data_8R96
# 
_entry.id   8R96 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8R96         pdb_00008r96 10.2210/pdb8r96/pdb 
WWPDB D_1292134700 ?            ?                   
# 
_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       2024-12-11 
# 
_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                        8R96 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-30 
_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                 2 
_pdbx_contact_author.email              kirkovalev94@gmail.com 
_pdbx_contact_author.name_first         Kirill 
_pdbx_contact_author.name_last          Kovalev 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2229-181X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kovalev, K.'  1 ? 
'Lamm, G.H.U.' 2 ? 
'Marin, E.'    3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'CryoRhodopsins: a new clade of microbial rhodopsins from cold environments' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lamm, G.H.U.' 1 ? 
primary 'Marin, E.'    2 ? 
primary 'Guskov, A.'   3 ? 
primary 'Kovalev, K.'  4 ? 
# 
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 cryorhodopsin   34973.539 5  ? ? ? ? 
2 non-polymer syn EICOSANE        282.547   14 ? ? ? ? 
3 non-polymer syn 'PHOSPHATE ION' 94.971    5  ? ? ? ? 
4 non-polymer man RETINAL         284.436   5  ? ? ? ? 
5 non-polymer syn 'OLEIC ACID'    282.461   1  ? ? ? ? 
6 water       nat water           18.015    31 ? ? ? ? 
# 
_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       
;MRLTNVSVPWGATLSNAEHQLIFYFLVVAALAFVAGFIRTYITRNEVGSRYRTAVSARLGMLGVALLAYILIIVAFLLGY
DSTAGGWVPNDGAINIFSTRYIEWTVSVPLLTIELLAVCATLGVQARRNTAIAVTATGAMIFCGFLGAIVIDNGTNTGAF
ILWAVISCVFWVIANVVLIRAVRQSLPTLTPESHTMLKSAAIVLLAGWVVYPIVYFLPLFGASGGLTTTILITLTVADVI
VKLGFSTQTHRVAKLRTAEDVRAGDDVHPESIWISSVKQSDAGLPREVYLAEGAAVHDRRTKPPTSAAVASPEAPLPPDS
TPLDGGY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRLTNVSVPWGATLSNAEHQLIFYFLVVAALAFVAGFIRTYITRNEVGSRYRTAVSARLGMLGVALLAYILIIVAFLLGY
DSTAGGWVPNDGAINIFSTRYIEWTVSVPLLTIELLAVCATLGVQARRNTAIAVTATGAMIFCGFLGAIVIDNGTNTGAF
ILWAVISCVFWVIANVVLIRAVRQSLPTLTPESHTMLKSAAIVLLAGWVVYPIVYFLPLFGASGGLTTTILITLTVADVI
VKLGFSTQTHRVAKLRTAEDVRAGDDVHPESIWISSVKQSDAGLPREVYLAEGAAVHDRRTKPPTSAAVASPEAPLPPDS
TPLDGGY
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 EICOSANE        LFA 
3 'PHOSPHATE ION' PO4 
4 RETINAL         RET 
5 'OLEIC ACID'    OLA 
6 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   LEU n 
1 4   THR n 
1 5   ASN n 
1 6   VAL n 
1 7   SER n 
1 8   VAL n 
1 9   PRO n 
1 10  TRP n 
1 11  GLY n 
1 12  ALA n 
1 13  THR n 
1 14  LEU n 
1 15  SER n 
1 16  ASN n 
1 17  ALA n 
1 18  GLU n 
1 19  HIS n 
1 20  GLN n 
1 21  LEU n 
1 22  ILE n 
1 23  PHE n 
1 24  TYR n 
1 25  PHE n 
1 26  LEU n 
1 27  VAL n 
1 28  VAL n 
1 29  ALA n 
1 30  ALA n 
1 31  LEU n 
1 32  ALA n 
1 33  PHE n 
1 34  VAL n 
1 35  ALA n 
1 36  GLY n 
1 37  PHE n 
1 38  ILE n 
1 39  ARG n 
1 40  THR n 
1 41  TYR n 
1 42  ILE n 
1 43  THR n 
1 44  ARG n 
1 45  ASN n 
1 46  GLU n 
1 47  VAL n 
1 48  GLY n 
1 49  SER n 
1 50  ARG n 
1 51  TYR n 
1 52  ARG n 
1 53  THR n 
1 54  ALA n 
1 55  VAL n 
1 56  SER n 
1 57  ALA n 
1 58  ARG n 
1 59  LEU n 
1 60  GLY n 
1 61  MET n 
1 62  LEU n 
1 63  GLY n 
1 64  VAL n 
1 65  ALA n 
1 66  LEU n 
1 67  LEU n 
1 68  ALA n 
1 69  TYR n 
1 70  ILE n 
1 71  LEU n 
1 72  ILE n 
1 73  ILE n 
1 74  VAL n 
1 75  ALA n 
1 76  PHE n 
1 77  LEU n 
1 78  LEU n 
1 79  GLY n 
1 80  TYR n 
1 81  ASP n 
1 82  SER n 
1 83  THR n 
1 84  ALA n 
1 85  GLY n 
1 86  GLY n 
1 87  TRP n 
1 88  VAL n 
1 89  PRO n 
1 90  ASN n 
1 91  ASP n 
1 92  GLY n 
1 93  ALA n 
1 94  ILE n 
1 95  ASN n 
1 96  ILE n 
1 97  PHE n 
1 98  SER n 
1 99  THR n 
1 100 ARG n 
1 101 TYR n 
1 102 ILE n 
1 103 GLU n 
1 104 TRP n 
1 105 THR n 
1 106 VAL n 
1 107 SER n 
1 108 VAL n 
1 109 PRO n 
1 110 LEU n 
1 111 LEU n 
1 112 THR n 
1 113 ILE n 
1 114 GLU n 
1 115 LEU n 
1 116 LEU n 
1 117 ALA n 
1 118 VAL n 
1 119 CYS n 
1 120 ALA n 
1 121 THR n 
1 122 LEU n 
1 123 GLY n 
1 124 VAL n 
1 125 GLN n 
1 126 ALA n 
1 127 ARG n 
1 128 ARG n 
1 129 ASN n 
1 130 THR n 
1 131 ALA n 
1 132 ILE n 
1 133 ALA n 
1 134 VAL n 
1 135 THR n 
1 136 ALA n 
1 137 THR n 
1 138 GLY n 
1 139 ALA n 
1 140 MET n 
1 141 ILE n 
1 142 PHE n 
1 143 CYS n 
1 144 GLY n 
1 145 PHE n 
1 146 LEU n 
1 147 GLY n 
1 148 ALA n 
1 149 ILE n 
1 150 VAL n 
1 151 ILE n 
1 152 ASP n 
1 153 ASN n 
1 154 GLY n 
1 155 THR n 
1 156 ASN n 
1 157 THR n 
1 158 GLY n 
1 159 ALA n 
1 160 PHE n 
1 161 ILE n 
1 162 LEU n 
1 163 TRP n 
1 164 ALA n 
1 165 VAL n 
1 166 ILE n 
1 167 SER n 
1 168 CYS n 
1 169 VAL n 
1 170 PHE n 
1 171 TRP n 
1 172 VAL n 
1 173 ILE n 
1 174 ALA n 
1 175 ASN n 
1 176 VAL n 
1 177 VAL n 
1 178 LEU n 
1 179 ILE n 
1 180 ARG n 
1 181 ALA n 
1 182 VAL n 
1 183 ARG n 
1 184 GLN n 
1 185 SER n 
1 186 LEU n 
1 187 PRO n 
1 188 THR n 
1 189 LEU n 
1 190 THR n 
1 191 PRO n 
1 192 GLU n 
1 193 SER n 
1 194 HIS n 
1 195 THR n 
1 196 MET n 
1 197 LEU n 
1 198 LYS n 
1 199 SER n 
1 200 ALA n 
1 201 ALA n 
1 202 ILE n 
1 203 VAL n 
1 204 LEU n 
1 205 LEU n 
1 206 ALA n 
1 207 GLY n 
1 208 TRP n 
1 209 VAL n 
1 210 VAL n 
1 211 TYR n 
1 212 PRO n 
1 213 ILE n 
1 214 VAL n 
1 215 TYR n 
1 216 PHE n 
1 217 LEU n 
1 218 PRO n 
1 219 LEU n 
1 220 PHE n 
1 221 GLY n 
1 222 ALA n 
1 223 SER n 
1 224 GLY n 
1 225 GLY n 
1 226 LEU n 
1 227 THR n 
1 228 THR n 
1 229 THR n 
1 230 ILE n 
1 231 LEU n 
1 232 ILE n 
1 233 THR n 
1 234 LEU n 
1 235 THR n 
1 236 VAL n 
1 237 ALA n 
1 238 ASP n 
1 239 VAL n 
1 240 ILE n 
1 241 VAL n 
1 242 LYS n 
1 243 LEU n 
1 244 GLY n 
1 245 PHE n 
1 246 SER n 
1 247 THR n 
1 248 GLN n 
1 249 THR n 
1 250 HIS n 
1 251 ARG n 
1 252 VAL n 
1 253 ALA n 
1 254 LYS n 
1 255 LEU n 
1 256 ARG n 
1 257 THR n 
1 258 ALA n 
1 259 GLU n 
1 260 ASP n 
1 261 VAL n 
1 262 ARG n 
1 263 ALA n 
1 264 GLY n 
1 265 ASP n 
1 266 ASP n 
1 267 VAL n 
1 268 HIS n 
1 269 PRO n 
1 270 GLU n 
1 271 SER n 
1 272 ILE n 
1 273 TRP n 
1 274 ILE n 
1 275 SER n 
1 276 SER n 
1 277 VAL n 
1 278 LYS n 
1 279 GLN n 
1 280 SER n 
1 281 ASP n 
1 282 ALA n 
1 283 GLY n 
1 284 LEU n 
1 285 PRO n 
1 286 ARG n 
1 287 GLU n 
1 288 VAL n 
1 289 TYR n 
1 290 LEU n 
1 291 ALA n 
1 292 GLU n 
1 293 GLY n 
1 294 ALA n 
1 295 ALA n 
1 296 VAL n 
1 297 HIS n 
1 298 ASP n 
1 299 ARG n 
1 300 ARG n 
1 301 THR n 
1 302 LYS n 
1 303 PRO n 
1 304 PRO n 
1 305 THR n 
1 306 SER n 
1 307 ALA n 
1 308 ALA n 
1 309 VAL n 
1 310 ALA n 
1 311 SER n 
1 312 PRO n 
1 313 GLU n 
1 314 ALA n 
1 315 PRO n 
1 316 LEU n 
1 317 PRO n 
1 318 PRO n 
1 319 ASP n 
1 320 SER n 
1 321 THR n 
1 322 PRO n 
1 323 LEU n 
1 324 ASP n 
1 325 GLY n 
1 326 GLY n 
1 327 TYR 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' 1 327 ? ? ? ? ? ? ? ? ? 'Subtercola endophyticus' 2895559 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 327 ? ? ? ? ? ? ? ? ? 'Subtercola endophyticus' 2895559 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
LFA non-polymer         . EICOSANE        'LIPID FRAGMENT' 'C20 H42'        282.547 
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 
OLA non-polymer         . 'OLEIC ACID'    ?                'C18 H34 O2'     282.461 
PHE 'L-peptide linking' y PHENYLALANINE   ?                'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ?                'O4 P -3'        94.971  
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ARG 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   ASN 5   5   5   ASN ASN A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  PHE 23  23  23  PHE PHE A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  TYR 41  41  41  TYR TYR A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  TRP 87  87  87  TRP TRP A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 TRP 104 104 104 TRP TRP A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 CYS 119 119 119 CYS CYS A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 MET 140 140 140 MET MET A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 TRP 163 163 163 TRP TRP A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 CYS 168 168 168 CYS CYS A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 VAL 172 172 172 VAL VAL A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 MET 196 196 196 MET MET A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 LYS 242 242 242 LYS LYR A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 ARG 251 251 251 ARG ARG A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 GLU 259 259 259 GLU GLU A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 ASP 265 265 265 ASP ASP A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 HIS 268 268 268 HIS HIS A . n 
A 1 269 PRO 269 269 269 PRO PRO A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 TRP 273 273 273 TRP TRP A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 TYR 289 289 289 TYR TYR A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 GLU 292 292 ?   ?   ?   A . n 
A 1 293 GLY 293 293 ?   ?   ?   A . n 
A 1 294 ALA 294 294 ?   ?   ?   A . n 
A 1 295 ALA 295 295 ?   ?   ?   A . n 
A 1 296 VAL 296 296 ?   ?   ?   A . n 
A 1 297 HIS 297 297 ?   ?   ?   A . n 
A 1 298 ASP 298 298 ?   ?   ?   A . n 
A 1 299 ARG 299 299 ?   ?   ?   A . n 
A 1 300 ARG 300 300 ?   ?   ?   A . n 
A 1 301 THR 301 301 ?   ?   ?   A . n 
A 1 302 LYS 302 302 ?   ?   ?   A . n 
A 1 303 PRO 303 303 ?   ?   ?   A . n 
A 1 304 PRO 304 304 ?   ?   ?   A . n 
A 1 305 THR 305 305 ?   ?   ?   A . n 
A 1 306 SER 306 306 ?   ?   ?   A . n 
A 1 307 ALA 307 307 ?   ?   ?   A . n 
A 1 308 ALA 308 308 ?   ?   ?   A . n 
A 1 309 VAL 309 309 ?   ?   ?   A . n 
A 1 310 ALA 310 310 ?   ?   ?   A . n 
A 1 311 SER 311 311 ?   ?   ?   A . n 
A 1 312 PRO 312 312 ?   ?   ?   A . n 
A 1 313 GLU 313 313 ?   ?   ?   A . n 
A 1 314 ALA 314 314 ?   ?   ?   A . n 
A 1 315 PRO 315 315 ?   ?   ?   A . n 
A 1 316 LEU 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 PRO 318 318 ?   ?   ?   A . n 
A 1 319 ASP 319 319 ?   ?   ?   A . n 
A 1 320 SER 320 320 ?   ?   ?   A . n 
A 1 321 THR 321 321 ?   ?   ?   A . n 
A 1 322 PRO 322 322 ?   ?   ?   A . n 
A 1 323 LEU 323 323 ?   ?   ?   A . n 
A 1 324 ASP 324 324 ?   ?   ?   A . n 
A 1 325 GLY 325 325 ?   ?   ?   A . n 
A 1 326 GLY 326 326 ?   ?   ?   A . n 
A 1 327 TYR 327 327 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ARG 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   THR 4   4   ?   ?   ?   B . n 
B 1 5   ASN 5   5   5   ASN ASN B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   VAL 8   8   8   VAL VAL B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  HIS 19  19  19  HIS HIS B . n 
B 1 20  GLN 20  20  20  GLN GLN B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  PHE 23  23  23  PHE PHE B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  PHE 25  25  25  PHE PHE B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  VAL 27  27  27  VAL VAL B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  ILE 38  38  38  ILE ILE B . n 
B 1 39  ARG 39  39  39  ARG ARG B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  TYR 41  41  41  TYR TYR B . n 
B 1 42  ILE 42  42  42  ILE ILE B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  ARG 44  44  44  ARG ARG B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  SER 49  49  49  SER SER B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ARG 52  52  52  ARG ARG B . n 
B 1 53  THR 53  53  53  THR THR B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  ILE 70  70  70  ILE ILE B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  VAL 74  74  74  VAL VAL B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  TYR 80  80  80  TYR TYR B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  TRP 87  87  87  TRP TRP B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  ASP 91  91  91  ASP ASP B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  PHE 97  97  97  PHE PHE B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 ARG 100 100 100 ARG ARG B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 TRP 104 104 104 TRP TRP B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 VAL 108 108 108 VAL VAL B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 CYS 119 119 119 CYS CYS B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 THR 121 121 121 THR THR B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLN 125 125 125 GLN GLN B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 ARG 128 128 128 ARG ARG B . n 
B 1 129 ASN 129 129 129 ASN ASN B . n 
B 1 130 THR 130 130 130 THR THR B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 ILE 132 132 132 ILE ILE B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ALA 136 136 136 ALA ALA B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ALA 139 139 139 ALA ALA B . n 
B 1 140 MET 140 140 140 MET MET B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 PHE 145 145 145 PHE PHE B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 ALA 148 148 148 ALA ALA B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ASP 152 152 152 ASP ASP B . n 
B 1 153 ASN 153 153 153 ASN ASN B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 PHE 160 160 160 PHE PHE B . n 
B 1 161 ILE 161 161 161 ILE ILE B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 TRP 163 163 163 TRP TRP B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 CYS 168 168 168 CYS CYS B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 TRP 171 171 171 TRP TRP B . n 
B 1 172 VAL 172 172 172 VAL VAL B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 ASN 175 175 175 ASN ASN B . n 
B 1 176 VAL 176 176 176 VAL VAL B . n 
B 1 177 VAL 177 177 177 VAL VAL B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 ARG 180 180 180 ARG ARG B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 GLN 184 184 184 GLN GLN B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 LEU 186 186 186 LEU LEU B . n 
B 1 187 PRO 187 187 187 PRO PRO B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 PRO 191 191 191 PRO PRO B . n 
B 1 192 GLU 192 192 192 GLU GLU B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 HIS 194 194 194 HIS HIS B . n 
B 1 195 THR 195 195 195 THR THR B . n 
B 1 196 MET 196 196 196 MET MET B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 LYS 198 198 198 LYS LYS B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 ALA 201 201 201 ALA ALA B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 GLY 207 207 207 GLY GLY B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 PRO 212 212 212 PRO PRO B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 TYR 215 215 215 TYR TYR B . n 
B 1 216 PHE 216 216 216 PHE PHE B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 PHE 220 220 220 PHE PHE B . n 
B 1 221 GLY 221 221 221 GLY GLY B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 LEU 226 226 226 LEU LEU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 THR 229 229 229 THR THR B . n 
B 1 230 ILE 230 230 230 ILE ILE B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 THR 233 233 233 THR THR B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 ILE 240 240 240 ILE ILE B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 LYS 242 242 242 LYS LYR B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 GLY 244 244 244 GLY GLY B . n 
B 1 245 PHE 245 245 245 PHE PHE B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 ARG 251 251 251 ARG ARG B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 ALA 253 253 253 ALA ALA B . n 
B 1 254 LYS 254 254 254 LYS LYS B . n 
B 1 255 LEU 255 255 255 LEU LEU B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 GLU 259 259 259 GLU GLU B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 ARG 262 262 262 ARG ARG B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 ASP 265 265 265 ASP ASP B . n 
B 1 266 ASP 266 266 266 ASP ASP B . n 
B 1 267 VAL 267 267 267 VAL VAL B . n 
B 1 268 HIS 268 268 268 HIS HIS B . n 
B 1 269 PRO 269 269 269 PRO PRO B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 TRP 273 273 273 TRP TRP B . n 
B 1 274 ILE 274 274 274 ILE ILE B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 SER 276 276 276 SER SER B . n 
B 1 277 VAL 277 277 277 VAL VAL B . n 
B 1 278 LYS 278 278 278 LYS LYS B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 SER 280 280 280 SER SER B . n 
B 1 281 ASP 281 281 281 ASP ASP B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 VAL 288 288 288 VAL VAL B . n 
B 1 289 TYR 289 289 289 TYR TYR B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 GLY 293 293 293 GLY GLY B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 ALA 295 295 ?   ?   ?   B . n 
B 1 296 VAL 296 296 ?   ?   ?   B . n 
B 1 297 HIS 297 297 ?   ?   ?   B . n 
B 1 298 ASP 298 298 ?   ?   ?   B . n 
B 1 299 ARG 299 299 ?   ?   ?   B . n 
B 1 300 ARG 300 300 ?   ?   ?   B . n 
B 1 301 THR 301 301 ?   ?   ?   B . n 
B 1 302 LYS 302 302 ?   ?   ?   B . n 
B 1 303 PRO 303 303 ?   ?   ?   B . n 
B 1 304 PRO 304 304 ?   ?   ?   B . n 
B 1 305 THR 305 305 ?   ?   ?   B . n 
B 1 306 SER 306 306 ?   ?   ?   B . n 
B 1 307 ALA 307 307 ?   ?   ?   B . n 
B 1 308 ALA 308 308 ?   ?   ?   B . n 
B 1 309 VAL 309 309 ?   ?   ?   B . n 
B 1 310 ALA 310 310 ?   ?   ?   B . n 
B 1 311 SER 311 311 ?   ?   ?   B . n 
B 1 312 PRO 312 312 ?   ?   ?   B . n 
B 1 313 GLU 313 313 ?   ?   ?   B . n 
B 1 314 ALA 314 314 ?   ?   ?   B . n 
B 1 315 PRO 315 315 ?   ?   ?   B . n 
B 1 316 LEU 316 316 ?   ?   ?   B . n 
B 1 317 PRO 317 317 ?   ?   ?   B . n 
B 1 318 PRO 318 318 ?   ?   ?   B . n 
B 1 319 ASP 319 319 ?   ?   ?   B . n 
B 1 320 SER 320 320 ?   ?   ?   B . n 
B 1 321 THR 321 321 ?   ?   ?   B . n 
B 1 322 PRO 322 322 ?   ?   ?   B . n 
B 1 323 LEU 323 323 ?   ?   ?   B . n 
B 1 324 ASP 324 324 ?   ?   ?   B . n 
B 1 325 GLY 325 325 ?   ?   ?   B . n 
B 1 326 GLY 326 326 ?   ?   ?   B . n 
B 1 327 TYR 327 327 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ARG 2   2   ?   ?   ?   C . n 
C 1 3   LEU 3   3   ?   ?   ?   C . n 
C 1 4   THR 4   4   4   THR ALA C . n 
C 1 5   ASN 5   5   5   ASN ASN C . n 
C 1 6   VAL 6   6   6   VAL VAL C . n 
C 1 7   SER 7   7   7   SER SER C . n 
C 1 8   VAL 8   8   8   VAL VAL C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  TRP 10  10  10  TRP TRP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  THR 13  13  13  THR THR C . n 
C 1 14  LEU 14  14  14  LEU LEU C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  ASN 16  16  16  ASN ASN C . n 
C 1 17  ALA 17  17  17  ALA ALA C . n 
C 1 18  GLU 18  18  18  GLU GLU C . n 
C 1 19  HIS 19  19  19  HIS HIS C . n 
C 1 20  GLN 20  20  20  GLN GLN C . n 
C 1 21  LEU 21  21  21  LEU LEU C . n 
C 1 22  ILE 22  22  22  ILE ILE C . n 
C 1 23  PHE 23  23  23  PHE PHE C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  PHE 25  25  25  PHE PHE C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  VAL 27  27  27  VAL VAL C . n 
C 1 28  VAL 28  28  28  VAL VAL C . n 
C 1 29  ALA 29  29  29  ALA ALA C . n 
C 1 30  ALA 30  30  30  ALA ALA C . n 
C 1 31  LEU 31  31  31  LEU LEU C . n 
C 1 32  ALA 32  32  32  ALA ALA C . n 
C 1 33  PHE 33  33  33  PHE PHE C . n 
C 1 34  VAL 34  34  34  VAL VAL C . n 
C 1 35  ALA 35  35  35  ALA ALA C . n 
C 1 36  GLY 36  36  36  GLY GLY C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  ILE 38  38  38  ILE ILE C . n 
C 1 39  ARG 39  39  39  ARG ARG C . n 
C 1 40  THR 40  40  40  THR THR C . n 
C 1 41  TYR 41  41  41  TYR TYR C . n 
C 1 42  ILE 42  42  42  ILE ILE C . n 
C 1 43  THR 43  43  43  THR THR C . n 
C 1 44  ARG 44  44  44  ARG ARG C . n 
C 1 45  ASN 45  45  45  ASN ASN C . n 
C 1 46  GLU 46  46  46  GLU GLU C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  GLY 48  48  48  GLY GLY C . n 
C 1 49  SER 49  49  49  SER SER C . n 
C 1 50  ARG 50  50  50  ARG ARG C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ARG 52  52  52  ARG ARG C . n 
C 1 53  THR 53  53  53  THR THR C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  VAL 55  55  55  VAL VAL C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  ALA 57  57  57  ALA ALA C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  LEU 59  59  59  LEU LEU C . n 
C 1 60  GLY 60  60  60  GLY GLY C . n 
C 1 61  MET 61  61  61  MET MET C . n 
C 1 62  LEU 62  62  62  LEU LEU C . n 
C 1 63  GLY 63  63  63  GLY GLY C . n 
C 1 64  VAL 64  64  64  VAL VAL C . n 
C 1 65  ALA 65  65  65  ALA ALA C . n 
C 1 66  LEU 66  66  66  LEU LEU C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  ALA 68  68  68  ALA ALA C . n 
C 1 69  TYR 69  69  69  TYR TYR C . n 
C 1 70  ILE 70  70  70  ILE ILE C . n 
C 1 71  LEU 71  71  71  LEU LEU C . n 
C 1 72  ILE 72  72  72  ILE ILE C . n 
C 1 73  ILE 73  73  73  ILE ILE C . n 
C 1 74  VAL 74  74  74  VAL VAL C . n 
C 1 75  ALA 75  75  75  ALA ALA C . n 
C 1 76  PHE 76  76  76  PHE PHE C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  GLY 79  79  79  GLY GLY C . n 
C 1 80  TYR 80  80  80  TYR TYR C . n 
C 1 81  ASP 81  81  81  ASP ASP C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  THR 83  83  83  THR THR C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  GLY 86  86  86  GLY GLY C . n 
C 1 87  TRP 87  87  87  TRP TRP C . n 
C 1 88  VAL 88  88  88  VAL VAL C . n 
C 1 89  PRO 89  89  89  PRO PRO C . n 
C 1 90  ASN 90  90  90  ASN ASN C . n 
C 1 91  ASP 91  91  91  ASP ASP C . n 
C 1 92  GLY 92  92  92  GLY GLY C . n 
C 1 93  ALA 93  93  93  ALA ALA C . n 
C 1 94  ILE 94  94  94  ILE ILE C . n 
C 1 95  ASN 95  95  95  ASN ASN C . n 
C 1 96  ILE 96  96  96  ILE ILE C . n 
C 1 97  PHE 97  97  97  PHE PHE C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  THR 99  99  99  THR THR C . n 
C 1 100 ARG 100 100 100 ARG ARG C . n 
C 1 101 TYR 101 101 101 TYR TYR C . n 
C 1 102 ILE 102 102 102 ILE ILE C . n 
C 1 103 GLU 103 103 103 GLU GLU C . n 
C 1 104 TRP 104 104 104 TRP TRP C . n 
C 1 105 THR 105 105 105 THR THR C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 VAL 108 108 108 VAL VAL C . n 
C 1 109 PRO 109 109 109 PRO PRO C . n 
C 1 110 LEU 110 110 110 LEU LEU C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 THR 112 112 112 THR THR C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLU 114 114 114 GLU GLU C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 ALA 117 117 117 ALA ALA C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 CYS 119 119 119 CYS CYS C . n 
C 1 120 ALA 120 120 120 ALA ALA C . n 
C 1 121 THR 121 121 121 THR THR C . n 
C 1 122 LEU 122 122 122 LEU LEU C . n 
C 1 123 GLY 123 123 123 GLY GLY C . n 
C 1 124 VAL 124 124 124 VAL VAL C . n 
C 1 125 GLN 125 125 125 GLN GLN C . n 
C 1 126 ALA 126 126 126 ALA ALA C . n 
C 1 127 ARG 127 127 127 ARG ARG C . n 
C 1 128 ARG 128 128 128 ARG ARG C . n 
C 1 129 ASN 129 129 129 ASN ASN C . n 
C 1 130 THR 130 130 130 THR THR C . n 
C 1 131 ALA 131 131 131 ALA ALA C . n 
C 1 132 ILE 132 132 132 ILE ILE C . n 
C 1 133 ALA 133 133 133 ALA ALA C . n 
C 1 134 VAL 134 134 134 VAL VAL C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 ALA 136 136 136 ALA ALA C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ALA 139 139 139 ALA ALA C . n 
C 1 140 MET 140 140 140 MET MET C . n 
C 1 141 ILE 141 141 141 ILE ILE C . n 
C 1 142 PHE 142 142 142 PHE PHE C . n 
C 1 143 CYS 143 143 143 CYS CYS C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 PHE 145 145 145 PHE PHE C . n 
C 1 146 LEU 146 146 146 LEU LEU C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 ALA 148 148 148 ALA ALA C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 VAL 150 150 150 VAL VAL C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ASP 152 152 152 ASP ASP C . n 
C 1 153 ASN 153 153 153 ASN ASN C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 THR 155 155 155 THR THR C . n 
C 1 156 ASN 156 156 156 ASN ASN C . n 
C 1 157 THR 157 157 157 THR THR C . n 
C 1 158 GLY 158 158 158 GLY GLY C . n 
C 1 159 ALA 159 159 159 ALA ALA C . n 
C 1 160 PHE 160 160 160 PHE PHE C . n 
C 1 161 ILE 161 161 161 ILE ILE C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 TRP 163 163 163 TRP TRP C . n 
C 1 164 ALA 164 164 164 ALA ALA C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 ILE 166 166 166 ILE ILE C . n 
C 1 167 SER 167 167 167 SER SER C . n 
C 1 168 CYS 168 168 168 CYS CYS C . n 
C 1 169 VAL 169 169 169 VAL VAL C . n 
C 1 170 PHE 170 170 170 PHE PHE C . n 
C 1 171 TRP 171 171 171 TRP TRP C . n 
C 1 172 VAL 172 172 172 VAL VAL C . n 
C 1 173 ILE 173 173 173 ILE ILE C . n 
C 1 174 ALA 174 174 174 ALA ALA C . n 
C 1 175 ASN 175 175 175 ASN ASN C . n 
C 1 176 VAL 176 176 176 VAL VAL C . n 
C 1 177 VAL 177 177 177 VAL VAL C . n 
C 1 178 LEU 178 178 178 LEU LEU C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 ARG 180 180 180 ARG ARG C . n 
C 1 181 ALA 181 181 181 ALA ALA C . n 
C 1 182 VAL 182 182 182 VAL VAL C . n 
C 1 183 ARG 183 183 183 ARG ARG C . n 
C 1 184 GLN 184 184 184 GLN GLN C . n 
C 1 185 SER 185 185 185 SER SER C . n 
C 1 186 LEU 186 186 186 LEU LEU C . n 
C 1 187 PRO 187 187 187 PRO PRO C . n 
C 1 188 THR 188 188 188 THR THR C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 PRO 191 191 191 PRO PRO C . n 
C 1 192 GLU 192 192 192 GLU GLU C . n 
C 1 193 SER 193 193 193 SER SER C . n 
C 1 194 HIS 194 194 194 HIS HIS C . n 
C 1 195 THR 195 195 195 THR THR C . n 
C 1 196 MET 196 196 196 MET MET C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 LYS 198 198 198 LYS LYS C . n 
C 1 199 SER 199 199 199 SER SER C . n 
C 1 200 ALA 200 200 200 ALA ALA C . n 
C 1 201 ALA 201 201 201 ALA ALA C . n 
C 1 202 ILE 202 202 202 ILE ILE C . n 
C 1 203 VAL 203 203 203 VAL VAL C . n 
C 1 204 LEU 204 204 204 LEU LEU C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 ALA 206 206 206 ALA ALA C . n 
C 1 207 GLY 207 207 207 GLY GLY C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 VAL 209 209 209 VAL VAL C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 TYR 211 211 211 TYR TYR C . n 
C 1 212 PRO 212 212 212 PRO PRO C . n 
C 1 213 ILE 213 213 213 ILE ILE C . n 
C 1 214 VAL 214 214 214 VAL VAL C . n 
C 1 215 TYR 215 215 215 TYR TYR C . n 
C 1 216 PHE 216 216 216 PHE PHE C . n 
C 1 217 LEU 217 217 217 LEU LEU C . n 
C 1 218 PRO 218 218 218 PRO PRO C . n 
C 1 219 LEU 219 219 219 LEU LEU C . n 
C 1 220 PHE 220 220 220 PHE PHE C . n 
C 1 221 GLY 221 221 221 GLY GLY C . n 
C 1 222 ALA 222 222 222 ALA ALA C . n 
C 1 223 SER 223 223 223 SER SER C . n 
C 1 224 GLY 224 224 224 GLY GLY C . n 
C 1 225 GLY 225 225 225 GLY GLY C . n 
C 1 226 LEU 226 226 226 LEU LEU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 THR 228 228 228 THR THR C . n 
C 1 229 THR 229 229 229 THR THR C . n 
C 1 230 ILE 230 230 230 ILE ILE C . n 
C 1 231 LEU 231 231 231 LEU LEU C . n 
C 1 232 ILE 232 232 232 ILE ILE C . n 
C 1 233 THR 233 233 233 THR THR C . n 
C 1 234 LEU 234 234 234 LEU LEU C . n 
C 1 235 THR 235 235 235 THR THR C . n 
C 1 236 VAL 236 236 236 VAL VAL C . n 
C 1 237 ALA 237 237 237 ALA ALA C . n 
C 1 238 ASP 238 238 238 ASP ASP C . n 
C 1 239 VAL 239 239 239 VAL VAL C . n 
C 1 240 ILE 240 240 240 ILE ILE C . n 
C 1 241 VAL 241 241 241 VAL VAL C . n 
C 1 242 LYS 242 242 242 LYS LYR C . n 
C 1 243 LEU 243 243 243 LEU LEU C . n 
C 1 244 GLY 244 244 244 GLY GLY C . n 
C 1 245 PHE 245 245 245 PHE PHE C . n 
C 1 246 SER 246 246 246 SER SER C . n 
C 1 247 THR 247 247 247 THR THR C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 THR 249 249 249 THR THR C . n 
C 1 250 HIS 250 250 250 HIS HIS C . n 
C 1 251 ARG 251 251 251 ARG ARG C . n 
C 1 252 VAL 252 252 252 VAL VAL C . n 
C 1 253 ALA 253 253 253 ALA ALA C . n 
C 1 254 LYS 254 254 254 LYS LYS C . n 
C 1 255 LEU 255 255 255 LEU LEU C . n 
C 1 256 ARG 256 256 256 ARG ARG C . n 
C 1 257 THR 257 257 257 THR THR C . n 
C 1 258 ALA 258 258 258 ALA ALA C . n 
C 1 259 GLU 259 259 259 GLU GLU C . n 
C 1 260 ASP 260 260 260 ASP ASP C . n 
C 1 261 VAL 261 261 261 VAL VAL C . n 
C 1 262 ARG 262 262 262 ARG ARG C . n 
C 1 263 ALA 263 263 263 ALA ALA C . n 
C 1 264 GLY 264 264 264 GLY GLY C . n 
C 1 265 ASP 265 265 265 ASP ASP C . n 
C 1 266 ASP 266 266 266 ASP ASP C . n 
C 1 267 VAL 267 267 267 VAL VAL C . n 
C 1 268 HIS 268 268 268 HIS HIS C . n 
C 1 269 PRO 269 269 269 PRO PRO C . n 
C 1 270 GLU 270 270 270 GLU GLU C . n 
C 1 271 SER 271 271 271 SER SER C . n 
C 1 272 ILE 272 272 272 ILE ILE C . n 
C 1 273 TRP 273 273 273 TRP TRP C . n 
C 1 274 ILE 274 274 274 ILE ILE C . n 
C 1 275 SER 275 275 275 SER SER C . n 
C 1 276 SER 276 276 276 SER SER C . n 
C 1 277 VAL 277 277 277 VAL VAL C . n 
C 1 278 LYS 278 278 278 LYS LYS C . n 
C 1 279 GLN 279 279 279 GLN GLN C . n 
C 1 280 SER 280 280 280 SER SER C . n 
C 1 281 ASP 281 281 281 ASP ASP C . n 
C 1 282 ALA 282 282 282 ALA ALA C . n 
C 1 283 GLY 283 283 283 GLY GLY C . n 
C 1 284 LEU 284 284 284 LEU LEU C . n 
C 1 285 PRO 285 285 285 PRO PRO C . n 
C 1 286 ARG 286 286 286 ARG ARG C . n 
C 1 287 GLU 287 287 287 GLU GLU C . n 
C 1 288 VAL 288 288 288 VAL VAL C . n 
C 1 289 TYR 289 289 289 TYR TYR C . n 
C 1 290 LEU 290 290 290 LEU LEU C . n 
C 1 291 ALA 291 291 ?   ?   ?   C . n 
C 1 292 GLU 292 292 ?   ?   ?   C . n 
C 1 293 GLY 293 293 ?   ?   ?   C . n 
C 1 294 ALA 294 294 ?   ?   ?   C . n 
C 1 295 ALA 295 295 ?   ?   ?   C . n 
C 1 296 VAL 296 296 ?   ?   ?   C . n 
C 1 297 HIS 297 297 ?   ?   ?   C . n 
C 1 298 ASP 298 298 ?   ?   ?   C . n 
C 1 299 ARG 299 299 ?   ?   ?   C . n 
C 1 300 ARG 300 300 ?   ?   ?   C . n 
C 1 301 THR 301 301 ?   ?   ?   C . n 
C 1 302 LYS 302 302 ?   ?   ?   C . n 
C 1 303 PRO 303 303 ?   ?   ?   C . n 
C 1 304 PRO 304 304 ?   ?   ?   C . n 
C 1 305 THR 305 305 ?   ?   ?   C . n 
C 1 306 SER 306 306 ?   ?   ?   C . n 
C 1 307 ALA 307 307 ?   ?   ?   C . n 
C 1 308 ALA 308 308 ?   ?   ?   C . n 
C 1 309 VAL 309 309 ?   ?   ?   C . n 
C 1 310 ALA 310 310 ?   ?   ?   C . n 
C 1 311 SER 311 311 ?   ?   ?   C . n 
C 1 312 PRO 312 312 ?   ?   ?   C . n 
C 1 313 GLU 313 313 ?   ?   ?   C . n 
C 1 314 ALA 314 314 ?   ?   ?   C . n 
C 1 315 PRO 315 315 ?   ?   ?   C . n 
C 1 316 LEU 316 316 ?   ?   ?   C . n 
C 1 317 PRO 317 317 ?   ?   ?   C . n 
C 1 318 PRO 318 318 ?   ?   ?   C . n 
C 1 319 ASP 319 319 ?   ?   ?   C . n 
C 1 320 SER 320 320 ?   ?   ?   C . n 
C 1 321 THR 321 321 ?   ?   ?   C . n 
C 1 322 PRO 322 322 ?   ?   ?   C . n 
C 1 323 LEU 323 323 ?   ?   ?   C . n 
C 1 324 ASP 324 324 ?   ?   ?   C . n 
C 1 325 GLY 325 325 ?   ?   ?   C . n 
C 1 326 GLY 326 326 ?   ?   ?   C . n 
C 1 327 TYR 327 327 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ARG 2   2   ?   ?   ?   D . n 
D 1 3   LEU 3   3   3   LEU ALA D . n 
D 1 4   THR 4   4   4   THR THR D . n 
D 1 5   ASN 5   5   5   ASN ASN D . n 
D 1 6   VAL 6   6   6   VAL VAL D . n 
D 1 7   SER 7   7   7   SER SER D . n 
D 1 8   VAL 8   8   8   VAL VAL D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  TRP 10  10  10  TRP TRP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  ALA 12  12  12  ALA ALA D . n 
D 1 13  THR 13  13  13  THR THR D . n 
D 1 14  LEU 14  14  14  LEU LEU D . n 
D 1 15  SER 15  15  15  SER SER D . n 
D 1 16  ASN 16  16  16  ASN ASN D . n 
D 1 17  ALA 17  17  17  ALA ALA D . n 
D 1 18  GLU 18  18  18  GLU GLU D . n 
D 1 19  HIS 19  19  19  HIS HIS D . n 
D 1 20  GLN 20  20  20  GLN GLN D . n 
D 1 21  LEU 21  21  21  LEU LEU D . n 
D 1 22  ILE 22  22  22  ILE ILE D . n 
D 1 23  PHE 23  23  23  PHE PHE D . n 
D 1 24  TYR 24  24  24  TYR TYR D . n 
D 1 25  PHE 25  25  25  PHE PHE D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  VAL 27  27  27  VAL VAL D . n 
D 1 28  VAL 28  28  28  VAL VAL D . n 
D 1 29  ALA 29  29  29  ALA ALA D . n 
D 1 30  ALA 30  30  30  ALA ALA D . n 
D 1 31  LEU 31  31  31  LEU LEU D . n 
D 1 32  ALA 32  32  32  ALA ALA D . n 
D 1 33  PHE 33  33  33  PHE PHE D . n 
D 1 34  VAL 34  34  34  VAL VAL D . n 
D 1 35  ALA 35  35  35  ALA ALA D . n 
D 1 36  GLY 36  36  36  GLY GLY D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  ILE 38  38  38  ILE ILE D . n 
D 1 39  ARG 39  39  39  ARG ARG D . n 
D 1 40  THR 40  40  40  THR THR D . n 
D 1 41  TYR 41  41  41  TYR TYR D . n 
D 1 42  ILE 42  42  42  ILE ILE D . n 
D 1 43  THR 43  43  43  THR THR D . n 
D 1 44  ARG 44  44  44  ARG ARG D . n 
D 1 45  ASN 45  45  45  ASN ASN D . n 
D 1 46  GLU 46  46  46  GLU GLU D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  GLY 48  48  48  GLY GLY D . n 
D 1 49  SER 49  49  49  SER SER D . n 
D 1 50  ARG 50  50  50  ARG ARG D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ARG 52  52  52  ARG ARG D . n 
D 1 53  THR 53  53  53  THR THR D . n 
D 1 54  ALA 54  54  54  ALA ALA D . n 
D 1 55  VAL 55  55  55  VAL VAL D . n 
D 1 56  SER 56  56  56  SER SER D . n 
D 1 57  ALA 57  57  57  ALA ALA D . n 
D 1 58  ARG 58  58  58  ARG ARG D . n 
D 1 59  LEU 59  59  59  LEU LEU D . n 
D 1 60  GLY 60  60  60  GLY GLY D . n 
D 1 61  MET 61  61  61  MET MET D . n 
D 1 62  LEU 62  62  62  LEU LEU D . n 
D 1 63  GLY 63  63  63  GLY GLY D . n 
D 1 64  VAL 64  64  64  VAL VAL D . n 
D 1 65  ALA 65  65  65  ALA ALA D . n 
D 1 66  LEU 66  66  66  LEU LEU D . n 
D 1 67  LEU 67  67  67  LEU LEU D . n 
D 1 68  ALA 68  68  68  ALA ALA D . n 
D 1 69  TYR 69  69  69  TYR TYR D . n 
D 1 70  ILE 70  70  70  ILE ILE D . n 
D 1 71  LEU 71  71  71  LEU LEU D . n 
D 1 72  ILE 72  72  72  ILE ILE D . n 
D 1 73  ILE 73  73  73  ILE ILE D . n 
D 1 74  VAL 74  74  74  VAL VAL D . n 
D 1 75  ALA 75  75  75  ALA ALA D . n 
D 1 76  PHE 76  76  76  PHE PHE D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  GLY 79  79  79  GLY GLY D . n 
D 1 80  TYR 80  80  80  TYR TYR D . n 
D 1 81  ASP 81  81  81  ASP ASP D . n 
D 1 82  SER 82  82  82  SER SER D . n 
D 1 83  THR 83  83  83  THR THR D . n 
D 1 84  ALA 84  84  84  ALA ALA D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  GLY 86  86  86  GLY GLY D . n 
D 1 87  TRP 87  87  87  TRP TRP D . n 
D 1 88  VAL 88  88  88  VAL VAL D . n 
D 1 89  PRO 89  89  89  PRO PRO D . n 
D 1 90  ASN 90  90  90  ASN ASN D . n 
D 1 91  ASP 91  91  91  ASP ASP D . n 
D 1 92  GLY 92  92  92  GLY GLY D . n 
D 1 93  ALA 93  93  93  ALA ALA D . n 
D 1 94  ILE 94  94  94  ILE ILE D . n 
D 1 95  ASN 95  95  95  ASN ASN D . n 
D 1 96  ILE 96  96  96  ILE ILE D . n 
D 1 97  PHE 97  97  97  PHE PHE D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  THR 99  99  99  THR THR D . n 
D 1 100 ARG 100 100 100 ARG ARG D . n 
D 1 101 TYR 101 101 101 TYR TYR D . n 
D 1 102 ILE 102 102 102 ILE ILE D . n 
D 1 103 GLU 103 103 103 GLU GLU D . n 
D 1 104 TRP 104 104 104 TRP TRP D . n 
D 1 105 THR 105 105 105 THR THR D . n 
D 1 106 VAL 106 106 106 VAL VAL D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 VAL 108 108 108 VAL VAL D . n 
D 1 109 PRO 109 109 109 PRO PRO D . n 
D 1 110 LEU 110 110 110 LEU LEU D . n 
D 1 111 LEU 111 111 111 LEU LEU D . n 
D 1 112 THR 112 112 112 THR THR D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLU 114 114 114 GLU GLU D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 ALA 117 117 117 ALA ALA D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 CYS 119 119 119 CYS CYS D . n 
D 1 120 ALA 120 120 120 ALA ALA D . n 
D 1 121 THR 121 121 121 THR THR D . n 
D 1 122 LEU 122 122 122 LEU LEU D . n 
D 1 123 GLY 123 123 123 GLY GLY D . n 
D 1 124 VAL 124 124 124 VAL VAL D . n 
D 1 125 GLN 125 125 125 GLN GLN D . n 
D 1 126 ALA 126 126 126 ALA ALA D . n 
D 1 127 ARG 127 127 127 ARG ARG D . n 
D 1 128 ARG 128 128 128 ARG ARG D . n 
D 1 129 ASN 129 129 129 ASN ASN D . n 
D 1 130 THR 130 130 130 THR THR D . n 
D 1 131 ALA 131 131 131 ALA ALA D . n 
D 1 132 ILE 132 132 132 ILE ILE D . n 
D 1 133 ALA 133 133 133 ALA ALA D . n 
D 1 134 VAL 134 134 134 VAL VAL D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 ALA 136 136 136 ALA ALA D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 ALA 139 139 139 ALA ALA D . n 
D 1 140 MET 140 140 140 MET MET D . n 
D 1 141 ILE 141 141 141 ILE ILE D . n 
D 1 142 PHE 142 142 142 PHE PHE D . n 
D 1 143 CYS 143 143 143 CYS CYS D . n 
D 1 144 GLY 144 144 144 GLY GLY D . n 
D 1 145 PHE 145 145 145 PHE PHE D . n 
D 1 146 LEU 146 146 146 LEU LEU D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 ALA 148 148 148 ALA ALA D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 VAL 150 150 150 VAL VAL D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ASP 152 152 152 ASP ASP D . n 
D 1 153 ASN 153 153 153 ASN ASN D . n 
D 1 154 GLY 154 154 154 GLY GLY D . n 
D 1 155 THR 155 155 155 THR THR D . n 
D 1 156 ASN 156 156 156 ASN ASN D . n 
D 1 157 THR 157 157 157 THR THR D . n 
D 1 158 GLY 158 158 158 GLY GLY D . n 
D 1 159 ALA 159 159 159 ALA ALA D . n 
D 1 160 PHE 160 160 160 PHE PHE D . n 
D 1 161 ILE 161 161 161 ILE ILE D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 TRP 163 163 163 TRP TRP D . n 
D 1 164 ALA 164 164 164 ALA ALA D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 ILE 166 166 166 ILE ILE D . n 
D 1 167 SER 167 167 167 SER SER D . n 
D 1 168 CYS 168 168 168 CYS CYS D . n 
D 1 169 VAL 169 169 169 VAL VAL D . n 
D 1 170 PHE 170 170 170 PHE PHE D . n 
D 1 171 TRP 171 171 171 TRP TRP D . n 
D 1 172 VAL 172 172 172 VAL VAL D . n 
D 1 173 ILE 173 173 173 ILE ILE D . n 
D 1 174 ALA 174 174 174 ALA ALA D . n 
D 1 175 ASN 175 175 175 ASN ASN D . n 
D 1 176 VAL 176 176 176 VAL VAL D . n 
D 1 177 VAL 177 177 177 VAL VAL D . n 
D 1 178 LEU 178 178 178 LEU LEU D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 ARG 180 180 180 ARG ARG D . n 
D 1 181 ALA 181 181 181 ALA ALA D . n 
D 1 182 VAL 182 182 182 VAL VAL D . n 
D 1 183 ARG 183 183 183 ARG ARG D . n 
D 1 184 GLN 184 184 184 GLN GLN D . n 
D 1 185 SER 185 185 185 SER SER D . n 
D 1 186 LEU 186 186 186 LEU LEU D . n 
D 1 187 PRO 187 187 187 PRO PRO D . n 
D 1 188 THR 188 188 188 THR THR D . n 
D 1 189 LEU 189 189 189 LEU LEU D . n 
D 1 190 THR 190 190 190 THR THR D . n 
D 1 191 PRO 191 191 191 PRO PRO D . n 
D 1 192 GLU 192 192 192 GLU GLU D . n 
D 1 193 SER 193 193 193 SER SER D . n 
D 1 194 HIS 194 194 194 HIS HIS D . n 
D 1 195 THR 195 195 195 THR THR D . n 
D 1 196 MET 196 196 196 MET MET D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 LYS 198 198 198 LYS LYS D . n 
D 1 199 SER 199 199 199 SER SER D . n 
D 1 200 ALA 200 200 200 ALA ALA D . n 
D 1 201 ALA 201 201 201 ALA ALA D . n 
D 1 202 ILE 202 202 202 ILE ILE D . n 
D 1 203 VAL 203 203 203 VAL VAL D . n 
D 1 204 LEU 204 204 204 LEU LEU D . n 
D 1 205 LEU 205 205 205 LEU LEU D . n 
D 1 206 ALA 206 206 206 ALA ALA D . n 
D 1 207 GLY 207 207 207 GLY GLY D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 VAL 209 209 209 VAL VAL D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 TYR 211 211 211 TYR TYR D . n 
D 1 212 PRO 212 212 212 PRO PRO D . n 
D 1 213 ILE 213 213 213 ILE ILE D . n 
D 1 214 VAL 214 214 214 VAL VAL D . n 
D 1 215 TYR 215 215 215 TYR TYR D . n 
D 1 216 PHE 216 216 216 PHE PHE D . n 
D 1 217 LEU 217 217 217 LEU LEU D . n 
D 1 218 PRO 218 218 218 PRO PRO D . n 
D 1 219 LEU 219 219 219 LEU LEU D . n 
D 1 220 PHE 220 220 220 PHE PHE D . n 
D 1 221 GLY 221 221 221 GLY GLY D . n 
D 1 222 ALA 222 222 222 ALA ALA D . n 
D 1 223 SER 223 223 223 SER SER D . n 
D 1 224 GLY 224 224 224 GLY GLY D . n 
D 1 225 GLY 225 225 225 GLY GLY D . n 
D 1 226 LEU 226 226 226 LEU LEU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 THR 228 228 228 THR THR D . n 
D 1 229 THR 229 229 229 THR THR D . n 
D 1 230 ILE 230 230 230 ILE ILE D . n 
D 1 231 LEU 231 231 231 LEU LEU D . n 
D 1 232 ILE 232 232 232 ILE ILE D . n 
D 1 233 THR 233 233 233 THR THR D . n 
D 1 234 LEU 234 234 234 LEU LEU D . n 
D 1 235 THR 235 235 235 THR THR D . n 
D 1 236 VAL 236 236 236 VAL VAL D . n 
D 1 237 ALA 237 237 237 ALA ALA D . n 
D 1 238 ASP 238 238 238 ASP ASP D . n 
D 1 239 VAL 239 239 239 VAL VAL D . n 
D 1 240 ILE 240 240 240 ILE ILE D . n 
D 1 241 VAL 241 241 241 VAL VAL D . n 
D 1 242 LYS 242 242 242 LYS LYR D . n 
D 1 243 LEU 243 243 243 LEU LEU D . n 
D 1 244 GLY 244 244 244 GLY GLY D . n 
D 1 245 PHE 245 245 245 PHE PHE D . n 
D 1 246 SER 246 246 246 SER SER D . n 
D 1 247 THR 247 247 247 THR THR D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 THR 249 249 249 THR THR D . n 
D 1 250 HIS 250 250 250 HIS HIS D . n 
D 1 251 ARG 251 251 251 ARG ARG D . n 
D 1 252 VAL 252 252 252 VAL VAL D . n 
D 1 253 ALA 253 253 253 ALA ALA D . n 
D 1 254 LYS 254 254 254 LYS LYS D . n 
D 1 255 LEU 255 255 255 LEU LEU D . n 
D 1 256 ARG 256 256 256 ARG ARG D . n 
D 1 257 THR 257 257 257 THR THR D . n 
D 1 258 ALA 258 258 258 ALA ALA D . n 
D 1 259 GLU 259 259 259 GLU GLU D . n 
D 1 260 ASP 260 260 260 ASP ASP D . n 
D 1 261 VAL 261 261 261 VAL VAL D . n 
D 1 262 ARG 262 262 262 ARG ARG D . n 
D 1 263 ALA 263 263 263 ALA ALA D . n 
D 1 264 GLY 264 264 264 GLY GLY D . n 
D 1 265 ASP 265 265 265 ASP ASP D . n 
D 1 266 ASP 266 266 266 ASP ASP D . n 
D 1 267 VAL 267 267 267 VAL VAL D . n 
D 1 268 HIS 268 268 268 HIS HIS D . n 
D 1 269 PRO 269 269 269 PRO PRO D . n 
D 1 270 GLU 270 270 270 GLU GLU D . n 
D 1 271 SER 271 271 271 SER SER D . n 
D 1 272 ILE 272 272 272 ILE ILE D . n 
D 1 273 TRP 273 273 273 TRP TRP D . n 
D 1 274 ILE 274 274 274 ILE ILE D . n 
D 1 275 SER 275 275 275 SER SER D . n 
D 1 276 SER 276 276 276 SER SER D . n 
D 1 277 VAL 277 277 277 VAL VAL D . n 
D 1 278 LYS 278 278 278 LYS LYS D . n 
D 1 279 GLN 279 279 279 GLN GLN D . n 
D 1 280 SER 280 280 280 SER SER D . n 
D 1 281 ASP 281 281 281 ASP ASP D . n 
D 1 282 ALA 282 282 282 ALA ALA D . n 
D 1 283 GLY 283 283 283 GLY GLY D . n 
D 1 284 LEU 284 284 284 LEU LEU D . n 
D 1 285 PRO 285 285 285 PRO PRO D . n 
D 1 286 ARG 286 286 286 ARG ARG D . n 
D 1 287 GLU 287 287 287 GLU GLU D . n 
D 1 288 VAL 288 288 288 VAL VAL D . n 
D 1 289 TYR 289 289 289 TYR TYR D . n 
D 1 290 LEU 290 290 290 LEU LEU D . n 
D 1 291 ALA 291 291 291 ALA ALA D . n 
D 1 292 GLU 292 292 ?   ?   ?   D . n 
D 1 293 GLY 293 293 ?   ?   ?   D . n 
D 1 294 ALA 294 294 ?   ?   ?   D . n 
D 1 295 ALA 295 295 ?   ?   ?   D . n 
D 1 296 VAL 296 296 ?   ?   ?   D . n 
D 1 297 HIS 297 297 ?   ?   ?   D . n 
D 1 298 ASP 298 298 ?   ?   ?   D . n 
D 1 299 ARG 299 299 ?   ?   ?   D . n 
D 1 300 ARG 300 300 ?   ?   ?   D . n 
D 1 301 THR 301 301 ?   ?   ?   D . n 
D 1 302 LYS 302 302 ?   ?   ?   D . n 
D 1 303 PRO 303 303 ?   ?   ?   D . n 
D 1 304 PRO 304 304 ?   ?   ?   D . n 
D 1 305 THR 305 305 ?   ?   ?   D . n 
D 1 306 SER 306 306 ?   ?   ?   D . n 
D 1 307 ALA 307 307 ?   ?   ?   D . n 
D 1 308 ALA 308 308 ?   ?   ?   D . n 
D 1 309 VAL 309 309 ?   ?   ?   D . n 
D 1 310 ALA 310 310 ?   ?   ?   D . n 
D 1 311 SER 311 311 ?   ?   ?   D . n 
D 1 312 PRO 312 312 ?   ?   ?   D . n 
D 1 313 GLU 313 313 ?   ?   ?   D . n 
D 1 314 ALA 314 314 ?   ?   ?   D . n 
D 1 315 PRO 315 315 ?   ?   ?   D . n 
D 1 316 LEU 316 316 ?   ?   ?   D . n 
D 1 317 PRO 317 317 ?   ?   ?   D . n 
D 1 318 PRO 318 318 ?   ?   ?   D . n 
D 1 319 ASP 319 319 ?   ?   ?   D . n 
D 1 320 SER 320 320 ?   ?   ?   D . n 
D 1 321 THR 321 321 ?   ?   ?   D . n 
D 1 322 PRO 322 322 ?   ?   ?   D . n 
D 1 323 LEU 323 323 ?   ?   ?   D . n 
D 1 324 ASP 324 324 ?   ?   ?   D . n 
D 1 325 GLY 325 325 ?   ?   ?   D . n 
D 1 326 GLY 326 326 ?   ?   ?   D . n 
D 1 327 TYR 327 327 ?   ?   ?   D . n 
E 1 1   MET 1   1   ?   ?   ?   E . n 
E 1 2   ARG 2   2   ?   ?   ?   E . n 
E 1 3   LEU 3   3   ?   ?   ?   E . n 
E 1 4   THR 4   4   ?   ?   ?   E . n 
E 1 5   ASN 5   5   5   ASN ASN E . n 
E 1 6   VAL 6   6   6   VAL VAL E . n 
E 1 7   SER 7   7   7   SER SER E . n 
E 1 8   VAL 8   8   8   VAL VAL E . n 
E 1 9   PRO 9   9   9   PRO PRO E . n 
E 1 10  TRP 10  10  10  TRP TRP E . n 
E 1 11  GLY 11  11  11  GLY GLY E . n 
E 1 12  ALA 12  12  12  ALA ALA E . n 
E 1 13  THR 13  13  13  THR THR E . n 
E 1 14  LEU 14  14  14  LEU LEU E . n 
E 1 15  SER 15  15  15  SER SER E . n 
E 1 16  ASN 16  16  16  ASN ASN E . n 
E 1 17  ALA 17  17  17  ALA ALA E . n 
E 1 18  GLU 18  18  18  GLU GLU E . n 
E 1 19  HIS 19  19  19  HIS HIS E . n 
E 1 20  GLN 20  20  20  GLN GLN E . n 
E 1 21  LEU 21  21  21  LEU LEU E . n 
E 1 22  ILE 22  22  22  ILE ILE E . n 
E 1 23  PHE 23  23  23  PHE PHE E . n 
E 1 24  TYR 24  24  24  TYR TYR E . n 
E 1 25  PHE 25  25  25  PHE PHE E . n 
E 1 26  LEU 26  26  26  LEU LEU E . n 
E 1 27  VAL 27  27  27  VAL VAL E . n 
E 1 28  VAL 28  28  28  VAL VAL E . n 
E 1 29  ALA 29  29  29  ALA ALA E . n 
E 1 30  ALA 30  30  30  ALA ALA E . n 
E 1 31  LEU 31  31  31  LEU LEU E . n 
E 1 32  ALA 32  32  32  ALA ALA E . n 
E 1 33  PHE 33  33  33  PHE PHE E . n 
E 1 34  VAL 34  34  34  VAL VAL E . n 
E 1 35  ALA 35  35  35  ALA ALA E . n 
E 1 36  GLY 36  36  36  GLY GLY E . n 
E 1 37  PHE 37  37  37  PHE PHE E . n 
E 1 38  ILE 38  38  38  ILE ILE E . n 
E 1 39  ARG 39  39  39  ARG ARG E . n 
E 1 40  THR 40  40  40  THR THR E . n 
E 1 41  TYR 41  41  41  TYR TYR E . n 
E 1 42  ILE 42  42  42  ILE ILE E . n 
E 1 43  THR 43  43  43  THR THR E . n 
E 1 44  ARG 44  44  44  ARG ARG E . n 
E 1 45  ASN 45  45  45  ASN ASN E . n 
E 1 46  GLU 46  46  46  GLU GLU E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  GLY 48  48  48  GLY GLY E . n 
E 1 49  SER 49  49  49  SER SER E . n 
E 1 50  ARG 50  50  50  ARG ARG E . n 
E 1 51  TYR 51  51  51  TYR TYR E . n 
E 1 52  ARG 52  52  52  ARG ARG E . n 
E 1 53  THR 53  53  53  THR THR E . n 
E 1 54  ALA 54  54  54  ALA ALA E . n 
E 1 55  VAL 55  55  55  VAL VAL E . n 
E 1 56  SER 56  56  56  SER SER E . n 
E 1 57  ALA 57  57  57  ALA ALA E . n 
E 1 58  ARG 58  58  58  ARG ARG E . n 
E 1 59  LEU 59  59  59  LEU LEU E . n 
E 1 60  GLY 60  60  60  GLY GLY E . n 
E 1 61  MET 61  61  61  MET MET E . n 
E 1 62  LEU 62  62  62  LEU LEU E . n 
E 1 63  GLY 63  63  63  GLY GLY E . n 
E 1 64  VAL 64  64  64  VAL VAL E . n 
E 1 65  ALA 65  65  65  ALA ALA E . n 
E 1 66  LEU 66  66  66  LEU LEU E . n 
E 1 67  LEU 67  67  67  LEU LEU E . n 
E 1 68  ALA 68  68  68  ALA ALA E . n 
E 1 69  TYR 69  69  69  TYR TYR E . n 
E 1 70  ILE 70  70  70  ILE ILE E . n 
E 1 71  LEU 71  71  71  LEU LEU E . n 
E 1 72  ILE 72  72  72  ILE ILE E . n 
E 1 73  ILE 73  73  73  ILE ILE E . n 
E 1 74  VAL 74  74  74  VAL VAL E . n 
E 1 75  ALA 75  75  75  ALA ALA E . n 
E 1 76  PHE 76  76  76  PHE PHE E . n 
E 1 77  LEU 77  77  77  LEU LEU E . n 
E 1 78  LEU 78  78  78  LEU LEU E . n 
E 1 79  GLY 79  79  79  GLY GLY E . n 
E 1 80  TYR 80  80  80  TYR TYR E . n 
E 1 81  ASP 81  81  81  ASP ASP E . n 
E 1 82  SER 82  82  82  SER SER E . n 
E 1 83  THR 83  83  83  THR THR E . n 
E 1 84  ALA 84  84  84  ALA ALA E . n 
E 1 85  GLY 85  85  85  GLY GLY E . n 
E 1 86  GLY 86  86  86  GLY GLY E . n 
E 1 87  TRP 87  87  87  TRP TRP E . n 
E 1 88  VAL 88  88  88  VAL VAL E . n 
E 1 89  PRO 89  89  89  PRO PRO E . n 
E 1 90  ASN 90  90  90  ASN ASN E . n 
E 1 91  ASP 91  91  91  ASP ASP E . n 
E 1 92  GLY 92  92  92  GLY GLY E . n 
E 1 93  ALA 93  93  93  ALA ALA E . n 
E 1 94  ILE 94  94  94  ILE ILE E . n 
E 1 95  ASN 95  95  95  ASN ASN E . n 
E 1 96  ILE 96  96  96  ILE ILE E . n 
E 1 97  PHE 97  97  97  PHE PHE E . n 
E 1 98  SER 98  98  98  SER SER E . n 
E 1 99  THR 99  99  99  THR THR E . n 
E 1 100 ARG 100 100 100 ARG ARG E . n 
E 1 101 TYR 101 101 101 TYR TYR E . n 
E 1 102 ILE 102 102 102 ILE ILE E . n 
E 1 103 GLU 103 103 103 GLU GLU E . n 
E 1 104 TRP 104 104 104 TRP TRP E . n 
E 1 105 THR 105 105 105 THR THR E . n 
E 1 106 VAL 106 106 106 VAL VAL E . n 
E 1 107 SER 107 107 107 SER SER E . n 
E 1 108 VAL 108 108 108 VAL VAL E . n 
E 1 109 PRO 109 109 109 PRO PRO E . n 
E 1 110 LEU 110 110 110 LEU LEU E . n 
E 1 111 LEU 111 111 111 LEU LEU E . n 
E 1 112 THR 112 112 112 THR THR E . n 
E 1 113 ILE 113 113 113 ILE ILE E . n 
E 1 114 GLU 114 114 114 GLU GLU E . n 
E 1 115 LEU 115 115 115 LEU LEU E . n 
E 1 116 LEU 116 116 116 LEU LEU E . n 
E 1 117 ALA 117 117 117 ALA ALA E . n 
E 1 118 VAL 118 118 118 VAL VAL E . n 
E 1 119 CYS 119 119 119 CYS CYS E . n 
E 1 120 ALA 120 120 120 ALA ALA E . n 
E 1 121 THR 121 121 121 THR THR E . n 
E 1 122 LEU 122 122 122 LEU LEU E . n 
E 1 123 GLY 123 123 123 GLY GLY E . n 
E 1 124 VAL 124 124 124 VAL VAL E . n 
E 1 125 GLN 125 125 125 GLN GLN E . n 
E 1 126 ALA 126 126 126 ALA ALA E . n 
E 1 127 ARG 127 127 127 ARG ARG E . n 
E 1 128 ARG 128 128 128 ARG ARG E . n 
E 1 129 ASN 129 129 129 ASN ASN E . n 
E 1 130 THR 130 130 130 THR THR E . n 
E 1 131 ALA 131 131 131 ALA ALA E . n 
E 1 132 ILE 132 132 132 ILE ILE E . n 
E 1 133 ALA 133 133 133 ALA ALA E . n 
E 1 134 VAL 134 134 134 VAL VAL E . n 
E 1 135 THR 135 135 135 THR THR E . n 
E 1 136 ALA 136 136 136 ALA ALA E . n 
E 1 137 THR 137 137 137 THR THR E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ALA 139 139 139 ALA ALA E . n 
E 1 140 MET 140 140 140 MET MET E . n 
E 1 141 ILE 141 141 141 ILE ILE E . n 
E 1 142 PHE 142 142 142 PHE PHE E . n 
E 1 143 CYS 143 143 143 CYS CYS E . n 
E 1 144 GLY 144 144 144 GLY GLY E . n 
E 1 145 PHE 145 145 145 PHE PHE E . n 
E 1 146 LEU 146 146 146 LEU LEU E . n 
E 1 147 GLY 147 147 147 GLY GLY E . n 
E 1 148 ALA 148 148 148 ALA ALA E . n 
E 1 149 ILE 149 149 149 ILE ILE E . n 
E 1 150 VAL 150 150 150 VAL VAL E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 ASP 152 152 152 ASP ASP E . n 
E 1 153 ASN 153 153 153 ASN ASN E . n 
E 1 154 GLY 154 154 154 GLY GLY E . n 
E 1 155 THR 155 155 155 THR THR E . n 
E 1 156 ASN 156 156 156 ASN ASN E . n 
E 1 157 THR 157 157 157 THR THR E . n 
E 1 158 GLY 158 158 158 GLY GLY E . n 
E 1 159 ALA 159 159 159 ALA ALA E . n 
E 1 160 PHE 160 160 160 PHE PHE E . n 
E 1 161 ILE 161 161 161 ILE ILE E . n 
E 1 162 LEU 162 162 162 LEU LEU E . n 
E 1 163 TRP 163 163 163 TRP TRP E . n 
E 1 164 ALA 164 164 164 ALA ALA E . n 
E 1 165 VAL 165 165 165 VAL VAL E . n 
E 1 166 ILE 166 166 166 ILE ILE E . n 
E 1 167 SER 167 167 167 SER SER E . n 
E 1 168 CYS 168 168 168 CYS CYS E . n 
E 1 169 VAL 169 169 169 VAL VAL E . n 
E 1 170 PHE 170 170 170 PHE PHE E . n 
E 1 171 TRP 171 171 171 TRP TRP E . n 
E 1 172 VAL 172 172 172 VAL VAL E . n 
E 1 173 ILE 173 173 173 ILE ILE E . n 
E 1 174 ALA 174 174 174 ALA ALA E . n 
E 1 175 ASN 175 175 175 ASN ASN E . n 
E 1 176 VAL 176 176 176 VAL VAL E . n 
E 1 177 VAL 177 177 177 VAL VAL E . n 
E 1 178 LEU 178 178 178 LEU LEU E . n 
E 1 179 ILE 179 179 179 ILE ILE E . n 
E 1 180 ARG 180 180 180 ARG ARG E . n 
E 1 181 ALA 181 181 181 ALA ALA E . n 
E 1 182 VAL 182 182 182 VAL VAL E . n 
E 1 183 ARG 183 183 183 ARG ARG E . n 
E 1 184 GLN 184 184 184 GLN GLN E . n 
E 1 185 SER 185 185 185 SER SER E . n 
E 1 186 LEU 186 186 186 LEU LEU E . n 
E 1 187 PRO 187 187 187 PRO PRO E . n 
E 1 188 THR 188 188 188 THR THR E . n 
E 1 189 LEU 189 189 189 LEU LEU E . n 
E 1 190 THR 190 190 190 THR THR E . n 
E 1 191 PRO 191 191 191 PRO PRO E . n 
E 1 192 GLU 192 192 192 GLU GLU E . n 
E 1 193 SER 193 193 193 SER SER E . n 
E 1 194 HIS 194 194 194 HIS HIS E . n 
E 1 195 THR 195 195 195 THR THR E . n 
E 1 196 MET 196 196 196 MET MET E . n 
E 1 197 LEU 197 197 197 LEU LEU E . n 
E 1 198 LYS 198 198 198 LYS LYS E . n 
E 1 199 SER 199 199 199 SER SER E . n 
E 1 200 ALA 200 200 200 ALA ALA E . n 
E 1 201 ALA 201 201 201 ALA ALA E . n 
E 1 202 ILE 202 202 202 ILE ILE E . n 
E 1 203 VAL 203 203 203 VAL VAL E . n 
E 1 204 LEU 204 204 204 LEU LEU E . n 
E 1 205 LEU 205 205 205 LEU LEU E . n 
E 1 206 ALA 206 206 206 ALA ALA E . n 
E 1 207 GLY 207 207 207 GLY GLY E . n 
E 1 208 TRP 208 208 208 TRP TRP E . n 
E 1 209 VAL 209 209 209 VAL VAL E . n 
E 1 210 VAL 210 210 210 VAL VAL E . n 
E 1 211 TYR 211 211 211 TYR TYR E . n 
E 1 212 PRO 212 212 212 PRO PRO E . n 
E 1 213 ILE 213 213 213 ILE ILE E . n 
E 1 214 VAL 214 214 214 VAL VAL E . n 
E 1 215 TYR 215 215 215 TYR TYR E . n 
E 1 216 PHE 216 216 216 PHE PHE E . n 
E 1 217 LEU 217 217 217 LEU LEU E . n 
E 1 218 PRO 218 218 218 PRO PRO E . n 
E 1 219 LEU 219 219 219 LEU LEU E . n 
E 1 220 PHE 220 220 220 PHE PHE E . n 
E 1 221 GLY 221 221 221 GLY GLY E . n 
E 1 222 ALA 222 222 222 ALA ALA E . n 
E 1 223 SER 223 223 223 SER SER E . n 
E 1 224 GLY 224 224 224 GLY GLY E . n 
E 1 225 GLY 225 225 225 GLY GLY E . n 
E 1 226 LEU 226 226 226 LEU LEU E . n 
E 1 227 THR 227 227 227 THR THR E . n 
E 1 228 THR 228 228 228 THR THR E . n 
E 1 229 THR 229 229 229 THR THR E . n 
E 1 230 ILE 230 230 230 ILE ILE E . n 
E 1 231 LEU 231 231 231 LEU LEU E . n 
E 1 232 ILE 232 232 232 ILE ILE E . n 
E 1 233 THR 233 233 233 THR THR E . n 
E 1 234 LEU 234 234 234 LEU LEU E . n 
E 1 235 THR 235 235 235 THR THR E . n 
E 1 236 VAL 236 236 236 VAL VAL E . n 
E 1 237 ALA 237 237 237 ALA ALA E . n 
E 1 238 ASP 238 238 238 ASP ASP E . n 
E 1 239 VAL 239 239 239 VAL VAL E . n 
E 1 240 ILE 240 240 240 ILE ILE E . n 
E 1 241 VAL 241 241 241 VAL VAL E . n 
E 1 242 LYS 242 242 242 LYS LYR E . n 
E 1 243 LEU 243 243 243 LEU LEU E . n 
E 1 244 GLY 244 244 244 GLY GLY E . n 
E 1 245 PHE 245 245 245 PHE PHE E . n 
E 1 246 SER 246 246 246 SER SER E . n 
E 1 247 THR 247 247 247 THR THR E . n 
E 1 248 GLN 248 248 248 GLN GLN E . n 
E 1 249 THR 249 249 249 THR THR E . n 
E 1 250 HIS 250 250 250 HIS HIS E . n 
E 1 251 ARG 251 251 251 ARG ARG E . n 
E 1 252 VAL 252 252 252 VAL VAL E . n 
E 1 253 ALA 253 253 253 ALA ALA E . n 
E 1 254 LYS 254 254 254 LYS LYS E . n 
E 1 255 LEU 255 255 255 LEU LEU E . n 
E 1 256 ARG 256 256 256 ARG ARG E . n 
E 1 257 THR 257 257 257 THR THR E . n 
E 1 258 ALA 258 258 258 ALA ALA E . n 
E 1 259 GLU 259 259 259 GLU GLU E . n 
E 1 260 ASP 260 260 260 ASP ASP E . n 
E 1 261 VAL 261 261 261 VAL VAL E . n 
E 1 262 ARG 262 262 262 ARG ARG E . n 
E 1 263 ALA 263 263 263 ALA ALA E . n 
E 1 264 GLY 264 264 264 GLY GLY E . n 
E 1 265 ASP 265 265 265 ASP ASP E . n 
E 1 266 ASP 266 266 266 ASP ASP E . n 
E 1 267 VAL 267 267 267 VAL VAL E . n 
E 1 268 HIS 268 268 268 HIS HIS E . n 
E 1 269 PRO 269 269 269 PRO PRO E . n 
E 1 270 GLU 270 270 270 GLU GLU E . n 
E 1 271 SER 271 271 271 SER SER E . n 
E 1 272 ILE 272 272 272 ILE ILE E . n 
E 1 273 TRP 273 273 273 TRP TRP E . n 
E 1 274 ILE 274 274 274 ILE ILE E . n 
E 1 275 SER 275 275 275 SER SER E . n 
E 1 276 SER 276 276 276 SER SER E . n 
E 1 277 VAL 277 277 277 VAL VAL E . n 
E 1 278 LYS 278 278 278 LYS LYS E . n 
E 1 279 GLN 279 279 279 GLN GLN E . n 
E 1 280 SER 280 280 280 SER SER E . n 
E 1 281 ASP 281 281 281 ASP ASP E . n 
E 1 282 ALA 282 282 282 ALA ALA E . n 
E 1 283 GLY 283 283 283 GLY GLY E . n 
E 1 284 LEU 284 284 284 LEU LEU E . n 
E 1 285 PRO 285 285 285 PRO PRO E . n 
E 1 286 ARG 286 286 286 ARG ARG E . n 
E 1 287 GLU 287 287 287 GLU GLU E . n 
E 1 288 VAL 288 288 288 VAL VAL E . n 
E 1 289 TYR 289 289 289 TYR TYR E . n 
E 1 290 LEU 290 290 290 LEU LEU E . n 
E 1 291 ALA 291 291 ?   ?   ?   E . n 
E 1 292 GLU 292 292 ?   ?   ?   E . n 
E 1 293 GLY 293 293 ?   ?   ?   E . n 
E 1 294 ALA 294 294 ?   ?   ?   E . n 
E 1 295 ALA 295 295 ?   ?   ?   E . n 
E 1 296 VAL 296 296 ?   ?   ?   E . n 
E 1 297 HIS 297 297 ?   ?   ?   E . n 
E 1 298 ASP 298 298 ?   ?   ?   E . n 
E 1 299 ARG 299 299 ?   ?   ?   E . n 
E 1 300 ARG 300 300 ?   ?   ?   E . n 
E 1 301 THR 301 301 ?   ?   ?   E . n 
E 1 302 LYS 302 302 ?   ?   ?   E . n 
E 1 303 PRO 303 303 ?   ?   ?   E . n 
E 1 304 PRO 304 304 ?   ?   ?   E . n 
E 1 305 THR 305 305 ?   ?   ?   E . n 
E 1 306 SER 306 306 ?   ?   ?   E . n 
E 1 307 ALA 307 307 ?   ?   ?   E . n 
E 1 308 ALA 308 308 ?   ?   ?   E . n 
E 1 309 VAL 309 309 ?   ?   ?   E . n 
E 1 310 ALA 310 310 ?   ?   ?   E . n 
E 1 311 SER 311 311 ?   ?   ?   E . n 
E 1 312 PRO 312 312 ?   ?   ?   E . n 
E 1 313 GLU 313 313 ?   ?   ?   E . n 
E 1 314 ALA 314 314 ?   ?   ?   E . n 
E 1 315 PRO 315 315 ?   ?   ?   E . n 
E 1 316 LEU 316 316 ?   ?   ?   E . n 
E 1 317 PRO 317 317 ?   ?   ?   E . n 
E 1 318 PRO 318 318 ?   ?   ?   E . n 
E 1 319 ASP 319 319 ?   ?   ?   E . n 
E 1 320 SER 320 320 ?   ?   ?   E . n 
E 1 321 THR 321 321 ?   ?   ?   E . n 
E 1 322 PRO 322 322 ?   ?   ?   E . n 
E 1 323 LEU 323 323 ?   ?   ?   E . n 
E 1 324 ASP 324 324 ?   ?   ?   E . n 
E 1 325 GLY 325 325 ?   ?   ?   E . n 
E 1 326 GLY 326 326 ?   ?   ?   E . n 
E 1 327 TYR 327 327 ?   ?   ?   E . 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 
F  2 LFA 1 401 301 LFA LFA A . 
