ATOM   3205 C CD1 A PHE A 1 235 ? 6.53000   45.40700  9.76000  0.700 44.34893  ? 565 PHE A CD1 1 
ATOM   3206 C CD1 B PHE A 1 235 ? 6.17400   45.87800  9.65400  0.300 44.43624  ? 565 PHE A CD1 1 
ATOM   3207 C CD2 A PHE A 1 235 ? 4.87500   45.54100  8.04600  0.700 35.62162  ? 565 PHE A CD2 1 
ATOM   3208 C CD2 B PHE A 1 235 ? 4.67100   46.03900  7.81200  0.300 43.27553  ? 565 PHE A CD2 1 
ATOM   3209 C CE1 A PHE A 1 235 ? 5.54200   45.19100  10.70500 0.700 47.73934  ? 565 PHE A CE1 1 
ATOM   3210 C CE1 B PHE A 1 235 ? 5.10600   45.81100  10.52000 0.300 43.52167  ? 565 PHE A CE1 1 
ATOM   3211 C CE2 A PHE A 1 235 ? 3.88300   45.32200  8.98600  0.700 31.68788  ? 565 PHE A CE2 1 
ATOM   3212 C CE2 B PHE A 1 235 ? 3.60000   45.95700  8.67300  0.300 42.34275  ? 565 PHE A CE2 1 
ATOM   3213 C CZ  A PHE A 1 235 ? 4.21600   45.14900  10.31700 0.700 36.32670  ? 565 PHE A CZ  1 
ATOM   3214 C CZ  B PHE A 1 235 ? 3.81600   45.84400  10.02900 0.300 37.94393  ? 565 PHE A CZ  1 
ATOM   3215 N N   A PHE A 1 236 ? 6.18800   44.22500  5.05500  0.700 50.30809  ? 566 PHE A N   1 
ATOM   3216 N N   B PHE A 1 236 ? 6.10300   44.49800  4.98100  0.300 50.31116  ? 566 PHE A N   1 
ATOM   3217 C CA  A PHE A 1 236 ? 5.03400   43.57900  4.44300  0.700 47.01133  ? 566 PHE A CA  1 
ATOM   3218 C CA  B PHE A 1 236 ? 4.97100   43.90400  4.27600  0.300 48.93932  ? 566 PHE A CA  1 
ATOM   3219 C C   A PHE A 1 236 ? 5.42500   42.26400  3.79100  0.700 47.39565  ? 566 PHE A C   1 
ATOM   3220 C C   B PHE A 1 236 ? 5.35400   42.56200  3.66000  0.300 48.57362  ? 566 PHE A C   1 
ATOM   3221 O O   A PHE A 1 236 ? 4.62200   41.32400  3.76200  0.700 42.36304  ? 566 PHE A O   1 
ATOM   3222 O O   B PHE A 1 236 ? 4.50600   41.67100  3.53400  0.300 46.49466  ? 566 PHE A O   1 
ATOM   3223 C CB  A PHE A 1 236 ? 4.39000   44.52800  3.43600  0.700 47.51713  ? 566 PHE A CB  1 
ATOM   3224 C CB  B PHE A 1 236 ? 4.44600   44.87900  3.22500  0.300 49.22554  ? 566 PHE A CB  1 
ATOM   3225 C CG  A PHE A 1 236 ? 3.62700   45.64800  4.08000  0.700 46.95805  ? 566 PHE A CG  1 
ATOM   3226 C CG  B PHE A 1 236 ? 3.68200   46.03200  3.81400  0.300 51.09644  ? 566 PHE A CG  1 
ATOM   3227 C CD1 A PHE A 1 236 ? 2.60500   45.37500  4.97900  0.700 48.56017  ? 566 PHE A CD1 1 
ATOM   3228 C CD1 B PHE A 1 236 ? 2.49300   45.81800  4.49200  0.300 51.14630  ? 566 PHE A CD1 1 
ATOM   3229 C CD2 A PHE A 1 236 ? 3.93700   46.96800  3.80500  0.700 56.96364  ? 566 PHE A CD2 1 
ATOM   3230 C CD2 B PHE A 1 236 ? 4.16600   47.32600  3.71400  0.300 55.03649  ? 566 PHE A CD2 1 
ATOM   3231 C CE1 A PHE A 1 236 ? 1.90000   46.39800  5.58400  0.700 52.81822  ? 566 PHE A CE1 1 
ATOM   3232 C CE1 B PHE A 1 236 ? 1.79300   46.87500  5.04500  0.300 55.24981  ? 566 PHE A CE1 1 
ATOM   3233 C CE2 A PHE A 1 236 ? 3.23600   47.99900  4.40800  0.700 58.38502  ? 566 PHE A CE2 1 
ATOM   3234 C CE2 B PHE A 1 236 ? 3.47100   48.38700  4.26500  0.300 56.97036  ? 566 PHE A CE2 1 
ATOM   3235 C CZ  A PHE A 1 236 ? 2.21700   47.71000  5.30000  0.700 56.38344  ? 566 PHE A CZ  1 
ATOM   3236 C CZ  B PHE A 1 236 ? 2.28300   48.16100  4.93100  0.300 54.57123  ? 566 PHE A CZ  1 
ATOM   3237 N N   A VAL A 1 237 ? 6.65600   42.17000  3.29000  0.700 46.96745  ? 567 VAL A N   1 
ATOM   3238 N N   B VAL A 1 237 ? 6.62100   42.40700  3.27400  0.300 47.49711  ? 567 VAL A N   1 
ATOM   3239 C CA  A VAL A 1 237 ? 7.09800   40.94100  2.64400  0.700 44.37745  ? 567 VAL A CA  1 
ATOM   3240 C CA  B VAL A 1 237 ? 7.09100   41.16500  2.66600  0.300 44.84066  ? 567 VAL A CA  1 
ATOM   3241 C C   A VAL A 1 237 ? 7.35800   39.87500  3.69800  0.700 50.75982  ? 567 VAL A C   1 
ATOM   3242 C C   B VAL A 1 237 ? 7.20400   40.08600  3.73600  0.300 50.00685  ? 567 VAL A C   1 
ATOM   3243 O O   A VAL A 1 237 ? 6.87600   38.74100  3.59100  0.700 56.70248  ? 567 VAL A O   1 
ATOM   3244 O O   B VAL A 1 237 ? 6.73900   38.95400  3.55600  0.300 55.08155  ? 567 VAL A O   1 
ATOM   3245 C CB  A VAL A 1 237 ? 8.34300   41.20200  1.77800  0.700 44.46537  ? 567 VAL A CB  1 
ATOM   3246 C CB  B VAL A 1 237 ? 8.42600   41.38400  1.93100  0.300 44.78997  ? 567 VAL A CB  1 
ATOM   3247 C CG1 A VAL A 1 237 ? 9.01900   39.89200  1.41100  0.700 30.76432  ? 567 VAL A CG1 1 
ATOM   3248 C CG1 B VAL A 1 237 ? 9.08900   40.04900  1.63000  0.300 32.57316  ? 567 VAL A CG1 1 
ATOM   3249 C CG2 A VAL A 1 237 ? 7.95900   41.97900  0.52500  0.700 46.74132  ? 567 VAL A CG2 1 
ATOM   3250 C CG2 B VAL A 1 237 ? 8.19500   42.15800  0.64200  0.300 47.25291  ? 567 VAL A CG2 1 
ATOM   3251 N N   A SER A 1 238 ? 8.10600   40.23000  4.74500  0.700 52.10310  ? 568 SER A N   1 
ATOM   3252 N N   B SER A 1 238 ? 7.82300   40.42600  4.86700  0.300 50.62874  ? 568 SER A N   1 
ATOM   3253 C CA  A SER A 1 238 ? 8.47600   39.24300  5.75400  0.700 48.28620  ? 568 SER A CA  1 
ATOM   3254 C CA  B SER A 1 238 ? 8.06400   39.44900  5.92200  0.300 48.83065  ? 568 SER A CA  1 
ATOM   3255 C C   A SER A 1 238 ? 7.26600   38.83800  6.59100  0.700 37.17062  ? 568 SER A C   1 
ATOM   3256 C C   B SER A 1 238 ? 6.75000   39.05000  6.58000  0.300 43.74926  ? 568 SER A C   1 
ATOM   3257 O O   A SER A 1 238 ? 7.02400   37.64500  6.80400  0.700 52.70288  ? 568 SER A O   1 
ATOM   3258 O O   B SER A 1 238 ? 6.51000   37.86200  6.82000  0.300 49.86555  ? 568 SER A O   1 
ATOM   3259 C CB  A SER A 1 238 ? 9.59100   39.79600  6.63700  0.700 50.12851  ? 568 SER A CB  1 
ATOM   3260 C CB  B SER A 1 238 ? 9.04300   40.00500  6.95600  0.300 51.14129  ? 568 SER A CB  1 
ATOM   3261 O OG  A SER A 1 238 ? 9.13600   40.91800  7.37200  0.700 58.17891  ? 568 SER A OG  1 
ATOM   3262 O OG  B SER A 1 238 ? 8.49300   41.12300  7.63200  0.300 56.41519  ? 568 SER A OG  1 
ATOM   3263 N N   A TRP A 1 239 ? 6.46500   39.81300  7.03500  0.700 42.51782  ? 569 TRP A N   1 
ATOM   3264 N N   B TRP A 1 239 ? 5.87800   40.02400  6.86400  0.300 47.29127  ? 569 TRP A N   1 
ATOM   3265 C CA  A TRP A 1 239 ? 5.26700   39.46900  7.80000  0.700 53.80865  ? 569 TRP A CA  1 
ATOM   3266 C CA  B TRP A 1 239 ? 4.58400   39.69100  7.45300  0.300 51.16169  ? 569 TRP A CA  1 
ATOM   3267 C C   A TRP A 1 239 ? 4.25500   38.75300  6.91900  0.700 46.23199  ? 569 TRP A C   1 
ATOM   3268 C C   B TRP A 1 239 ? 3.73500   38.90200  6.46800  0.300 50.48122  ? 569 TRP A C   1 
ATOM   3269 O O   A TRP A 1 239 ? 3.54100   37.85600  7.38300  0.700 44.61290  ? 569 TRP A O   1 
ATOM   3270 O O   B TRP A 1 239 ? 2.98200   38.00800  6.86900  0.300 50.22136  ? 569 TRP A O   1 
ATOM   3271 C CB  A TRP A 1 239 ? 4.64100   40.71100  8.43500  0.700 44.77302  ? 569 TRP A CB  1 
ATOM   3272 C CB  B TRP A 1 239 ? 3.82600   40.95500  7.85400  0.300 46.31198  ? 569 TRP A CB  1 
ATOM   3273 C CG  A TRP A 1 239 ? 5.38000   41.23600  9.62300  0.700 41.76037  ? 569 TRP A CG  1 
ATOM   3274 C CG  B TRP A 1 239 ? 4.28300   41.66700  9.07300  0.300 43.81321  ? 569 TRP A CG  1 
ATOM   3275 C CD1 A TRP A 1 239 ? 6.70900   41.53300  9.70400  0.700 45.00240  ? 569 TRP A CD1 1 
ATOM   3276 C CD1 B TRP A 1 239 ? 5.54600   42.07700  9.37200  0.300 48.55656  ? 569 TRP A CD1 1 
ATOM   3277 C CD2 A TRP A 1 239 ? 4.82200   41.54100  10.90700 0.700 42.89160  ? 569 TRP A CD2 1 
ATOM   3278 C CD2 B TRP A 1 239 ? 3.45000   42.10600  10.15100 0.300 46.40994  ? 569 TRP A CD2 1 
ATOM   3279 N NE1 A TRP A 1 239 ? 7.01400   41.99900  10.96100 0.700 46.41952  ? 569 TRP A NE1 1 
ATOM   3280 N NE1 B TRP A 1 239 ? 5.55600   42.72500  10.58500 0.300 51.81778  ? 569 TRP A NE1 1 
ATOM   3281 C CE2 A TRP A 1 239 ? 5.87100   42.01800  11.71700 0.700 48.35574  ? 569 TRP A CE2 1 
ATOM   3282 C CE2 B TRP A 1 239 ? 4.27800   42.76000  11.08000 0.300 47.70926  ? 569 TRP A CE2 1 
ATOM   3283 C CE3 A TRP A 1 239 ? 3.53500   41.45700  11.44900 0.700 43.74594  ? 569 TRP A CE3 1 
ATOM   3284 C CE3 B TRP A 1 239 ? 2.08200   42.00100  10.42400 0.300 46.20961  ? 569 TRP A CE3 1 
ATOM   3285 C CZ2 A TRP A 1 239 ? 5.67500   42.40700  13.04300 0.700 48.12592  ? 569 TRP A CZ2 1 
ATOM   3286 C CZ2 B TRP A 1 239 ? 3.78500   43.30200  12.26800 0.300 43.71983  ? 569 TRP A CZ2 1 
ATOM   3287 C CZ3 A TRP A 1 239 ? 3.34100   41.84400  12.76400 0.700 41.23431  ? 569 TRP A CZ3 1 
ATOM   3288 C CZ3 B TRP A 1 239 ? 1.59700   42.54100  11.59900 0.300 46.15387  ? 569 TRP A CZ3 1 
ATOM   3289 C CH2 A TRP A 1 239 ? 4.40600   42.31400  13.54600 0.700 46.57813  ? 569 TRP A CH2 1 
ATOM   3290 C CH2 B TRP A 1 239 ? 2.44500   43.18400  12.50600 0.300 42.24686  ? 569 TRP A CH2 1 
ATOM   3291 N N   A GLY A 1 240 ? 4.17000   39.14500  5.64800  0.700 51.12365  ? 570 GLY A N   1 
ATOM   3292 N N   B GLY A 1 240 ? 3.83500   39.22000  5.17600  0.300 53.52248  ? 570 GLY A N   1 
ATOM   3293 C CA  A GLY A 1 240 ? 3.23600   38.51600  4.73800  0.700 59.17145  ? 570 GLY A CA  1 
ATOM   3294 C CA  B GLY A 1 240 ? 3.04800   38.49000  4.20200  0.300 56.39840  ? 570 GLY A CA  1 
ATOM   3295 C C   A GLY A 1 240 ? 3.59900   37.08300  4.42100  0.700 54.74168  ? 570 GLY A C   1 
ATOM   3296 C C   B GLY A 1 240 ? 3.49300   37.05300  4.04500  0.300 54.46777  ? 570 GLY A C   1 
ATOM   3297 O O   A GLY A 1 240 ? 2.71800   36.29500  4.05400  0.700 47.87829  ? 570 GLY A O   1 
ATOM   3298 O O   B GLY A 1 240 ? 2.69700   36.21000  3.61700  0.300 50.83328  ? 570 GLY A O   1 
ATOM   3299 N N   A MET A 1 241 ? 4.87400   36.72300  4.58300  0.700 52.39317  ? 571 MET A N   1 
ATOM   3300 N N   B MET A 1 241 ? 4.75200   36.75700  4.38200  0.300 52.39583  ? 571 MET A N   1 
ATOM   3301 C CA  A MET A 1 241 ? 5.31700   35.36700  4.29900  0.700 55.38471  ? 571 MET A CA  1 
ATOM   3302 C CA  B MET A 1 241 ? 5.26100   35.39500  4.27400  0.300 55.44491  ? 571 MET A CA  1 
ATOM   3303 C C   A MET A 1 241 ? 4.82800   34.39000  5.36300  0.700 50.14380  ? 571 MET A C   1 
ATOM   3304 C C   B MET A 1 241 ? 4.70900   34.48900  5.36500  0.300 50.56720  ? 571 MET A C   1 
ATOM   3305 O O   A MET A 1 241 ? 4.78900   33.18000  5.11300  0.700 54.68627  ? 571 MET A O   1 
ATOM   3306 O O   B MET A 1 241 ? 4.73200   33.26400  5.20500  0.300 54.11394  ? 571 MET A O   1 
ATOM   3307 C CB  A MET A 1 241 ? 6.84400   35.31500  4.23300  0.700 57.11628  ? 571 MET A CB  1 
ATOM   3308 C CB  B MET A 1 241 ? 6.78900   35.39900  4.32900  0.300 56.79649  ? 571 MET A CB  1 
ATOM   3309 C CG  A MET A 1 241 ? 7.46700   35.69000  2.89000  0.700 57.80140  ? 571 MET A CG  1 
ATOM   3310 C CG  B MET A 1 241 ? 7.46700   35.63800  2.99300  0.300 57.87550  ? 571 MET A CG  1 
ATOM   3311 S SD  A MET A 1 241 ? 7.15600   34.58500  1.50700  0.700 81.70658  ? 571 MET A SD  1 
ATOM   3312 S SD  B MET A 1 241 ? 7.21400   34.26000  1.86100  0.300 72.60019  ? 571 MET A SD  1 
ATOM   3313 C CE  A MET A 1 241 ? 5.83100   35.48400  0.68700  0.700 58.08752  ? 571 MET A CE  1 
ATOM   3314 C CE  B MET A 1 241 ? 8.52800   33.16100  2.38500  0.300 42.27341  ? 571 MET A CE  1 
ATOM   3315 N N   A PHE A 1 242 ? 4.46600   34.89500  6.54700  0.700 54.65811  ? 572 PHE A N   1 
ATOM   3316 N N   B PHE A 1 242 ? 4.22300   35.06300  6.47400  0.300 55.53417  ? 572 PHE A N   1 
ATOM   3317 C CA  A PHE A 1 242 ? 4.15300   34.01600  7.67400  0.700 53.41009  ? 572 PHE A CA  1 
ATOM   3318 C CA  B PHE A 1 242 ? 3.84600   34.23700  7.62000  0.300 53.92432  ? 572 PHE A CA  1 
ATOM   3319 C C   A PHE A 1 242 ? 2.88600   33.20300  7.43100  0.700 51.07275  ? 572 PHE A C   1 
ATOM   3320 C C   B PHE A 1 242 ? 2.63000   33.37300  7.30700  0.300 51.43575  ? 572 PHE A C   1 
ATOM   3321 O O   A PHE A 1 242 ? 2.93400   31.97000  7.59000  0.700 53.26104  ? 572 PHE A O   1 
ATOM   3322 O O   B PHE A 1 242 ? 2.70300   32.14800  7.51000  0.300 53.92196  ? 572 PHE A O   1 
ATOM   3323 C CB  A PHE A 1 242 ? 4.08200   34.81900  8.97900  0.700 47.29373  ? 572 PHE A CB  1 
ATOM   3324 C CB  B PHE A 1 242 ? 3.64100   35.11400  8.86200  0.300 50.73002  ? 572 PHE A CB  1 
ATOM   3325 C CG  A PHE A 1 242 ? 5.42700   35.14300  9.57500  0.700 50.78045  ? 572 PHE A CG  1 
ATOM   3326 C CG  B PHE A 1 242 ? 4.92000   35.52600  9.53400  0.300 51.89489  ? 572 PHE A CG  1 
ATOM   3327 C CD1 A PHE A 1 242 ? 6.06700   34.23600  10.40700 0.700 50.12397  ? 572 PHE A CD1 1 
ATOM   3328 C CD1 B PHE A 1 242 ? 5.61000   34.64300  10.34700 0.300 50.69149  ? 572 PHE A CD1 1 
ATOM   3329 C CD2 A PHE A 1 242 ? 6.04400   36.35500  9.32100  0.700 58.91144  ? 572 PHE A CD2 1 
ATOM   3330 C CD2 B PHE A 1 242 ? 5.43200   36.79700  9.35200  0.300 51.82228  ? 572 PHE A CD2 1 
ATOM   3331 C CE1 A PHE A 1 242 ? 7.30400   34.52900  10.96900 0.700 43.61391  ? 572 PHE A CE1 1 
ATOM   3332 C CE1 B PHE A 1 242 ? 6.78800   35.02500  10.96800 0.300 49.91330  ? 572 PHE A CE1 1 
ATOM   3333 C CE2 A PHE A 1 242 ? 7.28000   36.65600  9.87800  0.700 60.78954  ? 572 PHE A CE2 1 
ATOM   3334 C CE2 B PHE A 1 242 ? 6.61200   37.18200  9.96000  0.300 52.91513  ? 572 PHE A CE2 1 
ATOM   3335 C CZ  A PHE A 1 242 ? 7.91100   35.74200  10.70100 0.700 49.76087  ? 572 PHE A CZ  1 
ATOM   3336 C CZ  B PHE A 1 242 ? 7.29000   36.29500  10.77100 0.300 53.29962  ? 572 PHE A CZ  1 
ATOM   3337 N N   A PRO A 1 243 ? 1.73200   33.79600  7.08300  0.700 48.18820  ? 573 PRO A N   1 
ATOM   3338 N N   B PRO A 1 243 ? 1.49400   33.91600  6.84400  0.300 50.84480  ? 573 PRO A N   1 
ATOM   3339 C CA  A PRO A 1 243 ? 0.56000   32.94900  6.79100  0.700 47.63602  ? 573 PRO A CA  1 
ATOM   3340 C CA  B PRO A 1 243 ? 0.37400   33.03400  6.47300  0.300 51.19303  ? 573 PRO A CA  1 
ATOM   3341 C C   A PRO A 1 243 ? 0.82200   31.95900  5.67400  0.700 56.97888  ? 573 PRO A C   1 
ATOM   3342 C C   B PRO A 1 243 ? 0.73600   32.03200  5.39300  0.300 57.68009  ? 573 PRO A C   1 
ATOM   3343 O O   A PRO A 1 243 ? 0.24600   30.86300  5.67900  0.700 58.27207  ? 573 PRO A O   1 
ATOM   3344 O O   B PRO A 1 243 ? 0.16000   30.93700  5.36000  0.300 57.80627  ? 573 PRO A O   1 
ATOM   3345 C CB  A PRO A 1 243 ? -0.53400  33.95400  6.39900  0.700 55.38695  ? 573 PRO A CB  1 
ATOM   3346 C CB  B PRO A 1 243 ? -0.71400  34.00200  5.98600  0.300 56.20285  ? 573 PRO A CB  1 
ATOM   3347 C CG  A PRO A 1 243 ? 0.14700   35.26100  6.20600  0.700 59.81782  ? 573 PRO A CG  1 
ATOM   3348 C CG  B PRO A 1 243 ? -0.06600  35.31700  5.83200  0.300 59.78813  ? 573 PRO A CG  1 
ATOM   3349 C CD  A PRO A 1 243 ? 1.41900   35.23400  6.97300  0.700 55.52145  ? 573 PRO A CD  1 
ATOM   3350 C CD  B PRO A 1 243 ? 1.14300   35.34100  6.69300  0.300 56.11583  ? 573 PRO A CD  1 
ATOM   3351 N N   A ILE A 1 244 ? 1.69500   32.30600  4.72600  0.700 58.46899  ? 574 ILE A N   1 
ATOM   3352 N N   B ILE A 1 244 ? 1.67000   32.37300  4.50300  0.300 57.93675  ? 574 ILE A N   1 
ATOM   3353 C CA  A ILE A 1 244 ? 2.01700   31.39000  3.63700  0.700 52.07454  ? 574 ILE A CA  1 
ATOM   3354 C CA  B ILE A 1 244 ? 2.06200   31.43900  3.45200  0.300 52.21270  ? 574 ILE A CA  1 
ATOM   3355 C C   A ILE A 1 244 ? 2.80700   30.19900  4.16600  0.700 50.05169  ? 574 ILE A C   1 
ATOM   3356 C C   B ILE A 1 244 ? 2.81300   30.25600  4.05000  0.300 50.70717  ? 574 ILE A C   1 
ATOM   3357 O O   A ILE A 1 244 ? 2.52200   29.05000  3.81100  0.700 57.67172  ? 574 ILE A O   1 
ATOM   3358 O O   B ILE A 1 244 ? 2.55200   29.09900  3.70200  0.300 57.38563  ? 574 ILE A O   1 
ATOM   3359 C CB  A ILE A 1 244 ? 2.74100   32.13300  2.50200  0.700 48.84724  ? 574 ILE A CB  1 
ATOM   3360 C CB  B ILE A 1 244 ? 2.90200   32.16100  2.38300  0.300 49.35927  ? 574 ILE A CB  1 
ATOM   3361 C CG1 A ILE A 1 244 ? 1.89300   33.33600  2.07800  0.700 50.90412  ? 574 ILE A CG1 1 
ATOM   3362 C CG1 B ILE A 1 244 ? 2.16200   33.39700  1.86600  0.300 53.69696  ? 574 ILE A CG1 1 
ATOM   3363 C CG2 A ILE A 1 244 ? 3.01900   31.20100  1.33900  0.700 47.06798  ? 574 ILE A CG2 1 
ATOM   3364 C CG2 B ILE A 1 244 ? 3.24000   31.21600  1.24000  0.300 47.50626  ? 574 ILE A CG2 1 
ATOM   3365 C CD1 A ILE A 1 244 ? 2.62500   34.36800  1.28600  0.700 56.59533  ? 574 ILE A CD1 1 
ATOM   3366 C CD1 B ILE A 1 244 ? 0.77500   33.10300  1.33500  0.300 46.31948  ? 574 ILE A CD1 1 
ATOM   3367 N N   A LEU A 1 245 ? 3.80200   30.44100  5.02600  0.700 50.51401  ? 575 LEU A N   1 
ATOM   3368 N N   B LEU A 1 245 ? 3.76200   30.52500  4.95100  0.300 51.05914  ? 575 LEU A N   1 
ATOM   3369 C CA  A LEU A 1 245 ? 4.57800   29.31900  5.54900  0.700 49.20826  ? 575 LEU A CA  1 
ATOM   3370 C CA  B LEU A 1 245 ? 4.51100   29.42600  5.55000  0.300 50.06723  ? 575 LEU A CA  1 
ATOM   3371 C C   A LEU A 1 245 ? 3.69600   28.43200  6.41300  0.700 50.89523  ? 575 LEU A C   1 
ATOM   3372 C C   B LEU A 1 245 ? 3.61100   28.57000  6.43000  0.300 51.25858  ? 575 LEU A C   1 
ATOM   3373 O O   A LEU A 1 245 ? 3.92100   27.21900  6.50100  0.700 47.94620  ? 575 LEU A O   1 
ATOM   3374 O O   B LEU A 1 245 ? 3.83100   27.35900  6.55400  0.300 48.23968  ? 575 LEU A O   1 
ATOM   3375 C CB  A LEU A 1 245 ? 5.79200   29.80100  6.34300  0.700 47.17418  ? 575 LEU A CB  1 
ATOM   3376 C CB  B LEU A 1 245 ? 5.69900   29.95700  6.35200  0.300 47.58956  ? 575 LEU A CB  1 
ATOM   3377 C CG  A LEU A 1 245 ? 6.97000   30.33700  5.53100  0.700 45.52850  ? 575 LEU A CG  1 
ATOM   3378 C CG  B LEU A 1 245 ? 6.89100   30.45200  5.53200  0.300 46.20256  ? 575 LEU A CG  1 
ATOM   3379 C CD1 A LEU A 1 245 ? 8.15100   30.64100  6.44500  0.700 50.41445  ? 575 LEU A CD1 1 
ATOM   3380 C CD1 B LEU A 1 245 ? 8.05100   30.81900  6.43900  0.300 50.58862  ? 575 LEU A CD1 1 
ATOM   3381 C CD2 A LEU A 1 245 ? 7.35900   29.33300  4.45800  0.700 39.19194  ? 575 LEU A CD2 1 
ATOM   3382 C CD2 B LEU A 1 245 ? 7.31400   29.40400  4.51500  0.300 39.09358  ? 575 LEU A CD2 1 
ATOM   3383 N N   A PHE A 1 246 ? 2.70100   29.03400  7.06600  0.700 55.18941  ? 576 PHE A N   1 
ATOM   3384 N N   B PHE A 1 246 ? 2.60300   29.18600  7.05100  0.300 55.36700  ? 576 PHE A N   1 
ATOM   3385 C CA  A PHE A 1 246 ? 1.74800   28.28400  7.87600  0.700 57.74490  ? 576 PHE A CA  1 
ATOM   3386 C CA  B PHE A 1 246 ? 1.65300   28.44900  7.87500  0.300 57.45637  ? 576 PHE A CA  1 
ATOM   3387 C C   A PHE A 1 246 ? 0.96900   27.30800  7.00100  0.700 59.74599  ? 576 PHE A C   1 
ATOM   3388 C C   B PHE A 1 246 ? 0.87800   27.44600  7.02800  0.300 60.00577  ? 576 PHE A C   1 
ATOM   3389 O O   A PHE A 1 246 ? 0.92900   26.10200  7.27300  0.700 69.71550  ? 576 PHE A O   1 
ATOM   3390 O O   B PHE A 1 246 ? 0.84700   26.24700  7.32800  0.300 68.67525  ? 576 PHE A O   1 
ATOM   3391 C CB  A PHE A 1 246 ? 0.80700   29.25900  8.59200  0.700 57.15212  ? 576 PHE A CB  1 
ATOM   3392 C CB  B PHE A 1 246 ? 0.70900   29.43200  8.57600  0.300 56.97971  ? 576 PHE A CB  1 
ATOM   3393 C CG  A PHE A 1 246 ? -0.05200  28.62500  9.65500  0.700 60.35745  ? 576 PHE A CG  1 
ATOM   3394 C CG  B PHE A 1 246 ? -0.14200  28.81200  9.65100  0.300 59.81077  ? 576 PHE A CG  1 
ATOM   3395 C CD1 A PHE A 1 246 ? -1.15600  27.85600  9.31300  0.700 56.27461  ? 576 PHE A CD1 1 
ATOM   3396 C CD1 B PHE A 1 246 ? -1.24100  28.03000  9.33100  0.300 55.89981  ? 576 PHE A CD1 1 
ATOM   3397 C CD2 A PHE A 1 246 ? 0.24000   28.80900  10.99900 0.700 57.85591  ? 576 PHE A CD2 1 
ATOM   3398 C CD2 B PHE A 1 246 ? 0.15800   29.01900  10.98800 0.300 57.71287  ? 576 PHE A CD2 1 
ATOM   3399 C CE1 A PHE A 1 246 ? -1.94600  27.27600  10.28800 0.700 46.69289  ? 576 PHE A CE1 1 
ATOM   3400 C CE1 B PHE A 1 246 ? -2.02100  27.46400  10.32200 0.300 47.16428  ? 576 PHE A CE1 1 
ATOM   3401 C CE2 A PHE A 1 246 ? -0.54800  28.23000  11.98000 0.700 51.26046  ? 576 PHE A CE2 1 