G  2 LFA 1 402 302 LFA LFA A . 
H  3 PO4 1 403 2   PO4 PO4 A . 
I  2 LFA 1 404 1   LFA LFA A . 
J  2 LFA 1 405 5   LFA LFA A . 
K  2 LFA 1 406 6   LFA LFA A . 
L  4 RET 1 407 242 RET LYR A . 
M  2 LFA 1 401 301 LFA LFA B . 
N  2 LFA 1 402 302 LFA LFA B . 
O  3 PO4 1 403 3   PO4 PO4 B . 
P  4 RET 1 404 242 RET LYR B . 
Q  2 LFA 1 401 301 LFA LFA C . 
R  3 PO4 1 402 4   PO4 PO4 C . 
S  2 LFA 1 403 3   LFA LFA C . 
T  4 RET 1 404 242 RET LYR C . 
U  5 OLA 1 401 301 OLA OLA D . 
V  3 PO4 1 402 5   PO4 PO4 D . 
W  2 LFA 1 403 4   LFA LFA D . 
X  2 LFA 1 404 7   LFA LFA D . 
Y  2 LFA 1 405 8   LFA LFA D . 
Z  4 RET 1 406 242 RET LYR D . 
AA 2 LFA 1 401 301 LFA LFA E . 
BA 3 PO4 1 402 1   PO4 PO4 E . 
CA 2 LFA 1 403 2   LFA LFA E . 
DA 4 RET 1 404 242 RET LYR E . 
EA 6 HOH 1 501 26  HOH HOH A . 
EA 6 HOH 2 502 8   HOH HOH A . 
EA 6 HOH 3 503 23  HOH HOH A . 
EA 6 HOH 4 504 6   HOH HOH A . 
FA 6 HOH 1 501 16  HOH HOH B . 
FA 6 HOH 2 502 30  HOH HOH B . 
FA 6 HOH 3 503 13  HOH HOH B . 
FA 6 HOH 4 504 3   HOH HOH B . 
FA 6 HOH 5 505 27  HOH HOH B . 
FA 6 HOH 6 506 12  HOH HOH B . 
FA 6 HOH 7 507 20  HOH HOH B . 
FA 6 HOH 8 508 9   HOH HOH B . 
FA 6 HOH 9 509 17  HOH HOH B . 
GA 6 HOH 1 501 24  HOH HOH C . 
GA 6 HOH 2 502 1   HOH HOH C . 
GA 6 HOH 3 503 21  HOH HOH C . 
GA 6 HOH 4 504 10  HOH HOH C . 
GA 6 HOH 5 505 18  HOH HOH C . 
GA 6 HOH 6 506 2   HOH HOH C . 
HA 6 HOH 1 501 29  HOH HOH D . 
HA 6 HOH 2 502 25  HOH HOH D . 
HA 6 HOH 3 503 19  HOH HOH D . 
HA 6 HOH 4 504 4   HOH HOH D . 
HA 6 HOH 5 505 14  HOH HOH D . 
HA 6 HOH 6 506 7   HOH HOH D . 
HA 6 HOH 7 507 11  HOH HOH D . 
IA 6 HOH 1 501 28  HOH HOH E . 
IA 6 HOH 2 502 22  HOH HOH E . 
IA 6 HOH 3 503 15  HOH HOH E . 
IA 6 HOH 4 504 31  HOH HOH E . 
IA 6 HOH 5 505 5   HOH HOH E . 
# 
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 THR 4   ? OG1 ? A  THR 4   OG1 
2   1 Y 1 A THR 4   ? CG2 ? A  THR 4   CG2 
3   1 Y 1 A GLN 125 ? CG  ? A  GLN 125 CG  
4   1 Y 1 A GLN 125 ? CD  ? A  GLN 125 CD  
5   1 Y 1 A GLN 125 ? OE1 ? A  GLN 125 OE1 
6   1 Y 1 A GLN 125 ? NE2 ? A  GLN 125 NE2 
7   1 Y 1 A ARG 127 ? CG  ? A  ARG 127 CG  
8   1 Y 1 A ARG 127 ? CD  ? A  ARG 127 CD  
9   1 Y 1 A ARG 127 ? NE  ? A  ARG 127 NE  
10  1 Y 1 A ARG 127 ? CZ  ? A  ARG 127 CZ  
11  1 Y 1 A ARG 127 ? NH1 ? A  ARG 127 NH1 
12  1 Y 1 A ARG 127 ? NH2 ? A  ARG 127 NH2 
13  1 Y 1 A ARG 128 ? CG  ? A  ARG 128 CG  
14  1 Y 1 A ARG 128 ? CD  ? A  ARG 128 CD  
15  1 Y 1 A ARG 128 ? NE  ? A  ARG 128 NE  
16  1 Y 1 A ARG 128 ? CZ  ? A  ARG 128 CZ  
17  1 Y 1 A ARG 128 ? NH1 ? A  ARG 128 NH1 
18  1 Y 1 A ARG 128 ? NH2 ? A  ARG 128 NH2 
19  1 Y 1 A ARG 180 ? CZ  ? A  ARG 180 CZ  
20  1 Y 1 A ARG 180 ? NH1 ? A  ARG 180 NH1 
21  1 Y 1 A ARG 180 ? NH2 ? A  ARG 180 NH2 
22  1 Y 1 A LYS 198 ? CG  ? A  LYS 198 CG  
23  1 Y 1 A LYS 198 ? CD  ? A  LYS 198 CD  
24  1 Y 1 A LYS 198 ? CE  ? A  LYS 198 CE  
25  1 Y 1 A LYS 198 ? NZ  ? A  LYS 198 NZ  
26  1 Y 1 A ARG 251 ? CG  ? A  ARG 251 CG  
27  1 Y 1 A ARG 251 ? CD  ? A  ARG 251 CD  
28  1 Y 1 A ARG 251 ? NE  ? A  ARG 251 NE  
29  1 Y 1 A ARG 251 ? CZ  ? A  ARG 251 CZ  
30  1 Y 1 A ARG 251 ? NH1 ? A  ARG 251 NH1 
31  1 Y 1 A ARG 251 ? NH2 ? A  ARG 251 NH2 
32  1 Y 1 B ARG 39  ? CZ  ? B  ARG 39  CZ  
33  1 Y 1 B ARG 39  ? NH1 ? B  ARG 39  NH1 
34  1 Y 1 B ARG 39  ? NH2 ? B  ARG 39  NH2 
35  1 Y 1 B GLN 125 ? CG  ? B  GLN 125 CG  
36  1 Y 1 B GLN 125 ? CD  ? B  GLN 125 CD  
37  1 Y 1 B GLN 125 ? OE1 ? B  GLN 125 OE1 
38  1 Y 1 B GLN 125 ? NE2 ? B  GLN 125 NE2 
39  1 Y 1 B ARG 127 ? CG  ? B  ARG 127 CG  
40  1 Y 1 B ARG 127 ? CD  ? B  ARG 127 CD  
41  1 Y 1 B ARG 127 ? NE  ? B  ARG 127 NE  
42  1 Y 1 B ARG 127 ? CZ  ? B  ARG 127 CZ  
43  1 Y 1 B ARG 127 ? NH1 ? B  ARG 127 NH1 
44  1 Y 1 B ARG 127 ? NH2 ? B  ARG 127 NH2 
45  1 Y 1 B ARG 128 ? CG  ? B  ARG 128 CG  
46  1 Y 1 B ARG 128 ? CD  ? B  ARG 128 CD  
47  1 Y 1 B ARG 128 ? NE  ? B  ARG 128 NE  
48  1 Y 1 B ARG 128 ? CZ  ? B  ARG 128 CZ  
49  1 Y 1 B ARG 128 ? NH1 ? B  ARG 128 NH1 
50  1 Y 1 B ARG 128 ? NH2 ? B  ARG 128 NH2 
51  1 Y 1 B LYS 198 ? CG  ? B  LYS 198 CG  
52  1 Y 1 B LYS 198 ? CD  ? B  LYS 198 CD  
53  1 Y 1 B LYS 198 ? CE  ? B  LYS 198 CE  
54  1 Y 1 B LYS 198 ? NZ  ? B  LYS 198 NZ  
55  1 Y 1 B ARG 251 ? CG  ? B  ARG 251 CG  
56  1 Y 1 B ARG 251 ? CD  ? B  ARG 251 CD  
57  1 Y 1 B ARG 251 ? NE  ? B  ARG 251 NE  
58  1 Y 1 B ARG 251 ? CZ  ? B  ARG 251 CZ  
59  1 Y 1 B ARG 251 ? NH1 ? B  ARG 251 NH1 
60  1 Y 1 B ARG 251 ? NH2 ? B  ARG 251 NH2 
61  1 Y 1 B ARG 286 ? CG  ? B  ARG 286 CG  
62  1 Y 1 B ARG 286 ? CD  ? B  ARG 286 CD  
63  1 Y 1 B ARG 286 ? NE  ? B  ARG 286 NE  
64  1 Y 1 B ARG 286 ? CZ  ? B  ARG 286 CZ  
65  1 Y 1 B ARG 286 ? NH1 ? B  ARG 286 NH1 
66  1 Y 1 B ARG 286 ? NH2 ? B  ARG 286 NH2 
67  1 Y 1 C THR 4   ? OG1 ? C  THR 4   OG1 
68  1 Y 1 C THR 4   ? CG2 ? C  THR 4   CG2 
69  1 Y 1 C ASN 5   ? CG  ? C  ASN 5   CG  
70  1 Y 1 C ASN 5   ? OD1 ? C  ASN 5   OD1 
71  1 Y 1 C ASN 5   ? ND2 ? C  ASN 5   ND2 
72  1 Y 1 C ARG 39  ? CD  ? C  ARG 39  CD  
73  1 Y 1 C ARG 39  ? NE  ? C  ARG 39  NE  
74  1 Y 1 C ARG 39  ? CZ  ? C  ARG 39  CZ  
75  1 Y 1 C ARG 39  ? NH1 ? C  ARG 39  NH1 
76  1 Y 1 C ARG 39  ? NH2 ? C  ARG 39  NH2 
77  1 Y 1 C GLN 125 ? CG  ? C  GLN 125 CG  
78  1 Y 1 C GLN 125 ? CD  ? C  GLN 125 CD  
79  1 Y 1 C GLN 125 ? OE1 ? C  GLN 125 OE1 
80  1 Y 1 C GLN 125 ? NE2 ? C  GLN 125 NE2 
81  1 Y 1 C ARG 127 ? CG  ? C  ARG 127 CG  
82  1 Y 1 C ARG 127 ? CD  ? C  ARG 127 CD  
83  1 Y 1 C ARG 127 ? NE  ? C  ARG 127 NE  
84  1 Y 1 C ARG 127 ? CZ  ? C  ARG 127 CZ  
85  1 Y 1 C ARG 127 ? NH1 ? C  ARG 127 NH1 
86  1 Y 1 C ARG 127 ? NH2 ? C  ARG 127 NH2 
87  1 Y 1 C ARG 128 ? CG  ? C  ARG 128 CG  
88  1 Y 1 C ARG 128 ? CD  ? C  ARG 128 CD  
89  1 Y 1 C ARG 128 ? NE  ? C  ARG 128 NE  
90  1 Y 1 C ARG 128 ? CZ  ? C  ARG 128 CZ  
91  1 Y 1 C ARG 128 ? NH1 ? C  ARG 128 NH1 
92  1 Y 1 C ARG 128 ? NH2 ? C  ARG 128 NH2 
93  1 Y 1 C ARG 180 ? CG  ? C  ARG 180 CG  
94  1 Y 1 C ARG 180 ? CD  ? C  ARG 180 CD  
95  1 Y 1 C ARG 180 ? NE  ? C  ARG 180 NE  
96  1 Y 1 C ARG 180 ? CZ  ? C  ARG 180 CZ  
97  1 Y 1 C ARG 180 ? NH1 ? C  ARG 180 NH1 
98  1 Y 1 C ARG 180 ? NH2 ? C  ARG 180 NH2 
99  1 Y 1 C GLU 192 ? CG  ? C  GLU 192 CG  
100 1 Y 1 C GLU 192 ? CD  ? C  GLU 192 CD  
101 1 Y 1 C GLU 192 ? OE1 ? C  GLU 192 OE1 
102 1 Y 1 C GLU 192 ? OE2 ? C  GLU 192 OE2 
103 1 Y 1 C LYS 198 ? CD  ? C  LYS 198 CD  
104 1 Y 1 C LYS 198 ? CE  ? C  LYS 198 CE  
105 1 Y 1 C LYS 198 ? NZ  ? C  LYS 198 NZ  
106 1 Y 1 C ARG 251 ? NE  ? C  ARG 251 NE  
107 1 Y 1 C ARG 251 ? CZ  ? C  ARG 251 CZ  
108 1 Y 1 C ARG 251 ? NH1 ? C  ARG 251 NH1 
109 1 Y 1 C ARG 251 ? NH2 ? C  ARG 251 NH2 
110 1 Y 1 D LEU 3   ? CG  ? D  LEU 3   CG  
111 1 Y 1 D LEU 3   ? CD1 ? D  LEU 3   CD1 
112 1 Y 1 D LEU 3   ? CD2 ? D  LEU 3   CD2 
113 1 Y 1 D ARG 39  ? CD  ? D  ARG 39  CD  
114 1 Y 1 D ARG 39  ? NE  ? D  ARG 39  NE  
115 1 Y 1 D ARG 39  ? CZ  ? D  ARG 39  CZ  
116 1 Y 1 D ARG 39  ? NH1 ? D  ARG 39  NH1 
117 1 Y 1 D ARG 39  ? NH2 ? D  ARG 39  NH2 
118 1 Y 1 D GLN 125 ? CG  ? D  GLN 125 CG  
119 1 Y 1 D GLN 125 ? CD  ? D  GLN 125 CD  
120 1 Y 1 D GLN 125 ? OE1 ? D  GLN 125 OE1 
121 1 Y 1 D GLN 125 ? NE2 ? D  GLN 125 NE2 
122 1 Y 1 D ARG 127 ? CG  ? D  ARG 127 CG  
123 1 Y 1 D ARG 127 ? CD  ? D  ARG 127 CD  
124 1 Y 1 D ARG 127 ? NE  ? D  ARG 127 NE  
125 1 Y 1 D ARG 127 ? CZ  ? D  ARG 127 CZ  
126 1 Y 1 D ARG 127 ? NH1 ? D  ARG 127 NH1 
127 1 Y 1 D ARG 127 ? NH2 ? D  ARG 127 NH2 
128 1 Y 1 D ARG 128 ? CG  ? D  ARG 128 CG  
129 1 Y 1 D ARG 128 ? CD  ? D  ARG 128 CD  
130 1 Y 1 D ARG 128 ? NE  ? D  ARG 128 NE  
131 1 Y 1 D ARG 128 ? CZ  ? D  ARG 128 CZ  
132 1 Y 1 D ARG 128 ? NH1 ? D  ARG 128 NH1 
133 1 Y 1 D ARG 128 ? NH2 ? D  ARG 128 NH2 
134 1 Y 1 D ARG 180 ? CG  ? D  ARG 180 CG  
135 1 Y 1 D ARG 180 ? CD  ? D  ARG 180 CD  
136 1 Y 1 D ARG 180 ? NE  ? D  ARG 180 NE  
137 1 Y 1 D ARG 180 ? CZ  ? D  ARG 180 CZ  
138 1 Y 1 D ARG 180 ? NH1 ? D  ARG 180 NH1 
139 1 Y 1 D ARG 180 ? NH2 ? D  ARG 180 NH2 
140 1 Y 1 D ARG 183 ? CD  ? D  ARG 183 CD  
141 1 Y 1 D ARG 183 ? NE  ? D  ARG 183 NE  
142 1 Y 1 D ARG 183 ? CZ  ? D  ARG 183 CZ  
143 1 Y 1 D ARG 183 ? NH1 ? D  ARG 183 NH1 
144 1 Y 1 D ARG 183 ? NH2 ? D  ARG 183 NH2 
145 1 Y 1 D GLU 192 ? CG  ? D  GLU 192 CG  
146 1 Y 1 D GLU 192 ? CD  ? D  GLU 192 CD  
147 1 Y 1 D GLU 192 ? OE1 ? D  GLU 192 OE1 
148 1 Y 1 D GLU 192 ? OE2 ? D  GLU 192 OE2 
149 1 Y 1 D LYS 198 ? CD  ? D  LYS 198 CD  
150 1 Y 1 D LYS 198 ? CE  ? D  LYS 198 CE  
151 1 Y 1 D LYS 198 ? NZ  ? D  LYS 198 NZ  
152 1 Y 1 D ARG 251 ? CG  ? D  ARG 251 CG  
153 1 Y 1 D ARG 251 ? CD  ? D  ARG 251 CD  
154 1 Y 1 D ARG 251 ? NE  ? D  ARG 251 NE  
155 1 Y 1 D ARG 251 ? CZ  ? D  ARG 251 CZ  
156 1 Y 1 D ARG 251 ? NH1 ? D  ARG 251 NH1 
157 1 Y 1 D ARG 251 ? NH2 ? D  ARG 251 NH2 
158 1 Y 1 D ARG 286 ? CG  ? D  ARG 286 CG  
159 1 Y 1 D ARG 286 ? CD  ? D  ARG 286 CD  
160 1 Y 1 D ARG 286 ? NE  ? D  ARG 286 NE  
161 1 Y 1 D ARG 286 ? CZ  ? D  ARG 286 CZ  
162 1 Y 1 D ARG 286 ? NH1 ? D  ARG 286 NH1 
163 1 Y 1 D ARG 286 ? NH2 ? D  ARG 286 NH2 
164 1 Y 1 E GLN 125 ? CG  ? E  GLN 125 CG  
165 1 Y 1 E GLN 125 ? CD  ? E  GLN 125 CD  
166 1 Y 1 E GLN 125 ? OE1 ? E  GLN 125 OE1 
167 1 Y 1 E GLN 125 ? NE2 ? E  GLN 125 NE2 
168 1 Y 1 E ARG 127 ? CG  ? E  ARG 127 CG  
169 1 Y 1 E ARG 127 ? CD  ? E  ARG 127 CD  
170 1 Y 1 E ARG 127 ? NE  ? E  ARG 127 NE  
171 1 Y 1 E ARG 127 ? CZ  ? E  ARG 127 CZ  
172 1 Y 1 E ARG 127 ? NH1 ? E  ARG 127 NH1 
173 1 Y 1 E ARG 127 ? NH2 ? E  ARG 127 NH2 
174 1 Y 1 E ARG 128 ? CG  ? E  ARG 128 CG  
175 1 Y 1 E ARG 128 ? CD  ? E  ARG 128 CD  
176 1 Y 1 E ARG 128 ? NE  ? E  ARG 128 NE  
177 1 Y 1 E ARG 128 ? CZ  ? E  ARG 128 CZ  
178 1 Y 1 E ARG 128 ? NH1 ? E  ARG 128 NH1 
179 1 Y 1 E ARG 128 ? NH2 ? E  ARG 128 NH2 
180 1 Y 1 E ARG 180 ? CG  ? E  ARG 180 CG  
181 1 Y 1 E ARG 180 ? CD  ? E  ARG 180 CD  
182 1 Y 1 E ARG 180 ? NE  ? E  ARG 180 NE  
183 1 Y 1 E ARG 180 ? CZ  ? E  ARG 180 CZ  
184 1 Y 1 E ARG 180 ? NH1 ? E  ARG 180 NH1 
185 1 Y 1 E ARG 180 ? NH2 ? E  ARG 180 NH2 
186 1 Y 1 E ARG 183 ? CD  ? E  ARG 183 CD  
187 1 Y 1 E ARG 183 ? NE  ? E  ARG 183 NE  
188 1 Y 1 E ARG 183 ? CZ  ? E  ARG 183 CZ  
189 1 Y 1 E ARG 183 ? NH1 ? E  ARG 183 NH1 
190 1 Y 1 E ARG 183 ? NH2 ? E  ARG 183 NH2 
191 1 Y 1 E LYS 198 ? CG  ? E  LYS 198 CG  
192 1 Y 1 E LYS 198 ? CD  ? E  LYS 198 CD  
193 1 Y 1 E LYS 198 ? CE  ? E  LYS 198 CE  
194 1 Y 1 E LYS 198 ? NZ  ? E  LYS 198 NZ  
195 1 N 1 A LFA 401 ? C12 ? F  LFA 1   C12 
196 1 N 1 A LFA 401 ? C13 ? F  LFA 1   C13 
197 1 N 1 A LFA 401 ? C14 ? F  LFA 1   C14 
198 1 N 1 A LFA 401 ? C15 ? F  LFA 1   C15 
199 1 N 1 A LFA 401 ? C16 ? F  LFA 1   C16 
200 1 N 1 A LFA 401 ? C17 ? F  LFA 1   C17 
201 1 N 1 A LFA 401 ? C18 ? F  LFA 1   C18 
202 1 N 1 A LFA 401 ? C19 ? F  LFA 1   C19 
203 1 N 1 A LFA 401 ? C20 ? F  LFA 1   C20 
204 1 N 1 A LFA 402 ? C8  ? G  LFA 1   C8  
205 1 N 1 A LFA 402 ? C9  ? G  LFA 1   C9  
206 1 N 1 A LFA 402 ? C10 ? G  LFA 1   C10 
207 1 N 1 A LFA 402 ? C11 ? G  LFA 1   C11 
208 1 N 1 A LFA 402 ? C12 ? G  LFA 1   C12 
209 1 N 1 A LFA 402 ? C13 ? G  LFA 1   C13 
210 1 N 1 A LFA 402 ? C14 ? G  LFA 1   C14 
211 1 N 1 A LFA 402 ? C15 ? G  LFA 1   C15 
212 1 N 1 A LFA 402 ? C16 ? G  LFA 1   C16 
213 1 N 1 A LFA 402 ? C17 ? G  LFA 1   C17 
214 1 N 1 A LFA 402 ? C18 ? G  LFA 1   C18 
215 1 N 1 A LFA 402 ? C19 ? G  LFA 1   C19 
216 1 N 1 A LFA 402 ? C20 ? G  LFA 1   C20 
217 1 N 1 A LFA 404 ? C8  ? I  LFA 1   C8  
218 1 N 1 A LFA 404 ? C9  ? I  LFA 1   C9  
219 1 N 1 A LFA 404 ? C10 ? I  LFA 1   C10 
220 1 N 1 A LFA 404 ? C11 ? I  LFA 1   C11 
221 1 N 1 A LFA 404 ? C12 ? I  LFA 1   C12 
222 1 N 1 A LFA 404 ? C13 ? I  LFA 1   C13 
223 1 N 1 A LFA 404 ? C14 ? I  LFA 1   C14 
224 1 N 1 A LFA 404 ? C15 ? I  LFA 1   C15 
225 1 N 1 A LFA 404 ? C16 ? I  LFA 1   C16 
226 1 N 1 A LFA 404 ? C17 ? I  LFA 1   C17 
227 1 N 1 A LFA 404 ? C18 ? I  LFA 1   C18 
228 1 N 1 A LFA 404 ? C19 ? I  LFA 1   C19 
229 1 N 1 A LFA 404 ? C20 ? I  LFA 1   C20 
230 1 N 1 A LFA 405 ? C11 ? J  LFA 1   C11 
231 1 N 1 A LFA 405 ? C12 ? J  LFA 1   C12 
232 1 N 1 A LFA 405 ? C13 ? J  LFA 1   C13 
233 1 N 1 A LFA 405 ? C14 ? J  LFA 1   C14 
234 1 N 1 A LFA 405 ? C15 ? J  LFA 1   C15 
235 1 N 1 A LFA 405 ? C16 ? J  LFA 1   C16 
236 1 N 1 A LFA 405 ? C17 ? J  LFA 1   C17 
237 1 N 1 A LFA 405 ? C18 ? J  LFA 1   C18 
238 1 N 1 A LFA 405 ? C19 ? J  LFA 1   C19 
239 1 N 1 A LFA 405 ? C20 ? J  LFA 1   C20 
240 1 N 1 A LFA 406 ? C1  ? K  LFA 1   C1  
241 1 N 1 A LFA 406 ? C2  ? K  LFA 1   C2  
242 1 N 1 A LFA 406 ? C3  ? K  LFA 1   C3  
243 1 N 1 A LFA 406 ? C4  ? K  LFA 1   C4  
244 1 N 1 A LFA 406 ? C5  ? K  LFA 1   C5  
245 1 N 1 A LFA 406 ? C6  ? K  LFA 1   C6  
246 1 N 1 A LFA 406 ? C7  ? K  LFA 1   C7  
247 1 N 1 A LFA 406 ? C8  ? K  LFA 1   C8  
248 1 N 1 A LFA 406 ? C9  ? K  LFA 1   C9  
249 1 N 1 A LFA 406 ? C10 ? K  LFA 1   C10 
250 1 N 1 A LFA 406 ? C11 ? K  LFA 1   C11 
251 1 N 1 A LFA 406 ? C12 ? K  LFA 1   C12 
252 1 N 1 A LFA 406 ? C13 ? K  LFA 1   C13 
253 1 N 1 B LFA 401 ? C12 ? M  LFA 1   C12 
254 1 N 1 B LFA 401 ? C13 ? M  LFA 1   C13 
255 1 N 1 B LFA 401 ? C14 ? M  LFA 1   C14 
256 1 N 1 B LFA 401 ? C15 ? M  LFA 1   C15 
257 1 N 1 B LFA 401 ? C16 ? M  LFA 1   C16 
258 1 N 1 B LFA 401 ? C17 ? M  LFA 1   C17 
259 1 N 1 B LFA 401 ? C18 ? M  LFA 1   C18 
260 1 N 1 B LFA 401 ? C19 ? M  LFA 1   C19 
261 1 N 1 B LFA 401 ? C20 ? M  LFA 1   C20 
262 1 N 1 B LFA 402 ? C13 ? N  LFA 1   C13 
263 1 N 1 B LFA 402 ? C14 ? N  LFA 1   C14 
264 1 N 1 B LFA 402 ? C15 ? N  LFA 1   C15 
265 1 N 1 B LFA 402 ? C16 ? N  LFA 1   C16 
266 1 N 1 B LFA 402 ? C17 ? N  LFA 1   C17 
267 1 N 1 B LFA 402 ? C18 ? N  LFA 1   C18 
268 1 N 1 B LFA 402 ? C19 ? N  LFA 1   C19 
269 1 N 1 B LFA 402 ? C20 ? N  LFA 1   C20 
270 1 N 1 C LFA 401 ? C7  ? Q  LFA 1   C7  
271 1 N 1 C LFA 401 ? C8  ? Q  LFA 1   C8  
272 1 N 1 C LFA 401 ? C9  ? Q  LFA 1   C9  
273 1 N 1 C LFA 401 ? C10 ? Q  LFA 1   C10 
274 1 N 1 C LFA 401 ? C11 ? Q  LFA 1   C11 
275 1 N 1 C LFA 401 ? C12 ? Q  LFA 1   C12 
276 1 N 1 C LFA 401 ? C13 ? Q  LFA 1   C13 
277 1 N 1 C LFA 401 ? C14 ? Q  LFA 1   C14 
278 1 N 1 C LFA 401 ? C15 ? Q  LFA 1   C15 
279 1 N 1 C LFA 401 ? C16 ? Q  LFA 1   C16 
280 1 N 1 C LFA 401 ? C17 ? Q  LFA 1   C17 
281 1 N 1 C LFA 401 ? C18 ? Q  LFA 1   C18 
282 1 N 1 C LFA 401 ? C19 ? Q  LFA 1   C19 
283 1 N 1 C LFA 401 ? C20 ? Q  LFA 1   C20 
284 1 N 1 C LFA 403 ? C7  ? S  LFA 1   C7  
285 1 N 1 C LFA 403 ? C8  ? S  LFA 1   C8  
286 1 N 1 C LFA 403 ? C9  ? S  LFA 1   C9  
287 1 N 1 C LFA 403 ? C10 ? S  LFA 1   C10 
288 1 N 1 C LFA 403 ? C11 ? S  LFA 1   C11 
289 1 N 1 C LFA 403 ? C12 ? S  LFA 1   C12 
290 1 N 1 C LFA 403 ? C13 ? S  LFA 1   C13 
291 1 N 1 C LFA 403 ? C14 ? S  LFA 1   C14 
292 1 N 1 C LFA 403 ? C15 ? S  LFA 1   C15 
293 1 N 1 C LFA 403 ? C16 ? S  LFA 1   C16 
294 1 N 1 C LFA 403 ? C17 ? S  LFA 1   C17 
295 1 N 1 C LFA 403 ? C18 ? S  LFA 1   C18 
296 1 N 1 C LFA 403 ? C19 ? S  LFA 1   C19 
297 1 N 1 C LFA 403 ? C20 ? S  LFA 1   C20 
298 1 N 1 D LFA 403 ? C11 ? W  LFA 1   C11 
299 1 N 1 D LFA 403 ? C12 ? W  LFA 1   C12 
300 1 N 1 D LFA 403 ? C13 ? W  LFA 1   C13 
301 1 N 1 D LFA 403 ? C14 ? W  LFA 1   C14 
302 1 N 1 D LFA 403 ? C15 ? W  LFA 1   C15 
303 1 N 1 D LFA 403 ? C16 ? W  LFA 1   C16 
304 1 N 1 D LFA 403 ? C17 ? W  LFA 1   C17 
305 1 N 1 D LFA 403 ? C18 ? W  LFA 1   C18 
306 1 N 1 D LFA 403 ? C19 ? W  LFA 1   C19 
307 1 N 1 D LFA 403 ? C20 ? W  LFA 1   C20 
308 1 N 1 D LFA 404 ? C12 ? X  LFA 1   C12 
309 1 N 1 D LFA 404 ? C13 ? X  LFA 1   C13 
310 1 N 1 D LFA 404 ? C14 ? X  LFA 1   C14 
311 1 N 1 D LFA 404 ? C15 ? X  LFA 1   C15 
312 1 N 1 D LFA 404 ? C16 ? X  LFA 1   C16 
313 1 N 1 D LFA 404 ? C17 ? X  LFA 1   C17 
314 1 N 1 D LFA 404 ? C18 ? X  LFA 1   C18 
315 1 N 1 D LFA 404 ? C19 ? X  LFA 1   C19 
316 1 N 1 D LFA 404 ? C20 ? X  LFA 1   C20 
317 1 N 1 D LFA 405 ? C9  ? Y  LFA 1   C9  
318 1 N 1 D LFA 405 ? C10 ? Y  LFA 1   C10 
319 1 N 1 D LFA 405 ? C11 ? Y  LFA 1   C11 
320 1 N 1 D LFA 405 ? C12 ? Y  LFA 1   C12 
321 1 N 1 D LFA 405 ? C13 ? Y  LFA 1   C13 
322 1 N 1 D LFA 405 ? C14 ? Y  LFA 1   C14 
323 1 N 1 D LFA 405 ? C15 ? Y  LFA 1   C15 
324 1 N 1 D LFA 405 ? C16 ? Y  LFA 1   C16 
325 1 N 1 D LFA 405 ? C17 ? Y  LFA 1   C17 
326 1 N 1 D LFA 405 ? C18 ? Y  LFA 1   C18 
327 1 N 1 D LFA 405 ? C19 ? Y  LFA 1   C19 
328 1 N 1 D LFA 405 ? C20 ? Y  LFA 1   C20 
329 1 N 1 E LFA 401 ? C12 ? AA LFA 1   C12 
330 1 N 1 E LFA 401 ? C13 ? AA LFA 1   C13 
331 1 N 1 E LFA 401 ? C14 ? AA LFA 1   C14 
332 1 N 1 E LFA 401 ? C15 ? AA LFA 1   C15 
333 1 N 1 E LFA 401 ? C16 ? AA LFA 1   C16 
334 1 N 1 E LFA 401 ? C17 ? AA LFA 1   C17 
335 1 N 1 E LFA 401 ? C18 ? AA LFA 1   C18 
336 1 N 1 E LFA 401 ? C19 ? AA LFA 1   C19 
337 1 N 1 E LFA 401 ? C20 ? AA LFA 1   C20 
338 1 N 1 E LFA 403 ? C1  ? CA LFA 1   C1  
339 1 N 1 E LFA 403 ? C2  ? CA LFA 1   C2  
340 1 N 1 E LFA 403 ? C3  ? CA LFA 1   C3  
341 1 N 1 E LFA 403 ? C4  ? CA LFA 1   C4  
342 1 N 1 E LFA 403 ? C5  ? CA LFA 1   C5  
343 1 N 1 E LFA 403 ? C6  ? CA LFA 1   C6  
344 1 N 1 E LFA 403 ? C7  ? CA LFA 1   C7  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP    ? ? ? .        3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R96 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.565 
_cell.length_a_esd                 ? 
_cell.length_b                     295.665 
_cell.length_b_esd                 ? 
_cell.length_c                     185.500 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        40 
_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                         8R96 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_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                   8R96 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.05 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.2M Na/K-Pi pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R96 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.457 
_reflns.d_resolution_low                               92.75 
_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                                     56393 
_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                           65.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.44 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.493 
_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                                0.064 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9964 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.457 
_reflns_shell.d_res_low                                     2.719 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             38364 
_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                               0.962 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.3040 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.72 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.10 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.38 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               57.574 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8R96 
_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                            2.46 
_refine.ls_d_res_low                             20.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     53453 
_refine.ls_number_reflns_R_free                  2746 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    65.39 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.23952 
_refine.ls_R_factor_R_free                       0.25445 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23874 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.750 
_refine.pdbx_overall_ESU_R_Free                  0.333 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             16.383 
_refine.overall_SU_ML                            0.310 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.46 
_refine_hist.d_res_low                        20.00 
_refine_hist.number_atoms_solvent             31 
_refine_hist.number_atoms_total               11044 
_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        10838 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         175 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  0.013  11238 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.015  11134 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.062  1.626  15377 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.067  1.555  25355 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 4.534  5.000  1435  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 24.460 20.392 434   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.734 15.000 1565  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.642 15.000 45    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.026  0.200  1580  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  12480 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.020  2530  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.720  6.146  5755  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.719  6.146  5754  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 7.408  9.221  7185  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.408  9.221  7186  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.734  6.421  5483  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.758  6.421  5484  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.324  9.513  8193  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.238 75.319 12944 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.238 75.320 12945 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 1  'interatomic distance' ? A 9358 ? ? 1  
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 2  'interatomic distance' ? B 9358 ? ? 1  
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 3  'interatomic distance' ? A 9342 ? ? 2  
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 4  'interatomic distance' ? C 9342 ? ? 2  
'X-RAY DIFFRACTION' 1 ? ? 0.06 ? 0.05 5  'interatomic distance' ? A 9312 ? ? 3  
'X-RAY DIFFRACTION' 2 ? ? 0.06 ? 0.05 6  'interatomic distance' ? D 9312 ? ? 3  
'X-RAY DIFFRACTION' 1 ? ? 0.06 ? 0.05 7  'interatomic distance' ? A 9337 ? ? 4  
'X-RAY DIFFRACTION' 2 ? ? 0.06 ? 0.05 8  'interatomic distance' ? E 9337 ? ? 4  
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 9  'interatomic distance' ? B 9332 ? ? 5  
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 10 'interatomic distance' ? C 9332 ? ? 5  
'X-RAY DIFFRACTION' 1 ? ? 0.06 ? 0.05 11 'interatomic distance' ? B 9310 ? ? 6  
'X-RAY DIFFRACTION' 2 ? ? 0.06 ? 0.05 12 'interatomic distance' ? D 9310 ? ? 6  
'X-RAY DIFFRACTION' 1 ? ? 0.06 ? 0.05 13 'interatomic distance' ? B 9306 ? ? 7  
'X-RAY DIFFRACTION' 2 ? ? 0.06 ? 0.05 14 'interatomic distance' ? E 9306 ? ? 7  
'X-RAY DIFFRACTION' 1 ? ? 0.06 ? 0.05 15 'interatomic distance' ? C 9314 ? ? 8  
'X-RAY DIFFRACTION' 2 ? ? 0.06 ? 0.05 16 'interatomic distance' ? D 9314 ? ? 8  
'X-RAY DIFFRACTION' 1 ? ? 0.06 ? 0.05 17 'interatomic distance' ? C 9325 ? ? 9  
'X-RAY DIFFRACTION' 2 ? ? 0.06 ? 0.05 18 'interatomic distance' ? E 9325 ? ? 9  
'X-RAY DIFFRACTION' 1 ? ? 0.05 ? 0.05 19 'interatomic distance' ? D 9315 ? ? 10 
'X-RAY DIFFRACTION' 2 ? ? 0.05 ? 0.05 20 'interatomic distance' ? E 9315 ? ? 10 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.46 
_refine_ls_shell.d_res_low                        2.520 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             9 
_refine_ls_shell.number_reflns_R_work             208 
_refine_ls_shell.percent_reflns_obs               3.49 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.427 
_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                  0.334 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1  ? 1  
2  ? 2  
3  ? 3  
4  ? 4  
5  ? 5  
6  ? 6  
7  ? 7  
8  ? 8  
9  ? 9  
10 ? 10 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1  ? 
2  ? 
3  ? 
4  ? 
5  ? 
6  ? 
7  ? 
8  ? 
9  ? 
10 ? 
# 
_struct.entry_id                     8R96 
_struct.title                        'Crystal structure of the cryorhodopsin CryoR2 at pH 4.6, type A crystals' 
_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        8R96 
_struct_keywords.text            'retinal, rhodopsin, photocycle, 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 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 3 ? 
I  N N 2 ? 
J  N N 2 ? 
K  N N 2 ? 
L  N N 4 ? 
M  N N 2 ? 
N  N N 2 ? 
O  N N 3 ? 
P  N N 4 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 2 ? 
T  N N 4 ? 
U  N N 5 ? 
V  N N 3 ? 
W  N N 2 ? 
X  N N 2 ? 
Y  N N 2 ? 
Z  N N 4 ? 
AA N N 2 ? 
BA N N 3 ? 
CA N N 2 ? 
DA N N 4 ? 
EA N N 6 ? 
FA N N 6 ? 
GA N N 6 ? 
HA N N 6 ? 
IA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8R96 
_struct_ref.pdbx_db_accession          8R96 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8R96 A 1 ? 327 ? 8R96 1 ? 327 ? 1 327 
2 1 8R96 B 1 ? 327 ? 8R96 1 ? 327 ? 1 327 
3 1 8R96 C 1 ? 327 ? 8R96 1 ? 327 ? 1 327 
4 1 8R96 D 1 ? 327 ? 8R96 1 ? 327 ? 1 327 
5 1 8R96 E 1 ? 327 ? 8R96 1 ? 327 ? 1 327 
# 
_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   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
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)' 25230 ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  47520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 VAL A 8   ? ALA A 12  ? VAL A 8   ALA A 12  5 ? 5  
HELX_P HELX_P2  AA2 SER A 15  ? THR A 43  ? SER A 15  THR A 43  1 ? 29 
HELX_P HELX_P3  AA3 ARG A 44  ? VAL A 47  ? ARG A 44  VAL A 47  5 ? 4  
HELX_P HELX_P4  AA4 GLY A 48  ? ARG A 50  ? GLY A 48  ARG A 50  5 ? 3  
HELX_P HELX_P5  AA5 TYR A 51  ? LEU A 78  ? TYR A 51  LEU A 78  1 ? 28 
HELX_P HELX_P6  AA6 ASP A 91  ? ALA A 93  ? ASP A 91  ALA A 93  5 ? 3  
HELX_P HELX_P7  AA7 ILE A 94  ? CYS A 119 ? ILE A 94  CYS A 119 1 ? 26 
HELX_P HELX_P8  AA8 GLY A 123 ? ILE A 149 ? GLY A 123 ILE A 149 1 ? 27 
HELX_P HELX_P9  AA9 VAL A 150 ? THR A 155 ? VAL A 150 THR A 155 5 ? 6  
HELX_P HELX_P10 AB1 ASN A 156 ? LEU A 189 ? ASN A 156 LEU A 189 1 ? 34 
HELX_P HELX_P11 AB2 THR A 190 ? TRP A 208 ? THR A 190 TRP A 208 1 ? 19 
HELX_P HELX_P12 AB3 VAL A 209 ? PHE A 216 ? VAL A 209 PHE A 216 1 ? 8  
HELX_P HELX_P13 AB4 LEU A 217 ? GLY A 221 ? LEU A 217 GLY A 221 5 ? 5  
HELX_P HELX_P14 AB5 SER A 223 ? ALA A 263 ? SER A 223 ALA A 263 1 ? 41 
HELX_P HELX_P15 AB6 VAL B 8   ? ALA B 12  ? VAL B 8   ALA B 12  5 ? 5  
HELX_P HELX_P16 AB7 ASN B 16  ? THR B 43  ? ASN B 16  THR B 43  1 ? 28 
HELX_P HELX_P17 AB8 ARG B 44  ? VAL B 47  ? ARG B 44  VAL B 47  5 ? 4  
HELX_P HELX_P18 AB9 GLY B 48  ? ARG B 50  ? GLY B 48  ARG B 50  5 ? 3  
HELX_P HELX_P19 AC1 TYR B 51  ? LEU B 78  ? TYR B 51  LEU B 78  1 ? 28 
HELX_P HELX_P20 AC2 ASP B 91  ? ALA B 93  ? ASP B 91  ALA B 93  5 ? 3  
HELX_P HELX_P21 AC3 ILE B 94  ? CYS B 119 ? ILE B 94  CYS B 119 1 ? 26 
HELX_P HELX_P22 AC4 GLY B 123 ? ILE B 149 ? GLY B 123 ILE B 149 1 ? 27 
HELX_P HELX_P23 AC5 VAL B 150 ? THR B 155 ? VAL B 150 THR B 155 5 ? 6  
HELX_P HELX_P24 AC6 ASN B 156 ? LEU B 189 ? ASN B 156 LEU B 189 1 ? 34 
HELX_P HELX_P25 AC7 THR B 190 ? TRP B 208 ? THR B 190 TRP B 208 1 ? 19 
HELX_P HELX_P26 AC8 VAL B 209 ? PHE B 216 ? VAL B 209 PHE B 216 1 ? 8  
HELX_P HELX_P27 AC9 LEU B 217 ? GLY B 221 ? LEU B 217 GLY B 221 5 ? 5  
HELX_P HELX_P28 AD1 SER B 223 ? ALA B 263 ? SER B 223 ALA B 263 1 ? 41 
HELX_P HELX_P29 AD2 VAL C 8   ? ALA C 12  ? VAL C 8   ALA C 12  5 ? 5  
HELX_P HELX_P30 AD3 SER C 15  ? THR C 43  ? SER C 15  THR C 43  1 ? 29 
HELX_P HELX_P31 AD4 ARG C 44  ? VAL C 47  ? ARG C 44  VAL C 47  5 ? 4  
HELX_P HELX_P32 AD5 GLY C 48  ? ARG C 50  ? GLY C 48  ARG C 50  5 ? 3  
HELX_P HELX_P33 AD6 TYR C 51  ? LEU C 78  ? TYR C 51  LEU C 78  1 ? 28 
HELX_P HELX_P34 AD7 ASP C 91  ? ALA C 93  ? ASP C 91  ALA C 93  5 ? 3  
HELX_P HELX_P35 AD8 ILE C 94  ? CYS C 119 ? ILE C 94  CYS C 119 1 ? 26 
HELX_P HELX_P36 AD9 GLY C 123 ? ILE C 149 ? GLY C 123 ILE C 149 1 ? 27 
HELX_P HELX_P37 AE1 VAL C 150 ? THR C 155 ? VAL C 150 THR C 155 5 ? 6  
HELX_P HELX_P38 AE2 ASN C 156 ? LEU C 189 ? ASN C 156 LEU C 189 1 ? 34 
HELX_P HELX_P39 AE3 THR C 190 ? TRP C 208 ? THR C 190 TRP C 208 1 ? 19 
HELX_P HELX_P40 AE4 VAL C 209 ? PHE C 216 ? VAL C 209 PHE C 216 1 ? 8  
HELX_P HELX_P41 AE5 LEU C 217 ? GLY C 221 ? LEU C 217 GLY C 221 5 ? 5  
HELX_P HELX_P42 AE6 SER C 223 ? ALA C 263 ? SER C 223 ALA C 263 1 ? 41 
HELX_P HELX_P43 AE7 VAL D 8   ? ALA D 12  ? VAL D 8   ALA D 12  5 ? 5  
HELX_P HELX_P44 AE8 SER D 15  ? THR D 43  ? SER D 15  THR D 43  1 ? 29 
HELX_P HELX_P45 AE9 ARG D 44  ? VAL D 47  ? ARG D 44  VAL D 47  5 ? 4  
HELX_P HELX_P46 AF1 GLY D 48  ? ARG D 50  ? GLY D 48  ARG D 50  5 ? 3  
HELX_P HELX_P47 AF2 TYR D 51  ? LEU D 78  ? TYR D 51  LEU D 78  1 ? 28 
HELX_P HELX_P48 AF3 ASP D 91  ? ALA D 93  ? ASP D 91  ALA D 93  5 ? 3  
HELX_P HELX_P49 AF4 ILE D 94  ? CYS D 119 ? ILE D 94  CYS D 119 1 ? 26 
HELX_P HELX_P50 AF5 GLY D 123 ? ILE D 149 ? GLY D 123 ILE D 149 1 ? 27 
HELX_P HELX_P51 AF6 VAL D 150 ? THR D 155 ? VAL D 150 THR D 155 5 ? 6  
HELX_P HELX_P52 AF7 ASN D 156 ? LEU D 189 ? ASN D 156 LEU D 189 1 ? 34 
HELX_P HELX_P53 AF8 THR D 190 ? TRP D 208 ? THR D 190 TRP D 208 1 ? 19 
HELX_P HELX_P54 AF9 VAL D 209 ? PHE D 216 ? VAL D 209 PHE D 216 1 ? 8  
HELX_P HELX_P55 AG1 LEU D 217 ? GLY D 221 ? LEU D 217 GLY D 221 5 ? 5  
HELX_P HELX_P56 AG2 SER D 223 ? ALA D 263 ? SER D 223 ALA D 263 1 ? 41 
HELX_P HELX_P57 AG3 VAL E 8   ? ALA E 12  ? VAL E 8   ALA E 12  5 ? 5  
HELX_P HELX_P58 AG4 SER E 15  ? THR E 43  ? SER E 15  THR E 43  1 ? 29 
HELX_P HELX_P59 AG5 ARG E 44  ? VAL E 47  ? ARG E 44  VAL E 47  5 ? 4  
HELX_P HELX_P60 AG6 GLY E 48  ? ARG E 50  ? GLY E 48  ARG E 50  5 ? 3  
HELX_P HELX_P61 AG7 TYR E 51  ? LEU E 78  ? TYR E 51  LEU E 78  1 ? 28 
HELX_P HELX_P62 AG8 ASP E 91  ? ALA E 93  ? ASP E 91  ALA E 93  5 ? 3  
HELX_P HELX_P63 AG9 ILE E 94  ? CYS E 119 ? ILE E 94  CYS E 119 1 ? 26 
HELX_P HELX_P64 AH1 GLY E 123 ? ILE E 149 ? GLY E 123 ILE E 149 1 ? 27 
HELX_P HELX_P65 AH2 VAL E 150 ? THR E 155 ? VAL E 150 THR E 155 5 ? 6  
HELX_P HELX_P66 AH3 ASN E 156 ? LEU E 186 ? ASN E 156 LEU E 186 1 ? 31 
HELX_P HELX_P67 AH4 PRO E 187 ? LEU E 189 ? PRO E 187 LEU E 189 5 ? 3  
HELX_P HELX_P68 AH5 THR E 190 ? TRP E 208 ? THR E 190 TRP E 208 1 ? 19 
HELX_P HELX_P69 AH6 VAL E 209 ? PHE E 216 ? VAL E 209 PHE E 216 1 ? 8  
HELX_P HELX_P70 AH7 LEU E 217 ? GLY E 221 ? LEU E 217 GLY E 221 5 ? 5  
HELX_P HELX_P71 AH8 SER E 223 ? ALA E 263 ? SER E 223 ALA E 263 1 ? 41 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A LYS 242 NZ ? ? ? 1_555 L  RET . C15 ? ? A LYS 242 A RET 407 1_555 ? ? ? ? ? ? ? 1.460 ? ? 
covale2 covale one ? B LYS 242 NZ ? ? ? 1_555 P  RET . C15 ? ? B LYS 242 B RET 404 1_555 ? ? ? ? ? ? ? 1.461 ? ? 
covale3 covale one ? C LYS 242 NZ ? ? ? 1_555 T  RET . C15 ? ? C LYS 242 C RET 404 1_555 ? ? ? ? ? ? ? 1.450 ? ? 
covale4 covale one ? D LYS 242 NZ ? ? ? 1_555 Z  RET . C15 ? ? D LYS 242 D RET 406 1_555 ? ? ? ? ? ? ? 1.461 ? ? 
covale5 covale one ? E LYS 242 NZ ? ? ? 1_555 DA RET . C15 ? ? E LYS 242 E RET 404 1_555 ? ? ? ? ? ? ? 1.460 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 RET DA . ? LYS E 242 ? RET E 404 ? 1_555 LYS E 242 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
2 RET L  . ? LYS A 242 ? RET A 407 ? 1_555 LYS A 242 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
3 RET P  . ? LYS B 242 ? RET B 404 ? 1_555 LYS B 242 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
4 RET T  . ? LYS C 242 ? RET C 404 ? 1_555 LYS C 242 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
5 RET Z  . ? LYS D 242 ? RET D 406 ? 1_555 LYS D 242 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 2 ? 
AB5 ? 2 ? 