ATOM   3402 C CE2 B PHE A 1 246 ? -0.61800  28.45600  11.98400 0.300 51.23925  ? 576 PHE A CE2 1 
ATOM   3403 C CZ  A PHE A 1 246 ? -1.64300  27.46300  11.62300 0.700 38.27427  ? 576 PHE A CZ  1 
ATOM   3404 C CZ  B PHE A 1 246 ? -1.70900  27.67700  11.65000 0.300 39.49710  ? 576 PHE A CZ  1 
ATOM   3405 N N   A ILE A 1 247 ? 0.33800   27.82500  5.94100  0.700 62.54140  ? 577 ILE A N   1 
ATOM   3406 N N   B ILE A 1 247 ? 0.22400   27.93600  5.96900  0.300 62.15055  ? 577 ILE A N   1 
ATOM   3407 C CA  A ILE A 1 247 ? -0.44600  27.00700  5.01300  0.700 63.83635  ? 577 ILE A CA  1 
ATOM   3408 C CA  B ILE A 1 247 ? -0.54600  27.07600  5.07000  0.300 63.90236  ? 577 ILE A CA  1 
ATOM   3409 C C   A ILE A 1 247 ? 0.37800   25.84300  4.46000  0.700 71.03537  ? 577 ILE A C   1 
ATOM   3410 C C   B ILE A 1 247 ? 0.31700   25.94500  4.52800  0.300 71.24314  ? 577 ILE A C   1 
ATOM   3411 O O   A ILE A 1 247 ? -0.12800  24.72200  4.31700  0.700 94.98081  ? 577 ILE A O   1 
ATOM   3412 O O   B ILE A 1 247 ? -0.13600  24.80000  4.39900  0.300 94.41278  ? 577 ILE A O   1 
ATOM   3413 C CB  A ILE A 1 247 ? -1.00200  27.89800  3.88400  0.700 58.99984  ? 577 ILE A CB  1 
ATOM   3414 C CB  B ILE A 1 247 ? -1.14800  27.91500  3.92500  0.300 59.75844  ? 577 ILE A CB  1 
ATOM   3415 C CG1 A ILE A 1 247 ? -2.11300  28.80400  4.42000  0.700 65.36937  ? 577 ILE A CG1 1 
ATOM   3416 C CG1 B ILE A 1 247 ? -2.28900  28.79300  4.43600  0.300 65.50430  ? 577 ILE A CG1 1 
ATOM   3417 C CG2 A ILE A 1 247 ? -1.53300  27.05600  2.74200  0.700 75.17644  ? 577 ILE A CG2 1 
ATOM   3418 C CG2 B ILE A 1 247 ? -1.63200  27.02300  2.78900  0.300 75.14293  ? 577 ILE A CG2 1 
ATOM   3419 C CD1 A ILE A 1 247 ? -2.47600  29.94300  3.48800  0.700 69.75065  ? 577 ILE A CD1 1 
ATOM   3420 C CD1 B ILE A 1 247 ? -2.68600  29.88400  3.46600  0.300 69.15474  ? 577 ILE A CD1 1 
ATOM   3421 N N   A LEU A 1 248 ? 1.66500   26.07300  4.17900  0.700 58.31966  ? 578 LEU A N   1 
ATOM   3422 N N   B LEU A 1 248 ? 1.58000   26.24000  4.22100  0.300 59.18044  ? 578 LEU A N   1 
ATOM   3423 C CA  A LEU A 1 248 ? 2.50700   25.03500  3.58000  0.700 56.30189  ? 578 LEU A CA  1 
ATOM   3424 C CA  B LEU A 1 248 ? 2.45600   25.24500  3.62000  0.300 57.48311  ? 578 LEU A CA  1 
ATOM   3425 C C   A LEU A 1 248 ? 3.03900   24.04100  4.60500  0.700 60.34109  ? 578 LEU A C   1 
ATOM   3426 C C   B LEU A 1 248 ? 3.07400   24.29300  4.63600  0.300 61.53461  ? 578 LEU A C   1 
ATOM   3427 O O   A LEU A 1 248 ? 3.39800   22.91900  4.23000  0.700 74.20814  ? 578 LEU A O   1 
ATOM   3428 O O   B LEU A 1 248 ? 3.45300   23.17800  4.26300  0.300 70.79619  ? 578 LEU A O   1 
ATOM   3429 C CB  A LEU A 1 248 ? 3.69700   25.63000  2.81500  0.700 53.71121  ? 578 LEU A CB  1 
ATOM   3430 C CB  B LEU A 1 248 ? 3.56600   25.94100  2.82800  0.300 56.57252  ? 578 LEU A CB  1 
ATOM   3431 C CG  A LEU A 1 248 ? 3.58900   26.36800  1.47500  0.700 55.13754  ? 578 LEU A CG  1 
ATOM   3432 C CG  B LEU A 1 248 ? 3.17000   26.63600  1.52400  0.300 57.77192  ? 578 LEU A CG  1 
ATOM   3433 C CD1 A LEU A 1 248 ? 2.38100   27.28800  1.35600  0.700 60.47157  ? 578 LEU A CD1 1 
ATOM   3434 C CD1 B LEU A 1 248 ? 4.39400   27.23300  0.84500  0.300 52.71855  ? 578 LEU A CD1 1 
ATOM   3435 C CD2 A LEU A 1 248 ? 4.88600   27.13500  1.21600  0.700 48.18105  ? 578 LEU A CD2 1 
ATOM   3436 C CD2 B LEU A 1 248 ? 2.45500   25.67000  0.59200  0.300 54.80405  ? 578 LEU A CD2 1 
ATOM   3437 N N   A GLY A 1 249 ? 3.11300   24.42400  5.87500  0.700 61.64501  ? 579 GLY A N   1 
ATOM   3438 N N   B GLY A 1 249 ? 3.18600   24.69500  5.90300  0.300 62.95244  ? 579 GLY A N   1 
ATOM   3439 C CA  A GLY A 1 249 ? 3.80500   23.63700  6.86500  0.700 58.71811  ? 579 GLY A CA  1 
ATOM   3440 C CA  B GLY A 1 249 ? 3.96100   23.93200  6.85000  0.300 61.20341  ? 579 GLY A CA  1 
ATOM   3441 C C   A GLY A 1 249 ? 2.92800   22.53800  7.42900  0.700 59.96794  ? 579 GLY A C   1 
ATOM   3442 C C   B GLY A 1 249 ? 3.16800   22.80500  7.47500  0.300 62.49734  ? 579 GLY A C   1 
ATOM   3443 O O   A GLY A 1 249 ? 1.76700   22.35000  7.03600  0.700 71.32998  ? 579 GLY A O   1 
ATOM   3444 O O   B GLY A 1 249 ? 1.98400   22.58500  7.18400  0.300 71.54257  ? 579 GLY A O   1 
ATOM   3445 N N   A PRO A 1 250 ? 3.49900   21.76800  8.36100  0.700 51.10405  ? 580 PRO A N   1 
ATOM   3446 N N   B PRO A 1 250 ? 3.84200   22.05100  8.34900  0.300 56.47593  ? 580 PRO A N   1 
ATOM   3447 C CA  A PRO A 1 250 ? 2.69500   20.76200  9.08000  0.700 46.90959  ? 580 PRO A CA  1 
ATOM   3448 C CA  B PRO A 1 250 ? 3.14600   21.01800  9.13800  0.300 52.42590  ? 580 PRO A CA  1 
ATOM   3449 C C   A PRO A 1 250 ? 1.42800   21.33000  9.69300  0.700 59.07152  ? 580 PRO A C   1 
ATOM   3450 C C   B PRO A 1 250 ? 1.93500   21.51500  9.91100  0.300 59.83257  ? 580 PRO A C   1 
ATOM   3451 O O   A PRO A 1 250 ? 0.45100   20.59100  9.87900  0.700 55.93944  ? 580 PRO A O   1 
ATOM   3452 O O   B PRO A 1 250 ? 1.01100   20.72900  10.16000 0.300 57.94075  ? 580 PRO A O   1 
ATOM   3453 C CB  A PRO A 1 250 ? 3.66100   20.23700  10.15200 0.700 43.86123  ? 580 PRO A CB  1 
ATOM   3454 C CB  B PRO A 1 250 ? 4.23900   20.50700  10.08800 0.300 51.42627  ? 580 PRO A CB  1 
ATOM   3455 C CG  A PRO A 1 250 ? 5.02400   20.55300  9.63800  0.700 59.24391  ? 580 PRO A CG  1 
ATOM   3456 C CG  B PRO A 1 250 ? 5.52400   20.86200  9.43200  0.300 59.09185  ? 580 PRO A CG  1 
ATOM   3457 C CD  A PRO A 1 250 ? 4.89900   21.80100  8.81700  0.700 59.57599  ? 580 PRO A CD  1 
ATOM   3458 C CD  B PRO A 1 250 ? 5.28100   22.11300  8.64800  0.300 59.37494  ? 580 PRO A CD  1 
ATOM   3459 N N   A GLU A 1 251 ? 1.41800   22.62100  10.02900 0.700 68.81630  ? 581 GLU A N   1 
ATOM   3460 N N   B GLU A 1 251 ? 1.90200   22.79200  10.30100 0.300 65.50116  ? 581 GLU A N   1 
ATOM   3461 C CA  A GLU A 1 251 ? 0.23700   23.25300  10.60100 0.700 65.72702  ? 581 GLU A CA  1 
ATOM   3462 C CA  B GLU A 1 251 ? 0.75400   23.30200  11.04200 0.300 63.01557  ? 581 GLU A CA  1 
ATOM   3463 C C   A GLU A 1 251 ? -0.88700  23.39900  9.58000  0.700 73.61914  ? 581 GLU A C   1 
ATOM   3464 C C   B GLU A 1 251 ? -0.50300  23.42100  10.19200 0.300 69.19766  ? 581 GLU A C   1 
ATOM   3465 O O   A GLU A 1 251 ? -2.00900  23.74900  9.96100  0.700 68.87554  ? 581 GLU A O   1 
ATOM   3466 O O   B GLU A 1 251 ? -1.57900  23.66200  10.74800 0.300 64.49213  ? 581 GLU A O   1 
ATOM   3467 C CB  A GLU A 1 251 ? 0.60900   24.62000  11.18400 0.700 66.55030  ? 581 GLU A CB  1 
ATOM   3468 C CB  B GLU A 1 251 ? 1.08900   24.65800  11.66300 0.300 63.09971  ? 581 GLU A CB  1 
ATOM   3469 C CG  A GLU A 1 251 ? 1.50800   25.46000  10.28200 0.700 61.10894  ? 581 GLU A CG  1 
ATOM   3470 C CG  B GLU A 1 251 ? 1.42400   25.73900  10.65400 0.300 61.98232  ? 581 GLU A CG  1 
ATOM   3471 C CD  A GLU A 1 251 ? 2.93000   25.59600  10.80900 0.700 65.35211  ? 581 GLU A CD  1 
ATOM   3472 C CD  B GLU A 1 251 ? 2.91400   25.99100  10.54700 0.300 64.21129  ? 581 GLU A CD  1 
ATOM   3473 O OE1 A GLU A 1 251 ? 3.70600   24.62000  10.69500 0.700 65.44931  ? 581 GLU A OE1 1 
ATOM   3474 O OE1 B GLU A 1 251 ? 3.61600   25.16500  9.92600  0.300 60.69375  ? 581 GLU A OE1 1 
ATOM   3475 O OE2 A GLU A 1 251 ? 3.27500   26.68300  11.32600 0.700 71.03027  ? 581 GLU A OE2 1 
ATOM   3476 O OE2 B GLU A 1 251 ? 3.38400   27.01400  11.08900 0.300 66.26562  ? 581 GLU A OE2 1 
ATOM   3477 N N   A GLY A 1 252 ? -0.60300  23.16700  8.29900  0.700 79.86181  ? 582 GLY A N   1 
ATOM   3478 N N   B GLY A 1 252 ? -0.39600  23.29900  8.87200  0.300 76.72811  ? 582 GLY A N   1 
ATOM   3479 C CA  A GLY A 1 252 ? -1.55600  23.34600  7.22000  0.700 96.90594  ? 582 GLY A CA  1 
ATOM   3480 C CA  B GLY A 1 252 ? -1.55100  23.47200  8.01400  0.300 86.60299  ? 582 GLY A CA  1 
ATOM   3481 C C   A GLY A 1 252 ? -1.67200  22.08100  6.39200  0.700 142.88420 ? 582 GLY A C   1 
ATOM   3482 C C   B GLY A 1 252 ? -1.71900  22.27100  7.10900  0.300 121.42567 ? 582 GLY A C   1 
ATOM   3483 O O   A GLY A 1 252 ? -2.31300  21.11100  6.81100  0.700 137.15548 ? 582 GLY A O   1 
ATOM   3484 O O   B GLY A 1 252 ? -2.17000  21.20600  7.54300  0.300 123.97284 ? 582 GLY A O   1 
ATOM   3485 N N   A PHE A 1 253 ? -1.04900  22.08000  5.21300  0.700 159.43539 ? 583 PHE A N   1 
ATOM   3486 N N   B PHE A 1 253 ? -1.35300  22.43600  5.84200  0.300 281.01500 ? 583 PHE A N   1 
ATOM   3487 C CA  A PHE A 1 253 ? -1.15500  20.99700  4.24300  0.700 176.02734 ? 583 PHE A CA  1 
ATOM   3488 C CA  B PHE A 1 253 ? -1.54900  21.41600  4.81500  0.300 281.73877 ? 583 PHE A CA  1 
ATOM   3489 C C   A PHE A 1 253 ? 0.07900   20.10200  4.21200  0.700 139.36582 ? 583 PHE A C   1 
ATOM   3490 C C   B PHE A 1 253 ? -0.18400  20.78800  4.55700  0.300 278.78315 ? 583 PHE A C   1 
ATOM   3491 O O   A PHE A 1 253 ? 0.18100   19.23500  3.33900  0.700 131.22813 ? 583 PHE A O   1 
ATOM   3492 O O   B PHE A 1 253 ? 0.68800   21.40600  3.94100  0.300 278.89896 ? 583 PHE A O   1 
ATOM   3493 C CB  A PHE A 1 253 ? -1.45300  21.54500  2.84600  0.700 173.70589 ? 583 PHE A CB  1 
ATOM   3494 C CB  B PHE A 1 253 ? -2.17400  22.01200  3.55900  0.300 282.68888 ? 583 PHE A CB  1 
ATOM   3495 C CG  A PHE A 1 253 ? -2.80300  22.19400  2.73000  0.700 208.76944 ? 583 PHE A CG  1 
ATOM   3496 C CG  B PHE A 1 253 ? -3.57400  22.51800  3.77000  0.300 296.03259 ? 583 PHE A CG  1 
ATOM   3497 C CD1 A PHE A 1 253 ? -3.94300  21.51500  3.13900  0.700 227.99232 ? 583 PHE A CD1 1 
ATOM   3498 C CD1 B PHE A 1 253 ? -4.54000  21.69800  4.33100  0.300 295.92205 ? 583 PHE A CD1 1 
ATOM   3499 C CD2 A PHE A 1 253 ? -2.94000  23.46700  2.20200  0.700 204.58367 ? 583 PHE A CD2 1 
ATOM   3500 C CD2 B PHE A 1 253 ? -3.92200  23.81100  3.42000  0.300 298.46446 ? 583 PHE A CD2 1 
ATOM   3501 C CE1 A PHE A 1 253 ? -5.19100  22.09500  3.03300  0.700 239.04735 ? 583 PHE A CE1 1 
ATOM   3502 C CE1 B PHE A 1 253 ? -5.82900  22.15500  4.53300  0.300 297.16957 ? 583 PHE A CE1 1 
ATOM   3503 C CE2 A PHE A 1 253 ? -4.19000  24.05500  2.09300  0.700 224.12039 ? 583 PHE A CE2 1 
ATOM   3504 C CE2 B PHE A 1 253 ? -5.21100  24.27500  3.62000  0.300 307.79453 ? 583 PHE A CE2 1 
ATOM   3505 C CZ  A PHE A 1 253 ? -5.31600  23.36800  2.50900  0.700 241.08814 ? 583 PHE A CZ  1 
ATOM   3506 C CZ  B PHE A 1 253 ? -6.16500  23.44500  4.17700  0.300 309.52631 ? 583 PHE A CZ  1 
ATOM   3507 N N   A GLY A 1 254 ? 1.01400   20.29700  5.13800  0.700 103.22318 ? 584 GLY A N   1 
ATOM   3508 N N   B GLY A 1 254 ? -0.00100  19.56400  5.05200  0.300 134.56606 ? 584 GLY A N   1 
ATOM   3509 C CA  A GLY A 1 254 ? 2.16800   19.41900  5.24400  0.700 85.25250  ? 584 GLY A CA  1 
ATOM   3510 C CA  B GLY A 1 254 ? 1.19300   18.76800  4.82900  0.300 107.62896 ? 584 GLY A CA  1 
ATOM   3511 C C   A GLY A 1 254 ? 3.03400   19.32500  4.00900  0.700 73.95379  ? 584 GLY A C   1 
ATOM   3512 C C   B GLY A 1 254 ? 1.89100   18.90900  3.49000  0.300 96.23429  ? 584 GLY A C   1 
ATOM   3513 O O   A GLY A 1 254 ? 3.71300   18.31000  3.81300  0.700 92.66582  ? 584 GLY A O   1 
ATOM   3514 O O   B GLY A 1 254 ? 1.70700   18.07800  2.59500  0.300 104.56524 ? 584 GLY A O   1 
ATOM   3515 N N   A VAL A 1 255 ? 3.02300   20.35300  3.15900  0.700 70.12224  ? 585 VAL A N   1 
ATOM   3516 N N   B VAL A 1 255 ? 2.69600   19.96100  3.34300  0.300 76.60453  ? 585 VAL A N   1 
ATOM   3517 C CA  A VAL A 1 255 ? 3.97900   20.40400  2.05600  0.700 68.42124  ? 585 VAL A CA  1 
ATOM   3518 C CA  B VAL A 1 255 ? 3.56400   20.11300  2.18000  0.300 71.04337  ? 585 VAL A CA  1 
ATOM   3519 C C   A VAL A 1 255 ? 5.39600   20.43000  2.61300  0.700 59.32795  ? 585 VAL A C   1 
ATOM   3520 C C   B VAL A 1 255 ? 5.00000   20.22300  2.67500  0.300 63.28568  ? 585 VAL A C   1 
ATOM   3521 O O   A VAL A 1 255 ? 6.24000   19.59600  2.26300  0.700 59.67810  ? 585 VAL A O   1 
ATOM   3522 O O   B VAL A 1 255 ? 5.87400   19.45200  2.26100  0.300 61.30551  ? 585 VAL A O   1 
ATOM   3523 C CB  A VAL A 1 255 ? 3.70000   21.61800  1.15200  0.700 66.56805  ? 585 VAL A CB  1 
ATOM   3524 C CB  B VAL A 1 255 ? 3.17100   21.33700  1.33300  0.300 71.43696  ? 585 VAL A CB  1 
ATOM   3525 C CG1 A VAL A 1 255 ? 4.77000   21.73400  0.07300  0.700 47.50318  ? 585 VAL A CG1 1 
ATOM   3526 C CG1 B VAL A 1 255 ? 4.16500   21.53700  0.19900  0.300 55.81985  ? 585 VAL A CG1 1 
ATOM   3527 C CG2 A VAL A 1 255 ? 2.31400   21.50900  0.53100  0.700 72.44196  ? 585 VAL A CG2 1 
ATOM   3528 C CG2 B VAL A 1 255 ? 1.75900   21.17800  0.79200  0.300 79.79895  ? 585 VAL A CG2 1 
ATOM   3529 N N   A LEU A 1 256 ? 5.67500   21.38900  3.49000  0.700 57.67600  ? 586 LEU A N   1 
ATOM   3530 N N   B LEU A 1 256 ? 5.25200   21.18300  3.56000  0.300 62.37388  ? 586 LEU A N   1 
ATOM   3531 C CA  A LEU A 1 256 ? 6.97700   21.49100  4.12900  0.700 57.66567  ? 586 LEU A CA  1 
ATOM   3532 C CA  B LEU A 1 256 ? 6.57500   21.35000  4.14100  0.300 59.82257  ? 586 LEU A CA  1 
ATOM   3533 C C   A LEU A 1 256 ? 7.03800   20.54000  5.32100  0.700 65.12235  ? 586 LEU A C   1 
ATOM   3534 C C   B LEU A 1 256 ? 6.74900   20.39300  5.31300  0.300 65.40291  ? 586 LEU A C   1 
ATOM   3535 O O   A LEU A 1 256 ? 6.04300   20.31500  6.01600  0.700 71.33904  ? 586 LEU A O   1 
ATOM   3536 O O   B LEU A 1 256 ? 5.80200   20.10200  6.05000  0.300 69.42354  ? 586 LEU A O   1 
ATOM   3537 C CB  A LEU A 1 256 ? 7.24000   22.92900  4.58100  0.700 64.09601  ? 586 LEU A CB  1 
ATOM   3538 C CB  B LEU A 1 256 ? 6.80700   22.79000  4.59900  0.300 62.27414  ? 586 LEU A CB  1 
ATOM   3539 C CG  A LEU A 1 256 ? 7.47900   23.96300  3.47600  0.700 54.30833  ? 586 LEU A CG  1 
ATOM   3540 C CG  B LEU A 1 256 ? 6.95800   23.84200  3.49900  0.300 56.72471  ? 586 LEU A CG  1 
ATOM   3541 C CD1 A LEU A 1 256 ? 7.33200   25.37900  4.01200  0.700 53.79978  ? 586 LEU A CD1 1 
ATOM   3542 C CD1 B LEU A 1 256 ? 6.78900   25.24000  4.07000  0.300 53.31243  ? 586 LEU A CD1 1 
ATOM   3543 C CD2 A LEU A 1 256 ? 8.84900   23.77100  2.84500  0.700 58.12396  ? 586 LEU A CD2 1 
ATOM   3544 C CD2 B LEU A 1 256 ? 8.30200   23.70100  2.79900  0.300 56.59312  ? 586 LEU A CD2 1 
ATOM   3545 N N   A SER A 1 257 ? 8.22300   19.98000  5.55200  0.700 56.35628  ? 587 SER A N   1 
ATOM   3546 N N   B SER A 1 257 ? 7.97200   19.90300  5.48400  0.300 58.11385  ? 587 SER A N   1 
ATOM   3547 C CA  A SER A 1 257 ? 8.50900   19.24700  6.77600  0.700 58.19137  ? 587 SER A CA  1 
ATOM   3548 C CA  B SER A 1 257 ? 8.30500   19.18800  6.70300  0.300 58.37619  ? 587 SER A CA  1 
ATOM   3549 C C   A SER A 1 257 ? 8.78400   20.20200  7.93700  0.700 52.51515  ? 587 SER A C   1 
ATOM   3550 C C   B SER A 1 257 ? 8.55200   20.16800  7.85000  0.300 53.51532  ? 587 SER A C   1 
ATOM   3551 O O   A SER A 1 257 ? 8.75400   21.42700  7.79600  0.700 54.18959  ? 587 SER A O   1 
ATOM   3552 O O   B SER A 1 257 ? 8.47700   21.39100  7.69500  0.300 55.11514  ? 587 SER A O   1 
ATOM   3553 C CB  A SER A 1 257 ? 9.69800   18.31500  6.56400  0.700 61.74802  ? 587 SER A CB  1 
ATOM   3554 C CB  B SER A 1 257 ? 9.52100   18.29400  6.47500  0.300 61.15238  ? 587 SER A CB  1 
ATOM   3555 O OG  A SER A 1 257 ? 10.89300  19.06700  6.45900  0.700 45.90497  ? 587 SER A OG  1 
ATOM   3556 O OG  B SER A 1 257 ? 10.70400  19.06300  6.34100  0.300 47.55735  ? 587 SER A OG  1 
ATOM   3557 N N   A VAL A 1 258 ? 9.04900   19.62000  9.11000  0.700 51.57535  ? 588 VAL A N   1 
ATOM   3558 N N   B VAL A 1 258 ? 8.84800   19.60900  9.02300  0.300 52.07529  ? 588 VAL A N   1 
ATOM   3559 C CA  A VAL A 1 258 ? 9.32100   20.42000  10.30100 0.700 50.36080  ? 588 VAL A CA  1 
ATOM   3560 C CA  B VAL A 1 258 ? 9.10000   20.41900  10.21200 0.300 50.91337  ? 588 VAL A CA  1 
ATOM   3561 C C   A VAL A 1 258 ? 10.61400  21.20500  10.12300 0.700 48.26361  ? 588 VAL A C   1 
ATOM   3562 C C   B VAL A 1 258 ? 10.36600  21.24700  10.03100 0.300 49.26894  ? 588 VAL A C   1 
ATOM   3563 O O   A VAL A 1 258 ? 10.67900  22.40500  10.41900 0.700 53.80006  ? 588 VAL A O   1 
ATOM   3564 O O   B VAL A 1 258 ? 10.38900  22.45100  10.31300 0.300 53.26931  ? 588 VAL A O   1 
ATOM   3565 C CB  A VAL A 1 258 ? 9.37000   19.52400  11.55000 0.700 52.90342  ? 588 VAL A CB  1 
ATOM   3566 C CB  B VAL A 1 258 ? 9.17700   19.52600  11.46400 0.300 52.67065  ? 588 VAL A CB  1 
ATOM   3567 C CG1 A VAL A 1 258 ? 9.90100   20.30700  12.74200 0.700 49.94392  ? 588 VAL A CG1 1 
ATOM   3568 C CG1 B VAL A 1 258 ? 9.68900   20.32200  12.65300 0.300 49.80756  ? 588 VAL A CG1 1 
ATOM   3569 C CG2 A VAL A 1 258 ? 7.99100   18.95900  11.83800 0.700 45.42751  ? 588 VAL A CG2 1 
ATOM   3570 C CG2 B VAL A 1 258 ? 7.81400   18.92200  11.76800 0.300 46.01411  ? 588 VAL A CG2 1 
ATOM   3571 N N   A TYR A 1 259 ? 11.67100  20.53200  9.66300  0.700 55.85783  ? 589 TYR A N   1 
ATOM   3572 N N   B TYR A 1 259 ? 11.43700  20.60800  9.55800  0.300 55.67839  ? 589 TYR A N   1 
ATOM   3573 C CA  A TYR A 1 259 ? 12.92900  21.22000  9.39100  0.700 52.19178  ? 589 TYR A CA  1 
ATOM   3574 C CA  B TYR A 1 259 ? 12.68700  21.31600  9.29900  0.300 52.84304  ? 589 TYR A CA  1 
ATOM   3575 C C   A TYR A 1 259 ? 12.74100  22.25200  8.28600  0.700 45.54060  ? 589 TYR A C   1 
ATOM   3576 C C   B TYR A 1 259 ? 12.49800  22.37800  8.22300  0.300 47.68329  ? 589 TYR A C   1 
ATOM   3577 O O   A TYR A 1 259 ? 13.22100  23.38700  8.39200  0.700 51.67349  ? 589 TYR A O   1 
ATOM   3578 O O   B TYR A 1 259 ? 12.98800  23.50600  8.35800  0.300 52.48205  ? 589 TYR A O   1 
ATOM   3579 C CB  A TYR A 1 259 ? 14.02700  20.22100  9.02500  0.700 66.45851  ? 589 TYR A CB  1 
ATOM   3580 C CB  B TYR A 1 259 ? 13.77700  20.32300  8.89600  0.300 64.58793  ? 589 TYR A CB  1 
ATOM   3581 C CG  A TYR A 1 259 ? 14.40600  19.26600  10.13500 0.700 66.95133  ? 589 TYR A CG  1 
ATOM   3582 C CG  B TYR A 1 259 ? 14.12400  19.34000  9.99000  0.300 66.01807  ? 589 TYR A CG  1 
ATOM   3583 C CD1 A TYR A 1 259 ? 14.57700  19.72100  11.43600 0.700 64.76784  ? 589 TYR A CD1 1 
ATOM   3584 C CD1 B TYR A 1 259 ? 14.27800  19.75800  11.30300 0.300 64.13088  ? 589 TYR A CD1 1 
ATOM   3585 C CD2 A TYR A 1 259 ? 14.62500  17.91700  9.87700  0.700 64.56675  ? 589 TYR A CD2 1 
ATOM   3586 C CD2 B TYR A 1 259 ? 14.30200  17.99300  9.70500  0.300 64.53890  ? 589 TYR A CD2 1 
ATOM   3587 C CE1 A TYR A 1 259 ? 14.94600  18.86100  12.45000 0.700 73.50895  ? 589 TYR A CE1 1 
ATOM   3588 C CE1 B TYR A 1 259 ? 14.60000  18.86100  12.30200 0.300 70.36243  ? 589 TYR A CE1 1 
ATOM   3589 C CE2 A TYR A 1 259 ? 14.98700  17.04600  10.89200 0.700 64.25805  ? 589 TYR A CE2 1 
ATOM   3590 C CE2 B TYR A 1 259 ? 14.61900  17.08700  10.69800 0.300 64.28454  ? 589 TYR A CE2 1 
ATOM   3591 C CZ  A TYR A 1 259 ? 15.14600  17.52800  12.17800 0.700 73.00011  ? 589 TYR A CZ  1 
ATOM   3592 C CZ  B TYR A 1 259 ? 14.76500  17.52700  11.99600 0.300 70.88067  ? 589 TYR A CZ  1 
ATOM   3593 O OH  A TYR A 1 259 ? 15.49600  16.68100  13.20600 0.700 78.51183  ? 589 TYR A OH  1 
ATOM   3594 O OH  B TYR A 1 259 ? 15.07100  16.63000  12.99400 0.300 76.68917  ? 589 TYR A OH  1 
ATOM   3595 N N   A GLY A 1 260 ? 12.05600  21.86100  7.20600  0.700 54.20618  ? 590 GLY A N   1 
ATOM   3596 N N   B GLY A 1 260 ? 11.81700  22.02400  7.12900  0.300 54.61901  ? 590 GLY A N   1 
ATOM   3597 C CA  A GLY A 1 260 ? 11.72100  22.80900  6.15200  0.700 54.07081  ? 590 GLY A CA  1 
ATOM   3598 C CA  B GLY A 1 260 ? 11.49300  23.01500  6.11200  0.300 54.61716  ? 590 GLY A CA  1 
ATOM   3599 C C   A GLY A 1 260 ? 11.05000  24.05600  6.69100  0.700 51.97915  ? 590 GLY A C   1 
ATOM   3600 C C   B GLY A 1 260 ? 10.82500  24.24400  6.69800  0.300 53.46328  ? 590 GLY A C   1 
ATOM   3601 O O   A GLY A 1 260 ? 11.36200  25.17500  6.28100  0.700 60.79724  ? 590 GLY A O   1 
ATOM   3602 O O   B GLY A 1 260 ? 11.17900  25.37700  6.36500  0.300 59.34522  ? 590 GLY A O   1 
ATOM   3603 N N   A SER A 1 261 ? 10.08000  23.87800  7.58500  0.700 58.20962  ? 591 SER A N   1 
ATOM   3604 N N   B SER A 1 261 ? 9.84200   24.03500  7.57700  0.300 57.03971  ? 591 SER A N   1 
ATOM   3605 C CA  A SER A 1 261 ? 9.37800   25.03200  8.13300  0.700 52.10200  ? 591 SER A CA  1 
ATOM   3606 C CA  B SER A 1 261 ? 9.13600   25.16400  8.17400  0.300 52.07690  ? 591 SER A CA  1 
ATOM   3607 C C   A SER A 1 261 ? 10.31600  25.88100  8.98700  0.700 43.00026  ? 591 SER A C   1 
ATOM   3608 C C   B SER A 1 261 ? 10.07500  25.95900  9.07200  0.300 44.69137  ? 591 SER A C   1 
ATOM   3609 O O   A SER A 1 261 ? 10.28600  27.11600  8.91100  0.700 51.53838  ? 591 SER A O   1 
ATOM   3610 O O   B SER A 1 261 ? 10.03300  27.19600  9.08900  0.300 51.50367  ? 591 SER A O   1 
ATOM   3611 C CB  A SER A 1 261 ? 8.16900   24.57300  8.94800  0.700 53.60412  ? 591 SER A CB  1 
ATOM   3612 C CB  B SER A 1 261 ? 7.91900   24.67600  8.95900  0.300 52.69707  ? 591 SER A CB  1 
ATOM   3613 O OG  A SER A 1 261 ? 7.54100   25.66800  9.59700  0.700 41.69044  ? 591 SER A OG  1 
ATOM   3614 O OG  B SER A 1 261 ? 8.25000   24.43700  10.31600 0.300 42.40811  ? 591 SER A OG  1 
ATOM   3615 N N   A THR A 1 262 ? 11.17200  25.23200  9.78400  0.700 43.83786  ? 592 THR A N   1 
ATOM   3616 N N   B THR A 1 262 ? 10.91600  25.25800  9.83700  0.300 45.20873  ? 592 THR A N   1 
ATOM   3617 C CA  A THR A 1 262 ? 12.16800  25.94900  10.57900 0.700 47.35086  ? 592 THR A CA  1 
ATOM   3618 C CA  B THR A 1 262 ? 11.93000  25.91700  10.65300 0.300 48.09358  ? 592 THR A CA  1 
ATOM   3619 C C   A THR A 1 262 ? 13.07700  26.82000  9.71300  0.700 48.06644  ? 592 THR A C   1 
ATOM   3620 C C   B THR A 1 262 ? 12.83300  26.78700  9.78700  0.300 48.79509  ? 592 THR A C   1 
ATOM   3621 O O   A THR A 1 262 ? 13.27100  28.00600  10.00800 0.700 52.83262  ? 592 THR A O   1 
ATOM   3622 O O   B THR A 1 262 ? 13.06500  27.96000  10.09600 0.300 52.30897  ? 592 THR A O   1 
ATOM   3623 C CB  A THR A 1 262 ? 13.00000  24.95400  11.39400 0.700 43.17641  ? 592 THR A CB  1 
ATOM   3624 C CB  B THR A 1 262 ? 12.75200  24.87700  11.41500 0.300 43.99393  ? 592 THR A CB  1 
ATOM   3625 O OG1 A THR A 1 262 ? 12.14500  24.21800  12.27900 0.700 35.89647  ? 592 THR A OG1 1 
ATOM   3626 O OG1 B THR A 1 262 ? 11.89100  24.12000  12.27500 0.300 37.34318  ? 592 THR A OG1 1 
ATOM   3627 C CG2 A THR A 1 262 ? 14.05100  25.68600  12.21400 0.700 42.58613  ? 592 THR A CG2 1 
ATOM   3628 C CG2 B THR A 1 262 ? 13.83000  25.55300  12.25000 0.300 44.16506  ? 592 THR A CG2 1 
ATOM   3629 N N   A VAL A 1 263 ? 13.65100  26.25300  8.64500  0.700 52.84957  ? 593 VAL A N   1 
ATOM   3630 N N   B VAL A 1 263 ? 13.34900  26.22100  8.69200  0.300 52.10993  ? 593 VAL A N   1 
ATOM   3631 C CA  A VAL A 1 263 ? 14.53000  27.03600  7.76900  0.700 52.03851  ? 593 VAL A CA  1 
ATOM   3632 C CA  B VAL A 1 263 ? 14.22000  26.97100  7.78900  0.300 52.95625  ? 593 VAL A CA  1 
ATOM   3633 C C   A VAL A 1 263 ? 13.79300  28.26600  7.23500  0.700 53.69335  ? 593 VAL A C   1 
ATOM   3634 C C   B VAL A 1 263 ? 13.51600  28.23300  7.30800  0.300 53.86714  ? 593 VAL A C   1 
ATOM   3635 O O   A VAL A 1 263 ? 14.29900  29.39200  7.31900  0.700 57.51451  ? 593 VAL A O   1 
ATOM   3636 O O   B VAL A 1 263 ? 14.05900  29.34100  7.39700  0.300 56.46618  ? 593 VAL A O   1 
ATOM   3637 C CB  A VAL A 1 263 ? 15.15900  26.16600  6.65600  0.700 61.95657  ? 593 VAL A CB  1 
ATOM   3638 C CB  B VAL A 1 263 ? 14.66000  26.09000  6.60600  0.300 60.17193  ? 593 VAL A CB  1 
ATOM   3639 C CG1 A VAL A 1 263 ? 15.80700  24.91800  7.25800  0.700 57.35242  ? 593 VAL A CG1 1 
ATOM   3640 C CG1 B VAL A 1 263 ? 15.25400  26.94700  5.49500  0.300 54.44374  ? 593 VAL A CG1 1 
ATOM   3641 C CG2 A VAL A 1 263 ? 14.19300  25.79000  5.54500  0.700 55.66275  ? 593 VAL A CG2 1 
ATOM   3642 C CG2 B VAL A 1 263 ? 15.65600  25.04100  7.06500  0.300 58.00790  ? 593 VAL A CG2 1 
ATOM   3643 N N   A GLY A 1 264 ? 12.60200  28.07300  6.66100  0.700 54.13344  ? 594 GLY A N   1 
ATOM   3644 N N   B GLY A 1 264 ? 12.30100  28.08000  6.77500  0.300 54.34912  ? 594 GLY A N   1 
ATOM   3645 C CA  A GLY A 1 264 ? 11.85600  29.21200  6.14800  0.700 43.60151  ? 594 GLY A CA  1 
ATOM   3646 C CA  B GLY A 1 264 ? 11.56100  29.24000  6.30600  0.300 46.59266  ? 594 GLY A CA  1 
ATOM   3647 C C   A GLY A 1 264 ? 11.61300  30.25700  7.22100  0.700 53.29553  ? 594 GLY A C   1 
ATOM   3648 C C   B GLY A 1 264 ? 11.36300  30.27600  7.39600  0.300 54.33693  ? 594 GLY A C   1 
ATOM   3649 O O   A GLY A 1 264 ? 11.77100  31.45600  6.97900  0.700 58.59666  ? 594 GLY A O   1 
ATOM   3650 O O   B GLY A 1 264 ? 11.50000  31.47800  7.15400  0.300 57.43468  ? 594 GLY A O   1 
ATOM   3651 N N   A HIS A 1 265 ? 11.26100  29.81600  8.43300  0.700 57.10347  ? 595 HIS A N   1 
ATOM   3652 N N   B HIS A 1 265 ? 11.03500  29.82800  8.61200  0.300 55.85388  ? 595 HIS A N   1 
ATOM   3653 C CA  A HIS A 1 265 ? 10.83900  30.76200  9.45900  0.700 52.96557  ? 595 HIS A CA  1 
ATOM   3654 C CA  B HIS A 1 265 ? 10.64500  30.77400  9.65200  0.300 52.15766  ? 595 HIS A CA  1 
ATOM   3655 C C   A HIS A 1 265 ? 12.02800  31.56400  9.96200  0.700 54.68995  ? 595 HIS A C   1 
ATOM   3656 C C   B HIS A 1 265 ? 11.84600  31.56300  10.15500 0.300 54.15179  ? 595 HIS A C   1 
ATOM   3657 O O   A HIS A 1 265 ? 11.88500  32.74600  10.29300 0.700 56.65528  ? 595 HIS A O   1 
ATOM   3658 O O   B HIS A 1 265 ? 11.71000  32.74700  10.48100 0.300 56.50081  ? 595 HIS A O   1 
ATOM   3659 C CB  A HIS A 1 265 ? 10.15000  30.04400  10.61800 0.700 45.60239  ? 595 HIS A CB  1 
ATOM   3660 C CB  B HIS A 1 265 ? 9.94800   30.04700  10.80100 0.300 46.28190  ? 595 HIS A CB  1 
ATOM   3661 C CG  A HIS A 1 265 ? 8.68400   29.83000  10.40900 0.700 40.44024  ? 595 HIS A CG  1 
ATOM   3662 C CG  B HIS A 1 265 ? 8.47700   29.86700  10.59100 0.300 41.72232  ? 595 HIS A CG  1 
ATOM   3663 N ND1 A HIS A 1 265 ? 8.15700   28.62700  9.99000  0.700 44.80643  ? 595 HIS A ND1 1 
ATOM   3664 N ND1 B HIS A 1 265 ? 7.92500   28.68400  10.14900 0.300 45.54135  ? 595 HIS A ND1 1 
ATOM   3665 C CD2 A HIS A 1 265 ? 7.63200   30.66900  10.56400 0.700 41.80521  ? 595 HIS A CD2 1 
ATOM   3666 C CD2 B HIS A 1 265 ? 7.44300   30.72600  10.75500 0.300 43.02822  ? 595 HIS A CD2 1 
ATOM   3667 C CE1 A HIS A 1 265 ? 6.84300   28.73500  9.89500  0.700 49.07499  ? 595 HIS A CE1 1 
ATOM   3668 C CE1 B HIS A 1 265 ? 6.61400   28.82100  10.05300 0.300 49.16381  ? 595 HIS A CE1 1 
ATOM   3669 N NE2 A HIS A 1 265 ? 6.50000   29.96400  10.23800 0.700 37.71364  ? 595 HIS A NE2 1 
ATOM   3670 N NE2 B HIS A 1 265 ? 6.29600   30.05000  10.41600 0.300 38.74130  ? 595 HIS A NE2 1 
ATOM   3671 N N   A THR A 1 266 ? 13.20900  30.94100  10.01300 0.700 46.66869  ? 596 THR A N   1 
ATOM   3672 N N   B THR A 1 266 ? 13.02800  30.93900  10.20900 0.300 47.85151  ? 596 THR A N   1 
ATOM   3673 C CA  A THR A 1 266 ? 14.39700  31.65000  10.47200 0.700 47.74207  ? 596 THR A CA  1 
ATOM   3674 C CA  B THR A 1 266 ? 14.21500  31.65600  10.66500 0.300 49.90940  ? 596 THR A CA  1 
ATOM   3675 C C   A THR A 1 266 ? 14.81600  32.70400  9.45700  0.700 52.53072  ? 596 THR A C   1 
ATOM   3676 C C   B THR A 1 266 ? 14.63800  32.69600  9.63800  0.300 53.07433  ? 596 THR A C   1 
ATOM   3677 O O   A THR A 1 266 ? 15.34200  33.75700  9.83700  0.700 58.36610  ? 596 THR A O   1 
ATOM   3678 O O   B THR A 1 266 ? 15.17900  33.74600  10.00500 0.300 57.84218  ? 596 THR A O   1 
ATOM   3679 C CB  A THR A 1 266 ? 15.53700  30.66600  10.72800 0.700 52.96209  ? 596 THR A CB  1 
ATOM   3680 C CB  B THR A 1 266 ? 15.36400  30.68900  10.96600 0.300 53.93427  ? 596 THR A CB  1 
ATOM   3681 O OG1 A THR A 1 266 ? 15.01400  29.47700  11.33400 0.700 55.42444  ? 596 THR A OG1 1 
ATOM   3682 O OG1 B THR A 1 266 ? 15.86300  30.12900  9.74500  0.300 61.11149  ? 596 THR A OG1 1 
ATOM   3683 C CG2 A THR A 1 266 ? 16.57200  31.28100  11.65600 0.700 60.60107  ? 596 THR A CG2 1 
ATOM   3684 C CG2 B THR A 1 266 ? 14.92000  29.58600  11.91900 0.300 52.70578  ? 596 THR A CG2 1 
ATOM   3685 N N   A ILE A 1 267 ? 14.59200  32.43800  8.16900  0.700 53.69204  ? 597 ILE A N   1 
ATOM   3686 N N   B ILE A 1 267 ? 14.41200  32.41300  8.35300  0.300 53.99458  ? 597 ILE A N   1 
ATOM   3687 C CA  A ILE A 1 267 ? 14.92100  33.41600  7.13300  0.700 51.39999  ? 597 ILE A CA  1 
ATOM   3688 C CA  B ILE A 1 267 ? 14.74100  33.36800  7.29800  0.300 52.19249  ? 597 ILE A CA  1 
ATOM   3689 C C   A ILE A 1 267 ? 14.10300  34.68200  7.34800  0.700 52.53096  ? 597 ILE A C   1 
ATOM   3690 C C   B ILE A 1 267 ? 13.93200  34.64200  7.50000  0.300 52.60757  ? 597 ILE A C   1 
ATOM   3691 O O   A ILE A 1 267 ? 14.64700  35.78100  7.51100  0.700 63.16939  ? 597 ILE A O   1 
ATOM   3692 O O   B ILE A 1 267 ? 14.48400  35.74100  7.63100  0.300 60.65387  ? 597 ILE A O   1 
ATOM   3693 C CB  A ILE A 1 267 ? 14.68600  32.82700  5.73300  0.700 52.28208  ? 597 ILE A CB  1 
ATOM   3694 C CB  B ILE A 1 267 ? 14.48700  32.75300  5.91000  0.300 52.42362  ? 597 ILE A CB  1 
ATOM   3695 C CG1 A ILE A 1 267 ? 15.73500  31.75700  5.42200  0.700 57.32486  ? 597 ILE A CG1 1 
ATOM   3696 C CG1 B ILE A 1 267 ? 15.52300  31.66900  5.60700  0.300 57.81184  ? 597 ILE A CG1 1 
ATOM   3697 C CG2 A ILE A 1 267 ? 14.71500  33.93200  4.68700  0.700 52.58299  ? 597 ILE A CG2 1 
ATOM   3698 C CG2 B ILE A 1 267 ? 14.50600  33.83000  4.83600  0.300 52.28819  ? 597 ILE A CG2 1 
ATOM   3699 C CD1 A ILE A 1 267 ? 15.52100  31.06000  4.09700  0.700 53.24696  ? 597 ILE A CD1 1 
ATOM   3700 C CD1 B ILE A 1 267 ? 15.28900  30.94900  4.29500  0.300 54.91804  ? 597 ILE A CD1 1 
ATOM   3701 N N   A ILE A 1 268 ? 12.77400  34.53900  7.35300  0.700 43.71914  ? 598 ILE A N   1 
ATOM   3702 N N   B ILE A 1 268 ? 12.60400  34.51000  7.52200  0.300 45.23151  ? 598 ILE A N   1 
ATOM   3703 C CA  A ILE A 1 268 ? 11.89300  35.69300  7.47100  0.700 53.53878  ? 598 ILE A CA  1 
ATOM   3704 C CA  B ILE A 1 268 ? 11.74600  35.68000  7.63500  0.300 53.39597  ? 598 ILE A CA  1 
ATOM   3705 C C   A ILE A 1 268 ? 11.97600  36.29400  8.87100  0.700 53.93055  ? 598 ILE A C   1 
ATOM   3706 C C   B ILE A 1 268 ? 11.86700  36.28600  9.02700  0.300 53.95903  ? 598 ILE A C   1 
ATOM   3707 O O   A ILE A 1 268 ? 11.60300  37.45700  9.06500  0.700 43.04793  ? 598 ILE A O   1 
ATOM   3708 O O   B ILE A 1 268 ? 11.53000  37.45800  9.22300  0.300 43.40152  ? 598 ILE A O   1 
ATOM   3709 C CB  A ILE A 1 268 ? 10.44800  35.32900  7.08300  0.700 46.91710  ? 598 ILE A CB  1 
ATOM   3710 C CB  B ILE A 1 268 ? 10.28600  35.33000  7.29000  0.300 48.70774  ? 598 ILE A CB  1 
ATOM   3711 C CG1 A ILE A 1 268 ? 9.84000   34.33800  8.07200  0.700 56.43168  ? 598 ILE A CG1 1 
ATOM   3712 C CG1 B ILE A 1 268 ? 9.69400   34.37000  8.32200  0.300 57.34357  ? 598 ILE A CG1 1 
ATOM   3713 C CG2 A ILE A 1 268 ? 10.40600  34.75800  5.67300  0.700 54.49236  ? 598 ILE A CG2 1 
ATOM   3714 C CG2 B ILE A 1 268 ? 10.19600  34.73300  5.89300  0.300 54.88209  ? 598 ILE A CG2 1 
ATOM   3715 C CD1 A ILE A 1 268 ? 8.41200   33.97300  7.73000  0.700 55.56489  ? 598 ILE A CD1 1 
ATOM   3716 C CD1 B ILE A 1 268 ? 8.25500   34.01000  8.04000  0.300 56.02740  ? 598 ILE A CD1 1 
ATOM   3717 N N   A ASP A 1 269 ? 12.45700  35.52700  9.85700  0.700 59.55021  ? 599 ASP A N   1 
ATOM   3718 N N   B ASP A 1 269 ? 12.34500  35.50500  10.00100 0.300 59.32353  ? 599 ASP A N   1 
ATOM   3719 C CA  A ASP A 1 269 ? 12.77100  36.11000  11.16100 0.700 59.42824  ? 599 ASP A CA  1 
ATOM   3720 C CA  B ASP A 1 269 ? 12.70700  36.06600  11.29900 0.300 58.90032  ? 599 ASP A CA  1 
ATOM   3721 C C   A ASP A 1 269 ? 13.87600  37.15300  11.03500 0.700 58.77933  ? 599 ASP A C   1 
ATOM   3722 C C   B ASP A 1 269 ? 13.84100  37.06800  11.13600 0.300 58.31147  ? 599 ASP A C   1 
ATOM   3723 O O   A ASP A 1 269 ? 13.77300  38.25300  11.59300 0.700 57.79211  ? 599 ASP A O   1 
ATOM   3724 O O   B ASP A 1 269 ? 13.79900  38.17000  11.69500 0.300 57.41435  ? 599 ASP A O   1 
ATOM   3725 C CB  A ASP A 1 269 ? 13.17700  35.01300  12.14600 0.700 49.99240  ? 599 ASP A CB  1 
ATOM   3726 C CB  B ASP A 1 269 ? 13.11000  34.95900  12.27600 0.300 50.41969  ? 599 ASP A CB  1 
ATOM   3727 C CG  A ASP A 1 269 ? 11.98400  34.33200  12.79700 0.700 57.95264  ? 599 ASP A CG  1 
ATOM   3728 C CG  B ASP A 1 269 ? 11.91900  34.30500  12.94400 0.300 57.72258  ? 599 ASP A CG  1 
ATOM   3729 O OD1 A ASP A 1 269 ? 10.84200  34.81500  12.62800 0.700 66.66502  ? 599 ASP A OD1 1 
ATOM   3730 O OD1 B ASP A 1 269 ? 10.79000  34.81200  12.78200 0.300 65.61964  ? 599 ASP A OD1 1 
ATOM   3731 O OD2 A ASP A 1 269 ? 12.19500  33.30800  13.48100 0.700 52.06645  ? 599 ASP A OD2 1 
ATOM   3732 O OD2 B ASP A 1 269 ? 12.11400  33.28900  13.64300 0.300 52.19913  ? 599 ASP A OD2 1 
ATOM   3733 N N   A LEU A 1 270 ? 14.95600  36.80500  10.32800 0.700 58.01491  ? 600 LEU A N   1 
ATOM   3734 N N   B LEU A 1 270 ? 14.88000  36.68500  10.39000 0.300 58.03469  ? 600 LEU A N   1 
ATOM   3735 C CA  A LEU A 1 270 ? 16.07100  37.72000  10.10900 0.700 56.38040  ? 600 LEU A CA  1 
ATOM   3736 C CA  B LEU A 1 270 ? 16.00400  37.58600  10.16500 0.300 56.55178  ? 600 LEU A CA  1 
ATOM   3737 C C   A LEU A 1 270 ? 15.56400  38.99800  9.45100  0.700 53.85480  ? 600 LEU A C   1 
ATOM   3738 C C   B LEU A 1 270 ? 15.53000  38.90400  9.56200  0.300 53.33114  ? 600 LEU A C   1 
ATOM   3739 O O   A LEU A 1 270 ? 15.97700  40.10700  9.81900  0.700 57.19359  ? 600 LEU A O   1 
ATOM   3740 O O   B LEU A 1 270 ? 16.00500  39.97700  9.94900  0.300 57.06094  ? 600 LEU A O   1 
ATOM   3741 C CB  A LEU A 1 270 ? 17.16400  37.03000  9.30300  0.700 53.47187  ? 600 LEU A CB  1 
ATOM   3742 C CB  B LEU A 1 270 ? 17.03500  36.91400  9.25800  0.300 54.19001  ? 600 LEU A CB  1 
ATOM   3743 C CG  A LEU A 1 270 ? 17.91500  36.03600  10.22400 0.700 59.34278  ? 600 LEU A CG  1 
ATOM   3744 C CG  B LEU A 1 270 ? 17.91800  35.83800  9.89600  0.300 60.33334  ? 600 LEU A CG  1 
ATOM   3745 C CD1 A LEU A 1 270 ? 18.73700  35.04100  9.40400  0.700 61.61389  ? 600 LEU A CD1 1 
ATOM   3746 C CD1 B LEU A 1 270 ? 18.54900  34.95300  8.83000  0.300 60.94259  ? 600 LEU A CD1 1 
ATOM   3747 C CD2 A LEU A 1 270 ? 18.77600  36.70400  11.34100 0.700 73.32275  ? 600 LEU A CD2 1 
ATOM   3748 C CD2 B LEU A 1 270 ? 18.99100  36.46800  10.76600 0.300 65.50880  ? 600 LEU A CD2 1 
ATOM   3749 N N   A MET A 1 271 ? 14.61900  38.85800  8.51200  0.700 44.32149  ? 601 MET A N   1 
ATOM   3750 N N   B MET A 1 271 ? 14.59800  38.84600  8.61000  0.300 44.65451  ? 601 MET A N   1 
ATOM   3751 C CA  A MET A 1 271 ? 14.06400  40.01800  7.81900  0.700 44.61090  ? 601 MET A CA  1 
ATOM   3752 C CA  B MET A 1 271 ? 14.09900  40.07800  8.01000  0.300 46.07090  ? 601 MET A CA  1 
ATOM   3753 C C   A MET A 1 271 ? 13.19800  40.83700  8.76200  0.700 54.27736  ? 601 MET A C   1 
ATOM   3754 C C   B MET A 1 271 ? 13.21300  40.83700  8.99300  0.300 53.85858  ? 601 MET A C   1 
ATOM   3755 O O   A MET A 1 271 ? 13.37100  42.05700  8.87800  0.700 50.36059  ? 601 MET A O   1 
ATOM   3756 O O   B MET A 1 271 ? 13.40400  42.03800  9.21700  0.300 51.23835  ? 601 MET A O   1 
ATOM   3757 C CB  A MET A 1 271 ? 13.17700  39.56300  6.65400  0.700 54.40660  ? 601 MET A CB  1 
ATOM   3758 C CB  B MET A 1 271 ? 13.33700  39.78000  6.71700  0.300 54.67330  ? 601 MET A CB  1 
ATOM   3759 C CG  A MET A 1 271 ? 13.80800  38.80500  5.50600  0.700 57.73923  ? 601 MET A CG  1 
ATOM   3760 C CG  B MET A 1 271 ? 14.18100  39.24200  5.57500  0.300 56.34323  ? 601 MET A CG  1 
ATOM   3761 S SD  A MET A 1 271 ? 12.51100  38.43300  4.30800  0.700 46.77878  ? 601 MET A SD  1 
ATOM   3762 S SD  B MET A 1 271 ? 13.19400  38.97400  4.08500  0.300 56.69202  ? 601 MET A SD  1 
ATOM   3763 C CE  A MET A 1 271 ? 12.74300  39.82300  3.19600  0.700 55.00686  ? 601 MET A CE  1 
ATOM   3764 C CE  B MET A 1 271 ? 13.69600  37.31700  3.62000  0.300 58.18840  ? 601 MET A CE  1 
ATOM   3765 N N   A SER A 1 272 ? 12.26300  40.18400  9.44300  0.700 57.81587  ? 602 SER A N   1 
ATOM   3766 N N   B SER A 1 272 ? 12.23200  40.15500  9.57900  0.300 57.25057  ? 602 SER A N   1 
ATOM   3767 C CA  A SER A 1 272 ? 11.21700  40.87600  10.18000 0.700 52.06518  ? 602 SER A CA  1 
ATOM   3768 C CA  B SER A 1 272 ? 11.17700  40.82000  10.33500 0.300 51.79077  ? 602 SER A CA  1 
ATOM   3769 C C   A SER A 1 272 ? 11.77700  41.52400  11.43600 0.700 45.84407  ? 602 SER A C   1 
ATOM   3770 C C   B SER A 1 272 ? 11.69000  41.35000  11.67100 0.300 47.03441  ? 602 SER A C   1 
ATOM   3771 O O   A SER A 1 272 ? 11.26600  42.54400  11.89300 0.700 46.87183  ? 602 SER A O   1 
ATOM   3772 O O   B SER A 1 272 ? 11.32100  42.44400  12.09600 0.300 47.19213  ? 602 SER A O   1 
ATOM   3773 C CB  A SER A 1 272 ? 10.08200  39.91000  10.54300 0.700 53.59476  ? 602 SER A CB  1 
ATOM   3774 C CB  B SER A 1 272 ? 10.00100  39.86900  10.57300 0.300 53.64032  ? 602 SER A CB  1 
ATOM   3775 O OG  A SER A 1 272 ? 10.55000  38.85900  11.37600 0.700 62.91082  ? 602 SER A OG  1 
ATOM   3776 O OG  B SER A 1 272 ? 10.39900  38.74100  11.33500 0.300 61.87149  ? 602 SER A OG  1 
ATOM   3777 N N   A LYS A 1 273 ? 12.83700  40.93300  11.97900 0.700 37.60399  ? 603 LYS A N   1 
ATOM   3778 N N   B LYS A 1 273 ? 12.53500  40.56600  12.33200 0.300 46.33280  ? 603 LYS A N   1 
ATOM   3779 C CA  A LYS A 1 273 ? 13.38000  41.35800  13.29900 0.700 43.27675  ? 603 LYS A CA  1 
ATOM   3780 C CA  B LYS A 1 273 ? 13.07700  40.94300  13.66700 0.300 49.98082  ? 603 LYS A CA  1 
ATOM   3781 C C   A LYS A 1 273 ? 14.77100  41.97200  13.11800 0.700 42.99626  ? 603 LYS A C   1 
ATOM   3782 C C   B LYS A 1 273 ? 14.42000  41.66300  13.49700 0.300 47.92776  ? 603 LYS A C   1 
ATOM   3783 O O   A LYS A 1 273 ? 14.87900  43.21300  13.19900 0.700 54.24234  ? 603 LYS A O   1 
ATOM   3784 O O   B LYS A 1 273 ? 14.46500  42.89000  13.73100 0.300 46.50496  ? 603 LYS A O   1 
ATOM   3785 C CB  A LYS A 1 273 ? 13.45800  40.17100  14.25800 0.700 56.88345  ? 603 LYS A CB  1 
ATOM   3786 C CB  B LYS A 1 273 ? 13.25100  39.70900  14.55500 0.300 55.87288  ? 603 LYS A CB  1 
ATOM   3787 C CG  A LYS A 1 273 ? 12.13400  39.46100  14.47600 0.700 59.97649  ? 603 LYS A CG  1 
ATOM   3788 C CG  B LYS A 1 273 ? 11.94600  39.05900  14.99200 0.300 55.87511  ? 603 LYS A CG  1 
ATOM   3789 C CD  A LYS A 1 273 ? 12.30300  38.01400  14.89800 0.700 56.38292  ? 603 LYS A CD  1 
ATOM   3790 C CD  B LYS A 1 273 ? 11.81600  37.60100  14.58300 0.300 56.11350  ? 603 LYS A CD  1 
ATOM   3791 C CE  A LYS A 1 273 ? 11.34400  37.62400  15.99900 0.700 54.02416  ? 603 LYS A CE  1 
ATOM   3792 C CE  B LYS A 1 273 ? 10.41300  37.07800  14.82400 0.300 57.47064  ? 603 LYS A CE  1 
ATOM   3793 N NZ  A LYS A 1 273 ? 10.08100  37.07500  15.45700 0.700 59.38532  ? 603 LYS A NZ  1 
ATOM   3794 N NZ  B LYS A 1 273 ? 9.41800   38.07600  14.44800 0.300 53.70400  ? 603 LYS A NZ  1 