AB6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? parallel      
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 80  ? THR A 83  ? TYR A 80  THR A 83  
AA1 2 GLY A 86  ? PRO A 89  ? GLY A 86  PRO A 89  
AA2 1 ILE A 272 ? ILE A 274 ? ILE A 272 ILE A 274 
AA2 2 VAL A 277 ? SER A 280 ? VAL A 277 SER A 280 
AA3 1 LEU A 284 ? PRO A 285 ? LEU A 284 PRO A 285 
AA3 2 GLU B 287 ? VAL B 288 ? GLU B 287 VAL B 288 
AA4 1 GLU A 287 ? VAL A 288 ? GLU A 287 VAL A 288 
AA4 2 LEU E 284 ? PRO E 285 ? LEU E 284 PRO E 285 
AA5 1 LEU B 14  ? SER B 15  ? LEU B 14  SER B 15  
AA5 2 GLY B 86  ? PRO B 89  ? GLY B 86  PRO B 89  
AA5 3 TYR B 80  ? SER B 82  ? TYR B 80  SER B 82  
AA6 1 ILE B 272 ? ILE B 274 ? ILE B 272 ILE B 274 
AA6 2 VAL B 277 ? SER B 280 ? VAL B 277 SER B 280 
AA7 1 LEU B 284 ? PRO B 285 ? LEU B 284 PRO B 285 
AA7 2 GLU C 287 ? VAL C 288 ? GLU C 287 VAL C 288 
AA8 1 TYR C 80  ? SER C 82  ? TYR C 80  SER C 82  
AA8 2 TRP C 87  ? PRO C 89  ? TRP C 87  PRO C 89  
AA9 1 ILE C 272 ? ILE C 274 ? ILE C 272 ILE C 274 
AA9 2 VAL C 277 ? SER C 280 ? VAL C 277 SER C 280 
AB1 1 LEU C 284 ? PRO C 285 ? LEU C 284 PRO C 285 
AB1 2 GLU D 287 ? VAL D 288 ? GLU D 287 VAL D 288 
AB2 1 TYR D 80  ? THR D 83  ? TYR D 80  THR D 83  
AB2 2 GLY D 86  ? PRO D 89  ? GLY D 86  PRO D 89  
AB3 1 ILE D 272 ? ILE D 274 ? ILE D 272 ILE D 274 
AB3 2 VAL D 277 ? SER D 280 ? VAL D 277 SER D 280 
AB4 1 LEU D 284 ? PRO D 285 ? LEU D 284 PRO D 285 
AB4 2 GLU E 287 ? VAL E 288 ? GLU E 287 VAL E 288 
AB5 1 TYR E 80  ? THR E 83  ? TYR E 80  THR E 83  
AB5 2 GLY E 86  ? PRO E 89  ? GLY E 86  PRO E 89  
AB6 1 ILE E 272 ? ILE E 274 ? ILE E 272 ILE E 274 
AB6 2 VAL E 277 ? SER E 280 ? VAL E 277 SER E 280 
# 
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 THR A 83  ? N THR A 83  O GLY A 86  ? O GLY A 86  
AA2 1 2 N ILE A 272 ? N ILE A 272 O GLN A 279 ? O GLN A 279 
AA3 1 2 N LEU A 284 ? N LEU A 284 O VAL B 288 ? O VAL B 288 
AA4 1 2 N VAL A 288 ? N VAL A 288 O LEU E 284 ? O LEU E 284 
AA5 1 2 N LEU B 14  ? N LEU B 14  O TRP B 87  ? O TRP B 87  
AA5 2 3 O VAL B 88  ? O VAL B 88  N ASP B 81  ? N ASP B 81  
AA6 1 2 N ILE B 272 ? N ILE B 272 O GLN B 279 ? O GLN B 279 
AA7 1 2 N LEU B 284 ? N LEU B 284 O VAL C 288 ? O VAL C 288 
AA8 1 2 N ASP C 81  ? N ASP C 81  O VAL C 88  ? O VAL C 88  
AA9 1 2 N ILE C 272 ? N ILE C 272 O GLN C 279 ? O GLN C 279 
AB1 1 2 N LEU C 284 ? N LEU C 284 O VAL D 288 ? O VAL D 288 
AB2 1 2 N THR D 83  ? N THR D 83  O GLY D 86  ? O GLY D 86  
AB3 1 2 N ILE D 272 ? N ILE D 272 O GLN D 279 ? O GLN D 279 
AB4 1 2 N LEU D 284 ? N LEU D 284 O VAL E 288 ? O VAL E 288 
AB5 1 2 N ASP E 81  ? N ASP E 81  O VAL E 88  ? O VAL E 88  
AB6 1 2 N ILE E 272 ? N ILE E 272 O GLN E 279 ? O GLN E 279 
# 
_pdbx_entry_details.entry_id                   8R96 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 149 ? ? -125.81 -64.85 
2  1 ILE B 149 ? ? -125.56 -64.45 
3  1 SER B 223 ? ? -177.70 145.33 
4  1 GLU B 292 ? ? -171.18 135.08 
5  1 ALA C 84  ? ? 82.44   -16.50 
6  1 ILE C 149 ? ? -126.17 -64.52 
7  1 SER C 223 ? ? -179.33 144.91 
8  1 ILE D 149 ? ? -126.69 -64.46 
9  1 SER D 223 ? ? -178.54 144.43 
10 1 ILE E 149 ? ? -125.84 -64.74 
11 1 SER E 223 ? ? -176.08 145.16 
12 1 SER E 276 ? ? 80.63   7.69   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ARG 2   ? A ARG 2   
3   1 Y 1 A LEU 3   ? A LEU 3   
4   1 Y 1 A GLU 292 ? A GLU 292 
5   1 Y 1 A GLY 293 ? A GLY 293 
6   1 Y 1 A ALA 294 ? A ALA 294 
7   1 Y 1 A ALA 295 ? A ALA 295 
8   1 Y 1 A VAL 296 ? A VAL 296 
9   1 Y 1 A HIS 297 ? A HIS 297 
10  1 Y 1 A ASP 298 ? A ASP 298 
11  1 Y 1 A ARG 299 ? A ARG 299 
12  1 Y 1 A ARG 300 ? A ARG 300 
13  1 Y 1 A THR 301 ? A THR 301 
14  1 Y 1 A LYS 302 ? A LYS 302 
15  1 Y 1 A PRO 303 ? A PRO 303 
16  1 Y 1 A PRO 304 ? A PRO 304 
17  1 Y 1 A THR 305 ? A THR 305 
18  1 Y 1 A SER 306 ? A SER 306 
19  1 Y 1 A ALA 307 ? A ALA 307 
20  1 Y 1 A ALA 308 ? A ALA 308 
21  1 Y 1 A VAL 309 ? A VAL 309 
22  1 Y 1 A ALA 310 ? A ALA 310 
23  1 Y 1 A SER 311 ? A SER 311 
24  1 Y 1 A PRO 312 ? A PRO 312 
25  1 Y 1 A GLU 313 ? A GLU 313 
26  1 Y 1 A ALA 314 ? A ALA 314 
27  1 Y 1 A PRO 315 ? A PRO 315 
28  1 Y 1 A LEU 316 ? A LEU 316 
29  1 Y 1 A PRO 317 ? A PRO 317 
30  1 Y 1 A PRO 318 ? A PRO 318 
31  1 Y 1 A ASP 319 ? A ASP 319 
32  1 Y 1 A SER 320 ? A SER 320 
33  1 Y 1 A THR 321 ? A THR 321 
34  1 Y 1 A PRO 322 ? A PRO 322 
35  1 Y 1 A LEU 323 ? A LEU 323 
36  1 Y 1 A ASP 324 ? A ASP 324 
37  1 Y 1 A GLY 325 ? A GLY 325 
38  1 Y 1 A GLY 326 ? A GLY 326 
39  1 Y 1 A TYR 327 ? A TYR 327 
40  1 Y 1 B MET 1   ? B MET 1   
41  1 Y 1 B ARG 2   ? B ARG 2   
42  1 Y 1 B LEU 3   ? B LEU 3   
43  1 Y 1 B THR 4   ? B THR 4   
44  1 Y 1 B ALA 295 ? B ALA 295 
45  1 Y 1 B VAL 296 ? B VAL 296 
46  1 Y 1 B HIS 297 ? B HIS 297 
47  1 Y 1 B ASP 298 ? B ASP 298 
48  1 Y 1 B ARG 299 ? B ARG 299 
49  1 Y 1 B ARG 300 ? B ARG 300 
50  1 Y 1 B THR 301 ? B THR 301 
51  1 Y 1 B LYS 302 ? B LYS 302 
52  1 Y 1 B PRO 303 ? B PRO 303 
53  1 Y 1 B PRO 304 ? B PRO 304 
54  1 Y 1 B THR 305 ? B THR 305 
55  1 Y 1 B SER 306 ? B SER 306 
56  1 Y 1 B ALA 307 ? B ALA 307 
57  1 Y 1 B ALA 308 ? B ALA 308 
58  1 Y 1 B VAL 309 ? B VAL 309 
59  1 Y 1 B ALA 310 ? B ALA 310 
60  1 Y 1 B SER 311 ? B SER 311 
61  1 Y 1 B PRO 312 ? B PRO 312 
62  1 Y 1 B GLU 313 ? B GLU 313 
63  1 Y 1 B ALA 314 ? B ALA 314 
64  1 Y 1 B PRO 315 ? B PRO 315 
65  1 Y 1 B LEU 316 ? B LEU 316 
66  1 Y 1 B PRO 317 ? B PRO 317 
67  1 Y 1 B PRO 318 ? B PRO 318 
68  1 Y 1 B ASP 319 ? B ASP 319 
69  1 Y 1 B SER 320 ? B SER 320 
70  1 Y 1 B THR 321 ? B THR 321 
71  1 Y 1 B PRO 322 ? B PRO 322 
72  1 Y 1 B LEU 323 ? B LEU 323 
73  1 Y 1 B ASP 324 ? B ASP 324 
74  1 Y 1 B GLY 325 ? B GLY 325 
75  1 Y 1 B GLY 326 ? B GLY 326 
76  1 Y 1 B TYR 327 ? B TYR 327 
77  1 Y 1 C MET 1   ? C MET 1   
78  1 Y 1 C ARG 2   ? C ARG 2   
79  1 Y 1 C LEU 3   ? C LEU 3   
80  1 Y 1 C ALA 291 ? C ALA 291 
81  1 Y 1 C GLU 292 ? C GLU 292 
82  1 Y 1 C GLY 293 ? C GLY 293 
83  1 Y 1 C ALA 294 ? C ALA 294 
84  1 Y 1 C ALA 295 ? C ALA 295 
85  1 Y 1 C VAL 296 ? C VAL 296 
86  1 Y 1 C HIS 297 ? C HIS 297 
87  1 Y 1 C ASP 298 ? C ASP 298 
88  1 Y 1 C ARG 299 ? C ARG 299 
89  1 Y 1 C ARG 300 ? C ARG 300 
90  1 Y 1 C THR 301 ? C THR 301 
91  1 Y 1 C LYS 302 ? C LYS 302 
92  1 Y 1 C PRO 303 ? C PRO 303 
93  1 Y 1 C PRO 304 ? C PRO 304 
94  1 Y 1 C THR 305 ? C THR 305 
95  1 Y 1 C SER 306 ? C SER 306 
96  1 Y 1 C ALA 307 ? C ALA 307 
97  1 Y 1 C ALA 308 ? C ALA 308 
98  1 Y 1 C VAL 309 ? C VAL 309 
99  1 Y 1 C ALA 310 ? C ALA 310 
100 1 Y 1 C SER 311 ? C SER 311 
101 1 Y 1 C PRO 312 ? C PRO 312 
102 1 Y 1 C GLU 313 ? C GLU 313 
103 1 Y 1 C ALA 314 ? C ALA 314 
104 1 Y 1 C PRO 315 ? C PRO 315 
105 1 Y 1 C LEU 316 ? C LEU 316 
106 1 Y 1 C PRO 317 ? C PRO 317 
107 1 Y 1 C PRO 318 ? C PRO 318 
108 1 Y 1 C ASP 319 ? C ASP 319 
109 1 Y 1 C SER 320 ? C SER 320 
110 1 Y 1 C THR 321 ? C THR 321 
111 1 Y 1 C PRO 322 ? C PRO 322 
112 1 Y 1 C LEU 323 ? C LEU 323 
113 1 Y 1 C ASP 324 ? C ASP 324 
114 1 Y 1 C GLY 325 ? C GLY 325 
115 1 Y 1 C GLY 326 ? C GLY 326 
116 1 Y 1 C TYR 327 ? C TYR 327 
117 1 Y 1 D MET 1   ? D MET 1   
118 1 Y 1 D ARG 2   ? D ARG 2   
119 1 Y 1 D GLU 292 ? D GLU 292 
120 1 Y 1 D GLY 293 ? D GLY 293 
121 1 Y 1 D ALA 294 ? D ALA 294 
122 1 Y 1 D ALA 295 ? D ALA 295 
123 1 Y 1 D VAL 296 ? D VAL 296 
124 1 Y 1 D HIS 297 ? D HIS 297 
125 1 Y 1 D ASP 298 ? D ASP 298 
126 1 Y 1 D ARG 299 ? D ARG 299 
127 1 Y 1 D ARG 300 ? D ARG 300 
128 1 Y 1 D THR 301 ? D THR 301 
129 1 Y 1 D LYS 302 ? D LYS 302 
130 1 Y 1 D PRO 303 ? D PRO 303 
131 1 Y 1 D PRO 304 ? D PRO 304 
132 1 Y 1 D THR 305 ? D THR 305 
133 1 Y 1 D SER 306 ? D SER 306 
134 1 Y 1 D ALA 307 ? D ALA 307 
135 1 Y 1 D ALA 308 ? D ALA 308 
136 1 Y 1 D VAL 309 ? D VAL 309 
137 1 Y 1 D ALA 310 ? D ALA 310 
138 1 Y 1 D SER 311 ? D SER 311 
139 1 Y 1 D PRO 312 ? D PRO 312 
140 1 Y 1 D GLU 313 ? D GLU 313 
141 1 Y 1 D ALA 314 ? D ALA 314 
142 1 Y 1 D PRO 315 ? D PRO 315 
143 1 Y 1 D LEU 316 ? D LEU 316 
144 1 Y 1 D PRO 317 ? D PRO 317 
145 1 Y 1 D PRO 318 ? D PRO 318 
146 1 Y 1 D ASP 319 ? D ASP 319 
147 1 Y 1 D SER 320 ? D SER 320 
148 1 Y 1 D THR 321 ? D THR 321 
149 1 Y 1 D PRO 322 ? D PRO 322 
150 1 Y 1 D LEU 323 ? D LEU 323 
151 1 Y 1 D ASP 324 ? D ASP 324 
152 1 Y 1 D GLY 325 ? D GLY 325 
153 1 Y 1 D GLY 326 ? D GLY 326 
154 1 Y 1 D TYR 327 ? D TYR 327 
155 1 Y 1 E MET 1   ? E MET 1   
156 1 Y 1 E ARG 2   ? E ARG 2   
157 1 Y 1 E LEU 3   ? E LEU 3   
158 1 Y 1 E THR 4   ? E THR 4   
159 1 Y 1 E ALA 291 ? E ALA 291 
160 1 Y 1 E GLU 292 ? E GLU 292 
161 1 Y 1 E GLY 293 ? E GLY 293 
162 1 Y 1 E ALA 294 ? E ALA 294 
163 1 Y 1 E ALA 295 ? E ALA 295 
164 1 Y 1 E VAL 296 ? E VAL 296 
165 1 Y 1 E HIS 297 ? E HIS 297 
166 1 Y 1 E ASP 298 ? E ASP 298 
167 1 Y 1 E ARG 299 ? E ARG 299 
168 1 Y 1 E ARG 300 ? E ARG 300 
169 1 Y 1 E THR 301 ? E THR 301 
170 1 Y 1 E LYS 302 ? E LYS 302 
171 1 Y 1 E PRO 303 ? E PRO 303 
172 1 Y 1 E PRO 304 ? E PRO 304 
173 1 Y 1 E THR 305 ? E THR 305 
174 1 Y 1 E SER 306 ? E SER 306 
175 1 Y 1 E ALA 307 ? E ALA 307 
176 1 Y 1 E ALA 308 ? E ALA 308 
177 1 Y 1 E VAL 309 ? E VAL 309 
178 1 Y 1 E ALA 310 ? E ALA 310 
179 1 Y 1 E SER 311 ? E SER 311 
180 1 Y 1 E PRO 312 ? E PRO 312 
181 1 Y 1 E GLU 313 ? E GLU 313 
182 1 Y 1 E ALA 314 ? E ALA 314 
183 1 Y 1 E PRO 315 ? E PRO 315 
184 1 Y 1 E LEU 316 ? E LEU 316 
185 1 Y 1 E PRO 317 ? E PRO 317 
186 1 Y 1 E PRO 318 ? E PRO 318 
187 1 Y 1 E ASP 319 ? E ASP 319 
188 1 Y 1 E SER 320 ? E SER 320 
189 1 Y 1 E THR 321 ? E THR 321 
190 1 Y 1 E PRO 322 ? E PRO 322 
191 1 Y 1 E LEU 323 ? E LEU 323 
192 1 Y 1 E ASP 324 ? E ASP 324 
193 1 Y 1 E GLY 325 ? E GLY 325 
194 1 Y 1 E GLY 326 ? E GLY 326 
195 1 Y 1 E TYR 327 ? E TYR 327 
# 
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 
LFA C1   C N N 205 
LFA C2   C N N 206 
LFA C3   C N N 207 
LFA C4   C N N 208 
LFA C5   C N N 209 
LFA C6   C N N 210 
LFA C7   C N N 211 
LFA C8   C N N 212 
LFA C9   C N N 213 
LFA C10  C N N 214 
LFA C11  C N N 215 
LFA C12  C N N 216 
LFA C13  C N N 217 
LFA C14  C N N 218 
LFA C15  C N N 219 
LFA C16  C N N 220 
LFA C17  C N N 221 
LFA C18  C N N 222 
LFA C19  C N N 223 
LFA C20  C N N 224 
LFA H11  H N N 225 
LFA H12  H N N 226 
LFA H13  H N N 227 
LFA H21  H N N 228 
LFA H22  H N N 229 
LFA H31  H N N 230 
LFA H32  H N N 231 
LFA H41  H N N 232 
LFA H42  H N N 233 
LFA H51  H N N 234 
LFA H52  H N N 235 
LFA H61  H N N 236 
LFA H62  H N N 237 
LFA H71  H N N 238 
LFA H72  H N N 239 
LFA H81  H N N 240 
LFA H82  H N N 241 
LFA H91  H N N 242 
LFA H92  H N N 243 
LFA H101 H N N 244 
LFA H102 H N N 245 
LFA H111 H N N 246 
LFA H112 H N N 247 
LFA H121 H N N 248 
LFA H122 H N N 249 
LFA H131 H N N 250 
LFA H132 H N N 251 
LFA H141 H N N 252 
LFA H142 H N N 253 
LFA H151 H N N 254 
LFA H152 H N N 255 
LFA H161 H N N 256 
LFA H162 H N N 257 
LFA H171 H N N 258 
LFA H172 H N N 259 
LFA H181 H N N 260 
LFA H182 H N N 261 
LFA H191 H N N 262 
LFA H192 H N N 263 
LFA H201 H N N 264 
LFA H202 H N N 265 
LFA H203 H N N 266 
LYS N    N N N 267 
LYS CA   C N S 268 
LYS C    C N N 269 
LYS O    O N N 270 
LYS CB   C N N 271 
LYS CG   C N N 272 
LYS CD   C N N 273 
LYS CE   C N N 274 
LYS NZ   N N N 275 
LYS OXT  O N N 276 
LYS H    H N N 277 
LYS H2   H N N 278 
LYS HA   H N N 279 
LYS HB2  H N N 280 
LYS HB3  H N N 281 
LYS HG2  H N N 282 
LYS HG3  H N N 283 
LYS HD2  H N N 284 
LYS HD3  H N N 285 
LYS HE2  H N N 286 
LYS HE3  H N N 287 
LYS HZ1  H N N 288 
LYS HZ2  H N N 289 
LYS HZ3  H N N 290 
LYS HXT  H N N 291 
MET N    N N N 292 
MET CA   C N S 293 
MET C    C N N 294 
MET O    O N N 295 
MET CB   C N N 296 
MET CG   C N N 297 
MET SD   S N N 298 
MET CE   C N N 299 
MET OXT  O N N 300 
MET H    H N N 301 
MET H2   H N N 302 
MET HA   H N N 303 
MET HB2  H N N 304 
MET HB3  H N N 305 
MET HG2  H N N 306 
MET HG3  H N N 307 
MET HE1  H N N 308 
MET HE2  H N N 309 
MET HE3  H N N 310 
MET HXT  H N N 311 
OLA C1   C N N 312 
OLA O1   O N N 313 
OLA O2   O N N 314 
OLA C2   C N N 315 
OLA C3   C N N 316 
OLA C4   C N N 317 
OLA C5   C N N 318 
OLA C6   C N N 319 
OLA C7   C N N 320 
OLA C8   C N N 321 
OLA C9   C N N 322 
OLA C10  C N N 323 
OLA C11  C N N 324 
OLA C12  C N N 325 
OLA C13  C N N 326 
OLA C14  C N N 327 
OLA C15  C N N 328 
OLA C16  C N N 329 
OLA C17  C N N 330 
OLA C18  C N N 331 
OLA HO2  H N N 332 
OLA H21  H N N 333 
OLA H22  H N N 334 
OLA H31  H N N 335 
OLA H32  H N N 336 
OLA H41  H N N 337 
OLA H42  H N N 338 
OLA H51  H N N 339 
OLA H52  H N N 340 
OLA H61  H N N 341 
OLA H62  H N N 342 
OLA H71  H N N 343 
OLA H72  H N N 344 
OLA H81  H N N 345 
OLA H82  H N N 346 
OLA H9   H N N 347 
OLA H10  H N N 348 
OLA H111 H N N 349 
OLA H112 H N N 350 
OLA H121 H N N 351 
OLA H122 H N N 352 
OLA H131 H N N 353 
OLA H132 H N N 354 
OLA H141 H N N 355 
OLA H142 H N N 356 
OLA H151 H N N 357 
OLA H152 H N N 358 
OLA H161 H N N 359 
OLA H162 H N N 360 
OLA H171 H N N 361 
OLA H172 H N N 362 
OLA H181 H N N 363 
OLA H182 H N N 364 
OLA H183 H N N 365 
PHE N    N N N 366 
PHE CA   C N S 367 
PHE C    C N N 368 
PHE O    O N N 369 
PHE CB   C N N 370 
PHE CG   C Y N 371 
PHE CD1  C Y N 372 
PHE CD2  C Y N 373 
PHE CE1  C Y N 374 
PHE CE2  C Y N 375 
PHE CZ   C Y N 376 
PHE OXT  O N N 377 
PHE H    H N N 378 
PHE H2   H N N 379 
PHE HA   H N N 380 
PHE HB2  H N N 381 
PHE HB3  H N N 382 
PHE HD1  H N N 383 
PHE HD2  H N N 384 
PHE HE1  H N N 385 
PHE HE2  H N N 386 
PHE HZ   H N N 387 
PHE HXT  H N N 388 
PO4 P    P N N 389 
PO4 O1   O N N 390 
PO4 O2   O N N 391 
PO4 O3   O N N 392 
PO4 O4   O N N 393 
PRO N    N N N 394 
PRO CA   C N S 395 
PRO C    C N N 396 
PRO O    O N N 397 
PRO CB   C N N 398 
PRO CG   C N N 399 
PRO CD   C N N 400 
PRO OXT  O N N 401 
PRO H    H N N 402 
PRO HA   H N N 403 
PRO HB2  H N N 404 
PRO HB3  H N N 405 
PRO HG2  H N N 406 
PRO HG3  H N N 407 
PRO HD2  H N N 408 
PRO HD3  H N N 409 
PRO HXT  H N N 410 
RET C1   C N N 411 
RET C2   C N N 412 
RET C3   C N N 413 
RET C4   C N N 414 
RET C5   C N N 415 
RET C6   C N N 416 
RET C7   C N N 417 
RET C8   C N N 418 
RET C9   C N N 419 
RET C10  C N N 420 
RET C11  C N N 421 
RET C12  C N N 422 
RET C13  C N N 423 
RET C14  C N N 424 
RET C15  C N N 425 
RET O1   O N N 426 
RET C16  C N N 427 
RET C17  C N N 428 
RET C18  C N N 429 
RET C19  C N N 430 
RET C20  C N N 431 
RET H21  H N N 432 
RET H22  H N N 433 
RET H31  H N N 434 
RET H32  H N N 435 
RET H41  H N N 436 
RET H42  H N N 437 
RET H7   H N N 438 
RET H8   H N N 439 
RET H10  H N N 440 
RET H11  H N N 441 
RET H12  H N N 442 
RET H14  H N N 443 
RET H15  H N N 444 
RET H161 H N N 445 
RET H162 H N N 446 
RET H163 H N N 447 
RET H171 H N N 448 
RET H172 H N N 449 
RET H173 H N N 450 
RET H181 H N N 451 
RET H182 H N N 452 
RET H183 H N N 453 
RET H191 H N N 454 
RET H192 H N N 455 
RET H193 H N N 456 
RET H201 H N N 457 
RET H202 H N N 458 
RET H203 H N N 459 
SER N    N N N 460 
SER CA   C N S 461 
SER C    C N N 462 
SER O    O N N 463 
SER CB   C N N 464 
SER OG   O N N 465 
SER OXT  O N N 466 
SER H    H N N 467 
SER H2   H N N 468 
SER HA   H N N 469 
SER HB2  H N N 470 
SER HB3  H N N 471 
SER HG   H N N 472 
SER HXT  H N N 473 
THR N    N N N 474 
THR CA   C N S 475 
THR C    C N N 476 
THR O    O N N 477 
THR CB   C N R 478 
THR OG1  O N N 479 
THR CG2  C N N 480 
THR OXT  O N N 481 
THR H    H N N 482 
THR H2   H N N 483 
THR HA   H N N 484 
THR HB   H N N 485 
THR HG1  H N N 486 
THR HG21 H N N 487 
THR HG22 H N N 488 
THR HG23 H N N 489 
THR HXT  H N N 490 
TRP N    N N N 491 
TRP CA   C N S 492 
TRP C    C N N 493 
TRP O    O N N 494 
TRP CB   C N N 495 
TRP CG   C Y N 496 
TRP CD1  C Y N 497 
TRP CD2  C Y N 498 
TRP NE1  N Y N 499 
TRP CE2  C Y N 500 
TRP CE3  C Y N 501 
TRP CZ2  C Y N 502 
TRP CZ3  C Y N 503 
TRP CH2  C Y N 504 
TRP OXT  O N N 505 
TRP H    H N N 506 
TRP H2   H N N 507 
TRP HA   H N N 508 
TRP HB2  H N N 509 
TRP HB3  H N N 510 
TRP HD1  H N N 511 
TRP HE1  H N N 512 
TRP HE3  H N N 513 
TRP HZ2  H N N 514 
TRP HZ3  H N N 515 
TRP HH2  H N N 516 
TRP HXT  H N N 517 
TYR N    N N N 518 
TYR CA   C N S 519 
TYR C    C N N 520 
TYR O    O N N 521 
TYR CB   C N N 522 
TYR CG   C Y N 523 
TYR CD1  C Y N 524 
TYR CD2  C Y N 525 
TYR CE1  C Y N 526 
TYR CE2  C Y N 527 
TYR CZ   C Y N 528 
TYR OH   O N N 529 
TYR OXT  O N N 530 
TYR H    H N N 531 
TYR H2   H N N 532 
TYR HA   H N N 533 
TYR HB2  H N N 534 
TYR HB3  H N N 535 
TYR HD1  H N N 536 
TYR HD2  H N N 537 
TYR HE1  H N N 538 
TYR HE2  H N N 539 
TYR HH   H N N 540 
TYR HXT  H N N 541 
VAL N    N N N 542 
VAL CA   C N S 543 
VAL C    C N N 544 
VAL O    O N N 545 
VAL CB   C N N 546 
VAL CG1  C N N 547 
VAL CG2  C N N 548 
VAL OXT  O N N 549 
VAL H    H N N 550 
VAL H2   H N N 551 
VAL HA   H N N 552 
VAL HB   H N N 553 
VAL HG11 H N N 554 
VAL HG12 H N N 555 
VAL HG13 H N N 556 
VAL HG21 H N N 557 
VAL HG22 H N N 558 
VAL HG23 H N N 559 
VAL HXT  H N N 560 
# 
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 
LFA C1  C2   sing N N 194 
LFA C1  H11  sing N N 195 
LFA C1  H12  sing N N 196 
LFA C1  H13  sing N N 197 
LFA C2  C3   sing N N 198 
LFA C2  H21  sing N N 199 
LFA C2  H22  sing N N 200 
LFA C3  C4   sing N N 201 
LFA C3  H31  sing N N 202 
LFA C3  H32  sing N N 203 
LFA C4  C5   sing N N 204 
LFA C4  H41  sing N N 205 
LFA C4  H42  sing N N 206 
LFA C5  C6   sing N N 207 
LFA C5  H51  sing N N 208 
LFA C5  H52  sing N N 209 
LFA C6  C7   sing N N 210 
LFA C6  H61  sing N N 211 
LFA C6  H62  sing N N 212 
LFA C7  C8   sing N N 213 
LFA C7  H71  sing N N 214 
LFA C7  H72  sing N N 215 
LFA C8  C9   sing N N 216 
LFA C8  H81  sing N N 217 
LFA C8  H82  sing N N 218 
LFA C9  C10  sing N N 219 
LFA C9  H91  sing N N 220 
LFA C9  H92  sing N N 221 
LFA C10 C11  sing N N 222 
LFA C10 H101 sing N N 223 
LFA C10 H102 sing N N 224 
LFA C11 C12  sing N N 225 
LFA C11 H111 sing N N 226 
LFA C11 H112 sing N N 227 
LFA C12 C13  sing N N 228 
LFA C12 H121 sing N N 229 
LFA C12 H122 sing N N 230 
LFA C13 C14  sing N N 231 
LFA C13 H131 sing N N 232 
LFA C13 H132 sing N N 233 
LFA C14 C15  sing N N 234 
LFA C14 H141 sing N N 235 
LFA C14 H142 sing N N 236 
LFA C15 C16  sing N N 237 
LFA C15 H151 sing N N 238 
LFA C15 H152 sing N N 239 
LFA C16 C17  sing N N 240 
LFA C16 H161 sing N N 241 
LFA C16 H162 sing N N 242 
LFA C17 C18  sing N N 243 
LFA C17 H171 sing N N 244 
LFA C17 H172 sing N N 245 
LFA C18 C19  sing N N 246 
LFA C18 H181 sing N N 247 
LFA C18 H182 sing N N 248 
LFA C19 C20  sing N N 249 
LFA C19 H191 sing N N 250 
LFA C19 H192 sing N N 251 
LFA C20 H201 sing N N 252 
LFA C20 H202 sing N N 253 
LFA C20 H203 sing N N 254 
LYS N   CA   sing N N 255 
LYS N   H    sing N N 256 
LYS N   H2   sing N N 257 
LYS CA  C    sing N N 258 
LYS CA  CB   sing N N 259 
LYS CA  HA   sing N N 260 
LYS C   O    doub N N 261 
LYS C   OXT  sing N N 262 
LYS CB  CG   sing N N 263 
LYS CB  HB2  sing N N 264 
LYS CB  HB3  sing N N 265 
LYS CG  CD   sing N N 266 
LYS CG  HG2  sing N N 267 
LYS CG  HG3  sing N N 268 
LYS CD  CE   sing N N 269 
LYS CD  HD2  sing N N 270 
LYS CD  HD3  sing N N 271 
LYS CE  NZ   sing N N 272 
LYS CE  HE2  sing N N 273 
LYS CE  HE3  sing N N 274 
LYS NZ  HZ1  sing N N 275 
LYS NZ  HZ2  sing N N 276 
LYS NZ  HZ3  sing N N 277 
LYS OXT HXT  sing N N 278 
MET N   CA   sing N N 279 
MET N   H    sing N N 280 
MET N   H2   sing N N 281 
MET CA  C    sing N N 282 
MET CA  CB   sing N N 283 
MET CA  HA   sing N N 284 
MET C   O    doub N N 285 
MET C   OXT  sing N N 286 
MET CB  CG   sing N N 287 
MET CB  HB2  sing N N 288 
MET CB  HB3  sing N N 289 
MET CG  SD   sing N N 290 
MET CG  HG2  sing N N 291 
MET CG  HG3  sing N N 292 
MET SD  CE   sing N N 293 
MET CE  HE1  sing N N 294 
MET CE  HE2  sing N N 295 
MET CE  HE3  sing N N 296 
MET OXT HXT  sing N N 297 
OLA C1  O1   doub N N 298 
OLA C1  O2   sing N N 299 
OLA C1  C2   sing N N 300 
OLA O2  HO2  sing N N 301 
OLA C2  C3   sing N N 302 
OLA C2  H21  sing N N 303 
OLA C2  H22  sing N N 304 
OLA C3  C4   sing N N 305 
OLA C3  H31  sing N N 306 
OLA C3  H32  sing N N 307 
OLA C4  C5   sing N N 308 
OLA C4  H41  sing N N 309 
OLA C4  H42  sing N N 310 
OLA C5  C6   sing N N 311 
OLA C5  H51  sing N N 312 
OLA C5  H52  sing N N 313 
OLA C6  C7   sing N N 314 
OLA C6  H61  sing N N 315 
OLA C6  H62  sing N N 316 
OLA C7  C8   sing N N 317 
OLA C7  H71  sing N N 318 
OLA C7  H72  sing N N 319 
OLA C8  C9   sing N N 320 
OLA C8  H81  sing N N 321 
OLA C8  H82  sing N N 322 
OLA C9  C10  doub N Z 323 
OLA C9  H9   sing N N 324 
OLA C10 C11  sing N N 325 
OLA C10 H10  sing N N 326 
OLA C11 C12  sing N N 327 
OLA C11 H111 sing N N 328 
OLA C11 H112 sing N N 329 
OLA C12 C13  sing N N 330 
OLA C12 H121 sing N N 331 
OLA C12 H122 sing N N 332 
OLA C13 C14  sing N N 333 
OLA C13 H131 sing N N 334 
OLA C13 H132 sing N N 335 
OLA C14 C15  sing N N 336 
OLA C14 H141 sing N N 337 
OLA C14 H142 sing N N 338 
OLA C15 C16  sing N N 339 
OLA C15 H151 sing N N 340 
OLA C15 H152 sing N N 341 
OLA C16 C17  sing N N 342 
OLA C16 H161 sing N N 343 
OLA C16 H162 sing N N 344 
OLA C17 C18  sing N N 345 
OLA C17 H171 sing N N 346 
OLA C17 H172 sing N N 347 
OLA C18 H181 sing N N 348 
OLA C18 H182 sing N N 349 
OLA C18 H183 sing N N 350 
PHE N   CA   sing N N 351 
PHE N   H    sing N N 352 
PHE N   H2   sing N N 353 
PHE CA  C    sing N N 354 
PHE CA  CB   sing N N 355 
PHE CA  HA   sing N N 356 
PHE C   O    doub N N 357 
PHE C   OXT  sing N N 358 
PHE CB  CG   sing N N 359 
PHE CB  HB2  sing N N 360 
PHE CB  HB3  sing N N 361 
PHE CG  CD1  doub Y N 362 
PHE CG  CD2  sing Y N 363 
PHE CD1 CE1  sing Y N 364 
PHE CD1 HD1  sing N N 365 
PHE CD2 CE2  doub Y N 366 
PHE CD2 HD2  sing N N 367 
PHE CE1 CZ   doub Y N 368 
PHE CE1 HE1  sing N N 369 
PHE CE2 CZ   sing Y N 370 
PHE CE2 HE2  sing N N 371 
PHE CZ  HZ   sing N N 372 
PHE OXT HXT  sing N N 373 
PO4 P   O1   doub N N 374 
PO4 P   O2   sing N N 375 
PO4 P   O3   sing N N 376 
PO4 P   O4   sing N N 377 
PRO N   CA   sing N N 378 
PRO N   CD   sing N N 379 
PRO N   H    sing N N 380 
PRO CA  C    sing N N 381 
PRO CA  CB   sing N N 382 
PRO CA  HA   sing N N 383 
PRO C   O    doub N N 384 
PRO C   OXT  sing N N 385 
PRO CB  CG   sing N N 386 
PRO CB  HB2  sing N N 387 
PRO CB  HB3  sing N N 388 
PRO CG  CD   sing N N 389 
PRO CG  HG2  sing N N 390 
PRO CG  HG3  sing N N 391 
PRO CD  HD2  sing N N 392 
PRO CD  HD3  sing N N 393 
PRO OXT HXT  sing N N 394 
RET C1  C2   sing N N 395 
RET C1  C6   sing N N 396 
RET C1  C16  sing N N 397 
RET C1  C17  sing N N 398 
RET C2  C3   sing N N 399 
RET C2  H21  sing N N 400 
RET C2  H22  sing N N 401 
RET C3  C4   sing N N 402 
RET C3  H31  sing N N 403 
RET C3  H32  sing N N 404 
RET C4  C5   sing N N 405 
RET C4  H41  sing N N 406 
RET C4  H42  sing N N 407 
RET C5  C6   doub N N 408 
RET C5  C18  sing N N 409 
RET C6  C7   sing N N 410 
RET C7  C8   doub N E 411 
RET C7  H7   sing N N 412 
RET C8  C9   sing N N 413 
RET C8  H8   sing N N 414 
RET C9  C10  doub N E 415 
RET C9  C19  sing N N 416 
RET C10 C11  sing N N 417 
RET C10 H10  sing N N 418 
RET C11 C12  doub N E 419 
RET C11 H11  sing N N 420 
RET C12 C13  sing N N 421 
RET C12 H12  sing N N 422 
RET C13 C14  doub N E 423 
RET C13 C20  sing N N 424 
RET C14 C15  sing N N 425 
RET C14 H14  sing N N 426 
RET C15 O1   doub N N 427 
RET C15 H15  sing N N 428 
RET C16 H161 sing N N 429 
RET C16 H162 sing N N 430 
RET C16 H163 sing N N 431 
RET C17 H171 sing N N 432 
RET C17 H172 sing N N 433 
RET C17 H173 sing N N 434 
RET C18 H181 sing N N 435 
RET C18 H182 sing N N 436 
RET C18 H183 sing N N 437 
RET C19 H191 sing N N 438 
RET C19 H192 sing N N 439 
RET C19 H193 sing N N 440 
RET C20 H201 sing N N 441 
RET C20 H202 sing N N 442 
RET C20 H203 sing N N 443 
SER N   CA   sing N N 444 
SER N   H    sing N N 445 
SER N   H2   sing N N 446 
SER CA  C    sing N N 447 
SER CA  CB   sing N N 448 
SER CA  HA   sing N N 449 
SER C   O    doub N N 450 
SER C   OXT  sing N N 451 
SER CB  OG   sing N N 452 
SER CB  HB2  sing N N 453 
SER CB  HB3  sing N N 454 
SER OG  HG   sing N N 455 
SER OXT HXT  sing N N 456 
THR N   CA   sing N N 457 
THR N   H    sing N N 458 
THR N   H2   sing N N 459 
THR CA  C    sing N N 460 
THR CA  CB   sing N N 461 
THR CA  HA   sing N N 462 
THR C   O    doub N N 463 
THR C   OXT  sing N N 464 
THR CB  OG1  sing N N 465 
THR CB  CG2  sing N N 466 
THR CB  HB   sing N N 467 
THR OG1 HG1  sing N N 468 
THR CG2 HG21 sing N N 469 
THR CG2 HG22 sing N N 470 
THR CG2 HG23 sing N N 471 
THR OXT HXT  sing N N 472 
TRP N   CA   sing N N 473 
TRP N   H    sing N N 474 
TRP N   H2   sing N N 475 
TRP CA  C    sing N N 476 
TRP CA  CB   sing N N 477 
TRP CA  HA   sing N N 478 
TRP C   O    doub N N 479 
TRP C   OXT  sing N N 480 
TRP CB  CG   sing N N 481 
TRP CB  HB2  sing N N 482 
TRP CB  HB3  sing N N 483 
TRP CG  CD1  doub Y N 484 
TRP CG  CD2  sing Y N 485 
TRP CD1 NE1  sing Y N 486 
TRP CD1 HD1  sing N N 487 
TRP CD2 CE2  doub Y N 488 
TRP CD2 CE3  sing Y N 489 
TRP NE1 CE2  sing Y N 490 
TRP NE1 HE1  sing N N 491 
TRP CE2 CZ2  sing Y N 492 
TRP CE3 CZ3  doub Y N 493 
TRP CE3 HE3  sing N N 494 
TRP CZ2 CH2  doub Y N 495 
TRP CZ2 HZ2  sing N N 496 
TRP CZ3 CH2  sing Y N 497 
TRP CZ3 HZ3  sing N N 498 
TRP CH2 HH2  sing N N 499 
TRP OXT HXT  sing N N 500 
TYR N   CA   sing N N 501 
TYR N   H    sing N N 502 
TYR N   H2   sing N N 503 
TYR CA  C    sing N N 504 
TYR CA  CB   sing N N 505 
TYR CA  HA   sing N N 506 
TYR C   O    doub N N 507 
TYR C   OXT  sing N N 508 
TYR CB  CG   sing N N 509 
TYR CB  HB2  sing N N 510 
TYR CB  HB3  sing N N 511 
TYR CG  CD1  doub Y N 512 
TYR CG  CD2  sing Y N 513 
TYR CD1 CE1  sing Y N 514 
TYR CD1 HD1  sing N N 515 
TYR CD2 CE2  doub Y N 516 
TYR CD2 HD2  sing N N 517 
TYR CE1 CZ   doub Y N 518 
TYR CE1 HE1  sing N N 519 
TYR CE2 CZ   sing Y N 520 
TYR CE2 HE2  sing N N 521 
TYR CZ  OH   sing N N 522 
TYR OH  HH   sing N N 523 
TYR OXT HXT  sing N N 524 
VAL N   CA   sing N N 525 
VAL N   H    sing N N 526 
VAL N   H2   sing N N 527 
VAL CA  C    sing N N 528 
VAL CA  CB   sing N N 529 
VAL CA  HA   sing N N 530 
VAL C   O    doub N N 531 
VAL C   OXT  sing N N 532 
VAL CB  CG1  sing N N 533 
VAL CB  CG2  sing N N 534 
VAL CB  HB   sing N N 535 
VAL CG1 HG11 sing N N 536 
VAL CG1 HG12 sing N N 537 
VAL CG1 HG13 sing N N 538 
VAL CG2 HG21 sing N N 539 
VAL CG2 HG22 sing N N 540 
VAL CG2 HG23 sing N N 541 
VAL OXT HXT  sing N N 542 
# 
_pdbx_audit_support.funding_organization   'EIPOD fellowship under Marie Sklodowska-Curie Actions COFUND' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           847543 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8R96 
_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]   0.011687 
_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]   0.003382 
_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]   0.005391 
_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 
P 
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   . THR A  1 4   ? 10.247  65.925 37.047  1.00 111.84 ? 4   THR A N   1 
ATOM   2     C CA  . THR A  1 4   ? 10.983  66.616 35.951  1.00 113.95 ? 4   THR A CA  1 
ATOM   3     C C   . THR A  1 4   ? 9.981   67.130 34.909  1.00 116.28 ? 4   THR A C   1 
ATOM   4     O O   . THR A  1 4   ? 8.787   67.252 35.245  1.00 127.22 ? 4   THR A O   1 
ATOM   5     C CB  . THR A  1 4   ? 12.021  65.682 35.316  1.00 96.64  ? 4   THR A CB  1 
ATOM   6     N N   . ASN A  1 5   ? 10.465  67.429 33.699  1.00 116.45 ? 5   ASN A N   1 
ATOM   7     C CA  . ASN A  1 5   ? 9.647   67.836 32.524  1.00 118.40 ? 5   ASN A CA  1 
ATOM   8     C C   . ASN A  1 5   ? 10.278  67.211 31.275  1.00 120.15 ? 5   ASN A C   1 
ATOM   9     O O   . ASN A  1 5   ? 11.514  67.032 31.276  1.00 121.81 ? 5   ASN A O   1 
ATOM   10    C CB  . ASN A  1 5   ? 9.532   69.360 32.419  1.00 113.32 ? 5   ASN A CB  1 
ATOM   11    C CG  . ASN A  1 5   ? 8.106   69.830 32.224  1.00 110.49 ? 5   ASN A CG  1 
ATOM   12    O OD1 . ASN A  1 5   ? 7.477   70.317 33.161  1.00 97.96  ? 5   ASN A OD1 1 
ATOM   13    N ND2 . ASN A  1 5   ? 7.584   69.675 31.019  1.00 111.70 ? 5   ASN A ND2 1 
ATOM   14    N N   . VAL A  1 6   ? 9.470   66.886 30.259  1.00 111.49 ? 6   VAL A N   1 
ATOM   15    C CA  . VAL A  1 6   ? 9.908   66.082 29.077  1.00 104.89 ? 6   VAL A CA  1 
ATOM   16    C C   . VAL A  1 6   ? 10.674  66.983 28.106  1.00 90.58  ? 6   VAL A C   1 
ATOM   17    O O   . VAL A  1 6   ? 10.058  67.900 27.535  1.00 72.51  ? 6   VAL A O   1 
ATOM   18    C CB  . VAL A  1 6   ? 8.731   65.394 28.364  1.00 108.43 ? 6   VAL A CB  1 
ATOM   19    C CG1 . VAL A  1 6   ? 9.221   64.477 27.255  1.00 110.71 ? 6   VAL A CG1 1 
ATOM   20    C CG2 . VAL A  1 6   ? 7.842   64.638 29.336  1.00 106.82 ? 6   VAL A CG2 1 
ATOM   21    N N   . SER A  1 7   ? 11.971  66.717 27.945  1.00 89.50  ? 7   SER A N   1 
ATOM   22    C CA  . SER A  1 7   ? 12.873  67.383 26.972  1.00 85.32  ? 7   SER A CA  1 
ATOM   23    C C   . SER A  1 7   ? 13.061  66.459 25.764  1.00 79.08  ? 7   SER A C   1 
ATOM   24    O O   . SER A  1 7   ? 13.949  65.583 25.827  1.00 78.91  ? 7   SER A O   1 
ATOM   25    C CB  . SER A  1 7   ? 14.187  67.733 27.619  1.00 85.98  ? 7   SER A CB  1 
ATOM   26    O OG  . SER A  1 7   ? 13.978  68.284 28.910  1.00 86.13  ? 7   SER A OG  1 
ATOM   27    N N   . VAL A  1 8   ? 12.233  66.631 24.727  1.00 67.71  ? 8   VAL A N   1 
ATOM   28    C CA  . VAL A  1 8   ? 12.226  65.776 23.502  1.00 61.57  ? 8   VAL A CA  1 
ATOM   29    C C   . VAL A  1 8   ? 13.642  65.720 22.940  1.00 62.22  ? 8   VAL A C   1 
ATOM   30    O O   . VAL A  1 8   ? 14.302  66.746 22.792  1.00 68.53  ? 8   VAL A O   1 
ATOM   31    C CB  . VAL A  1 8   ? 11.220  66.279 22.449  1.00 59.90  ? 8   VAL A CB  1 
ATOM   32    C CG1 . VAL A  1 8   ? 9.789   66.195 22.954  1.00 54.81  ? 8   VAL A CG1 1 
ATOM   33    C CG2 . VAL A  1 8   ? 11.543  67.689 21.982  1.00 72.10  ? 8   VAL A CG2 1 
ATOM   34    N N   . PRO A  1 9   ? 14.150  64.509 22.619  1.00 60.21  ? 9   PRO A N   1 
ATOM   35    C CA  . PRO A  1 9   ? 15.539  64.331 22.198  1.00 59.63  ? 9   PRO A CA  1 
ATOM   36    C C   . PRO A  1 9   ? 15.817  64.871 20.787  1.00 63.88  ? 9   PRO A C   1 
ATOM   37    O O   . PRO A  1 9   ? 16.976  65.078 20.462  1.00 69.80  ? 9   PRO A O   1 
ATOM   38    C CB  . PRO A  1 9   ? 15.747  62.807 22.233  1.00 57.07  ? 9   PRO A CB  1 
ATOM   39    C CG  . PRO A  1 9   ? 14.536  62.255 22.967  1.00 55.76  ? 9   PRO A CG  1 
ATOM   40    C CD  . PRO A  1 9   ? 13.421  63.236 22.677  1.00 56.69  ? 9   PRO A CD  1 
ATOM   41    N N   . TRP A  1 10  ? 14.762  65.080 19.992  1.00 60.06  ? 10  TRP A N   1 
ATOM   42    C CA  . TRP A  1 10  ? 14.853  65.587 18.596  1.00 62.63  ? 10  TRP A CA  1 
ATOM   43    C C   . TRP A  1 10  ? 14.853  67.121 18.596  1.00 61.01  ? 10  TRP A C   1 
ATOM   44    O O   . TRP A  1 10  ? 14.665  67.713 17.513  1.00 59.05  ? 10  TRP A O   1 
ATOM   45    C CB  . TRP A  1 10  ? 13.723  65.013 17.729  1.00 62.24  ? 10  TRP A CB  1 
ATOM   46    C CG  . TRP A  1 10  ? 12.347  65.221 18.285  1.00 59.62  ? 10  TRP A CG  1 
ATOM   47    C CD1 . TRP A  1 10  ? 11.560  66.328 18.146  1.00 58.73  ? 10  TRP A CD1 1 
ATOM   48    C CD2 . TRP A  1 10  ? 11.584  64.285 19.066  1.00 57.63  ? 10  TRP A CD2 1 
ATOM   49    N NE1 . TRP A  1 10  ? 10.366  66.148 18.791  1.00 56.20  ? 10  TRP A NE1 1 
ATOM   50    C CE2 . TRP A  1 10  ? 10.350  64.904 19.363  1.00 56.18  ? 10  TRP A CE2 1 
ATOM   51    C CE3 . TRP A  1 10  ? 11.821  62.991 19.542  1.00 54.53  ? 10  TRP A CE3 1 
ATOM   52    C CZ2 . TRP A  1 10  ? 9.362   64.269 20.115  1.00 54.11  ? 10  TRP A CZ2 1 
ATOM   53    C CZ3 . TRP A  1 10  ? 10.845  62.367 20.287  1.00 53.15  ? 10  TRP A CZ3 1 
ATOM   54    C CH2 . TRP A  1 10  ? 9.633   62.998 20.566  1.00 52.96  ? 10  TRP A CH2 1 
ATOM   55    N N   . GLY A  1 11  ? 15.057  67.731 19.768  1.00 59.29  ? 11  GLY A N   1 
ATOM   56    C CA  . GLY A  1 11  ? 15.199  69.190 19.932  1.00 61.87  ? 11  GLY A CA  1 
ATOM   57    C C   . GLY A  1 11  ? 16.658  69.593 20.052  1.00 62.28  ? 11  GLY A C   1 
ATOM   58    O O   . GLY A  1 11  ? 16.987  70.741 19.693  1.00 68.51  ? 11  GLY A O   1 
ATOM   59    N N   . ALA A  1 12  ? 17.504  68.670 20.521  1.00 58.07  ? 12  ALA A N   1 
ATOM   60    C CA  . ALA A  1 12  ? 18.942  68.886 20.805  1.00 60.88  ? 12  ALA A CA  1 
ATOM   61    C C   . ALA A  1 12  ? 19.738  68.944 19.496  1.00 62.28  ? 12  ALA A C   1 
ATOM   62    O O   . ALA A  1 12  ? 19.559  68.049 18.646  1.00 69.81  ? 12  ALA A O   1 
ATOM   63    C CB  . ALA A  1 12  ? 19.458  67.790 21.707  1.00 64.16  ? 12  ALA A CB  1 
ATOM   64    N N   . THR A  1 13  ? 20.594  69.961 19.360  1.00 63.85  ? 13  THR A N   1 
ATOM   65    C CA  . THR A  1 13  ? 21.574  70.120 18.254  1.00 61.83  ? 13  THR A CA  1 
ATOM   66    C C   . THR A  1 13  ? 22.740  69.150 18.484  1.00 61.77  ? 13  THR A C   1 
ATOM   67    O O   . THR A  1 13  ? 23.136  68.973 19.652  1.00 63.69  ? 13  THR A O   1 
ATOM   68    C CB  . THR A  1 13  ? 22.046  71.575 18.150  1.00 58.10  ? 13  THR A CB  1 
ATOM   69    O OG1 . THR A  1 13  ? 20.919  72.362 17.766  1.00 67.66  ? 13  THR A OG1 1 
ATOM   70    C CG2 . THR A  1 13  ? 23.168  71.773 17.155  1.00 57.95  ? 13  THR A CG2 1 
ATOM   71    N N   . LEU A  1 14  ? 23.262  68.549 17.411  1.00 60.11  ? 14  LEU A N   1 
ATOM   72    C CA  . LEU A  1 14  ? 24.362  67.549 17.462  1.00 58.88  ? 14  LEU A CA  1 
ATOM   73    C C   . LEU A  1 14  ? 25.657  68.176 16.936  1.00 57.43  ? 14  LEU A C   1 
ATOM   74    O O   . LEU A  1 14  ? 25.591  68.922 15.939  1.00 51.22  ? 14  LEU A O   1 
ATOM   75    C CB  . LEU A  1 14  ? 23.981  66.333 16.612  1.00 60.15  ? 14  LEU A CB  1 
ATOM   76    C CG  . LEU A  1 14  ? 22.687  65.625 17.003  1.00 60.21  ? 14  LEU A CG  1 
ATOM   77    C CD1 . LEU A  1 14  ? 22.330  64.560 15.980  1.00 62.23  ? 14  LEU A CD1 1 
ATOM   78    C CD2 . LEU A  1 14  ? 22.798  65.017 18.391  1.00 61.60  ? 14  LEU A CD2 1 
ATOM   79    N N   . SER A  1 15  ? 26.787  67.868 17.580  1.00 55.74  ? 15  SER A N   1 
ATOM   80    C CA  . SER A  1 15  ? 28.152  68.154 17.066  1.00 60.63  ? 15  SER A CA  1 
ATOM   81    C C   . SER A  1 15  ? 28.404  67.272 15.838  1.00 61.15  ? 15  SER A C   1 
ATOM   82    O O   . SER A  1 15  ? 27.582  66.368 15.585  1.00 66.39  ? 15  SER A O   1 
ATOM   83    C CB  . SER A  1 15  ? 29.198  67.931 18.127  1.00 61.31  ? 15  SER A CB  1 
ATOM   84    O OG  . SER A  1 15  ? 29.324  66.549 18.432  1.00 57.57  ? 15  SER A OG  1 
ATOM   85    N N   . ASN A  1 16  ? 29.491  67.526 15.105  1.00 58.07  ? 16  ASN A N   1 
ATOM   86    C CA  . ASN A  1 16  ? 29.905  66.703 13.938  1.00 57.97  ? 16  ASN A CA  1 
ATOM   87    C C   . ASN A  1 16  ? 30.279  65.302 14.433  1.00 61.63  ? 16  ASN A C   1 
ATOM   88    O O   . ASN A  1 16  ? 29.840  64.316 13.804  1.00 60.45  ? 16  ASN A O   1 
ATOM   89    C CB  . ASN A  1 16  ? 31.053  67.349 13.162  1.00 53.99  ? 16  ASN A CB  1 
ATOM   90    C CG  . ASN A  1 16  ? 30.608  68.553 12.364  1.00 59.91  ? 16  ASN A CG  1 
ATOM   91    O OD1 . ASN A  1 16  ? 29.441  68.937 12.406  1.00 69.13  ? 16  ASN A OD1 1 
ATOM   92    N ND2 . ASN A  1 16  ? 31.530  69.153 11.631  1.00 72.85  ? 16  ASN A ND2 1 
ATOM   93    N N   . ALA A  1 17  ? 31.055  65.230 15.519  1.00 57.23  ? 17  ALA A N   1 
ATOM   94    C CA  . ALA A  1 17  ? 31.489  63.974 16.173  1.00 58.17  ? 17  ALA A CA  1 
ATOM   95    C C   . ALA A  1 17  ? 30.264  63.092 16.440  1.00 62.25  ? 17  ALA A C   1 
ATOM   96    O O   . ALA A  1 17  ? 30.302  61.895 16.085  1.00 70.24  ? 17  ALA A O   1 
ATOM   97    C CB  . ALA A  1 17  ? 32.231  64.289 17.448  1.00 58.85  ? 17  ALA A CB  1 
ATOM   98    N N   . GLU A  1 18  ? 29.220  63.674 17.037  1.00 59.93  ? 18  GLU A N   1 
ATOM   99    C CA  . GLU A  1 18  ? 27.963  62.972 17.409  1.00 66.00  ? 18  GLU A CA  1 
ATOM   100   C C   . GLU A  1 18  ? 27.256  62.494 16.135  1.00 65.57  ? 18  GLU A C   1 
ATOM   101   O O   . GLU A  1 18  ? 26.945  61.290 16.047  1.00 68.06  ? 18  GLU A O   1 
ATOM   102   C CB  . GLU A  1 18  ? 27.077  63.898 18.246  1.00 75.65  ? 18  GLU A CB  1 
ATOM   103   C CG  . GLU A  1 18  ? 27.615  64.142 19.646  1.00 80.50  ? 18  GLU A CG  1 
ATOM   104   C CD  . GLU A  1 18  ? 26.992  65.314 20.385  1.00 87.96  ? 18  GLU A CD  1 
ATOM   105   O OE1 . GLU A  1 18  ? 26.973  65.279 21.631  1.00 94.57  ? 18  GLU A OE1 1 
ATOM   106   O OE2 . GLU A  1 18  ? 26.537  66.264 19.718  1.00 87.98  ? 18  GLU A OE2 1 
ATOM   107   N N   . HIS A  1 19  ? 27.023  63.404 15.184  1.00 59.25  ? 19  HIS A N   1 
ATOM   108   C CA  . HIS A  1 19  ? 26.330  63.134 13.895  1.00 55.16  ? 19  HIS A CA  1 
ATOM   109   C C   . HIS A  1 19  ? 27.037  61.992 13.153  1.00 55.03  ? 19  HIS A C   1 
ATOM   110   O O   . HIS A  1 19  ? 26.338  61.182 12.512  1.00 53.19  ? 19  HIS A O   1 
ATOM   111   C CB  . HIS A  1 19  ? 26.263  64.414 13.052  1.00 50.38  ? 19  HIS A CB  1 
ATOM   112   C CG  . HIS A  1 19  ? 25.389  64.299 11.849  1.00 49.88  ? 19  HIS A CG  1 
ATOM   113   N ND1 . HIS A  1 19  ? 25.885  63.963 10.603  1.00 55.23  ? 19  HIS A ND1 1 
ATOM   114   C CD2 . HIS A  1 19  ? 24.059  64.475 11.693  1.00 48.39  ? 19  HIS A CD2 1 
ATOM   115   C CE1 . HIS A  1 19  ? 24.897  63.939 9.731   1.00 54.17  ? 19  HIS A CE1 1 
ATOM   116   N NE2 . HIS A  1 19  ? 23.765  64.249 10.376  1.00 47.87  ? 19  HIS A NE2 1 
ATOM   117   N N   . GLN A  1 20  ? 28.370  61.937 13.242  1.00 53.18  ? 20  GLN A N   1 
ATOM   118   C CA  . GLN A  1 20  ? 29.217  60.923 12.559  1.00 56.02  ? 20  GLN A CA  1 
ATOM   119   C C   . GLN A  1 20  ? 29.052  59.573 13.270  1.00 56.86  ? 20  GLN A C   1 
ATOM   120   O O   . GLN A  1 20  ? 28.941  58.544 12.573  1.00 57.78  ? 20  GLN A O   1 
ATOM   121   C CB  . GLN A  1 20  ? 30.680  61.373 12.551  1.00 57.24  ? 20  GLN A CB  1 
ATOM   122   C CG  . GLN A  1 20  ? 31.488  60.818 11.385  1.00 63.03  ? 20  GLN A CG  1 
ATOM   123   C CD  . GLN A  1 20  ? 31.300  61.616 10.117  1.00 67.86  ? 20  GLN A CD  1 
ATOM   124   O OE1 . GLN A  1 20  ? 30.784  62.731 10.129  1.00 100.19 ? 20  GLN A OE1 1 
ATOM   125   N NE2 . GLN A  1 20  ? 31.731  61.049 9.002   1.00 62.28  ? 20  GLN A NE2 1 
ATOM   126   N N   . LEU A  1 21  ? 29.033  59.588 14.606  1.00 57.40  ? 21  LEU A N   1 
ATOM   127   C CA  . LEU A  1 21  ? 28.906  58.380 15.465  1.00 59.89  ? 21  LEU A CA  1 
ATOM   128   C C   . LEU A  1 21  ? 27.548  57.713 15.223  1.00 55.07  ? 21  LEU A C   1 
ATOM   129   O O   . LEU A  1 21  ? 27.521  56.486 15.020  1.00 54.93  ? 21  LEU A O   1 
ATOM   130   C CB  . LEU A  1 21  ? 29.049  58.788 16.934  1.00 67.38  ? 21  LEU A CB  1 
ATOM   131   C CG  . LEU A  1 21  ? 30.479  58.874 17.460  1.00 71.66  ? 21  LEU A CG  1 
ATOM   132   C CD1 . LEU A  1 21  ? 30.491  59.340 18.907  1.00 74.89  ? 21  LEU A CD1 1 
ATOM   133   C CD2 . LEU A  1 21  ? 31.190  57.536 17.321  1.00 74.59  ? 21  LEU A CD2 1 
ATOM   134   N N   . ILE A  1 22  ? 26.468  58.496 15.265  1.00 54.14  ? 22  ILE A N   1 
ATOM   135   C CA  . ILE A  1 22  ? 25.069  58.002 15.100  1.00 58.12  ? 22  ILE A CA  1 
ATOM   136   C C   . ILE A  1 22  ? 24.968  57.272 13.756  1.00 59.62  ? 22  ILE A C   1 
ATOM   137   O O   . ILE A  1 22  ? 24.569  56.089 13.757  1.00 66.00  ? 22  ILE A O   1 
ATOM   138   C CB  . ILE A  1 22  ? 24.054  59.157 15.212  1.00 58.23  ? 22  ILE A CB  1 
ATOM   139   C CG1 . ILE A  1 22  ? 24.087  59.805 16.599  1.00 58.87  ? 22  ILE A CG1 1 
ATOM   140   C CG2 . ILE A  1 22  ? 22.656  58.680 14.850  1.00 54.56  ? 22  ILE A CG2 1 
ATOM   141   C CD1 . ILE A  1 22  ? 23.407  61.152 16.666  1.00 56.80  ? 22  ILE A CD1 1 
ATOM   142   N N   . PHE A  1 23  ? 25.332  57.948 12.662  1.00 48.16  ? 23  PHE A N   1 
ATOM   143   C CA  . PHE A  1 23  ? 25.300  57.400 11.280  1.00 47.89  ? 23  PHE A CA  1 
ATOM   144   C C   . PHE A  1 23  ? 26.071  56.074 11.234  1.00 49.58  ? 23  PHE A C   1 
ATOM   145   O O   . PHE A  1 23  ? 25.528  55.077 10.721  1.00 47.17  ? 23  PHE A O   1 
ATOM   146   C CB  . PHE A  1 23  ? 25.884  58.404 10.284  1.00 46.03  ? 23  PHE A CB  1 
ATOM   147   C CG  . PHE A  1 23  ? 25.809  57.965 8.843   1.00 46.94  ? 23  PHE A CG  1 
ATOM   148   C CD1 . PHE A  1 23  ? 26.947  57.568 8.160   1.00 49.22  ? 23  PHE A CD1 1 
ATOM   149   C CD2 . PHE A  1 23  ? 24.598  57.944 8.170   1.00 48.97  ? 23  PHE A CD2 1 
ATOM   150   C CE1 . PHE A  1 23  ? 26.876  57.172 6.833   1.00 48.58  ? 23  PHE A CE1 1 
ATOM   151   C CE2 . PHE A  1 23  ? 24.528  57.544 6.844   1.00 47.25  ? 23  PHE A CE2 1 
ATOM   152   C CZ  . PHE A  1 23  ? 25.667  57.158 6.179   1.00 44.03  ? 23  PHE A CZ  1 
ATOM   153   N N   . TYR A  1 24  ? 27.302  56.077 11.754  1.00 47.30  ? 24  TYR A N   1 
ATOM   154   C CA  . TYR A  1 24  ? 28.212  54.903 11.820  1.00 42.56  ? 24  TYR A CA  1 
ATOM   155   C C   . TYR A  1 24  ? 27.448  53.692 12.372  1.00 44.59  ? 24  TYR A C   1 
ATOM   156   O O   . TYR A  1 24  ? 27.369  52.665 11.675  1.00 43.09  ? 24  TYR A O   1 
ATOM   157   C CB  . TYR A  1 24  ? 29.437  55.231 12.679  1.00 41.55  ? 24  TYR A CB  1 
ATOM   158   C CG  . TYR A  1 24  ? 30.388  54.081 12.901  1.00 40.10  ? 24  TYR A CG  1 
ATOM   159   C CD1 . TYR A  1 24  ? 30.297  53.283 14.030  1.00 37.28  ? 24  TYR A CD1 1 
ATOM   160   C CD2 . TYR A  1 24  ? 31.390  53.796 11.987  1.00 40.81  ? 24  TYR A CD2 1 
ATOM   161   C CE1 . TYR A  1 24  ? 31.169  52.228 14.241  1.00 43.23  ? 24  TYR A CE1 1 
ATOM   162   C CE2 . TYR A  1 24  ? 32.271  52.746 12.182  1.00 43.15  ? 24  TYR A CE2 1 
ATOM   163   C CZ  . TYR A  1 24  ? 32.161  51.958 13.314  1.00 45.35  ? 24  TYR A CZ  1 
ATOM   164   O OH  . TYR A  1 24  ? 33.027  50.921 13.512  1.00 41.21  ? 24  TYR A OH  1 
ATOM   165   N N   . PHE A  1 25  ? 26.900  53.818 13.584  1.00 45.24  ? 25  PHE A N   1 
ATOM   166   C CA  . PHE A  1 25  ? 26.214  52.726 14.325  1.00 47.45  ? 25  PHE A CA  1 
ATOM   167   C C   . PHE A  1 25  ? 24.936  52.320 13.586  1.00 49.24  ? 25  PHE A C   1 
ATOM   168   O O   . PHE A  1 25  ? 24.652  51.109 13.507  1.00 52.29  ? 25  PHE A O   1 
ATOM   169   C CB  . PHE A  1 25  ? 25.931  53.148 15.768  1.00 51.00  ? 25  PHE A CB  1 
ATOM   170   C CG  . PHE A  1 25  ? 27.112  52.979 16.689  1.00 59.03  ? 25  PHE A CG  1 
ATOM   171   C CD1 . PHE A  1 25  ? 27.386  51.750 17.267  1.00 58.75  ? 25  PHE A CD1 1 
ATOM   172   C CD2 . PHE A  1 25  ? 27.957  54.042 16.966  1.00 64.94  ? 25  PHE A CD2 1 
ATOM   173   C CE1 . PHE A  1 25  ? 28.477  51.589 18.107  1.00 61.30  ? 25  PHE A CE1 1 
ATOM   174   C CE2 . PHE A  1 25  ? 29.048  53.880 17.804  1.00 64.23  ? 25  PHE A CE2 1 
ATOM   175   C CZ  . PHE A  1 25  ? 29.305  52.654 18.373  1.00 66.60  ? 25  PHE A CZ  1 
ATOM   176   N N   . LEU A  1 26  ? 24.199  53.300 13.056  1.00 46.32  ? 26  LEU A N   1 
ATOM   177   C CA  . LEU A  1 26  ? 22.953  53.065 12.280  1.00 44.25  ? 26  LEU A CA  1 
ATOM   178   C C   . LEU A  1 26  ? 23.257  52.127 11.107  1.00 41.22  ? 26  LEU A C   1 
ATOM   179   O O   . LEU A  1 26  ? 22.594  51.078 11.005  1.00 44.40  ? 26  LEU A O   1 
ATOM   180   C CB  . LEU A  1 26  ? 22.395  54.403 11.784  1.00 43.66  ? 26  LEU A CB  1 
ATOM   181   C CG  . LEU A  1 26  ? 21.517  55.159 12.780  1.00 43.33  ? 26  LEU A CG  1 
ATOM   182   C CD1 . LEU A  1 26  ? 20.828  56.333 12.106  1.00 46.25  ? 26  LEU A CD1 1 
ATOM   183   C CD2 . LEU A  1 26  ? 20.491  54.235 13.418  1.00 43.99  ? 26  LEU A CD2 1 
ATOM   184   N N   . VAL A  1 27  ? 24.231  52.493 10.269  1.00 37.78  ? 27  VAL A N   1 
ATOM   185   C CA  . VAL A  1 27  ? 24.585  51.763 9.015   1.00 37.82  ? 27  VAL A CA  1 
ATOM   186   C C   . VAL A  1 27  ? 25.234  50.423 9.383   1.00 40.51  ? 27  VAL A C   1 
ATOM   187   O O   . VAL A  1 27  ? 24.874  49.406 8.760   1.00 45.46  ? 27  VAL A O   1 
ATOM   188   C CB  . VAL A  1 27  ? 25.498  52.606 8.105   1.00 34.87  ? 27  VAL A CB  1 
ATOM   189   C CG1 . VAL A  1 27  ? 25.886  51.849 6.845   1.00 36.35  ? 27  VAL A CG1 1 
ATOM   190   C CG2 . VAL A  1 27  ? 24.863  53.942 7.752   1.00 33.87  ? 27  VAL A CG2 1 
ATOM   191   N N   . VAL A  1 28  ? 26.150  50.418 10.355  1.00 42.73  ? 28  VAL A N   1 
ATOM   192   C CA  . VAL A  1 28  ? 26.813  49.179 10.863  1.00 43.65  ? 28  VAL A CA  1 
ATOM   193   C C   . VAL A  1 28  ? 25.719  48.183 11.258  1.00 42.98  ? 28  VAL A C   1 
ATOM   194   O O   . VAL A  1 28  ? 25.844  46.995 10.901  1.00 40.83  ? 28  VAL A O   1 
ATOM   195   C CB  . VAL A  1 28  ? 27.761  49.476 12.041  1.00 41.46  ? 28  VAL A CB  1 
ATOM   196   C CG1 . VAL A  1 28  ? 28.171  48.208 12.775  1.00 38.06  ? 28  VAL A CG1 1 
ATOM   197   C CG2 . VAL A  1 28  ? 28.986  50.251 11.583  1.00 44.78  ? 28  VAL A CG2 1 
ATOM   198   N N   . ALA A  1 29  ? 24.687  48.662 11.957  1.00 42.37  ? 29  ALA A N   1 
ATOM   199   C CA  . ALA A  1 29  ? 23.505  47.874 12.372  1.00 45.60  ? 29  ALA A CA  1 
ATOM   200   C C   . ALA A  1 29  ? 22.856  47.257 11.128  1.00 51.99  ? 29  ALA A C   1 
ATOM   201   O O   . ALA A  1 29  ? 22.782  46.016 11.053  1.00 53.64  ? 29  ALA A O   1 
ATOM   202   C CB  . ALA A  1 29  ? 22.537  48.755 13.125  1.00 47.49  ? 29  ALA A CB  1 
ATOM   203   N N   . ALA A  1 30  ? 22.416  48.103 10.191  1.00 54.50  ? 30  ALA A N   1 
ATOM   204   C CA  . ALA A  1 30  ? 21.748  47.715 8.925   1.00 49.31  ? 30  ALA A CA  1 
ATOM   205   C C   . ALA A  1 30  ? 22.531  46.584 8.249   1.00 44.77  ? 30  ALA A C   1 
ATOM   206   O O   . ALA A  1 30  ? 21.901  45.586 7.853   1.00 50.45  ? 30  ALA A O   1 
ATOM   207   C CB  . ALA A  1 30  ? 21.625  48.918 8.023   1.00 48.69  ? 30  ALA A CB  1 
ATOM   208   N N   . LEU A  1 31  ? 23.853  46.739 8.131   1.00 40.49  ? 31  LEU A N   1 
ATOM   209   C CA  . LEU A  1 31  ? 24.756  45.779 7.441   1.00 43.13  ? 31  LEU A CA  1 
ATOM   210   C C   . LEU A  1 31  ? 24.844  44.480 8.250   1.00 43.31  ? 31  LEU A C   1 
ATOM   211   O O   . LEU A  1 31  ? 24.833  43.394 7.636   1.00 39.83  ? 31  LEU A O   1 
ATOM   212   C CB  . LEU A  1 31  ? 26.134  46.427 7.271   1.00 44.07  ? 31  LEU A CB  1 
ATOM   213   C CG  . LEU A  1 31  ? 26.177  47.616 6.313   1.00 45.86  ? 31  LEU A CG  1 
ATOM   214   C CD1 . LEU A  1 31  ? 27.506  48.349 6.410   1.00 50.05  ? 31  LEU A CD1 1 
ATOM   215   C CD2 . LEU A  1 31  ? 25.918  47.168 4.884   1.00 43.77  ? 31  LEU A CD2 1 
ATOM   216   N N   . ALA A  1 32  ? 24.938  44.591 9.577   1.00 43.44  ? 32  ALA A N   1 
ATOM   217   C CA  . ALA A  1 32  ? 24.936  43.449 10.518  1.00 40.94  ? 32  ALA A CA  1 
ATOM   218   C C   . ALA A  1 32  ? 23.694  42.593 10.254  1.00 42.49  ? 32  ALA A C   1 
ATOM   219   O O   . ALA A  1 32  ? 23.809  41.352 10.271  1.00 41.88  ? 32  ALA A O   1 
ATOM   220   C CB  . ALA A  1 32  ? 24.966  43.949 11.941  1.00 41.58  ? 32  ALA A CB  1 
ATOM   221   N N   . PHE A  1 33  ? 22.554  43.248 10.015  1.00 44.78  ? 33  PHE A N   1 
ATOM   222   C CA  . PHE A  1 33  ? 21.232  42.608 9.794   1.00 48.54  ? 33  PHE A CA  1 
ATOM   223   C C   . PHE A  1 33  ? 21.215  41.930 8.419   1.00 46.27  ? 33  PHE A C   1 
ATOM   224   O O   . PHE A  1 33  ? 20.657  40.822 8.310   1.00 46.60  ? 33  PHE A O   1 
ATOM   225   C CB  . PHE A  1 33  ? 20.110  43.637 9.956   1.00 49.10  ? 33  PHE A CB  1 
ATOM   226   C CG  . PHE A  1 33  ? 19.825  44.034 11.384  1.00 48.67  ? 33  PHE A CG  1 
ATOM   227   C CD1 . PHE A  1 33  ? 19.726  43.077 12.382  1.00 45.09  ? 33  PHE A CD1 1 
ATOM   228   C CD2 . PHE A  1 33  ? 19.635  45.364 11.729  1.00 54.07  ? 33  PHE A CD2 1 
ATOM   229   C CE1 . PHE A  1 33  ? 19.451  43.440 13.691  1.00 44.44  ? 33  PHE A CE1 1 
ATOM   230   C CE2 . PHE A  1 33  ? 19.362  45.727 13.039  1.00 51.07  ? 33  PHE A CE2 1 
ATOM   231   C CZ  . PHE A  1 33  ? 19.268  44.764 14.017  1.00 49.19  ? 33  PHE A CZ  1 
ATOM   232   N N   . VAL A  1 34  ? 21.814  42.569 7.409   1.00 48.05  ? 34  VAL A N   1 
ATOM   233   C CA  . VAL A  1 34  ? 22.015  41.984 6.049   1.00 45.77  ? 34  VAL A CA  1 
ATOM   234   C C   . VAL A  1 34  ? 22.765  40.657 6.205   1.00 44.66  ? 34  VAL A C   1 
ATOM   235   O O   . VAL A  1 34  ? 22.259  39.630 5.716   1.00 42.39  ? 34  VAL A O   1 
ATOM   236   C CB  . VAL A  1 34  ? 22.774  42.950 5.118   1.00 40.61  ? 34  VAL A CB  1 
ATOM   237   C CG1 . VAL A  1 34  ? 23.408  42.224 3.941   1.00 38.11  ? 34  VAL A CG1 1 
ATOM   238   C CG2 . VAL A  1 34  ? 21.883  44.084 4.636   1.00 40.05  ? 34  VAL A CG2 1 
ATOM   239   N N   . ALA A  1 35  ? 23.926  40.689 6.868   1.00 47.02  ? 35  ALA A N   1 
ATOM   240   C CA  . ALA A  1 35  ? 24.793  39.518 7.136   1.00 49.22  ? 35  ALA A CA  1 
ATOM   241   C C   . ALA A  1 35  ? 23.989  38.446 7.879   1.00 47.49  ? 35  ALA A C   1 
ATOM   242   O O   . ALA A  1 35  ? 24.089  37.261 7.501   1.00 54.26  ? 35  ALA A O   1 
ATOM   243   C CB  . ALA A  1 35  ? 26.004  39.945 7.929   1.00 50.08  ? 35  ALA A CB  1 
ATOM   244   N N   . GLY A  1 36  ? 23.229  38.857 8.899   1.00 41.05  ? 36  GLY A N   1 
ATOM   245   C CA  . GLY A  1 36  ? 22.365  37.972 9.703   1.00 38.50  ? 36  GLY A CA  1 
ATOM   246   C C   . GLY A  1 36  ? 21.303  37.315 8.842   1.00 37.44  ? 36  GLY A C   1 
ATOM   247   O O   . GLY A  1 36  ? 21.184  36.072 8.888   1.00 33.68  ? 36  GLY A O   1 
ATOM   248   N N   . PHE A  1 37  ? 20.567  38.124 8.074   1.00 37.74  ? 37  PHE A N   1 
ATOM   249   C CA  . PHE A  1 37  ? 19.490  37.675 7.155   1.00 37.90  ? 37  PHE A CA  1 
ATOM   250   C C   . PHE A  1 37  ? 20.042  36.592 6.225   1.00 38.76  ? 37  PHE A C   1 
ATOM   251   O O   . PHE A  1 37  ? 19.427  35.517 6.119   1.00 41.81  ? 37  PHE A O   1 
ATOM   252   C CB  . PHE A  1 37  ? 18.932  38.847 6.345   1.00 37.79  ? 37  PHE A CB  1 
ATOM   253   C CG  . PHE A  1 37  ? 17.775  38.471 5.457   1.00 38.94  ? 37  PHE A CG  1 
ATOM   254   C CD1 . PHE A  1 37  ? 16.469  38.607 5.900   1.00 41.57  ? 37  PHE A CD1 1 
ATOM   255   C CD2 . PHE A  1 37  ? 17.994  37.947 4.193   1.00 40.87  ? 37  PHE A CD2 1 
ATOM   256   C CE1 . PHE A  1 37  ? 15.407  38.243 5.088   1.00 44.37  ? 37  PHE A CE1 1 
ATOM   257   C CE2 . PHE A  1 37  ? 16.931  37.584 3.383   1.00 41.58  ? 37  PHE A CE2 1 
ATOM   258   C CZ  . PHE A  1 37  ? 15.640  37.733 3.832   1.00 44.84  ? 37  PHE A CZ  1 
ATOM   259   N N   . ILE A  1 38  ? 21.172  36.877 5.574   1.00 38.16  ? 38  ILE A N   1 
ATOM   260   C CA  . ILE A  1 38  ? 21.849  35.955 4.616   1.00 37.39  ? 38  ILE A CA  1 
ATOM   261   C C   . ILE A  1 38  ? 22.178  34.646 5.343   1.00 41.52  ? 38  ILE A C   1 
ATOM   262   O O   . ILE A  1 38  ? 21.747  33.580 4.861   1.00 42.63  ? 38  ILE A O   1 
ATOM   263   C CB  . ILE A  1 38  ? 23.104  36.614 4.013   1.00 36.01  ? 38  ILE A CB  1 
ATOM   264   C CG1 . ILE A  1 38  ? 22.742  37.827 3.154   1.00 37.68  ? 38  ILE A CG1 1 
ATOM   265   C CG2 . ILE A  1 38  ? 23.922  35.599 3.232   1.00 40.44  ? 38  ILE A CG2 1 
ATOM   266   C CD1 . ILE A  1 38  ? 23.935  38.528 2.547   1.00 41.56  ? 38  ILE A CD1 1 
ATOM   267   N N   . ARG A  1 39  ? 22.909  34.724 6.458   1.00 47.98  ? 39  ARG A N   1 
ATOM   268   C CA  . ARG A  1 39  ? 23.295  33.534 7.262   1.00 57.19  ? 39  ARG A CA  1 
ATOM   269   C C   . ARG A  1 39  ? 22.038  32.713 7.563   1.00 49.60  ? 39  ARG A C   1 
ATOM   270   O O   . ARG A  1 39  ? 22.044  31.499 7.286   1.00 48.09  ? 39  ARG A O   1 
ATOM   271   C CB  . ARG A  1 39  ? 23.987  33.931 8.569   1.00 69.98  ? 39  ARG A CB  1 
ATOM   272   C CG  . ARG A  1 39  ? 24.431  32.738 9.403   1.00 77.60  ? 39  ARG A CG  1 
ATOM   273   C CD  . ARG A  1 39  ? 24.972  33.140 10.763  1.00 86.05  ? 39  ARG A CD  1 
ATOM   274   N NE  . ARG A  1 39  ? 26.242  32.494 11.074  1.00 99.30  ? 39  ARG A NE  1 
ATOM   275   C CZ  . ARG A  1 39  ? 26.894  32.620 12.225  1.00 106.51 ? 39  ARG A CZ  1 
ATOM   276   N NH1 . ARG A  1 39  ? 26.395  33.366 13.196  1.00 108.63 ? 39  ARG A NH1 1 
ATOM   277   N NH2 . ARG A  1 39  ? 28.045  31.996 12.403  1.00 110.52 ? 39  ARG A NH2 1 
ATOM   278   N N   . THR A  1 40  ? 21.001  33.363 8.099   1.00 43.04  ? 40  THR A N   1 
ATOM   279   C CA  . THR A  1 40  ? 19.730  32.720 8.524   1.00 49.11  ? 40  THR A CA  1 
ATOM   280   C C   . THR A  1 40  ? 19.106  31.975 7.339   1.00 53.51  ? 40  THR A C   1 
ATOM   281   O O   . THR A  1 40  ? 18.666  30.820 7.533   1.00 68.33  ? 40  THR A O   1 
ATOM   282   C CB  . THR A  1 40  ? 18.751  33.745 9.106   1.00 51.30  ? 40  THR A CB  1 
ATOM   283   O OG1 . THR A  1 40  ? 19.282  34.202 10.350  1.00 53.67  ? 40  THR A OG1 1 
ATOM   284   C CG2 . THR A  1 40  ? 17.365  33.175 9.317   1.00 52.36  ? 40  THR A CG2 1 
ATOM   285   N N   . TYR A  1 41  ? 19.065  32.613 6.166   1.00 53.37  ? 41  TYR A N   1 
ATOM   286   C CA  . TYR A  1 41  ? 18.468  32.057 4.924   1.00 52.63  ? 41  TYR A CA  1 
ATOM   287   C C   . TYR A  1 41  ? 19.235  30.795 4.511   1.00 50.67  ? 41  TYR A C   1 
ATOM   288   O O   . TYR A  1 41  ? 18.596  29.774 4.220   1.00 52.61  ? 41  TYR A O   1 
ATOM   289   C CB  . TYR A  1 41  ? 18.466  33.094 3.798   1.00 52.25  ? 41  TYR A CB  1 
ATOM   290   C CG  . TYR A  1 41  ? 17.866  32.592 2.509   1.00 59.70  ? 41  TYR A CG  1 
ATOM   291   C CD1 . TYR A  1 41  ? 18.670  32.190 1.456   1.00 63.89  ? 41  TYR A CD1 1 
ATOM   292   C CD2 . TYR A  1 41  ? 16.494  32.486 2.353   1.00 64.90  ? 41  TYR A CD2 1 
ATOM   293   C CE1 . TYR A  1 41  ? 18.128  31.715 0.273   1.00 71.14  ? 41  TYR A CE1 1 
ATOM   294   C CE2 . TYR A  1 41  ? 15.935  32.007 1.180   1.00 69.95  ? 41  TYR A CE2 1 
ATOM   295   C CZ  . TYR A  1 41  ? 16.754  31.622 0.134   1.00 74.02  ? 41  TYR A CZ  1 
ATOM   296   O OH  . TYR A  1 41  ? 16.209  31.151 -1.026  1.00 80.02  ? 41  TYR A OH  1 
ATOM   297   N N   . ILE A  1 42  ? 20.567  30.866 4.492   1.00 49.93  ? 42  ILE A N   1 
ATOM   298   C CA  . ILE A  1 42  ? 21.462  29.780 3.990   1.00 51.45  ? 42  ILE A CA  1 
ATOM   299   C C   . ILE A  1 42  ? 21.361  28.559 4.913   1.00 48.68  ? 42  ILE A C   1 
ATOM   300   O O   . ILE A  1 42  ? 21.462  27.428 4.401   1.00 45.48  ? 42  ILE A O   1 
ATOM   301   C CB  . ILE A  1 42  ? 22.910  30.292 3.855   1.00 56.71  ? 42  ILE A CB  1 
ATOM   302   C CG1 . ILE A  1 42  ? 23.080  31.133 2.588   1.00 61.44  ? 42  ILE A CG1 1 
ATOM   303   C CG2 . ILE A  1 42  ? 23.909  29.146 3.912   1.00 59.05  ? 42  ILE A CG2 1 
ATOM   304   C CD1 . ILE A  1 42  ? 24.400  30.920 1.881   1.00 67.36  ? 42  ILE A CD1 1 
ATOM   305   N N   . THR A  1 43  ? 21.164  28.782 6.216   1.00 50.22  ? 43  THR A N   1 
ATOM   306   C CA  . THR A  1 43  ? 21.155  27.726 7.264   1.00 52.85  ? 43  THR A CA  1 
ATOM   307   C C   . THR A  1 43  ? 19.714  27.333 7.613   1.00 57.44  ? 43  THR A C   1 
ATOM   308   O O   . THR A  1 43  ? 19.506  26.773 8.707   1.00 61.70  ? 43  THR A O   1 
ATOM   309   C CB  . THR A  1 43  ? 21.917  28.191 8.512   1.00 52.02  ? 43  THR A CB  1 
ATOM   310   O OG1 . THR A  1 43  ? 21.240  29.322 9.061   1.00 50.96  ? 43  THR A OG1 1 
ATOM   311   C CG2 . THR A  1 43  ? 23.357  28.549 8.215   1.00 54.08  ? 43  THR A CG2 1 
ATOM   312   N N   . ARG A  1 44  ? 18.761  27.594 6.713   1.00 55.87  ? 44  ARG A N   1 
ATOM   313   C CA  . ARG A  1 44  ? 17.308  27.400 6.969   1.00 54.89  ? 44  ARG A CA  1 
ATOM   314   C C   . ARG A  1 44  ? 16.982  25.900 7.018   1.00 53.60  ? 44  ARG A C   1 
ATOM   315   O O   . ARG A  1 44  ? 16.125  25.510 7.836   1.00 53.36  ? 44  ARG A O   1 
ATOM   316   C CB  . ARG A  1 44  ? 16.471  28.130 5.912   1.00 55.07  ? 44  ARG A CB  1 
ATOM   317   C CG  . ARG A  1 44  ? 16.535  27.533 4.512   1.00 54.57  ? 44  ARG A CG  1 
ATOM   318   C CD  . ARG A  1 44  ? 15.815  28.403 3.494   1.00 55.29  ? 44  ARG A CD  1 
ATOM   319   N NE  . ARG A  1 44  ? 15.743  27.796 2.172   1.00 54.77  ? 44  ARG A NE  1 
ATOM   320   C CZ  . ARG A  1 44  ? 16.661  27.938 1.221   1.00 64.87  ? 44  ARG A CZ  1 
ATOM   321   N NH1 . ARG A  1 44  ? 17.736  28.674 1.438   1.00 68.38  ? 44  ARG A NH1 1 
ATOM   322   N NH2 . ARG A  1 44  ? 16.500  27.346 0.050   1.00 78.30  ? 44  ARG A NH2 1 
ATOM   323   N N   . ASN A  1 45  ? 17.653  25.089 6.196   1.00 53.03  ? 45  ASN A N   1 
ATOM   324   C CA  . ASN A  1 45  ? 17.330  23.649 6.005   1.00 52.21  ? 45  ASN A CA  1 
ATOM   325   C C   . ASN A  1 45  ? 18.159  22.790 6.966   1.00 51.40  ? 45  ASN A C   1 
ATOM   326   O O   . ASN A  1 45  ? 18.246  21.571 6.734   1.00 60.51  ? 45  ASN A O   1 
ATOM   327   C CB  . ASN A  1 45  ? 17.536  23.222 4.551   1.00 53.87  ? 45  ASN A CB  1 
ATOM   328   C CG  . ASN A  1 45  ? 16.473  23.783 3.633   1.00 52.06  ? 45  ASN A CG  1 
ATOM   329   O OD1 . ASN A  1 45  ? 15.329  23.968 4.042   1.00 51.35  ? 45  ASN A OD1 1 
ATOM   330   N ND2 . ASN A  1 45  ? 16.839  24.055 2.392   1.00 56.84  ? 45  ASN A ND2 1 
ATOM   331   N N   . GLU A  1 46  ? 18.736  23.407 8.002   1.00 56.06  ? 46  GLU A N   1 
ATOM   332   C CA  . GLU A  1 46  ? 19.447  22.709 9.106   1.00 59.20  ? 46  GLU A CA  1 
ATOM   333   C C   . GLU A  1 46  ? 18.425  22.302 10.171  1.00 56.39  ? 46  GLU A C   1 
ATOM   334   O O   . GLU A  1 46  ? 18.840  21.746 11.203  1.00 57.15  ? 46  GLU A O   1 
ATOM   335   C CB  . GLU A  1 46  ? 20.523  23.611 9.717   1.00 64.26  ? 46  GLU A CB  1 
ATOM   336   C CG  . GLU A  1 46  ? 21.722  23.829 8.812   1.00 67.76  ? 46  GLU A CG  1 
ATOM   337   C CD  . GLU A  1 46  ? 22.841  24.657 9.422   1.00 71.70  ? 46  GLU A CD  1 
ATOM   338   O OE1 . GLU A  1 46  ? 23.890  24.807 8.765   1.00 74.83  ? 46  GLU A OE1 1 
ATOM   339   O OE2 . GLU A  1 46  ? 22.662  25.147 10.553  1.00 68.05  ? 46  GLU A OE2 1 
ATOM   340   N N   . VAL A  1 47  ? 17.142  22.578 9.922   1.00 54.84  ? 47  VAL A N   1 
ATOM   341   C CA  . VAL A  1 47  ? 16.042  22.438 10.922  1.00 56.60  ? 47  VAL A CA  1 
ATOM   342   C C   . VAL A  1 47  ? 14.889  21.643 10.300  1.00 59.59  ? 47  VAL A C   1 
ATOM   343   O O   . VAL A  1 47  ? 14.543  21.917 9.131   1.00 56.65  ? 47  VAL A O   1 
ATOM   344   C CB  . VAL A  1 47  ? 15.574  23.821 11.413  1.00 58.53  ? 47  VAL A CB  1 
ATOM   345   C CG1 . VAL A  1 47  ? 14.236  23.746 12.133  1.00 60.62  ? 47  VAL A CG1 1 
ATOM   346   C CG2 . VAL A  1 47  ? 16.622  24.487 12.291  1.00 60.45  ? 47  VAL A CG2 1 
ATOM   347   N N   . GLY A  1 48  ? 14.326  20.701 11.065  1.00 59.20  ? 48  GLY A N   1 
ATOM   348   C CA  . GLY A  1 48  ? 13.184  19.861 10.657  1.00 58.41  ? 48  GLY A CA  1 
ATOM   349   C C   . GLY A  1 48  ? 11.936  20.695 10.438  1.00 54.79  ? 48  GLY A C   1 
ATOM   350   O O   . GLY A  1 48  ? 11.837  21.774 11.053  1.00 47.51  ? 48  GLY A O   1 
ATOM   351   N N   . SER A  1 49  ? 11.018  20.215 9.594   1.00 56.33  ? 49  SER A N   1 
ATOM   352   C CA  . SER A  1 49  ? 9.749   20.902 9.239   1.00 59.88  ? 49  SER A CA  1 
ATOM   353   C C   . SER A  1 49  ? 8.984   21.263 10.517  1.00 65.96  ? 49  SER A C   1 
ATOM   354   O O   . SER A  1 49  ? 8.177   22.212 10.477  1.00 64.11  ? 49  SER A O   1 
ATOM   355   C CB  . SER A  1 49  ? 8.910   20.049 8.323   1.00 59.00  ? 49  SER A CB  1 
ATOM   356   O OG  . SER A  1 49  ? 8.547   18.830 8.956   1.00 52.91  ? 49  SER A OG  1 
ATOM   357   N N   . ARG A  1 50  ? 9.244   20.531 11.605  1.00 72.49  ? 50  ARG A N   1 
ATOM   358   C CA  . ARG A  1 50  ? 8.516   20.649 12.895  1.00 68.28  ? 50  ARG A CA  1 
ATOM   359   C C   . ARG A  1 50  ? 8.840   21.989 13.563  1.00 60.05  ? 50  ARG A C   1 
ATOM   360   O O   . ARG A  1 50  ? 7.949   22.537 14.233  1.00 57.76  ? 50  ARG A O   1 
ATOM   361   C CB  . ARG A  1 50  ? 8.888   19.496 13.831  1.00 73.32  ? 50  ARG A CB  1 
ATOM   362   C CG  . ARG A  1 50  ? 8.167   19.546 15.170  1.00 82.91  ? 50  ARG A CG  1 
ATOM   363   C CD  . ARG A  1 50  ? 8.560   18.410 16.091  1.00 90.32  ? 50  ARG A CD  1 
ATOM   364   N NE  . ARG A  1 50  ? 7.758   18.413 17.305  1.00 91.81  ? 50  ARG A NE  1 
ATOM   365   C CZ  . ARG A  1 50  ? 7.926   17.574 18.319  1.00 93.55  ? 50  ARG A CZ  1 
ATOM   366   N NH1 . ARG A  1 50  ? 8.876   16.656 18.266  1.00 90.64  ? 50  ARG A NH1 1 
ATOM   367   N NH2 . ARG A  1 50  ? 7.145   17.657 19.381  1.00 100.07 ? 50  ARG A NH2 1 
ATOM   368   N N   . TYR A  1 51  ? 10.069  22.485 13.394  1.00 60.57  ? 51  TYR A N   1 
ATOM   369   C CA  . TYR A  1 51  ? 10.598  23.685 14.094  1.00 64.92  ? 51  TYR A CA  1 
ATOM   370   C C   . TYR A  1 51  ? 10.861  24.814 13.090  1.00 63.97  ? 51  TYR A C   1 
ATOM   371   O O   . TYR A  1 51  ? 11.646  25.729 13.409  1.00 72.68  ? 51  TYR A O   1 
ATOM   372   C CB  . TYR A  1 51  ? 11.869  23.320 14.865  1.00 62.83  ? 51  TYR A CB  1 
ATOM   373   C CG  . TYR A  1 51  ? 11.704  22.169 15.825  1.00 63.61  ? 51  TYR A CG  1 
ATOM   374   C CD1 . TYR A  1 51  ? 10.996  22.318 17.006  1.00 67.23  ? 51  TYR A CD1 1 
ATOM   375   C CD2 . TYR A  1 51  ? 12.255  20.927 15.553  1.00 68.02  ? 51  TYR A CD2 1 
ATOM   376   C CE1 . TYR A  1 51  ? 10.837  21.265 17.891  1.00 68.07  ? 51  TYR A CE1 1 
ATOM   377   C CE2 . TYR A  1 51  ? 12.109  19.864 16.430  1.00 68.25  ? 51  TYR A CE2 1 
ATOM   378   C CZ  . TYR A  1 51  ? 11.399  20.033 17.605  1.00 70.29  ? 51  TYR A CZ  1 
ATOM   379   O OH  . TYR A  1 51  ? 11.251  18.990 18.473  1.00 77.77  ? 51  TYR A OH  1 
ATOM   380   N N   . ARG A  1 52  ? 10.218  24.759 11.920  1.00 58.64  ? 52  ARG A N   1 
ATOM   381   C CA  . ARG A  1 52  ? 10.461  25.713 10.804  1.00 60.41  ? 52  ARG A CA  1 
ATOM   382   C C   . ARG A  1 52  ? 9.910   27.098 11.167  1.00 62.84  ? 52  ARG A C   1 
ATOM   383   O O   . ARG A  1 52  ? 10.463  28.101 10.667  1.00 69.06  ? 52  ARG A O   1 
ATOM   384   C CB  . ARG A  1 52  ? 9.826   25.215 9.504   1.00 57.02  ? 52  ARG A CB  1 
ATOM   385   C CG  . ARG A  1 52  ? 10.139  26.094 8.302   1.00 57.89  ? 52  ARG A CG  1 
ATOM   386   C CD  . ARG A  1 52  ? 9.890   25.367 6.999   1.00 60.38  ? 52  ARG A CD  1 
ATOM   387   N NE  . ARG A  1 52  ? 10.673  24.143 6.910   1.00 59.38  ? 52  ARG A NE  1 
ATOM   388   C CZ  . ARG A  1 52  ? 10.280  23.045 6.276   1.00 59.87  ? 52  ARG A CZ  1 
ATOM   389   N NH1 . ARG A  1 52  ? 9.099   23.007 5.683   1.00 57.27  ? 52  ARG A NH1 1 
ATOM   390   N NH2 . ARG A  1 52  ? 11.063  21.982 6.253   1.00 70.01  ? 52  ARG A NH2 1 
ATOM   391   N N   . THR A  1 53  ? 8.857   27.154 11.988  1.00 61.99  ? 53  THR A N   1 
ATOM   392   C CA  . THR A  1 53  ? 8.221   28.420 12.440  1.00 64.70  ? 53  THR A CA  1 
ATOM   393   C C   . THR A  1 53  ? 9.285   29.292 13.117  1.00 62.52  ? 53  THR A C   1 
ATOM   394   O O   . THR A  1 53  ? 9.183   30.531 13.017  1.00 75.21  ? 53  THR A O   1 
ATOM   395   C CB  . THR A  1 53  ? 7.031   28.158 13.372  1.00 67.48  ? 53  THR A CB  1 
ATOM   396   O OG1 . THR A  1 53  ? 6.210   27.151 12.781  1.00 76.69  ? 53  THR A OG1 1 
ATOM   397   C CG2 . THR A  1 53  ? 6.207   29.401 13.631  1.00 65.23  ? 53  THR A CG2 1 
ATOM   398   N N   . ALA A  1 54  ? 10.263  28.663 13.775  1.00 54.54  ? 54  ALA A N   1 
ATOM   399   C CA  . ALA A  1 54  ? 11.407  29.332 14.436  1.00 59.30  ? 54  ALA A CA  1 
ATOM   400   C C   . ALA A  1 54  ? 12.235  30.076 13.383  1.00 60.63  ? 54  ALA A C   1 
ATOM   401   O O   . ALA A  1 54  ? 12.666  31.213 13.661  1.00 73.25  ? 54  ALA A O   1 
ATOM   402   C CB  . ALA A  1 54  ? 12.244  28.318 15.176  1.00 61.15  ? 54  ALA A CB  1 
ATOM   403   N N   . VAL A  1 55  ? 12.433  29.450 12.219  1.00 52.63  ? 55  VAL A N   1 
ATOM   404   C CA  . VAL A  1 55  ? 13.287  29.967 11.108  1.00 47.62  ? 55  VAL A CA  1 
ATOM   405   C C   . VAL A  1 55  ? 12.559  31.119 10.407  1.00 49.82  ? 55  VAL A C   1 
ATOM   406   O O   . VAL A  1 55  ? 13.162  32.206 10.271  1.00 57.58  ? 55  VAL A O   1 
ATOM   407   C CB  . VAL A  1 55  ? 13.647  28.854 10.107  1.00 45.64  ? 55  VAL A CB  1 
ATOM   408   C CG1 . VAL A  1 55  ? 14.499  29.382 8.962   1.00 44.45  ? 55  VAL A CG1 1 
ATOM   409   C CG2 . VAL A  1 55  ? 14.335  27.684 10.791  1.00 47.66  ? 55  VAL A CG2 1 
ATOM   410   N N   . SER A  1 56  ? 11.321  30.882 9.966   1.00 49.37  ? 56  SER A N   1 
ATOM   411   C CA  . SER A  1 56  ? 10.490  31.867 9.225   1.00 52.55  ? 56  SER A CA  1 
ATOM   412   C C   . SER A  1 56  ? 10.350  33.151 10.052  1.00 50.11  ? 56  SER A C   1 
ATOM   413   O O   . SER A  1 56  ? 10.393  34.248 9.458   1.00 54.77  ? 56  SER A O   1 
ATOM   414   C CB  . SER A  1 56  ? 9.148   31.288 8.857   1.00 54.50  ? 56  SER A CB  1 
ATOM   415   O OG  . SER A  1 56  ? 8.453   30.836 10.009  1.00 58.49  ? 56  SER A OG  1 
ATOM   416   N N   . ALA A  1 57  ? 10.200  33.014 11.373  1.00 44.91  ? 57  ALA A N   1 
ATOM   417   C CA  . ALA A  1 57  ? 10.088  34.136 12.333  1.00 44.49  ? 57  ALA A CA  1 
ATOM   418   C C   . ALA A  1 57  ? 11.415  34.902 12.378  1.00 46.71  ? 57  ALA A C   1 
ATOM   419   O O   . ALA A  1 57  ? 11.391  36.142 12.246  1.00 46.06  ? 57  ALA A O   1 
ATOM   420   C CB  . ALA A  1 57  ? 9.701   33.613 13.693  1.00 44.02  ? 57  ALA A CB  1 
ATOM   421   N N   . ARG A  1 58  ? 12.529  34.184 12.551  1.00 48.53  ? 58  ARG A N   1 
ATOM   422   C CA  . ARG A  1 58  ? 13.890  34.777 12.650  1.00 50.10  ? 58  ARG A CA  1 
ATOM   423   C C   . ARG A  1 58  ? 14.187  35.564 11.369  1.00 50.10  ? 58  ARG A C   1 
ATOM   424   O O   . ARG A  1 58  ? 14.607  36.734 11.473  1.00 53.22  ? 58  ARG A O   1 
ATOM   425   C CB  . ARG A  1 58  ? 14.939  33.688 12.891  1.00 47.88  ? 58  ARG A CB  1 
ATOM   426   C CG  . ARG A  1 58  ? 16.363  34.214 13.002  1.00 56.40  ? 58  ARG A CG  1 
ATOM   427   C CD  . ARG A  1 58  ? 17.314  33.215 13.637  1.00 71.26  ? 58  ARG A CD  1 
ATOM   428   N NE  . ARG A  1 58  ? 17.245  31.877 13.060  1.00 88.62  ? 58  ARG A NE  1 
ATOM   429   C CZ  . ARG A  1 58  ? 16.605  30.846 13.608  1.00 92.03  ? 58  ARG A CZ  1 
ATOM   430   N NH1 . ARG A  1 58  ? 15.960  30.992 14.754  1.00 95.29  ? 58  ARG A NH1 1 
ATOM   431   N NH2 . ARG A  1 58  ? 16.611  29.671 13.006  1.00 85.01  ? 58  ARG A NH2 1 
ATOM   432   N N   . LEU A  1 59  ? 13.976  34.945 10.204  1.00 49.73  ? 59  LEU A N   1 
ATOM   433   C CA  . LEU A  1 59  ? 14.236  35.575 8.884   1.00 47.41  ? 59  LEU A CA  1 
ATOM   434   C C   . LEU A  1 59  ? 13.275  36.755 8.702   1.00 45.40  ? 59  LEU A C   1 
ATOM   435   O O   . LEU A  1 59  ? 13.728  37.823 8.241   1.00 40.55  ? 59  LEU A O   1 
ATOM   436   C CB  . LEU A  1 59  ? 14.062  34.532 7.778   1.00 51.37  ? 59  LEU A CB  1 
ATOM   437   C CG  . LEU A  1 59  ? 14.788  34.851 6.472   1.00 55.34  ? 59  LEU A CG  1 
ATOM   438   C CD1 . LEU A  1 59  ? 16.268  35.096 6.719   1.00 54.54  ? 59  LEU A CD1 1 
ATOM   439   C CD2 . LEU A  1 59  ? 14.600  33.736 5.457   1.00 56.42  ? 59  LEU A CD2 1 
ATOM   440   N N   . GLY A  1 60  ? 12.003  36.560 9.060   1.00 43.78  ? 60  GLY A N   1 
ATOM   441   C CA  . GLY A  1 60  ? 10.973  37.616 9.058   1.00 44.57  ? 60  GLY A CA  1 
ATOM   442   C C   . GLY A  1 60  ? 11.435  38.842 9.826   1.00 44.21  ? 60  GLY A C   1 
ATOM   443   O O   . GLY A  1 60  ? 11.348  39.956 9.274   1.00 41.22  ? 60  GLY A O   1 
ATOM   444   N N   . MET A  1 61  ? 11.924  38.647 11.054  1.00 44.67  ? 61  MET A N   1 
ATOM   445   C CA  . MET A  1 61  ? 12.308  39.746 11.979  1.00 49.44  ? 61  MET A CA  1 
ATOM   446   C C   . MET A  1 61  ? 13.566  40.451 11.453  1.00 48.06  ? 61  MET A C   1 
ATOM   447   O O   . MET A  1 61  ? 13.620  41.695 11.534  1.00 52.81  ? 61  MET A O   1 
ATOM   448   C CB  . MET A  1 61  ? 12.564  39.217 13.394  1.00 54.95  ? 61  MET A CB  1 
ATOM   449   C CG  . MET A  1 61  ? 13.878  38.474 13.533  1.00 67.52  ? 61  MET A CG  1 
ATOM   450   S SD  . MET A  1 61  ? 14.838  39.049 14.948  1.00 67.28  ? 61  MET A SD  1 
ATOM   451   C CE  . MET A  1 61  ? 14.486  40.803 14.852  1.00 68.52  ? 61  MET A CE  1 
ATOM   452   N N   . LEU A  1 62  ? 14.534  39.691 10.931  1.00 43.65  ? 62  LEU A N   1 
ATOM   453   C CA  . LEU A  1 62  ? 15.804  40.236 10.380  1.00 42.76  ? 62  LEU A CA  1 
ATOM   454   C C   . LEU A  1 62  ? 15.493  41.075 9.134   1.00 42.71  ? 62  LEU A C   1 
ATOM   455   O O   . LEU A  1 62  ? 16.083  42.163 8.992   1.00 43.49  ? 62  LEU A O   1 
ATOM   456   C CB  . LEU A  1 62  ? 16.759  39.083 10.060  1.00 39.55  ? 62  LEU A CB  1 
ATOM   457   C CG  . LEU A  1 62  ? 17.354  38.376 11.278  1.00 43.39  ? 62  LEU A CG  1 
ATOM   458   C CD1 . LEU A  1 62  ? 18.188  37.177 10.855  1.00 46.87  ? 62  LEU A CD1 1 
ATOM   459   C CD2 . LEU A  1 62  ? 18.187  39.336 12.117  1.00 41.19  ? 62  LEU A CD2 1 
ATOM   460   N N   . GLY A  1 63  ? 14.593  40.585 8.276   1.00 41.87  ? 63  GLY A N   1 
ATOM   461   C CA  . GLY A  1 63  ? 14.098  41.313 7.092   1.00 40.60  ? 63  GLY A CA  1 
ATOM   462   C C   . GLY A  1 63  ? 13.486  42.647 7.484   1.00 39.95  ? 63  GLY A C   1 
ATOM   463   O O   . GLY A  1 63  ? 13.853  43.674 6.879   1.00 37.24  ? 63  GLY A O   1 
ATOM   464   N N   . VAL A  1 64  ? 12.588  42.630 8.472   1.00 42.10  ? 64  VAL A N   1 
ATOM   465   C CA  . VAL A  1 64  ? 11.899  43.835 9.018   1.00 44.84  ? 64  VAL A CA  1 
ATOM   466   C C   . VAL A  1 64  ? 12.959  44.806 9.551   1.00 44.50  ? 64  VAL A C   1 
ATOM   467   O O   . VAL A  1 64  ? 12.990  45.961 9.084   1.00 45.55  ? 64  VAL A O   1 
ATOM   468   C CB  . VAL A  1 64  ? 10.885  43.442 10.110  1.00 48.51  ? 64  VAL A CB  1 
ATOM   469   C CG1 . VAL A  1 64  ? 10.410  44.642 10.915  1.00 54.94  ? 64  VAL A CG1 1 
ATOM   470   C CG2 . VAL A  1 64  ? 9.703   42.685 9.525   1.00 47.78  ? 64  VAL A CG2 1 
ATOM   471   N N   . ALA A  1 65  ? 13.792  44.341 10.488  1.00 46.10  ? 65  ALA A N   1 
ATOM   472   C CA  . ALA A  1 65  ? 14.877  45.117 11.130  1.00 45.05  ? 65  ALA A CA  1 
ATOM   473   C C   . ALA A  1 65  ? 15.704  45.827 10.053  1.00 42.56  ? 65  ALA A C   1 
ATOM   474   O O   . ALA A  1 65  ? 15.850  47.065 10.121  1.00 40.22  ? 65  ALA A O   1 
ATOM   475   C CB  . ALA A  1 65  ? 15.734  44.196 11.962  1.00 44.67  ? 65  ALA A CB  1 
ATOM   476   N N   . LEU A  1 66  ? 16.221  45.053 9.098   1.00 41.74  ? 66  LEU A N   1 
ATOM   477   C CA  . LEU A  1 66  ? 17.013  45.539 7.940   1.00 45.02  ? 66  LEU A CA  1 
ATOM   478   C C   . LEU A  1 66  ? 16.323  46.763 7.323   1.00 44.29  ? 66  LEU A C   1 
ATOM   479   O O   . LEU A  1 66  ? 16.939  47.847 7.308   1.00 51.22  ? 66  LEU A O   1 
ATOM   480   C CB  . LEU A  1 66  ? 17.128  44.398 6.925   1.00 49.30  ? 66  LEU A CB  1 
ATOM   481   C CG  . LEU A  1 66  ? 18.263  44.522 5.911   1.00 52.63  ? 66  LEU A CG  1 
ATOM   482   C CD1 . LEU A  1 66  ? 18.125  43.468 4.826   1.00 54.36  ? 66  LEU A CD1 1 
ATOM   483   C CD2 . LEU A  1 66  ? 18.309  45.915 5.298   1.00 57.96  ? 66  LEU A CD2 1 
ATOM   484   N N   . LEU A  1 67  ? 15.090  46.587 6.839   1.00 39.43  ? 67  LEU A N   1 
ATOM   485   C CA  . LEU A  1 67  ? 14.311  47.625 6.112   1.00 38.63  ? 67  LEU A CA  1 
ATOM   486   C C   . LEU A  1 67  ? 14.017  48.802 7.046   1.00 36.19  ? 67  LEU A C   1 
ATOM   487   O O   . LEU A  1 67  ? 14.214  49.955 6.623   1.00 38.31  ? 67  LEU A O   1 
ATOM   488   C CB  . LEU A  1 67  ? 13.011  47.010 5.587   1.00 40.28  ? 67  LEU A CB  1 
ATOM   489   C CG  . LEU A  1 67  ? 13.181  45.906 4.546   1.00 42.93  ? 67  LEU A CG  1 
ATOM   490   C CD1 . LEU A  1 67  ? 11.829  45.383 4.097   1.00 48.59  ? 67  LEU A CD1 1 
ATOM   491   C CD2 . LEU A  1 67  ? 13.984  46.394 3.352   1.00 45.10  ? 67  LEU A CD2 1 
ATOM   492   N N   . ALA A  1 68  ? 13.543  48.519 8.260   1.00 33.97  ? 68  ALA A N   1 
ATOM   493   C CA  . ALA A  1 68  ? 13.247  49.536 9.294   1.00 33.34  ? 68  ALA A CA  1 
ATOM   494   C C   . ALA A  1 68  ? 14.449  50.474 9.422   1.00 31.71  ? 68  ALA A C   1 
ATOM   495   O O   . ALA A  1 68  ? 14.248  51.699 9.399   1.00 31.29  ? 68  ALA A O   1 
ATOM   496   C CB  . ALA A  1 68  ? 12.919  48.869 10.608  1.00 34.02  ? 68  ALA A CB  1 
ATOM   497   N N   . TYR A  1 69  ? 15.656  49.911 9.523   1.00 33.60  ? 69  TYR A N   1 
ATOM   498   C CA  . TYR A  1 69  ? 16.911  50.665 9.775   1.00 38.66  ? 69  TYR A CA  1 
ATOM   499   C C   . TYR A  1 69  ? 17.262  51.525 8.557   1.00 40.41  ? 69  TYR A C   1 
ATOM   500   O O   . TYR A  1 69  ? 17.835  52.612 8.748   1.00 44.14  ? 69  TYR A O   1 
ATOM   501   C CB  . TYR A  1 69  ? 18.037  49.718 10.195  1.00 40.98  ? 69  TYR A CB  1 
ATOM   502   C CG  . TYR A  1 69  ? 18.208  49.660 11.690  1.00 42.26  ? 69  TYR A CG  1 
ATOM   503   C CD1 . TYR A  1 69  ? 19.186  50.404 12.326  1.00 40.27  ? 69  TYR A CD1 1 
ATOM   504   C CD2 . TYR A  1 69  ? 17.347  48.911 12.475  1.00 45.71  ? 69  TYR A CD2 1 
ATOM   505   C CE1 . TYR A  1 69  ? 19.331  50.375 13.702  1.00 43.15  ? 69  TYR A CE1 1 
ATOM   506   C CE2 . TYR A  1 69  ? 17.475  48.872 13.853  1.00 48.90  ? 69  TYR A CE2 1 
ATOM   507   C CZ  . TYR A  1 69  ? 18.471  49.607 14.467  1.00 46.98  ? 69  TYR A CZ  1 
ATOM   508   O OH  . TYR A  1 69  ? 18.605  49.567 15.823  1.00 49.16  ? 69  TYR A OH  1 
ATOM   509   N N   . ILE A  1 70  ? 16.908  51.073 7.352   1.00 41.39  ? 70  ILE A N   1 
ATOM   510   C CA  . ILE A  1 70  ? 17.049  51.882 6.105   1.00 40.93  ? 70  ILE A CA  1 
ATOM   511   C C   . ILE A  1 70  ? 16.211  53.155 6.263   1.00 39.73  ? 70  ILE A C   1 
ATOM   512   O O   . ILE A  1 70  ? 16.729  54.241 5.948   1.00 40.76  ? 70  ILE A O   1 
ATOM   513   C CB  . ILE A  1 70  ? 16.645  51.074 4.857   1.00 41.85  ? 70  ILE A CB  1 
ATOM   514   C CG1 . ILE A  1 70  ? 17.614  49.916 4.600   1.00 43.44  ? 70  ILE A CG1 1 
ATOM   515   C CG2 . ILE A  1 70  ? 16.520  51.989 3.649   1.00 39.53  ? 70  ILE A CG2 1 
ATOM   516   C CD1 . ILE A  1 70  ? 17.242  49.049 3.419   1.00 45.00  ? 70  ILE A CD1 1 
ATOM   517   N N   . LEU A  1 71  ? 14.972  53.026 6.749   1.00 40.87  ? 71  LEU A N   1 
ATOM   518   C CA  . LEU A  1 71  ? 14.063  54.175 7.010   1.00 46.55  ? 71  LEU A CA  1 
ATOM   519   C C   . LEU A  1 71  ? 14.697  55.092 8.061   1.00 45.76  ? 71  LEU A C   1 
ATOM   520   O O   . LEU A  1 71  ? 14.759  56.310 7.819   1.00 49.25  ? 71  LEU A O   1 
ATOM   521   C CB  . LEU A  1 71  ? 12.697  53.668 7.483   1.00 47.60  ? 71  LEU A CB  1 
ATOM   522   C CG  . LEU A  1 71  ? 11.844  52.968 6.428   1.00 52.07  ? 71  LEU A CG  1 
ATOM   523   C CD1 . LEU A  1 71  ? 10.384  52.934 6.859   1.00 52.54  ? 71  LEU A CD1 1 
ATOM   524   C CD2 . LEU A  1 71  ? 11.976  53.647 5.073   1.00 52.52  ? 71  LEU A CD2 1 
ATOM   525   N N   . ILE A  1 72  ? 15.151  54.524 9.181   1.00 42.32  ? 72  ILE A N   1 
ATOM   526   C CA  . ILE A  1 72  ? 15.789  55.284 10.296  1.00 45.44  ? 72  ILE A CA  1 
ATOM   527   C C   . ILE A  1 72  ? 16.954  56.094 9.721   1.00 42.23  ? 72  ILE A C   1 
ATOM   528   O O   . ILE A  1 72  ? 17.051  57.293 10.036  1.00 44.52  ? 72  ILE A O   1 
ATOM   529   C CB  . ILE A  1 72  ? 16.241  54.347 11.433  1.00 47.10  ? 72  ILE A CB  1 
ATOM   530   C CG1 . ILE A  1 72  ? 15.057  53.605 12.060  1.00 52.74  ? 72  ILE A CG1 1 
ATOM   531   C CG2 . ILE A  1 72  ? 17.027  55.124 12.476  1.00 42.98  ? 72  ILE A CG2 1 
ATOM   532   C CD1 . ILE A  1 72  ? 15.442  52.585 13.109  1.00 53.88  ? 72  ILE A CD1 1 
ATOM   533   N N   . ILE A  1 73  ? 17.793  55.459 8.900   1.00 41.45  ? 73  ILE A N   1 
ATOM   534   C CA  . ILE A  1 73  ? 18.970  56.100 8.240   1.00 41.22  ? 73  ILE A CA  1 
ATOM   535   C C   . ILE A  1 73  ? 18.476  57.269 7.380   1.00 39.84  ? 73  ILE A C   1 
ATOM   536   O O   . ILE A  1 73  ? 19.049  58.369 7.501   1.00 38.61  ? 73  ILE A O   1 
ATOM   537   C CB  . ILE A  1 73  ? 19.775  55.070 7.421   1.00 42.42  ? 73  ILE A CB  1 
ATOM   538   C CG1 . ILE A  1 73  ? 20.421  54.019 8.328   1.00 43.59  ? 73  ILE A CG1 1 
ATOM   539   C CG2 . ILE A  1 73  ? 20.803  55.767 6.544   1.00 43.51  ? 73  ILE A CG2 1 
ATOM   540   C CD1 . ILE A  1 73  ? 20.960  52.811 7.599   1.00 42.17  ? 73  ILE A CD1 1 
ATOM   541   N N   . VAL A  1 74  ? 17.449  57.040 6.555   1.00 38.58  ? 74  VAL A N   1 
ATOM   542   C CA  . VAL A  1 74  ? 16.849  58.074 5.659   1.00 38.82  ? 74  VAL A CA  1 
ATOM   543   C C   . VAL A  1 74  ? 16.358  59.242 6.521   1.00 42.87  ? 74  VAL A C   1 
ATOM   544   O O   . VAL A  1 74  ? 16.698  60.406 6.202   1.00 45.35  ? 74  VAL A O   1 
ATOM   545   C CB  . VAL A  1 74  ? 15.704  57.499 4.803   1.00 36.56  ? 74  VAL A CB  1 
ATOM   546   C CG1 . VAL A  1 74  ? 14.921  58.600 4.104   1.00 36.72  ? 74  VAL A CG1 1 
ATOM   547   C CG2 . VAL A  1 74  ? 16.206  56.475 3.798   1.00 37.61  ? 74  VAL A CG2 1 
ATOM   548   N N   . ALA A  1 75  ? 15.587  58.935 7.570   1.00 43.91  ? 75  ALA A N   1 
ATOM   549   C CA  . ALA A  1 75  ? 15.008  59.915 8.517   1.00 46.09  ? 75  ALA A CA  1 
ATOM   550   C C   . ALA A  1 75  ? 16.135  60.763 9.118   1.00 48.49  ? 75  ALA A C   1 
ATOM   551   O O   . ALA A  1 75  ? 15.966  61.998 9.217   1.00 48.85  ? 75  ALA A O   1 
ATOM   552   C CB  . ALA A  1 75  ? 14.224  59.195 9.585   1.00 43.34  ? 75  ALA A CB  1 
ATOM   553   N N   . PHE A  1 76  ? 17.238  60.112 9.501   1.00 46.80  ? 76  PHE A N   1 
ATOM   554   C CA  . PHE A  1 76  ? 18.430  60.746 10.119  1.00 47.60  ? 76  PHE A CA  1 
ATOM   555   C C   . PHE A  1 76  ? 19.039  61.748 9.134   1.00 49.21  ? 76  PHE A C   1 
ATOM   556   O O   . PHE A  1 76  ? 19.354  62.883 9.551   1.00 57.38  ? 76  PHE A O   1 
ATOM   557   C CB  . PHE A  1 76  ? 19.456  59.689 10.534  1.00 49.72  ? 76  PHE A CB  1 
ATOM   558   C CG  . PHE A  1 76  ? 20.760  60.254 11.039  1.00 52.78  ? 76  PHE A CG  1 
ATOM   559   C CD1 . PHE A  1 76  ? 21.880  60.297 10.222  1.00 55.66  ? 76  PHE A CD1 1 
ATOM   560   C CD2 . PHE A  1 76  ? 20.864  60.756 12.326  1.00 52.55  ? 76  PHE A CD2 1 
ATOM   561   C CE1 . PHE A  1 76  ? 23.077  60.822 10.685  1.00 56.10  ? 76  PHE A CE1 1 
ATOM   562   C CE2 . PHE A  1 76  ? 22.060  61.285 12.785  1.00 55.49  ? 76  PHE A CE2 1 
ATOM   563   C CZ  . PHE A  1 76  ? 23.165  61.316 11.966  1.00 57.23  ? 76  PHE A CZ  1 
ATOM   564   N N   . LEU A  1 77  ? 19.192  61.341 7.871   1.00 48.07  ? 77  LEU A N   1 
ATOM   565   C CA  . LEU A  1 77  ? 19.852  62.151 6.813   1.00 55.43  ? 77  LEU A CA  1 
ATOM   566   C C   . LEU A  1 77  ? 18.994  63.380 6.490   1.00 53.02  ? 77  LEU A C   1 
ATOM   567   O O   . LEU A  1 77  ? 19.576  64.409 6.096   1.00 52.31  ? 77  LEU A O   1 
ATOM   568   C CB  . LEU A  1 77  ? 20.073  61.282 5.571   1.00 59.58  ? 77  LEU A CB  1 
ATOM   569   C CG  . LEU A  1 77  ? 21.126  60.184 5.722   1.00 62.78  ? 77  LEU A CG  1 
ATOM   570   C CD1 . LEU A  1 77  ? 21.326  59.442 4.410   1.00 62.62  ? 77  LEU A CD1 1 
ATOM   571   C CD2 . LEU A  1 77  ? 22.448  60.756 6.214   1.00 66.27  ? 77  LEU A CD2 1 
ATOM   572   N N   . LEU A  1 78  ? 17.672  63.278 6.661   1.00 52.09  ? 78  LEU A N   1 
ATOM   573   C CA  . LEU A  1 78  ? 16.705  64.359 6.325   1.00 52.37  ? 78  LEU A CA  1 
ATOM   574   C C   . LEU A  1 78  ? 16.232  65.067 7.600   1.00 52.48  ? 78  LEU A C   1 
ATOM   575   O O   . LEU A  1 78  ? 15.396  65.984 7.485   1.00 55.43  ? 78  LEU A O   1 
ATOM   576   C CB  . LEU A  1 78  ? 15.520  63.750 5.570   1.00 52.20  ? 78  LEU A CB  1 
ATOM   577   C CG  . LEU A  1 78  ? 15.864  63.064 4.247   1.00 55.44  ? 78  LEU A CG  1 
ATOM   578   C CD1 . LEU A  1 78  ? 14.602  62.644 3.512   1.00 53.21  ? 78  LEU A CD1 1 
ATOM   579   C CD2 . LEU A  1 78  ? 16.710  63.968 3.363   1.00 58.63  ? 78  LEU A CD2 1 
ATOM   580   N N   . GLY A  1 79  ? 16.755  64.668 8.763   1.00 55.76  ? 79  GLY A N   1 
ATOM   581   C CA  . GLY A  1 79  ? 16.271  65.126 10.081  1.00 59.41  ? 79  GLY A CA  1 
ATOM   582   C C   . GLY A  1 79  ? 17.077  66.293 10.624  1.00 63.13  ? 79  GLY A C   1 
ATOM   583   O O   . GLY A  1 79  ? 16.551  67.023 11.487  1.00 71.99  ? 79  GLY A O   1 
ATOM   584   N N   . TYR A  1 80  ? 18.311  66.465 10.143  1.00 55.93  ? 80  TYR A N   1 
ATOM   585   C CA  . TYR A  1 80  ? 19.267  67.491 10.632  1.00 52.29  ? 80  TYR A CA  1 
ATOM   586   C C   . TYR A  1 80  ? 19.842  68.266 9.444   1.00 56.46  ? 80  TYR A C   1 
ATOM   587   O O   . TYR A  1 80  ? 20.049  67.667 8.371   1.00 50.46  ? 80  TYR A O   1 
ATOM   588   C CB  . TYR A  1 80  ? 20.371  66.835 11.463  1.00 51.57  ? 80  TYR A CB  1 
ATOM   589   C CG  . TYR A  1 80  ? 19.910  66.293 12.792  1.00 50.48  ? 80  TYR A CG  1 
ATOM   590   C CD1 . TYR A  1 80  ? 19.909  67.089 13.924  1.00 55.16  ? 80  TYR A CD1 1 
ATOM   591   C CD2 . TYR A  1 80  ? 19.467  64.986 12.919  1.00 54.64  ? 80  TYR A CD2 1 
ATOM   592   C CE1 . TYR A  1 80  ? 19.485  66.603 15.149  1.00 59.83  ? 80  TYR A CE1 1 
ATOM   593   C CE2 . TYR A  1 80  ? 19.038  64.484 14.137  1.00 56.91  ? 80  TYR A CE2 1 
ATOM   594   C CZ  . TYR A  1 80  ? 19.048  65.295 15.258  1.00 62.02  ? 80  TYR A CZ  1 
ATOM   595   O OH  . TYR A  1 80  ? 18.630  64.813 16.465  1.00 66.15  ? 80  TYR A OH  1 
ATOM   596   N N   . ASP A  1 81  ? 20.085  69.564 9.645   1.00 62.52  ? 81  ASP A N   1 
ATOM   597   C CA  . ASP A  1 81  ? 20.735  70.469 8.661   1.00 64.29  ? 81  ASP A CA  1 
ATOM   598   C C   . ASP A  1 81  ? 22.047  70.976 9.265   1.00 68.10  ? 81  ASP A C   1 
ATOM   599   O O   . ASP A  1 81  ? 22.030  71.410 10.434  1.00 53.33  ? 81  ASP A O   1 
ATOM   600   C CB  . ASP A  1 81  ? 19.812  71.626 8.270   1.00 62.68  ? 81  ASP A CB  1 
ATOM   601   C CG  . ASP A  1 81  ? 18.365  71.207 8.077   1.00 64.66  ? 81  ASP A CG  1 
ATOM   602   O OD1 . ASP A  1 81  ? 17.661  71.051 9.095   1.00 70.59  ? 81  ASP A OD1 1 
ATOM   603   O OD2 . ASP A  1 81  ? 17.961  71.023 6.912   1.00 60.74  ? 81  ASP A OD2 1 
ATOM   604   N N   . SER A  1 82  ? 23.141  70.905 8.501   1.00 79.73  ? 82  SER A N   1 
ATOM   605   C CA  . SER A  1 82  ? 24.493  71.347 8.930   1.00 76.59  ? 82  SER A CA  1 
ATOM   606   C C   . SER A  1 82  ? 24.540  72.877 8.964   1.00 80.43  ? 82  SER A C   1 
ATOM   607   O O   . SER A  1 82  ? 24.080  73.508 7.995   1.00 73.20  ? 82  SER A O   1 
ATOM   608   C CB  . SER A  1 82  ? 25.563  70.785 8.038   1.00 71.03  ? 82  SER A CB  1 
ATOM   609   O OG  . SER A  1 82  ? 26.846  70.980 8.613   1.00 78.45  ? 82  SER A OG  1 
ATOM   610   N N   . THR A  1 83  ? 25.071  73.439 10.053  1.00 88.34  ? 83  THR A N   1 
ATOM   611   C CA  . THR A  1 83  ? 25.194  74.900 10.297  1.00 89.20  ? 83  THR A CA  1 
ATOM   612   C C   . THR A  1 83  ? 26.572  75.183 10.906  1.00 95.99  ? 83  THR A C   1 
ATOM   613   O O   . THR A  1 83  ? 27.370  74.232 11.023  1.00 94.84  ? 83  THR A O   1 
ATOM   614   C CB  . THR A  1 83  ? 24.067  75.400 11.210  1.00 88.77  ? 83  THR A CB  1 
ATOM   615   O OG1 . THR A  1 83  ? 24.255  74.825 12.504  1.00 85.40  ? 83  THR A OG1 1 
ATOM   616   C CG2 . THR A  1 83  ? 22.687  75.049 10.698  1.00 83.08  ? 83  THR A CG2 1 
ATOM   617   N N   . ALA A  1 84  ? 26.831  76.439 11.279  1.00 97.58  ? 84  ALA A N   1 
ATOM   618   C CA  . ALA A  1 84  ? 28.058  76.876 11.984  1.00 100.86 ? 84  ALA A CA  1 
ATOM   619   C C   . ALA A  1 84  ? 28.071  76.271 13.393  1.00 99.62  ? 84  ALA A C   1 
ATOM   620   O O   . ALA A  1 84  ? 29.164  76.165 13.982  1.00 100.74 ? 84  ALA A O   1 
ATOM   621   C CB  . ALA A  1 84  ? 28.119  78.383 12.029  1.00 105.96 ? 84  ALA A CB  1 
ATOM   622   N N   . GLY A  1 85  ? 26.894  75.883 13.897  1.00 100.62 ? 85  GLY A N   1 
ATOM   623   C CA  . GLY A  1 85  ? 26.693  75.419 15.284  1.00 99.56  ? 85  GLY A CA  1 
ATOM   624   C C   . GLY A  1 85  ? 26.610  73.905 15.381  1.00 100.69 ? 85  GLY A C   1 
ATOM   625   O O   . GLY A  1 85  ? 26.324  73.405 16.488  1.00 96.25  ? 85  GLY A O   1 
ATOM   626   N N   . GLY A  1 86  ? 26.849  73.201 14.269  1.00 104.01 ? 86  GLY A N   1 
ATOM   627   C CA  . GLY A  1 86  ? 26.841  71.725 14.201  1.00 100.56 ? 86  GLY A CA  1 
ATOM   628   C C   . GLY A  1 86  ? 25.755  71.206 13.273  1.00 90.85  ? 86  GLY A C   1 
ATOM   629   O O   . GLY A  1 86  ? 25.765  71.591 12.090  1.00 95.09  ? 86  GLY A O   1 
ATOM   630   N N   . TRP A  1 87  ? 24.860  70.355 13.789  1.00 76.14  ? 87  TRP A N   1 
ATOM   631   C CA  . TRP A  1 87  ? 23.703  69.779 13.051  1.00 68.63  ? 87  TRP A CA  1 
ATOM   632   C C   . TRP A  1 87  ? 22.406  70.135 13.785  1.00 70.99  ? 87  TRP A C   1 
ATOM   633   O O   . TRP A  1 87  ? 22.166  69.580 14.875  1.00 74.04  ? 87  TRP A O   1 
ATOM   634   C CB  . TRP A  1 87  ? 23.867  68.262 12.882  1.00 58.80  ? 87  TRP A CB  1 
ATOM   635   C CG  . TRP A  1 87  ? 24.954  67.879 11.927  1.00 53.21  ? 87  TRP A CG  1 
ATOM   636   C CD1 . TRP A  1 87  ? 26.276  67.696 12.214  1.00 50.89  ? 87  TRP A CD1 1 
ATOM   637   C CD2 . TRP A  1 87  ? 24.818  67.648 10.513  1.00 53.86  ? 87  TRP A CD2 1 
ATOM   638   N NE1 . TRP A  1 87  ? 26.968  67.361 11.081  1.00 50.68  ? 87  TRP A NE1 1 
ATOM   639   C CE2 . TRP A  1 87  ? 26.100  67.322 10.022  1.00 48.78  ? 87  TRP A CE2 1 
ATOM   640   C CE3 . TRP A  1 87  ? 23.741  67.675 9.619   1.00 56.37  ? 87  TRP A CE3 1 
ATOM   641   C CZ2 . TRP A  1 87  ? 26.331  67.030 8.679   1.00 46.36  ? 87  TRP A CZ2 1 
ATOM   642   C CZ3 . TRP A  1 87  ? 23.970  67.387 8.291   1.00 53.18  ? 87  TRP A CZ3 1 
ATOM   643   C CH2 . TRP A  1 87  ? 25.248  67.070 7.831   1.00 51.44  ? 87  TRP A CH2 1 
ATOM   644   N N   . VAL A  1 88  ? 21.604  71.030 13.203  1.00 71.38  ? 88  VAL A N   1 
ATOM   645   C CA  . VAL A  1 88  ? 20.379  71.597 13.843  1.00 67.40  ? 88  VAL A CA  1 
ATOM   646   C C   . VAL A  1 88  ? 19.175  70.747 13.456  1.00 60.80  ? 88  VAL A C   1 
ATOM   647   O O   . VAL A  1 88  ? 18.921  70.512 12.277  1.00 58.60  ? 88  VAL A O   1 
ATOM   648   C CB  . VAL A  1 88  ? 20.169  73.072 13.454  1.00 70.62  ? 88  VAL A CB  1 
ATOM   649   C CG1 . VAL A  1 88  ? 18.827  73.595 13.939  1.00 65.55  ? 88  VAL A CG1 1 
ATOM   650   C CG2 . VAL A  1 88  ? 21.304  73.948 13.960  1.00 83.45  ? 88  VAL A CG2 1 
ATOM   651   N N   . PRO A  1 89  ? 18.392  70.273 14.450  1.00 54.19  ? 89  PRO A N   1 
ATOM   652   C CA  . PRO A  1 89  ? 17.176  69.510 14.176  1.00 52.51  ? 89  PRO A CA  1 
ATOM   653   C C   . PRO A  1 89  ? 16.184  70.313 13.324  1.00 51.25  ? 89  PRO A C   1 
ATOM   654   O O   . PRO A  1 89  ? 16.019  71.489 13.581  1.00 53.70  ? 89  PRO A O   1 
ATOM   655   C CB  . PRO A  1 89  ? 16.576  69.243 15.565  1.00 54.84  ? 89  PRO A CB  1 
ATOM   656   C CG  . PRO A  1 89  ? 17.736  69.419 16.530  1.00 58.70  ? 89  PRO A CG  1 
ATOM   657   C CD  . PRO A  1 89  ? 18.641  70.450 15.888  1.00 56.19  ? 89  PRO A CD  1 
ATOM   658   N N   . ASN A  1 90  ? 15.563  69.665 12.334  1.00 52.99  ? 90  ASN A N   1 
ATOM   659   C CA  . ASN A  1 90  ? 14.403  70.213 11.581  1.00 58.12  ? 90  ASN A CA  1 
ATOM   660   C C   . ASN A  1 90  ? 13.146  69.480 12.063  1.00 62.24  ? 90  ASN A C   1 
ATOM   661   O O   . ASN A  1 90  ? 13.252  68.715 13.043  1.00 68.03  ? 90  ASN A O   1 
ATOM   662   C CB  . ASN A  1 90  ? 14.611  70.136 10.064  1.00 60.77  ? 90  ASN A CB  1 
ATOM   663   C CG  . ASN A  1 90  ? 14.713  68.719 9.539   1.00 59.77  ? 90  ASN A CG  1 
ATOM   664   O OD1 . ASN A  1 90  ? 13.846  67.891 9.810   1.00 62.28  ? 90  ASN A OD1 1 
ATOM   665   N ND2 . ASN A  1 90  ? 15.761  68.433 8.780   1.00 57.94  ? 90  ASN A ND2 1 
ATOM   666   N N   . ASP A  1 91  ? 12.005  69.712 11.410  1.00 68.20  ? 91  ASP A N   1 
ATOM   667   C CA  . ASP A  1 91  ? 10.685  69.164 11.822  1.00 77.37  ? 91  ASP A CA  1 
ATOM   668   C C   . ASP A  1 91  ? 10.715  67.633 11.763  1.00 72.43  ? 91  ASP A C   1 
ATOM   669   O O   . ASP A  1 91  ? 10.012  67.007 12.577  1.00 69.73  ? 91  ASP A O   1 
ATOM   670   C CB  . ASP A  1 91  ? 9.560   69.747 10.964  1.00 88.37  ? 91  ASP A CB  1 
ATOM   671   C CG  . ASP A  1 91  ? 9.277   71.207 11.271  1.00 95.87  ? 91  ASP A CG  1 
ATOM   672   O OD1 . ASP A  1 91  ? 10.040  71.795 12.068  1.00 95.00  ? 91  ASP A OD1 1 
ATOM   673   O OD2 . ASP A  1 91  ? 8.296   71.744 10.717  1.00 95.81  ? 91  ASP A OD2 1 
ATOM   674   N N   . GLY A  1 92  ? 11.507  67.060 10.850  1.00 71.58  ? 92  GLY A N   1 
ATOM   675   C CA  . GLY A  1 92  ? 11.518  65.614 10.552  1.00 74.84  ? 92  GLY A CA  1 
ATOM   676   C C   . GLY A  1 92  ? 12.431  64.822 11.476  1.00 72.18  ? 92  GLY A C   1 
ATOM   677   O O   . GLY A  1 92  ? 12.475  63.582 11.330  1.00 70.37  ? 92  GLY A O   1 
ATOM   678   N N   . ALA A  1 93  ? 13.132  65.499 12.394  1.00 70.76  ? 93  ALA A N   1 
ATOM   679   C CA  . ALA A  1 93  ? 14.100  64.893 13.340  1.00 65.93  ? 93  ALA A CA  1 
ATOM   680   C C   . ALA A  1 93  ? 13.378  63.890 14.249  1.00 66.63  ? 93  ALA A C   1 
ATOM   681   O O   . ALA A  1 93  ? 14.002  62.879 14.635  1.00 61.56  ? 93  ALA A O   1 
ATOM   682   C CB  . ALA A  1 93  ? 14.786  65.972 14.142  1.00 63.28  ? 93  ALA A CB  1 
ATOM   683   N N   . ILE A  1 94  ? 12.113  64.169 14.574  1.00 66.11  ? 94  ILE A N   1 
ATOM   684   C CA  . ILE A  1 94  ? 11.239  63.316 15.434  1.00 64.11  ? 94  ILE A CA  1 
ATOM   685   C C   . ILE A  1 94  ? 11.100  61.931 14.788  1.00 64.49  ? 94  ILE A C   1 
ATOM   686   O O   . ILE A  1 94  ? 10.992  60.934 15.535  1.00 66.71  ? 94  ILE A O   1 
ATOM   687   C CB  . ILE A  1 94  ? 9.869   63.993 15.649  1.00 61.01  ? 94  ILE A CB  1 
ATOM   688   C CG1 . ILE A  1 94  ? 8.985   63.198 16.614  1.00 67.07  ? 94  ILE A CG1 1 
ATOM   689   C CG2 . ILE A  1 94  ? 9.168   64.231 14.320  1.00 56.81  ? 94  ILE A CG2 1 
ATOM   690   C CD1 . ILE A  1 94  ? 7.649   63.853 16.899  1.00 65.78  ? 94  ILE A CD1 1 
ATOM   691   N N   . ASN A  1 95  ? 11.113  61.877 13.451  1.00 58.14  ? 95  ASN A N   1 
ATOM   692   C CA  . ASN A  1 95  ? 10.867  60.644 12.656  1.00 56.25  ? 95  ASN A CA  1 
ATOM   693   C C   . ASN A  1 95  ? 11.944  59.599 12.967  1.00 52.23  ? 95  ASN A C   1 
ATOM   694   O O   . ASN A  1 95  ? 11.640  58.396 12.860  1.00 52.67  ? 95  ASN A O   1 
ATOM   695   C CB  . ASN A  1 95  ? 10.794  60.941 11.157  1.00 58.08  ? 95  ASN A CB  1 
ATOM   696   C CG  . ASN A  1 95  ? 9.411   61.383 10.736  1.00 60.83  ? 95  ASN A CG  1 
ATOM   697   O OD1 . ASN A  1 95  ? 8.688   61.980 11.529  1.00 57.37  ? 95  ASN A OD1 1 
ATOM   698   N ND2 . ASN A  1 95  ? 9.026   61.073 9.508   1.00 68.94  ? 95  ASN A ND2 1 
ATOM   699   N N   . ILE A  1 96  ? 13.149  60.042 13.330  1.00 49.72  ? 96  ILE A N   1 
ATOM   700   C CA  . ILE A  1 96  ? 14.286  59.147 13.698  1.00 54.58  ? 96  ILE A CA  1 
ATOM   701   C C   . ILE A  1 96  ? 13.837  58.237 14.846  1.00 55.72  ? 96  ILE A C   1 
ATOM   702   O O   . ILE A  1 96  ? 14.181  57.035 14.820  1.00 64.60  ? 96  ILE A O   1 
ATOM   703   C CB  . ILE A  1 96  ? 15.537  59.970 14.063  1.00 57.53  ? 96  ILE A CB  1 
ATOM   704   C CG1 . ILE A  1 96  ? 16.045  60.776 12.864  1.00 67.40  ? 96  ILE A CG1 1 
ATOM   705   C CG2 . ILE A  1 96  ? 16.622  59.074 14.638  1.00 53.10  ? 96  ILE A CG2 1 
ATOM   706   C CD1 . ILE A  1 96  ? 17.173  61.723 13.194  1.00 73.23  ? 96  ILE A CD1 1 
ATOM   707   N N   . PHE A  1 97  ? 13.084  58.792 15.801  1.00 52.16  ? 97  PHE A N   1 
ATOM   708   C CA  . PHE A  1 97  ? 12.555  58.085 16.997  1.00 51.99  ? 97  PHE A CA  1 