ATOM   3795 N N   A ASN A 1 274 ? 15.78000  41.13200  12.90100 0.700 42.86367  ? 604 ASN A N   1 
ATOM   3796 N N   B ASN A 1 274 ? 15.45900  40.93000  13.11500 0.300 48.41453  ? 604 ASN A N   1 
ATOM   3797 C CA  A ASN A 1 274 ? 17.17300  41.55900  12.82300 0.700 44.02719  ? 604 ASN A CA  1 
ATOM   3798 C CA  B ASN A 1 274 ? 16.81500  41.46100  13.08600 0.300 47.73988  ? 604 ASN A CA  1 
ATOM   3799 C C   A ASN A 1 274 ? 17.36900  42.70500  11.83800 0.700 47.51200  ? 604 ASN A C   1 
ATOM   3800 C C   B ASN A 1 274 ? 16.96600  42.64700  12.13700 0.300 49.44335  ? 604 ASN A C   1 
ATOM   3801 O O   A ASN A 1 274 ? 17.86000  43.76800  12.22400 0.700 51.02301  ? 604 ASN A O   1 
ATOM   3802 O O   B ASN A 1 274 ? 17.35500  43.73100  12.56800 0.300 52.12868  ? 604 ASN A O   1 
ATOM   3803 C CB  A ASN A 1 274 ? 18.05100  40.36800  12.47000 0.700 54.72496  ? 604 ASN A CB  1 
ATOM   3804 C CB  B ASN A 1 274 ? 17.80100  40.35100  12.71900 0.300 55.71053  ? 604 ASN A CB  1 
ATOM   3805 C CG  A ASN A 1 274 ? 17.94100  39.25600  13.49500 0.700 64.86528  ? 604 ASN A CG  1 
ATOM   3806 C CG  B ASN A 1 274 ? 17.76200  39.19700  13.70500 0.300 63.78766  ? 604 ASN A CG  1 
ATOM   3807 O OD1 A ASN A 1 274 ? 17.03200  38.42700  13.43200 0.700 65.80189  ? 604 ASN A OD1 1 
ATOM   3808 O OD1 B ASN A 1 274 ? 17.89700  38.03500  13.32600 0.300 65.50455  ? 604 ASN A OD1 1 
ATOM   3809 N ND2 A ASN A 1 274 ? 18.85900  39.24300  14.45800 0.700 64.28822  ? 604 ASN A ND2 1 
ATOM   3810 N ND2 B ASN A 1 274 ? 17.57100  39.51700  14.98000 0.300 56.54918  ? 604 ASN A ND2 1 
ATOM   3811 N N   A CYS A 1 275 ? 16.99800  42.49700  10.57000 0.700 52.77441  ? 605 CYS A N   1 
ATOM   3812 N N   B CYS A 1 275 ? 16.65300  42.45300  10.85200 0.300 51.50769  ? 605 CYS A N   1 
ATOM   3813 C CA  A CYS A 1 275 ? 17.30600  43.50300  9.55500  0.700 46.15442  ? 605 CYS A CA  1 
ATOM   3814 C CA  B CYS A 1 275 ? 16.94500  43.49600  9.87300  0.300 47.78721  ? 605 CYS A CA  1 
ATOM   3815 C C   A CYS A 1 275 ? 16.45500  44.74100  9.78700  0.700 48.22701  ? 605 CYS A C   1 
ATOM   3816 C C   B CYS A 1 275 ? 16.03600  44.70300  10.06700 0.300 48.97123  ? 605 CYS A C   1 
ATOM   3817 O O   A CYS A 1 275 ? 16.93000  45.87400  9.63600  0.700 63.12127  ? 605 CYS A O   1 
ATOM   3818 O O   B CYS A 1 275 ? 16.48900  45.84900  9.95800  0.300 55.65102  ? 605 CYS A O   1 
ATOM   3819 C CB  A CYS A 1 275 ? 17.07200  42.94700  8.15100  0.700 49.05581  ? 605 CYS A CB  1 
ATOM   3820 C CB  B CYS A 1 275 ? 16.81100  42.94600  8.45400  0.300 51.17957  ? 605 CYS A CB  1 
ATOM   3821 S SG  A CYS A 1 275 ? 18.11000  41.53500  7.70800  0.700 53.66557  ? 605 CYS A SG  1 
ATOM   3822 S SG  B CYS A 1 275 ? 17.96500  41.61100  8.05600  0.300 58.91271  ? 605 CYS A SG  1 
ATOM   3823 N N   A TRP A 1 276 ? 15.18600  44.53200  10.13800 0.700 45.25828  ? 606 TRP A N   1 
ATOM   3824 N N   B TRP A 1 276 ? 14.75100  44.47100  10.34600 0.300 47.54187  ? 606 TRP A N   1 
ATOM   3825 C CA  A TRP A 1 276 ? 14.25200  45.63100  10.34600 0.700 36.56718  ? 606 TRP A CA  1 
ATOM   3826 C CA  B TRP A 1 276 ? 13.81800  45.58700  10.48600 0.300 40.37059  ? 606 TRP A CA  1 
ATOM   3827 C C   A TRP A 1 276 ? 14.70400  46.44200  11.55900 0.700 39.25638  ? 606 TRP A C   1 
ATOM   3828 C C   B TRP A 1 276 ? 14.17100  46.42200  11.71100 0.300 44.36035  ? 606 TRP A C   1 
ATOM   3829 O O   A TRP A 1 276 ? 14.71400  47.67900  11.53200 0.700 49.41721  ? 606 TRP A O   1 
ATOM   3830 O O   B TRP A 1 276 ? 14.20600  47.65800  11.64900 0.300 49.97743  ? 606 TRP A O   1 
ATOM   3831 C CB  A TRP A 1 276 ? 12.83800  45.06200  10.50100 0.700 38.89636  ? 606 TRP A CB  1 
ATOM   3832 C CB  B TRP A 1 276 ? 12.38600  45.06200  10.57200 0.300 41.17958  ? 606 TRP A CB  1 
ATOM   3833 C CG  A TRP A 1 276 ? 11.72300  46.05400  10.51400 0.700 36.32734  ? 606 TRP A CG  1 
ATOM   3834 C CG  B TRP A 1 276 ? 11.33900  46.13100  10.52100 0.300 39.77639  ? 606 TRP A CG  1 
ATOM   3835 C CD1 A TRP A 1 276 ? 10.99500  46.47800  9.43600  0.700 33.33208  ? 606 TRP A CD1 1 
ATOM   3836 C CD1 B TRP A 1 276 ? 10.69500  46.59600  9.41100  0.300 35.90315  ? 606 TRP A CD1 1 
ATOM   3837 C CD2 A TRP A 1 276 ? 11.17600  46.72000  11.65400 0.700 40.03270  ? 606 TRP A CD2 1 
ATOM   3838 C CD2 B TRP A 1 276 ? 10.82000  46.87600  11.62800 0.300 42.53725  ? 606 TRP A CD2 1 
ATOM   3839 N NE1 A TRP A 1 276 ? 10.04100  47.38100  9.83600  0.700 40.81743  ? 606 TRP A NE1 1 
ATOM   3840 N NE1 B TRP A 1 276 ? 9.80300   47.58100  9.76000  0.300 42.60996  ? 606 TRP A NE1 1 
ATOM   3841 C CE2 A TRP A 1 276 ? 10.13000  47.54700  11.19400 0.700 45.51742  ? 606 TRP A CE2 1 
ATOM   3842 C CE2 B TRP A 1 276 ? 9.86200   47.77200  11.11500 0.300 45.90111  ? 606 TRP A CE2 1 
ATOM   3843 C CE3 A TRP A 1 276 ? 11.47500  46.70700  13.01800 0.700 36.60401  ? 606 TRP A CE3 1 
ATOM   3844 C CE3 B TRP A 1 276 ? 11.07100  46.87000  13.00300 0.300 40.01392  ? 606 TRP A CE3 1 
ATOM   3845 C CZ2 A TRP A 1 276 ? 9.38300   48.35000  12.05000 0.700 42.30033  ? 606 TRP A CZ2 1 
ATOM   3846 C CZ2 B TRP A 1 276 ? 9.15500   48.65400  11.93000 0.300 43.91106  ? 606 TRP A CZ2 1 
ATOM   3847 C CZ3 A TRP A 1 276 ? 10.73200  47.50400  13.86600 0.700 38.40533  ? 606 TRP A CZ3 1 
ATOM   3848 C CZ3 B TRP A 1 276 ? 10.36900  47.74600  13.80900 0.300 40.41244  ? 606 TRP A CZ3 1 
ATOM   3849 C CH2 A TRP A 1 276 ? 9.69800   48.31500  13.37900 0.700 39.12968  ? 606 TRP A CH2 1 
ATOM   3850 C CH2 B TRP A 1 276 ? 9.42200   48.62500  13.27100 0.300 43.67939  ? 606 TRP A CH2 1 
ATOM   3851 N N   A GLY A 1 277 ? 15.08200  45.73900  12.63700 0.700 51.22781  ? 607 GLY A N   1 
ATOM   3852 N N   B GLY A 1 277 ? 14.43000  45.75200  12.84000 0.300 49.77344  ? 607 GLY A N   1 
ATOM   3853 C CA  A GLY A 1 277 ? 15.61800  46.39000  13.83000 0.700 60.50582  ? 607 GLY A CA  1 
ATOM   3854 C CA  B GLY A 1 277 ? 14.86500  46.45500  14.03700 0.300 54.41452  ? 607 GLY A CA  1 
ATOM   3855 C C   A GLY A 1 277 ? 16.88500  47.17600  13.52900 0.700 56.97831  ? 607 GLY A C   1 
ATOM   3856 C C   B GLY A 1 277 ? 16.17700  47.18200  13.82100 0.300 55.59627  ? 607 GLY A C   1 
ATOM   3857 O O   A GLY A 1 277 ? 17.07300  48.28200  14.04300 0.700 55.26291  ? 607 GLY A O   1 
ATOM   3858 O O   B GLY A 1 277 ? 16.36000  48.30800  14.28900 0.300 55.41710  ? 607 GLY A O   1 
ATOM   3859 N N   A LEU A 1 278 ? 17.77400  46.61200  12.69500 0.700 62.75687  ? 608 LEU A N   1 
ATOM   3860 N N   B LEU A 1 278 ? 17.11100  46.53100  13.12300 0.300 57.80179  ? 608 LEU A N   1 
ATOM   3861 C CA  A LEU A 1 278 ? 18.96800  47.34000  12.25300 0.700 57.49786  ? 608 LEU A CA  1 
ATOM   3862 C CA  B LEU A 1 278 ? 18.38600  47.14400  12.77300 0.300 58.23880  ? 608 LEU A CA  1 
ATOM   3863 C C   A LEU A 1 278 ? 18.61000  48.65000  11.60400 0.700 54.89279  ? 608 LEU A C   1 
ATOM   3864 C C   B LEU A 1 278 ? 18.16500  48.43000  11.98700 0.300 54.73594  ? 608 LEU A C   1 
ATOM   3865 O O   A LEU A 1 278 ? 19.15900  49.70000  11.95900 0.700 60.23295  ? 608 LEU A O   1 
ATOM   3866 O O   B LEU A 1 278 ? 18.73300  49.47800  12.31300 0.300 57.35970  ? 608 LEU A O   1 
ATOM   3867 C CB  A LEU A 1 278 ? 19.81300  46.52200  11.27400 0.700 51.47292  ? 608 LEU A CB  1 
ATOM   3868 C CB  B LEU A 1 278 ? 19.23300  46.14500  11.98400 0.300 58.03421  ? 608 LEU A CB  1 
ATOM   3869 C CG  A LEU A 1 278 ? 21.32800  46.47100  11.50300 0.700 53.79873  ? 608 LEU A CG  1 
ATOM   3870 C CG  B LEU A 1 278 ? 20.58100  45.73800  12.59500 0.300 59.74519  ? 608 LEU A CG  1 
ATOM   3871 C CD1 A LEU A 1 278 ? 21.79200  46.37900  12.92400 0.700 62.07333  ? 608 LEU A CD1 1 
ATOM   3872 C CD1 B LEU A 1 278 ? 21.34200  44.81500  11.65300 0.300 48.83488  ? 608 LEU A CD1 1 
ATOM   3873 C CD2 A LEU A 1 278 ? 21.91700  45.32400  10.66900 0.700 51.43501  ? 608 LEU A CD2 1 
ATOM   3874 C CD2 B LEU A 1 278 ? 21.42200  46.94600  12.98000 0.300 57.60578  ? 608 LEU A CD2 1 
ATOM   3875 N N   A LEU A 1 279 ? 17.69500  48.60900  10.64700 0.700 52.43191  ? 609 LEU A N   1 
ATOM   3876 N N   B LEU A 1 279 ? 17.34600  48.36200  10.93400 0.300 52.58053  ? 609 LEU A N   1 
ATOM   3877 C CA  A LEU A 1 279 ? 17.28000  49.83300  9.99300  0.700 48.98502  ? 609 LEU A CA  1 
ATOM   3878 C CA  B LEU A 1 279 ? 17.04800  49.54900  10.13500 0.300 50.77471  ? 609 LEU A CA  1 
ATOM   3879 C C   A LEU A 1 279 ? 16.68900  50.78800  11.01800 0.700 47.87385  ? 609 LEU A C   1 
ATOM   3880 C C   B LEU A 1 279 ? 16.38000  50.61700  10.99300 0.300 49.42475  ? 609 LEU A C   1 
ATOM   3881 O O   A LEU A 1 279 ? 16.95300  51.99500  10.97300 0.700 54.86788  ? 609 LEU A O   1 
ATOM   3882 O O   B LEU A 1 279 ? 16.67900  51.80900  10.85600 0.300 53.12757  ? 609 LEU A O   1 
ATOM   3883 C CB  A LEU A 1 279 ? 16.27900  49.51700  8.88700  0.700 52.30704  ? 609 LEU A CB  1 
ATOM   3884 C CB  B LEU A 1 279 ? 16.16500  49.18400  8.94300  0.300 53.31626  ? 609 LEU A CB  1 
ATOM   3885 C CG  A LEU A 1 279 ? 16.85600  48.92700  7.60300  0.700 50.55599  ? 609 LEU A CG  1 
ATOM   3886 C CG  B LEU A 1 279 ? 16.83400  48.48300  7.76100  0.300 52.96808  ? 609 LEU A CG  1 
ATOM   3887 C CD1 A LEU A 1 279 ? 15.73100  48.63700  6.62100  0.700 53.85650  ? 609 LEU A CD1 1 
ATOM   3888 C CD1 B LEU A 1 279 ? 15.80300  48.16800  6.69100  0.300 53.93252  ? 609 LEU A CD1 1 
ATOM   3889 C CD2 A LEU A 1 279 ? 17.88200  49.87400  7.00000  0.700 42.15706  ? 609 LEU A CD2 1 
ATOM   3890 C CD2 B LEU A 1 279 ? 17.95300  49.34000  7.19200  0.300 45.32186  ? 609 LEU A CD2 1 
ATOM   3891 N N   A GLY A 1 280 ? 15.90100  50.26300  11.96400 0.700 45.17052  ? 610 GLY A N   1 
ATOM   3892 N N   B GLY A 1 280 ? 15.46200  50.21000  11.87300 0.300 46.96318  ? 610 GLY A N   1 
ATOM   3893 C CA  A GLY A 1 280 ? 15.24300  51.13900  12.91900 0.700 39.39379  ? 610 GLY A CA  1 
ATOM   3894 C CA  B GLY A 1 280 ? 14.73200  51.17900  12.67700 0.300 43.35295  ? 610 GLY A CA  1 
ATOM   3895 C C   A GLY A 1 280 ? 16.24200  51.88500  13.77300 0.700 50.63776  ? 610 GLY A C   1 
ATOM   3896 C C   B GLY A 1 280 ? 15.67300  51.94500  13.58500 0.300 51.24876  ? 610 GLY A C   1 
ATOM   3897 O O   A GLY A 1 280 ? 16.07200  53.07700  14.04100 0.700 58.85217  ? 610 GLY A O   1 
ATOM   3898 O O   B GLY A 1 280 ? 15.51900  53.15200  13.78600 0.300 54.14952  ? 610 GLY A O   1 
ATOM   3899 N N   A HIS A 1 281 ? 17.30200  51.20000  14.20200 0.700 54.34758  ? 611 HIS A N   1 
ATOM   3900 N N   B HIS A 1 281 ? 16.65700  51.24400  14.15300 0.300 55.28835  ? 611 HIS A N   1 
ATOM   3901 C CA  A HIS A 1 281 ? 18.36000  51.89300  14.92200 0.700 55.82688  ? 611 HIS A CA  1 
ATOM   3902 C CA  B HIS A 1 281 ? 17.68800  51.89600  14.95300 0.300 56.04147  ? 611 HIS A CA  1 
ATOM   3903 C C   A HIS A 1 281 ? 18.98000  52.94500  14.01400 0.700 57.42020  ? 611 HIS A C   1 
ATOM   3904 C C   B HIS A 1 281 ? 18.45000  52.89500  14.09100 0.300 57.69027  ? 611 HIS A C   1 
ATOM   3905 O O   A HIS A 1 281 ? 19.14000  54.10800  14.40100 0.700 61.28747  ? 611 HIS A O   1 
ATOM   3906 O O   B HIS A 1 281 ? 18.69700  54.03300  14.50600 0.300 59.55522  ? 611 HIS A O   1 
ATOM   3907 C CB  A HIS A 1 281 ? 19.40600  50.89600  15.41600 0.700 59.03347  ? 611 HIS A CB  1 
ATOM   3908 C CB  B HIS A 1 281 ? 18.62800  50.84800  15.54800 0.300 56.97486  ? 611 HIS A CB  1 
ATOM   3909 C CG  A HIS A 1 281 ? 20.48200  51.51800  16.25000 0.700 70.17857  ? 611 HIS A CG  1 
ATOM   3910 C CG  B HIS A 1 281 ? 19.66800  51.41700  16.46300 0.300 65.09427  ? 611 HIS A CG  1 
ATOM   3911 N ND1 A HIS A 1 281 ? 20.31800  51.79100  17.59100 0.700 64.13248  ? 611 HIS A ND1 1 
ATOM   3912 N ND1 B HIS A 1 281 ? 19.41200  51.72200  17.78300 0.300 60.66880  ? 611 HIS A ND1 1 
ATOM   3913 C CD2 A HIS A 1 281 ? 21.73400  51.92300  15.93200 0.700 73.59488  ? 611 HIS A CD2 1 
ATOM   3914 C CD2 B HIS A 1 281 ? 20.96700  51.73200  16.24900 0.300 70.06344  ? 611 HIS A CD2 1 
ATOM   3915 C CE1 A HIS A 1 281 ? 21.42500  52.33600  18.06500 0.700 74.28588  ? 611 HIS A CE1 1 
ATOM   3916 C CE1 B HIS A 1 281 ? 20.50800  52.20200  18.34200 0.300 64.13330  ? 611 HIS A CE1 1 
ATOM   3917 N NE2 A HIS A 1 281 ? 22.29900  52.42800  17.07900 0.700 89.75980  ? 611 HIS A NE2 1 
ATOM   3918 N NE2 B HIS A 1 281 ? 21.46600  52.21900  17.43300 0.300 74.29329  ? 611 HIS A NE2 1 
ATOM   3919 N N   A TYR A 1 282 ? 19.31200  52.54600  12.78200 0.700 54.10983  ? 612 TYR A N   1 
ATOM   3920 N N   B TYR A 1 282 ? 18.85100  52.46800  12.89000 0.300 55.23258  ? 612 TYR A N   1 
ATOM   3921 C CA  A TYR A 1 282 ? 19.86800  53.47300  11.80000 0.700 50.27672  ? 612 TYR A CA  1 
ATOM   3922 C CA  B TYR A 1 282 ? 19.54000  53.35600  11.95700 0.300 52.28052  ? 612 TYR A CA  1 
ATOM   3923 C C   A TYR A 1 282 ? 18.92800  54.65000  11.56100 0.700 50.53294  ? 612 TYR A C   1 
ATOM   3924 C C   B TYR A 1 282 ? 18.69300  54.59300  11.68100 0.300 51.40055  ? 612 TYR A C   1 
ATOM   3925 O O   A TYR A 1 282 ? 19.35700  55.80800  11.55800 0.700 51.74029  ? 612 TYR A O   1 
ATOM   3926 O O   B TYR A 1 282 ? 19.20100  55.71800  11.67100 0.300 51.36364  ? 612 TYR A O   1 
ATOM   3927 C CB  A TYR A 1 282 ? 20.15500  52.72900  10.49500 0.700 55.80035  ? 612 TYR A CB  1 
ATOM   3928 C CB  B TYR A 1 282 ? 19.85900  52.61500  10.65800 0.300 55.56051  ? 612 TYR A CB  1 
ATOM   3929 C CG  A TYR A 1 282 ? 20.77300  53.59000  9.41900  0.700 61.11547  ? 612 TYR A CG  1 
ATOM   3930 C CG  B TYR A 1 282 ? 20.60900  53.45000  9.64200  0.300 60.23007  ? 612 TYR A CG  1 
ATOM   3931 C CD1 A TYR A 1 282 ? 21.98000  54.24700  9.63200  0.700 61.63155  ? 612 TYR A CD1 1 
ATOM   3932 C CD1 B TYR A 1 282 ? 21.84100  54.01200  9.94800  0.300 60.53839  ? 612 TYR A CD1 1 
ATOM   3933 C CD2 A TYR A 1 282 ? 20.15000  53.74600  8.18600  0.700 58.10312  ? 612 TYR A CD2 1 
ATOM   3934 C CD2 B TYR A 1 282 ? 20.08100  53.67600  8.37600  0.300 57.89401  ? 612 TYR A CD2 1 
ATOM   3935 C CE1 A TYR A 1 282 ? 22.55000  55.03600  8.64700  0.700 63.82652  ? 612 TYR A CE1 1 
ATOM   3936 C CE1 B TYR A 1 282 ? 22.53000  54.77300  9.02000  0.300 62.77403  ? 612 TYR A CE1 1 
ATOM   3937 C CE2 A TYR A 1 282 ? 20.71000  54.53300  7.19500  0.700 59.97804  ? 612 TYR A CE2 1 
ATOM   3938 C CE2 B TYR A 1 282 ? 20.76200  54.43700  7.44300  0.300 60.48334  ? 612 TYR A CE2 1 
ATOM   3939 C CZ  A TYR A 1 282 ? 21.91000  55.17500  7.43000  0.700 59.41767  ? 612 TYR A CZ  1 
ATOM   3940 C CZ  B TYR A 1 282 ? 21.98500  54.98400  7.77100  0.300 61.23628  ? 612 TYR A CZ  1 
ATOM   3941 O OH  A TYR A 1 282 ? 22.46700  55.96200  6.44600  0.700 58.39184  ? 612 TYR A OH  1 
ATOM   3942 O OH  B TYR A 1 282 ? 22.66300  55.74500  6.84600  0.300 59.57558  ? 612 TYR A OH  1 
ATOM   3943 N N   A LEU A 1 283 ? 17.64100  54.37600  11.33100 0.700 54.16756  ? 613 LEU A N   1 
ATOM   3944 N N   B LEU A 1 283 ? 17.40600  54.39700  11.39400 0.300 54.06318  ? 613 LEU A N   1 
ATOM   3945 C CA  A LEU A 1 283 ? 16.70000  55.47000  11.09900 0.700 45.66775  ? 613 LEU A CA  1 
ATOM   3946 C CA  B LEU A 1 283 ? 16.53300  55.53700  11.13200 0.300 45.96412  ? 613 LEU A CA  1 
ATOM   3947 C C   A LEU A 1 283 ? 16.69300  56.44200  12.27200 0.700 50.04257  ? 613 LEU A C   1 
ATOM   3948 C C   B LEU A 1 283 ? 16.54400  56.50500  12.31000 0.300 50.57029  ? 613 LEU A C   1 
ATOM   3949 O O   A LEU A 1 283 ? 16.70800  57.66200  12.07700 0.700 64.27566  ? 613 LEU A O   1 
ATOM   3950 O O   B LEU A 1 283 ? 16.60900  57.72500  12.11900 0.300 63.43437  ? 613 LEU A O   1 
ATOM   3951 C CB  A LEU A 1 283 ? 15.28900  54.93000  10.85700 0.700 45.84693  ? 613 LEU A CB  1 
ATOM   3952 C CB  B LEU A 1 283 ? 15.11000  55.05700  10.85000 0.300 45.63707  ? 613 LEU A CB  1 
ATOM   3953 C CG  A LEU A 1 283 ? 14.20200  56.00400  10.68600 0.700 37.20626  ? 613 LEU A CG  1 
ATOM   3954 C CG  B LEU A 1 283 ? 14.06400  56.15400  10.64000 0.300 38.39267  ? 613 LEU A CG  1 
ATOM   3955 C CD1 A LEU A 1 283 ? 14.54700  56.96000  9.55300  0.700 42.72577  ? 613 LEU A CD1 1 
ATOM   3956 C CD1 B LEU A 1 283 ? 14.46600  57.09400  9.50900  0.300 43.34284  ? 613 LEU A CD1 1 
ATOM   3957 C CD2 A LEU A 1 283 ? 12.82600  55.39300  10.47400 0.700 43.90811  ? 613 LEU A CD2 1 
ATOM   3958 C CD2 B LEU A 1 283 ? 12.69000  55.55200  10.39600 0.300 43.57531  ? 613 LEU A CD2 1 
ATOM   3959 N N   A ARG A 1 284 ? 16.68500  55.91300  13.50000 0.700 58.07568  ? 614 ARG A N   1 
ATOM   3960 N N   B ARG A 1 284 ? 16.48100  55.97800  13.53600 0.300 57.16191  ? 614 ARG A N   1 
ATOM   3961 C CA  A ARG A 1 284 ? 16.60900  56.76100  14.68700 0.700 55.55696  ? 614 ARG A CA  1 
ATOM   3962 C CA  B ARG A 1 284 ? 16.42700  56.83200  14.71900 0.300 55.13991  ? 614 ARG A CA  1 
ATOM   3963 C C   A ARG A 1 284 ? 17.86200  57.61900  14.85000 0.700 56.48299  ? 614 ARG A C   1 
ATOM   3964 C C   B ARG A 1 284 ? 17.71900  57.62500  14.89700 0.300 56.07952  ? 614 ARG A C   1 
ATOM   3965 O O   A ARG A 1 284 ? 17.76600  58.78100  15.26400 0.700 54.41514  ? 614 ARG A O   1 
ATOM   3966 O O   B ARG A 1 284 ? 17.68100  58.78300  15.33000 0.300 54.58934  ? 614 ARG A O   1 
ATOM   3967 C CB  A ARG A 1 284 ? 16.35300  55.89200  15.91500 0.700 48.50162  ? 614 ARG A CB  1 
ATOM   3968 C CB  B ARG A 1 284 ? 16.12400  55.99600  15.96100 0.300 50.02072  ? 614 ARG A CB  1 
ATOM   3969 C CG  A ARG A 1 284 ? 14.89100  55.49600  16.02200 0.700 49.60176  ? 614 ARG A CG  1 
ATOM   3970 C CG  B ARG A 1 284 ? 14.65200  55.64700  16.09600 0.300 51.45437  ? 614 ARG A CG  1 
ATOM   3971 C CD  A ARG A 1 284 ? 14.65100  54.34700  16.98100 0.700 58.97263  ? 614 ARG A CD  1 
ATOM   3972 C CD  B ARG A 1 284 ? 14.40400  54.52900  17.09000 0.300 58.69603  ? 614 ARG A CD  1 
ATOM   3973 N NE  A ARG A 1 284 ? 13.24200  54.26300  17.34800 0.700 59.22217  ? 614 ARG A NE  1 
ATOM   3974 N NE  B ARG A 1 284 ? 13.00200  54.48500  17.49000 0.300 59.39663  ? 614 ARG A NE  1 
ATOM   3975 C CZ  A ARG A 1 284 ? 12.76200  53.49900  18.32000 0.700 52.42749  ? 614 ARG A CZ  1 
ATOM   3976 C CZ  B ARG A 1 284 ? 12.52700  53.76000  18.49300 0.300 54.13031  ? 614 ARG A CZ  1 
ATOM   3977 N NH1 A ARG A 1 284 ? 13.55300  52.72000  19.04100 0.700 59.71323  ? 614 ARG A NH1 1 
ATOM   3978 N NH1 B ARG A 1 284 ? 13.32000  53.00300  19.23400 0.300 57.87824  ? 614 ARG A NH1 1 
ATOM   3979 N NH2 A ARG A 1 284 ? 11.45600  53.51500  18.57200 0.700 41.06747  ? 614 ARG A NH2 1 
ATOM   3980 N NH2 B ARG A 1 284 ? 11.22400  53.79300  18.75800 0.300 45.09767  ? 614 ARG A NH2 1 
ATOM   3981 N N   A VAL A 1 285 ? 19.04200  57.07300  14.53000 0.700 54.10053  ? 615 VAL A N   1 
ATOM   3982 N N   B VAL A 1 285 ? 18.87100  57.02000  14.58800 0.300 54.42814  ? 615 VAL A N   1 
ATOM   3983 C CA  A VAL A 1 285 ? 20.25900  57.88600  14.56300 0.700 49.91699  ? 615 VAL A CA  1 
ATOM   3984 C CA  B VAL A 1 285 ? 20.13000  57.76500  14.64200 0.300 50.41147  ? 615 VAL A CA  1 
ATOM   3985 C C   A VAL A 1 285 ? 20.11900  59.03900  13.57600 0.700 58.11444  ? 615 VAL A C   1 
ATOM   3986 C C   B VAL A 1 285 ? 20.07100  58.93700  13.66700 0.300 57.57295  ? 615 VAL A C   1 
ATOM   3987 O O   A VAL A 1 285 ? 20.46300  60.18600  13.88700 0.700 62.18229  ? 615 VAL A O   1 
ATOM   3988 O O   B VAL A 1 285 ? 20.47800  60.05700  13.99700 0.300 61.63137  ? 615 VAL A O   1 
ATOM   3989 C CB  A VAL A 1 285 ? 21.54300  57.04900  14.34500 0.700 50.39516  ? 615 VAL A CB  1 
ATOM   3990 C CB  B VAL A 1 285 ? 21.35400  56.84600  14.42300 0.300 52.86884  ? 615 VAL A CB  1 
ATOM   3991 C CG1 A VAL A 1 285 ? 21.54600  55.80600  15.23600 0.700 56.19906  ? 615 VAL A CG1 1 
ATOM   3992 C CG1 B VAL A 1 285 ? 21.70200  56.63400  12.95700 0.300 61.68715  ? 615 VAL A CG1 1 
ATOM   3993 C CG2 A VAL A 1 285 ? 21.81300  56.71100  12.88900 0.700 62.33766  ? 615 VAL A CG2 1 
ATOM   3994 C CG2 B VAL A 1 285 ? 22.56100  57.38700  15.18300 0.300 46.55791  ? 615 VAL A CG2 1 
ATOM   3995 N N   A LEU A 1 286 ? 19.61300  58.75200  12.37000 0.700 61.95947  ? 616 LEU A N   1 
ATOM   3996 N N   B LEU A 1 286 ? 19.57500  58.69600  12.44700 0.300 61.61761  ? 616 LEU A N   1 
ATOM   3997 C CA  A LEU A 1 286 ? 19.49900  59.78600  11.34800 0.700 60.86577  ? 616 LEU A CA  1 
ATOM   3998 C CA  B LEU A 1 286 ? 19.53300  59.75100  11.44000 0.300 60.88231  ? 616 LEU A CA  1 
ATOM   3999 C C   A LEU A 1 286 ? 18.52900  60.86300  11.80900 0.700 50.37982  ? 616 LEU A C   1 
ATOM   4000 C C   B LEU A 1 286 ? 18.59800  60.86600  11.89000 0.300 51.00639  ? 616 LEU A C   1 
ATOM   4001 O O   A LEU A 1 286 ? 18.76500  62.05700  11.58500 0.700 63.28593  ? 616 LEU A O   1 
ATOM   4002 O O   B LEU A 1 286 ? 18.89100  62.05000  11.68700 0.300 62.27809  ? 616 LEU A O   1 
ATOM   4003 C CB  A LEU A 1 286 ? 19.02800  59.16600  10.03300 0.700 57.22066  ? 616 LEU A CB  1 
ATOM   4004 C CB  B LEU A 1 286 ? 19.08600  59.18600  10.09200 0.300 57.41451  ? 616 LEU A CB  1 
ATOM   4005 C CG  A LEU A 1 286 ? 19.99600  59.10900  8.85100  0.700 56.26822  ? 616 LEU A CG  1 
ATOM   4006 C CG  B LEU A 1 286 ? 20.02200  58.19100  9.40300  0.300 55.10311  ? 616 LEU A CG  1 
ATOM   4007 C CD1 A LEU A 1 286 ? 21.22900  58.29500  9.19900  0.700 53.24306  ? 616 LEU A CD1 1 
ATOM   4008 C CD1 B LEU A 1 286 ? 19.33700  57.57200  8.19400  0.300 58.65489  ? 616 LEU A CD1 1 
ATOM   4009 C CD2 A LEU A 1 286 ? 19.29100  58.52000  7.63800  0.700 55.17270  ? 616 LEU A CD2 1 
ATOM   4010 C CD2 B LEU A 1 286 ? 21.32500  58.86300  9.00200  0.300 55.43728  ? 616 LEU A CD2 1 
ATOM   4011 N N   A ILE A 1 287 ? 17.42300  60.46000  12.43900 0.700 45.50760  ? 617 ILE A N   1 
ATOM   4012 N N   B ILE A 1 287 ? 17.46000  60.50400  12.48900 0.300 45.95666  ? 617 ILE A N   1 
ATOM   4013 C CA  A ILE A 1 287 ? 16.46300  61.43700  12.94200 0.700 52.66881  ? 617 ILE A CA  1 
ATOM   4014 C CA  B ILE A 1 287 ? 16.52300  61.51600  12.96900 0.300 52.93964  ? 617 ILE A CA  1 
ATOM   4015 C C   A ILE A 1 287 ? 17.13900  62.29100  14.00700 0.700 50.77419  ? 617 ILE A C   1 
ATOM   4016 C C   B ILE A 1 287 ? 17.20100  62.35100  14.04600 0.300 51.11293  ? 617 ILE A C   1 
ATOM   4017 O O   A ILE A 1 287 ? 16.94000  63.51100  14.07800 0.700 54.81632  ? 617 ILE A O   1 
ATOM   4018 O O   B ILE A 1 287 ? 17.02500  63.57400  14.11500 0.300 54.92098  ? 617 ILE A O   1 
ATOM   4019 C CB  A ILE A 1 287 ? 15.20600  60.73300  13.48700 0.700 58.98734  ? 617 ILE A CB  1 
ATOM   4020 C CB  B ILE A 1 287 ? 15.23000  60.85700  13.48700 0.300 58.50535  ? 617 ILE A CB  1 
ATOM   4021 C CG1 A ILE A 1 287 ? 14.48200  59.99300  12.36100 0.700 53.96145  ? 617 ILE A CG1 1 
ATOM   4022 C CG1 B ILE A 1 287 ? 14.50000  60.13900  12.35100 0.300 53.84725  ? 617 ILE A CG1 1 
ATOM   4023 C CG2 A ILE A 1 287 ? 14.27900  61.73700  14.16400 0.700 51.03767  ? 617 ILE A CG2 1 
ATOM   4024 C CG2 B ILE A 1 287 ? 14.32000  61.89300  14.13000 0.300 50.89908  ? 617 ILE A CG2 1 
ATOM   4025 C CD1 A ILE A 1 287 ? 13.93200  60.90600  11.28600 0.700 54.10081  ? 617 ILE A CD1 1 
ATOM   4026 C CD1 B ILE A 1 287 ? 14.00200  61.06200  11.26700 0.300 54.04331  ? 617 ILE A CD1 1 
ATOM   4027 N N   A HIS A 1 288 ? 17.97200  61.65600  14.83800 0.700 56.50445  ? 618 HIS A N   1 
ATOM   4028 N N   B HIS A 1 288 ? 17.99300  61.69800  14.90100 0.300 56.49255  ? 618 HIS A N   1 
ATOM   4029 C CA  A HIS A 1 288 ? 18.61200  62.34100  15.95400 0.700 50.24554  ? 618 HIS A CA  1 
ATOM   4030 C CA  B HIS A 1 288 ? 18.62700  62.38500  16.02000 0.300 50.66463  ? 618 HIS A CA  1 
ATOM   4031 C C   A HIS A 1 288 ? 19.61900  63.35800  15.43400 0.700 49.53796  ? 618 HIS A C   1 
ATOM   4032 C C   B HIS A 1 288 ? 19.67500  63.36000  15.50100 0.300 49.97305  ? 618 HIS A C   1 
ATOM   4033 O O   A HIS A 1 288 ? 19.67600  64.49400  15.92100 0.700 54.12791  ? 618 HIS A O   1 
ATOM   4034 O O   B HIS A 1 288 ? 19.76500  64.49800  15.97600 0.300 54.39417  ? 618 HIS A O   1 
ATOM   4035 C CB  A HIS A 1 288 ? 19.28000  61.32300  16.87800 0.700 51.25321  ? 618 HIS A CB  1 
ATOM   4036 C CB  B HIS A 1 288 ? 19.24700  61.37300  16.98300 0.300 51.80560  ? 618 HIS A CB  1 
ATOM   4037 C CG  A HIS A 1 288 ? 19.76100  61.90400  18.17100 0.700 62.61944  ? 618 HIS A CG  1 
ATOM   4038 C CG  B HIS A 1 288 ? 19.70900  61.97200  18.27400 0.300 62.32642  ? 618 HIS A CG  1 
ATOM   4039 N ND1 A HIS A 1 288 ? 18.90200  62.31100  19.16900 0.700 63.51253  ? 618 HIS A ND1 1 
ATOM   4040 N ND1 B HIS A 1 288 ? 20.91600  61.64900  18.85500 0.300 67.35531  ? 618 HIS A ND1 1 
ATOM   4041 C CD2 A HIS A 1 288 ? 21.01100  62.14900  18.62800 0.700 70.95570  ? 618 HIS A CD2 1 
ATOM   4042 C CD2 B HIS A 1 288 ? 19.12300  62.87100  19.10000 0.300 59.94012  ? 618 HIS A CD2 1 
ATOM   4043 C CE1 A HIS A 1 288 ? 19.60300  62.78000  20.18600 0.700 62.67776  ? 618 HIS A CE1 1 
ATOM   4044 C CE1 B HIS A 1 288 ? 21.05500  62.32400  19.98200 0.300 65.24350  ? 618 HIS A CE1 1 
ATOM   4045 N NE2 A HIS A 1 288 ? 20.88500  62.69300  19.88300 0.700 66.95565  ? 618 HIS A NE2 1 
ATOM   4046 N NE2 B HIS A 1 288 ? 19.98100  63.07300  20.15400 0.300 62.84296  ? 618 HIS A NE2 1 
ATOM   4047 N N   A GLU A 1 289 ? 20.41500  62.96400  14.43800 0.700 56.70267  ? 619 GLU A N   1 
ATOM   4048 N N   B GLU A 1 289 ? 20.48400  62.91900  14.53200 0.300 56.82984  ? 619 GLU A N   1 
ATOM   4049 C CA  A GLU A 1 289 ? 21.38700  63.87600  13.84400 0.700 58.26416  ? 619 GLU A CA  1 
ATOM   4050 C CA  B GLU A 1 289 ? 21.49100  63.79400  13.94100 0.300 58.24494  ? 619 GLU A CA  1 
ATOM   4051 C C   A GLU A 1 289 ? 20.67500  65.08200  13.24300 0.700 57.77382  ? 619 GLU A C   1 
ATOM   4052 C C   B GLU A 1 289 ? 20.81400  64.99300  13.29400 0.300 57.68313  ? 619 GLU A C   1 
ATOM   4053 O O   A GLU A 1 289 ? 21.16900  66.21300  13.33100 0.700 51.49546  ? 619 GLU A O   1 
ATOM   4054 O O   B GLU A 1 289 ? 21.30700  66.12400  13.38500 0.300 52.15890  ? 619 GLU A O   1 
ATOM   4055 C CB  A GLU A 1 289 ? 22.22700  63.15600  12.78800 0.700 59.53783  ? 619 GLU A CB  1 
ATOM   4056 C CB  B GLU A 1 289 ? 22.32100  63.02400  12.91500 0.300 60.18659  ? 619 GLU A CB  1 
ATOM   4057 C CG  A GLU A 1 289 ? 23.37400  62.33200  13.36400 0.700 69.45374  ? 619 GLU A CG  1 
ATOM   4058 C CG  B GLU A 1 289 ? 23.42700  62.17300  13.51200 0.300 69.52190  ? 619 GLU A CG  1 
ATOM   4059 C CD  A GLU A 1 289 ? 24.05900  61.46700  12.32000 0.700 81.80885  ? 619 GLU A CD  1 
ATOM   4060 C CD  B GLU A 1 289 ? 24.08100  61.27200  12.48300 0.300 80.48589  ? 619 GLU A CD  1 
ATOM   4061 O OE1 A GLU A 1 289 ? 23.80700  61.67300  11.11300 0.700 80.74173  ? 619 GLU A OE1 1 
ATOM   4062 O OE1 B GLU A 1 289 ? 23.83900  61.47500  11.27400 0.300 80.81790  ? 619 GLU A OE1 1 
ATOM   4063 O OE2 A GLU A 1 289 ? 24.85200  60.58100  12.70600 0.700 81.13595  ? 619 GLU A OE2 1 
ATOM   4064 O OE2 B GLU A 1 289 ? 24.83400  60.35900  12.88200 0.300 79.09592  ? 619 GLU A OE2 1 
ATOM   4065 N N   A HIS A 1 290 ? 19.52500  64.85500  12.60100 0.700 58.13103  ? 620 HIS A N   1 
ATOM   4066 N N   B HIS A 1 290 ? 19.68600  64.75300  12.62000 0.300 57.85417  ? 620 HIS A N   1 
ATOM   4067 C CA  A HIS A 1 290 ? 18.79000  65.95400  11.98800 0.700 51.34220  ? 620 HIS A CA  1 
ATOM   4068 C CA  B HIS A 1 290 ? 18.95400  65.82500  11.95700 0.300 52.32014  ? 620 HIS A CA  1 
ATOM   4069 C C   A HIS A 1 290 ? 18.40000  66.97800  13.04400 0.700 54.48182  ? 620 HIS A C   1 
ATOM   4070 C C   B HIS A 1 290 ? 18.50200  66.86000  12.97600 0.300 54.63763  ? 620 HIS A C   1 
ATOM   4071 O O   A HIS A 1 290 ? 18.54400  68.18800  12.83300 0.700 58.48484  ? 620 HIS A O   1 
ATOM   4072 O O   B HIS A 1 290 ? 18.61200  68.06900  12.74300 0.300 58.10824  ? 620 HIS A O   1 
ATOM   4073 C CB  A HIS A 1 290 ? 17.55900  65.41900  11.25700 0.700 53.17844  ? 620 HIS A CB  1 
ATOM   4074 C CB  B HIS A 1 290 ? 17.75200  65.25400  11.20400 0.300 54.20942  ? 620 HIS A CB  1 
ATOM   4075 C CG  A HIS A 1 290 ? 16.73900  66.48400  10.59900 0.700 62.53862  ? 620 HIS A CG  1 
ATOM   4076 C CG  B HIS A 1 290 ? 16.93000  66.28700  10.49600 0.300 62.84431  ? 620 HIS A CG  1 
ATOM   4077 N ND1 A HIS A 1 290 ? 15.80900  67.23800  11.28200 0.700 62.94444  ? 620 HIS A ND1 1 
ATOM   4078 N ND1 B HIS A 1 290 ? 17.33900  66.89400  9.32800  0.300 63.64191  ? 620 HIS A ND1 1 
ATOM   4079 C CD2 A HIS A 1 290 ? 16.71500  66.92800  9.31900  0.700 66.99715  ? 620 HIS A CD2 1 
ATOM   4080 C CD2 B HIS A 1 290 ? 15.72500  66.82600  10.79800 0.300 65.14532  ? 620 HIS A CD2 1 
ATOM   4081 C CE1 A HIS A 1 290 ? 15.24400  68.09600  10.45100 0.700 70.28675  ? 620 HIS A CE1 1 
ATOM   4082 C CE1 B HIS A 1 290 ? 16.41700  67.75600  8.93600  0.300 67.24759  ? 620 HIS A CE1 1 
ATOM   4083 N NE2 A HIS A 1 290 ? 15.77600  67.92900  9.25400  0.700 71.83497  ? 620 HIS A NE2 1 
ATOM   4084 N NE2 B HIS A 1 290 ? 15.42900  67.73600  9.81200  0.300 68.72880  ? 620 HIS A NE2 1 
ATOM   4085 N N   A ILE A 1 291 ? 17.91300  66.51100  14.19500 0.700 57.27297  ? 621 ILE A N   1 
ATOM   4086 N N   B ILE A 1 291 ? 17.98900  66.39600  14.11800 0.300 57.19207  ? 621 ILE A N   1 
ATOM   4087 C CA  A ILE A 1 291 ? 17.42700  67.43600  15.20700 0.700 60.54596  ? 621 ILE A CA  1 
ATOM   4088 C CA  B ILE A 1 291 ? 17.41700  67.29500  15.11200 0.300 59.84287  ? 621 ILE A CA  1 
ATOM   4089 C C   A ILE A 1 291 ? 18.60500  68.13100  15.87700 0.700 52.29051  ? 621 ILE A C   1 
ATOM   4090 C C   B ILE A 1 291 ? 18.52700  68.05300  15.83000 0.300 52.98705  ? 621 ILE A C   1 
ATOM   4091 O O   A ILE A 1 291 ? 18.50600  69.29200  16.28800 0.700 56.74557  ? 621 ILE A O   1 
ATOM   4092 O O   B ILE A 1 291 ? 18.35800  69.21900  16.20400 0.300 56.55138  ? 621 ILE A O   1 
ATOM   4093 C CB  A ILE A 1 291 ? 16.53900  66.70100  16.23200 0.700 57.09348  ? 621 ILE A CB  1 
ATOM   4094 C CB  B ILE A 1 291 ? 16.56600  66.46900  16.09700 0.300 57.17730  ? 621 ILE A CB  1 
ATOM   4095 C CG1 A ILE A 1 291 ? 15.12700  66.50600  15.67800 0.700 50.45586  ? 621 ILE A CG1 1 
ATOM   4096 C CG1 B ILE A 1 291 ? 15.19700  66.14600  15.49700 0.300 53.17176  ? 621 ILE A CG1 1 
ATOM   4097 C CG2 A ILE A 1 291 ? 16.49400  67.44200  17.57400 0.700 66.42308  ? 621 ILE A CG2 1 
ATOM   4098 C CG2 B ILE A 1 291 ? 16.41100  67.18600  17.43500 0.300 64.62704  ? 621 ILE A CG2 1 
ATOM   4099 C CD1 A ILE A 1 291 ? 14.15300  66.02600  16.70500 0.700 48.23457  ? 621 ILE A CD1 1 
ATOM   4100 C CD1 B ILE A 1 291 ? 14.22200  67.27200  15.56500 0.300 59.12041  ? 621 ILE A CD1 1 
ATOM   4101 N N   A LEU A 1 292 ? 19.73600  67.43900  16.01600 0.700 51.00520  ? 622 LEU A N   1 
ATOM   4102 N N   B LEU A 1 292 ? 19.68000  67.41500  16.02200 0.300 51.27033  ? 622 LEU A N   1 
ATOM   4103 C CA  A LEU A 1 292 ? 20.90400  68.06700  16.63000 0.700 50.58406  ? 622 LEU A CA  1 
ATOM   4104 C CA  B LEU A 1 292 ? 20.81200  68.07300  16.66800 0.300 50.88521  ? 622 LEU A CA  1 
ATOM   4105 C C   A LEU A 1 292 ? 21.46900  69.17600  15.74700 0.700 54.92530  ? 622 LEU A C   1 
ATOM   4106 C C   B LEU A 1 292 ? 21.38900  69.18200  15.79300 0.300 55.04842  ? 622 LEU A C   1 
ATOM   4107 O O   A LEU A 1 292 ? 21.69000  70.30300  16.20500 0.700 62.76924  ? 622 LEU A O   1 
ATOM   4108 O O   B LEU A 1 292 ? 21.59500  70.31100  16.25400 0.300 62.12818  ? 622 LEU A O   1 
ATOM   4109 C CB  A LEU A 1 292 ? 21.96300  67.00900  16.93900 0.700 52.34401  ? 622 LEU A CB  1 
ATOM   4110 C CB  B LEU A 1 292 ? 21.88400  67.03900  17.01400 0.300 52.56316  ? 622 LEU A CB  1 
ATOM   4111 C CG  A LEU A 1 292 ? 21.61800  66.10400  18.13400 0.700 43.43815  ? 622 LEU A CG  1 
ATOM   4112 C CG  B LEU A 1 292 ? 21.55000  66.12600  18.19600 0.300 43.36302  ? 622 LEU A CG  1 
ATOM   4113 C CD1 A LEU A 1 292 ? 22.74800  65.12500  18.38800 0.700 49.07744  ? 622 LEU A CD1 1 
ATOM   4114 C CD1 B LEU A 1 292 ? 22.69400  65.17200  18.48800 0.300 49.49853  ? 622 LEU A CD1 1 
ATOM   4115 C CD2 A LEU A 1 292 ? 21.32900  66.94300  19.37500 0.700 40.47112  ? 622 LEU A CD2 1 
ATOM   4116 C CD2 B LEU A 1 292 ? 21.20900  66.95000  19.42800 0.300 41.65149  ? 622 LEU A CD2 1 
ATOM   4117 N N   A ILE A 1 293 ? 21.69300  68.88000  14.46900 0.700 57.36448  ? 623 ILE A N   1 
ATOM   4118 N N   B ILE A 1 293 ? 21.65600  68.87200  14.52300 0.300 57.25360  ? 623 ILE A N   1 
ATOM   4119 C CA  A ILE A 1 293 ? 22.23200  69.88700  13.56100 0.700 54.88737  ? 623 ILE A CA  1 
ATOM   4120 C CA  B ILE A 1 293 ? 22.21900  69.84800  13.59200 0.300 54.95879  ? 623 ILE A CA  1 
ATOM   4121 C C   A ILE A 1 293 ? 21.20800  70.98000  13.29000 0.700 50.92202  ? 623 ILE A C   1 
ATOM   4122 C C   B ILE A 1 293 ? 21.21500  70.95200  13.26500 0.300 51.25315  ? 623 ILE A C   1 
ATOM   4123 O O   A ILE A 1 293 ? 21.53400  72.17000  13.33600 0.700 60.97635  ? 623 ILE A O   1 
ATOM   4124 O O   B ILE A 1 293 ? 21.56000  72.14000  13.26400 0.300 60.70921  ? 623 ILE A O   1 
ATOM   4125 C CB  A ILE A 1 293 ? 22.70900  69.23300  12.25300 0.700 51.37521  ? 623 ILE A CB  1 
ATOM   4126 C CB  B ILE A 1 293 ? 22.71800  69.14300  12.31800 0.300 51.81614  ? 623 ILE A CB  1 
ATOM   4127 C CG1 A ILE A 1 293 ? 23.85900  68.25100  12.51300 0.700 53.82267  ? 623 ILE A CG1 1 
ATOM   4128 C CG1 B ILE A 1 293 ? 23.87500  68.20000  12.65100 0.300 53.80921  ? 623 ILE A CG1 1 
ATOM   4129 C CG2 A ILE A 1 293 ? 23.18100  70.32900  11.26500 0.700 58.72366  ? 623 ILE A CG2 1 
ATOM   4130 C CG2 B ILE A 1 293 ? 23.19300  70.16400  11.30400 0.300 57.93564  ? 623 ILE A CG2 1 
ATOM   4131 C CD1 A ILE A 1 293 ? 24.02300  67.20600  11.42600 0.700 62.95485  ? 623 ILE A CD1 1 
ATOM   4132 C CD1 B ILE A 1 293 ? 24.05400  67.07700  11.65100 0.300 62.28128  ? 623 ILE A CD1 1 
ATOM   4133 N N   A HIS A 1 294 ? 19.95300  70.59800  13.01900 0.700 46.42042  ? 624 HIS A N   1 
ATOM   4134 N N   B HIS A 1 294 ? 19.96300  70.58800  12.98900 0.300 46.90040  ? 624 HIS A N   1 
ATOM   4135 C CA  A HIS A 1 294 ? 18.94600  71.53500  12.52800 0.700 54.36862  ? 624 HIS A CA  1 
ATOM   4136 C CA  B HIS A 1 294 ? 18.98800  71.53400  12.45200 0.300 54.62596  ? 624 HIS A CA  1 
ATOM   4137 C C   A HIS A 1 294 ? 17.90200  71.95600  13.55200 0.700 54.04158  ? 624 HIS A C   1 
ATOM   4138 C C   B HIS A 1 294 ? 17.95300  72.01600  13.46300 0.300 54.69872  ? 624 HIS A C   1 
ATOM   4139 O O   A HIS A 1 294 ? 17.15700  72.90200  13.27900 0.700 56.01306  ? 624 HIS A O   1 
ATOM   4140 O O   B HIS A 1 294 ? 17.20900  72.95200  13.15300 0.300 56.16258  ? 624 HIS A O   1 
ATOM   4141 C CB  A HIS A 1 294 ? 18.20400  70.96200  11.30400 0.700 56.83946  ? 624 HIS A CB  1 
ATOM   4142 C CB  B HIS A 1 294 ? 18.26200  70.93000  11.24100 0.300 57.12207  ? 624 HIS A CB  1 
ATOM   4143 C CG  A HIS A 1 294 ? 19.10300  70.56900  10.17600 0.700 55.63147  ? 624 HIS A CG  1 
ATOM   4144 C CG  B HIS A 1 294 ? 19.17800  70.48500  10.14200 0.300 56.53607  ? 624 HIS A CG  1 
ATOM   4145 N ND1 A HIS A 1 294 ? 19.86500  69.42100  10.20400 0.700 65.11682  ? 624 HIS A ND1 1 
ATOM   4146 N ND1 B HIS A 1 294 ? 20.36100  71.12900  9.85200  0.300 53.03755  ? 624 HIS A ND1 1 
ATOM   4147 C CD2 A HIS A 1 294 ? 19.35700  71.16100  8.98500  0.700 51.85076  ? 624 HIS A CD2 1 
ATOM   4148 C CD2 B HIS A 1 294 ? 19.07500  69.47000  9.25200  0.300 61.33612  ? 624 HIS A CD2 1 
ATOM   4149 C CE1 A HIS A 1 294 ? 20.55500  69.32500  9.08200  0.700 63.10630  ? 624 HIS A CE1 1 
ATOM   4150 C CE1 B HIS A 1 294 ? 20.95000  70.52700  8.83300  0.300 57.81080  ? 624 HIS A CE1 1 
ATOM   4151 N NE2 A HIS A 1 294 ? 20.26500  70.36800  8.32500  0.700 61.16788  ? 624 HIS A NE2 1 
ATOM   4152 N NE2 B HIS A 1 294 ? 20.19200  69.51600  8.45200  0.300 61.50574  ? 624 HIS A NE2 1 
ATOM   4153 N N   A GLY A 1 295 ? 17.83600  71.32000  14.71200 0.700 57.15716  ? 625 GLY A N   1 
ATOM   4154 N N   B GLY A 1 295 ? 17.87800  71.42200  14.64800 0.300 56.89520  ? 625 GLY A N   1 
ATOM   4155 C CA  A GLY A 1 295 ? 16.70700  71.48900  15.61200 0.700 55.57493  ? 625 GLY A CA  1 
ATOM   4156 C CA  B GLY A 1 295 ? 16.75500  71.66000  15.53600 0.300 55.81035  ? 625 GLY A CA  1 
ATOM   4157 C C   A GLY A 1 295 ? 15.42900  70.83800  15.11200 0.700 61.72723  ? 625 GLY A C   1 
ATOM   4158 C C   B GLY A 1 295 ? 15.45900  71.02600  15.06000 0.300 61.25372  ? 625 GLY A C   1 
ATOM   4159 O O   A GLY A 1 295 ? 15.34800  70.27300  14.02100 0.700 68.90040  ? 625 GLY A O   1 
ATOM   4160 O O   B GLY A 1 295 ? 15.36800  70.41100  13.99800 0.300 67.75297  ? 625 GLY A O   1 
ATOM   4161 N N   A ASP A 1 296 ? 14.40800  70.93200  15.95900 0.700 61.50439  ? 626 ASP A N   1 
ATOM   4162 N N   B ASP A 1 296 ? 14.43200  71.19100  15.89200 0.300 62.92533  ? 626 ASP A N   1 
ATOM   4163 C CA  A ASP A 1 296 ? 13.09200  70.34500  15.71500 0.700 62.46996  ? 626 ASP A CA  1 
ATOM   4164 C CA  B ASP A 1 296 ? 13.11100  70.61600  15.64500 0.300 64.18214  ? 626 ASP A CA  1 
ATOM   4165 C C   A ASP A 1 296 ? 12.20200  71.43700  15.12900 0.700 71.83247  ? 626 ASP A C   1 
ATOM   4166 C C   B ASP A 1 296 ? 12.22500  71.66300  14.97900 0.300 72.05063  ? 626 ASP A C   1 
ATOM   4167 O O   A ASP A 1 296 ? 11.52800  72.17600  15.85400 0.700 74.52555  ? 626 ASP A O   1 
ATOM   4168 O O   B ASP A 1 296 ? 11.53700  72.44100  15.64200 0.300 73.76321  ? 626 ASP A O   1 
ATOM   4169 C CB  A ASP A 1 296 ? 12.52400  69.75600  17.00300 0.700 55.80849  ? 626 ASP A CB  1 
ATOM   4170 C CB  B ASP A 1 296 ? 12.50400  70.11100  16.95100 0.300 57.72957  ? 626 ASP A CB  1 
ATOM   4171 C CG  A ASP A 1 296 ? 11.33800  68.84600  16.76400 0.700 64.24342  ? 626 ASP A CG  1 
ATOM   4172 C CG  B ASP A 1 296 ? 11.30500  69.20300  16.73300 0.300 65.52949  ? 626 ASP A CG  1 
ATOM   4173 O OD1 A ASP A 1 296 ? 10.43000  69.24300  16.00800 0.700 68.53901  ? 626 ASP A OD1 1 
ATOM   4174 O OD1 B ASP A 1 296 ? 10.41400  69.55800  15.93500 0.300 68.86018  ? 626 ASP A OD1 1 
ATOM   4175 O OD2 A ASP A 1 296 ? 11.31500  67.73200  17.32500 0.700 56.07349  ? 626 ASP A OD2 1 
ATOM   4176 O OD2 B ASP A 1 296 ? 11.25700  68.12600  17.36400 0.300 60.76789  ? 626 ASP A OD2 1 
ATOM   4177 N N   A ILE A 1 297 ? 12.19400  71.52900  13.79900 0.700 72.80575  ? 627 ILE A N   1 
ATOM   4178 N N   B ILE A 1 297 ? 12.24900  71.67600  13.64900 0.300 72.55066  ? 627 ILE A N   1 
ATOM   4179 C CA  A ILE A 1 297 ? 11.36600  72.48700  13.07300 0.700 70.44076  ? 627 ILE A CA  1 
ATOM   4180 C CA  B ILE A 1 297 ? 11.42200  72.56300  12.84100 0.300 71.20766  ? 627 ILE A CA  1 
ATOM   4181 C C   A ILE A 1 297 ? 10.28700  71.70700  12.33600 0.700 74.79503  ? 627 ILE A C   1 
ATOM   4182 C C   B ILE A 1 297 ? 10.39500  71.70000  12.12500 0.300 74.64890  ? 627 ILE A C   1 
ATOM   4183 O O   A ILE A 1 297 ? 10.59600  70.77800  11.57800 0.700 69.73000  ? 627 ILE A O   1 
ATOM   4184 O O   B ILE A 1 297 ? 10.75900  70.74100  11.43300 0.300 70.51037  ? 627 ILE A O   1 
ATOM   4185 C CB  A ILE A 1 297 ? 12.20000  73.30900  12.07500 0.700 76.13045  ? 627 ILE A CB  1 
ATOM   4186 C CB  B ILE A 1 297 ? 12.26200  73.36900  11.83700 0.300 76.01703  ? 627 ILE A CB  1 
ATOM   4187 C CG1 A ILE A 1 297 ? 13.56400  73.66800  12.66500 0.700 69.23206  ? 627 ILE A CG1 1 