ATOM   709   C C   . PHE A  1 97  ? 11.248  57.380 16.627  1.00 48.56  ? 97  PHE A C   1 
ATOM   710   O O   . PHE A  1 97  ? 11.072  56.197 16.987  1.00 53.37  ? 97  PHE A O   1 
ATOM   711   C CB  . PHE A  1 97  ? 12.378  59.072 18.151  1.00 52.72  ? 97  PHE A CB  1 
ATOM   712   C CG  . PHE A  1 97  ? 13.673  59.691 18.607  1.00 55.08  ? 97  PHE A CG  1 
ATOM   713   C CD1 . PHE A  1 97  ? 14.373  59.157 19.678  1.00 54.66  ? 97  PHE A CD1 1 
ATOM   714   C CD2 . PHE A  1 97  ? 14.213  60.777 17.937  1.00 54.45  ? 97  PHE A CD2 1 
ATOM   715   C CE1 . PHE A  1 97  ? 15.575  59.714 20.083  1.00 56.31  ? 97  PHE A CE1 1 
ATOM   716   C CE2 . PHE A  1 97  ? 15.413  61.336 18.346  1.00 53.55  ? 97  PHE A CE2 1 
ATOM   717   C CZ  . PHE A  1 97  ? 16.094  60.799 19.414  1.00 58.31  ? 97  PHE A CZ  1 
ATOM   718   N N   . SER A  1 98  ? 10.371  58.096 15.921  1.00 47.77  ? 98  SER A N   1 
ATOM   719   C CA  . SER A  1 98  ? 9.097   57.578 15.361  1.00 50.80  ? 98  SER A CA  1 
ATOM   720   C C   . SER A  1 98  ? 9.339   56.229 14.671  1.00 53.29  ? 98  SER A C   1 
ATOM   721   O O   . SER A  1 98  ? 8.638   55.253 15.013  1.00 50.64  ? 98  SER A O   1 
ATOM   722   C CB  . SER A  1 98  ? 8.498   58.577 14.409  1.00 50.87  ? 98  SER A CB  1 
ATOM   723   O OG  . SER A  1 98  ? 7.254   58.115 13.908  1.00 59.60  ? 98  SER A OG  1 
ATOM   724   N N   . THR A  1 99  ? 10.299  56.186 13.741  1.00 60.41  ? 99  THR A N   1 
ATOM   725   C CA  . THR A  1 99  ? 10.603  55.020 12.867  1.00 55.07  ? 99  THR A CA  1 
ATOM   726   C C   . THR A  1 99  ? 11.004  53.808 13.716  1.00 51.91  ? 99  THR A C   1 
ATOM   727   O O   . THR A  1 99  ? 10.653  52.679 13.323  1.00 56.90  ? 99  THR A O   1 
ATOM   728   C CB  . THR A  1 99  ? 11.715  55.350 11.863  1.00 55.53  ? 99  THR A CB  1 
ATOM   729   O OG1 . THR A  1 99  ? 11.405  56.605 11.259  1.00 60.74  ? 99  THR A OG1 1 
ATOM   730   C CG2 . THR A  1 99  ? 11.874  54.294 10.790  1.00 60.73  ? 99  THR A CG2 1 
ATOM   731   N N   . ARG A  1 100 ? 11.724  54.027 14.819  1.00 46.06  ? 100 ARG A N   1 
ATOM   732   C CA  . ARG A  1 100 ? 12.261  52.927 15.661  1.00 48.26  ? 100 ARG A CA  1 
ATOM   733   C C   . ARG A  1 100 ? 11.093  52.191 16.327  1.00 48.64  ? 100 ARG A C   1 
ATOM   734   O O   . ARG A  1 100 ? 11.158  50.949 16.424  1.00 52.78  ? 100 ARG A O   1 
ATOM   735   C CB  . ARG A  1 100 ? 13.255  53.454 16.698  1.00 49.62  ? 100 ARG A CB  1 
ATOM   736   C CG  . ARG A  1 100 ? 14.241  52.396 17.170  1.00 55.58  ? 100 ARG A CG  1 
ATOM   737   C CD  . ARG A  1 100 ? 15.219  52.924 18.197  1.00 66.93  ? 100 ARG A CD  1 
ATOM   738   N NE  . ARG A  1 100 ? 16.329  53.660 17.604  1.00 70.07  ? 100 ARG A NE  1 
ATOM   739   C CZ  . ARG A  1 100 ? 17.431  53.097 17.120  1.00 64.22  ? 100 ARG A CZ  1 
ATOM   740   N NH1 . ARG A  1 100 ? 17.571  51.783 17.149  1.00 67.38  ? 100 ARG A NH1 1 
ATOM   741   N NH2 . ARG A  1 100 ? 18.390  53.846 16.606  1.00 62.94  ? 100 ARG A NH2 1 
ATOM   742   N N   . TYR A  1 101 ? 10.064  52.925 16.761  1.00 47.85  ? 101 TYR A N   1 
ATOM   743   C CA  . TYR A  1 101 ? 8.818   52.359 17.342  1.00 52.44  ? 101 TYR A CA  1 
ATOM   744   C C   . TYR A  1 101 ? 8.169   51.439 16.304  1.00 52.71  ? 101 TYR A C   1 
ATOM   745   O O   . TYR A  1 101 ? 7.856   50.277 16.634  1.00 57.82  ? 101 TYR A O   1 
ATOM   746   C CB  . TYR A  1 101 ? 7.876   53.472 17.812  1.00 54.78  ? 101 TYR A CB  1 
ATOM   747   C CG  . TYR A  1 101 ? 8.265   54.082 19.134  1.00 56.83  ? 101 TYR A CG  1 
ATOM   748   C CD1 . TYR A  1 101 ? 7.897   53.488 20.330  1.00 56.16  ? 101 TYR A CD1 1 
ATOM   749   C CD2 . TYR A  1 101 ? 9.027   55.237 19.194  1.00 66.29  ? 101 TYR A CD2 1 
ATOM   750   C CE1 . TYR A  1 101 ? 8.263   54.031 21.550  1.00 59.50  ? 101 TYR A CE1 1 
ATOM   751   C CE2 . TYR A  1 101 ? 9.402   55.794 20.406  1.00 69.98  ? 101 TYR A CE2 1 
ATOM   752   C CZ  . TYR A  1 101 ? 9.019   55.189 21.590  1.00 66.35  ? 101 TYR A CZ  1 
ATOM   753   O OH  . TYR A  1 101 ? 9.383   55.732 22.788  1.00 74.75  ? 101 TYR A OH  1 
ATOM   754   N N   . ILE A  1 102 ? 7.994   51.946 15.081  1.00 52.77  ? 102 ILE A N   1 
ATOM   755   C CA  . ILE A  1 102 ? 7.452   51.181 13.919  1.00 51.21  ? 102 ILE A CA  1 
ATOM   756   C C   . ILE A  1 102 ? 8.182   49.836 13.839  1.00 48.74  ? 102 ILE A C   1 
ATOM   757   O O   . ILE A  1 102 ? 7.501   48.799 13.741  1.00 48.76  ? 102 ILE A O   1 
ATOM   758   C CB  . ILE A  1 102 ? 7.593   51.987 12.613  1.00 52.25  ? 102 ILE A CB  1 
ATOM   759   C CG1 . ILE A  1 102 ? 6.824   53.309 12.676  1.00 52.17  ? 102 ILE A CG1 1 
ATOM   760   C CG2 . ILE A  1 102 ? 7.172   51.146 11.418  1.00 53.88  ? 102 ILE A CG2 1 
ATOM   761   C CD1 . ILE A  1 102 ? 6.876   54.113 11.398  1.00 55.45  ? 102 ILE A CD1 1 
ATOM   762   N N   . GLU A  1 103 ? 9.518   49.862 13.879  1.00 45.56  ? 103 GLU A N   1 
ATOM   763   C CA  . GLU A  1 103 ? 10.376  48.648 13.838  1.00 47.01  ? 103 GLU A CA  1 
ATOM   764   C C   . GLU A  1 103 ? 9.924   47.675 14.931  1.00 45.91  ? 103 GLU A C   1 
ATOM   765   O O   . GLU A  1 103 ? 9.485   46.559 14.588  1.00 50.90  ? 103 GLU A O   1 
ATOM   766   C CB  . GLU A  1 103 ? 11.847  49.009 14.046  1.00 47.74  ? 103 GLU A CB  1 
ATOM   767   C CG  . GLU A  1 103 ? 12.735  47.793 14.233  1.00 47.02  ? 103 GLU A CG  1 
ATOM   768   C CD  . GLU A  1 103 ? 13.967  48.040 15.083  1.00 53.12  ? 103 GLU A CD  1 
ATOM   769   O OE1 . GLU A  1 103 ? 14.505  47.059 15.629  1.00 57.69  ? 103 GLU A OE1 1 
ATOM   770   O OE2 . GLU A  1 103 ? 14.385  49.212 15.200  1.00 60.55  ? 103 GLU A OE2 1 
ATOM   771   N N   . TRP A  1 104 ? 10.036  48.093 16.195  1.00 42.17  ? 104 TRP A N   1 
ATOM   772   C CA  . TRP A  1 104 ? 9.730   47.266 17.393  1.00 42.43  ? 104 TRP A CA  1 
ATOM   773   C C   . TRP A  1 104 ? 8.337   46.651 17.257  1.00 41.95  ? 104 TRP A C   1 
ATOM   774   O O   . TRP A  1 104 ? 8.190   45.450 17.553  1.00 46.54  ? 104 TRP A O   1 
ATOM   775   C CB  . TRP A  1 104 ? 9.839   48.100 18.673  1.00 45.23  ? 104 TRP A CB  1 
ATOM   776   C CG  . TRP A  1 104 ? 11.213  48.627 18.935  1.00 46.12  ? 104 TRP A CG  1 
ATOM   777   C CD1 . TRP A  1 104 ? 12.392  48.118 18.475  1.00 48.72  ? 104 TRP A CD1 1 
ATOM   778   C CD2 . TRP A  1 104 ? 11.554  49.761 19.750  1.00 49.87  ? 104 TRP A CD2 1 
ATOM   779   N NE1 . TRP A  1 104 ? 13.442  48.863 18.935  1.00 50.05  ? 104 TRP A NE1 1 
ATOM   780   C CE2 . TRP A  1 104 ? 12.960  49.878 19.720  1.00 53.70  ? 104 TRP A CE2 1 
ATOM   781   C CE3 . TRP A  1 104 ? 10.813  50.687 20.492  1.00 51.14  ? 104 TRP A CE3 1 
ATOM   782   C CZ2 . TRP A  1 104 ? 13.635  50.886 20.406  1.00 57.23  ? 104 TRP A CZ2 1 
ATOM   783   C CZ3 . TRP A  1 104 ? 11.482  51.683 21.169  1.00 55.78  ? 104 TRP A CZ3 1 
ATOM   784   C CH2 . TRP A  1 104 ? 12.873  51.778 21.124  1.00 59.22  ? 104 TRP A CH2 1 
ATOM   785   N N   . THR A  1 105 ? 7.357   47.456 16.839  1.00 40.78  ? 105 THR A N   1 
ATOM   786   C CA  . THR A  1 105 ? 5.931   47.058 16.716  1.00 42.45  ? 105 THR A CA  1 
ATOM   787   C C   . THR A  1 105 ? 5.842   45.693 16.025  1.00 40.41  ? 105 THR A C   1 
ATOM   788   O O   . THR A  1 105 ? 5.008   44.874 16.450  1.00 37.91  ? 105 THR A O   1 
ATOM   789   C CB  . THR A  1 105 ? 5.125   48.128 15.971  1.00 46.95  ? 105 THR A CB  1 
ATOM   790   O OG1 . THR A  1 105 ? 5.237   49.358 16.689  1.00 48.21  ? 105 THR A OG1 1 
ATOM   791   C CG2 . THR A  1 105 ? 3.666   47.763 15.816  1.00 49.95  ? 105 THR A CG2 1 
ATOM   792   N N   . VAL A  1 106 ? 6.679   45.459 15.009  1.00 45.48  ? 106 VAL A N   1 
ATOM   793   C CA  . VAL A  1 106 ? 6.650   44.234 14.154  1.00 45.03  ? 106 VAL A CA  1 
ATOM   794   C C   . VAL A  1 106 ? 7.757   43.271 14.600  1.00 43.53  ? 106 VAL A C   1 
ATOM   795   O O   . VAL A  1 106 ? 7.462   42.075 14.748  1.00 42.84  ? 106 VAL A O   1 
ATOM   796   C CB  . VAL A  1 106 ? 6.789   44.587 12.660  1.00 48.03  ? 106 VAL A CB  1 
ATOM   797   C CG1 . VAL A  1 106 ? 6.595   43.368 11.771  1.00 46.75  ? 106 VAL A CG1 1 
ATOM   798   C CG2 . VAL A  1 106 ? 5.836   45.702 12.256  1.00 49.63  ? 106 VAL A CG2 1 
ATOM   799   N N   . SER A  1 107 ? 8.981   43.769 14.799  1.00 46.48  ? 107 SER A N   1 
ATOM   800   C CA  . SER A  1 107 ? 10.189  42.942 15.066  1.00 52.22  ? 107 SER A CA  1 
ATOM   801   C C   . SER A  1 107 ? 10.018  42.151 16.370  1.00 52.58  ? 107 SER A C   1 
ATOM   802   O O   . SER A  1 107 ? 10.427  40.974 16.399  1.00 61.41  ? 107 SER A O   1 
ATOM   803   C CB  . SER A  1 107 ? 11.442  43.782 15.085  1.00 52.07  ? 107 SER A CB  1 
ATOM   804   O OG  . SER A  1 107 ? 11.371  44.787 16.084  1.00 54.89  ? 107 SER A OG  1 
ATOM   805   N N   . VAL A  1 108 ? 9.423   42.764 17.397  1.00 50.87  ? 108 VAL A N   1 
ATOM   806   C CA  . VAL A  1 108 ? 9.295   42.178 18.766  1.00 54.90  ? 108 VAL A CA  1 
ATOM   807   C C   . VAL A  1 108 ? 8.314   41.007 18.737  1.00 52.18  ? 108 VAL A C   1 
ATOM   808   O O   . VAL A  1 108 ? 8.669   39.892 19.114  1.00 53.38  ? 108 VAL A O   1 
ATOM   809   C CB  . VAL A  1 108 ? 8.883   43.247 19.796  1.00 56.78  ? 108 VAL A CB  1 
ATOM   810   C CG1 . VAL A  1 108 ? 8.442   42.627 21.114  1.00 57.15  ? 108 VAL A CG1 1 
ATOM   811   C CG2 . VAL A  1 108 ? 9.999   44.257 20.019  1.00 58.13  ? 108 VAL A CG2 1 
ATOM   812   N N   . PRO A  1 109 ? 7.048   41.215 18.310  1.00 51.76  ? 109 PRO A N   1 
ATOM   813   C CA  . PRO A  1 109 ? 6.082   40.120 18.214  1.00 51.53  ? 109 PRO A CA  1 
ATOM   814   C C   . PRO A  1 109 ? 6.663   38.870 17.534  1.00 50.85  ? 109 PRO A C   1 
ATOM   815   O O   . PRO A  1 109 ? 6.374   37.773 17.981  1.00 54.18  ? 109 PRO A O   1 
ATOM   816   C CB  . PRO A  1 109 ? 4.948   40.733 17.379  1.00 48.89  ? 109 PRO A CB  1 
ATOM   817   C CG  . PRO A  1 109 ? 4.998   42.205 17.728  1.00 48.28  ? 109 PRO A CG  1 
ATOM   818   C CD  . PRO A  1 109 ? 6.471   42.510 17.918  1.00 51.11  ? 109 PRO A CD  1 
ATOM   819   N N   . LEU A  1 110 ? 7.465   39.064 16.482  1.00 46.28  ? 110 LEU A N   1 
ATOM   820   C CA  . LEU A  1 110 ? 8.145   37.970 15.739  1.00 47.79  ? 110 LEU A CA  1 
ATOM   821   C C   . LEU A  1 110 ? 9.113   37.249 16.682  1.00 49.35  ? 110 LEU A C   1 
ATOM   822   O O   . LEU A  1 110 ? 9.247   36.017 16.565  1.00 54.00  ? 110 LEU A O   1 
ATOM   823   C CB  . LEU A  1 110 ? 8.883   38.554 14.529  1.00 47.51  ? 110 LEU A CB  1 
ATOM   824   C CG  . LEU A  1 110 ? 7.989   39.018 13.379  1.00 51.12  ? 110 LEU A CG  1 
ATOM   825   C CD1 . LEU A  1 110 ? 8.810   39.688 12.290  1.00 52.66  ? 110 LEU A CD1 1 
ATOM   826   C CD2 . LEU A  1 110 ? 7.188   37.859 12.804  1.00 51.63  ? 110 LEU A CD2 1 
ATOM   827   N N   . LEU A  1 111 ? 9.757   37.998 17.583  1.00 51.74  ? 111 LEU A N   1 
ATOM   828   C CA  . LEU A  1 111 ? 10.715  37.461 18.585  1.00 52.01  ? 111 LEU A CA  1 
ATOM   829   C C   . LEU A  1 111 ? 9.976   36.521 19.543  1.00 50.98  ? 111 LEU A C   1 
ATOM   830   O O   . LEU A  1 111 ? 10.536  35.455 19.863  1.00 53.38  ? 111 LEU A O   1 
ATOM   831   C CB  . LEU A  1 111 ? 11.368  38.624 19.335  1.00 58.11  ? 111 LEU A CB  1 
ATOM   832   C CG  . LEU A  1 111 ? 12.427  39.393 18.545  1.00 65.23  ? 111 LEU A CG  1 
ATOM   833   C CD1 . LEU A  1 111 ? 12.911  40.607 19.323  1.00 69.85  ? 111 LEU A CD1 1 
ATOM   834   C CD2 . LEU A  1 111 ? 13.596  38.491 18.181  1.00 66.40  ? 111 LEU A CD2 1 
ATOM   835   N N   . THR A  1 112 ? 8.771   36.900 19.983  1.00 49.59  ? 112 THR A N   1 
ATOM   836   C CA  . THR A  1 112 ? 7.897   36.055 20.842  1.00 51.83  ? 112 THR A CA  1 
ATOM   837   C C   . THR A  1 112 ? 7.613   34.740 20.108  1.00 52.89  ? 112 THR A C   1 
ATOM   838   O O   . THR A  1 112 ? 7.940   33.670 20.659  1.00 57.61  ? 112 THR A O   1 
ATOM   839   C CB  . THR A  1 112 ? 6.590   36.768 21.216  1.00 52.28  ? 112 THR A CB  1 
ATOM   840   O OG1 . THR A  1 112 ? 5.767   36.840 20.052  1.00 59.40  ? 112 THR A OG1 1 
ATOM   841   C CG2 . THR A  1 112 ? 6.809   38.156 21.777  1.00 50.80  ? 112 THR A CG2 1 
ATOM   842   N N   . ILE A  1 113 ? 7.034   34.831 18.908  1.00 53.66  ? 113 ILE A N   1 
ATOM   843   C CA  . ILE A  1 113 ? 6.670   33.670 18.041  1.00 54.94  ? 113 ILE A CA  1 
ATOM   844   C C   . ILE A  1 113 ? 7.878   32.733 17.924  1.00 51.89  ? 113 ILE A C   1 
ATOM   845   O O   . ILE A  1 113 ? 7.690   31.507 18.043  1.00 48.33  ? 113 ILE A O   1 
ATOM   846   C CB  . ILE A  1 113 ? 6.193   34.161 16.660  1.00 56.34  ? 113 ILE A CB  1 
ATOM   847   C CG1 . ILE A  1 113 ? 4.887   34.952 16.762  1.00 55.52  ? 113 ILE A CG1 1 
ATOM   848   C CG2 . ILE A  1 113 ? 6.078   33.002 15.682  1.00 59.34  ? 113 ILE A CG2 1 
ATOM   849   C CD1 . ILE A  1 113 ? 4.619   35.847 15.575  1.00 55.19  ? 113 ILE A CD1 1 
ATOM   850   N N   . GLU A  1 114 ? 9.066   33.300 17.693  1.00 51.51  ? 114 GLU A N   1 
ATOM   851   C CA  . GLU A  1 114 ? 10.335  32.554 17.485  1.00 53.64  ? 114 GLU A CA  1 
ATOM   852   C C   . GLU A  1 114 ? 10.636  31.708 18.726  1.00 55.04  ? 114 GLU A C   1 
ATOM   853   O O   . GLU A  1 114 ? 11.034  30.538 18.562  1.00 62.16  ? 114 GLU A O   1 
ATOM   854   C CB  . GLU A  1 114 ? 11.478  33.528 17.192  1.00 61.37  ? 114 GLU A CB  1 
ATOM   855   C CG  . GLU A  1 114 ? 12.792  32.847 16.859  1.00 66.31  ? 114 GLU A CG  1 
ATOM   856   C CD  . GLU A  1 114 ? 13.908  33.800 16.459  1.00 80.36  ? 114 GLU A CD  1 
ATOM   857   O OE1 . GLU A  1 114 ? 15.082  33.371 16.454  1.00 95.14  ? 114 GLU A OE1 1 
ATOM   858   O OE2 . GLU A  1 114 ? 13.602  34.969 16.149  1.00 88.50  ? 114 GLU A OE2 1 
ATOM   859   N N   . LEU A  1 115 ? 10.450  32.281 19.919  1.00 53.48  ? 115 LEU A N   1 
ATOM   860   C CA  . LEU A  1 115 ? 10.710  31.602 21.216  1.00 56.24  ? 115 LEU A CA  1 
ATOM   861   C C   . LEU A  1 115 ? 9.656   30.511 21.447  1.00 53.76  ? 115 LEU A C   1 
ATOM   862   O O   . LEU A  1 115 ? 10.039  29.398 21.852  1.00 57.93  ? 115 LEU A O   1 
ATOM   863   C CB  . LEU A  1 115 ? 10.686  32.638 22.343  1.00 64.37  ? 115 LEU A CB  1 
ATOM   864   C CG  . LEU A  1 115 ? 11.013  32.090 23.731  1.00 67.08  ? 115 LEU A CG  1 
ATOM   865   C CD1 . LEU A  1 115 ? 12.368  31.397 23.731  1.00 65.75  ? 115 LEU A CD1 1 
ATOM   866   C CD2 . LEU A  1 115 ? 10.974  33.196 24.774  1.00 67.59  ? 115 LEU A CD2 1 
ATOM   867   N N   . LEU A  1 116 ? 8.381   30.823 21.200  1.00 52.45  ? 116 LEU A N   1 
ATOM   868   C CA  . LEU A  1 116 ? 7.236   29.892 21.395  1.00 55.41  ? 116 LEU A CA  1 
ATOM   869   C C   . LEU A  1 116 ? 7.352   28.711 20.425  1.00 58.13  ? 116 LEU A C   1 
ATOM   870   O O   . LEU A  1 116 ? 6.849   27.618 20.757  1.00 56.34  ? 116 LEU A O   1 
ATOM   871   C CB  . LEU A  1 116 ? 5.926   30.656 21.180  1.00 54.81  ? 116 LEU A CB  1 
ATOM   872   C CG  . LEU A  1 116 ? 5.596   31.692 22.252  1.00 56.55  ? 116 LEU A CG  1 
ATOM   873   C CD1 . LEU A  1 116 ? 4.241   32.331 21.986  1.00 61.71  ? 116 LEU A CD1 1 
ATOM   874   C CD2 . LEU A  1 116 ? 5.633   31.068 23.640  1.00 52.41  ? 116 LEU A CD2 1 
ATOM   875   N N   . ALA A  1 117 ? 7.991   28.926 19.273  1.00 60.78  ? 117 ALA A N   1 
ATOM   876   C CA  . ALA A  1 117 ? 8.173   27.917 18.204  1.00 56.85  ? 117 ALA A CA  1 
ATOM   877   C C   . ALA A  1 117 ? 9.107   26.803 18.693  1.00 57.52  ? 117 ALA A C   1 
ATOM   878   O O   . ALA A  1 117 ? 8.860   25.633 18.345  1.00 63.18  ? 117 ALA A O   1 
ATOM   879   C CB  . ALA A  1 117 ? 8.709   28.578 16.960  1.00 59.29  ? 117 ALA A CB  1 
ATOM   880   N N   . VAL A  1 118 ? 10.139  27.158 19.467  1.00 59.16  ? 118 VAL A N   1 
ATOM   881   C CA  . VAL A  1 118 ? 11.164  26.205 19.992  1.00 60.94  ? 118 VAL A CA  1 
ATOM   882   C C   . VAL A  1 118 ? 10.681  25.638 21.332  1.00 58.44  ? 118 VAL A C   1 
ATOM   883   O O   . VAL A  1 118 ? 11.321  24.691 21.835  1.00 52.37  ? 118 VAL A O   1 
ATOM   884   C CB  . VAL A  1 118 ? 12.549  26.869 20.124  1.00 65.38  ? 118 VAL A CB  1 
ATOM   885   C CG1 . VAL A  1 118 ? 13.185  27.116 18.764  1.00 70.26  ? 118 VAL A CG1 1 
ATOM   886   C CG2 . VAL A  1 118 ? 12.487  28.158 20.927  1.00 67.47  ? 118 VAL A CG2 1 
ATOM   887   N N   . CYS A  1 119 ? 9.597   26.198 21.882  1.00 64.35  ? 119 CYS A N   1 
ATOM   888   C CA  . CYS A  1 119 ? 8.881   25.674 23.078  1.00 70.89  ? 119 CYS A CA  1 
ATOM   889   C C   . CYS A  1 119 ? 8.062   24.439 22.679  1.00 82.25  ? 119 CYS A C   1 
ATOM   890   O O   . CYS A  1 119 ? 7.781   24.275 21.474  1.00 77.47  ? 119 CYS A O   1 
ATOM   891   C CB  . CYS A  1 119 ? 7.970   26.727 23.700  1.00 72.70  ? 119 CYS A CB  1 
ATOM   892   S SG  . CYS A  1 119 ? 8.851   27.982 24.666  1.00 70.24  ? 119 CYS A SG  1 
ATOM   893   N N   . ALA A  1 120 ? 7.685   23.615 23.661  1.00 103.04 ? 120 ALA A N   1 
ATOM   894   C CA  . ALA A  1 120 ? 7.025   22.302 23.470  1.00 112.75 ? 120 ALA A CA  1 
ATOM   895   C C   . ALA A  1 120 ? 5.498   22.449 23.533  1.00 120.96 ? 120 ALA A C   1 
ATOM   896   O O   . ALA A  1 120 ? 4.806   21.415 23.456  1.00 131.47 ? 120 ALA A O   1 
ATOM   897   C CB  . ALA A  1 120 ? 7.526   21.330 24.510  1.00 108.70 ? 120 ALA A CB  1 
ATOM   898   N N   . THR A  1 121 ? 4.994   23.680 23.671  1.00 125.91 ? 121 THR A N   1 
ATOM   899   C CA  . THR A  1 121 ? 3.541   24.002 23.719  1.00 124.15 ? 121 THR A CA  1 
ATOM   900   C C   . THR A  1 121 ? 2.833   23.286 22.561  1.00 121.44 ? 121 THR A C   1 
ATOM   901   O O   . THR A  1 121 ? 3.386   23.296 21.443  1.00 118.12 ? 121 THR A O   1 
ATOM   902   C CB  . THR A  1 121 ? 3.311   25.519 23.682  1.00 126.77 ? 121 THR A CB  1 
ATOM   903   O OG1 . THR A  1 121 ? 3.971   26.038 22.527  1.00 133.33 ? 121 THR A OG1 1 
ATOM   904   C CG2 . THR A  1 121 ? 3.818   26.223 24.921  1.00 126.82 ? 121 THR A CG2 1 
ATOM   905   N N   . LEU A  1 122 ? 1.665   22.686 22.825  1.00 119.48 ? 122 LEU A N   1 
ATOM   906   C CA  . LEU A  1 122 ? 0.895   21.870 21.843  1.00 118.88 ? 122 LEU A CA  1 
ATOM   907   C C   . LEU A  1 122 ? -0.567  22.332 21.800  1.00 120.15 ? 122 LEU A C   1 
ATOM   908   O O   . LEU A  1 122 ? -1.111  22.674 22.869  1.00 103.03 ? 122 LEU A O   1 
ATOM   909   C CB  . LEU A  1 122 ? 0.974   20.392 22.241  1.00 109.68 ? 122 LEU A CB  1 
ATOM   910   C CG  . LEU A  1 122 ? 2.362   19.869 22.603  1.00 111.40 ? 122 LEU A CG  1 
ATOM   911   C CD1 . LEU A  1 122 ? 2.278   18.466 23.187  1.00 99.64  ? 122 LEU A CD1 1 
ATOM   912   C CD2 . LEU A  1 122 ? 3.283   19.891 21.394  1.00 121.98 ? 122 LEU A CD2 1 
ATOM   913   N N   . GLY A  1 123 ? -1.171  22.322 20.605  1.00 121.50 ? 123 GLY A N   1 
ATOM   914   C CA  . GLY A  1 123 ? -2.619  22.521 20.383  1.00 117.01 ? 123 GLY A CA  1 
ATOM   915   C C   . GLY A  1 123 ? -3.064  23.948 20.657  1.00 120.32 ? 123 GLY A C   1 
ATOM   916   O O   . GLY A  1 123 ? -2.510  24.868 20.026  1.00 116.51 ? 123 GLY A O   1 
ATOM   917   N N   . VAL A  1 124 ? -4.035  24.116 21.563  1.00 126.69 ? 124 VAL A N   1 
ATOM   918   C CA  . VAL A  1 124 ? -4.668  25.420 21.925  1.00 135.24 ? 124 VAL A CA  1 
ATOM   919   C C   . VAL A  1 124 ? -3.717  26.214 22.828  1.00 133.39 ? 124 VAL A C   1 
ATOM   920   O O   . VAL A  1 124 ? -3.593  27.437 22.613  1.00 144.82 ? 124 VAL A O   1 
ATOM   921   C CB  . VAL A  1 124 ? -6.034  25.201 22.606  1.00 136.27 ? 124 VAL A CB  1 
ATOM   922   C CG1 . VAL A  1 124 ? -6.578  26.478 23.234  1.00 138.16 ? 124 VAL A CG1 1 
ATOM   923   C CG2 . VAL A  1 124 ? -7.044  24.603 21.641  1.00 126.86 ? 124 VAL A CG2 1 
ATOM   924   N N   . GLN A  1 125 ? -3.091  25.544 23.802  1.00 121.71 ? 125 GLN A N   1 
ATOM   925   C CA  . GLN A  1 125 ? -2.145  26.159 24.771  1.00 112.38 ? 125 GLN A CA  1 
ATOM   926   C C   . GLN A  1 125 ? -1.093  26.958 23.995  1.00 122.39 ? 125 GLN A C   1 
ATOM   927   O O   . GLN A  1 125 ? -0.717  28.046 24.468  1.00 131.23 ? 125 GLN A O   1 
ATOM   928   C CB  . GLN A  1 125 ? -1.490  25.086 25.643  1.00 94.45  ? 125 GLN A CB  1 
ATOM   929   N N   . ALA A  1 126 ? -0.653  26.431 22.846  1.00 124.84 ? 126 ALA A N   1 
ATOM   930   C CA  . ALA A  1 126 ? 0.365   27.034 21.954  1.00 109.83 ? 126 ALA A CA  1 
ATOM   931   C C   . ALA A  1 126 ? -0.230  28.247 21.230  1.00 99.94  ? 126 ALA A C   1 
ATOM   932   O O   . ALA A  1 126 ? 0.329   29.354 21.367  1.00 110.37 ? 126 ALA A O   1 
ATOM   933   C CB  . ALA A  1 126 ? 0.863   25.999 20.975  1.00 104.30 ? 126 ALA A CB  1 
ATOM   934   N N   . ARG A  1 127 ? -1.325  28.036 20.491  1.00 84.99  ? 127 ARG A N   1 
ATOM   935   C CA  . ARG A  1 127 ? -1.999  29.071 19.662  1.00 79.19  ? 127 ARG A CA  1 
ATOM   936   C C   . ARG A  1 127 ? -2.467  30.227 20.555  1.00 87.17  ? 127 ARG A C   1 
ATOM   937   O O   . ARG A  1 127 ? -2.367  31.388 20.110  1.00 99.95  ? 127 ARG A O   1 
ATOM   938   C CB  . ARG A  1 127 ? -3.176  28.462 18.894  1.00 67.95  ? 127 ARG A CB  1 
ATOM   939   N N   . ARG A  1 128 ? -2.959  29.922 21.761  1.00 83.99  ? 128 ARG A N   1 
ATOM   940   C CA  . ARG A  1 128 ? -3.449  30.931 22.742  1.00 81.03  ? 128 ARG A CA  1 
ATOM   941   C C   . ARG A  1 128 ? -2.274  31.805 23.190  1.00 84.93  ? 128 ARG A C   1 
ATOM   942   O O   . ARG A  1 128 ? -2.406  33.044 23.137  1.00 95.44  ? 128 ARG A O   1 
ATOM   943   C CB  . ARG A  1 128 ? -4.111  30.250 23.944  1.00 72.97  ? 128 ARG A CB  1 
ATOM   944   N N   . ASN A  1 129 ? -1.171  31.175 23.609  1.00 89.88  ? 129 ASN A N   1 
ATOM   945   C CA  . ASN A  1 129 ? 0.059   31.859 24.091  1.00 91.97  ? 129 ASN A CA  1 
ATOM   946   C C   . ASN A  1 129 ? 0.517   32.874 23.039  1.00 88.95  ? 129 ASN A C   1 
ATOM   947   O O   . ASN A  1 129 ? 0.656   34.063 23.391  1.00 98.96  ? 129 ASN A O   1 
ATOM   948   C CB  . ASN A  1 129 ? 1.173   30.863 24.419  1.00 98.84  ? 129 ASN A CB  1 
ATOM   949   C CG  . ASN A  1 129 ? 0.884   30.050 25.663  1.00 97.95  ? 129 ASN A CG  1 
ATOM   950   O OD1 . ASN A  1 129 ? -0.148  30.236 26.303  1.00 101.62 ? 129 ASN A OD1 1 
ATOM   951   N ND2 . ASN A  1 129 ? 1.787   29.149 26.013  1.00 94.28  ? 129 ASN A ND2 1 
ATOM   952   N N   . THR A  1 130 ? 0.737   32.414 21.803  1.00 74.48  ? 130 THR A N   1 
ATOM   953   C CA  . THR A  1 130 ? 1.179   33.245 20.650  1.00 73.96  ? 130 THR A CA  1 
ATOM   954   C C   . THR A  1 130 ? 0.280   34.483 20.547  1.00 68.41  ? 130 THR A C   1 
ATOM   955   O O   . THR A  1 130 ? 0.822   35.608 20.548  1.00 70.54  ? 130 THR A O   1 
ATOM   956   C CB  . THR A  1 130 ? 1.168   32.434 19.347  1.00 69.38  ? 130 THR A CB  1 
ATOM   957   O OG1 . THR A  1 130 ? 1.832   31.196 19.595  1.00 70.30  ? 130 THR A OG1 1 
ATOM   958   C CG2 . THR A  1 130 ? 1.832   33.153 18.192  1.00 71.61  ? 130 THR A CG2 1 
ATOM   959   N N   . ALA A  1 131 ? -1.038  34.274 20.475  1.00 63.41  ? 131 ALA A N   1 
ATOM   960   C CA  . ALA A  1 131 ? -2.065  35.327 20.297  1.00 70.74  ? 131 ALA A CA  1 
ATOM   961   C C   . ALA A  1 131 ? -1.893  36.412 21.366  1.00 73.77  ? 131 ALA A C   1 
ATOM   962   O O   . ALA A  1 131 ? -1.939  37.607 21.010  1.00 76.06  ? 131 ALA A O   1 
ATOM   963   C CB  . ALA A  1 131 ? -3.442  34.714 20.353  1.00 72.54  ? 131 ALA A CB  1 
ATOM   964   N N   . ILE A  1 132 ? -1.707  36.002 22.625  1.00 71.23  ? 132 ILE A N   1 
ATOM   965   C CA  . ILE A  1 132 ? -1.555  36.914 23.798  1.00 72.73  ? 132 ILE A CA  1 
ATOM   966   C C   . ILE A  1 132 ? -0.206  37.633 23.690  1.00 69.55  ? 132 ILE A C   1 
ATOM   967   O O   . ILE A  1 132 ? -0.200  38.880 23.710  1.00 69.36  ? 132 ILE A O   1 
ATOM   968   C CB  . ILE A  1 132 ? -1.691  36.134 25.121  1.00 79.82  ? 132 ILE A CB  1 
ATOM   969   C CG1 . ILE A  1 132 ? -3.066  35.471 25.241  1.00 88.02  ? 132 ILE A CG1 1 
ATOM   970   C CG2 . ILE A  1 132 ? -1.392  37.032 26.312  1.00 80.94  ? 132 ILE A CG2 1 
ATOM   971   C CD1 . ILE A  1 132 ? -3.225  34.599 26.464  1.00 99.29  ? 132 ILE A CD1 1 
ATOM   972   N N   . ALA A  1 133 ? 0.885   36.870 23.575  1.00 65.85  ? 133 ALA A N   1 
ATOM   973   C CA  . ALA A  1 133 ? 2.275   37.376 23.481  1.00 69.96  ? 133 ALA A CA  1 
ATOM   974   C C   . ALA A  1 133 ? 2.370   38.431 22.375  1.00 74.58  ? 133 ALA A C   1 
ATOM   975   O O   . ALA A  1 133 ? 2.941   39.509 22.635  1.00 77.62  ? 133 ALA A O   1 
ATOM   976   C CB  . ALA A  1 133 ? 3.228   36.233 23.228  1.00 71.77  ? 133 ALA A CB  1 
ATOM   977   N N   . VAL A  1 134 ? 1.837   38.125 21.187  1.00 66.60  ? 134 VAL A N   1 
ATOM   978   C CA  . VAL A  1 134 ? 1.891   39.015 19.989  1.00 65.03  ? 134 VAL A CA  1 
ATOM   979   C C   . VAL A  1 134 ? 1.149   40.317 20.309  1.00 62.82  ? 134 VAL A C   1 
ATOM   980   O O   . VAL A  1 134 ? 1.790   41.384 20.268  1.00 72.25  ? 134 VAL A O   1 
ATOM   981   C CB  . VAL A  1 134 ? 1.311   38.324 18.740  1.00 63.07  ? 134 VAL A CB  1 
ATOM   982   C CG1 . VAL A  1 134 ? 1.037   39.313 17.616  1.00 58.00  ? 134 VAL A CG1 1 
ATOM   983   C CG2 . VAL A  1 134 ? 2.217   37.202 18.256  1.00 62.21  ? 134 VAL A CG2 1 
ATOM   984   N N   . THR A  1 135 ? -0.146  40.227 20.622  1.00 58.12  ? 135 THR A N   1 
ATOM   985   C CA  . THR A  1 135 ? -1.029  41.396 20.880  1.00 59.23  ? 135 THR A CA  1 
ATOM   986   C C   . THR A  1 135 ? -0.489  42.180 22.082  1.00 59.08  ? 135 THR A C   1 
ATOM   987   O O   . THR A  1 135 ? -0.541  43.424 22.044  1.00 66.25  ? 135 THR A O   1 
ATOM   988   C CB  . THR A  1 135 ? -2.486  40.959 21.075  1.00 59.72  ? 135 THR A CB  1 
ATOM   989   O OG1 . THR A  1 135 ? -2.522  40.027 22.156  1.00 73.93  ? 135 THR A OG1 1 
ATOM   990   C CG2 . THR A  1 135 ? -3.078  40.331 19.832  1.00 59.48  ? 135 THR A CG2 1 
ATOM   991   N N   . ALA A  1 136 ? 0.017   41.476 23.099  1.00 59.44  ? 136 ALA A N   1 
ATOM   992   C CA  . ALA A  1 136 ? 0.625   42.067 24.314  1.00 58.78  ? 136 ALA A CA  1 
ATOM   993   C C   . ALA A  1 136 ? 1.811   42.949 23.909  1.00 62.19  ? 136 ALA A C   1 
ATOM   994   O O   . ALA A  1 136 ? 1.774   44.157 24.207  1.00 72.51  ? 136 ALA A O   1 
ATOM   995   C CB  . ALA A  1 136 ? 1.045   40.978 25.269  1.00 59.75  ? 136 ALA A CB  1 
ATOM   996   N N   . THR A  1 137 ? 2.816   42.364 23.248  1.00 61.65  ? 137 THR A N   1 
ATOM   997   C CA  . THR A  1 137 ? 4.061   43.052 22.806  1.00 63.68  ? 137 THR A CA  1 
ATOM   998   C C   . THR A  1 137 ? 3.713   44.158 21.803  1.00 59.51  ? 137 THR A C   1 
ATOM   999   O O   . THR A  1 137 ? 4.321   45.244 21.892  1.00 59.22  ? 137 THR A O   1 
ATOM   1000  C CB  . THR A  1 137 ? 5.075   42.057 22.226  1.00 67.89  ? 137 THR A CB  1 
ATOM   1001  O OG1 . THR A  1 137 ? 4.410   41.231 21.271  1.00 71.73  ? 137 THR A OG1 1 
ATOM   1002  C CG2 . THR A  1 137 ? 5.716   41.190 23.288  1.00 68.65  ? 137 THR A CG2 1 
ATOM   1003  N N   . GLY A  1 138 ? 2.777   43.892 20.887  1.00 57.56  ? 138 GLY A N   1 
ATOM   1004  C CA  . GLY A  1 138 ? 2.263   44.888 19.927  1.00 54.47  ? 138 GLY A CA  1 
ATOM   1005  C C   . GLY A  1 138 ? 1.746   46.121 20.648  1.00 53.46  ? 138 GLY A C   1 
ATOM   1006  O O   . GLY A  1 138 ? 2.220   47.234 20.341  1.00 48.08  ? 138 GLY A O   1 
ATOM   1007  N N   . ALA A  1 139 ? 0.814   45.920 21.584  1.00 51.34  ? 139 ALA A N   1 
ATOM   1008  C CA  . ALA A  1 139 ? 0.209   46.968 22.439  1.00 55.02  ? 139 ALA A CA  1 
ATOM   1009  C C   . ALA A  1 139 ? 1.305   47.669 23.251  1.00 54.41  ? 139 ALA A C   1 
ATOM   1010  O O   . ALA A  1 139 ? 1.312   48.915 23.285  1.00 50.57  ? 139 ALA A O   1 
ATOM   1011  C CB  . ALA A  1 139 ? -0.831  46.347 23.338  1.00 56.40  ? 139 ALA A CB  1 
ATOM   1012  N N   . MET A  1 140 ? 2.188   46.887 23.880  1.00 52.93  ? 140 MET A N   1 
ATOM   1013  C CA  . MET A  1 140 ? 3.330   47.386 24.694  1.00 54.83  ? 140 MET A CA  1 
ATOM   1014  C C   . MET A  1 140 ? 4.031   48.522 23.940  1.00 57.18  ? 140 MET A C   1 
ATOM   1015  O O   . MET A  1 140 ? 4.201   49.610 24.525  1.00 57.61  ? 140 MET A O   1 
ATOM   1016  C CB  . MET A  1 140 ? 4.336   46.264 24.969  1.00 52.80  ? 140 MET A CB  1 
ATOM   1017  C CG  . MET A  1 140 ? 5.596   46.740 25.666  1.00 54.53  ? 140 MET A CG  1 
ATOM   1018  S SD  . MET A  1 140 ? 6.724   45.382 26.072  1.00 60.25  ? 140 MET A SD  1 
ATOM   1019  C CE  . MET A  1 140 ? 7.258   44.887 24.435  1.00 61.63  ? 140 MET A CE  1 
ATOM   1020  N N   . ILE A  1 141 ? 4.419   48.269 22.687  1.00 57.21  ? 141 ILE A N   1 
ATOM   1021  C CA  . ILE A  1 141 ? 5.155   49.233 21.816  1.00 52.34  ? 141 ILE A CA  1 
ATOM   1022  C C   . ILE A  1 141 ? 4.232   50.411 21.484  1.00 52.71  ? 141 ILE A C   1 
ATOM   1023  O O   . ILE A  1 141 ? 4.638   51.563 21.725  1.00 53.33  ? 141 ILE A O   1 
ATOM   1024  C CB  . ILE A  1 141 ? 5.672   48.541 20.540  1.00 48.19  ? 141 ILE A CB  1 
ATOM   1025  C CG1 . ILE A  1 141 ? 6.541   47.322 20.861  1.00 42.73  ? 141 ILE A CG1 1 
ATOM   1026  C CG2 . ILE A  1 141 ? 6.398   49.539 19.651  1.00 45.30  ? 141 ILE A CG2 1 
ATOM   1027  C CD1 . ILE A  1 141 ? 7.767   47.641 21.681  1.00 43.94  ? 141 ILE A CD1 1 
ATOM   1028  N N   . PHE A  1 142 ? 3.040   50.125 20.949  1.00 52.54  ? 142 PHE A N   1 
ATOM   1029  C CA  . PHE A  1 142 ? 2.060   51.140 20.481  1.00 49.42  ? 142 PHE A CA  1 
ATOM   1030  C C   . PHE A  1 142 ? 1.783   52.146 21.601  1.00 50.74  ? 142 PHE A C   1 
ATOM   1031  O O   . PHE A  1 142 ? 1.573   53.332 21.296  1.00 50.57  ? 142 PHE A O   1 
ATOM   1032  C CB  . PHE A  1 142 ? 0.758   50.484 20.017  1.00 51.21  ? 142 PHE A CB  1 
ATOM   1033  C CG  . PHE A  1 142 ? -0.284  51.464 19.543  1.00 52.84  ? 142 PHE A CG  1 
ATOM   1034  C CD1 . PHE A  1 142 ? -1.440  51.686 20.275  1.00 51.13  ? 142 PHE A CD1 1 
ATOM   1035  C CD2 . PHE A  1 142 ? -0.097  52.184 18.374  1.00 57.47  ? 142 PHE A CD2 1 
ATOM   1036  C CE1 . PHE A  1 142 ? -2.391  52.593 19.837  1.00 54.47  ? 142 PHE A CE1 1 
ATOM   1037  C CE2 . PHE A  1 142 ? -1.050  53.091 17.938  1.00 55.46  ? 142 PHE A CE2 1 
ATOM   1038  C CZ  . PHE A  1 142 ? -2.195  53.294 18.671  1.00 54.09  ? 142 PHE A CZ  1 
ATOM   1039  N N   . CYS A  1 143 ? 1.771   51.682 22.854  1.00 55.15  ? 143 CYS A N   1 
ATOM   1040  C CA  . CYS A  1 143 ? 1.556   52.523 24.063  1.00 55.03  ? 143 CYS A CA  1 
ATOM   1041  C C   . CYS A  1 143 ? 2.719   53.509 24.210  1.00 51.26  ? 143 CYS A C   1 
ATOM   1042  O O   . CYS A  1 143 ? 2.459   54.727 24.224  1.00 51.13  ? 143 CYS A O   1 
ATOM   1043  C CB  . CYS A  1 143 ? 1.413   51.667 25.315  1.00 57.26  ? 143 CYS A CB  1 
ATOM   1044  S SG  . CYS A  1 143 ? -0.208  50.869 25.443  1.00 60.21  ? 143 CYS A SG  1 
ATOM   1045  N N   . GLY A  1 144 ? 3.948   52.995 24.307  1.00 50.17  ? 144 GLY A N   1 
ATOM   1046  C CA  . GLY A  1 144 ? 5.180   53.807 24.351  1.00 53.83  ? 144 GLY A CA  1 
ATOM   1047  C C   . GLY A  1 144 ? 5.197   54.853 23.248  1.00 54.20  ? 144 GLY A C   1 
ATOM   1048  O O   . GLY A  1 144 ? 5.680   55.974 23.504  1.00 50.54  ? 144 GLY A O   1 
ATOM   1049  N N   . PHE A  1 145 ? 4.684   54.500 22.063  1.00 53.21  ? 145 PHE A N   1 
ATOM   1050  C CA  . PHE A  1 145 ? 4.594   55.383 20.869  1.00 48.89  ? 145 PHE A CA  1 
ATOM   1051  C C   . PHE A  1 145 ? 3.669   56.567 21.178  1.00 48.67  ? 145 PHE A C   1 
ATOM   1052  O O   . PHE A  1 145 ? 4.058   57.721 20.906  1.00 48.02  ? 145 PHE A O   1 
ATOM   1053  C CB  . PHE A  1 145 ? 4.106   54.594 19.651  1.00 49.60  ? 145 PHE A CB  1 
ATOM   1054  C CG  . PHE A  1 145 ? 3.981   55.401 18.383  1.00 51.50  ? 145 PHE A CG  1 
ATOM   1055  C CD1 . PHE A  1 145 ? 2.763   55.522 17.731  1.00 50.26  ? 145 PHE A CD1 1 
ATOM   1056  C CD2 . PHE A  1 145 ? 5.083   56.046 17.842  1.00 54.45  ? 145 PHE A CD2 1 
ATOM   1057  C CE1 . PHE A  1 145 ? 2.652   56.266 16.567  1.00 50.38  ? 145 PHE A CE1 1 
ATOM   1058  C CE2 . PHE A  1 145 ? 4.970   56.790 16.678  1.00 50.61  ? 145 PHE A CE2 1 
ATOM   1059  C CZ  . PHE A  1 145 ? 3.755   56.898 16.042  1.00 49.60  ? 145 PHE A CZ  1 
ATOM   1060  N N   . LEU A  1 146 ? 2.484   56.287 21.731  1.00 46.71  ? 146 LEU A N   1 
ATOM   1061  C CA  . LEU A  1 146 ? 1.473   57.310 22.111  1.00 47.27  ? 146 LEU A CA  1 
ATOM   1062  C C   . LEU A  1 146 ? 2.100   58.303 23.097  1.00 45.66  ? 146 LEU A C   1 
ATOM   1063  O O   . LEU A  1 146 ? 1.963   59.523 22.879  1.00 46.47  ? 146 LEU A O   1 
ATOM   1064  C CB  . LEU A  1 146 ? 0.257   56.614 22.730  1.00 48.69  ? 146 LEU A CB  1 
ATOM   1065  C CG  . LEU A  1 146 ? -0.646  55.868 21.749  1.00 50.07  ? 146 LEU A CG  1 
ATOM   1066  C CD1 . LEU A  1 146 ? -1.820  55.230 22.476  1.00 52.78  ? 146 LEU A CD1 1 
ATOM   1067  C CD2 . LEU A  1 146 ? -1.142  56.794 20.650  1.00 47.29  ? 146 LEU A CD2 1 
ATOM   1068  N N   . GLY A  1 147 ? 2.768   57.790 24.133  1.00 42.38  ? 147 GLY A N   1 
ATOM   1069  C CA  . GLY A  1 147 ? 3.375   58.598 25.208  1.00 45.51  ? 147 GLY A CA  1 
ATOM   1070  C C   . GLY A  1 147 ? 4.476   59.512 24.694  1.00 46.30  ? 147 GLY A C   1 
ATOM   1071  O O   . GLY A  1 147 ? 4.396   60.733 24.944  1.00 41.81  ? 147 GLY A O   1 
ATOM   1072  N N   . ALA A  1 148 ? 5.460   58.944 23.990  1.00 51.19  ? 148 ALA A N   1 
ATOM   1073  C CA  . ALA A  1 148 ? 6.755   59.585 23.660  1.00 51.80  ? 148 ALA A CA  1 
ATOM   1074  C C   . ALA A  1 148 ? 6.648   60.445 22.393  1.00 52.49  ? 148 ALA A C   1 
ATOM   1075  O O   . ALA A  1 148 ? 7.463   61.380 22.252  1.00 54.00  ? 148 ALA A O   1 
ATOM   1076  C CB  . ALA A  1 148 ? 7.816   58.522 23.507  1.00 49.97  ? 148 ALA A CB  1 
ATOM   1077  N N   . ILE A  1 149 ? 5.691   60.145 21.508  1.00 52.17  ? 149 ILE A N   1 
ATOM   1078  C CA  . ILE A  1 149 ? 5.642   60.703 20.122  1.00 52.95  ? 149 ILE A CA  1 
ATOM   1079  C C   . ILE A  1 149 ? 4.286   61.365 19.859  1.00 51.02  ? 149 ILE A C   1 
ATOM   1080  O O   . ILE A  1 149 ? 4.264   62.593 19.643  1.00 56.05  ? 149 ILE A O   1 
ATOM   1081  C CB  . ILE A  1 149 ? 5.934   59.601 19.084  1.00 60.60  ? 149 ILE A CB  1 
ATOM   1082  C CG1 . ILE A  1 149 ? 7.330   58.996 19.264  1.00 65.95  ? 149 ILE A CG1 1 
ATOM   1083  C CG2 . ILE A  1 149 ? 5.728   60.130 17.673  1.00 62.74  ? 149 ILE A CG2 1 
ATOM   1084  C CD1 . ILE A  1 149 ? 8.453   59.888 18.790  1.00 67.47  ? 149 ILE A CD1 1 
ATOM   1085  N N   . VAL A  1 150 ? 3.208   60.575 19.858  1.00 54.26  ? 150 VAL A N   1 
ATOM   1086  C CA  . VAL A  1 150 ? 1.880   60.955 19.287  1.00 62.64  ? 150 VAL A CA  1 
ATOM   1087  C C   . VAL A  1 150 ? 1.259   62.090 20.111  1.00 61.23  ? 150 VAL A C   1 
ATOM   1088  O O   . VAL A  1 150 ? 0.938   63.138 19.517  1.00 70.31  ? 150 VAL A O   1 
ATOM   1089  C CB  . VAL A  1 150 ? 0.933   59.743 19.211  1.00 66.74  ? 150 VAL A CB  1 
ATOM   1090  C CG1 . VAL A  1 150 ? -0.433  60.131 18.669  1.00 69.76  ? 150 VAL A CG1 1 
ATOM   1091  C CG2 . VAL A  1 150 ? 1.532   58.612 18.389  1.00 71.62  ? 150 VAL A CG2 1 
ATOM   1092  N N   . ILE A  1 151 ? 1.089   61.880 21.420  1.00 59.04  ? 151 ILE A N   1 
ATOM   1093  C CA  . ILE A  1 151 ? 0.319   62.781 22.329  1.00 62.87  ? 151 ILE A CA  1 
ATOM   1094  C C   . ILE A  1 151 ? 1.109   64.072 22.570  1.00 63.17  ? 151 ILE A C   1 
ATOM   1095  O O   . ILE A  1 151 ? 2.200   64.001 23.172  1.00 61.86  ? 151 ILE A O   1 
ATOM   1096  C CB  . ILE A  1 151 ? -0.021  62.060 23.647  1.00 65.54  ? 151 ILE A CB  1 
ATOM   1097  C CG1 . ILE A  1 151 ? -0.985  60.895 23.411  1.00 69.60  ? 151 ILE A CG1 1 
ATOM   1098  C CG2 . ILE A  1 151 ? -0.564  63.042 24.673  1.00 67.54  ? 151 ILE A CG2 1 
ATOM   1099  C CD1 . ILE A  1 151 ? -1.258  60.066 24.641  1.00 73.00  ? 151 ILE A CD1 1 
ATOM   1100  N N   . ASP A  1 152 ? 0.556   65.205 22.123  1.00 60.85  ? 152 ASP A N   1 
ATOM   1101  C CA  . ASP A  1 152 ? 1.111   66.569 22.335  1.00 61.22  ? 152 ASP A CA  1 
ATOM   1102  C C   . ASP A  1 152 ? 2.592   66.573 21.943  1.00 62.99  ? 152 ASP A C   1 
ATOM   1103  O O   . ASP A  1 152 ? 3.400   67.152 22.692  1.00 72.64  ? 152 ASP A O   1 
ATOM   1104  C CB  . ASP A  1 152 ? 0.890   67.026 23.778  1.00 64.37  ? 152 ASP A CB  1 
ATOM   1105  C CG  . ASP A  1 152 ? -0.577  67.098 24.169  1.00 68.27  ? 152 ASP A CG  1 
ATOM   1106  O OD1 . ASP A  1 152 ? -1.387  67.523 23.321  1.00 75.06  ? 152 ASP A OD1 1 
ATOM   1107  O OD2 . ASP A  1 152 ? -0.901  66.721 25.314  1.00 59.62  ? 152 ASP A OD2 1 
ATOM   1108  N N   . ASN A  1 153 ? 2.919   65.937 20.813  1.00 65.22  ? 153 ASN A N   1 
ATOM   1109  C CA  . ASN A  1 153 ? 4.275   65.915 20.203  1.00 65.44  ? 153 ASN A CA  1 
ATOM   1110  C C   . ASN A  1 153 ? 5.298   65.446 21.243  1.00 62.03  ? 153 ASN A C   1 
ATOM   1111  O O   . ASN A  1 153 ? 6.477   65.844 21.135  1.00 52.97  ? 153 ASN A O   1 
ATOM   1112  C CB  . ASN A  1 153 ? 4.626   67.283 19.616  1.00 66.93  ? 153 ASN A CB  1 
ATOM   1113  C CG  . ASN A  1 153 ? 3.533   67.809 18.710  1.00 66.96  ? 153 ASN A CG  1 
ATOM   1114  O OD1 . ASN A  1 153 ? 2.753   67.036 18.158  1.00 73.60  ? 153 ASN A OD1 1 
ATOM   1115  N ND2 . ASN A  1 153 ? 3.464   69.120 18.553  1.00 68.75  ? 153 ASN A ND2 1 
ATOM   1116  N N   . GLY A  1 154 ? 4.847   64.632 22.205  1.00 65.41  ? 154 GLY A N   1 
ATOM   1117  C CA  . GLY A  1 154 ? 5.689   63.961 23.215  1.00 65.76  ? 154 GLY A CA  1 
ATOM   1118  C C   . GLY A  1 154 ? 6.285   64.941 24.212  1.00 64.66  ? 154 GLY A C   1 
ATOM   1119  O O   . GLY A  1 154 ? 7.390   64.660 24.712  1.00 64.34  ? 154 GLY A O   1 
ATOM   1120  N N   . THR A  1 155 ? 5.586   66.045 24.496  1.00 66.68  ? 155 THR A N   1 
ATOM   1121  C CA  . THR A  1 155 ? 6.018   67.099 25.454  1.00 70.37  ? 155 THR A CA  1 
ATOM   1122  C C   . THR A  1 155 ? 5.244   66.946 26.770  1.00 72.73  ? 155 THR A C   1 
ATOM   1123  O O   . THR A  1 155 ? 5.795   67.327 27.823  1.00 79.49  ? 155 THR A O   1 
ATOM   1124  C CB  . THR A  1 155 ? 5.846   68.502 24.855  1.00 66.30  ? 155 THR A CB  1 
ATOM   1125  O OG1 . THR A  1 155 ? 4.484   68.651 24.454  1.00 67.82  ? 155 THR A OG1 1 
ATOM   1126  C CG2 . THR A  1 155 ? 6.759   68.751 23.675  1.00 70.33  ? 155 THR A CG2 1 
ATOM   1127  N N   . ASN A  1 156 ? 4.024   66.402 26.707  1.00 66.55  ? 156 ASN A N   1 
ATOM   1128  C CA  . ASN A  1 156 ? 3.130   66.201 27.881  1.00 67.48  ? 156 ASN A CA  1 
ATOM   1129  C C   . ASN A  1 156 ? 3.734   65.135 28.805  1.00 64.15  ? 156 ASN A C   1 
ATOM   1130  O O   . ASN A  1 156 ? 3.692   63.944 28.438  1.00 69.03  ? 156 ASN A O   1 
ATOM   1131  C CB  . ASN A  1 156 ? 1.713   65.818 27.449  1.00 68.22  ? 156 ASN A CB  1 
ATOM   1132  C CG  . ASN A  1 156 ? 0.790   65.549 28.618  1.00 72.32  ? 156 ASN A CG  1 
ATOM   1133  O OD1 . ASN A  1 156 ? 1.240   65.183 29.702  1.00 82.56  ? 156 ASN A OD1 1 
ATOM   1134  N ND2 . ASN A  1 156 ? -0.505  65.721 28.408  1.00 73.84  ? 156 ASN A ND2 1 
ATOM   1135  N N   . THR A  1 157 ? 4.261   65.554 29.962  1.00 59.73  ? 157 THR A N   1 
ATOM   1136  C CA  . THR A  1 157 ? 4.950   64.684 30.955  1.00 55.62  ? 157 THR A CA  1 
ATOM   1137  C C   . THR A  1 157 ? 3.947   63.712 31.589  1.00 54.66  ? 157 THR A C   1 
ATOM   1138  O O   . THR A  1 157 ? 4.369   62.602 31.976  1.00 51.71  ? 157 THR A O   1 
ATOM   1139  C CB  . THR A  1 157 ? 5.660   65.516 32.031  1.00 54.18  ? 157 THR A CB  1 
ATOM   1140  O OG1 . THR A  1 157 ? 6.372   66.575 31.389  1.00 59.50  ? 157 THR A OG1 1 
ATOM   1141  C CG2 . THR A  1 157 ? 6.614   64.693 32.868  1.00 53.14  ? 157 THR A CG2 1 
ATOM   1142  N N   . GLY A  1 158 ? 2.678   64.118 31.701  1.00 54.49  ? 158 GLY A N   1 
ATOM   1143  C CA  . GLY A  1 158 ? 1.587   63.273 32.223  1.00 51.66  ? 158 GLY A CA  1 
ATOM   1144  C C   . GLY A  1 158 ? 1.422   62.012 31.392  1.00 54.26  ? 158 GLY A C   1 
ATOM   1145  O O   . GLY A  1 158 ? 1.675   60.914 31.924  1.00 53.32  ? 158 GLY A O   1 
ATOM   1146  N N   . ALA A  1 159 ? 1.027   62.172 30.125  1.00 61.39  ? 159 ALA A N   1 
ATOM   1147  C CA  . ALA A  1 159 ? 0.812   61.085 29.141  1.00 59.11  ? 159 ALA A CA  1 
ATOM   1148  C C   . ALA A  1 159 ? 2.094   60.256 28.990  1.00 55.35  ? 159 ALA A C   1 
ATOM   1149  O O   . ALA A  1 159 ? 1.998   59.011 28.987  1.00 44.91  ? 159 ALA A O   1 
ATOM   1150  C CB  . ALA A  1 159 ? 0.376   61.674 27.823  1.00 56.20  ? 159 ALA A CB  1 
ATOM   1151  N N   . PHE A  1 160 ? 3.243   60.929 28.868  1.00 57.39  ? 160 PHE A N   1 
ATOM   1152  C CA  . PHE A  1 160 ? 4.589   60.313 28.722  1.00 61.30  ? 160 PHE A CA  1 
ATOM   1153  C C   . PHE A  1 160 ? 4.760   59.205 29.766  1.00 67.14  ? 160 PHE A C   1 
ATOM   1154  O O   . PHE A  1 160 ? 5.164   58.084 29.395  1.00 73.16  ? 160 PHE A O   1 
ATOM   1155  C CB  . PHE A  1 160 ? 5.682   61.374 28.870  1.00 64.53  ? 160 PHE A CB  1 
ATOM   1156  C CG  . PHE A  1 160 ? 7.079   60.893 28.567  1.00 67.57  ? 160 PHE A CG  1 
ATOM   1157  C CD1 . PHE A  1 160 ? 7.928   60.481 29.583  1.00 67.48  ? 160 PHE A CD1 1 
ATOM   1158  C CD2 . PHE A  1 160 ? 7.551   60.862 27.264  1.00 72.68  ? 160 PHE A CD2 1 
ATOM   1159  C CE1 . PHE A  1 160 ? 9.213   60.046 29.301  1.00 69.79  ? 160 PHE A CE1 1 
ATOM   1160  C CE2 . PHE A  1 160 ? 8.839   60.429 26.985  1.00 73.46  ? 160 PHE A CE2 1 
ATOM   1161  C CZ  . PHE A  1 160 ? 9.667   60.021 28.003  1.00 72.06  ? 160 PHE A CZ  1 
ATOM   1162  N N   . ILE A  1 161 ? 4.460   59.519 31.031  1.00 70.47  ? 161 ILE A N   1 
ATOM   1163  C CA  . ILE A  1 161 ? 4.633   58.598 32.195  1.00 67.93  ? 161 ILE A CA  1 
ATOM   1164  C C   . ILE A  1 161 ? 3.434   57.645 32.264  1.00 65.04  ? 161 ILE A C   1 
ATOM   1165  O O   . ILE A  1 161 ? 3.655   56.438 32.480  1.00 68.17  ? 161 ILE A O   1 
ATOM   1166  C CB  . ILE A  1 161 ? 4.824   59.390 33.503  1.00 66.76  ? 161 ILE A CB  1 
ATOM   1167  C CG1 . ILE A  1 161 ? 6.110   60.221 33.471  1.00 68.78  ? 161 ILE A CG1 1 
ATOM   1168  C CG2 . ILE A  1 161 ? 4.781   58.460 34.705  1.00 68.44  ? 161 ILE A CG2 1 
ATOM   1169  C CD1 . ILE A  1 161 ? 6.532   60.764 34.817  1.00 67.63  ? 161 ILE A CD1 1 
ATOM   1170  N N   . LEU A  1 162 ? 2.217   58.167 32.087  1.00 60.30  ? 162 LEU A N   1 
ATOM   1171  C CA  . LEU A  1 162 ? 0.958   57.374 32.114  1.00 58.94  ? 162 LEU A CA  1 
ATOM   1172  C C   . LEU A  1 162 ? 1.116   56.145 31.210  1.00 58.33  ? 162 LEU A C   1 
ATOM   1173  O O   . LEU A  1 162 ? 1.091   55.016 31.737  1.00 59.76  ? 162 LEU A O   1 
ATOM   1174  C CB  . LEU A  1 162 ? -0.205  58.252 31.643  1.00 61.98  ? 162 LEU A CB  1 
ATOM   1175  C CG  . LEU A  1 162 ? -1.606  57.742 31.983  1.00 60.37  ? 162 LEU A CG  1 
ATOM   1176  C CD1 . LEU A  1 162 ? -2.645  58.361 31.060  1.00 59.42  ? 162 LEU A CD1 1 
ATOM   1177  C CD2 . LEU A  1 162 ? -1.671  56.224 31.914  1.00 55.51  ? 162 LEU A CD2 1 
ATOM   1178  N N   . TRP A  1 163 ? 1.285   56.369 29.903  1.00 58.61  ? 163 TRP A N   1 
ATOM   1179  C CA  . TRP A  1 163 ? 1.245   55.319 28.850  1.00 62.06  ? 163 TRP A CA  1 
ATOM   1180  C C   . TRP A  1 163 ? 2.461   54.390 28.969  1.00 60.87  ? 163 TRP A C   1 
ATOM   1181  O O   . TRP A  1 163 ? 2.331   53.206 28.599  1.00 66.73  ? 163 TRP A O   1 
ATOM   1182  C CB  . TRP A  1 163 ? 1.131   55.956 27.461  1.00 60.30  ? 163 TRP A CB  1 
ATOM   1183  C CG  . TRP A  1 163 ? -0.227  56.530 27.194  1.00 62.36  ? 163 TRP A CG  1 
ATOM   1184  C CD1 . TRP A  1 163 ? -0.609  57.835 27.320  1.00 66.68  ? 163 TRP A CD1 1 
ATOM   1185  C CD2 . TRP A  1 163 ? -1.402  55.809 26.780  1.00 62.36  ? 163 TRP A CD2 1 
ATOM   1186  N NE1 . TRP A  1 163 ? -1.934  57.976 27.002  1.00 70.99  ? 163 TRP A NE1 1 
ATOM   1187  C CE2 . TRP A  1 163 ? -2.447  56.751 26.667  1.00 61.28  ? 163 TRP A CE2 1 
ATOM   1188  C CE3 . TRP A  1 163 ? -1.672  54.468 26.488  1.00 63.27  ? 163 TRP A CE3 1 
ATOM   1189  C CZ2 . TRP A  1 163 ? -3.736  56.393 26.272  1.00 55.83  ? 163 TRP A CZ2 1 
ATOM   1190  C CZ3 . TRP A  1 163 ? -2.946  54.115 26.100  1.00 65.45  ? 163 TRP A CZ3 1 
ATOM   1191  C CH2 . TRP A  1 163 ? -3.961  55.066 25.992  1.00 61.09  ? 163 TRP A CH2 1 
ATOM   1192  N N   . ALA A  1 164 ? 3.588   54.900 29.472  1.00 55.54  ? 164 ALA A N   1 
ATOM   1193  C CA  . ALA A  1 164 ? 4.792   54.099 29.801  1.00 62.26  ? 164 ALA A CA  1 
ATOM   1194  C C   . ALA A  1 164 ? 4.405   53.012 30.812  1.00 67.24  ? 164 ALA A C   1 
ATOM   1195  O O   . ALA A  1 164 ? 4.928   51.882 30.706  1.00 63.52  ? 164 ALA A O   1 
ATOM   1196  C CB  . ALA A  1 164 ? 5.887   54.991 30.337  1.00 62.88  ? 164 ALA A CB  1 
ATOM   1197  N N   . VAL A  1 165 ? 3.514   53.351 31.751  1.00 74.19  ? 165 VAL A N   1 
ATOM   1198  C CA  . VAL A  1 165 ? 3.003   52.437 32.815  1.00 70.28  ? 165 VAL A CA  1 
ATOM   1199  C C   . VAL A  1 165 ? 2.046   51.430 32.172  1.00 63.30  ? 165 VAL A C   1 
ATOM   1200  O O   . VAL A  1 165 ? 2.253   50.217 32.363  1.00 58.43  ? 165 VAL A O   1 
ATOM   1201  C CB  . VAL A  1 165 ? 2.322   53.219 33.954  1.00 70.06  ? 165 VAL A CB  1 
ATOM   1202  C CG1 . VAL A  1 165 ? 1.514   52.309 34.869  1.00 70.22  ? 165 VAL A CG1 1 
ATOM   1203  C CG2 . VAL A  1 165 ? 3.331   54.029 34.754  1.00 68.60  ? 165 VAL A CG2 1 
ATOM   1204  N N   . ILE A  1 166 ? 1.041   51.923 31.441  1.00 56.22  ? 166 ILE A N   1 
ATOM   1205  C CA  . ILE A  1 166 ? 0.090   51.081 30.656  1.00 60.90  ? 166 ILE A CA  1 
ATOM   1206  C C   . ILE A  1 166 ? 0.913   50.089 29.830  1.00 66.25  ? 166 ILE A C   1 
ATOM   1207  O O   . ILE A  1 166 ? 0.563   48.892 29.818  1.00 77.74  ? 166 ILE A O   1 
ATOM   1208  C CB  . ILE A  1 166 ? -0.823  51.947 29.766  1.00 58.14  ? 166 ILE A CB  1 
ATOM   1209  C CG1 . ILE A  1 166 ? -1.663  52.919 30.598  1.00 57.68  ? 166 ILE A CG1 1 
ATOM   1210  C CG2 . ILE A  1 166 ? -1.690  51.072 28.871  1.00 55.58  ? 166 ILE A CG2 1 
ATOM   1211  C CD1 . ILE A  1 166 ? -2.676  53.703 29.796  1.00 58.73  ? 166 ILE A CD1 1 
ATOM   1212  N N   . SER A  1 167 ? 1.967   50.580 29.171  1.00 62.52  ? 167 SER A N   1 