ATOM   4188 C CG1 B ILE A 1 297 ? 13.56300  73.84400  12.48700 0.300 70.46619  ? 627 ILE A CG1 1 
ATOM   4189 C CG2 A ILE A 1 297 ? 11.46400  74.58100  11.69200 0.700 75.49546  ? 627 ILE A CG2 1 
ATOM   4190 C CG2 B ILE A 1 297 ? 11.46300  74.54600  11.29800 0.300 75.87542  ? 627 ILE A CG2 1 
ATOM   4191 C CD1 A ILE A 1 297 ? 14.59700  74.02200  11.60400 0.700 67.48643  ? 627 ILE A CD1 1 
ATOM   4192 C CD1 B ILE A 1 297 ? 14.65200  74.17700  11.49300 0.300 67.99629  ? 627 ILE A CD1 1 
ATOM   4193 N N   A ARG A 1 298 ? 9.02700   72.06900  12.55800 0.700 79.54237  ? 628 ARG A N   1 
ATOM   4194 N N   B ARG A 1 298 ? 9.11900   72.03300  12.28700 0.300 77.70143  ? 628 ARG A N   1 
ATOM   4195 C CA  A ARG A 1 298 ? 7.92000   71.30400  12.01200 0.700 71.30051  ? 628 ARG A CA  1 
ATOM   4196 C CA  B ARG A 1 298 ? 8.04400   71.20300  11.77200 0.300 71.34946  ? 628 ARG A CA  1 
ATOM   4197 C C   A ARG A 1 298 ? 7.08600   72.13700  11.05000 0.700 76.79237  ? 628 ARG A C   1 
ATOM   4198 C C   B ARG A 1 298 ? 7.22500   71.96200  10.73800 0.300 74.60056  ? 628 ARG A C   1 
ATOM   4199 O O   A ARG A 1 298 ? 6.98500   73.36200  11.17900 0.700 82.26618  ? 628 ARG A O   1 
ATOM   4200 O O   B ARG A 1 298 ? 7.12700   73.19200  10.77400 0.300 80.44791  ? 628 ARG A O   1 
ATOM   4201 C CB  A ARG A 1 298 ? 6.98200   70.82300  13.13000 0.700 70.24614  ? 628 ARG A CB  1 
ATOM   4202 C CB  B ARG A 1 298 ? 7.12900   70.72000  12.90500 0.300 70.40685  ? 628 ARG A CB  1 
ATOM   4203 C CG  A ARG A 1 298 ? 6.89400   69.32800  13.34000 0.700 68.36267  ? 628 ARG A CG  1 
ATOM   4204 C CG  B ARG A 1 298 ? 7.87300   70.04000  14.03900 0.300 72.43228  ? 628 ARG A CG  1 
ATOM   4205 C CD  A ARG A 1 298 ? 7.87400   68.88800  14.40500 0.700 72.52974  ? 628 ARG A CD  1 
ATOM   4206 C CD  B ARG A 1 298 ? 8.17800   68.58800  13.71000 0.300 68.47128  ? 628 ARG A CD  1 
ATOM   4207 N NE  A ARG A 1 298 ? 8.11900   67.45200  14.37500 0.700 72.15400  ? 628 ARG A NE  1 
ATOM   4208 N NE  B ARG A 1 298 ? 8.52100   67.82100  14.90100 0.300 69.15918  ? 628 ARG A NE  1 
ATOM   4209 C CZ  A ARG A 1 298 ? 7.42100   66.56200  15.06700 0.700 83.49225  ? 628 ARG A CZ  1 
ATOM   4210 C CZ  B ARG A 1 298 ? 8.37100   66.50800  15.01800 0.300 72.30915  ? 628 ARG A CZ  1 
ATOM   4211 N NH1 A ARG A 1 298 ? 6.41500   66.92500  15.84700 0.700 83.64327  ? 628 ARG A NH1 1 
ATOM   4212 N NH1 B ARG A 1 298 ? 7.89800   65.77600  14.02300 0.300 69.83815  ? 628 ARG A NH1 1 
ATOM   4213 N NH2 A ARG A 1 298 ? 7.73300   65.27300  14.96600 0.700 77.32528  ? 628 ARG A NH2 1 
ATOM   4214 N NH2 B ARG A 1 298 ? 8.71200   65.91500  16.15900 0.300 66.66273  ? 628 ARG A NH2 1 
ATOM   4215 N N   A LYS A 1 299 ? 6.48300   71.44800  10.08200 0.700 68.55542  ? 629 LYS A N   1 
ATOM   4216 N N   B LYS A 1 299 ? 6.63900   71.20700  9.81400  0.300 68.92646  ? 629 LYS A N   1 
ATOM   4217 C CA  A LYS A 1 299 ? 5.51500   72.03400  9.16800  0.700 67.13282  ? 629 LYS A CA  1 
ATOM   4218 C CA  B LYS A 1 299 ? 5.70600   71.73000  8.82900  0.300 68.78531  ? 629 LYS A CA  1 
ATOM   4219 C C   A LYS A 1 299 ? 4.32000   71.09200  9.12300  0.700 61.77788  ? 629 LYS A C   1 
ATOM   4220 C C   B LYS A 1 299 ? 4.47300   70.84200  8.81800  0.300 66.77666  ? 629 LYS A C   1 
ATOM   4221 O O   A LYS A 1 299 ? 4.49400   69.87000  9.08400  0.700 71.46149  ? 629 LYS A O   1 
ATOM   4222 O O   B LYS A 1 299 ? 4.58900   69.61400  8.83700  0.300 72.17753  ? 629 LYS A O   1 
ATOM   4223 C CB  A LYS A 1 299 ? 6.11900   72.27200  7.76700  0.700 78.00221  ? 629 LYS A CB  1 
ATOM   4224 C CB  B LYS A 1 299 ? 6.34300   71.77500  7.43500  0.300 75.40791  ? 629 LYS A CB  1 
ATOM   4225 C CG  A LYS A 1 299 ? 5.90700   71.16900  6.73900  0.700 74.59713  ? 629 LYS A CG  1 
ATOM   4226 C CG  B LYS A 1 299 ? 5.50400   72.46400  6.37700  0.300 79.37776  ? 629 LYS A CG  1 
ATOM   4227 C CD  A LYS A 1 299 ? 5.92700   71.75000  5.33200  0.700 68.72522  ? 629 LYS A CD  1 
ATOM   4228 C CD  B LYS A 1 299 ? 6.07100   72.21000  4.99000  0.300 72.46429  ? 629 LYS A CD  1 
ATOM   4229 C CE  A LYS A 1 299 ? 6.29100   70.71400  4.28000  0.700 71.62861  ? 629 LYS A CE  1 
ATOM   4230 C CE  B LYS A 1 299 ? 6.20300   70.71800  4.72000  0.300 71.14162  ? 629 LYS A CE  1 
ATOM   4231 N NZ  A LYS A 1 299 ? 7.71300   70.28800  4.36500  0.700 75.65133  ? 629 LYS A NZ  1 
ATOM   4232 N NZ  B LYS A 1 299 ? 6.30900   70.41200  3.26700  0.300 80.19812  ? 629 LYS A NZ  1 
ATOM   4233 N N   A THR A 1 300 ? 3.10900   71.64000  9.16400  0.700 65.53506  ? 630 THR A N   1 
ATOM   4234 N N   B THR A 1 300 ? 3.29600   71.45800  8.76400  0.300 68.63602  ? 630 THR A N   1 
ATOM   4235 C CA  A THR A 1 300 ? 1.92900   70.78700  9.07300  0.700 77.42591  ? 630 THR A CA  1 
ATOM   4236 C CA  B THR A 1 300 ? 2.05600   70.69500  8.70500  0.300 77.40628  ? 630 THR A CA  1 
ATOM   4237 C C   A THR A 1 300 ? 1.60900   70.49800  7.61000  0.700 78.41895  ? 630 THR A C   1 
ATOM   4238 C C   B THR A 1 300 ? 1.77800   70.28500  7.26400  0.300 79.13548  ? 630 THR A C   1 
ATOM   4239 O O   A THR A 1 300 ? 1.31300   71.42500  6.84700  0.700 89.02251  ? 630 THR A O   1 
ATOM   4240 O O   B THR A 1 300 ? 1.60600   71.14400  6.39100  0.300 85.69113  ? 630 THR A O   1 
ATOM   4241 C CB  A THR A 1 300 ? 0.73700   71.45000  9.76100  0.700 83.54047  ? 630 THR A CB  1 
ATOM   4242 C CB  B THR A 1 300 ? 0.89500   71.51400  9.26700  0.300 82.78820  ? 630 THR A CB  1 
ATOM   4243 O OG1 A THR A 1 300 ? 0.38600   72.64800  9.05900  0.700 105.40572 ? 630 THR A OG1 1 
ATOM   4244 O OG1 B THR A 1 300 ? 1.04100   71.63700  10.68800 0.300 81.01966  ? 630 THR A OG1 1 
ATOM   4245 C CG2 A THR A 1 300 ? 1.07500   71.79200  11.20300 0.700 80.18863  ? 630 THR A CG2 1 
ATOM   4246 C CG2 B THR A 1 300 ? -0.43300  70.83800  8.95900  0.300 74.45987  ? 630 THR A CG2 1 
ATOM   4247 N N   A THR A 1 301 ? 1.66600   69.22700  7.21000  0.700 75.13719  ? 631 THR A N   1 
ATOM   4248 N N   B THR A 1 301 ? 1.73600   68.98000  7.01200  0.300 75.90802  ? 631 THR A N   1 
ATOM   4249 C CA  A THR A 1 301 ? 1.12000   68.80900  5.92700  0.700 80.53001  ? 631 THR A CA  1 
ATOM   4250 C CA  B THR A 1 301 ? 1.23400   68.44100  5.75700  0.300 80.82209  ? 631 THR A CA  1 
ATOM   4251 C C   A THR A 1 301 ? -0.10600  67.92800  6.13300  0.700 85.57704  ? 631 THR A C   1 
ATOM   4252 C C   B THR A 1 301 ? -0.08700  67.71700  5.97700  0.300 85.73801  ? 631 THR A C   1 
ATOM   4253 O O   A THR A 1 301 ? -0.12500  67.07600  7.02700  0.700 90.97506  ? 631 THR A O   1 
ATOM   4254 O O   B THR A 1 301 ? -0.26900  67.02000  6.98000  0.300 90.07816  ? 631 THR A O   1 
ATOM   4255 C CB  A THR A 1 301 ? 2.16600   68.07200  5.08400  0.700 77.20750  ? 631 THR A CB  1 
ATOM   4256 C CB  B THR A 1 301 ? 2.25000   67.49300  5.11500  0.300 75.28818  ? 631 THR A CB  1 
ATOM   4257 O OG1 A THR A 1 301 ? 2.21400   66.69600  5.47100  0.700 70.26164  ? 631 THR A OG1 1 
ATOM   4258 O OG1 B THR A 1 301 ? 2.12100   66.18500  5.68700  0.300 73.62095  ? 631 THR A OG1 1 
ATOM   4259 C CG2 A THR A 1 301 ? 3.53800   68.70300  5.25500  0.700 72.46769  ? 631 THR A CG2 1 
ATOM   4260 C CG2 B THR A 1 301 ? 3.66300   68.00900  5.32200  0.300 71.78452  ? 631 THR A CG2 1 
ATOM   4261 N N   A LYS A 1 302 ? -1.12600  68.12400  5.30200  0.700 89.49820  ? 632 LYS A N   1 
ATOM   4262 N N   B LYS A 1 302 ? -1.00300  67.89000  5.03000  0.300 89.62512  ? 632 LYS A N   1 
ATOM   4263 C CA  A LYS A 1 302 ? -2.35600  67.35400  5.41500  0.700 98.35825  ? 632 LYS A CA  1 
ATOM   4264 C CA  B LYS A 1 302 ? -2.33600  67.30900  5.07200  0.300 96.75302  ? 632 LYS A CA  1 
ATOM   4265 C C   A LYS A 1 302 ? -2.47800  66.47000  4.17800  0.700 99.33848  ? 632 LYS A C   1 
ATOM   4266 C C   B LYS A 1 302 ? -2.45000  66.27000  3.96500  0.300 97.77959  ? 632 LYS A C   1 
ATOM   4267 O O   A LYS A 1 302 ? -2.11500  66.88500  3.07300  0.700 95.31473  ? 632 LYS A O   1 
ATOM   4268 O O   B LYS A 1 302 ? -1.92600  66.46600  2.86400  0.300 93.89050  ? 632 LYS A O   1 
ATOM   4269 C CB  A LYS A 1 302 ? -3.58200  68.26400  5.65300  0.700 97.50039  ? 632 LYS A CB  1 
ATOM   4270 C CB  B LYS A 1 302 ? -3.41700  68.38500  4.92600  0.300 94.89615  ? 632 LYS A CB  1 
ATOM   4271 C CG  A LYS A 1 302 ? -4.19300  69.13100  4.53200  0.700 99.93041  ? 632 LYS A CG  1 
ATOM   4272 C CG  B LYS A 1 302 ? -4.83800  67.85400  4.81700  0.300 91.45219  ? 632 LYS A CG  1 
ATOM   4273 C CD  A LYS A 1 302 ? -4.87100  68.34600  3.41900  0.700 89.75904  ? 632 LYS A CD  1 
ATOM   4274 C CD  B LYS A 1 302 ? -5.85000  68.98900  4.85400  0.300 89.12110  ? 632 LYS A CD  1 
ATOM   4275 C CE  A LYS A 1 302 ? -5.52800  69.26000  2.39200  0.700 73.74692  ? 632 LYS A CE  1 
ATOM   4276 C CE  B LYS A 1 302 ? -7.26800  68.47500  4.66700  0.300 67.24262  ? 632 LYS A CE  1 
ATOM   4277 N NZ  A LYS A 1 302 ? -6.42500  68.51300  1.45800  0.700 72.88160  ? 632 LYS A NZ  1 
ATOM   4278 N NZ  B LYS A 1 302 ? -7.63200  67.45600  5.68900  0.300 49.11036  ? 632 LYS A NZ  1 
ATOM   4279 N N   A LEU A 1 303 ? -2.94900  65.24000  4.36700  0.700 97.05545  ? 633 LEU A N   1 
ATOM   4280 N N   B LEU A 1 303 ? -3.12600  65.16200  4.25300  0.300 96.73035  ? 633 LEU A N   1 
ATOM   4281 C CA  A LEU A 1 303 ? -3.00800  64.24900  3.29500  0.700 98.51003  ? 633 LEU A CA  1 
ATOM   4282 C CA  B LEU A 1 303 ? -3.20100  64.04500  3.32500  0.300 97.44038  ? 633 LEU A CA  1 
ATOM   4283 C C   A LEU A 1 303 ? -4.46500  63.86000  3.07400  0.700 101.45502 ? 633 LEU A C   1 
ATOM   4284 C C   B LEU A 1 303 ? -4.64500  63.79900  2.91500  0.300 100.15376 ? 633 LEU A C   1 
ATOM   4285 O O   A LEU A 1 303 ? -5.06000  63.17100  3.90900  0.700 94.06030  ? 633 LEU A O   1 
ATOM   4286 O O   B LEU A 1 303 ? -5.58100  64.07100  3.67300  0.300 93.43293  ? 633 LEU A O   1 
ATOM   4287 C CB  A LEU A 1 303 ? -2.16100  63.02500  3.63800  0.700 89.72784  ? 633 LEU A CB  1 
ATOM   4288 C CB  B LEU A 1 303 ? -2.61700  62.77200  3.94800  0.300 90.32680  ? 633 LEU A CB  1 
ATOM   4289 C CG  B LEU A 1 303 ? -1.14000  62.83000  4.34200  0.300 81.67708  ? 633 LEU A CG  1 
ATOM   4290 C CD1 B LEU A 1 303 ? -0.73100  61.56900  5.08500  0.300 70.02400  ? 633 LEU A CD1 1 
ATOM   4291 C CD2 B LEU A 1 303 ? -0.26900  63.03900  3.11700  0.300 83.40761  ? 633 LEU A CD2 1 
ATOM   4292 N N   A ASN A 1 304 ? -5.03100  64.27900  1.94500  0.700 104.52223 ? 634 ASN A N   1 
ATOM   4293 N N   B ASN A 1 304 ? -4.81500  63.29400  1.69400  0.300 97.13690  ? 634 ASN A N   1 
ATOM   4294 C CA  A ASN A 1 304 ? -6.42200  63.97500  1.61800  0.700 98.18182  ? 634 ASN A CA  1 
ATOM   4295 C CA  B ASN A 1 304 ? -6.14100  63.00300  1.15400  0.300 92.26638  ? 634 ASN A CA  1 
ATOM   4296 C C   A ASN A 1 304 ? -6.52600  62.82300  0.62200  0.700 89.53203  ? 634 ASN A C   1 
ATOM   4297 C C   B ASN A 1 304 ? -5.99400  61.88500  0.13100  0.300 87.99871  ? 634 ASN A C   1 
ATOM   4298 O O   A ASN A 1 304 ? -5.62000  62.60000  -0.18200 0.700 88.48336  ? 634 ASN A O   1 
ATOM   4299 O O   B ASN A 1 304 ? -5.36500  62.08000  -0.91400 0.300 90.82637  ? 634 ASN A O   1 
ATOM   4300 C CB  A ASN A 1 304 ? -7.12100  65.21500  1.05800  0.700 85.15620  ? 634 ASN A CB  1 
ATOM   4301 C CB  B ASN A 1 304 ? -6.76500  64.24500  0.52400  0.300 87.18391  ? 634 ASN A CB  1 
ATOM   4302 N N   A THR A 1 308 ? -9.41000  58.85400  2.64100  0.700 90.70335  ? 638 THR A N   1 
ATOM   4303 N N   B THR A 1 308 ? -7.99300  57.79400  4.52100  0.300 86.23821  ? 638 THR A N   1 
ATOM   4304 C CA  A THR A 1 308 ? -9.33000  59.42300  3.98100  0.700 101.80642 ? 638 THR A CA  1 
ATOM   4305 C CA  B THR A 1 308 ? -8.77600  58.98400  4.83400  0.300 93.38109  ? 638 THR A CA  1 
ATOM   4306 C C   A THR A 1 308 ? -8.42000  60.64800  3.99800  0.700 108.14266 ? 638 THR A C   1 
ATOM   4307 C C   B THR A 1 308 ? -7.90800  60.23600  4.76800  0.300 100.60964 ? 638 THR A C   1 
ATOM   4308 O O   A THR A 1 308 ? -7.48700  60.74900  3.20200  0.700 99.09604  ? 638 THR A O   1 
ATOM   4309 O O   B THR A 1 308 ? -6.97000  60.30200  3.97200  0.300 95.66844  ? 638 THR A O   1 
ATOM   4310 C CB  A THR A 1 308 ? -8.81200  58.39300  5.00200  0.700 90.55130  ? 638 THR A CB  1 
ATOM   4311 C CB  B THR A 1 308 ? -9.42200  58.88700  6.22800  0.300 86.74429  ? 638 THR A CB  1 
ATOM   4312 N N   A GLU A 1 309 ? -8.70100  61.58000  4.90700  0.700 114.05539 ? 639 GLU A N   1 
ATOM   4313 N N   B GLU A 1 309 ? -8.22200  61.22600  5.60200  0.300 105.48501 ? 639 GLU A N   1 
ATOM   4314 C CA  A GLU A 1 309 ? -7.92200  62.80600  5.05500  0.700 101.03687 ? 639 GLU A CA  1 
ATOM   4315 C CA  B GLU A 1 309 ? -7.47300  62.47800  5.64900  0.300 101.89967 ? 639 GLU A CA  1 
ATOM   4316 C C   A GLU A 1 309 ? -7.19100  62.76300  6.39300  0.700 105.73674 ? 639 GLU A C   1 
ATOM   4317 C C   B GLU A 1 309 ? -6.73700  62.58400  6.98200  0.300 101.29624 ? 639 GLU A C   1 
ATOM   4318 O O   A GLU A 1 309 ? -7.82500  62.77700  7.45400  0.700 99.73702  ? 639 GLU A O   1 
ATOM   4319 O O   B GLU A 1 309 ? -7.36500  62.68300  8.04000  0.300 97.13935  ? 639 GLU A O   1 
ATOM   4320 C CB  A GLU A 1 309 ? -8.81900  64.03800  4.95600  0.700 94.40166  ? 639 GLU A CB  1 
ATOM   4321 C CB  B GLU A 1 309 ? -8.40600  63.66900  5.43600  0.300 96.23765  ? 639 GLU A CB  1 
ATOM   4322 N N   A ILE A 1 310 ? -5.86200  62.71200  6.34000  0.700 106.23462 ? 640 ILE A N   1 
ATOM   4323 N N   B ILE A 1 310 ? -5.40800  62.56300  6.92000  0.300 101.66711 ? 640 ILE A N   1 
ATOM   4324 C CA  A ILE A 1 310 ? -5.02300  62.63400  7.53000  0.700 103.45251 ? 640 ILE A CA  1 
ATOM   4325 C CA  B ILE A 1 310 ? -4.52000  62.62200  8.07700  0.300 98.19933  ? 640 ILE A CA  1 
ATOM   4326 C C   A ILE A 1 310 ? -4.04000  63.79700  7.51600  0.700 101.31858 ? 640 ILE A C   1 
ATOM   4327 C C   B ILE A 1 310 ? -3.56700  63.79600  7.90100  0.300 97.95162  ? 640 ILE A C   1 
ATOM   4328 O O   A ILE A 1 310 ? -3.63400  64.27900  6.45300  0.700 98.41723  ? 640 ILE A O   1 
ATOM   4329 O O   B ILE A 1 310 ? -3.24000  64.19800  6.77900  0.300 95.95575  ? 640 ILE A O   1 
ATOM   4330 C CB  A ILE A 1 310 ? -4.27600  61.28500  7.62000  0.700 103.03705 ? 640 ILE A CB  1 
ATOM   4331 C CB  B ILE A 1 310 ? -3.74400  61.30800  8.32600  0.300 94.26297  ? 640 ILE A CB  1 
ATOM   4332 C CG1 A ILE A 1 310 ? -3.83500  60.82600  6.22900  0.700 92.05846  ? 640 ILE A CG1 1 
ATOM   4333 C CG1 B ILE A 1 310 ? -4.62000  60.10300  7.98300  0.300 97.96995  ? 640 ILE A CG1 1 
ATOM   4334 C CG2 A ILE A 1 310 ? -5.15500  60.23000  8.27700  0.700 101.77249 ? 640 ILE A CG2 1 
ATOM   4335 C CG2 B ILE A 1 310 ? -3.28000  61.22300  9.78200  0.300 80.87930  ? 640 ILE A CG2 1 
ATOM   4336 C CD1 A ILE A 1 310 ? -2.73200  59.79300  6.24800  0.700 81.45615  ? 640 ILE A CD1 1 
ATOM   4337 C CD1 B ILE A 1 310 ? -3.85300  58.81500  7.78900  0.300 76.47742  ? 640 ILE A CD1 1 
ATOM   4338 N N   A GLU A 1 311 ? -3.64600  64.24100  8.70900  0.700 102.35780 ? 641 GLU A N   1 
ATOM   4339 N N   B GLU A 1 311 ? -3.11900  64.33800  9.02800  0.300 97.24176  ? 641 GLU A N   1 
ATOM   4340 C CA  A GLU A 1 311 ? -2.68400  65.32000  8.87300  0.700 95.21292  ? 641 GLU A CA  1 
ATOM   4341 C CA  B GLU A 1 311 ? -2.17500  65.44300  9.09200  0.300 91.17383  ? 641 GLU A CA  1 
ATOM   4342 C C   A GLU A 1 311 ? -1.45400  64.80200  9.60100  0.700 92.36385  ? 641 GLU A C   1 
ATOM   4343 C C   B GLU A 1 311 ? -0.90700  64.95200  9.77300  0.300 86.85190  ? 641 GLU A C   1 
ATOM   4344 O O   A GLU A 1 311 ? -1.55800  64.03600  10.56500 0.700 86.37677  ? 641 GLU A O   1 
ATOM   4345 O O   B GLU A 1 311 ? -0.96000  64.19900  10.75100 0.300 85.90882  ? 641 GLU A O   1 
ATOM   4346 C CB  A GLU A 1 311 ? -3.29200  66.52000  9.61600  0.700 87.70970  ? 641 GLU A CB  1 
ATOM   4347 C CB  B GLU A 1 311 ? -2.74700  66.64600  9.84500  0.300 87.49233  ? 641 GLU A CB  1 
ATOM   4348 C CG  A GLU A 1 311 ? -2.28900  67.32200  10.43400 0.700 87.97448  ? 641 GLU A CG  1 
ATOM   4349 C CG  B GLU A 1 311 ? -3.60400  67.55100  8.98300  0.300 82.59867  ? 641 GLU A CG  1 
ATOM   4350 C CD  A GLU A 1 311 ? -2.91300  68.52100  11.11600 0.700 88.58323  ? 641 GLU A CD  1 
ATOM   4351 C CD  B GLU A 1 311 ? -4.18500  68.71600  9.75400  0.300 82.65051  ? 641 GLU A CD  1 
ATOM   4352 O OE1 A GLU A 1 311 ? -4.15500  68.64800  11.08100 0.700 90.64428  ? 641 GLU A OE1 1 
ATOM   4353 O OE1 B GLU A 1 311 ? -4.77700  68.48100  10.82900 0.300 86.34641  ? 641 GLU A OE1 1 
ATOM   4354 O OE2 A GLU A 1 311 ? -2.15700  69.34700  11.67100 0.700 88.70634  ? 641 GLU A OE2 1 
ATOM   4355 O OE2 B GLU A 1 311 ? -4.04500  69.86700  9.29300  0.300 80.33677  ? 641 GLU A OE2 1 
ATOM   4356 N N   A VAL A 1 312 ? -0.28800  65.23900  9.13400  0.700 85.05694  ? 642 VAL A N   1 
ATOM   4357 N N   B VAL A 1 312 ? 0.23100   65.38500  9.23900  0.300 80.94010  ? 642 VAL A N   1 
ATOM   4358 C CA  A VAL A 1 312 ? 1.01200   64.83100  9.66800  0.700 75.48708  ? 642 VAL A CA  1 
ATOM   4359 C CA  B VAL A 1 312 ? 1.55100   64.98500  9.70700  0.300 74.21244  ? 642 VAL A CA  1 
ATOM   4360 C C   A VAL A 1 312 ? 1.90400   66.06300  9.75600  0.700 76.10783  ? 642 VAL A C   1 
ATOM   4361 C C   B VAL A 1 312 ? 2.45400   66.20800  9.74500  0.300 74.88845  ? 642 VAL A C   1 
ATOM   4362 O O   A VAL A 1 312 ? 1.88300   66.93100  8.87400  0.700 86.92818  ? 642 VAL A O   1 
ATOM   4363 O O   B VAL A 1 312 ? 2.43900   67.03800  8.83000  0.300 79.80702  ? 642 VAL A O   1 
ATOM   4364 C CB  A VAL A 1 312 ? 1.69600   63.71400  8.83900  0.700 71.71071  ? 642 VAL A CB  1 
ATOM   4365 C CB  B VAL A 1 312 ? 2.14200   63.89000  8.79300  0.300 70.77628  ? 642 VAL A CB  1 
ATOM   4366 C CG1 A VAL A 1 312 ? 0.71000   62.60600  8.48000  0.700 85.08223  ? 642 VAL A CG1 1 
ATOM   4367 C CG1 B VAL A 1 312 ? 3.65200   63.90000  8.84200  0.300 66.62011  ? 642 VAL A CG1 1 
ATOM   4368 C CG2 A VAL A 1 312 ? 2.37300   64.26400  7.58600  0.700 72.38216  ? 642 VAL A CG2 1 
ATOM   4369 C CG2 B VAL A 1 312 ? 1.60600   62.52400  9.19200  0.300 73.04575  ? 642 VAL A CG2 1 
ATOM   4370 N N   A GLU A 1 313 ? 2.64100   66.16000  10.86200 0.700 76.21550  ? 643 GLU A N   1 
ATOM   4371 N N   B GLU A 1 313 ? 3.23900   66.31300  10.81600 0.300 72.57781  ? 643 GLU A N   1 
ATOM   4372 C CA  A GLU A 1 313 ? 3.59800   67.24100  11.06900 0.700 70.41820  ? 643 GLU A CA  1 
ATOM   4373 C CA  B GLU A 1 313 ? 4.22200   67.37700  10.99200 0.300 68.72556  ? 643 GLU A CA  1 
ATOM   4374 C C   A GLU A 1 313 ? 4.96800   66.75700  10.62400 0.700 63.45771  ? 643 GLU A C   1 
ATOM   4375 C C   B GLU A 1 313 ? 5.57700   66.86900  10.51200 0.300 64.25201  ? 643 GLU A C   1 
ATOM   4376 O O   A GLU A 1 313 ? 5.67500   66.04600  11.34500 0.700 68.88792  ? 643 GLU A O   1 
ATOM   4377 O O   B GLU A 1 313 ? 6.27400   66.14200  11.22400 0.300 65.39826  ? 643 GLU A O   1 
ATOM   4378 C CB  A GLU A 1 313 ? 3.59300   67.72100  12.51700 0.700 69.05179  ? 643 GLU A CB  1 
ATOM   4379 C CB  B GLU A 1 313 ? 4.28100   67.80600  12.45400 0.300 68.89171  ? 643 GLU A CB  1 
ATOM   4380 C CG  A GLU A 1 313 ? 3.22100   69.20300  12.67400 0.700 76.43990  ? 643 GLU A CG  1 
ATOM   4381 C CG  B GLU A 1 313 ? 3.10200   68.64400  12.91400 0.300 74.77427  ? 643 GLU A CG  1 
ATOM   4382 C CD  A GLU A 1 313 ? 3.25600   69.65300  14.11700 0.700 93.66010  ? 643 GLU A CD  1 
ATOM   4383 C CD  B GLU A 1 313 ? 3.23800   69.08700  14.35700 0.300 85.75207  ? 643 GLU A CD  1 
ATOM   4384 O OE1 A GLU A 1 313 ? 2.92000   68.82900  14.99000 0.700 85.42438  ? 643 GLU A OE1 1 
ATOM   4385 O OE1 B GLU A 1 313 ? 4.10000   68.53400  15.07200 0.300 75.41988  ? 643 GLU A OE1 1 
ATOM   4386 O OE2 A GLU A 1 313 ? 3.55300   70.84400  14.37500 0.700 99.23884  ? 643 GLU A OE2 1 
ATOM   4387 O OE2 B GLU A 1 313 ? 2.47900   69.98500  14.77900 0.300 94.46375  ? 643 GLU A OE2 1 
ATOM   4388 N N   A THR A 1 314 ? 5.33000   67.19100  9.42100  0.700 56.45627  ? 644 THR A N   1 
ATOM   4389 N N   B THR A 1 314 ? 5.94000   67.26100  9.29400  0.300 60.92534  ? 644 THR A N   1 
ATOM   4390 C CA  A THR A 1 314 ? 6.59700   66.88200  8.78900  0.700 58.43237  ? 644 THR A CA  1 
ATOM   4391 C CA  B THR A 1 314 ? 7.21500   66.88700  8.70200  0.300 60.44624  ? 644 THR A CA  1 
ATOM   4392 C C   A THR A 1 314 ? 7.74100   67.68400  9.40100  0.700 59.64179  ? 644 THR A C   1 
ATOM   4393 C C   B THR A 1 314 ? 8.34200   67.70600  9.31300  0.300 60.39223  ? 644 THR A C   1 
ATOM   4394 O O   A THR A 1 314 ? 7.61400   68.87900  9.69300  0.700 73.44810  ? 644 THR A O   1 
ATOM   4395 O O   B THR A 1 314 ? 8.21200   68.91600  9.51900  0.300 68.81855  ? 644 THR A O   1 
ATOM   4396 C CB  A THR A 1 314 ? 6.49000   67.14600  7.28100  0.700 65.18841  ? 644 THR A CB  1 
ATOM   4397 C CB  B THR A 1 314 ? 7.18600   67.09000  7.18600  0.300 62.06650  ? 644 THR A CB  1 
ATOM   4398 O OG1 A THR A 1 314 ? 5.32100   66.50500  6.74900  0.700 77.53816  ? 644 THR A OG1 1 
ATOM   4399 O OG1 B THR A 1 314 ? 6.03100   66.44400  6.64000  0.300 69.30206  ? 644 THR A OG1 1 
ATOM   4400 C CG2 A THR A 1 314 ? 7.78500   66.74100  6.52900  0.700 58.88228  ? 644 THR A CG2 1 
ATOM   4401 C CG2 B THR A 1 314 ? 8.43700   66.51100  6.53800  0.300 59.05007  ? 644 THR A CG2 1 
ATOM   4402 N N   A LEU A 1 315 ? 8.86700   66.99900  9.59900  0.700 52.92236  ? 645 LEU A N   1 
ATOM   4403 N N   B LEU A 1 315 ? 9.45600   67.03800  9.59600  0.300 56.27645  ? 645 LEU A N   1 
ATOM   4404 C CA  A LEU A 1 315 ? 10.12400  67.64500  9.96600  0.700 53.69117  ? 645 LEU A CA  1 
ATOM   4405 C CA  B LEU A 1 315 ? 10.67800  67.73200  9.96800  0.300 58.74242  ? 645 LEU A CA  1 
ATOM   4406 C C   A LEU A 1 315 ? 10.77900  68.27700  8.74800  0.700 60.17955  ? 645 LEU A C   1 
ATOM   4407 C C   B LEU A 1 315 ? 11.35400  68.28600  8.72100  0.300 63.43321  ? 645 LEU A C   1 
ATOM   4408 O O   A LEU A 1 315 ? 10.88000  67.65800  7.68400  0.700 66.09028  ? 645 LEU A O   1 
ATOM   4409 O O   B LEU A 1 315 ? 11.50800  67.58200  7.71900  0.300 65.38744  ? 645 LEU A O   1 
ATOM   4410 C CB  A LEU A 1 315 ? 11.07700  66.65000  10.63400 0.700 58.26742  ? 645 LEU A CB  1 
ATOM   4411 C CB  B LEU A 1 315 ? 11.62300  66.78800  10.70900 0.300 59.92690  ? 645 LEU A CB  1 
ATOM   4412 C CG  A LEU A 1 315 ? 10.67700  66.18200  12.03800 0.700 73.55393  ? 645 LEU A CG  1 
ATOM   4413 C CG  B LEU A 1 315 ? 11.18400  66.37700  12.11500 0.300 69.31393  ? 645 LEU A CG  1 
ATOM   4414 C CD1 A LEU A 1 315 ? 11.26700  64.81800  12.33300 0.700 67.91515  ? 645 LEU A CD1 1 
ATOM   4415 C CD1 B LEU A 1 315 ? 11.77600  65.02700  12.48700 0.300 65.22865  ? 645 LEU A CD1 1 
ATOM   4416 C CD2 A LEU A 1 315 ? 11.13900  67.19800  13.07500 0.700 73.80795  ? 645 LEU A CD2 1 
ATOM   4417 C CD2 B LEU A 1 315 ? 11.57800  67.44000  13.12500 0.300 69.55755  ? 645 LEU A CD2 1 
ATOM   4418 N N   A VAL A 1 316 ? 11.22600  69.51800  8.92200  0.700 74.90406  ? 646 VAL A N   1 
ATOM   4419 N N   B VAL A 1 316 ? 11.75400  69.55400  8.79100  0.300 71.09010  ? 646 VAL A N   1 
ATOM   4420 C CA  A VAL A 1 316 ? 11.86500  70.28100  7.86200  0.700 66.73359  ? 646 VAL A CA  1 
ATOM   4421 C CA  B VAL A 1 316 ? 12.41500  70.22900  7.68100  0.300 67.04102  ? 646 VAL A CA  1 
ATOM   4422 C C   A VAL A 1 316 ? 13.24600  70.68400  8.35100  0.700 65.57727  ? 646 VAL A C   1 
ATOM   4423 C C   B VAL A 1 316 ? 13.75300  70.77600  8.15900  0.300 68.96585  ? 646 VAL A C   1 
ATOM   4424 O O   A VAL A 1 316 ? 13.61900  70.41800  9.50200  0.700 68.11828  ? 646 VAL A O   1 
ATOM   4425 O O   B VAL A 1 316 ? 14.08600  70.68500  9.34600  0.300 69.84215  ? 646 VAL A O   1 
ATOM   4426 C CB  A VAL A 1 316 ? 11.04000  71.52500  7.46800  0.700 71.42183  ? 646 VAL A CB  1 
ATOM   4427 C CB  B VAL A 1 316 ? 11.53100  71.35000  7.10400  0.300 70.06670  ? 646 VAL A CB  1 
ATOM   4428 C CG1 A VAL A 1 316 ? 9.72900   71.12600  6.81500  0.700 66.20452  ? 646 VAL A CG1 1 
ATOM   4429 C CG1 B VAL A 1 316 ? 10.30200  70.76100  6.42900  0.300 64.98478  ? 646 VAL A CG1 1 
ATOM   4430 C CG2 A VAL A 1 316 ? 10.78000  72.40600  8.68200  0.700 66.92634  ? 646 VAL A CG2 1 
ATOM   4431 C CG2 B VAL A 1 316 ? 11.12700  72.32100  8.20200  0.300 70.79876  ? 646 VAL A CG2 1 
ATOM   4432 N N   A GLU A 1 317 ? 14.01700  71.31600  7.47100  0.700 71.60121  ? 647 GLU A N   1 
ATOM   4433 N N   B GLU A 1 317 ? 14.52600  71.34900  7.23900  0.300 73.69156  ? 647 GLU A N   1 
ATOM   4434 C CA  A GLU A 1 317 ? 15.41100  71.60800  7.75700  0.700 73.68342  ? 647 GLU A CA  1 
ATOM   4435 C CA  B GLU A 1 317 ? 15.88200  71.78900  7.53800  0.300 74.71413  ? 647 GLU A CA  1 
ATOM   4436 C C   A GLU A 1 317 ? 15.67900  73.04100  8.19200  0.700 88.57221  ? 647 GLU A C   1 
ATOM   4437 C C   B GLU A 1 317 ? 16.00500  73.28500  7.78400  0.300 84.83120  ? 647 GLU A C   1 
ATOM   4438 O O   A GLU A 1 317 ? 16.61900  73.27300  8.96000  0.700 91.67669  ? 647 GLU A O   1 
ATOM   4439 O O   B GLU A 1 317 ? 16.89600  73.70100  8.53200  0.300 86.77707  ? 647 GLU A O   1 
ATOM   4440 C CB  A GLU A 1 317 ? 16.21200  71.32600  6.48400  0.700 76.21474  ? 647 GLU A CB  1 
ATOM   4441 C CB  B GLU A 1 317 ? 16.82700  71.38900  6.39900  0.300 74.51806  ? 647 GLU A CB  1 
ATOM   4442 C CG  A GLU A 1 317 ? 16.45600  69.85400  6.21600  0.700 76.57791  ? 647 GLU A CG  1 
ATOM   4443 C CG  B GLU A 1 317 ? 16.17800  71.39700  5.02500  0.300 75.53261  ? 647 GLU A CG  1 
ATOM   4444 C CD  A GLU A 1 317 ? 17.21300  69.62800  4.92300  0.700 75.52737  ? 647 GLU A CD  1 
ATOM   4445 C CD  B GLU A 1 317 ? 17.14800  71.02600  3.92100  0.300 76.89420  ? 647 GLU A CD  1 
ATOM   4446 O OE1 A GLU A 1 317 ? 18.10500  70.43800  4.60500  0.700 82.71638  ? 647 GLU A OE1 1 
ATOM   4447 O OE1 B GLU A 1 317 ? 17.89600  71.91400  3.46100  0.300 69.23817  ? 647 GLU A OE1 1 
ATOM   4448 O OE2 A GLU A 1 317 ? 16.89800  68.64500  4.21400  0.700 71.33071  ? 647 GLU A OE2 1 
ATOM   4449 O OE2 B GLU A 1 317 ? 17.16200  69.84500  3.51200  0.300 77.33600  ? 647 GLU A OE2 1 
ATOM   4450 N N   A ASP A 1 318 ? 14.88500  74.00400  7.73200  0.700 85.37545  ? 648 ASP A N   1 
ATOM   4451 N N   B ASP A 1 318 ? 15.14700  74.10800  7.18600  0.300 83.27697  ? 648 ASP A N   1 
ATOM   4452 C CA  A ASP A 1 318 ? 15.13500  75.40700  8.02500  0.700 94.17743  ? 648 ASP A CA  1 
ATOM   4453 C CA  B ASP A 1 318 ? 15.28600  75.55100  7.30900  0.300 90.87651  ? 648 ASP A CA  1 
ATOM   4454 C C   A ASP A 1 318 ? 13.81600  76.10700  8.31600  0.700 93.62459  ? 648 ASP A C   1 
ATOM   4455 C C   B ASP A 1 318 ? 13.91600  76.18200  7.51400  0.300 91.82253  ? 648 ASP A C   1 
ATOM   4456 O O   A ASP A 1 318 ? 12.73800  75.61400  7.97400  0.700 89.87450  ? 648 ASP A O   1 
ATOM   4457 O O   B ASP A 1 318 ? 12.87800  75.57900  7.23100  0.300 89.05645  ? 648 ASP A O   1 
ATOM   4458 C CB  A ASP A 1 318 ? 15.88700  76.09600  6.88000  0.700 94.50188  ? 648 ASP A CB  1 
ATOM   4459 C CB  B ASP A 1 318 ? 15.97100  76.14700  6.06800  0.300 88.32244  ? 648 ASP A CB  1 
ATOM   4460 C CG  A ASP A 1 318 ? 15.06900  76.18000  5.61500  0.700 92.63984  ? 648 ASP A CG  1 
ATOM   4461 C CG  B ASP A 1 318 ? 16.50100  77.55200  6.30200  0.300 86.46073  ? 648 ASP A CG  1 
ATOM   4462 O OD1 A ASP A 1 318 ? 14.35600  75.20100  5.30800  0.700 90.58406  ? 648 ASP A OD1 1 
ATOM   4463 O OD1 B ASP A 1 318 ? 15.82500  78.35100  6.98300  0.300 90.42375  ? 648 ASP A OD1 1 
ATOM   4464 O OD2 A ASP A 1 318 ? 15.14800  77.21700  4.92300  0.700 70.49903  ? 648 ASP A OD2 1 
ATOM   4465 O OD2 B ASP A 1 318 ? 17.60200  77.85600  5.80000  0.300 81.55707  ? 648 ASP A OD2 1 
ATOM   4466 N N   A GLU A 1 319 ? 13.91300  77.27300  8.95400  0.700 88.81833  ? 649 GLU A N   1 
ATOM   4467 N N   B GLU A 1 319 ? 13.93300  77.41800  8.01800  0.300 89.39905  ? 649 GLU A N   1 
ATOM   4468 C CA  A GLU A 1 319 ? 12.72600  77.98000  9.41400  0.700 89.04382  ? 649 GLU A CA  1 
ATOM   4469 C CA  B GLU A 1 319 ? 12.71800  78.11900  8.40900  0.300 91.61086  ? 649 GLU A CA  1 
ATOM   4470 C C   A GLU A 1 319 ? 11.97600  78.67000  8.28200  0.700 96.54368  ? 649 GLU A C   1 
ATOM   4471 C C   B GLU A 1 319 ? 11.92700  78.65000  7.22200  0.300 95.91950  ? 649 GLU A C   1 
ATOM   4472 O O   A GLU A 1 319 ? 10.88500  79.20000  8.51900  0.700 93.67519  ? 649 GLU A O   1 
ATOM   4473 O O   B GLU A 1 319 ? 10.81800  79.16000  7.41900  0.300 93.93698  ? 649 GLU A O   1 
ATOM   4474 C CB  A GLU A 1 319 ? 13.10300  79.00600  10.48600 0.700 77.11564  ? 649 GLU A CB  1 
ATOM   4475 C CB  B GLU A 1 319 ? 13.06000  79.27500  9.35400  0.300 84.88864  ? 649 GLU A CB  1 
ATOM   4476 N N   A ALA A 1 320 ? 12.52800  78.67600  7.06300  0.700 98.96419  ? 650 ALA A N   1 
ATOM   4477 N N   B ALA A 1 320 ? 12.46300  78.54900  6.00300  0.300 93.68049  ? 650 ALA A N   1 
ATOM   4478 C CA  A ALA A 1 320 ? 11.80200  79.17600  5.90000  0.700 99.92462  ? 650 ALA A CA  1 
ATOM   4479 C CA  B ALA A 1 320 ? 11.69700  78.89700  4.81200  0.300 92.00166  ? 650 ALA A CA  1 
ATOM   4480 C C   A ALA A 1 320 ? 10.54500  78.37100  5.60300  0.700 95.68434  ? 650 ALA A C   1 
ATOM   4481 C C   B ALA A 1 320 ? 10.46700  78.02100  4.61600  0.300 91.03732  ? 650 ALA A C   1 
ATOM   4482 O O   A ALA A 1 320 ? 9.74700   78.78600  4.75500  0.700 96.39973  ? 650 ALA A O   1 
ATOM   4483 O O   B ALA A 1 320 ? 9.64400   78.32900  3.74700  0.300 92.82622  ? 650 ALA A O   1 
ATOM   4484 C CB  A ALA A 1 320 ? 12.70900  79.18400  4.66900  0.700 93.49134  ? 650 ALA A CB  1 
ATOM   4485 C CB  B ALA A 1 320 ? 12.59200  78.81400  3.57300  0.300 89.07862  ? 650 ALA A CB  1 
ATOM   4486 N N   A GLU A 1 321 ? 10.35800  77.23500  6.26800  0.700 96.52643  ? 651 GLU A N   1 
ATOM   4487 N N   B GLU A 1 321 ? 10.32000  76.94500  5.38700  0.300 90.36805  ? 651 GLU A N   1 
ATOM   4488 C CA  A GLU A 1 321 ? 9.15100   76.43000  6.15900  0.700 97.29178  ? 651 GLU A CA  1 
ATOM   4489 C CA  B GLU A 1 321 ? 9.13100   76.10500  5.34800  0.300 92.87537  ? 651 GLU A CA  1 
ATOM   4490 C C   A GLU A 1 321 ? 8.59600   76.29900  7.57000  0.700 97.98863  ? 651 GLU A C   1 
ATOM   4491 C C   B GLU A 1 321 ? 8.52600   76.04100  6.74300  0.300 95.24085  ? 651 GLU A C   1 
ATOM   4492 O O   A GLU A 1 321 ? 9.26900   75.76700  8.45900  0.700 98.12306  ? 651 GLU A O   1 
ATOM   4493 O O   B GLU A 1 321 ? 9.18100   75.57800  7.68400  0.300 95.92128  ? 651 GLU A O   1 
ATOM   4494 C CB  A GLU A 1 321 ? 9.44900   75.06800  5.52800  0.700 94.90266  ? 651 GLU A CB  1 
ATOM   4495 C CB  B GLU A 1 321 ? 9.46900   74.69700  4.84900  0.300 92.55934  ? 651 GLU A CB  1 
ATOM   4496 C CG  A GLU A 1 321 ? 9.51700   75.11300  4.00100  0.700 95.47477  ? 651 GLU A CG  1 
ATOM   4497 C CG  B GLU A 1 321 ? 10.61900  74.63500  3.85200  0.300 88.46008  ? 651 GLU A CG  1 
ATOM   4498 C CD  A GLU A 1 321 ? 8.46600   74.25100  3.32500  0.700 99.45480  ? 651 GLU A CD  1 
ATOM   4499 C CD  B GLU A 1 321 ? 10.30000  75.31900  2.53600  0.300 81.16619  ? 651 GLU A CD  1 
ATOM   4500 O OE1 A GLU A 1 321 ? 7.28900   74.30900  3.73800  0.700 99.66813  ? 651 GLU A OE1 1 
ATOM   4501 O OE1 B GLU A 1 321 ? 9.10400   75.43800  2.19800  0.300 82.38453  ? 651 GLU A OE1 1 
ATOM   4502 O OE2 A GLU A 1 321 ? 8.81900   73.52200  2.37300  0.700 76.54275  ? 651 GLU A OE2 1 
ATOM   4503 O OE2 B GLU A 1 321 ? 11.24900  75.73600  1.83900  0.300 76.56625  ? 651 GLU A OE2 1 
ATOM   4504 N N   A ALA A 1 322 ? 7.37200   76.78400  7.77000  0.700 97.57018  ? 652 ALA A N   1 
ATOM   4505 N N   B ALA A 1 322 ? 7.28200   76.50100  6.87400  0.300 95.57111  ? 652 ALA A N   1 
ATOM   4506 C CA  A ALA A 1 322 ? 6.58900   76.49900  8.96600  0.700 96.98986  ? 652 ALA A CA  1 
ATOM   4507 C CA  B ALA A 1 322 ? 6.48700   76.21500  8.06300  0.300 93.81524  ? 652 ALA A CA  1 
ATOM   4508 C C   A ALA A 1 322 ? 5.11100   76.65100  8.64400  0.700 100.52566 ? 652 ALA A C   1 
ATOM   4509 C C   B ALA A 1 322 ? 5.00300   76.31100  7.73900  0.300 97.01843  ? 652 ALA A C   1 
ATOM   4510 O O   A ALA A 1 322 ? 4.29800   76.98200  9.51300  0.700 97.97282  ? 652 ALA A O   1 
ATOM   4511 O O   B ALA A 1 322 ? 4.18400   76.61400  8.61300  0.300 98.92006  ? 652 ALA A O   1 
ATOM   4512 C CB  A ALA A 1 322 ? 6.99400   77.42200  10.11700 0.700 102.85086 ? 652 ALA A CB  1 
ATOM   4513 C CB  B ALA A 1 322 ? 6.84900   77.17300  9.20000  0.300 98.31521  ? 652 ALA A CB  1 
ATOM   4514 N N   A GLY A 1 323 ? 4.77100   76.40100  7.39000  0.700 99.52912  ? 653 GLY A N   1 
ATOM   4515 N N   B GLY A 1 323 ? 4.65400   76.05900  6.48200  0.300 92.61808  ? 653 GLY A N   1 
ATOM   4516 C CA  A GLY A 1 323 ? 3.49600   76.77000  6.82000  0.700 101.40794 ? 653 GLY A CA  1 
ATOM   4517 C CA  B GLY A 1 323 ? 3.33800   76.39400  5.97800  0.300 93.38554  ? 653 GLY A CA  1 
ATOM   4518 C C   A GLY A 1 323 ? 2.48100   75.66000  6.96900  0.700 101.71398 ? 653 GLY A C   1 
ATOM   4519 C C   B GLY A 1 323 ? 2.35100   75.24700  6.09600  0.300 90.56512  ? 653 GLY A C   1 
ATOM   4520 O O   A GLY A 1 323 ? 2.58000   74.80000  7.84800  0.700 98.26820  ? 653 GLY A O   1 
ATOM   4521 O O   B GLY A 1 323 ? 2.72900   74.07900  6.12800  0.300 78.10853  ? 653 GLY A O   1 
ATOM   4522 N N   A ALA A 1 324 ? 1.49300   75.67600  6.08000  0.700 97.73987  ? 654 ALA A N   1 
ATOM   4523 N N   B ALA A 1 324 ? 1.06700   75.59500  6.16600  0.300 95.78944  ? 654 ALA A N   1 
ATOM   4524 C CA  A ALA A 1 324 ? 0.41100   74.69600  6.07700  0.700 90.63214  ? 654 ALA A CA  1 
ATOM   4525 C CA  B ALA A 1 324 ? 0.00900   74.59200  6.27400  0.300 89.57722  ? 654 ALA A CA  1 
ATOM   4526 C C   A ALA A 1 324 ? 0.35500   74.22300  4.63400  0.700 96.54056  ? 654 ALA A C   1 
ATOM   4527 C C   B ALA A 1 324 ? -0.13000  74.00500  4.87800  0.300 94.38689  ? 654 ALA A C   1 
ATOM   4528 O O   A ALA A 1 324 ? -0.33900  74.78600  3.78400  0.700 103.30281 ? 654 ALA A O   1 
ATOM   4529 O O   B ALA A 1 324 ? -0.88600  74.49900  4.04000  0.300 98.71130  ? 654 ALA A O   1 
ATOM   4530 C CB  A ALA A 1 324 ? -0.91100  75.29300  6.54900  0.700 87.01301  ? 654 ALA A CB  1 
ATOM   4531 C CB  B ALA A 1 324 ? -1.29100  75.21100  6.77200  0.300 85.37270  ? 654 ALA A CB  1 
ATOM   4532 N N   A VAL A 1 325 ? 1.11200   73.15900  4.39400  0.700 93.85778  ? 655 VAL A N   1 
ATOM   4533 N N   B VAL A 1 325 ? 0.61300   72.93500  4.62100  0.300 93.12931  ? 655 VAL A N   1 
ATOM   4534 C CA  A VAL A 1 325 ? 1.22000   72.49100  3.11700  0.700 102.94596 ? 655 VAL A CA  1 
ATOM   4535 C CA  B VAL A 1 325 ? 0.56800   72.26200  3.33900  0.300 99.78665  ? 655 VAL A CA  1 
ATOM   4536 C C   A VAL A 1 325 ? 0.25600   71.31200  3.10400  0.700 103.35163 ? 655 VAL A C   1 
ATOM   4537 C C   B VAL A 1 325 ? -0.37800  71.06500  3.36800  0.300 99.34655  ? 655 VAL A C   1 
ATOM   4538 O O   A VAL A 1 325 ? -0.18600  70.82700  4.14700  0.700 101.05270 ? 655 VAL A O   1 
ATOM   4539 O O   B VAL A 1 325 ? -0.68100  70.49600  4.41900  0.300 94.55116  ? 655 VAL A O   1 
ATOM   4540 C CB  A VAL A 1 325 ? 2.69100   72.05100  2.90700  0.700 91.79736  ? 655 VAL A CB  1 
ATOM   4541 C CB  B VAL A 1 325 ? 2.01100   71.83700  2.96800  0.300 94.30028  ? 655 VAL A CB  1 
ATOM   4542 C CG1 A VAL A 1 325 ? 2.91500   71.46700  1.55400  0.700 83.96843  ? 655 VAL A CG1 1 
ATOM   4543 C CG1 B VAL A 1 325 ? 2.08100   71.25300  1.60200  0.300 91.68162  ? 655 VAL A CG1 1 
ATOM   4544 C CG2 A VAL A 1 325 ? 3.62000   73.23900  3.11700  0.700 89.26157  ? 655 VAL A CG2 1 
ATOM   4545 C CG2 B VAL A 1 325 ? 2.95500   73.02600  3.08100  0.300 90.26067  ? 655 VAL A CG2 1 
ATOM   4546 N N   A SER A 1 326 ? -0.13300  70.87900  1.90500  0.700 102.63446 ? 656 SER A N   1 
ATOM   4547 N N   B SER A 1 326 ? -0.87600  70.69900  2.18400  0.300 101.94771 ? 656 SER A N   1 
ATOM   4548 C CA  A SER A 1 326 ? -0.95300  69.67800  1.78200  0.700 107.88862 ? 656 SER A CA  1 
ATOM   4549 C CA  B SER A 1 326 ? -1.67900  69.50100  1.96000  0.300 103.16522 ? 656 SER A CA  1 
ATOM   4550 C C   A SER A 1 326 ? -0.46600  68.73000  0.69300  0.700 109.28332 ? 656 SER A C   1 
ATOM   4551 C C   B SER A 1 326 ? -1.17200  68.81100  0.70200  0.300 104.16447 ? 656 SER A C   1 
ATOM   4552 O O   A SER A 1 326 ? 0.58000   68.96200  0.08100  0.700 111.45908 ? 656 SER A O   1 
ATOM   4553 O O   B SER A 1 326 ? -1.09200  69.45000  -0.35100 0.300 101.30519 ? 656 SER A O   1 
ATOM   4554 C CB  A SER A 1 326 ? -2.39800  70.07400  1.50300  0.700 103.62069 ? 656 SER A CB  1 
ATOM   4555 C CB  B SER A 1 326 ? -3.16600  69.83600  1.81900  0.300 99.23661  ? 656 SER A CB  1 
ATOM   4556 O OG  A SER A 1 326 ? -2.79900  71.15800  2.32000  0.700 102.29719 ? 656 SER A OG  1 
ATOM   4557 O OG  B SER A 1 326 ? -3.34700  71.08200  1.17800  0.300 95.41040  ? 656 SER A OG  1 
ATOM   4558 N N   A SER A 1 327 ? -1.22600  67.65900  0.44900  0.700 104.89372 ? 657 SER A N   1 
ATOM   4559 N N   B SER A 1 327 ? -0.82900  67.52700  0.78800  0.300 102.17542 ? 657 SER A N   1 
ATOM   4560 C CA  A SER A 1 327 ? -0.89600  66.69300  -0.59400 0.700 102.66154 ? 657 SER A CA  1 
ATOM   4561 C CA  B SER A 1 327 ? -0.36300  66.79300  -0.38700 0.300 99.85623  ? 657 SER A CA  1 
ATOM   4562 C C   A SER A 1 327 ? -2.06200  65.74700  -0.86400 0.700 104.20499 ? 657 SER A C   1 
ATOM   4563 C C   B SER A 1 327 ? -1.42700  65.78800  -0.82000 0.300 100.69498 ? 657 SER A C   1 
ATOM   4564 O O   A SER A 1 327 ? -2.43400  64.94100  -0.00500 0.700 99.82347  ? 657 SER A O   1 
ATOM   4565 O O   B SER A 1 327 ? -1.71700  64.83000  -0.09400 0.300 98.86398  ? 657 SER A O   1 
ATOM   4566 C CB  A SER A 1 327 ? 0.34600   65.88500  -0.21000 0.700 99.48750  ? 657 SER A CB  1 
ATOM   4567 C CB  B SER A 1 327 ? 0.96500   66.09600  -0.10200 0.300 95.46751  ? 657 SER A CB  1 
ATOM   4568 O OG  A SER A 1 327 ? 1.53000   66.51500  -0.66700 0.700 86.22622  ? 657 SER A OG  1 
ATOM   4569 O OG  B SER A 1 327 ? 0.82500   65.12800  0.92200  0.300 94.62165  ? 657 SER A OG  1 
ATOM   4570 N N   A GLU A 1 328 ? -2.63500  65.84100  -2.06200 0.700 97.42063  ? 658 GLU A N   1 
ATOM   4571 N N   B GLU A 1 328 ? -2.00400  66.00800  -2.00200 0.300 96.27612  ? 658 GLU A N   1 
ATOM   4572 C CA  A GLU A 1 328 ? -3.75400  64.99600  -2.46100 0.700 90.36597  ? 658 GLU A CA  1 
ATOM   4573 C CA  B GLU A 1 328 ? -3.02800  65.12000  -2.54200 0.300 91.73780  ? 658 GLU A CA  1 
ATOM   4574 C C   A GLU A 1 328 ? -3.26100  63.62400  -2.90600 0.700 94.23004  ? 658 GLU A C   1 
ATOM   4575 C C   B GLU A 1 328 ? -2.39000  63.89000  -3.17600 0.300 91.23203  ? 658 GLU A C   1 
ATOM   4576 O O   A GLU A 1 328 ? -2.31400  63.52100  -3.69300 0.700 91.81899  ? 658 GLU A O   1 
ATOM   4577 O O   B GLU A 1 328 ? -1.44300  64.00800  -3.96100 0.300 85.50493  ? 658 GLU A O   1 
ATOM   4578 C CB  A GLU A 1 328 ? -4.57400  65.66800  -3.56400 0.700 86.86152  ? 658 GLU A CB  1 
ATOM   4579 C CB  B GLU A 1 328 ? -3.90800  65.84600  -3.56200 0.300 88.44450  ? 658 GLU A CB  1 
ATOM   4580 C CG  A GLU A 1 328 ? -5.42200  66.86500  -3.10200 0.700 91.51976  ? 658 GLU A CG  1 