ATOM   1213  C CA  . SER A  1 167 ? 2.938   49.769 28.393  1.00 67.18  ? 167 SER A CA  1 
ATOM   1214  C C   . SER A  1 167 ? 3.486   48.640 29.276  1.00 65.85  ? 167 SER A C   1 
ATOM   1215  O O   . SER A  1 167 ? 3.357   47.463 28.882  1.00 62.01  ? 167 SER A O   1 
ATOM   1216  C CB  . SER A  1 167 ? 4.045   50.637 27.844  1.00 67.95  ? 167 SER A CB  1 
ATOM   1217  O OG  . SER A  1 167 ? 5.040   49.855 27.197  1.00 65.11  ? 167 SER A OG  1 
ATOM   1218  N N   . CYS A  1 168 ? 4.059   48.991 30.432  1.00 64.88  ? 168 CYS A N   1 
ATOM   1219  C CA  . CYS A  1 168 ? 4.711   48.049 31.383  1.00 62.55  ? 168 CYS A CA  1 
ATOM   1220  C C   . CYS A  1 168 ? 3.727   46.952 31.803  1.00 62.92  ? 168 CYS A C   1 
ATOM   1221  O O   . CYS A  1 168 ? 4.178   45.813 32.028  1.00 68.62  ? 168 CYS A O   1 
ATOM   1222  C CB  . CYS A  1 168 ? 5.237   48.779 32.610  1.00 62.40  ? 168 CYS A CB  1 
ATOM   1223  S SG  . CYS A  1 168 ? 6.703   49.781 32.257  1.00 77.51  ? 168 CYS A SG  1 
ATOM   1224  N N   . VAL A  1 169 ? 2.439   47.287 31.917  1.00 59.57  ? 169 VAL A N   1 
ATOM   1225  C CA  . VAL A  1 169 ? 1.351   46.304 32.197  1.00 61.32  ? 169 VAL A CA  1 
ATOM   1226  C C   . VAL A  1 169 ? 1.453   45.188 31.153  1.00 64.91  ? 169 VAL A C   1 
ATOM   1227  O O   . VAL A  1 169 ? 1.689   44.029 31.549  1.00 70.44  ? 169 VAL A O   1 
ATOM   1228  C CB  . VAL A  1 169 ? -0.040  46.967 32.180  1.00 65.28  ? 169 VAL A CB  1 
ATOM   1229  C CG1 . VAL A  1 169 ? -1.156  45.936 32.107  1.00 61.56  ? 169 VAL A CG1 1 
ATOM   1230  C CG2 . VAL A  1 169 ? -0.238  47.890 33.371  1.00 61.62  ? 169 VAL A CG2 1 
ATOM   1231  N N   . PHE A  1 170 ? 1.299   45.541 29.873  1.00 65.91  ? 170 PHE A N   1 
ATOM   1232  C CA  . PHE A  1 170 ? 1.399   44.619 28.711  1.00 61.42  ? 170 PHE A CA  1 
ATOM   1233  C C   . PHE A  1 170 ? 2.742   43.881 28.764  1.00 62.27  ? 170 PHE A C   1 
ATOM   1234  O O   . PHE A  1 170 ? 2.760   42.658 28.521  1.00 69.55  ? 170 PHE A O   1 
ATOM   1235  C CB  . PHE A  1 170 ? 1.233   45.384 27.395  1.00 58.88  ? 170 PHE A CB  1 
ATOM   1236  C CG  . PHE A  1 170 ? -0.163  45.892 27.133  1.00 59.75  ? 170 PHE A CG  1 
ATOM   1237  C CD1 . PHE A  1 170 ? -1.201  45.012 26.873  1.00 61.23  ? 170 PHE A CD1 1 
ATOM   1238  C CD2 . PHE A  1 170 ? -0.436  47.251 27.134  1.00 58.43  ? 170 PHE A CD2 1 
ATOM   1239  C CE1 . PHE A  1 170 ? -2.483  45.478 26.627  1.00 59.45  ? 170 PHE A CE1 1 
ATOM   1240  C CE2 . PHE A  1 170 ? -1.719  47.715 26.890  1.00 61.56  ? 170 PHE A CE2 1 
ATOM   1241  C CZ  . PHE A  1 170 ? -2.740  46.829 26.637  1.00 62.78  ? 170 PHE A CZ  1 
ATOM   1242  N N   . TRP A  1 171 ? 3.824   44.601 29.081  1.00 59.85  ? 171 TRP A N   1 
ATOM   1243  C CA  . TRP A  1 171 ? 5.201   44.046 29.193  1.00 63.24  ? 171 TRP A CA  1 
ATOM   1244  C C   . TRP A  1 171 ? 5.183   42.816 30.108  1.00 68.04  ? 171 TRP A C   1 
ATOM   1245  O O   . TRP A  1 171 ? 5.661   41.749 29.674  1.00 63.94  ? 171 TRP A O   1 
ATOM   1246  C CB  . TRP A  1 171 ? 6.186   45.108 29.698  1.00 63.99  ? 171 TRP A CB  1 
ATOM   1247  C CG  . TRP A  1 171 ? 7.609   44.639 29.751  1.00 65.05  ? 171 TRP A CG  1 
ATOM   1248  C CD1 . TRP A  1 171 ? 8.205   43.727 28.928  1.00 69.22  ? 171 TRP A CD1 1 
ATOM   1249  C CD2 . TRP A  1 171 ? 8.633   45.081 30.661  1.00 70.64  ? 171 TRP A CD2 1 
ATOM   1250  N NE1 . TRP A  1 171 ? 9.521   43.563 29.270  1.00 74.31  ? 171 TRP A NE1 1 
ATOM   1251  C CE2 . TRP A  1 171 ? 9.813   44.380 30.329  1.00 73.86  ? 171 TRP A CE2 1 
ATOM   1252  C CE3 . TRP A  1 171 ? 8.670   45.995 31.721  1.00 70.89  ? 171 TRP A CE3 1 
ATOM   1253  C CZ2 . TRP A  1 171 ? 11.010  44.567 31.020  1.00 74.79  ? 171 TRP A CZ2 1 
ATOM   1254  C CZ3 . TRP A  1 171 ? 9.853   46.178 32.403  1.00 71.57  ? 171 TRP A CZ3 1 
ATOM   1255  C CH2 . TRP A  1 171 ? 11.006  45.472 32.056  1.00 72.59  ? 171 TRP A CH2 1 
ATOM   1256  N N   . VAL A  1 172 ? 4.644   42.969 31.321  1.00 70.43  ? 172 VAL A N   1 
ATOM   1257  C CA  . VAL A  1 172 ? 4.569   41.895 32.356  1.00 67.43  ? 172 VAL A CA  1 
ATOM   1258  C C   . VAL A  1 172 ? 3.753   40.726 31.794  1.00 61.73  ? 172 VAL A C   1 
ATOM   1259  O O   . VAL A  1 172 ? 4.257   39.583 31.829  1.00 63.05  ? 172 VAL A O   1 
ATOM   1260  C CB  . VAL A  1 172 ? 3.967   42.418 33.675  1.00 63.93  ? 172 VAL A CB  1 
ATOM   1261  C CG1 . VAL A  1 172 ? 3.717   41.289 34.662  1.00 65.33  ? 172 VAL A CG1 1 
ATOM   1262  C CG2 . VAL A  1 172 ? 4.838   43.496 34.302  1.00 61.94  ? 172 VAL A CG2 1 
ATOM   1263  N N   . ILE A  1 173 ? 2.546   41.006 31.293  1.00 54.60  ? 173 ILE A N   1 
ATOM   1264  C CA  . ILE A  1 173 ? 1.633   39.991 30.686  1.00 58.52  ? 173 ILE A CA  1 
ATOM   1265  C C   . ILE A  1 173 ? 2.456   39.097 29.752  1.00 63.65  ? 173 ILE A C   1 
ATOM   1266  O O   . ILE A  1 173 ? 2.332   37.860 29.853  1.00 71.06  ? 173 ILE A O   1 
ATOM   1267  C CB  . ILE A  1 173 ? 0.462   40.664 29.945  1.00 55.85  ? 173 ILE A CB  1 
ATOM   1268  C CG1 . ILE A  1 173 ? -0.382  41.530 30.884  1.00 57.47  ? 173 ILE A CG1 1 
ATOM   1269  C CG2 . ILE A  1 173 ? -0.383  39.624 29.224  1.00 51.20  ? 173 ILE A CG2 1 
ATOM   1270  C CD1 . ILE A  1 173 ? -1.508  42.269 30.197  1.00 60.67  ? 173 ILE A CD1 1 
ATOM   1271  N N   . ALA A  1 174 ? 3.265   39.712 28.883  1.00 65.00  ? 174 ALA A N   1 
ATOM   1272  C CA  . ALA A  1 174 ? 4.141   39.028 27.903  1.00 65.64  ? 174 ALA A CA  1 
ATOM   1273  C C   . ALA A  1 174 ? 5.144   38.141 28.646  1.00 68.89  ? 174 ALA A C   1 
ATOM   1274  O O   . ALA A  1 174 ? 5.130   36.917 28.417  1.00 75.88  ? 174 ALA A O   1 
ATOM   1275  C CB  . ALA A  1 174 ? 4.843   40.046 27.038  1.00 68.92  ? 174 ALA A CB  1 
ATOM   1276  N N   . ASN A  1 175 ? 5.975   38.744 29.501  1.00 65.99  ? 175 ASN A N   1 
ATOM   1277  C CA  . ASN A  1 175 ? 7.020   38.043 30.294  1.00 65.71  ? 175 ASN A CA  1 
ATOM   1278  C C   . ASN A  1 175 ? 6.410   36.797 30.942  1.00 71.09  ? 175 ASN A C   1 
ATOM   1279  O O   . ASN A  1 175 ? 7.005   35.711 30.806  1.00 83.91  ? 175 ASN A O   1 
ATOM   1280  C CB  . ASN A  1 175 ? 7.648   38.960 31.344  1.00 62.37  ? 175 ASN A CB  1 
ATOM   1281  C CG  . ASN A  1 175 ? 8.647   39.930 30.751  1.00 64.97  ? 175 ASN A CG  1 
ATOM   1282  O OD1 . ASN A  1 175 ? 8.366   41.120 30.636  1.00 66.57  ? 175 ASN A OD1 1 
ATOM   1283  N ND2 . ASN A  1 175 ? 9.809   39.430 30.358  1.00 66.26  ? 175 ASN A ND2 1 
ATOM   1284  N N   . VAL A  1 176 ? 5.267   36.954 31.615  1.00 68.35  ? 176 VAL A N   1 
ATOM   1285  C CA  . VAL A  1 176 ? 4.522   35.847 32.286  1.00 70.42  ? 176 VAL A CA  1 
ATOM   1286  C C   . VAL A  1 176 ? 4.268   34.732 31.262  1.00 70.82  ? 176 VAL A C   1 
ATOM   1287  O O   . VAL A  1 176 ? 4.838   33.636 31.432  1.00 74.64  ? 176 VAL A O   1 
ATOM   1288  C CB  . VAL A  1 176 ? 3.209   36.357 32.911  1.00 64.88  ? 176 VAL A CB  1 
ATOM   1289  C CG1 . VAL A  1 176 ? 2.252   35.219 33.239  1.00 61.63  ? 176 VAL A CG1 1 
ATOM   1290  C CG2 . VAL A  1 176 ? 3.476   37.213 34.140  1.00 57.24  ? 176 VAL A CG2 1 
ATOM   1291  N N   . VAL A  1 177 ? 3.456   35.017 30.239  1.00 66.61  ? 177 VAL A N   1 
ATOM   1292  C CA  . VAL A  1 177 ? 3.038   34.050 29.179  1.00 66.35  ? 177 VAL A CA  1 
ATOM   1293  C C   . VAL A  1 177 ? 4.267   33.274 28.688  1.00 66.79  ? 177 VAL A C   1 
ATOM   1294  O O   . VAL A  1 177 ? 4.193   32.030 28.626  1.00 73.03  ? 177 VAL A O   1 
ATOM   1295  C CB  . VAL A  1 177 ? 2.330   34.769 28.015  1.00 67.37  ? 177 VAL A CB  1 
ATOM   1296  C CG1 . VAL A  1 177 ? 2.059   33.829 26.851  1.00 66.99  ? 177 VAL A CG1 1 
ATOM   1297  C CG2 . VAL A  1 177 ? 1.045   35.450 28.465  1.00 63.70  ? 177 VAL A CG2 1 
ATOM   1298  N N   . LEU A  1 178 ? 5.347   33.984 28.348  1.00 66.99  ? 178 LEU A N   1 
ATOM   1299  C CA  . LEU A  1 178 ? 6.594   33.403 27.779  1.00 70.94  ? 178 LEU A CA  1 
ATOM   1300  C C   . LEU A  1 178 ? 7.285   32.530 28.835  1.00 69.97  ? 178 LEU A C   1 
ATOM   1301  O O   . LEU A  1 178 ? 7.568   31.352 28.539  1.00 69.25  ? 178 LEU A O   1 
ATOM   1302  C CB  . LEU A  1 178 ? 7.511   34.537 27.310  1.00 73.60  ? 178 LEU A CB  1 
ATOM   1303  C CG  . LEU A  1 178 ? 7.037   35.306 26.076  1.00 79.03  ? 178 LEU A CG  1 
ATOM   1304  C CD1 . LEU A  1 178 ? 7.973   36.465 25.764  1.00 82.78  ? 178 LEU A CD1 1 
ATOM   1305  C CD2 . LEU A  1 178 ? 6.910   34.385 24.871  1.00 81.73  ? 178 LEU A CD2 1 
ATOM   1306  N N   . ILE A  1 179 ? 7.544   33.094 30.019  1.00 74.45  ? 179 ILE A N   1 
ATOM   1307  C CA  . ILE A  1 179 ? 8.242   32.410 31.149  1.00 76.13  ? 179 ILE A CA  1 
ATOM   1308  C C   . ILE A  1 179 ? 7.492   31.117 31.488  1.00 74.29  ? 179 ILE A C   1 
ATOM   1309  O O   . ILE A  1 179 ? 8.153   30.062 31.603  1.00 74.78  ? 179 ILE A O   1 
ATOM   1310  C CB  . ILE A  1 179 ? 8.360   33.349 32.367  1.00 78.01  ? 179 ILE A CB  1 
ATOM   1311  C CG1 . ILE A  1 179 ? 9.383   34.462 32.118  1.00 80.07  ? 179 ILE A CG1 1 
ATOM   1312  C CG2 . ILE A  1 179 ? 8.681   32.562 33.628  1.00 77.36  ? 179 ILE A CG2 1 
ATOM   1313  C CD1 . ILE A  1 179 ? 9.329   35.584 33.129  1.00 80.78  ? 179 ILE A CD1 1 
ATOM   1314  N N   . ARG A  1 180 ? 6.166   31.200 31.640  1.00 73.83  ? 180 ARG A N   1 
ATOM   1315  C CA  . ARG A  1 180 ? 5.285   30.035 31.920  1.00 72.93  ? 180 ARG A CA  1 
ATOM   1316  C C   . ARG A  1 180 ? 5.524   28.963 30.849  1.00 78.28  ? 180 ARG A C   1 
ATOM   1317  O O   . ARG A  1 180 ? 5.875   27.826 31.222  1.00 81.47  ? 180 ARG A O   1 
ATOM   1318  C CB  . ARG A  1 180 ? 3.815   30.466 31.958  1.00 67.96  ? 180 ARG A CB  1 
ATOM   1319  C CG  . ARG A  1 180 ? 2.845   29.348 32.311  1.00 71.11  ? 180 ARG A CG  1 
ATOM   1320  C CD  . ARG A  1 180 ? 1.405   29.824 32.357  1.00 66.67  ? 180 ARG A CD  1 
ATOM   1321  N NE  . ARG A  1 180 ? 1.246   31.011 33.183  1.00 62.73  ? 180 ARG A NE  1 
ATOM   1322  N N   . ALA A  1 181 ? 5.358   29.333 29.574  1.00 77.06  ? 181 ALA A N   1 
ATOM   1323  C CA  . ALA A  1 181 ? 5.461   28.442 28.394  1.00 77.28  ? 181 ALA A CA  1 
ATOM   1324  C C   . ALA A  1 181 ? 6.836   27.765 28.355  1.00 71.73  ? 181 ALA A C   1 
ATOM   1325  O O   . ALA A  1 181 ? 6.903   26.593 27.933  1.00 82.12  ? 181 ALA A O   1 
ATOM   1326  C CB  . ALA A  1 181 ? 5.207   29.231 27.132  1.00 81.88  ? 181 ALA A CB  1 
ATOM   1327  N N   . VAL A  1 182 ? 7.889   28.480 28.764  1.00 65.94  ? 182 VAL A N   1 
ATOM   1328  C CA  . VAL A  1 182 ? 9.294   27.973 28.781  1.00 81.51  ? 182 VAL A CA  1 
ATOM   1329  C C   . VAL A  1 182 ? 9.446   26.980 29.939  1.00 90.83  ? 182 VAL A C   1 
ATOM   1330  O O   . VAL A  1 182 ? 9.936   25.850 29.703  1.00 101.62 ? 182 VAL A O   1 
ATOM   1331  C CB  . VAL A  1 182 ? 10.312  29.124 28.900  1.00 86.29  ? 182 VAL A CB  1 
ATOM   1332  C CG1 . VAL A  1 182 ? 11.728  28.605 29.096  1.00 80.10  ? 182 VAL A CG1 1 
ATOM   1333  C CG2 . VAL A  1 182 ? 10.246  30.064 27.705  1.00 94.73  ? 182 VAL A CG2 1 
ATOM   1334  N N   . ARG A  1 183 ? 9.036   27.391 31.142  1.00 93.53  ? 183 ARG A N   1 
ATOM   1335  C CA  . ARG A  1 183 ? 9.163   26.594 32.391  1.00 92.37  ? 183 ARG A CA  1 
ATOM   1336  C C   . ARG A  1 183 ? 8.430   25.255 32.225  1.00 89.76  ? 183 ARG A C   1 
ATOM   1337  O O   . ARG A  1 183 ? 8.853   24.267 32.858  1.00 105.21 ? 183 ARG A O   1 
ATOM   1338  C CB  . ARG A  1 183 ? 8.631   27.394 33.583  1.00 96.89  ? 183 ARG A CB  1 
ATOM   1339  C CG  . ARG A  1 183 ? 9.049   26.832 34.934  1.00 103.24 ? 183 ARG A CG  1 
ATOM   1340  C CD  . ARG A  1 183 ? 9.655   27.894 35.830  1.00 104.17 ? 183 ARG A CD  1 
ATOM   1341  N NE  . ARG A  1 183 ? 8.725   28.977 36.111  1.00 106.98 ? 183 ARG A NE  1 
ATOM   1342  C CZ  . ARG A  1 183 ? 9.050   30.106 36.732  1.00 106.41 ? 183 ARG A CZ  1 
ATOM   1343  N NH1 . ARG A  1 183 ? 10.292  30.307 37.137  1.00 102.96 ? 183 ARG A NH1 1 
ATOM   1344  N NH2 . ARG A  1 183 ? 8.131   31.032 36.945  1.00 107.51 ? 183 ARG A NH2 1 
ATOM   1345  N N   . GLN A  1 184 ? 7.377   25.227 31.404  1.00 79.82  ? 184 GLN A N   1 
ATOM   1346  C CA  . GLN A  1 184 ? 6.544   24.020 31.148  1.00 80.64  ? 184 GLN A CA  1 
ATOM   1347  C C   . GLN A  1 184 ? 7.272   23.082 30.181  1.00 85.70  ? 184 GLN A C   1 
ATOM   1348  O O   . GLN A  1 184 ? 7.115   21.854 30.329  1.00 86.37  ? 184 GLN A O   1 
ATOM   1349  C CB  . GLN A  1 184 ? 5.180   24.421 30.588  1.00 85.41  ? 184 GLN A CB  1 
ATOM   1350  C CG  . GLN A  1 184 ? 4.320   25.174 31.592  1.00 96.71  ? 184 GLN A CG  1 
ATOM   1351  C CD  . GLN A  1 184 ? 3.000   25.604 31.005  1.00 107.28 ? 184 GLN A CD  1 
ATOM   1352  O OE1 . GLN A  1 184 ? 2.646   25.236 29.887  1.00 124.73 ? 184 GLN A OE1 1 
ATOM   1353  N NE2 . GLN A  1 184 ? 2.258   26.394 31.764  1.00 109.50 ? 184 GLN A NE2 1 
ATOM   1354  N N   . SER A  1 185 ? 8.029   23.639 29.231  1.00 97.97  ? 185 SER A N   1 
ATOM   1355  C CA  . SER A  1 185 ? 8.756   22.890 28.171  1.00 98.99  ? 185 SER A CA  1 
ATOM   1356  C C   . SER A  1 185 ? 9.977   22.179 28.769  1.00 101.62 ? 185 SER A C   1 
ATOM   1357  O O   . SER A  1 185 ? 10.184  20.989 28.453  1.00 115.63 ? 185 SER A O   1 
ATOM   1358  C CB  . SER A  1 185 ? 9.159   23.805 27.041  1.00 93.51  ? 185 SER A CB  1 
ATOM   1359  O OG  . SER A  1 185 ? 8.018   24.349 26.392  1.00 98.52  ? 185 SER A OG  1 
ATOM   1360  N N   . LEU A  1 186 ? 10.738  22.886 29.611  1.00 102.10 ? 186 LEU A N   1 
ATOM   1361  C CA  . LEU A  1 186 ? 12.061  22.451 30.139  1.00 115.03 ? 186 LEU A CA  1 
ATOM   1362  C C   . LEU A  1 186 ? 11.977  21.033 30.705  1.00 120.14 ? 186 LEU A C   1 
ATOM   1363  O O   . LEU A  1 186 ? 12.884  20.230 30.492  1.00 113.55 ? 186 LEU A O   1 
ATOM   1364  C CB  . LEU A  1 186 ? 12.530  23.456 31.197  1.00 119.87 ? 186 LEU A CB  1 
ATOM   1365  C CG  . LEU A  1 186 ? 12.907  24.839 30.662  1.00 124.06 ? 186 LEU A CG  1 
ATOM   1366  C CD1 . LEU A  1 186 ? 13.370  25.751 31.786  1.00 121.15 ? 186 LEU A CD1 1 
ATOM   1367  C CD2 . LEU A  1 186 ? 13.983  24.737 29.591  1.00 129.15 ? 186 LEU A CD2 1 
ATOM   1368  N N   . PRO A  1 187 ? 10.905  20.679 31.452  1.00 122.92 ? 187 PRO A N   1 
ATOM   1369  C CA  . PRO A  1 187 ? 10.740  19.318 31.969  1.00 110.82 ? 187 PRO A CA  1 
ATOM   1370  C C   . PRO A  1 187 ? 10.739  18.231 30.882  1.00 100.68 ? 187 PRO A C   1 
ATOM   1371  O O   . PRO A  1 187 ? 11.385  17.218 31.078  1.00 93.38  ? 187 PRO A O   1 
ATOM   1372  C CB  . PRO A  1 187 ? 9.368   19.356 32.663  1.00 111.08 ? 187 PRO A CB  1 
ATOM   1373  C CG  . PRO A  1 187 ? 9.165   20.816 33.013  1.00 111.05 ? 187 PRO A CG  1 
ATOM   1374  C CD  . PRO A  1 187 ? 9.822   21.577 31.880  1.00 123.65 ? 187 PRO A CD  1 
ATOM   1375  N N   . THR A  1 188 ? 10.021  18.466 29.776  1.00 103.27 ? 188 THR A N   1 
ATOM   1376  C CA  . THR A  1 188 ? 9.760   17.470 28.700  1.00 99.09  ? 188 THR A CA  1 
ATOM   1377  C C   . THR A  1 188 ? 10.963  17.382 27.751  1.00 89.80  ? 188 THR A C   1 
ATOM   1378  O O   . THR A  1 188 ? 10.997  16.434 26.943  1.00 83.98  ? 188 THR A O   1 
ATOM   1379  C CB  . THR A  1 188 ? 8.481   17.804 27.918  1.00 102.20 ? 188 THR A CB  1 
ATOM   1380  O OG1 . THR A  1 188 ? 8.725   18.960 27.116  1.00 103.45 ? 188 THR A OG1 1 
ATOM   1381  C CG2 . THR A  1 188 ? 7.284   18.055 28.810  1.00 98.16  ? 188 THR A CG2 1 
ATOM   1382  N N   . LEU A  1 189 ? 11.903  18.329 27.841  1.00 92.70  ? 189 LEU A N   1 
ATOM   1383  C CA  . LEU A  1 189 ? 13.098  18.408 26.956  1.00 101.85 ? 189 LEU A CA  1 
ATOM   1384  C C   . LEU A  1 189 ? 14.249  17.604 27.569  1.00 92.60  ? 189 LEU A C   1 
ATOM   1385  O O   . LEU A  1 189 ? 14.143  17.232 28.755  1.00 89.83  ? 189 LEU A O   1 
ATOM   1386  C CB  . LEU A  1 189 ? 13.502  19.875 26.772  1.00 111.17 ? 189 LEU A CB  1 
ATOM   1387  C CG  . LEU A  1 189 ? 12.480  20.755 26.053  1.00 116.77 ? 189 LEU A CG  1 
ATOM   1388  C CD1 . LEU A  1 189 ? 13.031  22.157 25.831  1.00 116.81 ? 189 LEU A CD1 1 
ATOM   1389  C CD2 . LEU A  1 189 ? 12.064  20.131 24.731  1.00 118.51 ? 189 LEU A CD2 1 
ATOM   1390  N N   . THR A  1 190 ? 15.302  17.361 26.781  1.00 91.54  ? 190 THR A N   1 
ATOM   1391  C CA  . THR A  1 190 ? 16.568  16.717 27.220  1.00 93.67  ? 190 THR A CA  1 
ATOM   1392  C C   . THR A  1 190 ? 17.381  17.724 28.030  1.00 90.62  ? 190 THR A C   1 
ATOM   1393  O O   . THR A  1 190 ? 17.035  18.903 28.088  1.00 77.76  ? 190 THR A O   1 
ATOM   1394  C CB  . THR A  1 190 ? 17.376  16.194 26.025  1.00 100.76 ? 190 THR A CB  1 
ATOM   1395  O OG1 . THR A  1 190 ? 18.028  17.301 25.402  1.00 101.95 ? 190 THR A OG1 1 
ATOM   1396  C CG2 . THR A  1 190 ? 16.526  15.466 25.007  1.00 105.81 ? 190 THR A CG2 1 
ATOM   1397  N N   . PRO A  1 191 ? 18.479  17.286 28.685  1.00 98.09  ? 191 PRO A N   1 
ATOM   1398  C CA  . PRO A  1 191 ? 19.356  18.194 29.427  1.00 96.59  ? 191 PRO A CA  1 
ATOM   1399  C C   . PRO A  1 191 ? 19.975  19.282 28.537  1.00 91.22  ? 191 PRO A C   1 
ATOM   1400  O O   . PRO A  1 191 ? 19.986  20.434 28.936  1.00 90.88  ? 191 PRO A O   1 
ATOM   1401  C CB  . PRO A  1 191 ? 20.460  17.275 29.976  1.00 91.55  ? 191 PRO A CB  1 
ATOM   1402  C CG  . PRO A  1 191 ? 19.843  15.890 29.969  1.00 91.43  ? 191 PRO A CG  1 
ATOM   1403  C CD  . PRO A  1 191 ? 18.918  15.885 28.770  1.00 94.34  ? 191 PRO A CD  1 
ATOM   1404  N N   . GLU A  1 192 ? 20.469  18.886 27.361  1.00 86.28  ? 192 GLU A N   1 
ATOM   1405  C CA  . GLU A  1 192 ? 21.196  19.762 26.403  1.00 94.70  ? 192 GLU A CA  1 
ATOM   1406  C C   . GLU A  1 192 ? 20.238  20.826 25.850  1.00 96.71  ? 192 GLU A C   1 
ATOM   1407  O O   . GLU A  1 192 ? 20.634  22.010 25.809  1.00 93.42  ? 192 GLU A O   1 
ATOM   1408  C CB  . GLU A  1 192 ? 21.806  18.911 25.287  1.00 101.46 ? 192 GLU A CB  1 
ATOM   1409  C CG  . GLU A  1 192 ? 22.409  17.610 25.788  1.00 104.10 ? 192 GLU A CG  1 
ATOM   1410  C CD  . GLU A  1 192 ? 23.114  16.781 24.728  1.00 102.54 ? 192 GLU A CD  1 
ATOM   1411  O OE1 . GLU A  1 192 ? 23.125  17.206 23.556  1.00 94.39  ? 192 GLU A OE1 1 
ATOM   1412  O OE2 . GLU A  1 192 ? 23.651  15.712 25.080  1.00 96.69  ? 192 GLU A OE2 1 
ATOM   1413  N N   . SER A  1 193 ? 19.032  20.420 25.437  1.00 95.69  ? 193 SER A N   1 
ATOM   1414  C CA  . SER A  1 193 ? 17.965  21.319 24.918  1.00 99.52  ? 193 SER A CA  1 
ATOM   1415  C C   . SER A  1 193 ? 17.495  22.254 26.038  1.00 104.73 ? 193 SER A C   1 
ATOM   1416  O O   . SER A  1 193 ? 17.484  23.482 25.824  1.00 104.36 ? 193 SER A O   1 
ATOM   1417  C CB  . SER A  1 193 ? 16.816  20.531 24.342  1.00 92.50  ? 193 SER A CB  1 
ATOM   1418  O OG  . SER A  1 193 ? 17.234  19.794 23.202  1.00 88.90  ? 193 SER A OG  1 
ATOM   1419  N N   . HIS A  1 194 ? 17.122  21.677 27.184  1.00 104.33 ? 194 HIS A N   1 
ATOM   1420  C CA  . HIS A  1 194 ? 16.721  22.390 28.427  1.00 104.24 ? 194 HIS A CA  1 
ATOM   1421  C C   . HIS A  1 194 ? 17.600  23.634 28.623  1.00 92.51  ? 194 HIS A C   1 
ATOM   1422  O O   . HIS A  1 194 ? 17.042  24.745 28.741  1.00 103.33 ? 194 HIS A O   1 
ATOM   1423  C CB  . HIS A  1 194 ? 16.788  21.411 29.608  1.00 116.54 ? 194 HIS A CB  1 
ATOM   1424  C CG  . HIS A  1 194 ? 16.701  22.039 30.958  1.00 125.00 ? 194 HIS A CG  1 
ATOM   1425  N ND1 . HIS A  1 194 ? 15.557  21.967 31.729  1.00 122.72 ? 194 HIS A ND1 1 
ATOM   1426  C CD2 . HIS A  1 194 ? 17.612  22.714 31.692  1.00 123.63 ? 194 HIS A CD2 1 
ATOM   1427  C CE1 . HIS A  1 194 ? 15.763  22.583 32.876  1.00 121.53 ? 194 HIS A CE1 1 
ATOM   1428  N NE2 . HIS A  1 194 ? 17.017  23.053 32.877  1.00 119.08 ? 194 HIS A NE2 1 
ATOM   1429  N N   . THR A  1 195 ? 18.923  23.448 28.642  1.00 74.94  ? 195 THR A N   1 
ATOM   1430  C CA  . THR A  1 195 ? 19.935  24.507 28.902  1.00 74.91  ? 195 THR A CA  1 
ATOM   1431  C C   . THR A  1 195 ? 19.805  25.636 27.871  1.00 84.84  ? 195 THR A C   1 
ATOM   1432  O O   . THR A  1 195 ? 19.750  26.815 28.288  1.00 91.42  ? 195 THR A O   1 
ATOM   1433  C CB  . THR A  1 195 ? 21.352  23.921 28.893  1.00 71.76  ? 195 THR A CB  1 
ATOM   1434  O OG1 . THR A  1 195 ? 21.372  22.818 29.799  1.00 72.13  ? 195 THR A OG1 1 
ATOM   1435  C CG2 . THR A  1 195 ? 22.408  24.932 29.280  1.00 67.94  ? 195 THR A CG2 1 
ATOM   1436  N N   . MET A  1 196 ? 19.772  25.289 26.580  1.00 93.02  ? 196 MET A N   1 
ATOM   1437  C CA  . MET A  1 196 ? 19.740  26.254 25.447  1.00 92.31  ? 196 MET A CA  1 
ATOM   1438  C C   . MET A  1 196 ? 18.491  27.139 25.547  1.00 91.13  ? 196 MET A C   1 
ATOM   1439  O O   . MET A  1 196 ? 18.640  28.379 25.510  1.00 82.05  ? 196 MET A O   1 
ATOM   1440  C CB  . MET A  1 196 ? 19.735  25.523 24.101  1.00 92.08  ? 196 MET A CB  1 
ATOM   1441  C CG  . MET A  1 196 ? 21.115  25.111 23.636  1.00 96.02  ? 196 MET A CG  1 
ATOM   1442  S SD  . MET A  1 196 ? 22.253  26.521 23.545  1.00 111.29 ? 196 MET A SD  1 
ATOM   1443  C CE  . MET A  1 196 ? 21.387  27.588 22.395  1.00 113.41 ? 196 MET A CE  1 
ATOM   1444  N N   . LEU A  1 197 ? 17.312  26.520 25.658  1.00 89.84  ? 197 LEU A N   1 
ATOM   1445  C CA  . LEU A  1 197 ? 16.002  27.222 25.728  1.00 88.26  ? 197 LEU A CA  1 
ATOM   1446  C C   . LEU A  1 197 ? 16.037  28.240 26.875  1.00 91.99  ? 197 LEU A C   1 
ATOM   1447  O O   . LEU A  1 197 ? 15.617  29.392 26.649  1.00 95.68  ? 197 LEU A O   1 
ATOM   1448  C CB  . LEU A  1 197 ? 14.885  26.193 25.926  1.00 88.46  ? 197 LEU A CB  1 
ATOM   1449  C CG  . LEU A  1 197 ? 13.461  26.732 25.794  1.00 91.33  ? 197 LEU A CG  1 
ATOM   1450  C CD1 . LEU A  1 197 ? 13.253  27.413 24.449  1.00 94.84  ? 197 LEU A CD1 1 
ATOM   1451  C CD2 . LEU A  1 197 ? 12.442  25.618 25.988  1.00 88.50  ? 197 LEU A CD2 1 
ATOM   1452  N N   . LYS A  1 198 ? 16.522  27.826 28.050  1.00 86.78  ? 198 LYS A N   1 
ATOM   1453  C CA  . LYS A  1 198 ? 16.702  28.704 29.238  1.00 78.53  ? 198 LYS A CA  1 
ATOM   1454  C C   . LYS A  1 198 ? 17.588  29.892 28.842  1.00 81.51  ? 198 LYS A C   1 
ATOM   1455  O O   . LYS A  1 198 ? 17.173  31.049 29.082  1.00 87.10  ? 198 LYS A O   1 
ATOM   1456  C CB  . LYS A  1 198 ? 17.308  27.913 30.401  1.00 71.84  ? 198 LYS A CB  1 
ATOM   1457  N N   . SER A  1 199 ? 18.751  29.613 28.243  1.00 78.05  ? 199 SER A N   1 
ATOM   1458  C CA  . SER A  1 199 ? 19.728  30.629 27.768  1.00 84.56  ? 199 SER A CA  1 
ATOM   1459  C C   . SER A  1 199 ? 19.031  31.637 26.846  1.00 92.72  ? 199 SER A C   1 
ATOM   1460  O O   . SER A  1 199 ? 19.056  32.849 27.158  1.00 96.46  ? 199 SER A O   1 
ATOM   1461  C CB  . SER A  1 199 ? 20.897  29.979 27.075  1.00 82.69  ? 199 SER A CB  1 
ATOM   1462  O OG  . SER A  1 199 ? 21.698  30.954 26.423  1.00 84.61  ? 199 SER A OG  1 
ATOM   1463  N N   . ALA A  1 200 ? 18.440  31.148 25.751  1.00 87.91  ? 200 ALA A N   1 
ATOM   1464  C CA  . ALA A  1 200 ? 17.737  31.954 24.725  1.00 83.73  ? 200 ALA A CA  1 
ATOM   1465  C C   . ALA A  1 200 ? 16.714  32.872 25.406  1.00 83.99  ? 200 ALA A C   1 
ATOM   1466  O O   . ALA A  1 200 ? 16.719  34.089 25.116  1.00 88.08  ? 200 ALA A O   1 
ATOM   1467  C CB  . ALA A  1 200 ? 17.076  31.042 23.720  1.00 86.90  ? 200 ALA A CB  1 
ATOM   1468  N N   . ALA A  1 201 ? 15.877  32.301 26.279  1.00 76.98  ? 201 ALA A N   1 
ATOM   1469  C CA  . ALA A  1 201 ? 14.789  32.996 27.007  1.00 77.36  ? 201 ALA A CA  1 
ATOM   1470  C C   . ALA A  1 201 ? 15.364  34.177 27.798  1.00 75.41  ? 201 ALA A C   1 
ATOM   1471  O O   . ALA A  1 201 ? 14.763  35.274 27.752  1.00 75.32  ? 201 ALA A O   1 
ATOM   1472  C CB  . ALA A  1 201 ? 14.074  32.023 27.912  1.00 72.53  ? 201 ALA A CB  1 
ATOM   1473  N N   . ILE A  1 202 ? 16.484  33.955 28.493  1.00 72.61  ? 202 ILE A N   1 
ATOM   1474  C CA  . ILE A  1 202 ? 17.182  34.982 29.321  1.00 72.71  ? 202 ILE A CA  1 
ATOM   1475  C C   . ILE A  1 202 ? 17.625  36.133 28.411  1.00 73.88  ? 202 ILE A C   1 
ATOM   1476  O O   . ILE A  1 202 ? 17.232  37.288 28.684  1.00 77.32  ? 202 ILE A O   1 
ATOM   1477  C CB  . ILE A  1 202 ? 18.369  34.362 30.083  1.00 73.25  ? 202 ILE A CB  1 
ATOM   1478  C CG1 . ILE A  1 202 ? 17.898  33.349 31.129  1.00 75.33  ? 202 ILE A CG1 1 
ATOM   1479  C CG2 . ILE A  1 202 ? 19.237  35.451 30.698  1.00 73.24  ? 202 ILE A CG2 1 
ATOM   1480  C CD1 . ILE A  1 202 ? 19.018  32.583 31.796  1.00 81.71  ? 202 ILE A CD1 1 
ATOM   1481  N N   . VAL A  1 203 ? 18.405  35.819 27.371  1.00 74.33  ? 203 VAL A N   1 
ATOM   1482  C CA  . VAL A  1 203 ? 18.980  36.807 26.407  1.00 75.64  ? 203 VAL A CA  1 
ATOM   1483  C C   . VAL A  1 203 ? 17.876  37.777 25.969  1.00 73.54  ? 203 VAL A C   1 
ATOM   1484  O O   . VAL A  1 203 ? 18.120  39.004 25.994  1.00 70.22  ? 203 VAL A O   1 
ATOM   1485  C CB  . VAL A  1 203 ? 19.624  36.107 25.194  1.00 70.58  ? 203 VAL A CB  1 
ATOM   1486  C CG1 . VAL A  1 203 ? 20.142  37.109 24.170  1.00 65.44  ? 203 VAL A CG1 1 
ATOM   1487  C CG2 . VAL A  1 203 ? 20.728  35.149 25.615  1.00 68.68  ? 203 VAL A CG2 1 
ATOM   1488  N N   . LEU A  1 204 ? 16.710  37.248 25.586  1.00 66.44  ? 204 LEU A N   1 
ATOM   1489  C CA  . LEU A  1 204 ? 15.563  38.052 25.085  1.00 73.23  ? 204 LEU A CA  1 
ATOM   1490  C C   . LEU A  1 204 ? 14.946  38.842 26.245  1.00 77.91  ? 204 LEU A C   1 
ATOM   1491  O O   . LEU A  1 204 ? 14.968  40.094 26.190  1.00 82.22  ? 204 LEU A O   1 
ATOM   1492  C CB  . LEU A  1 204 ? 14.528  37.126 24.439  1.00 77.21  ? 204 LEU A CB  1 
ATOM   1493  C CG  . LEU A  1 204 ? 13.298  37.830 23.863  1.00 81.53  ? 204 LEU A CG  1 
ATOM   1494  C CD1 . LEU A  1 204 ? 12.995  37.351 22.453  1.00 82.85  ? 204 LEU A CD1 1 
ATOM   1495  C CD2 . LEU A  1 204 ? 12.085  37.644 24.761  1.00 88.10  ? 204 LEU A CD2 1 
ATOM   1496  N N   . LEU A  1 205 ? 14.428  38.130 27.250  1.00 69.19  ? 205 LEU A N   1 
ATOM   1497  C CA  . LEU A  1 205 ? 13.629  38.697 28.370  1.00 65.26  ? 205 LEU A CA  1 
ATOM   1498  C C   . LEU A  1 205 ? 14.495  39.651 29.204  1.00 63.38  ? 205 LEU A C   1 
ATOM   1499  O O   . LEU A  1 205 ? 13.973  40.705 29.624  1.00 65.38  ? 205 LEU A O   1 
ATOM   1500  C CB  . LEU A  1 205 ? 13.083  37.542 29.214  1.00 70.44  ? 205 LEU A CB  1 
ATOM   1501  C CG  . LEU A  1 205 ? 12.162  36.573 28.472  1.00 71.52  ? 205 LEU A CG  1 
ATOM   1502  C CD1 . LEU A  1 205 ? 11.776  35.397 29.357  1.00 74.71  ? 205 LEU A CD1 1 
ATOM   1503  C CD2 . LEU A  1 205 ? 10.919  37.286 27.962  1.00 70.15  ? 205 LEU A CD2 1 
ATOM   1504  N N   . ALA A  1 206 ? 15.763  39.293 29.433  1.00 56.11  ? 206 ALA A N   1 
ATOM   1505  C CA  . ALA A  1 206 ? 16.755  40.113 30.168  1.00 56.89  ? 206 ALA A CA  1 
ATOM   1506  C C   . ALA A  1 206 ? 16.988  41.434 29.423  1.00 57.72  ? 206 ALA A C   1 
ATOM   1507  O O   . ALA A  1 206 ? 16.735  42.501 30.017  1.00 62.49  ? 206 ALA A O   1 
ATOM   1508  C CB  . ALA A  1 206 ? 18.038  39.337 30.336  1.00 59.78  ? 206 ALA A CB  1 
ATOM   1509  N N   . GLY A  1 207 ? 17.447  41.355 28.168  1.00 59.09  ? 207 GLY A N   1 
ATOM   1510  C CA  . GLY A  1 207 ? 17.763  42.519 27.314  1.00 60.83  ? 207 GLY A CA  1 
ATOM   1511  C C   . GLY A  1 207 ? 16.620  43.523 27.255  1.00 66.77  ? 207 GLY A C   1 
ATOM   1512  O O   . GLY A  1 207 ? 16.898  44.739 27.242  1.00 62.90  ? 207 GLY A O   1 
ATOM   1513  N N   . TRP A  1 208 ? 15.377  43.032 27.214  1.00 70.97  ? 208 TRP A N   1 
ATOM   1514  C CA  . TRP A  1 208 ? 14.131  43.840 27.105  1.00 69.21  ? 208 TRP A CA  1 
ATOM   1515  C C   . TRP A  1 208 ? 14.165  45.029 28.076  1.00 60.24  ? 208 TRP A C   1 
ATOM   1516  O O   . TRP A  1 208 ? 13.578  46.079 27.746  1.00 63.53  ? 208 TRP A O   1 
ATOM   1517  C CB  . TRP A  1 208 ? 12.910  42.944 27.349  1.00 83.03  ? 208 TRP A CB  1 
ATOM   1518  C CG  . TRP A  1 208 ? 12.426  42.248 26.114  1.00 96.48  ? 208 TRP A CG  1 
ATOM   1519  C CD1 . TRP A  1 208 ? 13.119  42.061 24.952  1.00 104.60 ? 208 TRP A CD1 1 
ATOM   1520  C CD2 . TRP A  1 208 ? 11.144  41.625 25.919  1.00 93.91  ? 208 TRP A CD2 1 
ATOM   1521  N NE1 . TRP A  1 208 ? 12.353  41.379 24.046  1.00 110.33 ? 208 TRP A NE1 1 
ATOM   1522  C CE2 . TRP A  1 208 ? 11.139  41.094 24.612  1.00 100.53 ? 208 TRP A CE2 1 
ATOM   1523  C CE3 . TRP A  1 208 ? 10.003  41.467 26.714  1.00 85.82  ? 208 TRP A CE3 1 
ATOM   1524  C CZ2 . TRP A  1 208 ? 10.038  40.419 24.087  1.00 95.37  ? 208 TRP A CZ2 1 
ATOM   1525  C CZ3 . TRP A  1 208 ? 8.916   40.801 26.194  1.00 85.86  ? 208 TRP A CZ3 1 
ATOM   1526  C CH2 . TRP A  1 208 ? 8.936   40.282 24.899  1.00 84.76  ? 208 TRP A CH2 1 
ATOM   1527  N N   . VAL A  1 209 ? 14.824  44.861 29.225  1.00 58.67  ? 209 VAL A N   1 
ATOM   1528  C CA  . VAL A  1 209 ? 14.873  45.854 30.341  1.00 59.93  ? 209 VAL A CA  1 
ATOM   1529  C C   . VAL A  1 209 ? 15.484  47.169 29.837  1.00 59.79  ? 209 VAL A C   1 
ATOM   1530  O O   . VAL A  1 209 ? 15.005  48.240 30.262  1.00 66.89  ? 209 VAL A O   1 
ATOM   1531  C CB  . VAL A  1 209 ? 15.662  45.287 31.537  1.00 62.15  ? 209 VAL A CB  1 
ATOM   1532  C CG1 . VAL A  1 209 ? 15.958  46.350 32.584  1.00 64.92  ? 209 VAL A CG1 1 
ATOM   1533  C CG2 . VAL A  1 209 ? 14.947  44.100 32.163  1.00 61.12  ? 209 VAL A CG2 1 
ATOM   1534  N N   . VAL A  1 210 ? 16.497  47.086 28.968  1.00 54.50  ? 210 VAL A N   1 
ATOM   1535  C CA  . VAL A  1 210 ? 17.282  48.252 28.460  1.00 50.98  ? 210 VAL A CA  1 
ATOM   1536  C C   . VAL A  1 210 ? 16.321  49.329 27.942  1.00 51.65  ? 210 VAL A C   1 
ATOM   1537  O O   . VAL A  1 210 ? 16.589  50.528 28.160  1.00 54.18  ? 210 VAL A O   1 
ATOM   1538  C CB  . VAL A  1 210 ? 18.268  47.827 27.356  1.00 49.51  ? 210 VAL A CB  1 
ATOM   1539  C CG1 . VAL A  1 210 ? 18.967  49.029 26.737  1.00 51.16  ? 210 VAL A CG1 1 
ATOM   1540  C CG2 . VAL A  1 210 ? 19.287  46.819 27.864  1.00 55.89  ? 210 VAL A CG2 1 
ATOM   1541  N N   . TYR A  1 211 ? 15.243  48.908 27.279  1.00 53.16  ? 211 TYR A N   1 
ATOM   1542  C CA  . TYR A  1 211 ? 14.356  49.778 26.465  1.00 59.02  ? 211 TYR A CA  1 
ATOM   1543  C C   . TYR A  1 211 ? 13.559  50.709 27.378  1.00 58.77  ? 211 TYR A C   1 
ATOM   1544  O O   . TYR A  1 211 ? 13.599  51.924 27.202  1.00 56.23  ? 211 TYR A O   1 
ATOM   1545  C CB  . TYR A  1 211 ? 13.514  48.909 25.527  1.00 59.49  ? 211 TYR A CB  1 
ATOM   1546  C CG  . TYR A  1 211 ? 14.340  48.227 24.465  1.00 62.98  ? 211 TYR A CG  1 
ATOM   1547  C CD1 . TYR A  1 211 ? 14.523  48.809 23.221  1.00 64.37  ? 211 TYR A CD1 1 
ATOM   1548  C CD2 . TYR A  1 211 ? 14.990  47.029 24.720  1.00 65.05  ? 211 TYR A CD2 1 
ATOM   1549  C CE1 . TYR A  1 211 ? 15.298  48.203 22.247  1.00 64.22  ? 211 TYR A CE1 1 
ATOM   1550  C CE2 . TYR A  1 211 ? 15.773  46.412 23.758  1.00 63.51  ? 211 TYR A CE2 1 
ATOM   1551  C CZ  . TYR A  1 211 ? 15.926  47.000 22.515  1.00 64.87  ? 211 TYR A CZ  1 
ATOM   1552  O OH  . TYR A  1 211 ? 16.692  46.402 21.556  1.00 68.46  ? 211 TYR A OH  1 
ATOM   1553  N N   . PRO A  1 212 ? 12.822  50.187 28.385  1.00 64.96  ? 212 PRO A N   1 
ATOM   1554  C CA  . PRO A  1 212 ? 12.093  51.045 29.318  1.00 65.54  ? 212 PRO A CA  1 
ATOM   1555  C C   . PRO A  1 212 ? 13.013  52.071 30.001  1.00 66.54  ? 212 PRO A C   1 
ATOM   1556  O O   . PRO A  1 212 ? 12.584  53.189 30.224  1.00 63.71  ? 212 PRO A O   1 
ATOM   1557  C CB  . PRO A  1 212 ? 11.513  50.066 30.350  1.00 66.48  ? 212 PRO A CB  1 
ATOM   1558  C CG  . PRO A  1 212 ? 11.466  48.733 29.628  1.00 67.72  ? 212 PRO A CG  1 
ATOM   1559  C CD  . PRO A  1 212 ? 12.640  48.756 28.670  1.00 70.38  ? 212 PRO A CD  1 
ATOM   1560  N N   . ILE A  1 213 ? 14.247  51.664 30.313  1.00 59.78  ? 213 ILE A N   1 
ATOM   1561  C CA  . ILE A  1 213 ? 15.278  52.512 30.982  1.00 55.98  ? 213 ILE A CA  1 
ATOM   1562  C C   . ILE A  1 213 ? 15.606  53.702 30.073  1.00 54.87  ? 213 ILE A C   1 
ATOM   1563  O O   . ILE A  1 213 ? 15.596  54.848 30.565  1.00 56.89  ? 213 ILE A O   1 
ATOM   1564  C CB  . ILE A  1 213 ? 16.533  51.682 31.313  1.00 53.74  ? 213 ILE A CB  1 
ATOM   1565  C CG1 . ILE A  1 213 ? 16.234  50.607 32.362  1.00 49.25  ? 213 ILE A CG1 1 
ATOM   1566  C CG2 . ILE A  1 213 ? 17.682  52.583 31.740  1.00 52.49  ? 213 ILE A CG2 1 
ATOM   1567  C CD1 . ILE A  1 213 ? 17.341  49.598 32.539  1.00 50.14  ? 213 ILE A CD1 1 
ATOM   1568  N N   . VAL A  1 214 ? 15.880  53.430 28.794  1.00 55.83  ? 214 VAL A N   1 
ATOM   1569  C CA  . VAL A  1 214 ? 16.278  54.452 27.780  1.00 57.59  ? 214 VAL A CA  1 
ATOM   1570  C C   . VAL A  1 214 ? 15.087  55.381 27.507  1.00 55.65  ? 214 VAL A C   1 
ATOM   1571  O O   . VAL A  1 214 ? 15.318  56.569 27.197  1.00 53.27  ? 214 VAL A O   1 
ATOM   1572  C CB  . VAL A  1 214 ? 16.782  53.785 26.486  1.00 52.87  ? 214 VAL A CB  1 
ATOM   1573  C CG1 . VAL A  1 214 ? 17.175  54.819 25.441  1.00 51.68  ? 214 VAL A CG1 1 
ATOM   1574  C CG2 . VAL A  1 214 ? 17.935  52.829 26.756  1.00 49.39  ? 214 VAL A CG2 1 
ATOM   1575  N N   . TYR A  1 215 ? 13.862  54.859 27.623  1.00 52.35  ? 215 TYR A N   1 
ATOM   1576  C CA  . TYR A  1 215 ? 12.597  55.592 27.354  1.00 53.73  ? 215 TYR A CA  1 
ATOM   1577  C C   . TYR A  1 215 ? 12.502  56.824 28.259  1.00 50.49  ? 215 TYR A C   1 
ATOM   1578  O O   . TYR A  1 215 ? 11.920  57.839 27.822  1.00 52.14  ? 215 TYR A O   1 
ATOM   1579  C CB  . TYR A  1 215 ? 11.386  54.680 27.570  1.00 57.40  ? 215 TYR A CB  1 
ATOM   1580  C CG  . TYR A  1 215 ? 10.049  55.363 27.429  1.00 58.23  ? 215 TYR A CG  1 
ATOM   1581  C CD1 . TYR A  1 215 ? 9.540   56.160 28.442  1.00 58.19  ? 215 TYR A CD1 1 
ATOM   1582  C CD2 . TYR A  1 215 ? 9.285   55.210 26.283  1.00 60.12  ? 215 TYR A CD2 1 
ATOM   1583  C CE1 . TYR A  1 215 ? 8.311   56.788 28.319  1.00 61.78  ? 215 TYR A CE1 1 
ATOM   1584  C CE2 . TYR A  1 215 ? 8.056   55.832 26.145  1.00 60.40  ? 215 TYR A CE2 1 
ATOM   1585  C CZ  . TYR A  1 215 ? 7.564   56.625 27.166  1.00 61.79  ? 215 TYR A CZ  1 
ATOM   1586  O OH  . TYR A  1 215 ? 6.353   57.242 27.035  1.00 57.91  ? 215 TYR A OH  1 
ATOM   1587  N N   . PHE A  1 216 ? 13.062  56.733 29.471  1.00 48.83  ? 216 PHE A N   1 
ATOM   1588  C CA  . PHE A  1 216 ? 12.840  57.690 30.588  1.00 53.23  ? 216 PHE A CA  1 
ATOM   1589  C C   . PHE A  1 216 ? 13.964  58.729 30.666  1.00 57.47  ? 216 PHE A C   1 
ATOM   1590  O O   . PHE A  1 216 ? 13.788  59.732 31.385  1.00 71.57  ? 216 PHE A O   1 
ATOM   1591  C CB  . PHE A  1 216 ? 12.707  56.940 31.916  1.00 51.05  ? 216 PHE A CB  1 
ATOM   1592  C CG  . PHE A  1 216 ? 11.346  56.334 32.147  1.00 52.81  ? 216 PHE A CG  1 
ATOM   1593  C CD1 . PHE A  1 216 ? 10.219  57.137 32.233  1.00 50.84  ? 216 PHE A CD1 1 
ATOM   1594  C CD2 . PHE A  1 216 ? 11.192  54.964 32.279  1.00 56.90  ? 216 PHE A CD2 1 
ATOM   1595  C CE1 . PHE A  1 216 ? 8.967   56.580 32.437  1.00 54.08  ? 216 PHE A CE1 1 
ATOM   1596  C CE2 . PHE A  1 216 ? 9.939   54.409 32.489  1.00 55.58  ? 216 PHE A CE2 1 
ATOM   1597  C CZ  . PHE A  1 216 ? 8.829   55.218 32.565  1.00 57.05  ? 216 PHE A CZ  1 
ATOM   1598  N N   . LEU A  1 217 ? 15.071  58.508 29.953  1.00 60.38  ? 217 LEU A N   1 
ATOM   1599  C CA  . LEU A  1 217 ? 16.264  59.398 29.985  1.00 70.56  ? 217 LEU A CA  1 
ATOM   1600  C C   . LEU A  1 217 ? 15.864  60.826 29.614  1.00 78.57  ? 217 LEU A C   1 
ATOM   1601  O O   . LEU A  1 217 ? 16.386  61.784 30.185  1.00 73.19  ? 217 LEU A O   1 
ATOM   1602  C CB  . LEU A  1 217 ? 17.331  58.844 29.035  1.00 77.04  ? 217 LEU A CB  1 
ATOM   1603  C CG  . LEU A  1 217 ? 17.915  57.485 29.424  1.00 74.09  ? 217 LEU A CG  1 
ATOM   1604  C CD1 . LEU A  1 217 ? 19.105  57.134 28.545  1.00 68.73  ? 217 LEU A CD1 1 
ATOM   1605  C CD2 . LEU A  1 217 ? 18.314  57.460 30.892  1.00 75.81  ? 217 LEU A CD2 1 
ATOM   1606  N N   . PRO A  1 218 ? 14.935  61.022 28.648  1.00 86.09  ? 218 PRO A N   1 
ATOM   1607  C CA  . PRO A  1 218 ? 14.495  62.365 28.263  1.00 85.38  ? 218 PRO A CA  1 
ATOM   1608  C C   . PRO A  1 218 ? 13.947  63.208 29.428  1.00 88.01  ? 218 PRO A C   1 
ATOM   1609  O O   . PRO A  1 218 ? 13.772  64.405 29.245  1.00 96.86  ? 218 PRO A O   1 
ATOM   1610  C CB  . PRO A  1 218 ? 13.380  62.104 27.238  1.00 80.69  ? 218 PRO A CB  1 
ATOM   1611  C CG  . PRO A  1 218 ? 13.692  60.728 26.684  1.00 80.07  ? 218 PRO A CG  1 
ATOM   1612  C CD  . PRO A  1 218 ? 14.290  59.967 27.849  1.00 84.10  ? 218 PRO A CD  1 
ATOM   1613  N N   . LEU A  1 219 ? 13.688  62.580 30.581  1.00 80.81  ? 219 LEU A N   1 
ATOM   1614  C CA  . LEU A  1 219 ? 13.132  63.244 31.792  1.00 78.41  ? 219 LEU A CA  1 
ATOM   1615  C C   . LEU A  1 219 ? 14.249  63.971 32.547  1.00 87.18  ? 219 LEU A C   1 
ATOM   1616  O O   . LEU A  1 219 ? 13.952  65.001 33.186  1.00 96.57  ? 219 LEU A O   1 
ATOM   1617  C CB  . LEU A  1 219 ? 12.467  62.195 32.688  1.00 71.39  ? 219 LEU A CB  1 
ATOM   1618  C CG  . LEU A  1 219 ? 11.099  61.707 32.218  1.00 75.47  ? 219 LEU A CG  1 
ATOM   1619  C CD1 . LEU A  1 219 ? 10.531  60.676 33.181  1.00 79.59  ? 219 LEU A CD1 1 
ATOM   1620  C CD2 . LEU A  1 219 ? 10.134  62.872 32.055  1.00 79.01  ? 219 LEU A CD2 1 
ATOM   1621  N N   . PHE A  1 220 ? 15.478  63.450 32.481  1.00 92.23  ? 220 PHE A N   1 
ATOM   1622  C CA  . PHE A  1 220 ? 16.663  63.993 33.196  1.00 91.03  ? 220 PHE A CA  1 
ATOM   1623  C C   . PHE A  1 220 ? 17.308  65.100 32.354  1.00 86.34  ? 220 PHE A C   1 
ATOM   1624  O O   . PHE A  1 220 ? 18.486  65.432 32.596  1.00 85.07  ? 220 PHE A O   1 
ATOM   1625  C CB  . PHE A  1 220 ? 17.642  62.868 33.542  1.00 93.67  ? 220 PHE A CB  1 
ATOM   1626  C CG  . PHE A  1 220 ? 17.074  61.824 34.471  1.00 97.73  ? 220 PHE A CG  1 
ATOM   1627  C CD1 . PHE A  1 220 ? 16.309  62.189 35.569  1.00 96.74  ? 220 PHE A CD1 1 
ATOM   1628  C CD2 . PHE A  1 220 ? 17.309  60.476 34.253  1.00 93.34  ? 220 PHE A CD2 1 
ATOM   1629  C CE1 . PHE A  1 220 ? 15.785  61.229 36.420  1.00 93.24  ? 220 PHE A CE1 1 
ATOM   1630  C CE2 . PHE A  1 220 ? 16.787  59.517 35.108  1.00 93.44  ? 220 PHE A CE2 1 
ATOM   1631  C CZ  . PHE A  1 220 ? 16.026  59.895 36.189  1.00 89.25  ? 220 PHE A CZ  1 
ATOM   1632  N N   . GLY A  1 221 ? 16.548  65.657 31.404  1.00 85.00  ? 221 GLY A N   1 
ATOM   1633  C CA  . GLY A  1 221 ? 16.950  66.820 30.587  1.00 83.96  ? 221 GLY A CA  1 
ATOM   1634  C C   . GLY A  1 221 ? 17.128  66.453 29.124  1.00 84.60  ? 221 GLY A C   1 
ATOM   1635  O O   . GLY A  1 221 ? 16.663  65.368 28.727  1.00 97.32  ? 221 GLY A O   1 
ATOM   1636  N N   . ALA A  1 222 ? 17.778  67.327 28.348  1.00 77.26  ? 222 ALA A N   1 
ATOM   1637  C CA  . ALA A  1 222 ? 18.065  67.134 26.906  1.00 79.24  ? 222 ALA A CA  1 
ATOM   1638  C C   . ALA A  1 222 ? 19.452  67.696 26.583  1.00 76.34  ? 222 ALA A C   1 
ATOM   1639  O O   . ALA A  1 222 ? 19.793  68.770 27.112  1.00 78.63  ? 222 ALA A O   1 
ATOM   1640  C CB  . ALA A  1 222 ? 16.995  67.787 26.066  1.00 76.87  ? 222 ALA A CB  1 
ATOM   1641  N N   . SER A  1 223 ? 20.228  66.976 25.768  1.00 81.19  ? 223 SER A N   1 
ATOM   1642  C CA  . SER A  1 223 ? 21.542  67.431 25.245  1.00 76.50  ? 223 SER A CA  1 
ATOM   1643  C C   . SER A  1 223 ? 21.936  66.593 24.028  1.00 81.37  ? 223 SER A C   1 
ATOM   1644  O O   . SER A  1 223 ? 21.465  65.448 23.928  1.00 94.84  ? 223 SER A O   1 
ATOM   1645  C CB  . SER A  1 223 ? 22.595  67.366 26.315  1.00 76.87  ? 223 SER A CB  1 
ATOM   1646  O OG  . SER A  1 223 ? 22.941  66.021 26.600  1.00 85.41  ? 223 SER A OG  1 
ATOM   1647  N N   . GLY A  1 224 ? 22.758  67.151 23.135  1.00 76.02  ? 224 GLY A N   1 
ATOM   1648  C CA  . GLY A  1 224 ? 23.345  66.409 22.002  1.00 72.72  ? 224 GLY A CA  1 
ATOM   1649  C C   . GLY A  1 224 ? 23.932  65.091 22.474  1.00 67.75  ? 224 GLY A C   1 
ATOM   1650  O O   . GLY A  1 224 ? 23.665  64.064 21.828  1.00 68.53  ? 224 GLY A O   1 
ATOM   1651  N N   . GLY A  1 225 ? 24.682  65.125 23.581  1.00 69.24  ? 225 GLY A N   1 
ATOM   1652  C CA  . GLY A  1 225 ? 25.310  63.948 24.213  1.00 69.06  ? 225 GLY A CA  1 
ATOM   1653  C C   . GLY A  1 225 ? 24.279  62.914 24.633  1.00 68.39  ? 225 GLY A C   1 
ATOM   1654  O O   . GLY A  1 225 ? 24.489  61.720 24.336  1.00 82.28  ? 225 GLY A O   1 
ATOM   1655  N N   . LEU A  1 226 ? 23.207  63.347 25.304  1.00 59.27  ? 226 LEU A N   1 
ATOM   1656  C CA  . LEU A  1 226 ? 22.104  62.458 25.759  1.00 62.03  ? 226 LEU A CA  1 
ATOM   1657  C C   . LEU A  1 226 ? 21.431  61.835 24.530  1.00 64.85  ? 226 LEU A C   1 
ATOM   1658  O O   . LEU A  1 226 ? 21.378  60.591 24.454  1.00 72.84  ? 226 LEU A O   1 
ATOM   1659  C CB  . LEU A  1 226 ? 21.102  63.262 26.595  1.00 65.80  ? 226 LEU A CB  1 
ATOM   1660  C CG  . LEU A  1 226 ? 19.944  62.453 27.180  1.00 69.08  ? 226 LEU A CG  1 
ATOM   1661  C CD1 . LEU A  1 226 ? 20.458  61.310 28.041  1.00 66.44  ? 226 LEU A CD1 1 
ATOM   1662  C CD2 . LEU A  1 226 ? 19.004  63.338 27.982  1.00 65.50  ? 226 LEU A CD2 1 
ATOM   1663  N N   . THR A  1 227 ? 20.949  62.674 23.608  1.00 60.77  ? 227 THR A N   1 
ATOM   1664  C CA  . THR A  1 227 ? 20.281  62.262 22.343  1.00 58.26  ? 227 THR A CA  1 
ATOM   1665  C C   . THR A  1 227 ? 21.140  61.201 21.643  1.00 55.32  ? 227 THR A C   1 
ATOM   1666  O O   . THR A  1 227 ? 20.583  60.156 21.256  1.00 54.24  ? 227 THR A O   1 
ATOM   1667  C CB  . THR A  1 227 ? 20.014  63.475 21.442  1.00 59.47  ? 227 THR A CB  1 
ATOM   1668  O OG1 . THR A  1 227 ? 19.105  64.339 22.123  1.00 60.78  ? 227 THR A OG1 1 
ATOM   1669  C CG2 . THR A  1 227 ? 19.441  63.097 20.093  1.00 58.65  ? 227 THR A CG2 1 
ATOM   1670  N N   . THR A  1 228 ? 22.444  61.462 21.495  1.00 49.74  ? 228 THR A N   1 
ATOM   1671  C CA  . THR A  1 228 ? 23.429  60.526 20.888  1.00 49.73  ? 228 THR A CA  1 
ATOM   1672  C C   . THR A  1 228 ? 23.400  59.198 21.652  1.00 50.99  ? 228 THR A C   1 
ATOM   1673  O O   . THR A  1 228 ? 23.308  58.142 20.995  1.00 50.57  ? 228 THR A O   1 
ATOM   1674  C CB  . THR A  1 228 ? 24.841  61.123 20.872  1.00 49.10  ? 228 THR A CB  1 
ATOM   1675  O OG1 . THR A  1 228 ? 24.822  62.295 20.056  1.00 48.79  ? 228 THR A OG1 1 
ATOM   1676  C CG2 . THR A  1 228 ? 25.881  60.160 20.342  1.00 51.88  ? 228 THR A CG2 1 
ATOM   1677  N N   . THR A  1 229 ? 23.473  59.260 22.985  1.00 50.17  ? 229 THR A N   1 
ATOM   1678  C CA  . THR A  1 229 ? 23.439  58.086 23.897  1.00 54.92  ? 229 THR A CA  1 
ATOM   1679  C C   . THR A  1 229 ? 22.171  57.269 23.628  1.00 58.44  ? 229 THR A C   1 
ATOM   1680  O O   . THR A  1 229 ? 22.290  56.054 23.368  1.00 61.72  ? 229 THR A O   1 
ATOM   1681  C CB  . THR A  1 229 ? 23.502  58.523 25.366  1.00 52.66  ? 229 THR A CB  1 
ATOM   1682  O OG1 . THR A  1 229 ? 24.703  59.276 25.537  1.00 47.11  ? 229 THR A OG1 1 
ATOM   1683  C CG2 . THR A  1 229 ? 23.474  57.360 26.333  1.00 51.70  ? 229 THR A CG2 1 
ATOM   1684  N N   . ILE A  1 230 ? 21.007  57.922 23.697  1.00 59.08  ? 230 ILE A N   1 
ATOM   1685  C CA  . ILE A  1 230 ? 19.670  57.299 23.469  1.00 65.53  ? 230 ILE A CA  1 
ATOM   1686  C C   . ILE A  1 230 ? 19.705  56.530 22.143  1.00 71.04  ? 230 ILE A C   1 
ATOM   1687  O O   . ILE A  1 230 ? 19.378  55.325 22.149  1.00 82.01  ? 230 ILE A O   1 
ATOM   1688  C CB  . ILE A  1 230 ? 18.561  58.371 23.488  1.00 68.08  ? 230 ILE A CB  1 
ATOM   1689  C CG1 . ILE A  1 230 ? 18.348  58.935 24.896  1.00 71.89  ? 230 ILE A CG1 1 
ATOM   1690  C CG2 . ILE A  1 230 ? 17.271  57.821 22.899  1.00 65.08  ? 230 ILE A CG2 1 
ATOM   1691  C CD1 . ILE A  1 230 ? 17.544  60.216 24.936  1.00 68.84  ? 230 ILE A CD1 1 
ATOM   1692  N N   . LEU A  1 231 ? 20.102  57.201 21.058  1.00 65.23  ? 231 LEU A N   1 
ATOM   1693  C CA  . LEU A  1 231 ? 20.100  56.646 19.677  1.00 57.93  ? 231 LEU A CA  1 
ATOM   1694  C C   . LEU A  1 231 ? 21.044  55.441 19.598  1.00 59.13  ? 231 LEU A C   1 
ATOM   1695  O O   . LEU A  1 231 ? 20.597  54.373 19.134  1.00 75.17  ? 231 LEU A O   1 
ATOM   1696  C CB  . LEU A  1 231 ? 20.521  57.741 18.692  1.00 54.69  ? 231 LEU A CB  1 
ATOM   1697  C CG  . LEU A  1 231 ? 19.500  58.857 18.471  1.00 54.76  ? 231 LEU A CG  1 
ATOM   1698  C CD1 . LEU A  1 231 ? 19.973  59.813 17.384  1.00 55.74  ? 231 LEU A CD1 1 
ATOM   1699  C CD2 . LEU A  1 231 ? 18.133  58.285 18.126  1.00 51.28  ? 231 LEU A CD2 1 
ATOM   1700  N N   . ILE A  1 232 ? 22.297  55.607 20.034  1.00 54.80  ? 232 ILE A N   1 
ATOM   1701  C CA  . ILE A  1 232 ? 23.377  54.584 19.896  1.00 53.47  ? 232 ILE A CA  1 
ATOM   1702  C C   . ILE A  1 232 ? 23.041  53.364 20.762  1.00 54.36  ? 232 ILE A C   1 
ATOM   1703  O O   . ILE A  1 232 ? 23.169  52.231 20.256  1.00 55.93  ? 232 ILE A O   1 
ATOM   1704  C CB  . ILE A  1 232 ? 24.753  55.177 20.253  1.00 50.48  ? 232 ILE A CB  1 
ATOM   1705  C CG1 . ILE A  1 232 ? 25.161  56.271 19.262  1.00 50.09  ? 232 ILE A CG1 1 
ATOM   1706  C CG2 . ILE A  1 232 ? 25.798  54.076 20.346  1.00 52.62  ? 232 ILE A CG2 1 
ATOM   1707  C CD1 . ILE A  1 232 ? 26.578  56.764 19.431  1.00 51.25  ? 232 ILE A CD1 1 
ATOM   1708  N N   . THR A  1 233 ? 22.637  53.587 22.016  1.00 55.05  ? 233 THR A N   1 
ATOM   1709  C CA  . THR A  1 233 ? 22.295  52.515 22.990  1.00 54.07  ? 233 THR A CA  1 
ATOM   1710  C C   . THR A  1 233 ? 21.230  51.600 22.374  1.00 49.87  ? 233 THR A C   1 
ATOM   1711  O O   . THR A  1 233 ? 21.450  50.372 22.339  1.00 46.98  ? 233 THR A O   1 
ATOM   1712  C CB  . THR A  1 233 ? 21.833  53.101 24.330  1.00 52.61  ? 233 THR A CB  1 
ATOM   1713  O OG1 . THR A  1 233 ? 22.931  53.824 24.888  1.00 52.07  ? 233 THR A OG1 1 
ATOM   1714  C CG2 . THR A  1 233 ? 21.368  52.044 25.308  1.00 54.36  ? 233 THR A CG2 1 
ATOM   1715  N N   . LEU A  1 234 ? 20.129  52.187 21.898  1.00 46.26  ? 234 LEU A N   1 