ATOM   4581 C CG  B GLU A 1 328 ? -4.88100  66.87400  -2.97900 0.300 92.91051  ? 658 GLU A CG  1 
ATOM   4582 C CD  A GLU A 1 328 ? -4.62400  68.12300  -2.79500 0.700 103.50366 ? 658 GLU A CD  1 
ATOM   4583 C CD  B GLU A 1 328 ? -4.22600  68.15700  -2.50100 0.300 101.36347 ? 658 GLU A CD  1 
ATOM   4584 O OE1 A GLU A 1 328 ? -3.65800  68.06000  -2.00600 0.700 106.43834 ? 658 GLU A OE1 1 
ATOM   4585 O OE1 B GLU A 1 328 ? -3.02100  68.15200  -2.17300 0.300 101.61589 ? 658 GLU A OE1 1 
ATOM   4586 O OE2 A GLU A 1 328 ? -4.98300  69.19300  -3.33100 0.700 104.36238 ? 658 GLU A OE2 1 
ATOM   4587 O OE2 B GLU A 1 328 ? -4.93200  69.18600  -2.44500 0.300 98.67610  ? 658 GLU A OE2 1 
ATOM   4588 N N   A ASP A 1 329 ? -3.90000  62.57400  -2.39900 0.700 106.23458 ? 659 ASP A N   1 
ATOM   4589 N N   B ASP A 1 329 ? -2.91000  62.71400  -2.84200 0.300 96.56976  ? 659 ASP A N   1 
ATOM   4590 C CA  A ASP A 1 329 ? -3.52100  61.20500  -2.73600 0.700 97.28885  ? 659 ASP A CA  1 
ATOM   4591 C CA  B ASP A 1 329 ? -2.37600  61.46800  -3.38300 0.300 87.95659  ? 659 ASP A CA  1 
ATOM   4592 C C   A ASP A 1 329 ? -4.43900  60.63400  -3.81200 0.700 95.91481  ? 659 ASP A C   1 
ATOM   4593 C C   B ASP A 1 329 ? -3.43100  60.36500  -3.35800 0.300 89.84281  ? 659 ASP A C   1 
ATOM   4594 O O   A ASP A 1 329 ? -4.07600  60.57800  -4.98700 0.700 85.23827  ? 659 ASP A O   1 
ATOM   4595 O O   B ASP A 1 329 ? -4.18300  60.19000  -4.31700 0.300 91.12332  ? 659 ASP A O   1 
ATOM   4596 C CB  A ASP A 1 329 ? -3.56400  60.31200  -1.49500 0.700 91.10110  ? 659 ASP A CB  1 
ATOM   4597 C CB  B ASP A 1 329 ? -1.13300  61.02900  -2.60600 0.300 74.16813  ? 659 ASP A CB  1 
ATOM   4598 C CG  A ASP A 1 329 ? -2.70300  60.83800  -0.36800 0.700 103.13155 ? 659 ASP A CG  1 
ATOM   4599 C CG  B ASP A 1 329 ? -1.42000  60.77000  -1.14200 0.300 91.93792  ? 659 ASP A CG  1 
ATOM   4600 O OD1 A ASP A 1 329 ? -1.69800  61.52300  -0.65600 0.700 104.79597 ? 659 ASP A OD1 1 
ATOM   4601 O OD1 B ASP A 1 329 ? -1.89200  59.66200  -0.81300 0.300 93.95349  ? 659 ASP A OD1 1 
ATOM   4602 O OD2 A ASP A 1 329 ? -3.03600  60.57200  0.80700  0.700 92.20321  ? 659 ASP A OD2 1 
ATOM   4603 O OD2 B ASP A 1 329 ? -1.17400  61.67600  -0.31800 0.300 97.75829  ? 659 ASP A OD2 1 
HETATM 4604 C C18 . OLC B 2 .   ? -1.77100  38.52200  5.87900  1.000 57.43487  ? 701 OLC A C18 1 
HETATM 4605 C C10 . OLC B 2 .   ? -3.30000  33.31400  2.81100  1.000 78.01430  ? 701 OLC A C10 1 
HETATM 4606 C C9  . OLC B 2 .   ? -4.25400  32.80800  2.01000  1.000 78.74286  ? 701 OLC A C9  1 
HETATM 4607 C C17 . OLC B 2 .   ? -2.62400  39.68200  5.32100  1.000 62.86772  ? 701 OLC A C17 1 
HETATM 4608 C C11 . OLC B 2 .   ? -2.05600  33.78800  2.01700  1.000 71.82486  ? 701 OLC A C11 1 
HETATM 4609 C C8  . OLC B 2 .   ? -5.64500  32.16300  1.74700  1.000 76.28633  ? 701 OLC A C8  1 
HETATM 4610 C C24 . OLC B 2 .   ? -5.62200  20.80700  6.36900  1.000 182.55800 ? 701 OLC A C24 1 
HETATM 4611 C C16 . OLC B 2 .   ? -2.76800  39.52900  3.78500  1.000 79.14417  ? 701 OLC A C16 1 
HETATM 4612 C C12 . OLC B 2 .   ? -1.44000  35.04000  2.70600  1.000 72.38346  ? 701 OLC A C12 1 
HETATM 4613 C C7  . OLC B 2 .   ? -6.19300  31.52700  3.05100  1.000 72.21657  ? 701 OLC A C7  1 
HETATM 4614 C C15 . OLC B 2 .   ? -3.55500  38.23400  3.45500  1.000 76.62653  ? 701 OLC A C15 1 
HETATM 4615 C C13 . OLC B 2 .   ? -2.57800  35.90200  3.32200  1.000 78.42802  ? 701 OLC A C13 1 
HETATM 4616 C C6  . OLC B 2 .   ? -6.14100  29.97500  2.94400  1.000 83.58781  ? 701 OLC A C6  1 
HETATM 4617 C C14 . OLC B 2 .   ? -2.67300  37.27900  2.60400  1.000 86.04359  ? 701 OLC A C14 1 
HETATM 4618 C C5  . OLC B 2 .   ? -7.16700  29.35500  3.93500  1.000 68.04621  ? 701 OLC A C5  1 
HETATM 4619 C C4  . OLC B 2 .   ? -6.96200  27.81400  4.00100  1.000 56.80006  ? 701 OLC A C4  1 
HETATM 4620 C C3  . OLC B 2 .   ? -6.25100  27.45800  5.33600  1.000 82.26025  ? 701 OLC A C3  1 
HETATM 4621 C C2  . OLC B 2 .   ? -6.88100  26.17500  5.94000  1.000 93.23832  ? 701 OLC A C2  1 
HETATM 4622 C C21 . OLC B 2 .   ? -6.42700  23.06200  7.14400  1.000 118.78444 ? 701 OLC A C21 1 
HETATM 4623 C C1  . OLC B 2 .   ? -5.75500  25.21100  6.38400  1.000 113.31532 ? 701 OLC A C1  1 
HETATM 4624 C C22 . OLC B 2 .   ? -6.85700  21.67700  6.63500  1.000 144.52798 ? 701 OLC A C22 1 
HETATM 4625 O O19 . OLC B 2 .   ? -4.80600  25.63600  6.96500  1.000 86.77769  ? 701 OLC A O19 1 
HETATM 4626 O O25 . OLC B 2 .   ? -5.90200  19.88100  5.34100  1.000 199.42876 ? 701 OLC A O25 1 
HETATM 4627 O O23 . OLC B 2 .   ? -7.66000  21.06100  7.60000  1.000 95.87096  ? 701 OLC A O23 1 
HETATM 4628 O O20 . OLC B 2 .   ? -5.85500  23.82600  6.09800  1.000 154.10672 ? 701 OLC A O20 1 
HETATM 4629 C C10 . OLC C 2 .   ? -19.96800 36.72400  19.42200 1.000 90.73813  ? 702 OLC A C10 1 
HETATM 4630 C C9  . OLC C 2 .   ? -19.93900 38.03200  19.11200 1.000 79.48034  ? 702 OLC A C9  1 
HETATM 4631 C C11 . OLC C 2 .   ? -21.34800 36.07800  19.14100 1.000 94.83515  ? 702 OLC A C11 1 
HETATM 4632 C C8  . OLC C 2 .   ? -20.57900 39.34700  18.58300 1.000 97.23860  ? 702 OLC A C8  1 
HETATM 4633 C C12 . OLC C 2 .   ? -22.37600 36.56500  20.20300 1.000 98.75720  ? 702 OLC A C12 1 
HETATM 4634 C C7  . OLC C 2 .   ? -19.46500 40.31300  18.09700 1.000 97.15157  ? 702 OLC A C7  1 
HETATM 4635 C C13 . OLC C 2 .   ? -23.81400 36.47500  19.61700 1.000 98.84439  ? 702 OLC A C13 1 
HETATM 4636 C C6  . OLC C 2 .   ? -19.86000 40.94300  16.72900 1.000 88.96698  ? 702 OLC A C6  1 
HETATM 4637 C C14 . OLC C 2 .   ? -24.73800 37.50300  20.33200 1.000 80.28974  ? 702 OLC A C14 1 
HETATM 4638 C C5  . OLC C 2 .   ? -18.85100 40.49500  15.63200 1.000 85.78414  ? 702 OLC A C5  1 
HETATM 4639 C C4  . OLC C 2 .   ? -19.28400 39.11600  15.05300 1.000 46.73148  ? 702 OLC A C4  1 
HETATM 4640 C C3  . OLC C 2 .   ? -18.30000 38.01800  15.54300 1.000 78.20778  ? 702 OLC A C3  1 
HETATM 4641 C C2  . OLC C 2 .   ? -19.05100 36.66600  15.67100 1.000 98.63698  ? 702 OLC A C2  1 
HETATM 4642 C C1  . OLC C 2 .   ? -18.03100 35.50200  15.67900 1.000 112.28530 ? 702 OLC A C1  1 
HETATM 4643 O O19 . OLC C 2 .   ? -18.39500 34.39400  15.91500 1.000 88.95393  ? 702 OLC A O19 1 
HETATM 4644 O O20 . OLC C 2 .   ? -16.66400 35.75200  15.40800 1.000 106.82843 ? 702 OLC A O20 1 
HETATM 4645 C C24 . OLC D 2 .   ? 24.71900  16.39400  0.14400  1.000 96.38856  ? 703 OLC A C24 1 
HETATM 4646 C C7  . OLC D 2 .   ? 22.79900  19.33000  1.21000  1.000 76.85440  ? 703 OLC A C7  1 
HETATM 4647 C C6  . OLC D 2 .   ? 22.73900  19.90200  -0.23600 1.000 81.05251  ? 703 OLC A C6  1 
HETATM 4648 C C5  . OLC D 2 .   ? 21.32400  20.48700  -0.51000 1.000 97.77831  ? 703 OLC A C5  1 
HETATM 4649 C C4  . OLC D 2 .   ? 20.50000  19.49700  -1.38300 1.000 103.94540 ? 703 OLC A C4  1 
HETATM 4650 C C3  . OLC D 2 .   ? 21.29500  19.17300  -2.67800 1.000 81.38542  ? 703 OLC A C3  1 
HETATM 4651 C C2  . OLC D 2 .   ? 20.66900  17.94000  -3.38100 1.000 97.24461  ? 703 OLC A C2  1 
HETATM 4652 C C21 . OLC D 2 .   ? 22.81000  15.65600  -1.30800 1.000 127.72064 ? 703 OLC A C21 1 
HETATM 4653 C C1  . OLC D 2 .   ? 21.40800  16.65800  -2.92900 1.000 120.82843 ? 703 OLC A C1  1 
HETATM 4654 C C22 . OLC D 2 .   ? 24.30700  15.48100  -1.01600 1.000 123.02740 ? 703 OLC A C22 1 
HETATM 4655 O O19 . OLC D 2 .   ? 20.97000  15.58800  -3.21200 1.000 118.69256 ? 703 OLC A O19 1 
HETATM 4656 O O25 . OLC D 2 .   ? 25.25700  17.59300  -0.36800 1.000 108.50671 ? 703 OLC A O25 1 
HETATM 4657 O O23 . OLC D 2 .   ? 24.56300  14.14900  -0.67600 1.000 118.72945 ? 703 OLC A O23 1 
HETATM 4658 O O20 . OLC D 2 .   ? 22.60300  16.75300  -2.17800 1.000 127.26024 ? 703 OLC A O20 1 
HETATM 4659 C C9  . OLC E 2 .   ? -11.88300 39.84300  12.87700 1.000 65.00335  ? 704 OLC A C9  1 
HETATM 4660 C C8  . OLC E 2 .   ? -11.66800 41.38200  12.78700 1.000 64.48422  ? 704 OLC A C8  1 
HETATM 4661 C C24 . OLC E 2 .   ? -12.79700 51.10000  18.31900 1.000 51.81432  ? 704 OLC A C24 1 
HETATM 4662 C C7  . OLC E 2 .   ? -11.78100 42.01100  14.20200 1.000 50.89478  ? 704 OLC A C7  1 
HETATM 4663 C C6  . OLC E 2 .   ? -10.65100 43.06400  14.40100 1.000 38.90094  ? 704 OLC A C6  1 
HETATM 4664 C C5  . OLC E 2 .   ? -10.28900 43.16600  15.91100 1.000 47.32008  ? 704 OLC A C5  1 
HETATM 4665 C C4  . OLC E 2 .   ? -9.32500  44.36600  16.13800 1.000 51.88202  ? 704 OLC A C4  1 
HETATM 4666 C C3  . OLC E 2 .   ? -9.96100  45.34200  17.16700 1.000 46.38485  ? 704 OLC A C3  1 
HETATM 4667 C C2  . OLC E 2 .   ? -9.06700  46.60400  17.29400 1.000 43.09245  ? 704 OLC A C2  1 
HETATM 4668 C C21 . OLC E 2 .   ? -10.83700 49.59600  18.79700 1.000 59.90685  ? 704 OLC A C21 1 
HETATM 4669 C C1  . OLC E 2 .   ? -9.69100  47.56400  18.33400 1.000 83.16924  ? 704 OLC A C1  1 
HETATM 4670 C C22 . OLC E 2 .   ? -11.28800 50.89100  18.10300 1.000 77.06511  ? 704 OLC A C22 1 
HETATM 4671 O O19 . OLC E 2 .   ? -10.06200 47.12800  19.37600 1.000 91.04230  ? 704 OLC A O19 1 
HETATM 4672 O O25 . OLC E 2 .   ? -13.06100 52.42000  18.74900 1.000 71.56080  ? 704 OLC A O25 1 
HETATM 4673 O O23 . OLC E 2 .   ? -10.57400 51.96700  18.63500 1.000 87.18371  ? 704 OLC A O23 1 
HETATM 4674 O O20 . OLC E 2 .   ? -9.82600  48.94700  18.04500 1.000 63.81354  ? 704 OLC A O20 1 
HETATM 4675 C C10 . OLC F 2 .   ? -9.91100  28.68200  21.06900 1.000 79.89790  ? 705 OLC A C10 1 
HETATM 4676 C C9  . OLC F 2 .   ? -9.87700  27.45200  21.61300 1.000 70.57176  ? 705 OLC A C9  1 
HETATM 4677 C C11 . OLC F 2 .   ? -9.06200  29.71500  21.85300 1.000 48.27251  ? 705 OLC A C11 1 
HETATM 4678 C C8  . OLC F 2 .   ? -10.27300 25.94500  21.65500 1.000 65.65388  ? 705 OLC A C8  1 
HETATM 4679 C C24 . OLC F 2 .   ? -16.26500 15.14000  17.80000 1.000 98.40155  ? 705 OLC A C24 1 
HETATM 4680 C C7  . OLC F 2 .   ? -10.55800 25.41600  20.22100 1.000 65.94064  ? 705 OLC A C7  1 
HETATM 4681 C C6  . OLC F 2 .   ? -12.01800 24.87700  20.13000 1.000 95.13875  ? 705 OLC A C6  1 
HETATM 4682 C C5  . OLC F 2 .   ? -12.08900 23.37600  20.54400 1.000 78.29824  ? 705 OLC A C5  1 
HETATM 4683 C C4  . OLC F 2 .   ? -11.90900 22.46800  19.29000 1.000 93.10425  ? 705 OLC A C4  1 
HETATM 4684 C C3  . OLC F 2 .   ? -12.57700 21.08200  19.52900 1.000 79.55691  ? 705 OLC A C3  1 
HETATM 4685 C C2  . OLC F 2 .   ? -13.51200 20.72500  18.34100 1.000 71.64821  ? 705 OLC A C2  1 
HETATM 4686 C C21 . OLC F 2 .   ? -14.78400 17.15600  17.98500 1.000 98.74505  ? 705 OLC A C21 1 
HETATM 4687 C C1  . OLC F 2 .   ? -13.55100 19.19200  18.12200 1.000 82.22352  ? 705 OLC A C1  1 
HETATM 4688 C C22 . OLC F 2 .   ? -15.96500 16.40200  18.61800 1.000 102.83035 ? 705 OLC A C22 1 
HETATM 4689 O O19 . OLC F 2 .   ? -12.64400 18.64300  17.58100 1.000 97.96009  ? 705 OLC A O19 1 
HETATM 4690 O O25 . OLC F 2 .   ? -16.97900 14.22200  18.59900 1.000 104.34526 ? 705 OLC A O25 1 
HETATM 4691 O O23 . OLC F 2 .   ? -15.65800 16.03600  19.93200 1.000 84.72086  ? 705 OLC A O23 1 
HETATM 4692 O O20 . OLC F 2 .   ? -14.66800 18.44400  18.56500 1.000 111.83020 ? 705 OLC A O20 1 
HETATM 4693 C C8  . OLC G 2 .   ? 3.48500   51.81700  2.18500  1.000 49.46807  ? 706 OLC A C8  1 
HETATM 4694 C C7  . OLC G 2 .   ? 4.90500   52.29300  1.78000  1.000 53.27034  ? 706 OLC A C7  1 
HETATM 4695 C C6  . OLC G 2 .   ? 4.96900   53.84800  1.84500  1.000 43.59376  ? 706 OLC A C6  1 
HETATM 4696 C C5  . OLC G 2 .   ? 6.20000   54.34700  1.03600  1.000 59.08682  ? 706 OLC A C5  1 
HETATM 4697 C C4  . OLC G 2 .   ? 5.88600   55.72700  0.38600  1.000 80.25286  ? 706 OLC A C4  1 
HETATM 4698 C C3  . OLC G 2 .   ? 6.24000   55.68100  -1.12800 1.000 81.54709  ? 706 OLC A C3  1 
HETATM 4699 C C2  . OLC G 2 .   ? 6.18400   57.11500  -1.72200 1.000 91.52624  ? 706 OLC A C2  1 
HETATM 4700 C C1  . OLC G 2 .   ? 4.78000   57.38000  -2.31600 1.000 111.46528 ? 706 OLC A C1  1 
HETATM 4701 O O19 . OLC G 2 .   ? 4.44900   56.84100  -3.32400 1.000 100.74744 ? 706 OLC A O19 1 
HETATM 4702 O O20 . OLC G 2 .   ? 3.89100   58.26300  -1.65900 1.000 99.97787  ? 706 OLC A O20 1 
HETATM 4703 C C8  . OLC H 2 .   ? -3.82800  43.87700  3.88800  1.000 69.98284  ? 707 OLC A C8  1 
HETATM 4704 C C7  . OLC H 2 .   ? -3.07700  45.17500  3.48800  1.000 62.40281  ? 707 OLC A C7  1 
HETATM 4705 C C6  . OLC H 2 .   ? -4.11300  46.27100  3.10300  1.000 67.36536  ? 707 OLC A C6  1 
HETATM 4706 C C5  . OLC H 2 .   ? -3.49500  47.21900  2.03600  1.000 77.76014  ? 707 OLC A C5  1 
HETATM 4707 C C4  . OLC H 2 .   ? -2.99900  48.52900  2.71300  1.000 75.07316  ? 707 OLC A C4  1 
HETATM 4708 C C3  . OLC H 2 .   ? -3.37200  49.74800  1.82500  1.000 63.75214  ? 707 OLC A C3  1 
HETATM 4709 C C2  . OLC H 2 .   ? -2.92700  51.05800  2.52800  1.000 91.21335  ? 707 OLC A C2  1 
HETATM 4710 C C1  . OLC H 2 .   ? -4.17200  51.90200  2.88700  1.000 101.86535 ? 707 OLC A C1  1 
HETATM 4711 O O19 . OLC H 2 .   ? -4.10100  52.75000  3.71800  1.000 103.29733 ? 707 OLC A O19 1 
HETATM 4712 O O20 . OLC H 2 .   ? -5.39800  51.66400  2.22200  1.000 85.19564  ? 707 OLC A O20 1 
HETATM 4713 C C10 . OLC I 2 .   ? 15.00200  37.67800  29.89500 1.000 74.06046  ? 708 OLC A C10 1 
HETATM 4714 C C9  . OLC I 2 .   ? 14.44300  38.65400  29.16200 1.000 63.67532  ? 708 OLC A C9  1 
HETATM 4715 C C8  . OLC I 2 .   ? 14.23800  40.14600  28.77100 1.000 58.80148  ? 708 OLC A C8  1 
HETATM 4716 C C7  . OLC I 2 .   ? 14.68500  41.05700  29.94600 1.000 74.76848  ? 708 OLC A C7  1 
HETATM 4717 C C6  . OLC I 2 .   ? 15.54800  42.23300  29.39900 1.000 71.87217  ? 708 OLC A C6  1 
HETATM 4718 C C5  . OLC I 2 .   ? 14.64100  43.19900  28.58200 1.000 77.37896  ? 708 OLC A C5  1 
HETATM 4719 C C4  . OLC I 2 .   ? 15.49900  44.30400  27.89600 1.000 65.63310  ? 708 OLC A C4  1 
HETATM 4720 C C3  . OLC I 2 .   ? 14.71500  45.64800  27.89000 1.000 70.68128  ? 708 OLC A C3  1 
HETATM 4721 C C2  . OLC I 2 .   ? 15.67900  46.82000  27.56000 1.000 66.60997  ? 708 OLC A C2  1 
HETATM 4722 C C9  . OLC J 2 .   ? 9.77000   56.51900  -3.40900 1.000 72.71810  ? 709 OLC A C9  1 
HETATM 4723 C C8  . OLC J 2 .   ? 10.13400  55.16900  -4.08900 1.000 80.15024  ? 709 OLC A C8  1 
HETATM 4724 C C7  . OLC J 2 .   ? 11.30800  54.49500  -3.33100 1.000 75.57502  ? 709 OLC A C7  1 
HETATM 4725 C C6  . OLC J 2 .   ? 11.38100  52.98900  -3.72300 1.000 91.76596  ? 709 OLC A C6  1 
HETATM 4726 C C5  . OLC J 2 .   ? 12.85500  52.50000  -3.64500 1.000 92.34056  ? 709 OLC A C5  1 
HETATM 4727 C C4  . OLC J 2 .   ? 12.94900  51.30200  -2.65600 1.000 75.85659  ? 709 OLC A C4  1 
HETATM 4728 C C3  . OLC J 2 .   ? 12.66700  49.97300  -3.41200 1.000 64.13519  ? 709 OLC A C3  1 
HETATM 4729 C C2  . OLC J 2 .   ? 13.13000  48.77300  -2.54100 1.000 64.49962  ? 709 OLC A C2  1 
HETATM 4730 C C1  A RET K 3 .   ? -0.65400  33.41300  11.01500 0.700 50.42593  ? 710 RET A C1  1 
HETATM 4731 C C1  B RET K 3 .   ? -0.53500  33.19400  11.10300 0.300 50.50485  ? 710 RET A C1  1 
HETATM 4732 C C2  A RET K 3 .   ? -1.86900  32.54800  10.63900 0.700 52.85933  ? 710 RET A C2  1 
HETATM 4733 C C2  B RET K 3 .   ? -1.61200  32.14400  10.77800 0.300 52.95140  ? 710 RET A C2  1 
HETATM 4734 C C3  A RET K 3 .   ? -3.18500  33.31000  10.68700 0.700 47.76592  ? 710 RET A C3  1 
HETATM 4735 C C3  B RET K 3 .   ? -3.03200  32.69200  10.80900 0.300 49.47518  ? 710 RET A C3  1 
HETATM 4736 C C4  A RET K 3 .   ? -3.15000  34.47600  9.72200  0.700 51.62773  ? 710 RET A C4  1 
HETATM 4737 C C4  B RET K 3 .   ? -3.19400  33.82800  9.81500  0.300 51.48241  ? 710 RET A C4  1 
HETATM 4738 C C5  A RET K 3 .   ? -1.85800  35.25000  9.75300  0.700 52.81128  ? 710 RET A C5  1 
HETATM 4739 C C5  B RET K 3 .   ? -2.00800  34.75300  9.76600  0.300 52.13410  ? 710 RET A C5  1 
HETATM 4740 C C6  A RET K 3 .   ? -0.77900  34.83300  10.43600 0.700 53.87696  ? 710 RET A C6  1 
HETATM 4741 C C6  B RET K 3 .   ? -0.92400  34.56700  10.53700 0.300 53.49269  ? 710 RET A C6  1 
HETATM 4742 C C7  A RET K 3 .   ? 0.35200   35.79400  10.64600 0.700 52.88608  ? 710 RET A C7  1 
HETATM 4743 C C7  B RET K 3 .   ? -0.05500  35.72800  10.87200 0.300 53.78868  ? 710 RET A C7  1 
HETATM 4744 C C8  A RET K 3 .   ? 1.50600   35.70800  11.31100 0.700 52.61835  ? 710 RET A C8  1 
HETATM 4745 C C8  B RET K 3 .   ? 1.19600   35.83100  11.32800 0.300 52.98591  ? 710 RET A C8  1 
HETATM 4746 C C9  A RET K 3 .   ? 2.52600   36.73700  11.43000 0.700 52.17529  ? 710 RET A C9  1 
HETATM 4747 C C9  B RET K 3 .   ? 1.90500   37.06900  11.60500 0.300 48.90947  ? 710 RET A C9  1 
HETATM 4748 C C10 A RET K 3 .   ? 3.65200   36.46400  12.13300 0.700 51.58871  ? 710 RET A C10 1 
HETATM 4749 C C10 B RET K 3 .   ? 3.17700   37.02100  12.07300 0.300 47.74498  ? 710 RET A C10 1 
HETATM 4750 C C11 A RET K 3 .   ? 4.78100   37.31600  12.35400 0.700 39.68476  ? 710 RET A C11 1 
HETATM 4751 C C11 B RET K 3 .   ? 4.02100   38.12900  12.39600 0.300 41.29931  ? 710 RET A C11 1 
HETATM 4752 C C12 A RET K 3 .   ? 5.84300   36.92500  13.07400 0.700 47.25254  ? 710 RET A C12 1 
HETATM 4753 C C12 B RET K 3 .   ? 5.27800   38.04400  12.86100 0.300 45.78788  ? 710 RET A C12 1 
HETATM 4754 C C13 A RET K 3 .   ? 7.04300   37.69100  13.36900 0.700 45.02184  ? 710 RET A C13 1 
HETATM 4755 C C13 B RET K 3 .   ? 6.13400   39.17100  13.18800 0.300 55.39672  ? 710 RET A C13 1 
HETATM 4756 C C14 A RET K 3 .   ? 7.99100   37.14400  14.16800 0.700 50.47687  ? 710 RET A C14 1 
HETATM 4757 C C14 B RET K 3 .   ? 7.38300   38.96800  13.66800 0.300 49.50191  ? 710 RET A C14 1 
HETATM 4758 C C15 A RET K 3 .   ? 9.24200   37.74500  14.66800 0.700 52.43233  ? 710 RET A C15 1 
HETATM 4759 C C15 B RET K 3 .   ? 8.19600   37.80600  13.97000 0.300 49.19488  ? 710 RET A C15 1 
HETATM 4760 C C16 A RET K 3 .   ? -0.58900  33.44400  12.54700 0.700 36.09029  ? 710 RET A C16 1 
HETATM 4761 C C16 B RET K 3 .   ? -0.38500  33.25100  12.62800 0.300 37.70262  ? 710 RET A C16 1 
HETATM 4762 C C17 A RET K 3 .   ? 0.58900   32.69600  10.47200 0.700 56.76213  ? 710 RET A C17 1 
HETATM 4763 C C17 B RET K 3 .   ? 0.77700   32.69600  10.48400 0.300 55.84592  ? 710 RET A C17 1 
HETATM 4764 C C18 A RET K 3 .   ? -1.91800  36.51900  8.95100  0.700 57.52669  ? 710 RET A C18 1 
HETATM 4765 C C18 B RET K 3 .   ? -2.17100  35.88000  8.78500  0.300 53.83906  ? 710 RET A C18 1 
HETATM 4766 C C19 A RET K 3 .   ? 2.28500   38.05600  10.75100 0.700 56.85744  ? 710 RET A C19 1 
HETATM 4767 C C19 B RET K 3 .   ? 1.18000   38.36200  11.35800 0.300 45.57536  ? 710 RET A C19 1 
HETATM 4768 C C20 A RET K 3 .   ? 7.15000   39.07900  12.80600 0.700 57.40854  ? 710 RET A C20 1 
HETATM 4769 C C20 B RET K 3 .   ? 5.57500   40.54600  12.98800 0.300 45.23965  ? 710 RET A C20 1 
HETATM 4770 O O   . HOH L 4 .   ? 4.09300   30.33600  10.33500 1.000 34.68343  ? 801 HOH A O   1 
HETATM 4771 O O   . HOH L 4 .   ? 1.86700   56.46900  14.25700 1.000 37.46754  ? 802 HOH A O   1 
HETATM 4772 O O   . HOH L 4 .   ? 6.17200   10.66600  27.37300 1.000 34.25859  ? 803 HOH A O   1 
HETATM 4773 O O   . HOH L 4 .   ? -7.91500  18.62800  17.74600 1.000 42.28358  ? 804 HOH A O   1 
HETATM 4774 O O   . HOH L 4 .   ? 1.67200   18.40000  12.67400 1.000 25.90517  ? 805 HOH A O   1 
HETATM 4775 O O   . HOH L 4 .   ? 27.18500  62.02000  2.66700  1.000 38.94426  ? 806 HOH A O   1 
HETATM 4776 O O   . HOH L 4 .   ? 25.83800  64.17800  0.83700  1.000 30.05063  ? 807 HOH A O   1 
# 