ATOM   1716  C CA  . LEU A  1 234 ? 18.980  51.462 21.293  1.00 47.01  ? 234 LEU A CA  1 
ATOM   1717  C C   . LEU A  1 234 ? 19.457  50.636 20.094  1.00 44.38  ? 234 LEU A C   1 
ATOM   1718  O O   . LEU A  1 234 ? 18.952  49.508 19.922  1.00 46.87  ? 234 LEU A O   1 
ATOM   1719  C CB  . LEU A  1 234 ? 17.916  52.480 20.876  1.00 50.85  ? 234 LEU A CB  1 
ATOM   1720  C CG  . LEU A  1 234 ? 17.144  53.123 22.027  1.00 54.32  ? 234 LEU A CG  1 
ATOM   1721  C CD1 . LEU A  1 234 ? 16.157  54.156 21.504  1.00 54.14  ? 234 LEU A CD1 1 
ATOM   1722  C CD2 . LEU A  1 234 ? 16.429  52.066 22.860  1.00 55.38  ? 234 LEU A CD2 1 
ATOM   1723  N N   . THR A  1 235 ? 20.383  51.178 19.297  1.00 42.33  ? 235 THR A N   1 
ATOM   1724  C CA  . THR A  1 235 ? 20.980  50.502 18.113  1.00 41.85  ? 235 THR A CA  1 
ATOM   1725  C C   . THR A  1 235 ? 21.761  49.268 18.580  1.00 42.47  ? 235 THR A C   1 
ATOM   1726  O O   . THR A  1 235 ? 21.476  48.160 18.079  1.00 44.50  ? 235 THR A O   1 
ATOM   1727  C CB  . THR A  1 235 ? 21.854  51.469 17.304  1.00 40.47  ? 235 THR A CB  1 
ATOM   1728  O OG1 . THR A  1 235 ? 21.038  52.580 16.929  1.00 39.54  ? 235 THR A OG1 1 
ATOM   1729  C CG2 . THR A  1 235 ? 22.458  50.833 16.070  1.00 41.92  ? 235 THR A CG2 1 
ATOM   1730  N N   . VAL A  1 236 ? 22.703  49.458 19.510  1.00 43.98  ? 236 VAL A N   1 
ATOM   1731  C CA  . VAL A  1 236 ? 23.526  48.366 20.111  1.00 42.88  ? 236 VAL A CA  1 
ATOM   1732  C C   . VAL A  1 236 ? 22.576  47.320 20.708  1.00 43.26  ? 236 VAL A C   1 
ATOM   1733  O O   . VAL A  1 236 ? 22.806  46.112 20.484  1.00 42.24  ? 236 VAL A O   1 
ATOM   1734  C CB  . VAL A  1 236 ? 24.508  48.915 21.166  1.00 38.74  ? 236 VAL A CB  1 
ATOM   1735  C CG1 . VAL A  1 236 ? 25.189  47.797 21.939  1.00 37.41  ? 236 VAL A CG1 1 
ATOM   1736  C CG2 . VAL A  1 236 ? 25.543  49.841 20.545  1.00 38.21  ? 236 VAL A CG2 1 
ATOM   1737  N N   . ALA A  1 237 ? 21.547  47.774 21.429  1.00 44.45  ? 237 ALA A N   1 
ATOM   1738  C CA  . ALA A  1 237 ? 20.504  46.925 22.053  1.00 50.11  ? 237 ALA A CA  1 
ATOM   1739  C C   . ALA A  1 237 ? 19.832  46.068 20.974  1.00 50.97  ? 237 ALA A C   1 
ATOM   1740  O O   . ALA A  1 237 ? 19.874  44.826 21.086  1.00 58.14  ? 237 ALA A O   1 
ATOM   1741  C CB  . ALA A  1 237 ? 19.496  47.786 22.775  1.00 50.96  ? 237 ALA A CB  1 
ATOM   1742  N N   . ASP A  1 238 ? 19.236  46.718 19.971  1.00 47.60  ? 238 ASP A N   1 
ATOM   1743  C CA  . ASP A  1 238 ? 18.546  46.055 18.833  1.00 45.55  ? 238 ASP A CA  1 
ATOM   1744  C C   . ASP A  1 238 ? 19.447  44.951 18.268  1.00 45.52  ? 238 ASP A C   1 
ATOM   1745  O O   . ASP A  1 238 ? 18.992  43.792 18.212  1.00 46.73  ? 238 ASP A O   1 
ATOM   1746  C CB  . ASP A  1 238 ? 18.163  47.067 17.750  1.00 47.96  ? 238 ASP A CB  1 
ATOM   1747  C CG  . ASP A  1 238 ? 16.864  47.801 18.035  1.00 54.58  ? 238 ASP A CG  1 
ATOM   1748  O OD1 . ASP A  1 238 ? 16.514  48.703 17.244  1.00 51.14  ? 238 ASP A OD1 1 
ATOM   1749  O OD2 . ASP A  1 238 ? 16.208  47.457 19.042  1.00 69.41  ? 238 ASP A OD2 1 
ATOM   1750  N N   . VAL A  1 239 ? 20.676  45.299 17.876  1.00 46.21  ? 239 VAL A N   1 
ATOM   1751  C CA  . VAL A  1 239 ? 21.630  44.379 17.185  1.00 45.87  ? 239 VAL A CA  1 
ATOM   1752  C C   . VAL A  1 239 ? 21.916  43.172 18.089  1.00 48.99  ? 239 VAL A C   1 
ATOM   1753  O O   . VAL A  1 239 ? 21.724  42.028 17.627  1.00 51.79  ? 239 VAL A O   1 
ATOM   1754  C CB  . VAL A  1 239 ? 22.930  45.103 16.785  1.00 40.78  ? 239 VAL A CB  1 
ATOM   1755  C CG1 . VAL A  1 239 ? 24.003  44.119 16.345  1.00 39.03  ? 239 VAL A CG1 1 
ATOM   1756  C CG2 . VAL A  1 239 ? 22.687  46.145 15.703  1.00 40.46  ? 239 VAL A CG2 1 
ATOM   1757  N N   . ILE A  1 240 ? 22.361  43.419 19.323  1.00 52.12  ? 240 ILE A N   1 
ATOM   1758  C CA  . ILE A  1 240 ? 22.777  42.364 20.296  1.00 56.55  ? 240 ILE A CA  1 
ATOM   1759  C C   . ILE A  1 240 ? 21.608  41.404 20.545  1.00 60.01  ? 240 ILE A C   1 
ATOM   1760  O O   . ILE A  1 240 ? 21.807  40.180 20.400  1.00 75.45  ? 240 ILE A O   1 
ATOM   1761  C CB  . ILE A  1 240 ? 23.286  42.999 21.605  1.00 55.54  ? 240 ILE A CB  1 
ATOM   1762  C CG1 . ILE A  1 240 ? 24.658  43.649 21.411  1.00 58.36  ? 240 ILE A CG1 1 
ATOM   1763  C CG2 . ILE A  1 240 ? 23.300  41.976 22.730  1.00 54.63  ? 240 ILE A CG2 1 
ATOM   1764  C CD1 . ILE A  1 240 ? 25.168  44.382 22.629  1.00 63.45  ? 240 ILE A CD1 1 
ATOM   1765  N N   . VAL A  1 241 ? 20.441  41.935 20.918  1.00 61.93  ? 241 VAL A N   1 
ATOM   1766  C CA  . VAL A  1 241 ? 19.229  41.135 21.268  1.00 67.61  ? 241 VAL A CA  1 
ATOM   1767  C C   . VAL A  1 241 ? 18.837  40.272 20.071  1.00 71.65  ? 241 VAL A C   1 
ATOM   1768  O O   . VAL A  1 241 ? 18.679  39.059 20.196  1.00 79.58  ? 241 VAL A O   1 
ATOM   1769  C CB  . VAL A  1 241 ? 18.059  42.037 21.703  1.00 67.98  ? 241 VAL A CB  1 
ATOM   1770  C CG1 . VAL A  1 241 ? 16.751  41.262 21.772  1.00 70.54  ? 241 VAL A CG1 1 
ATOM   1771  C CG2 . VAL A  1 241 ? 18.341  42.731 23.026  1.00 69.15  ? 241 VAL A CG2 1 
ATOM   1772  N N   . LYS A  1 242 ? 18.690  40.919 18.910  1.00 66.40  ? 242 LYS A N   1 
ATOM   1773  C CA  . LYS A  1 242 ? 18.122  40.281 17.735  1.00 61.63  ? 242 LYS A CA  1 
ATOM   1774  C C   . LYS A  1 242 ? 19.055  39.185 17.223  1.00 64.64  ? 242 LYS A C   1 
ATOM   1775  O O   . LYS A  1 242 ? 18.603  38.082 16.925  1.00 79.65  ? 242 LYS A O   1 
ATOM   1776  C CB  . LYS A  1 242 ? 17.834  41.332 16.660  1.00 61.02  ? 242 LYS A CB  1 
ATOM   1777  C CG  . LYS A  1 242 ? 16.682  42.274 16.988  1.00 62.99  ? 242 LYS A CG  1 
ATOM   1778  C CD  . LYS A  1 242 ? 16.413  43.309 15.914  1.00 65.00  ? 242 LYS A CD  1 
ATOM   1779  C CE  . LYS A  1 242 ? 15.476  44.425 16.356  1.00 63.68  ? 242 LYS A CE  1 
ATOM   1780  N NZ  . LYS A  1 242 ? 14.409  43.946 17.243  1.00 62.82  ? 242 LYS A NZ  1 
ATOM   1781  N N   . LEU A  1 243 ? 20.355  39.494 17.128  1.00 59.91  ? 243 LEU A N   1 
ATOM   1782  C CA  . LEU A  1 243 ? 21.336  38.550 16.614  1.00 54.20  ? 243 LEU A CA  1 
ATOM   1783  C C   . LEU A  1 243 ? 21.731  37.550 17.709  1.00 50.98  ? 243 LEU A C   1 
ATOM   1784  O O   . LEU A  1 243 ? 21.851  36.342 17.403  1.00 56.26  ? 243 LEU A O   1 
ATOM   1785  C CB  . LEU A  1 243 ? 22.554  39.325 16.105  1.00 51.92  ? 243 LEU A CB  1 
ATOM   1786  C CG  . LEU A  1 243 ? 22.317  40.139 14.834  1.00 52.79  ? 243 LEU A CG  1 
ATOM   1787  C CD1 . LEU A  1 243 ? 23.597  40.819 14.368  1.00 49.88  ? 243 LEU A CD1 1 
ATOM   1788  C CD2 . LEU A  1 243 ? 21.749  39.261 13.730  1.00 53.12  ? 243 LEU A CD2 1 
ATOM   1789  N N   . GLY A  1 244 ? 21.939  38.041 18.934  1.00 47.88  ? 244 GLY A N   1 
ATOM   1790  C CA  . GLY A  1 244 ? 22.250  37.207 20.109  1.00 50.77  ? 244 GLY A CA  1 
ATOM   1791  C C   . GLY A  1 244 ? 21.187  36.144 20.318  1.00 54.70  ? 244 GLY A C   1 
ATOM   1792  O O   . GLY A  1 244 ? 21.525  34.945 20.261  1.00 60.05  ? 244 GLY A O   1 
ATOM   1793  N N   . PHE A  1 245 ? 19.942  36.573 20.538  1.00 62.18  ? 245 PHE A N   1 
ATOM   1794  C CA  . PHE A  1 245 ? 18.761  35.699 20.768  1.00 69.65  ? 245 PHE A CA  1 
ATOM   1795  C C   . PHE A  1 245 ? 18.584  34.740 19.585  1.00 72.63  ? 245 PHE A C   1 
ATOM   1796  O O   . PHE A  1 245 ? 18.510  33.514 19.818  1.00 68.23  ? 245 PHE A O   1 
ATOM   1797  C CB  . PHE A  1 245 ? 17.503  36.542 20.983  1.00 74.21  ? 245 PHE A CB  1 
ATOM   1798  C CG  . PHE A  1 245 ? 16.210  35.773 20.882  1.00 77.88  ? 245 PHE A CG  1 
ATOM   1799  C CD1 . PHE A  1 245 ? 15.714  35.059 21.964  1.00 79.20  ? 245 PHE A CD1 1 
ATOM   1800  C CD2 . PHE A  1 245 ? 15.486  35.762 19.701  1.00 84.15  ? 245 PHE A CD2 1 
ATOM   1801  C CE1 . PHE A  1 245 ? 14.523  34.355 21.866  1.00 84.65  ? 245 PHE A CE1 1 
ATOM   1802  C CE2 . PHE A  1 245 ? 14.293  35.061 19.606  1.00 94.39  ? 245 PHE A CE2 1 
ATOM   1803  C CZ  . PHE A  1 245 ? 13.812  34.359 20.688  1.00 93.32  ? 245 PHE A CZ  1 
ATOM   1804  N N   . SER A  1 246 ? 18.513  35.283 18.364  1.00 75.25  ? 246 SER A N   1 
ATOM   1805  C CA  . SER A  1 246 ? 18.272  34.520 17.109  1.00 78.99  ? 246 SER A CA  1 
ATOM   1806  C C   . SER A  1 246 ? 19.211  33.308 17.034  1.00 73.54  ? 246 SER A C   1 
ATOM   1807  O O   . SER A  1 246 ? 18.710  32.183 16.822  1.00 76.98  ? 246 SER A O   1 
ATOM   1808  C CB  . SER A  1 246 ? 18.422  35.399 15.896  1.00 73.26  ? 246 SER A CB  1 
ATOM   1809  O OG  . SER A  1 246 ? 17.254  36.179 15.690  1.00 78.60  ? 246 SER A OG  1 
ATOM   1810  N N   . THR A  1 247 ? 20.518  33.531 17.191  1.00 68.17  ? 247 THR A N   1 
ATOM   1811  C CA  . THR A  1 247 ? 21.560  32.471 17.130  1.00 66.25  ? 247 THR A CA  1 
ATOM   1812  C C   . THR A  1 247 ? 21.200  31.346 18.105  1.00 60.18  ? 247 THR A C   1 
ATOM   1813  O O   . THR A  1 247 ? 21.421  30.173 17.754  1.00 64.32  ? 247 THR A O   1 
ATOM   1814  C CB  . THR A  1 247 ? 22.957  33.022 17.441  1.00 72.07  ? 247 THR A CB  1 
ATOM   1815  O OG1 . THR A  1 247 ? 23.200  34.153 16.603  1.00 88.68  ? 247 THR A OG1 1 
ATOM   1816  C CG2 . THR A  1 247 ? 24.040  31.984 17.239  1.00 71.90  ? 247 THR A CG2 1 
ATOM   1817  N N   . GLN A  1 248 ? 20.665  31.699 19.278  1.00 59.68  ? 248 GLN A N   1 
ATOM   1818  C CA  . GLN A  1 248 ? 20.331  30.754 20.378  1.00 59.91  ? 248 GLN A CA  1 
ATOM   1819  C C   . GLN A  1 248 ? 19.168  29.847 19.960  1.00 55.15  ? 248 GLN A C   1 
ATOM   1820  O O   . GLN A  1 248 ? 19.338  28.611 20.003  1.00 65.06  ? 248 GLN A O   1 
ATOM   1821  C CB  . GLN A  1 248 ? 20.001  31.531 21.654  1.00 62.56  ? 248 GLN A CB  1 
ATOM   1822  C CG  . GLN A  1 248 ? 21.220  32.187 22.286  1.00 64.31  ? 248 GLN A CG  1 
ATOM   1823  C CD  . GLN A  1 248 ? 22.186  31.162 22.830  1.00 68.25  ? 248 GLN A CD  1 
ATOM   1824  O OE1 . GLN A  1 248 ? 21.839  30.339 23.674  1.00 84.40  ? 248 GLN A OE1 1 
ATOM   1825  N NE2 . GLN A  1 248 ? 23.416  31.201 22.344  1.00 67.24  ? 248 GLN A NE2 1 
ATOM   1826  N N   . THR A  1 249 ? 18.032  30.435 19.576  1.00 51.81  ? 249 THR A N   1 
ATOM   1827  C CA  . THR A  1 249 ? 16.802  29.695 19.180  1.00 55.06  ? 249 THR A CA  1 
ATOM   1828  C C   . THR A  1 249 ? 17.122  28.755 18.014  1.00 49.70  ? 249 THR A C   1 
ATOM   1829  O O   . THR A  1 249 ? 16.504  27.677 17.938  1.00 45.55  ? 249 THR A O   1 
ATOM   1830  C CB  . THR A  1 249 ? 15.665  30.657 18.825  1.00 61.40  ? 249 THR A CB  1 
ATOM   1831  O OG1 . THR A  1 249 ? 16.127  31.526 17.790  1.00 67.50  ? 249 THR A OG1 1 
ATOM   1832  C CG2 . THR A  1 249 ? 15.201  31.458 20.020  1.00 66.31  ? 249 THR A CG2 1 
ATOM   1833  N N   . HIS A  1 250 ? 18.048  29.155 17.140  1.00 50.77  ? 250 HIS A N   1 
ATOM   1834  C CA  . HIS A  1 250 ? 18.557  28.320 16.021  1.00 53.26  ? 250 HIS A CA  1 
ATOM   1835  C C   . HIS A  1 250 ? 19.221  27.066 16.599  1.00 55.73  ? 250 HIS A C   1 
ATOM   1836  O O   . HIS A  1 250 ? 18.758  25.951 16.278  1.00 52.69  ? 250 HIS A O   1 
ATOM   1837  C CB  . HIS A  1 250 ? 19.513  29.127 15.137  1.00 52.32  ? 250 HIS A CB  1 
ATOM   1838  C CG  . HIS A  1 250 ? 19.895  28.423 13.880  1.00 60.89  ? 250 HIS A CG  1 
ATOM   1839  N ND1 . HIS A  1 250 ? 18.965  28.076 12.918  1.00 63.26  ? 250 HIS A ND1 1 
ATOM   1840  C CD2 . HIS A  1 250 ? 21.095  28.006 13.420  1.00 64.42  ? 250 HIS A CD2 1 
ATOM   1841  C CE1 . HIS A  1 250 ? 19.576  27.475 11.919  1.00 71.67  ? 250 HIS A CE1 1 
ATOM   1842  N NE2 . HIS A  1 250 ? 20.885  27.419 12.203  1.00 67.99  ? 250 HIS A NE2 1 
ATOM   1843  N N   . ARG A  1 251 ? 20.252  27.254 17.431  1.00 55.89  ? 251 ARG A N   1 
ATOM   1844  C CA  . ARG A  1 251 ? 21.006  26.157 18.096  1.00 54.56  ? 251 ARG A CA  1 
ATOM   1845  C C   . ARG A  1 251 ? 20.005  25.175 18.720  1.00 55.87  ? 251 ARG A C   1 
ATOM   1846  O O   . ARG A  1 251 ? 20.242  23.953 18.636  1.00 66.16  ? 251 ARG A O   1 
ATOM   1847  C CB  . ARG A  1 251 ? 21.978  26.728 19.135  1.00 45.07  ? 251 ARG A CB  1 
ATOM   1848  N N   . VAL A  1 252 ? 18.920  25.692 19.306  1.00 52.73  ? 252 VAL A N   1 
ATOM   1849  C CA  . VAL A  1 252 ? 17.841  24.883 19.950  1.00 53.05  ? 252 VAL A CA  1 
ATOM   1850  C C   . VAL A  1 252 ? 17.186  23.995 18.884  1.00 54.07  ? 252 VAL A C   1 
ATOM   1851  O O   . VAL A  1 252 ? 17.272  22.755 19.002  1.00 58.19  ? 252 VAL A O   1 
ATOM   1852  C CB  . VAL A  1 252 ? 16.797  25.782 20.641  1.00 50.40  ? 252 VAL A CB  1 
ATOM   1853  C CG1 . VAL A  1 252 ? 15.612  24.975 21.147  1.00 51.01  ? 252 VAL A CG1 1 
ATOM   1854  C CG2 . VAL A  1 252 ? 17.407  26.599 21.770  1.00 50.47  ? 252 VAL A CG2 1 
ATOM   1855  N N   . ALA A  1 253 ? 16.553  24.619 17.888  1.00 60.89  ? 253 ALA A N   1 
ATOM   1856  C CA  . ALA A  1 253 ? 15.806  23.954 16.794  1.00 61.85  ? 253 ALA A CA  1 
ATOM   1857  C C   . ALA A  1 253 ? 16.636  22.800 16.220  1.00 57.11  ? 253 ALA A C   1 
ATOM   1858  O O   . ALA A  1 253 ? 16.055  21.730 15.949  1.00 57.26  ? 253 ALA A O   1 
ATOM   1859  C CB  . ALA A  1 253 ? 15.459  24.962 15.728  1.00 67.90  ? 253 ALA A CB  1 
ATOM   1860  N N   . LYS A  1 254 ? 17.941  23.017 16.034  1.00 56.34  ? 254 LYS A N   1 
ATOM   1861  C CA  . LYS A  1 254 ? 18.880  22.020 15.455  1.00 59.15  ? 254 LYS A CA  1 
ATOM   1862  C C   . LYS A  1 254 ? 19.012  20.836 16.416  1.00 59.67  ? 254 LYS A C   1 
ATOM   1863  O O   . LYS A  1 254 ? 18.883  19.684 15.957  1.00 67.49  ? 254 LYS A O   1 
ATOM   1864  C CB  . LYS A  1 254 ? 20.244  22.662 15.182  1.00 60.58  ? 254 LYS A CB  1 
ATOM   1865  C CG  . LYS A  1 254 ? 20.261  23.668 14.039  1.00 63.79  ? 254 LYS A CG  1 
ATOM   1866  C CD  . LYS A  1 254 ? 21.599  24.347 13.851  1.00 65.55  ? 254 LYS A CD  1 
ATOM   1867  C CE  . LYS A  1 254 ? 22.667  23.422 13.310  1.00 67.25  ? 254 LYS A CE  1 
ATOM   1868  N NZ  . LYS A  1 254 ? 23.984  24.098 13.250  1.00 74.11  ? 254 LYS A NZ  1 
ATOM   1869  N N   . LEU A  1 255 ? 19.260  21.117 17.698  1.00 58.92  ? 255 LEU A N   1 
ATOM   1870  C CA  . LEU A  1 255 ? 19.384  20.096 18.771  1.00 67.40  ? 255 LEU A CA  1 
ATOM   1871  C C   . LEU A  1 255 ? 18.112  19.240 18.791  1.00 59.15  ? 255 LEU A C   1 
ATOM   1872  O O   . LEU A  1 255 ? 18.229  17.998 18.741  1.00 61.38  ? 255 LEU A O   1 
ATOM   1873  C CB  . LEU A  1 255 ? 19.602  20.811 20.109  1.00 83.54  ? 255 LEU A CB  1 
ATOM   1874  C CG  . LEU A  1 255 ? 20.397  20.038 21.161  1.00 101.50 ? 255 LEU A CG  1 
ATOM   1875  C CD1 . LEU A  1 255 ? 21.463  19.162 20.519  1.00 104.42 ? 255 LEU A CD1 1 
ATOM   1876  C CD2 . LEU A  1 255 ? 21.025  20.994 22.164  1.00 103.64 ? 255 LEU A CD2 1 
ATOM   1877  N N   . ARG A  1 256 ? 16.948  19.893 18.850  1.00 54.82  ? 256 ARG A N   1 
ATOM   1878  C CA  . ARG A  1 256 ? 15.614  19.238 18.900  1.00 57.37  ? 256 ARG A CA  1 
ATOM   1879  C C   . ARG A  1 256 ? 15.403  18.411 17.624  1.00 52.52  ? 256 ARG A C   1 
ATOM   1880  O O   . ARG A  1 256 ? 14.829  17.305 17.723  1.00 54.87  ? 256 ARG A O   1 
ATOM   1881  C CB  . ARG A  1 256 ? 14.526  20.298 19.089  1.00 63.46  ? 256 ARG A CB  1 
ATOM   1882  C CG  . ARG A  1 256 ? 14.468  20.876 20.495  1.00 69.88  ? 256 ARG A CG  1 
ATOM   1883  C CD  . ARG A  1 256 ? 13.288  20.354 21.294  1.00 77.74  ? 256 ARG A CD  1 
ATOM   1884  N NE  . ARG A  1 256 ? 12.157  21.271 21.231  1.00 85.34  ? 256 ARG A NE  1 
ATOM   1885  C CZ  . ARG A  1 256 ? 10.894  20.937 21.477  1.00 91.27  ? 256 ARG A CZ  1 
ATOM   1886  N NH1 . ARG A  1 256 ? 10.589  19.689 21.793  1.00 91.06  ? 256 ARG A NH1 1 
ATOM   1887  N NH2 . ARG A  1 256 ? 9.940   21.849 21.403  1.00 97.18  ? 256 ARG A NH2 1 
ATOM   1888  N N   . THR A  1 257 ? 15.850  18.928 16.476  1.00 50.86  ? 257 THR A N   1 
ATOM   1889  C CA  . THR A  1 257 ? 15.773  18.248 15.154  1.00 52.14  ? 257 THR A CA  1 
ATOM   1890  C C   . THR A  1 257 ? 16.651  16.992 15.176  1.00 51.67  ? 257 THR A C   1 
ATOM   1891  O O   . THR A  1 257 ? 16.152  15.915 14.789  1.00 48.26  ? 257 THR A O   1 
ATOM   1892  C CB  . THR A  1 257 ? 16.194  19.182 14.013  1.00 49.86  ? 257 THR A CB  1 
ATOM   1893  O OG1 . THR A  1 257 ? 15.307  20.300 13.995  1.00 54.27  ? 257 THR A OG1 1 
ATOM   1894  C CG2 . THR A  1 257 ? 16.180  18.496 12.665  1.00 49.70  ? 257 THR A CG2 1 
ATOM   1895  N N   . ALA A  1 258 ? 17.908  17.137 15.605  1.00 56.34  ? 258 ALA A N   1 
ATOM   1896  C CA  . ALA A  1 258 ? 18.908  16.048 15.707  1.00 56.59  ? 258 ALA A CA  1 
ATOM   1897  C C   . ALA A  1 258 ? 18.370  14.950 16.629  1.00 58.53  ? 258 ALA A C   1 
ATOM   1898  O O   . ALA A  1 258 ? 18.472  13.762 16.262  1.00 58.72  ? 258 ALA A O   1 
ATOM   1899  C CB  . ALA A  1 258 ? 20.221  16.599 16.208  1.00 59.38  ? 258 ALA A CB  1 
ATOM   1900  N N   . GLU A  1 259 ? 17.814  15.343 17.780  1.00 55.07  ? 259 GLU A N   1 
ATOM   1901  C CA  . GLU A  1 259 ? 17.228  14.422 18.789  1.00 56.23  ? 259 GLU A CA  1 
ATOM   1902  C C   . GLU A  1 259 ? 16.167  13.546 18.112  1.00 57.26  ? 259 GLU A C   1 
ATOM   1903  O O   . GLU A  1 259 ? 16.277  12.303 18.208  1.00 58.88  ? 259 GLU A O   1 
ATOM   1904  C CB  . GLU A  1 259 ? 16.634  15.217 19.953  1.00 62.24  ? 259 GLU A CB  1 
ATOM   1905  C CG  . GLU A  1 259 ? 17.682  15.814 20.876  1.00 71.33  ? 259 GLU A CG  1 
ATOM   1906  C CD  . GLU A  1 259 ? 17.131  16.731 21.956  1.00 75.56  ? 259 GLU A CD  1 
ATOM   1907  O OE1 . GLU A  1 259 ? 15.898  16.935 21.989  1.00 80.81  ? 259 GLU A OE1 1 
ATOM   1908  O OE2 . GLU A  1 259 ? 17.936  17.239 22.762  1.00 83.62  ? 259 GLU A OE2 1 
ATOM   1909  N N   . ASP A  1 260 ? 15.188  14.177 17.455  1.00 56.58  ? 260 ASP A N   1 
ATOM   1910  C CA  . ASP A  1 260 ? 14.074  13.497 16.741  1.00 57.96  ? 260 ASP A CA  1 
ATOM   1911  C C   . ASP A  1 260 ? 14.657  12.451 15.783  1.00 58.53  ? 260 ASP A C   1 
ATOM   1912  O O   . ASP A  1 260 ? 14.101  11.334 15.711  1.00 56.59  ? 260 ASP A O   1 
ATOM   1913  C CB  . ASP A  1 260 ? 13.190  14.505 16.000  1.00 64.67  ? 260 ASP A CB  1 
ATOM   1914  C CG  . ASP A  1 260 ? 12.326  15.360 16.914  1.00 70.95  ? 260 ASP A CG  1 
ATOM   1915  O OD1 . ASP A  1 260 ? 11.607  16.240 16.392  1.00 76.22  ? 260 ASP A OD1 1 
ATOM   1916  O OD2 . ASP A  1 260 ? 12.377  15.138 18.139  1.00 76.50  ? 260 ASP A OD2 1 
ATOM   1917  N N   . VAL A  1 261 ? 15.739  12.801 15.081  1.00 59.60  ? 261 VAL A N   1 
ATOM   1918  C CA  . VAL A  1 261 ? 16.421  11.916 14.090  1.00 65.32  ? 261 VAL A CA  1 
ATOM   1919  C C   . VAL A  1 261 ? 17.015  10.713 14.831  1.00 65.15  ? 261 VAL A C   1 
ATOM   1920  O O   . VAL A  1 261 ? 16.770  9.573  14.387  1.00 62.70  ? 261 VAL A O   1 
ATOM   1921  C CB  . VAL A  1 261 ? 17.500  12.675 13.294  1.00 69.05  ? 261 VAL A CB  1 
ATOM   1922  C CG1 . VAL A  1 261 ? 18.392  11.729 12.505  1.00 65.24  ? 261 VAL A CG1 1 
ATOM   1923  C CG2 . VAL A  1 261 ? 16.885  13.718 12.375  1.00 76.65  ? 261 VAL A CG2 1 
ATOM   1924  N N   . ARG A  1 262 ? 17.762  10.967 15.911  1.00 64.19  ? 262 ARG A N   1 
ATOM   1925  C CA  . ARG A  1 262 ? 18.440  9.926  16.732  1.00 60.70  ? 262 ARG A CA  1 
ATOM   1926  C C   . ARG A  1 262 ? 17.388  8.993  17.345  1.00 57.81  ? 262 ARG A C   1 
ATOM   1927  O O   . ARG A  1 262 ? 17.603  7.764  17.321  1.00 51.76  ? 262 ARG A O   1 
ATOM   1928  C CB  . ARG A  1 262 ? 19.291  10.564 17.835  1.00 62.34  ? 262 ARG A CB  1 
ATOM   1929  C CG  . ARG A  1 262 ? 20.563  11.231 17.337  1.00 65.29  ? 262 ARG A CG  1 
ATOM   1930  C CD  . ARG A  1 262 ? 21.553  11.496 18.458  1.00 68.83  ? 262 ARG A CD  1 
ATOM   1931  N NE  . ARG A  1 262 ? 21.009  12.328 19.524  1.00 73.28  ? 262 ARG A NE  1 
ATOM   1932  C CZ  . ARG A  1 262 ? 21.165  13.647 19.612  1.00 77.42  ? 262 ARG A CZ  1 
ATOM   1933  N NH1 . ARG A  1 262 ? 21.846  14.300 18.687  1.00 81.73  ? 262 ARG A NH1 1 
ATOM   1934  N NH2 . ARG A  1 262 ? 20.634  14.312 20.623  1.00 78.42  ? 262 ARG A NH2 1 
ATOM   1935  N N   . ALA A  1 263 ? 16.301  9.562  17.874  1.00 57.56  ? 263 ALA A N   1 
ATOM   1936  C CA  . ALA A  1 263 ? 15.192  8.828  18.525  1.00 58.31  ? 263 ALA A CA  1 
ATOM   1937  C C   . ALA A  1 263 ? 14.396  8.050  17.470  1.00 60.11  ? 263 ALA A C   1 
ATOM   1938  O O   . ALA A  1 263 ? 13.498  7.277  17.859  1.00 69.60  ? 263 ALA A O   1 
ATOM   1939  C CB  . ALA A  1 263 ? 14.314  9.792  19.282  1.00 61.43  ? 263 ALA A CB  1 
ATOM   1940  N N   . GLY A  1 264 ? 14.719  8.253  16.188  1.00 60.41  ? 264 GLY A N   1 
ATOM   1941  C CA  . GLY A  1 264 ? 14.053  7.600  15.044  1.00 59.36  ? 264 GLY A CA  1 
ATOM   1942  C C   . GLY A  1 264 ? 12.611  8.054  14.892  1.00 61.85  ? 264 GLY A C   1 
ATOM   1943  O O   . GLY A  1 264 ? 11.807  7.286  14.328  1.00 54.79  ? 264 GLY A O   1 
ATOM   1944  N N   . ASP A  1 265 ? 12.291  9.258  15.379  1.00 71.88  ? 265 ASP A N   1 
ATOM   1945  C CA  . ASP A  1 265 ? 10.936  9.870  15.298  1.00 73.39  ? 265 ASP A CA  1 
ATOM   1946  C C   . ASP A  1 265 ? 10.741  10.484 13.908  1.00 66.75  ? 265 ASP A C   1 
ATOM   1947  O O   . ASP A  1 265 ? 9.584   10.544 13.445  1.00 57.72  ? 265 ASP A O   1 
ATOM   1948  C CB  . ASP A  1 265 ? 10.732  10.927 16.387  1.00 83.64  ? 265 ASP A CB  1 
ATOM   1949  C CG  . ASP A  1 265 ? 10.606  10.356 17.790  1.00 91.38  ? 265 ASP A CG  1 
ATOM   1950  O OD1 . ASP A  1 265 ? 10.141  9.207  17.917  1.00 102.21 ? 265 ASP A OD1 1 
ATOM   1951  O OD2 . ASP A  1 265 ? 10.973  11.068 18.744  1.00 106.78 ? 265 ASP A OD2 1 
ATOM   1952  N N   . ASP A  1 266 ? 11.834  10.926 13.278  1.00 67.87  ? 266 ASP A N   1 
ATOM   1953  C CA  . ASP A  1 266 ? 11.834  11.572 11.938  1.00 69.62  ? 266 ASP A CA  1 
ATOM   1954  C C   . ASP A  1 266 ? 13.207  11.358 11.291  1.00 60.13  ? 266 ASP A C   1 
ATOM   1955  O O   . ASP A  1 266 ? 14.070  10.726 11.930  1.00 54.25  ? 266 ASP A O   1 
ATOM   1956  C CB  . ASP A  1 266 ? 11.488  13.060 12.045  1.00 76.10  ? 266 ASP A CB  1 
ATOM   1957  C CG  . ASP A  1 266 ? 10.726  13.612 10.851  1.00 79.93  ? 266 ASP A CG  1 
ATOM   1958  O OD1 . ASP A  1 266 ? 9.891   14.516 11.060  1.00 81.87  ? 266 ASP A OD1 1 
ATOM   1959  O OD2 . ASP A  1 266 ? 10.975  13.139 9.722   1.00 69.40  ? 266 ASP A OD2 1 
ATOM   1960  N N   . VAL A  1 267 ? 13.391  11.870 10.071  1.00 56.39  ? 267 VAL A N   1 
ATOM   1961  C CA  . VAL A  1 267 ? 14.657  11.758 9.286   1.00 55.81  ? 267 VAL A CA  1 
ATOM   1962  C C   . VAL A  1 267 ? 14.969  13.126 8.665   1.00 53.60  ? 267 VAL A C   1 
ATOM   1963  O O   . VAL A  1 267 ? 14.016  13.871 8.373   1.00 52.18  ? 267 VAL A O   1 
ATOM   1964  C CB  . VAL A  1 267 ? 14.546  10.647 8.224   1.00 51.80  ? 267 VAL A CB  1 
ATOM   1965  C CG1 . VAL A  1 267 ? 13.353  10.857 7.308   1.00 51.05  ? 267 VAL A CG1 1 
ATOM   1966  C CG2 . VAL A  1 267 ? 15.824  10.507 7.417   1.00 56.53  ? 267 VAL A CG2 1 
ATOM   1967  N N   . HIS A  1 268 ? 16.256  13.442 8.492   1.00 56.14  ? 268 HIS A N   1 
ATOM   1968  C CA  . HIS A  1 268 ? 16.763  14.728 7.939   1.00 56.78  ? 268 HIS A CA  1 
ATOM   1969  C C   . HIS A  1 268 ? 17.798  14.433 6.855   1.00 52.26  ? 268 HIS A C   1 
ATOM   1970  O O   . HIS A  1 268 ? 18.721  13.647 7.069   1.00 47.41  ? 268 HIS A O   1 
ATOM   1971  C CB  . HIS A  1 268 ? 17.321  15.607 9.067   1.00 62.72  ? 268 HIS A CB  1 
ATOM   1972  C CG  . HIS A  1 268 ? 17.391  17.058 8.729   1.00 67.71  ? 268 HIS A CG  1 
ATOM   1973  N ND1 . HIS A  1 268 ? 18.589  17.704 8.487   1.00 73.34  ? 268 HIS A ND1 1 
ATOM   1974  C CD2 . HIS A  1 268 ? 16.423  17.990 8.591   1.00 68.54  ? 268 HIS A CD2 1 
ATOM   1975  C CE1 . HIS A  1 268 ? 18.356  18.971 8.213   1.00 72.80  ? 268 HIS A CE1 1 
ATOM   1976  N NE2 . HIS A  1 268 ? 17.034  19.172 8.271   1.00 71.03  ? 268 HIS A NE2 1 
ATOM   1977  N N   . PRO A  1 269 ? 17.684  15.071 5.668   1.00 50.02  ? 269 PRO A N   1 
ATOM   1978  C CA  . PRO A  1 269 ? 18.459  14.673 4.492   1.00 51.44  ? 269 PRO A CA  1 
ATOM   1979  C C   . PRO A  1 269 ? 19.949  15.049 4.538   1.00 55.29  ? 269 PRO A C   1 
ATOM   1980  O O   . PRO A  1 269 ? 20.672  14.657 3.637   1.00 56.40  ? 269 PRO A O   1 
ATOM   1981  C CB  . PRO A  1 269 ? 17.763  15.435 3.354   1.00 50.03  ? 269 PRO A CB  1 
ATOM   1982  C CG  . PRO A  1 269 ? 17.227  16.681 4.023   1.00 52.63  ? 269 PRO A CG  1 
ATOM   1983  C CD  . PRO A  1 269 ? 16.808  16.222 5.404   1.00 51.40  ? 269 PRO A CD  1 
ATOM   1984  N N   . GLU A  1 270 ? 20.369  15.793 5.567   1.00 56.54  ? 270 GLU A N   1 
ATOM   1985  C CA  . GLU A  1 270 ? 21.783  16.209 5.771   1.00 50.78  ? 270 GLU A CA  1 
ATOM   1986  C C   . GLU A  1 270 ? 22.176  15.976 7.233   1.00 47.53  ? 270 GLU A C   1 
ATOM   1987  O O   . GLU A  1 270 ? 21.273  15.949 8.094   1.00 43.39  ? 270 GLU A O   1 
ATOM   1988  C CB  . GLU A  1 270 ? 21.978  17.678 5.390   1.00 57.39  ? 270 GLU A CB  1 
ATOM   1989  C CG  . GLU A  1 270 ? 21.470  18.651 6.438   1.00 64.97  ? 270 GLU A CG  1 
ATOM   1990  C CD  . GLU A  1 270 ? 21.792  20.109 6.157   1.00 69.42  ? 270 GLU A CD  1 
ATOM   1991  O OE1 . GLU A  1 270 ? 22.175  20.421 5.012   1.00 72.84  ? 270 GLU A OE1 1 
ATOM   1992  O OE2 . GLU A  1 270 ? 21.663  20.929 7.086   1.00 61.80  ? 270 GLU A OE2 1 
ATOM   1993  N N   . SER A  1 271 ? 23.476  15.807 7.488   1.00 51.70  ? 271 SER A N   1 
ATOM   1994  C CA  . SER A  1 271 ? 24.071  15.697 8.846   1.00 50.33  ? 271 SER A CA  1 
ATOM   1995  C C   . SER A  1 271 ? 23.979  17.055 9.549   1.00 54.77  ? 271 SER A C   1 
ATOM   1996  O O   . SER A  1 271 ? 24.250  18.083 8.897   1.00 55.87  ? 271 SER A O   1 
ATOM   1997  C CB  . SER A  1 271 ? 25.494  15.208 8.780   1.00 49.60  ? 271 SER A CB  1 
ATOM   1998  O OG  . SER A  1 271 ? 26.208  15.864 7.742   1.00 49.52  ? 271 SER A OG  1 
ATOM   1999  N N   . ILE A  1 272 ? 23.599  17.050 10.829  1.00 53.61  ? 272 ILE A N   1 
ATOM   2000  C CA  . ILE A  1 272 ? 23.454  18.274 11.671  1.00 52.31  ? 272 ILE A CA  1 
ATOM   2001  C C   . ILE A  1 272 ? 24.668  18.379 12.599  1.00 51.42  ? 272 ILE A C   1 
ATOM   2002  O O   . ILE A  1 272 ? 25.007  17.374 13.247  1.00 48.70  ? 272 ILE A O   1 
ATOM   2003  C CB  . ILE A  1 272 ? 22.125  18.240 12.449  1.00 53.89  ? 272 ILE A CB  1 
ATOM   2004  C CG1 . ILE A  1 272 ? 20.926  18.202 11.499  1.00 56.51  ? 272 ILE A CG1 1 
ATOM   2005  C CG2 . ILE A  1 272 ? 22.043  19.406 13.421  1.00 56.00  ? 272 ILE A CG2 1 
ATOM   2006  C CD1 . ILE A  1 272 ? 19.598  18.023 12.191  1.00 61.07  ? 272 ILE A CD1 1 
ATOM   2007  N N   . TRP A  1 273 ? 25.295  19.557 12.646  1.00 55.84  ? 273 TRP A N   1 
ATOM   2008  C CA  . TRP A  1 273 ? 26.517  19.841 13.444  1.00 60.12  ? 273 TRP A CA  1 
ATOM   2009  C C   . TRP A  1 273 ? 26.258  21.022 14.384  1.00 64.00  ? 273 TRP A C   1 
ATOM   2010  O O   . TRP A  1 273 ? 25.434  21.887 14.033  1.00 58.83  ? 273 TRP A O   1 
ATOM   2011  C CB  . TRP A  1 273 ? 27.707  20.122 12.517  1.00 63.72  ? 273 TRP A CB  1 
ATOM   2012  C CG  . TRP A  1 273 ? 28.045  18.990 11.598  1.00 63.68  ? 273 TRP A CG  1 
ATOM   2013  C CD1 . TRP A  1 273 ? 27.372  18.612 10.473  1.00 61.86  ? 273 TRP A CD1 1 
ATOM   2014  C CD2 . TRP A  1 273 ? 29.159  18.089 11.720  1.00 72.09  ? 273 TRP A CD2 1 
ATOM   2015  N NE1 . TRP A  1 273 ? 27.982  17.533 9.893   1.00 67.60  ? 273 TRP A NE1 1 
ATOM   2016  C CE2 . TRP A  1 273 ? 29.083  17.191 10.634  1.00 72.11  ? 273 TRP A CE2 1 
ATOM   2017  C CE3 . TRP A  1 273 ? 30.204  17.950 12.641  1.00 72.29  ? 273 TRP A CE3 1 
ATOM   2018  C CZ2 . TRP A  1 273 ? 30.017  16.173 10.446  1.00 75.26  ? 273 TRP A CZ2 1 
ATOM   2019  C CZ3 . TRP A  1 273 ? 31.125  16.943 12.454  1.00 74.89  ? 273 TRP A CZ3 1 
ATOM   2020  C CH2 . TRP A  1 273 ? 31.032  16.070 11.370  1.00 78.62  ? 273 TRP A CH2 1 
ATOM   2021  N N   . ILE A  1 274 ? 26.941  21.043 15.532  1.00 76.13  ? 274 ILE A N   1 
ATOM   2022  C CA  . ILE A  1 274 ? 26.932  22.170 16.512  1.00 78.48  ? 274 ILE A CA  1 
ATOM   2023  C C   . ILE A  1 274 ? 28.341  22.299 17.102  1.00 79.42  ? 274 ILE A C   1 
ATOM   2024  O O   . ILE A  1 274 ? 28.791  21.352 17.778  1.00 74.75  ? 274 ILE A O   1 
ATOM   2025  C CB  . ILE A  1 274 ? 25.865  21.952 17.605  1.00 80.66  ? 274 ILE A CB  1 
ATOM   2026  C CG1 . ILE A  1 274 ? 24.462  21.818 17.007  1.00 79.46  ? 274 ILE A CG1 1 
ATOM   2027  C CG2 . ILE A  1 274 ? 25.929  23.059 18.646  1.00 82.89  ? 274 ILE A CG2 1 
ATOM   2028  C CD1 . ILE A  1 274 ? 23.376  21.576 18.030  1.00 77.57  ? 274 ILE A CD1 1 
ATOM   2029  N N   . SER A  1 275 ? 29.010  23.424 16.837  1.00 86.61  ? 275 SER A N   1 
ATOM   2030  C CA  . SER A  1 275 ? 30.393  23.717 17.295  1.00 95.08  ? 275 SER A CA  1 
ATOM   2031  C C   . SER A  1 275 ? 31.345  22.627 16.790  1.00 93.45  ? 275 SER A C   1 
ATOM   2032  O O   . SER A  1 275 ? 32.292  22.281 17.524  1.00 99.43  ? 275 SER A O   1 
ATOM   2033  C CB  . SER A  1 275 ? 30.443  23.845 18.796  1.00 99.06  ? 275 SER A CB  1 
ATOM   2034  O OG  . SER A  1 275 ? 29.584  24.883 19.241  1.00 94.31  ? 275 SER A OG  1 
ATOM   2035  N N   . SER A  1 276 ? 31.082  22.105 15.588  1.00 89.10  ? 276 SER A N   1 
ATOM   2036  C CA  . SER A  1 276 ? 31.949  21.144 14.854  1.00 91.45  ? 276 SER A CA  1 
ATOM   2037  C C   . SER A  1 276 ? 31.755  19.721 15.392  1.00 87.45  ? 276 SER A C   1 
ATOM   2038  O O   . SER A  1 276 ? 32.535  18.833 14.991  1.00 82.66  ? 276 SER A O   1 
ATOM   2039  C CB  . SER A  1 276 ? 33.395  21.558 14.930  1.00 91.51  ? 276 SER A CB  1 
ATOM   2040  O OG  . SER A  1 276 ? 33.575  22.864 14.404  1.00 93.73  ? 276 SER A OG  1 
ATOM   2041  N N   . VAL A  1 277 ? 30.762  19.518 16.264  1.00 77.35  ? 277 VAL A N   1 
ATOM   2042  C CA  . VAL A  1 277 ? 30.412  18.191 16.854  1.00 71.00  ? 277 VAL A CA  1 
ATOM   2043  C C   . VAL A  1 277 ? 29.133  17.683 16.180  1.00 71.08  ? 277 VAL A C   1 
ATOM   2044  O O   . VAL A  1 277 ? 28.093  18.357 16.305  1.00 65.89  ? 277 VAL A O   1 
ATOM   2045  C CB  . VAL A  1 277 ? 30.246  18.278 18.384  1.00 69.31  ? 277 VAL A CB  1 
ATOM   2046  C CG1 . VAL A  1 277 ? 29.824  16.945 18.984  1.00 64.42  ? 277 VAL A CG1 1 
ATOM   2047  C CG2 . VAL A  1 277 ? 31.506  18.795 19.061  1.00 67.61  ? 277 VAL A CG2 1 
ATOM   2048  N N   . LYS A  1 278 ? 29.213  16.541 15.492  1.00 71.23  ? 278 LYS A N   1 
ATOM   2049  C CA  . LYS A  1 278 ? 28.070  15.921 14.771  1.00 68.28  ? 278 LYS A CA  1 
ATOM   2050  C C   . LYS A  1 278 ? 26.975  15.560 15.780  1.00 63.79  ? 278 LYS A C   1 
ATOM   2051  O O   . LYS A  1 278 ? 27.317  15.051 16.863  1.00 62.00  ? 278 LYS A O   1 
ATOM   2052  C CB  . LYS A  1 278 ? 28.527  14.683 13.997  1.00 72.01  ? 278 LYS A CB  1 
ATOM   2053  C CG  . LYS A  1 278 ? 27.463  14.065 13.101  1.00 70.48  ? 278 LYS A CG  1 
ATOM   2054  C CD  . LYS A  1 278 ? 27.915  12.802 12.405  1.00 73.28  ? 278 LYS A CD  1 
ATOM   2055  C CE  . LYS A  1 278 ? 28.978  13.042 11.356  1.00 75.43  ? 278 LYS A CE  1 
ATOM   2056  N NZ  . LYS A  1 278 ? 29.447  11.768 10.762  1.00 79.53  ? 278 LYS A NZ  1 
ATOM   2057  N N   . GLN A  1 279 ? 25.712  15.818 15.427  1.00 60.74  ? 279 GLN A N   1 
ATOM   2058  C CA  . GLN A  1 279 ? 24.526  15.603 16.299  1.00 61.72  ? 279 GLN A CA  1 
ATOM   2059  C C   . GLN A  1 279 ? 23.650  14.495 15.705  1.00 63.21  ? 279 GLN A C   1 
ATOM   2060  O O   . GLN A  1 279 ? 23.226  13.608 16.464  1.00 63.34  ? 279 GLN A O   1 
ATOM   2061  C CB  . GLN A  1 279 ? 23.735  16.904 16.439  1.00 63.72  ? 279 GLN A CB  1 
ATOM   2062  C CG  . GLN A  1 279 ? 24.532  18.022 17.091  1.00 68.04  ? 279 GLN A CG  1 
ATOM   2063  C CD  . GLN A  1 279 ? 24.837  17.722 18.537  1.00 68.83  ? 279 GLN A CD  1 
ATOM   2064  O OE1 . GLN A  1 279 ? 23.961  17.333 19.306  1.00 73.99  ? 279 GLN A OE1 1 
ATOM   2065  N NE2 . GLN A  1 279 ? 26.090  17.906 18.920  1.00 69.04  ? 279 GLN A NE2 1 
ATOM   2066  N N   . SER A  1 280 ? 23.384  14.563 14.398  1.00 65.76  ? 280 SER A N   1 
ATOM   2067  C CA  . SER A  1 280 ? 22.610  13.553 13.631  1.00 65.66  ? 280 SER A CA  1 
ATOM   2068  C C   . SER A  1 280 ? 23.359  13.213 12.338  1.00 69.82  ? 280 SER A C   1 
ATOM   2069  O O   . SER A  1 280 ? 24.268  13.978 11.964  1.00 63.22  ? 280 SER A O   1 
ATOM   2070  C CB  . SER A  1 280 ? 21.213  14.041 13.344  1.00 64.75  ? 280 SER A CB  1 
ATOM   2071  O OG  . SER A  1 280 ? 21.179  14.809 12.150  1.00 69.16  ? 280 SER A OG  1 
ATOM   2072  N N   . ASP A  1 281 ? 22.988  12.104 11.693  1.00 74.76  ? 281 ASP A N   1 
ATOM   2073  C CA  . ASP A  1 281 ? 23.515  11.685 10.367  1.00 70.57  ? 281 ASP A CA  1 
ATOM   2074  C C   . ASP A  1 281 ? 22.432  11.923 9.313   1.00 67.15  ? 281 ASP A C   1 
ATOM   2075  O O   . ASP A  1 281 ? 21.237  11.883 9.668   1.00 60.34  ? 281 ASP A O   1 
ATOM   2076  C CB  . ASP A  1 281 ? 23.960  10.220 10.374  1.00 74.46  ? 281 ASP A CB  1 
ATOM   2077  C CG  . ASP A  1 281 ? 25.315  9.991  11.020  1.00 74.59  ? 281 ASP A CG  1 
ATOM   2078  O OD1 . ASP A  1 281 ? 25.914  8.930  10.761  1.00 78.04  ? 281 ASP A OD1 1 
ATOM   2079  O OD2 . ASP A  1 281 ? 25.756  10.871 11.777  1.00 85.56  ? 281 ASP A OD2 1 
ATOM   2080  N N   . ALA A  1 282 ? 22.843  12.172 8.067   1.00 63.54  ? 282 ALA A N   1 
ATOM   2081  C CA  . ALA A  1 282 ? 21.943  12.338 6.904   1.00 63.46  ? 282 ALA A CA  1 
ATOM   2082  C C   . ALA A  1 282 ? 21.155  11.040 6.703   1.00 61.16  ? 282 ALA A C   1 
ATOM   2083  O O   . ALA A  1 282 ? 21.761  9.958  6.839   1.00 54.88  ? 282 ALA A O   1 
ATOM   2084  C CB  . ALA A  1 282 ? 22.743  12.703 5.678   1.00 64.84  ? 282 ALA A CB  1 
ATOM   2085  N N   . GLY A  1 283 ? 19.857  11.154 6.411   1.00 57.53  ? 283 GLY A N   1 
ATOM   2086  C CA  . GLY A  1 283 ? 18.968  10.010 6.136   1.00 58.75  ? 283 GLY A CA  1 
ATOM   2087  C C   . GLY A  1 283 ? 17.876  10.377 5.148   1.00 60.85  ? 283 GLY A C   1 
ATOM   2088  O O   . GLY A  1 283 ? 17.458  11.554 5.137   1.00 64.74  ? 283 GLY A O   1 
ATOM   2089  N N   . LEU A  1 284 ? 17.437  9.407  4.340   1.00 56.18  ? 284 LEU A N   1 
ATOM   2090  C CA  . LEU A  1 284 ? 16.276  9.541  3.422   1.00 53.18  ? 284 LEU A CA  1 
ATOM   2091  C C   . LEU A  1 284 ? 15.114  8.726  3.977   1.00 50.26  ? 284 LEU A C   1 
ATOM   2092  O O   . LEU A  1 284 ? 15.321  7.750  4.693   1.00 56.46  ? 284 LEU A O   1 
ATOM   2093  C CB  . LEU A  1 284 ? 16.670  9.052  2.025   1.00 55.64  ? 284 LEU A CB  1 
ATOM   2094  C CG  . LEU A  1 284 ? 17.730  9.893  1.316   1.00 58.65  ? 284 LEU A CG  1 
ATOM   2095  C CD1 . LEU A  1 284 ? 18.029  9.344  -0.070  1.00 57.91  ? 284 LEU A CD1 1 
ATOM   2096  C CD2 . LEU A  1 284 ? 17.295  11.346 1.236   1.00 57.07  ? 284 LEU A CD2 1 
ATOM   2097  N N   . PRO A  1 285 ? 13.855  9.115  3.680   1.00 49.42  ? 285 PRO A N   1 
ATOM   2098  C CA  . PRO A  1 285 ? 12.700  8.271  3.978   1.00 50.13  ? 285 PRO A CA  1 
ATOM   2099  C C   . PRO A  1 285 ? 12.714  7.008  3.103   1.00 55.61  ? 285 PRO A C   1 
ATOM   2100  O O   . PRO A  1 285 ? 13.301  7.043  2.036   1.00 57.35  ? 285 PRO A O   1 
ATOM   2101  C CB  . PRO A  1 285 ? 11.484  9.149  3.638   1.00 49.45  ? 285 PRO A CB  1 
ATOM   2102  C CG  . PRO A  1 285 ? 12.034  10.559 3.501   1.00 51.60  ? 285 PRO A CG  1 
ATOM   2103  C CD  . PRO A  1 285 ? 13.476  10.395 3.068   1.00 50.35  ? 285 PRO A CD  1 
ATOM   2104  N N   . ARG A  1 286 ? 12.073  5.931  3.559   1.00 61.80  ? 286 ARG A N   1 
ATOM   2105  C CA  . ARG A  1 286 ? 11.871  4.703  2.743   1.00 67.84  ? 286 ARG A CA  1 
ATOM   2106  C C   . ARG A  1 286 ? 11.030  5.061  1.513   1.00 64.63  ? 286 ARG A C   1 
ATOM   2107  O O   . ARG A  1 286 ? 10.052  5.820  1.673   1.00 65.73  ? 286 ARG A O   1 
ATOM   2108  C CB  . ARG A  1 286 ? 11.190  3.603  3.561   1.00 75.53  ? 286 ARG A CB  1 
ATOM   2109  C CG  . ARG A  1 286 ? 11.444  2.202  3.025   1.00 87.53  ? 286 ARG A CG  1 
ATOM   2110  C CD  . ARG A  1 286 ? 12.893  1.790  3.198   1.00 93.30  ? 286 ARG A CD  1 
ATOM   2111  N NE  . ARG A  1 286 ? 13.192  0.519  2.554   1.00 97.29  ? 286 ARG A NE  1 
ATOM   2112  C CZ  . ARG A  1 286 ? 14.356  -0.114 2.645   1.00 99.39  ? 286 ARG A CZ  1 
ATOM   2113  N NH1 . ARG A  1 286 ? 14.534  -1.267 2.021   1.00 103.06 ? 286 ARG A NH1 1 
ATOM   2114  N NH2 . ARG A  1 286 ? 15.338  0.405  3.360   1.00 98.01  ? 286 ARG A NH2 1 
ATOM   2115  N N   . GLU A  1 287 ? 11.411  4.553  0.336   1.00 57.08  ? 287 GLU A N   1 
ATOM   2116  C CA  . GLU A  1 287 ? 10.631  4.686  -0.924  1.00 55.07  ? 287 GLU A CA  1 
ATOM   2117  C C   . GLU A  1 287 ? 9.265   4.019  -0.728  1.00 52.79  ? 287 GLU A C   1 
ATOM   2118  O O   . GLU A  1 287 ? 9.209   2.973  -0.053  1.00 53.23  ? 287 GLU A O   1 
ATOM   2119  C CB  . GLU A  1 287 ? 11.384  4.059  -2.097  1.00 53.09  ? 287 GLU A CB  1 
ATOM   2120  C CG  . GLU A  1 287 ? 12.588  4.865  -2.539  1.00 54.67  ? 287 GLU A CG  1 
ATOM   2121  C CD  . GLU A  1 287 ? 13.346  4.261  -3.708  1.00 60.13  ? 287 GLU A CD  1 
ATOM   2122  O OE1 . GLU A  1 287 ? 12.759  3.425  -4.420  1.00 66.44  ? 287 GLU A OE1 1 
ATOM   2123  O OE2 . GLU A  1 287 ? 14.521  4.627  -3.901  1.00 64.40  ? 287 GLU A OE2 1 
ATOM   2124  N N   . VAL A  1 288 ? 8.211   4.600  -1.305  1.00 52.35  ? 288 VAL A N   1 
ATOM   2125  C CA  . VAL A  1 288 ? 6.796   4.198  -1.054  1.00 55.92  ? 288 VAL A CA  1 
ATOM   2126  C C   . VAL A  1 288 ? 6.131   3.810  -2.379  1.00 65.01  ? 288 VAL A C   1 
ATOM   2127  O O   . VAL A  1 288 ? 6.304   4.544  -3.375  1.00 61.76  ? 288 VAL A O   1 
ATOM   2128  C CB  . VAL A  1 288 ? 6.022   5.323  -0.340  1.00 61.37  ? 288 VAL A CB  1 
ATOM   2129  C CG1 . VAL A  1 288 ? 4.549   4.982  -0.173  1.00 66.44  ? 288 VAL A CG1 1 
ATOM   2130  C CG2 . VAL A  1 288 ? 6.647   5.668  1.003   1.00 62.03  ? 288 VAL A CG2 1 
ATOM   2131  N N   . TYR A  1 289 ? 5.414   2.681  -2.369  1.00 77.46  ? 289 TYR A N   1 
ATOM   2132  C CA  . TYR A  1 289 ? 4.587   2.150  -3.485  1.00 75.80  ? 289 TYR A CA  1 
ATOM   2133  C C   . TYR A  1 289 ? 3.146   2.626  -3.264  1.00 77.18  ? 289 TYR A C   1 
ATOM   2134  O O   . TYR A  1 289 ? 2.695   2.599  -2.103  1.00 81.74  ? 289 TYR A O   1 
ATOM   2135  C CB  . TYR A  1 289 ? 4.693   0.622  -3.519  1.00 73.82  ? 289 TYR A CB  1 
ATOM   2136  C CG  . TYR A  1 289 ? 4.689   -0.002 -4.891  1.00 85.77  ? 289 TYR A CG  1 
ATOM   2137  C CD1 . TYR A  1 289 ? 3.503   -0.289 -5.545  1.00 95.54  ? 289 TYR A CD1 1 
ATOM   2138  C CD2 . TYR A  1 289 ? 5.876   -0.332 -5.526  1.00 85.67  ? 289 TYR A CD2 1 
ATOM   2139  C CE1 . TYR A  1 289 ? 3.493   -0.874 -6.800  1.00 101.97 ? 289 TYR A CE1 1 
ATOM   2140  C CE2 . TYR A  1 289 ? 5.885   -0.918 -6.781  1.00 90.55  ? 289 TYR A CE2 1 
ATOM   2141  C CZ  . TYR A  1 289 ? 4.688   -1.190 -7.421  1.00 101.03 ? 289 TYR A CZ  1 
ATOM   2142  O OH  . TYR A  1 289 ? 4.679   -1.767 -8.658  1.00 105.90 ? 289 TYR A OH  1 
ATOM   2143  N N   . LEU A  1 290 ? 2.460   3.073  -4.320  1.00 76.42  ? 290 LEU A N   1 
ATOM   2144  C CA  . LEU A  1 290 ? 1.132   3.734  -4.205  1.00 80.97  ? 290 LEU A CA  1 
ATOM   2145  C C   . LEU A  1 290 ? 0.027   2.803  -4.718  1.00 93.01  ? 290 LEU A C   1 
ATOM   2146  O O   . LEU A  1 290 ? 0.245   2.126  -5.744  1.00 89.92  ? 290 LEU A O   1 
ATOM   2147  C CB  . LEU A  1 290 ? 1.167   5.058  -4.974  1.00 83.05  ? 290 LEU A CB  1 
ATOM   2148  C CG  . LEU A  1 290 ? 2.110   6.116  -4.402  1.00 85.42  ? 290 LEU A CG  1 
ATOM   2149  C CD1 . LEU A  1 290 ? 1.966   7.436  -5.145  1.00 82.22  ? 290 LEU A CD1 1 
ATOM   2150  C CD2 . LEU A  1 290 ? 1.869   6.317  -2.913  1.00 83.56  ? 290 LEU A CD2 1 
ATOM   2151  N N   . ALA A  1 291 ? -1.104  2.776  -4.004  1.00 96.29  ? 291 ALA A N   1 
ATOM   2152  C CA  . ALA A  1 291 ? -2.297  1.943  -4.286  1.00 100.85 ? 291 ALA A CA  1 
ATOM   2153  C C   . ALA A  1 291 ? -2.771  2.182  -5.725  1.00 105.90 ? 291 ALA A C   1 
ATOM   2154  O O   . ALA A  1 291 ? -3.871  1.780  -6.107  1.00 95.77  ? 291 ALA A O   1 
ATOM   2155  C CB  . ALA A  1 291 ? -3.385  2.259  -3.287  1.00 91.27  ? 291 ALA A CB  1 
ATOM   2156  N N   . ASN B  1 5   ? 49.516  69.651 12.961  1.00 104.88 ? 5   ASN B N   1 
ATOM   2157  C CA  . ASN B  1 5   ? 48.130  69.298 12.531  1.00 113.43 ? 5   ASN B CA  1 
ATOM   2158  C C   . ASN B  1 5   ? 48.213  68.206 11.455  1.00 116.88 ? 5   ASN B C   1 
ATOM   2159  O O   . ASN B  1 5   ? 49.217  68.183 10.721  1.00 145.54 ? 5   ASN B O   1 
ATOM   2160  C CB  . ASN B  1 5   ? 47.368  70.533 12.037  1.00 106.67 ? 5   ASN B CB  1 
ATOM   2161  C CG  . ASN B  1 5   ? 45.978  70.657 12.629  1.00 101.72 ? 5   ASN B CG  1 
ATOM   2162  O OD1 . ASN B  1 5   ? 45.581  69.863 13.478  1.00 104.41 ? 5   ASN B OD1 1 
ATOM   2163  N ND2 . ASN B  1 5   ? 45.233  71.659 12.193  1.00 94.30  ? 5   ASN B ND2 1 
ATOM   2164  N N   . VAL B  1 6   ? 47.198  67.338 11.378  1.00 102.12 ? 6   VAL B N   1 
ATOM   2165  C CA  . VAL B  1 6   ? 47.110  66.198 10.415  1.00 93.10  ? 6   VAL B CA  1 
ATOM   2166  C C   . VAL B  1 6   ? 46.452  66.694 9.122   1.00 85.91  ? 6   VAL B C   1 
ATOM   2167  O O   . VAL B  1 6   ? 45.352  67.274 9.213   1.00 86.24  ? 6   VAL B O   1 
ATOM   2168  C CB  . VAL B  1 6   ? 46.324  65.018 11.022  1.00 90.55  ? 6   VAL B CB  1 
ATOM   2169  C CG1 . VAL B  1 6   ? 46.060  63.919 10.004  1.00 88.80  ? 6   VAL B CG1 1 
ATOM   2170  C CG2 . VAL B  1 6   ? 47.017  64.444 12.248  1.00 98.81  ? 6   VAL B CG2 1 
ATOM   2171  N N   . SER B  1 7   ? 47.085  66.447 7.968   1.00 74.56  ? 7   SER B N   1 
ATOM   2172  C CA  . SER B  1 7   ? 46.581  66.831 6.621   1.00 69.29  ? 7   SER B CA  1 
ATOM   2173  C C   . SER B  1 7   ? 45.496  65.848 6.158   1.00 62.35  ? 7   SER B C   1 
ATOM   2174  O O   . SER B  1 7   ? 45.827  64.884 5.438   1.00 58.77  ? 7   SER B O   1 
ATOM   2175  C CB  . SER B  1 7   ? 47.704  66.910 5.620   1.00 77.99  ? 7   SER B CB  1 
ATOM   2176  O OG  . SER B  1 7   ? 48.859  67.508 6.189   1.00 85.55  ? 7   SER B OG  1 
ATOM   2177  N N   . VAL B  1 8   ? 44.244  66.097 6.550   1.00 60.08  ? 8   VAL B N   1 
ATOM   2178  C CA  . VAL B  1 8   ? 43.064  65.253 6.193   1.00 53.61  ? 8   VAL B CA  1 
ATOM   2179  C C   . VAL B  1 8   ? 43.022  65.091 4.676   1.00 52.07  ? 8   VAL B C   1 
ATOM   2180  O O   . VAL B  1 8   ? 43.161  66.061 3.934   1.00 53.96  ? 8   VAL B O   1 
ATOM   2181  C CB  . VAL B  1 8   ? 41.753  65.852 6.738   1.00 46.91  ? 8   VAL B CB  1 
ATOM   2182  C CG1 . VAL B  1 8   ? 41.721  65.840 8.259   1.00 44.34  ? 8   VAL B CG1 1 
ATOM   2183  C CG2 . VAL B  1 8   ? 41.508  67.253 6.201   1.00 51.87  ? 8   VAL B CG2 1 
ATOM   2184  N N   . PRO B  1 9   ? 42.830  63.850 4.176   1.00 48.69  ? 9   PRO B N   1 
ATOM   2185  C CA  . PRO B  1 9   ? 42.880  63.567 2.742   1.00 49.06  ? 9   PRO B CA  1 
ATOM   2186  C C   . PRO B  1 9   ? 41.677  64.124 1.964   1.00 47.39  ? 9   PRO B C   1 
ATOM   2187  O O   . PRO B  1 9   ? 41.772  64.237 0.756   1.00 54.50  ? 9   PRO B O   1 
ATOM   2188  C CB  . PRO B  1 9   ? 42.875  62.030 2.657   1.00 50.42  ? 9   PRO B CB  1 
ATOM   2189  C CG  . PRO B  1 9   ? 43.101  61.544 4.082   1.00 49.85  ? 9   PRO B CG  1 
ATOM   2190  C CD  . PRO B  1 9   ? 42.567  62.644 4.972   1.00 49.20  ? 9   PRO B CD  1 
ATOM   2191  N N   . TRP B  1 10  ? 40.586  64.445 2.666   1.00 44.21  ? 10  TRP B N   1 
ATOM   2192  C CA  . TRP B  1 10  ? 39.334  64.989 2.073   1.00 44.64  ? 10  TRP B CA  1 
ATOM   2193  C C   . TRP B  1 10  ? 39.421  66.517 1.971   1.00 44.67  ? 10  TRP B C   1 
ATOM   2194  O O   . TRP B  1 10  ? 38.375  67.157 1.746   1.00 53.63  ? 10  TRP B O   1 
ATOM   2195  C CB  . TRP B  1 10  ? 38.110  64.540 2.880   1.00 44.25  ? 10  TRP B CB  1 
ATOM   2196  C CG  . TRP B  1 10  ? 38.191  64.832 4.346   1.00 43.37  ? 10  TRP B CG  1 
ATOM   2197  C CD1 . TRP B  1 10  ? 37.857  65.997 4.971   1.00 42.48  ? 10  TRP B CD1 1 
ATOM   2198  C CD2 . TRP B  1 10  ? 38.616  63.927 5.382   1.00 45.29  ? 10  TRP B CD2 1 
ATOM   2199  N NE1 . TRP B  1 10  ? 38.046  65.882 6.322   1.00 45.77  ? 10  TRP B NE1 1 
ATOM   2200  C CE2 . TRP B  1 10  ? 38.512  64.624 6.604   1.00 46.44  ? 10  TRP B CE2 1 
ATOM   2201  C CE3 . TRP B  1 10  ? 39.070  62.603 5.399   1.00 47.83  ? 10  TRP B CE3 1 
ATOM   2202  C CZ2 . TRP B  1 10  ? 38.852  64.040 7.824   1.00 46.72  ? 10  TRP B CZ2 1 
ATOM   2203  C CZ3 . TRP B  1 10  ? 39.401  62.027 6.606   1.00 46.62  ? 10  TRP B CZ3 1 
ATOM   2204  C CH2 . TRP B  1 10  ? 39.295  62.738 7.801   1.00 44.07  ? 10  TRP B CH2 1 
ATOM   2205  N N   . GLY B  1 11  ? 40.627  67.073 2.124   1.00 41.23  ? 11  GLY B N   1 
ATOM   2206  C CA  . GLY B  1 11  ? 40.910  68.507 1.929   1.00 40.27  ? 11  GLY B CA  1 
ATOM   2207  C C   . GLY B  1 11  ? 41.503  68.774 0.556   1.00 41.19  ? 11  GLY B C   1 
ATOM   2208  O O   . GLY B  1 11  ? 41.341  69.900 0.049   1.00 43.50  ? 11  GLY B O   1 
ATOM   2209  N N   . ALA B  1 12  ? 42.151  67.764 -0.032  1.00 41.54  ? 12  ALA B N   1 
ATOM   2210  C CA  . ALA B  1 12  ? 42.905  67.852 -1.305  1.00 43.32  ? 12  ALA B CA  1 
ATOM   2211  C C   . ALA B  1 12  ? 41.946  67.898 -2.499  1.00 40.77  ? 12  ALA B C   1 
ATOM   2212  O O   . ALA B  1 12  ? 41.049  67.039 -2.569  1.00 44.77  ? 12  ALA B O   1 
ATOM   2213  C CB  . ALA B  1 12  ? 43.840  66.676 -1.415  1.00 46.54  ? 12  ALA B CB  1 
ATOM   2214  N N   . THR B  1 13  ? 42.152  68.857 -3.407  1.00 41.89  ? 13  THR B N   1 
ATOM   2215  C CA  . THR B  1 13  ? 41.437  68.974 -4.707  1.00 42.21  ? 13  THR B CA  1 
ATOM   2216  C C   . THR B  1 13  ? 41.994  67.919 -5.670  1.00 42.28  ? 13  THR B C   1 
ATOM   2217  O O   . THR B  1 13  ? 43.218  67.695 -5.650  1.00 45.24  ? 13  THR B O   1 
ATOM   2218  C CB  . THR B  1 13  ? 41.563  70.393 -5.278  1.00 40.46  ? 13  THR B CB  1 
ATOM   2219  O OG1 . THR B  1 13  ? 40.886  71.280 -4.387  1.00 41.74  ? 13  THR B OG1 1 
ATOM   2220  C CG2 . THR B  1 13  ? 40.996  70.529 -6.674  1.00 38.86  ? 13  THR B CG2 1 
ATOM   2221  N N   . LEU B  1 14  ? 41.126  67.298 -6.473  1.00 42.32  ? 14  LEU B N   1 
ATOM   2222  C CA  . LEU B  1 14  ? 41.495  66.214 -7.423  1.00 45.15  ? 14  LEU B CA  1 
ATOM   2223  C C   . LEU B  1 14  ? 41.436  66.750 -8.855  1.00 43.68  ? 14  LEU B C   1 
ATOM   2224  O O   . LEU B  1 14  ? 40.493  67.499 -9.158  1.00 44.36  ? 14  LEU B O   1 
ATOM   2225  C CB  . LEU B  1 14  ? 40.522  65.043 -7.260  1.00 49.06  ? 14  LEU B CB  1 
ATOM   2226  C CG  . LEU B  1 14  ? 40.424  64.446 -5.858  1.00 53.65  ? 14  LEU B CG  1 
ATOM   2227  C CD1 . LEU B  1 14  ? 39.286  63.439 -5.782  1.00 58.06  ? 14  LEU B CD1 1 
ATOM   2228  C CD2 . LEU B  1 14  ? 41.738  63.805 -5.448  1.00 54.97  ? 14  LEU B CD2 1 
ATOM   2229  N N   . SER B  1 15  ? 42.396  66.361 -9.700  1.00 44.45  ? 15  SER B N   1 
ATOM   2230  C CA  . SER B  1 15  ? 42.349  66.555 -11.172 1.00 47.80  ? 15  SER B CA  1 
ATOM   2231  C C   . SER B  1 15  ? 41.220  65.690 -11.745 1.00 54.56  ? 15  SER B C   1 
ATOM   2232  O O   . SER B  1 15  ? 40.664  64.866 -10.990 1.00 68.08  ? 15  SER B O   1 
ATOM   2233  C CB  . SER B  1 15  ? 43.673  66.223 -11.812 1.00 48.09  ? 15  SER B CB  1 
ATOM   2234  O OG  . SER B  1 15  ? 43.938  64.830 -11.739 1.00 50.24  ? 15  SER B OG  1 
ATOM   2235  N N   . ASN B  1 16  ? 40.886  65.874 -13.024 1.00 54.83  ? 16  ASN B N   1 
ATOM   2236  C CA  . ASN B  1 16  ? 39.872  65.048 -13.731 1.00 52.82  ? 16  ASN B CA  1 
ATOM   2237  C C   . ASN B  1 16  ? 40.396  63.612 -13.832 1.00 54.09  ? 16  ASN B C   1 
ATOM   2238  O O   . ASN B  1 16  ? 39.621  62.679 -13.544 1.00 60.53  ? 16  ASN B O   1 
ATOM   2239  C CB  . ASN B  1 16  ? 39.521  65.633 -15.100 1.00 50.73  ? 16  ASN B CB  1 
ATOM   2240  C CG  . ASN B  1 16  ? 38.650  66.865 -14.992 1.00 51.76  ? 16  ASN B CG  1 
ATOM   2241  O OD1 . ASN B  1 16  ? 38.341  67.317 -13.892 1.00 53.06  ? 16  ASN B OD1 1 
ATOM   2242  N ND2 . ASN B  1 16  ? 38.241  67.409 -16.125 1.00 56.45  ? 16  ASN B ND2 1 
ATOM   2243  N N   . ALA B  1 17  ? 41.667  63.451 -14.213 1.00 51.61  ? 17  ALA B N   1 
ATOM   2244  C CA  . ALA B  1 17  ? 42.362  62.147 -14.322 1.00 52.81  ? 17  ALA B CA  1 
ATOM   2245  C C   . ALA B  1 17  ? 42.192  61.369 -13.012 1.00 53.94  ? 17  ALA B C   1 
ATOM   2246  O O   . ALA B  1 17  ? 41.825  60.180 -13.070 1.00 53.13  ? 17  ALA B O   1 
ATOM   2247  C CB  . ALA B  1 17  ? 43.818  62.363 -14.652 1.00 50.30  ? 17  ALA B CB  1 
ATOM   2248  N N   . GLU B  1 18  ? 42.444  62.026 -11.876 1.00 55.12  ? 18  GLU B N   1 
ATOM   2249  C CA  . GLU B  1 18  ? 42.373  61.420 -10.519 1.00 60.21  ? 18  GLU B CA  1 
ATOM   2250  C C   . GLU B  1 18  ? 40.922  61.025 -10.219 1.00 52.97  ? 18  GLU B C   1 
ATOM   2251  O O   . GLU B  1 18  ? 40.690  59.848 -9.866  1.00 50.95  ? 18  GLU B O   1 
ATOM   2252  C CB  . GLU B  1 18  ? 42.939  62.392 -9.480  1.00 64.51  ? 18  GLU B CB  1 
ATOM   2253  C CG  . GLU B  1 18  ? 44.449  62.549 -9.561  1.00 64.37  ? 18  GLU B CG  1 
ATOM   2254  C CD  . GLU B  1 18  ? 45.020  63.743 -8.813  1.00 66.98  ? 18  GLU B CD  1 
ATOM   2255  O OE1 . GLU B  1 18  ? 46.187  63.660 -8.374  1.00 70.20  ? 18  GLU B OE1 1 
ATOM   2256  O OE2 . GLU B  1 18  ? 44.303  64.755 -8.677  1.00 69.66  ? 18  GLU B OE2 1 
ATOM   2257  N N   . HIS B  1 19  ? 39.986  61.968 -10.373 1.00 51.11  ? 19  HIS B N   1 
ATOM   2258  C CA  . HIS B  1 19  ? 38.532  61.773 -10.121 1.00 53.28  ? 19  HIS B CA  1 
ATOM   2259  C C   . HIS B  1 19  ? 38.017  60.588 -10.948 1.00 54.13  ? 19  HIS B C   1 
ATOM   2260  O O   . HIS B  1 19  ? 37.159  59.839 -10.440 1.00 44.97  ? 19  HIS B O   1 
ATOM   2261  C CB  . HIS B  1 19  ? 37.751  63.061 -10.423 1.00 46.96  ? 19  HIS B CB  1 
ATOM   2262  C CG  . HIS B  1 19  ? 36.323  63.016 -9.991  1.00 46.20  ? 19  HIS B CG  1 
ATOM   2263  N ND1 . HIS B  1 19  ? 35.298  62.657 -10.850 1.00 47.96  ? 19  HIS B ND1 1 
ATOM   2264  C CD2 . HIS B  1 19  ? 35.743  63.284 -8.800  1.00 45.58  ? 19  HIS B CD2 1 
ATOM   2265  C CE1 . HIS B  1 19  ? 34.150  62.708 -10.205 1.00 52.00  ? 19  HIS B CE1 1 
ATOM   2266  N NE2 . HIS B  1 19  ? 34.396  63.087 -8.943  1.00 47.89  ? 19  HIS B NE2 1 
ATOM   2267  N N   . GLN B  1 20  ? 38.522  60.433 -12.175 1.00 52.16  ? 20  GLN B N   1 
ATOM   2268  C CA  . GLN B  1 20  ? 38.105  59.367 -13.124 1.00 56.61  ? 20  GLN B CA  1 
ATOM   2269  C C   . GLN B  1 20  ? 38.663  58.022 -12.640 1.00 55.31  ? 20  GLN B C   1 
ATOM   2270  O O   . GLN B  1 20  ? 37.924  57.021 -12.695 1.00 61.12  ? 20  GLN B O   1 
ATOM   2271  C CB  . GLN B  1 20  ? 38.590  59.697 -14.536 1.00 60.39  ? 20  GLN B CB  1 
ATOM   2272  C CG  . GLN B  1 20  ? 37.712  59.115 -15.634 1.00 63.20  ? 20  GLN B CG  1 
ATOM   2273  C CD  . GLN B  1 20  ? 36.501  59.973 -15.905 1.00 64.25  ? 20  GLN B CD  1 
ATOM   2274  O OE1 . GLN B  1 20  ? 36.468  61.155 -15.575 1.00 73.99  ? 20  GLN B OE1 1 
ATOM   2275  N NE2 . GLN B  1 20  ? 35.490  59.380 -16.519 1.00 67.22  ? 20  GLN B NE2 1 
ATOM   2276  N N   . LEU B  1 21  ? 39.918  58.012 -12.180 1.00 50.26  ? 21  LEU B N   1 
ATOM   2277  C CA  . LEU B  1 21  ? 40.634  56.797 -11.708 1.00 48.60  ? 21  LEU B CA  1 
ATOM   2278  C C   . LEU B  1 21  ? 39.944  56.247 -10.456 1.00 48.84  ? 21  LEU B C   1 
ATOM   2279  O O   . LEU B  1 21  ? 39.677  55.031 -10.416 1.00 51.52  ? 21  LEU B O   1 
ATOM   2280  C CB  . LEU B  1 21  ? 42.097  57.151 -11.419 1.00 48.52  ? 21  LEU B CB  1 
ATOM   2281  C CG  . LEU B  1 21  ? 43.032  57.134 -12.628 1.00 45.84  ? 21  LEU B CG  1 
ATOM   2282  C CD1 . LEU B  1 21  ? 44.435  57.564 -12.230 1.00 45.90  ? 21  LEU B CD1 1 
ATOM   2283  C CD2 . LEU B  1 21  ? 43.060  55.759 -13.280 1.00 43.92  ? 21  LEU B CD2 1 
ATOM   2284  N N   . ILE B  1 22  ? 39.674  57.110 -9.473  1.00 44.75  ? 22  ILE B N   1 
ATOM   2285  C CA  . ILE B  1 22  ? 39.041  56.731 -8.175  1.00 43.98  ? 22  ILE B CA  1 
ATOM   2286  C C   . ILE B  1 22  ? 37.704  56.043 -8.469  1.00 44.99  ? 22  ILE B C   1 
ATOM   2287  O O   . ILE B  1 22  ? 37.513  54.900 -8.009  1.00 52.90  ? 22  ILE B O   1 
ATOM   2288  C CB  . ILE B  1 22  ? 38.872  57.962 -7.263  1.00 44.27  ? 22  ILE B CB  1 
ATOM   2289  C CG1 . ILE B  1 22  ? 40.227  58.554 -6.870  1.00 49.02  ? 22  ILE B CG1 1 
ATOM   2290  C CG2 . ILE B  1 22  ? 38.030  57.623 -6.041  1.00 40.21  ? 22  ILE B CG2 1 
ATOM   2291  C CD1 . ILE B  1 22  ? 40.147  59.953 -6.308  1.00 53.35  ? 22  ILE B CD1 1 
ATOM   2292  N N   . PHE B  1 23  ? 36.825  56.711 -9.221  1.00 43.43  ? 23  PHE B N   1 
ATOM   2293  C CA  . PHE B  1 23  ? 35.478  56.210 -9.599  1.00 43.55  ? 23  PHE B CA  1 
ATOM   2294  C C   . PHE B  1 23  ? 35.611  54.836 -10.262 1.00 44.85  ? 23  PHE B C   1 
ATOM   2295  O O   . PHE B  1 23  ? 34.892  53.900 -9.860  1.00 46.60  ? 23  PHE B O   1 
ATOM   2296  C CB  . PHE B  1 23  ? 34.778  57.201 -10.530 1.00 43.02  ? 23  PHE B CB  1 
ATOM   2297  C CG  . PHE B  1 23  ? 33.375  56.809 -10.917 1.00 45.23  ? 23  PHE B CG  1 
ATOM   2298  C CD1 . PHE B  1 23  ? 33.091  56.369 -12.200 1.00 49.33  ? 23  PHE B CD1 1 
ATOM   2299  C CD2 . PHE B  1 23  ? 32.341  56.874 -9.997  1.00 42.19  ? 23  PHE B CD2 1 
ATOM   2300  C CE1 . PHE B  1 23  ? 31.801  56.010 -12.556 1.00 49.36  ? 23  PHE B CE1 1 
ATOM   2301  C CE2 . PHE B  1 23  ? 31.051  56.515 -10.355 1.00 42.63  ? 23  PHE B CE2 1 
ATOM   2302  C CZ  . PHE B  1 23  ? 30.784  56.083 -11.633 1.00 48.34  ? 23  PHE B CZ  1 
ATOM   2303  N N   . TYR B  1 24  ? 36.504  54.729 -11.251 1.00 38.50  ? 24  TYR B N   1 
ATOM   2304  C CA  . TYR B  1 24  ? 36.797  53.487 -12.011 1.00 38.18  ? 24  TYR B CA  1 
ATOM   2305  C C   . TYR B  1 24  ? 37.000  52.326 -11.032 1.00 40.40  ? 24  TYR B C   1 
ATOM   2306  O O   . TYR B  1 24  ? 36.254  51.330 -11.118 1.00 40.31  ? 24  TYR B O   1 
ATOM   2307  C CB  . TYR B  1 24  ? 38.024  53.692 -12.903 1.00 41.11  ? 24  TYR B CB  1 
ATOM   2308  C CG  . TYR B  1 24  ? 38.485  52.466 -13.651 1.00 45.89  ? 24  TYR B CG  1 
ATOM   2309  C CD1 . TYR B  1 24  ? 39.482  51.651 -13.141 1.00 46.20  ? 24  TYR B CD1 1 
ATOM   2310  C CD2 . TYR B  1 24  ? 37.937  52.126 -14.878 1.00 47.26  ? 24  TYR B CD2 1 
ATOM   2311  C CE1 . TYR B  1 24  ? 39.919  50.527 -13.823 1.00 45.25  ? 24  TYR B CE1 1 
ATOM   2312  C CE2 . TYR B  1 24  ? 38.362  51.006 -15.574 1.00 46.30  ? 24  TYR B CE2 1 
ATOM   2313  C CZ  . TYR B  1 24  ? 39.356  50.203 -15.044 1.00 45.47  ? 24  TYR B CZ  1 
ATOM   2314  O OH  . TYR B  1 24  ? 39.779  49.098 -15.722 1.00 44.74  ? 24  TYR B OH  1 
ATOM   2315  N N   . PHE B  1 25  ? 37.972  52.459 -10.124 1.00 39.10  ? 25  PHE B N   1 
ATOM   2316  C CA  . PHE B  1 25  ? 38.386  51.403 -9.162  1.00 40.26  ? 25  PHE B CA  1 
ATOM   2317  C C   . PHE B  1 25  ? 37.247  51.128 -8.176  1.00 39.28  ? 25  PHE B C   1 
ATOM   2318  O O   . PHE B  1 25  ? 37.003  49.944 -7.865  1.00 42.26  ? 25  PHE B O   1 
ATOM   2319  C CB  . PHE B  1 25  ? 39.687  51.795 -8.458  1.00 43.54  ? 25  PHE B CB  1 
ATOM   2320  C CG  . PHE B  1 25  ? 40.921  51.519 -9.279  1.00 52.27  ? 25  PHE B CG  1 
ATOM   2321  C CD1 . PHE B  1 25  ? 41.459  50.243 -9.341  1.00 58.55  ? 25  PHE B CD1 1 
ATOM   2322  C CD2 . PHE B  1 25  ? 41.523  52.523 -10.019 1.00 56.77  ? 25  PHE B CD2 1 
ATOM   2323  C CE1 . PHE B  1 25  ? 42.583  49.984 -10.110 1.00 57.51  ? 25  PHE B CE1 1 
ATOM   2324  C CE2 . PHE B  1 25  ? 42.649  52.263 -10.785 1.00 55.06  ? 25  PHE B CE2 1 
ATOM   2325  C CZ  . PHE B  1 25  ? 43.176  50.994 -10.831 1.00 53.65  ? 25  PHE B CZ  1 
ATOM   2326  N N   . LEU B  1 26  ? 36.570  52.181 -7.710  1.00 35.77  ? 26  LEU B N   1 
ATOM   2327  C CA  . LEU B  1 26  ? 35.411  52.075 -6.784  1.00 39.35  ? 26  LEU B CA  1 
ATOM   2328  C C   . LEU B  1 26  ? 34.356  51.144 -7.392  1.00 42.25  ? 26  LEU B C   1 
ATOM   2329  O O   . LEU B  1 26  ? 33.991  50.151 -6.730  1.00 40.96  ? 26  LEU B O   1 
ATOM   2330  C CB  . LEU B  1 26  ? 34.828  53.468 -6.530  1.00 38.95  ? 26  LEU B CB  1 
ATOM   2331  C CG  . LEU B  1 26  ? 35.489  54.262 -5.406  1.00 40.73  ? 26  LEU B CG  1 
ATOM   2332  C CD1 . LEU B  1 26  ? 34.692  55.519 -5.096  1.00 44.22  ? 26  LEU B CD1 1 
ATOM   2333  C CD2 . LEU B  1 26  ? 35.645  53.406 -4.158  1.00 40.95  ? 26  LEU B CD2 1 
ATOM   2334  N N   . VAL B  1 27  ? 33.891  51.459 -8.606  1.00 40.41  ? 27  VAL B N   1 
ATOM   2335  C CA  . VAL B  1 27  ? 32.772  50.743 -9.286  1.00 39.27  ? 27  VAL B CA  1 
ATOM   2336  C C   . VAL B  1 27  ? 33.249  49.347 -9.696  1.00 40.62  ? 27  VAL B C   1 
ATOM   2337  O O   . VAL B  1 27  ? 32.485  48.385 -9.486  1.00 44.55  ? 27  VAL B O   1 
ATOM   2338  C CB  . VAL B  1 27  ? 32.236  51.529 -10.495 1.00 37.80  ? 27  VAL B CB  1 
ATOM   2339  C CG1 . VAL B  1 27  ? 31.100  50.787 -11.182 1.00 36.21  ? 27  VAL B CG1 1 
ATOM   2340  C CG2 . VAL B  1 27  ? 31.794  52.927 -10.098 1.00 39.07  ? 27  VAL B CG2 1 
ATOM   2341  N N   . VAL B  1 28  ? 34.458  49.242 -10.259 1.00 39.01  ? 28  VAL B N   1 
ATOM   2342  C CA  . VAL B  1 28  ? 35.075  47.939 -10.650 1.00 38.61  ? 28  VAL B CA  1 
ATOM   2343  C C   . VAL B  1 28  ? 35.046  47.017 -9.426  1.00 37.68  ? 28  VAL B C   1 
ATOM   2344  O O   . VAL B  1 28  ? 34.674  45.840 -9.580  1.00 36.42  ? 28  VAL B O   1 
ATOM   2345  C CB  . VAL B  1 28  ? 36.506  48.113 -11.193 1.00 39.71  ? 28  VAL B CB  1 
ATOM   2346  C CG1 . VAL B  1 28  ? 37.215  46.774 -11.328 1.00 42.54  ? 28  VAL B CG1 1 
ATOM   2347  C CG2 . VAL B  1 28  ? 36.524  48.858 -12.519 1.00 37.96  ? 28  VAL B CG2 1 
ATOM   2348  N N   . ALA B  1 29  ? 35.414  47.548 -8.257  1.00 39.91  ? 29  ALA B N   1 
ATOM   2349  C CA  . ALA B  1 29  ? 35.383  46.843 -6.955  1.00 40.70  ? 29  ALA B CA  1 
ATOM   2350  C C   . ALA B  1 29  ? 33.967  46.320 -6.698  1.00 43.76  ? 29  ALA B C   1 
ATOM   2351  O O   . ALA B  1 29  ? 33.803  45.094 -6.574  1.00 47.98  ? 29  ALA B O   1 
ATOM   2352  C CB  . ALA B  1 29  ? 35.833  47.774 -5.855  1.00 42.08  ? 29  ALA B CB  1 
ATOM   2353  N N   . ALA B  1 30  ? 32.990  47.229 -6.627  1.00 48.76  ? 30  ALA B N   1 
ATOM   2354  C CA  . ALA B  1 30  ? 31.563  46.937 -6.358  1.00 48.09  ? 30  ALA B CA  1 
ATOM   2355  C C   . ALA B  1 30  ? 31.093  45.782 -7.249  1.00 43.52  ? 30  ALA B C   1 
ATOM   2356  O O   . ALA B  1 30  ? 30.449  44.853 -6.723  1.00 46.85  ? 30  ALA B O   1 
ATOM   2357  C CB  . ALA B  1 30  ? 30.734  48.179 -6.583  1.00 46.76  ? 30  ALA B CB  1 
ATOM   2358  N N   . LEU B  1 31  ? 31.415  45.839 -8.545  1.00 38.40  ? 31  LEU B N   1 
ATOM   2359  C CA  . LEU B  1 31  ? 30.978  44.845 -9.563  1.00 41.46  ? 31  LEU B CA  1 
ATOM   2360  C C   . LEU B  1 31  ? 31.704  43.516 -9.328  1.00 41.90  ? 31  LEU B C   1 
ATOM   2361  O O   . LEU B  1 31  ? 31.057  42.462 -9.456  1.00 37.89  ? 31  LEU B O   1 
ATOM   2362  C CB  . LEU B  1 31  ? 31.267  45.397 -10.961 1.00 44.01  ? 31  LEU B CB  1 
ATOM   2363  C CG  . LEU B  1 31  ? 30.452  46.627 -11.356 1.00 47.13  ? 31  LEU B CG  1 
ATOM   2364  C CD1 . LEU B  1 31  ? 30.964  47.217 -12.660 1.00 46.42  ? 31  LEU B CD1 1 
ATOM   2365  C CD2 . LEU B  1 31  ? 28.970  46.292 -11.460 1.00 47.66  ? 31  LEU B CD2 1 
ATOM   2366  N N   . ALA B  1 32  ? 32.997  43.570 -9.000  1.00 46.01  ? 32  ALA B N   1 
ATOM   2367  C CA  . ALA B  1 32  ? 33.821  42.397 -8.630  1.00 45.29  ? 32  ALA B CA  1 
ATOM   2368  C C   . ALA B  1 32  ? 33.132  41.644 -7.487  1.00 42.24  ? 32  ALA B C   1 
ATOM   2369  O O   . ALA B  1 32  ? 33.116  40.402 -7.521  1.00 42.21  ? 32  ALA B O   1 
ATOM   2370  C CB  . ALA B  1 32  ? 35.208  42.842 -8.240  1.00 46.59  ? 32  ALA B CB  1 
ATOM   2371  N N   . PHE B  1 33  ? 32.579  42.386 -6.523  1.00 42.00  ? 33  PHE B N   1 
ATOM   2372  C CA  . PHE B  1 33  ? 31.898  41.854 -5.315  1.00 41.83  ? 33  PHE B CA  1 
ATOM   2373  C C   . PHE B  1 33  ? 30.557  41.228 -5.717  1.00 41.00  ? 33  PHE B C   1 
ATOM   2374  O O   . PHE B  1 33  ? 30.211  40.164 -5.169  1.00 41.52  ? 33  PHE B O   1 
ATOM   2375  C CB  . PHE B  1 33  ? 31.733  42.955 -4.263  1.00 42.98  ? 33  PHE B CB  1 
ATOM   2376  C CG  . PHE B  1 33  ? 33.010  43.339 -3.558  1.00 44.94  ? 33  PHE B CG  1 
ATOM   2377  C CD1 . PHE B  1 33  ? 33.878  42.368 -3.085  1.00 42.29  ? 33  PHE B CD1 1 
ATOM   2378  C CD2 . PHE B  1 33  ? 33.337  44.670 -3.349  1.00 51.84  ? 33  PHE B CD2 1 
ATOM   2379  C CE1 . PHE B  1 33  ? 35.049  42.718 -2.431  1.00 42.34  ? 33  PHE B CE1 1 
ATOM   2380  C CE2 . PHE B  1 33  ? 34.508  45.019 -2.693  1.00 49.19  ? 33  PHE B CE2 1 
ATOM   2381  C CZ  . PHE B  1 33  ? 35.362  44.042 -2.237  1.00 45.22  ? 33  PHE B CZ  1 
ATOM   2382  N N   . VAL B  1 34  ? 29.833  41.863 -6.643  1.00 37.69  ? 34  VAL B N   1 
ATOM   2383  C CA  . VAL B  1 34  ? 28.577  41.315 -7.240  1.00 39.41  ? 34  VAL B CA  1 
ATOM   2384  C C   . VAL B  1 34  ? 28.889  39.937 -7.836  1.00 40.65  ? 34  VAL B C   1 
ATOM   2385  O O   . VAL B  1 34  ? 28.208  38.960 -7.464  1.00 39.07  ? 34  VAL B O   1 
ATOM   2386  C CB  . VAL B  1 34  ? 27.990  42.261 -8.304  1.00 39.33  ? 34  VAL B CB  1 
ATOM   2387  C CG1 . VAL B  1 34  ? 27.031  41.535 -9.235  1.00 40.72  ? 34  VAL B CG1 1 
ATOM   2388  C CG2 . VAL B  1 34  ? 27.320  43.473 -7.678  1.00 38.43  ? 34  VAL B CG2 1 
ATOM   2389  N N   . ALA B  1 35  ? 29.887  39.872 -8.724  1.00 39.45  ? 35  ALA B N   1 
ATOM   2390  C CA  . ALA B  1 35  ? 30.362  38.639 -9.395  1.00 39.15  ? 35  ALA B CA  1 
ATOM   2391  C C   . ALA B  1 35  ? 30.738  37.593 -8.340  1.00 38.38  ? 35  ALA B C   1 
ATOM   2392  O O   . ALA B  1 35  ? 30.344  36.423 -8.500  1.00 35.87  ? 35  ALA B O   1 
ATOM   2393  C CB  . ALA B  1 35  ? 31.535  38.962 -10.287 1.00 42.14  ? 35  ALA B CB  1 
ATOM   2394  N N   . GLY B  1 36  ? 31.483  38.011 -7.312  1.00 40.36  ? 36  GLY B N   1 
ATOM   2395  C CA  . GLY B  1 36  ? 31.917  37.156 -6.193  1.00 37.79  ? 36  GLY B CA  1 
ATOM   2396  C C   . GLY B  1 36  ? 30.727  36.612 -5.426  1.00 37.93  ? 36  GLY B C   1 
ATOM   2397  O O   . GLY B  1 36  ? 30.669  35.387 -5.216  1.00 38.73  ? 36  GLY B O   1 
ATOM   2398  N N   . PHE B  1 37  ? 29.807  37.493 -5.025  1.00 38.65  ? 37  PHE B N   1 
ATOM   2399  C CA  . PHE B  1 37  ? 28.576  37.145 -4.270  1.00 39.84  ? 37  PHE B CA  1 
ATOM   2400  C C   . PHE B  1 37  ? 27.811  36.060 -5.032  1.00 39.58  ? 37  PHE B C   1 
ATOM   2401  O O   . PHE B  1 37  ? 27.448  35.035 -4.425  1.00 39.14  ? 37  PHE B O   1 
ATOM   2402  C CB  . PHE B  1 37  ? 27.702  38.381 -4.052  1.00 39.01  ? 37  PHE B CB  1 
ATOM   2403  C CG  . PHE B  1 37  ? 26.459  38.117 -3.244  1.00 39.50  ? 37  PHE B CG  1 
ATOM   2404  C CD1 . PHE B  1 37  ? 26.448  38.314 -1.874  1.00 41.39  ? 37  PHE B CD1 1 
ATOM   2405  C CD2 . PHE B  1 37  ? 25.303  37.654 -3.852  1.00 40.57  ? 37  PHE B CD2 1 
ATOM   2406  C CE1 . PHE B  1 37  ? 25.305  38.068 -1.130  1.00 43.14  ? 37  PHE B CE1 1 
ATOM   2407  C CE2 . PHE B  1 37  ? 24.160  37.409 -3.107  1.00 41.49  ? 37  PHE B CE2 1 
ATOM   2408  C CZ  . PHE B  1 37  ? 24.164  37.614 -1.748  1.00 41.88  ? 37  PHE B CZ  1 
ATOM   2409  N N   . ILE B  1 38  ? 27.582  36.287 -6.329  1.00 41.37  ? 38  ILE B N   1 
ATOM   2410  C CA  . ILE B  1 38  ? 26.849  35.349 -7.229  1.00 43.79  ? 38  ILE B CA  1 
ATOM   2411  C C   . ILE B  1 38  ? 27.583  34.003 -7.235  1.00 43.26  ? 38  ILE B C   1 
ATOM   2412  O O   . ILE B  1 38  ? 26.939  32.988 -6.923  1.00 42.87  ? 38  ILE B O   1 
ATOM   2413  C CB  . ILE B  1 38  ? 26.701  35.929 -8.648  1.00 43.55  ? 38  ILE B CB  1 
ATOM   2414  C CG1 . ILE B  1 38  ? 25.859  37.207 -8.655  1.00 43.69  ? 38  ILE B CG1 1 
ATOM   2415  C CG2 . ILE B  1 38  ? 26.133  34.881 -9.591  1.00 43.69  ? 38  ILE B CG2 1 
ATOM   2416  C CD1 . ILE B  1 38  ? 25.722  37.841 -10.021 1.00 49.13  ? 38  ILE B CD1 1 
ATOM   2417  N N   . ARG B  1 39  ? 28.876  34.000 -7.573  1.00 47.60  ? 39  ARG B N   1 
ATOM   2418  C CA  . ARG B  1 39  ? 29.721  32.774 -7.593  1.00 57.18  ? 39  ARG B CA  1 
ATOM   2419  C C   . ARG B  1 39  ? 29.533  32.030 -6.268  1.00 50.62  ? 39  ARG B C   1 
ATOM   2420  O O   . ARG B  1 39  ? 29.210  30.830 -6.308  1.00 44.03  ? 39  ARG B O   1 
ATOM   2421  C CB  . ARG B  1 39  ? 31.200  33.112 -7.827  1.00 69.66  ? 39  ARG B CB  1 
ATOM   2422  C CG  . ARG B  1 39  ? 32.162  31.965 -7.543  1.00 79.52  ? 39  ARG B CG  1 
ATOM   2423  C CD  . ARG B  1 39  ? 33.134  31.696 -8.680  1.00 84.78  ? 39  ARG B CD  1 
ATOM   2424  N NE  . ARG B  1 39  ? 34.424  31.220 -8.203  1.00 82.90  ? 39  ARG B NE  1 
ATOM   2425  N N   . THR B  1 40  ? 29.718  32.728 -5.144  1.00 48.89  ? 40  THR B N   1 
ATOM   2426  C CA  . THR B  1 40  ? 29.661  32.159 -3.770  1.00 47.69  ? 40  THR B CA  1 
ATOM   2427  C C   . THR B  1 40  ? 28.306  31.482 -3.545  1.00 49.80  ? 40  THR B C   1 
ATOM   2428  O O   . THR B  1 40  ? 28.299  30.348 -3.026  1.00 52.59  ? 40  THR B O   1 
ATOM   2429  C CB  . THR B  1 40  ? 29.916  33.233 -2.709  1.00 44.21  ? 40  THR B CB  1 
ATOM   2430  O OG1 . THR B  1 40  ? 31.283  33.630 -2.829  1.00 47.75  ? 40  THR B OG1 1 
ATOM   2431  C CG2 . THR B  1 40  ? 29.626  32.748 -1.305  1.00 41.20  ? 40  THR B CG2 1 
ATOM   2432  N N   . TYR B  1 41  ? 27.213  32.153 -3.921  1.00 49.25  ? 41  TYR B N   1 
ATOM   2433  C CA  . TYR B  1 41  ? 25.819  31.668 -3.744  1.00 52.99  ? 41  TYR B CA  1 
ATOM   2434  C C   . TYR B  1 41  ? 25.615  30.375 -4.542  1.00 56.15  ? 41  TYR B C   1 
ATOM   2435  O O   . TYR B  1 41  ? 25.083  29.396 -3.983  1.00 57.65  ? 41  TYR B O   1 
ATOM   2436  C CB  . TYR B  1 41  ? 24.805  32.732 -4.172  1.00 53.56  ? 41  TYR B CB  1 
ATOM   2437  C CG  . TYR B  1 41  ? 23.371  32.324 -3.950  1.00 58.55  ? 41  TYR B CG  1 
ATOM   2438  C CD1 . TYR B  1 41  ? 22.582  31.869 -4.994  1.00 63.40  ? 41  TYR B CD1 1 
ATOM   2439  C CD2 . TYR B  1 41  ? 22.808  32.361 -2.685  1.00 61.64  ? 41  TYR B CD2 1 
ATOM   2440  C CE1 . TYR B  1 41  ? 21.267  31.482 -4.791  1.00 65.48  ? 41  TYR B CE1 1 
ATOM   2441  C CE2 . TYR B  1 41  ? 21.496  31.976 -2.464  1.00 63.46  ? 41  TYR B CE2 1 
ATOM   2442  C CZ  . TYR B  1 41  ? 20.722  31.534 -3.521  1.00 66.26  ? 41  TYR B CZ  1 
ATOM   2443  O OH  . TYR B  1 41  ? 19.428  31.152 -3.310  1.00 72.30  ? 41  TYR B OH  1 
ATOM   2444  N N   . ILE B  1 42  ? 26.033  30.376 -5.811  1.00 56.22  ? 42  ILE B N   1 
ATOM   2445  C CA  . ILE B  1 42  ? 25.818  29.262 -6.782  1.00 53.16  ? 42  ILE B CA  1 
ATOM   2446  C C   . ILE B  1 42  ? 26.605  28.024 -6.335  1.00 51.14  ? 42  ILE B C   1 
ATOM   2447  O O   . ILE B  1 42  ? 26.106  26.904 -6.554  1.00 51.24  ? 42  ILE B O   1 
ATOM   2448  C CB  . ILE B  1 42  ? 26.204  29.705 -8.207  1.00 55.71  ? 42  ILE B CB  1 
ATOM   2449  C CG1 . ILE B  1 42  ? 25.116  30.584 -8.827  1.00 57.53  ? 42  ILE B CG1 1 
ATOM   2450  C CG2 . ILE B  1 42  ? 26.528  28.510 -9.090  1.00 57.37  ? 42  ILE B CG2 1 
ATOM   2451  C CD1 . ILE B  1 42  ? 25.015  30.454 -10.325 1.00 63.72  ? 42  ILE B CD1 1 
ATOM   2452  N N   . THR B  1 43  ? 27.782  28.219 -5.733  1.00 50.45  ? 43  THR B N   1 
ATOM   2453  C CA  . THR B  1 43  ? 28.722  27.133 -5.345  1.00 50.39  ? 43  THR B CA  1 
ATOM   2454  C C   . THR B  1 43  ? 28.577  26.814 -3.853  1.00 53.42  ? 43  THR B C   1 
ATOM   2455  O O   . THR B  1 43  ? 29.527  26.239 -3.284  1.00 73.91  ? 43  THR B O   1 
ATOM   2456  C CB  . THR B  1 43  ? 30.170  27.513 -5.678  1.00 48.27  ? 43  THR B CB  1 
ATOM   2457  O OG1 . THR B  1 43  ? 30.518  28.667 -4.910  1.00 46.16  ? 43  THR B OG1 1 
ATOM   2458  C CG2 . THR B  1 43  ? 30.381  27.792 -7.150  1.00 48.96  ? 43  THR B CG2 1 
ATOM   2459  N N   . ARG B  1 44  ? 27.438  27.159 -3.245  1.00 51.16  ? 44  ARG B N   1 
ATOM   2460  C CA  . ARG B  1 44  ? 27.238  27.064 -1.774  1.00 55.41  ? 44  ARG B CA  1 
ATOM   2461  C C   . ARG B  1 44  ? 27.119  25.591 -1.364  1.00 55.18  ? 44  ARG B C   1 
ATOM   2462  O O   . ARG B  1 44  ? 27.623  25.244 -0.281  1.00 64.01  ? 44  ARG B O   1 
ATOM   2463  C CB  . ARG B  1 44  ? 26.024  27.888 -1.326  1.00 54.35  ? 44  ARG B CB  1 
ATOM   2464  C CG  . ARG B  1 44  ? 24.671  27.334 -1.746  1.00 60.40  ? 44  ARG B CG  1 
ATOM   2465  C CD  . ARG B  1 44  ? 23.552  28.292 -1.376  1.00 67.85  ? 44  ARG B CD  1 
ATOM   2466  N NE  . ARG B  1 44  ? 22.221  27.751 -1.620  1.00 74.08  ? 44  ARG B NE  1 
ATOM   2467  C CZ  . ARG B  1 44  ? 21.557  27.855 -2.767  1.00 84.50  ? 44  ARG B CZ  1 
ATOM   2468  N NH1 . ARG B  1 44  ? 22.102  28.478 -3.798  1.00 83.54  ? 44  ARG B NH1 1 
ATOM   2469  N NH2 . ARG B  1 44  ? 20.351  27.328 -2.881  1.00 101.26 ? 44  ARG B NH2 1 
ATOM   2470  N N   . ASN B  1 45  ? 26.500  24.758 -2.204  1.00 57.22  ? 45  ASN B N   1 
ATOM   2471  C CA  . ASN B  1 45  ? 26.151  23.350 -1.868  1.00 59.48  ? 45  ASN B CA  1 
ATOM   2472  C C   . ASN B  1 45  ? 27.274  22.406 -2.316  1.00 58.59  ? 45  ASN B C   1 
ATOM   2473  O O   . ASN B  1 45  ? 27.022  21.187 -2.387  1.00 59.62  ? 45  ASN B O   1 
ATOM   2474  C CB  . ASN B  1 45  ? 24.797  22.959 -2.463  1.00 60.81  ? 45  ASN B CB  1 
ATOM   2475  C CG  . ASN B  1 45  ? 23.642  23.631 -1.753  1.00 63.52  ? 45  ASN B CG  1 
ATOM   2476  O OD1 . ASN B  1 45  ? 23.710  23.884 -0.552  1.00 57.13  ? 45  ASN B OD1 1 
ATOM   2477  N ND2 . ASN B  1 45  ? 22.578  23.928 -2.482  1.00 77.14  ? 45  ASN B ND2 1 
ATOM   2478  N N   . GLU B  1 46  ? 28.462  22.952 -2.599  1.00 59.80  ? 46  GLU B N   1 
ATOM   2479  C CA  . GLU B  1 46  ? 29.699  22.178 -2.893  1.00 60.56  ? 46  GLU B CA  1 
ATOM   2480  C C   . GLU B  1 46  ? 30.400  21.842 -1.572  1.00 61.53  ? 46  GLU B C   1 
ATOM   2481  O O   . GLU B  1 46  ? 31.506  21.265 -1.612  1.00 61.84  ? 46  GLU B O   1 
ATOM   2482  C CB  . GLU B  1 46  ? 30.650  22.977 -3.786  1.00 59.97  ? 46  GLU B CB  1 
ATOM   2483  C CG  . GLU B  1 46  ? 30.166  23.150 -5.212  1.00 61.76  ? 46  GLU B CG  1 
ATOM   2484  C CD  . GLU B  1 46  ? 31.140  23.899 -6.108  1.00 66.72  ? 46  GLU B CD  1 
ATOM   2485  O OE1 . GLU B  1 46  ? 30.859  24.016 -7.318  1.00 69.50  ? 46  GLU B OE1 1 
ATOM   2486  O OE2 . GLU B  1 46  ? 32.180  24.365 -5.593  1.00 60.41  ? 46  GLU B OE2 1 
ATOM   2487  N N   . VAL B  1 47  ? 29.773  22.205 -0.449  1.00 58.26  ? 47  VAL B N   1 
ATOM   2488  C CA  . VAL B  1 47  ? 30.372  22.145 0.916   1.00 54.28  ? 47  VAL B CA  1 
ATOM   2489  C C   . VAL B  1 47  ? 29.390  21.442 1.860   1.00 54.67  ? 47  VAL B C   1 
ATOM   2490  O O   . VAL B  1 47  ? 28.179  21.736 1.786   1.00 57.89  ? 47  VAL B O   1 
ATOM   2491  C CB  . VAL B  1 47  ? 30.731  23.558 1.415   1.00 53.96  ? 47  VAL B CB  1 
ATOM   2492  C CG1 . VAL B  1 47  ? 30.953  23.593 2.919   1.00 56.77  ? 47  VAL B CG1 1 
ATOM   2493  C CG2 . VAL B  1 47  ? 31.936  24.121 0.675   1.00 53.37  ? 47  VAL B CG2 1 
ATOM   2494  N N   . GLY B  1 48  ? 29.907  20.549 2.710   1.00 51.83  ? 48  GLY B N   1 
ATOM   2495  C CA  . GLY B  1 48  ? 29.124  19.793 3.707   1.00 51.47  ? 48  GLY B CA  1 
ATOM   2496  C C   . GLY B  1 48  ? 28.517  20.717 4.748   1.00 52.71  ? 48  GLY B C   1 
ATOM   2497  O O   . GLY B  1 48  ? 29.077  21.809 4.968   1.00 56.46  ? 48  GLY B O   1 
ATOM   2498  N N   . SER B  1 49  ? 27.413  20.300 5.373   1.00 51.07  ? 49  SER B N   1 
ATOM   2499  C CA  . SER B  1 49  ? 26.693  21.075 6.418   1.00 50.63  ? 49  SER B CA  1 
ATOM   2500  C C   . SER B  1 49  ? 27.671  21.461 7.534   1.00 49.50  ? 49  SER B C   1 
ATOM   2501  O O   . SER B  1 49  ? 27.399  22.445 8.244   1.00 54.97  ? 49  SER B O   1 
ATOM   2502  C CB  . SER B  1 49  ? 25.522  20.299 6.963   1.00 51.22  ? 49  SER B CB  1 
ATOM   2503  O OG  . SER B  1 49  ? 25.951  19.081 7.552   1.00 57.91  ? 49  SER B OG  1 
ATOM   2504  N N   . ARG B  1 50  ? 28.766  20.708 7.671   1.00 51.20  ? 50  ARG B N   1 
ATOM   2505  C CA  . ARG B  1 50  ? 29.764  20.866 8.762   1.00 54.60  ? 50  ARG B CA  1 
ATOM   2506  C C   . ARG B  1 50  ? 30.530  22.183 8.588   1.00 52.56  ? 50  ARG B C   1 
ATOM   2507  O O   . ARG B  1 50  ? 30.902  22.784 9.612   1.00 50.71  ? 50  ARG B O   1 
ATOM   2508  C CB  . ARG B  1 50  ? 30.749  19.694 8.779   1.00 58.29  ? 50  ARG B CB  1 
ATOM   2509  C CG  . ARG B  1 50  ? 31.795  19.803 9.879   1.00 64.19  ? 50  ARG B CG  1 
ATOM   2510  C CD  . ARG B  1 50  ? 32.792  18.665 9.887   1.00 73.02  ? 50  ARG B CD  1 
ATOM   2511  N NE  . ARG B  1 50  ? 33.679  18.753 11.038  1.00 76.44  ? 50  ARG B NE  1 
ATOM   2512  C CZ  . ARG B  1 50  ? 34.703  17.941 11.265  1.00 73.56  ? 50  ARG B CZ  1 
ATOM   2513  N NH1 . ARG B  1 50  ? 34.981  16.969 10.411  1.00 74.95  ? 50  ARG B NH1 1 
ATOM   2514  N NH2 . ARG B  1 50  ? 35.445  18.106 12.345  1.00 72.78  ? 50  ARG B NH2 1 
ATOM   2515  N N   . TYR B  1 51  ? 30.763  22.602 7.341   1.00 53.68  ? 51  TYR B N   1 
ATOM   2516  C CA  . TYR B  1 51  ? 31.619  23.764 6.988   1.00 58.18  ? 51  TYR B CA  1 
ATOM   2517  C C   . TYR B  1 51  ? 30.765  24.877 6.368   1.00 55.31  ? 51  TYR B C   1 
ATOM   2518  O O   . TYR B  1 51  ? 31.322  25.728 5.651   1.00 53.86  ? 51  TYR B O   1 
ATOM   2519  C CB  . TYR B  1 51  ? 32.737  23.321 6.041   1.00 58.17  ? 51  TYR B CB  1 
ATOM   2520  C CG  . TYR B  1 51  ? 33.575  22.182 6.563   1.00 60.38  ? 51  TYR B CG  1 
ATOM   2521  C CD1 . TYR B  1 51  ? 34.482  22.380 7.591   1.00 60.57  ? 51  TYR B CD1 1 
ATOM   2522  C CD2 . TYR B  1 51  ? 33.462  20.907 6.035   1.00 65.29  ? 51  TYR B CD2 1 
ATOM   2523  C CE1 . TYR B  1 51  ? 35.258  21.343 8.080   1.00 65.42  ? 51  TYR B CE1 1 
ATOM   2524  C CE2 . TYR B  1 51  ? 34.230  19.857 6.514   1.00 65.90  ? 51  TYR B CE2 1 
ATOM   2525  C CZ  . TYR B  1 51  ? 35.131  20.076 7.541   1.00 66.74  ? 51  TYR B CZ  1 
ATOM   2526  O OH  . TYR B  1 51  ? 35.891  19.052 8.025   1.00 71.29  ? 51  TYR B OH  1 
ATOM   2527  N N   . ARG B  1 52  ? 29.460  24.882 6.654   1.00 49.54  ? 52  ARG B N   1 
ATOM   2528  C CA  . ARG B  1 52  ? 28.491  25.848 6.071   1.00 51.14  ? 52  ARG B CA  1 
ATOM   2529  C C   . ARG B  1 52  ? 28.746  27.251 6.632   1.00 52.35  ? 52  ARG B C   1 
ATOM   2530  O O   . ARG B  1 52  ? 28.495  28.228 5.900   1.00 49.75  ? 52  ARG B O   1 
ATOM   2531  C CB  . ARG B  1 52  ? 27.049  25.417 6.349   1.00 51.25  ? 52  ARG B CB  1 
ATOM   2532  C CG  . ARG B  1 52  ? 26.009  26.291 5.663   1.00 54.27  ? 52  ARG B CG  1 
ATOM   2533  C CD  . ARG B  1 52  ? 24.690  25.564 5.500   1.00 58.40  ? 52  ARG B CD  1 
ATOM   2534  N NE  . ARG B  1 52  ? 24.845  24.323 4.754   1.00 60.86  ? 52  ARG B NE  1 
ATOM   2535  C CZ  . ARG B  1 52  ? 24.087  23.246 4.920   1.00 62.66  ? 52  ARG B CZ  1 
ATOM   2536  N NH1 . ARG B  1 52  ? 23.119  23.248 5.822   1.00 65.35  ? 52  ARG B NH1 1 
ATOM   2537  N NH2 . ARG B  1 52  ? 24.307  22.165 4.194   1.00 60.90  ? 52  ARG B NH2 1 
ATOM   2538  N N   . THR B  1 53  ? 29.217  27.346 7.880   1.00 50.73  ? 53  THR B N   1 
ATOM   2539  C CA  . THR B  1 53  ? 29.524  28.630 8.563   1.00 51.55  ? 53  THR B CA  1 
ATOM   2540  C C   . THR B  1 53  ? 30.535  29.411 7.717   1.00 51.47  ? 53  THR B C   1 
ATOM   2541  O O   . THR B  1 53  ? 30.468  30.656 7.718   1.00 52.27  ? 53  THR B O   1 
ATOM   2542  C CB  . THR B  1 53  ? 30.051  28.407 9.986   1.00 58.01  ? 53  THR B CB  1 
ATOM   2543  O OG1 . THR B  1 53  ? 29.200  27.462 10.635  1.00 64.77  ? 53  THR B OG1 1 
ATOM   2544  C CG2 . THR B  1 53  ? 30.108  29.686 10.795  1.00 60.18  ? 53  THR B CG2 1 
ATOM   2545  N N   . ALA B  1 54  ? 31.431  28.698 7.026   1.00 50.02  ? 54  ALA B N   1 
ATOM   2546  C CA  . ALA B  1 54  ? 32.448  29.266 6.112   1.00 50.12  ? 54  ALA B CA  1 
ATOM   2547  C C   . ALA B  1 54  ? 31.742  29.981 4.957   1.00 52.21  ? 54  ALA B C   1 
ATOM   2548  O O   . ALA B  1 54  ? 32.197  31.075 4.569   1.00 67.15  ? 54  ALA B O   1 
ATOM   2549  C CB  . ALA B  1 54  ? 33.359  28.177 5.603   1.00 49.33  ? 54  ALA B CB  1 
ATOM   2550  N N   . VAL B  1 55  ? 30.665  29.377 4.446   1.00 45.28  ? 55  VAL B N   1 
ATOM   2551  C CA  . VAL B  1 55  ? 29.900  29.859 3.258   1.00 44.60  ? 55  VAL B CA  1 
ATOM   2552  C C   . VAL B  1 55  ? 29.055  31.070 3.666   1.00 45.48  ? 55  VAL B C   1 
ATOM   2553  O O   . VAL B  1 55  ? 29.166  32.112 2.995   1.00 52.55  ? 55  VAL B O   1 
ATOM   2554  C CB  . VAL B  1 55  ? 29.026  28.739 2.663   1.00 43.64  ? 55  VAL B CB  1 
ATOM   2555  C CG1 . VAL B  1 55  ? 28.197  29.231 1.486   1.00 46.01  ? 55  VAL B CG1 1 
ATOM   2556  C CG2 . VAL B  1 55  ? 29.861  27.535 2.258   1.00 42.21  ? 55  VAL B CG2 1 
ATOM   2557  N N   . SER B  1 56  ? 28.243  30.934 4.718   1.00 46.45  ? 56  SER B N   1 
ATOM   2558  C CA  . SER B  1 56  ? 27.332  31.996 5.223   1.00 48.08  ? 56  SER B CA  1 
ATOM   2559  C C   . SER B  1 56  ? 28.140  33.260 5.538   1.00 45.81  ? 56  SER B C   1 
ATOM   2560  O O   . SER B  1 56  ? 27.645  34.366 5.246   1.00 48.49  ? 56  SER B O   1 
ATOM   2561  C CB  . SER B  1 56  ? 26.544  31.529 6.422   1.00 51.81  ? 56  SER B CB  1 
ATOM   2562  O OG  . SER B  1 56  ? 27.406  31.111 7.470   1.00 60.24  ? 56  SER B OG  1 
ATOM   2563  N N   . ALA B  1 57  ? 29.338  33.096 6.107   1.00 42.41  ? 57  ALA B N   1 
ATOM   2564  C CA  . ALA B  1 57  ? 30.270  34.197 6.444   1.00 39.56  ? 57  ALA B CA  1 
ATOM   2565  C C   . ALA B  1 57  ? 30.759  34.861 5.152   1.00 38.65  ? 57  ALA B C   1 
ATOM   2566  O O   . ALA B  1 57  ? 30.675  36.103 5.057   1.00 34.60  ? 57  ALA B O   1 
ATOM   2567  C CB  . ALA B  1 57  ? 31.419  33.668 7.266   1.00 39.58  ? 57  ALA B CB  1 
ATOM   2568  N N   . ARG B  1 58  ? 31.244  34.061 4.196   1.00 38.48  ? 58  ARG B N   1 
ATOM   2569  C CA  . ARG B  1 58  ? 31.787  34.546 2.899   1.00 42.22  ? 58  ARG B CA  1 
ATOM   2570  C C   . ARG B  1 58  ? 30.698  35.344 2.171   1.00 44.26  ? 58  ARG B C   1 
ATOM   2571  O O   . ARG B  1 58  ? 30.980  36.481 1.750   1.00 52.73  ? 58  ARG B O   1 
ATOM   2572  C CB  . ARG B  1 58  ? 32.293  33.378 2.046   1.00 43.23  ? 58  ARG B CB  1 
ATOM   2573  C CG  . ARG B  1 58  ? 32.897  33.801 0.714   1.00 50.17  ? 58  ARG B CG  1 
ATOM   2574  C CD  . ARG B  1 58  ? 33.787  32.746 0.073   1.00 57.79  ? 58  ARG B CD  1 
ATOM   2575  N NE  . ARG B  1 58  ? 33.175  31.422 0.013   1.00 70.13  ? 58  ARG B NE  1 
ATOM   2576  C CZ  . ARG B  1 58  ? 33.455  30.418 0.841   1.00 69.44  ? 58  ARG B CZ  1 
ATOM   2577  N NH1 . ARG B  1 58  ? 34.340  30.582 1.810   1.00 74.05  ? 58  ARG B NH1 1 
ATOM   2578  N NH2 . ARG B  1 58  ? 32.847  29.253 0.700   1.00 63.47  ? 58  ARG B NH2 1 
ATOM   2579  N N   . LEU B  1 59  ? 29.499  34.771 2.040   1.00 45.76  ? 59  LEU B N   1 
ATOM   2580  C CA  . LEU B  1 59  ? 28.350  35.409 1.345   1.00 41.70  ? 59  LEU B CA  1 
ATOM   2581  C C   . LEU B  1 59  ? 27.936  36.662 2.120   1.00 35.94  ? 59  LEU B C   1 
ATOM   2582  O O   . LEU B  1 59  ? 27.709  37.703 1.481   1.00 35.45  ? 59  LEU B O   1 
ATOM   2583  C CB  . LEU B  1 59  ? 27.195  34.409 1.246   1.00 46.04  ? 59  LEU B CB  1 
ATOM   2584  C CG  . LEU B  1 59  ? 26.187  34.696 0.135   1.00 54.70  ? 59  LEU B CG  1 
ATOM   2585  C CD1 . LEU B  1 59  ? 26.882  34.783 -1.217  1.00 58.52  ? 59  LEU B CD1 1 
ATOM   2586  C CD2 . LEU B  1 59  ? 25.094  33.641 0.111   1.00 54.60  ? 59  LEU B CD2 1 
ATOM   2587  N N   . GLY B  1 60  ? 27.853  36.555 3.448   1.00 34.29  ? 60  GLY B N   1 
ATOM   2588  C CA  . GLY B  1 60  ? 27.562  37.685 4.348   1.00 36.63  ? 60  GLY B CA  1 
ATOM   2589  C C   . GLY B  1 60  ? 28.504  38.850 4.095   1.00 40.06  ? 60  GLY B C   1 
ATOM   2590  O O   . GLY B  1 60  ? 28.009  39.985 3.937   1.00 42.70  ? 60  GLY B O   1 
ATOM   2591  N N   . MET B  1 61  ? 29.814  38.583 4.041   1.00 39.91  ? 61  MET B N   1 
ATOM   2592  C CA  . MET B  1 61  ? 30.865  39.629 3.917   1.00 48.45  ? 61  MET B CA  1 
ATOM   2593  C C   . MET B  1 61  ? 30.800  40.259 2.520   1.00 48.74  ? 61  MET B C   1 
ATOM   2594  O O   . MET B  1 61  ? 30.942  41.496 2.430   1.00 57.13  ? 61  MET B O   1 
ATOM   2595  C CB  . MET B  1 61  ? 32.267  39.057 4.155   1.00 53.66  ? 61  MET B CB  1 
ATOM   2596  C CG  . MET B  1 61  ? 32.791  38.228 2.998   1.00 64.30  ? 61  MET B CG  1 
ATOM   2597  S SD  . MET B  1 61  ? 34.446  38.733 2.470   1.00 63.06  ? 61  MET B SD  1 
ATOM   2598  C CE  . MET B  1 61  ? 34.288  40.514 2.595   1.00 62.91  ? 61  MET B CE  1 
ATOM   2599  N N   . LEU B  1 62  ? 30.588  39.446 1.480   1.00 44.38  ? 62  LEU B N   1 
ATOM   2600  C CA  . LEU B  1 62  ? 30.511  39.912 0.069   1.00 46.56  ? 62  LEU B CA  1 
ATOM   2601  C C   . LEU B  1 62  ? 29.272  40.800 -0.092  1.00 44.22  ? 62  LEU B C   1 
ATOM   2602  O O   . LEU B  1 62  ? 29.380  41.844 -0.761  1.00 48.23  ? 62  LEU B O   1 
ATOM   2603  C CB  . LEU B  1 62  ? 30.465  38.702 -0.869  1.00 49.96  ? 62  LEU B CB  1 
ATOM   2604  C CG  . LEU B  1 62  ? 31.767  37.908 -0.976  1.00 52.86  ? 62  LEU B CG  1 
ATOM   2605  C CD1 . LEU B  1 62  ? 31.578  36.654 -1.816  1.00 51.75  ? 62  LEU B CD1 1 
ATOM   2606  C CD2 . LEU B  1 62  ? 32.885  38.767 -1.546  1.00 52.92  ? 62  LEU B CD2 1 
ATOM   2607  N N   . GLY B  1 63  ? 28.150  40.399 0.512   1.00 40.67  ? 63  GLY B N   1 
ATOM   2608  C CA  . GLY B  1 63  ? 26.901  41.183 0.541   1.00 41.03  ? 63  GLY B CA  1 
ATOM   2609  C C   . GLY B  1 63  ? 27.129  42.550 1.160   1.00 42.47  ? 63  GLY B C   1 
ATOM   2610  O O   . GLY B  1 63  ? 26.725  43.561 0.548   1.00 36.41  ? 63  GLY B O   1 
ATOM   2611  N N   . VAL B  1 64  ? 27.769  42.576 2.331   1.00 47.80  ? 64  VAL B N   1 
ATOM   2612  C CA  . VAL B  1 64  ? 28.103  43.823 3.080   1.00 51.23  ? 64  VAL B CA  1 
ATOM   2613  C C   . VAL B  1 64  ? 29.017  44.690 2.208   1.00 51.22  ? 64  VAL B C   1 
ATOM   2614  O O   . VAL B  1 64  ? 28.657  45.855 1.954   1.00 56.86  ? 64  VAL B O   1 
ATOM   2615  C CB  . VAL B  1 64  ? 28.754  43.502 4.436   1.00 52.85  ? 64  VAL B CB  1 
ATOM   2616  C CG1 . VAL B  1 64  ? 29.364  44.743 5.069   1.00 61.32  ? 64  VAL B CG1 1 
ATOM   2617  C CG2 . VAL B  1 64  ? 27.765  42.841 5.385   1.00 51.76  ? 64  VAL B CG2 1 
ATOM   2618  N N   . ALA B  1 65  ? 30.151  44.136 1.770   1.00 50.44  ? 65  ALA B N   1 
ATOM   2619  C CA  . ALA B  1 65  ? 31.157  44.814 0.919   1.00 54.53  ? 65  ALA B CA  1 
ATOM   2620  C C   . ALA B  1 65  ? 30.450  45.487 -0.262  1.00 51.23  ? 65  ALA B C   1 
ATOM   2621  O O   . ALA B  1 65  ? 30.626  46.707 -0.446  1.00 60.04  ? 65  ALA B O   1 
ATOM   2622  C CB  . ALA B  1 65  ? 32.189  43.818 0.449   1.00 57.13  ? 65  ALA B CB  1 
ATOM   2623  N N   . LEU B  1 66  ? 29.678  44.705 -1.019  1.00 48.49  ? 66  LEU B N   1 
ATOM   2624  C CA  . LEU B  1 66  ? 28.862  45.164 -2.174  1.00 49.72  ? 66  LEU B CA  1 
ATOM   2625  C C   . LEU B  1 66  ? 28.118  46.453 -1.800  1.00 45.23  ? 66  LEU B C   1 
ATOM   2626  O O   . LEU B  1 66  ? 28.360  47.487 -2.455  1.00 42.77  ? 66  LEU B O   1 
ATOM   2627  C CB  . LEU B  1 66  ? 27.885  44.043 -2.539  1.00 51.34  ? 66  LEU B CB  1 
ATOM   2628  C CG  . LEU B  1 66  ? 27.264  44.134 -3.929  1.00 59.26  ? 66  LEU B CG  1 
ATOM   2629  C CD1 . LEU B  1 66  ? 26.339  42.955 -4.180  1.00 64.52  ? 66  LEU B CD1 1 
ATOM   2630  C CD2 . LEU B  1 66  ? 26.522  45.448 -4.106  1.00 64.16  ? 66  LEU B CD2 1 
ATOM   2631  N N   . LEU B  1 67  ? 27.251  46.386 -0.784  1.00 41.78  ? 67  LEU B N   1 
ATOM   2632  C CA  . LEU B  1 67  ? 26.365  47.501 -0.354  1.00 42.69  ? 67  LEU B CA  1 
ATOM   2633  C C   . LEU B  1 67  ? 27.215  48.670 0.154   1.00 44.95  ? 67  LEU B C   1 
ATOM   2634  O O   . LEU B  1 67  ? 26.952  49.814 -0.260  1.00 53.53  ? 67  LEU B O   1 
ATOM   2635  C CB  . LEU B  1 67  ? 25.418  46.996 0.738   1.00 43.12  ? 67  LEU B CB  1 
ATOM   2636  C CG  . LEU B  1 67  ? 24.416  45.933 0.295   1.00 43.76  ? 67  LEU B CG  1 
ATOM   2637  C CD1 . LEU B  1 67  ? 23.569  45.470 1.469   1.00 44.65  ? 67  LEU B CD1 1 
ATOM   2638  C CD2 . LEU B  1 67  ? 23.532  46.451 -0.831  1.00 41.79  ? 67  LEU B CD2 1 
ATOM   2639  N N   . ALA B  1 68  ? 28.186  48.392 1.027   1.00 44.67  ? 68  ALA B N   1 
ATOM   2640  C CA  . ALA B  1 68  ? 29.117  49.396 1.590   1.00 42.29  ? 68  ALA B CA  1 
ATOM   2641  C C   . ALA B  1 68  ? 29.697  50.232 0.445   1.00 41.65  ? 68  ALA B C   1 
ATOM   2642  O O   . ALA B  1 68  ? 29.671  51.474 0.542   1.00 48.34  ? 68  ALA B O   1 
ATOM   2643  C CB  . ALA B  1 68  ? 30.204  48.714 2.383   1.00 41.32  ? 68  ALA B CB  1 
ATOM   2644  N N   . TYR B  1 69  ? 30.176  49.568 -0.609  1.00 38.32  ? 69  TYR B N   1 
ATOM   2645  C CA  . TYR B  1 69  ? 30.874  50.208 -1.754  1.00 41.47  ? 69  TYR B CA  1 
ATOM   2646  C C   . TYR B  1 69  ? 29.892  51.082 -2.542  1.00 42.06  ? 69  TYR B C   1 
ATOM   2647  O O   . TYR B  1 69  ? 30.329  52.117 -3.082  1.00 49.28  ? 69  TYR B O   1 
ATOM   2648  C CB  . TYR B  1 69  ? 31.581  49.159 -2.614  1.00 42.36  ? 69  TYR B CB  1 
ATOM   2649  C CG  . TYR B  1 69  ? 33.048  49.045 -2.293  1.00 44.37  ? 69  TYR B CG  1 
ATOM   2650  C CD1 . TYR B  1 69  ? 33.999  49.688 -3.066  1.00 47.06  ? 69  TYR B CD1 1 
ATOM   2651  C CD2 . TYR B  1 69  ? 33.483  48.350 -1.177  1.00 45.25  ? 69  TYR B CD2 1 
ATOM   2652  C CE1 . TYR B  1 69  ? 35.347  49.618 -2.761  1.00 46.49  ? 69  TYR B CE1 1 
ATOM   2653  C CE2 . TYR B  1 69  ? 34.828  48.267 -0.859  1.00 48.93  ? 69  TYR B CE2 1 
ATOM   2654  C CZ  . TYR B  1 69  ? 35.765  48.904 -1.653  1.00 47.48  ? 69  TYR B CZ  1 
ATOM   2655  O OH  . TYR B  1 69  ? 37.093  48.829 -1.347  1.00 55.27  ? 69  TYR B OH  1 
ATOM   2656  N N   . ILE B  1 70  ? 28.614  50.699 -2.593  1.00 41.07  ? 70  ILE B N   1 
ATOM   2657  C CA  . ILE B  1 70  ? 27.540  51.531 -3.214  1.00 41.47  ? 70  ILE B CA  1 
ATOM   2658  C C   . ILE B  1 70  ? 27.484  52.869 -2.469  1.00 40.91  ? 70  ILE B C   1 
ATOM   2659  O O   . ILE B  1 70  ? 27.440  53.917 -3.144  1.00 36.32  ? 70  ILE B O   1 
ATOM   2660  C CB  . ILE B  1 70  ? 26.178  50.811 -3.211  1.00 40.92  ? 70  ILE B CB  1 
ATOM   2661  C CG1 . ILE B  1 70  ? 26.185  49.586 -4.130  1.00 41.97  ? 70  ILE B CG1 1 
ATOM   2662  C CG2 . ILE B  1 70  ? 25.064  51.781 -3.576  1.00 39.65  ? 70  ILE B CG2 1 
ATOM   2663  C CD1 . ILE B  1 70  ? 24.867  48.850 -4.187  1.00 41.86  ? 70  ILE B CD1 1 
ATOM   2664  N N   . LEU B  1 71  ? 27.501  52.830 -1.133  1.00 39.71  ? 71  LEU B N   1 
ATOM   2665  C CA  . LEU B  1 71  ? 27.489  54.040 -0.267  1.00 45.04  ? 71  LEU B CA  1 
ATOM   2666  C C   . LEU B  1 71  ? 28.738  54.880 -0.558  1.00 42.40  ? 71  LEU B C   1 
ATOM   2667  O O   . LEU B  1 71  ? 28.588  56.096 -0.805  1.00 43.51  ? 71  LEU B O   1 
ATOM   2668  C CB  . LEU B  1 71  ? 27.429  53.615 1.204   1.00 49.46  ? 71  LEU B CB  1 
ATOM   2669  C CG  . LEU B  1 71  ? 26.141  52.912 1.627   1.00 55.56  ? 71  LEU B CG  1 
ATOM   2670  C CD1 . LEU B  1 71  ? 26.074  52.760 3.138   1.00 57.71  ? 71  LEU B CD1 1 
ATOM   2671  C CD2 . LEU B  1 71  ? 24.922  53.661 1.113   1.00 60.20  ? 71  LEU B CD2 1 
ATOM   2672  N N   . ILE B  1 72  ? 29.918  54.252 -0.541  1.00 40.46  ? 72  ILE B N   1 
ATOM   2673  C CA  . ILE B  1 72  ? 31.225  54.920 -0.812  1.00 42.32  ? 72  ILE B CA  1 
ATOM   2674  C C   . ILE B  1 72  ? 31.131  55.648 -2.157  1.00 41.73  ? 72  ILE B C   1 
ATOM   2675  O O   . ILE B  1 72  ? 31.530  56.829 -2.223  1.00 44.44  ? 72  ILE B O   1 
ATOM   2676  C CB  . ILE B  1 72  ? 32.386  53.906 -0.800  1.00 46.13  ? 72  ILE B CB  1 
ATOM   2677  C CG1 . ILE B  1 72  ? 32.555  53.251 0.573   1.00 48.66  ? 72  ILE B CG1 1 
ATOM   2678  C CG2 . ILE B  1 72  ? 33.673  54.565 -1.275  1.00 47.15  ? 72  ILE B CG2 1 
ATOM   2679  C CD1 . ILE B  1 72  ? 33.607  52.166 0.608   1.00 48.71  ? 72  ILE B CD1 1 
ATOM   2680  N N   . ILE B  1 73  ? 30.625  54.960 -3.185  1.00 40.00  ? 73  ILE B N   1 
ATOM   2681  C CA  . ILE B  1 73  ? 30.470  55.510 -4.565  1.00 39.10  ? 73  ILE B CA  1 
ATOM   2682  C C   . ILE B  1 73  ? 29.555  56.736 -4.500  1.00 38.57  ? 73  ILE B C   1 
ATOM   2683  O O   . ILE B  1 73  ? 29.927  57.779 -5.073  1.00 36.47  ? 73  ILE B O   1 
ATOM   2684  C CB  . ILE B  1 73  ? 29.930  54.447 -5.540  1.00 38.07  ? 73  ILE B CB  1 
ATOM   2685  C CG1 . ILE B  1 73  ? 30.916  53.292 -5.724  1.00 39.13  ? 73  ILE B CG1 1 
ATOM   2686  C CG2 . ILE B  1 73  ? 29.565  55.091 -6.870  1.00 38.48  ? 73  ILE B CG2 1 
ATOM   2687  C CD1 . ILE B  1 73  ? 30.330  52.085 -6.416  1.00 37.66  ? 73  ILE B CD1 1 
ATOM   2688  N N   . VAL B  1 74  ? 28.410  56.614 -3.821  1.00 38.23  ? 74  VAL B N   1 
ATOM   2689  C CA  . VAL B  1 74  ? 27.410  57.713 -3.678  1.00 38.66  ? 74  VAL B CA  1 
ATOM   2690  C C   . VAL B  1 74  ? 28.090  58.897 -2.985  1.00 40.07  ? 74  VAL B C   1 
ATOM   2691  O O   . VAL B  1 74  ? 27.966  60.026 -3.494  1.00 42.23  ? 74  VAL B O   1 
ATOM   2692  C CB  . VAL B  1 74  ? 26.154  57.260 -2.912  1.00 36.81  ? 74  VAL B CB  1 
ATOM   2693  C CG1 . VAL B  1 74  ? 25.257  58.440 -2.573  1.00 39.04  ? 74  VAL B CG1 1 
ATOM   2694  C CG2 . VAL B  1 74  ? 25.379  56.207 -3.685  1.00 36.41  ? 74  VAL B CG2 1 
ATOM   2695  N N   . ALA B  1 75  ? 28.792  58.641 -1.878  1.00 39.16  ? 75  ALA B N   1 
ATOM   2696  C CA  . ALA B  1 75  ? 29.525  59.662 -1.095  1.00 37.88  ? 75  ALA B CA  1 
ATOM   2697  C C   . ALA B  1 75  ? 30.527  60.383 -2.002  1.00 38.90  ? 75  ALA B C   1 
ATOM   2698  O O   . ALA B  1 75  ? 30.622  61.618 -1.894  1.00 41.67  ? 75  ALA B O   1 
ATOM   2699  C CB  . ALA B  1 75  ? 30.212  59.026 0.084   1.00 35.58  ? 75  ALA B CB  1 
ATOM   2700  N N   . PHE B  1 76  ? 31.235  59.637 -2.856  1.00 37.28  ? 76  PHE B N   1 
ATOM   2701  C CA  . PHE B  1 76  ? 32.251  60.167 -3.805  1.00 41.25  ? 76  PHE B CA  1 
ATOM   2702  C C   . PHE B  1 76  ? 31.575  61.127 -4.790  1.00 44.92  ? 76  PHE B C   1 
ATOM   2703  O O   . PHE B  1 76  ? 32.122  62.223 -5.025  1.00 52.50  ? 76  PHE B O   1 
ATOM   2704  C CB  . PHE B  1 76  ? 32.960  59.025 -4.538  1.00 40.94  ? 76  PHE B CB  1 
ATOM   2705  C CG  . PHE B  1 76  ? 33.899  59.464 -5.633  1.00 40.69  ? 76  PHE B CG  1 
ATOM   2706  C CD1 . PHE B  1 76  ? 33.511  59.405 -6.962  1.00 39.86  ? 76  PHE B CD1 1 
ATOM   2707  C CD2 . PHE B  1 76  ? 35.169  59.937 -5.333  1.00 39.35  ? 76  PHE B CD2 1 
ATOM   2708  C CE1 . PHE B  1 76  ? 34.375  59.799 -7.968  1.00 39.28  ? 76  PHE B CE1 1 
ATOM   2709  C CE2 . PHE B  1 76  ? 36.032  60.333 -6.342  1.00 41.92  ? 76  PHE B CE2 1 
ATOM   2710  C CZ  . PHE B  1 76  ? 35.632  60.262 -7.656  1.00 45.53  ? 76  PHE B CZ  1 
ATOM   2711  N N   . LEU B  1 77  ? 30.417  60.732 -5.330  1.00 46.84  ? 77  LEU B N   1 
ATOM   2712  C CA  . LEU B  1 77  ? 29.646  61.517 -6.336  1.00 46.06  ? 77  LEU B CA  1 
ATOM   2713  C C   . LEU B  1 77  ? 29.131  62.814 -5.701  1.00 45.88  ? 77  LEU B C   1 
ATOM   2714  O O   . LEU B  1 77  ? 28.992  63.813 -6.433  1.00 44.37  ? 77  LEU B O   1 
ATOM   2715  C CB  . LEU B  1 77  ? 28.480  60.676 -6.866  1.00 43.69  ? 77  LEU B CB  1 
ATOM   2716  C CG  . LEU B  1 77  ? 28.867  59.382 -7.579  1.00 49.68  ? 77  LEU B CG  1 
ATOM   2717  C CD1 . LEU B  1 77  ? 27.632  58.619 -8.035  1.00 50.12  ? 77  LEU B CD1 1 
ATOM   2718  C CD2 . LEU B  1 77  ? 29.788  59.667 -8.754  1.00 50.81  ? 77  LEU B CD2 1 
ATOM   2719  N N   . LEU B  1 78  ? 28.847  62.797 -4.394  1.00 44.42  ? 78  LEU B N   1 
ATOM   2720  C CA  . LEU B  1 78  ? 28.262  63.949 -3.653  1.00 47.95  ? 78  LEU B CA  1 
ATOM   2721  C C   . LEU B  1 78  ? 29.343  64.648 -2.819  1.00 49.58  ? 78  LEU B C   1 
ATOM   2722  O O   . LEU B  1 78  ? 29.002  65.613 -2.107  1.00 53.40  ? 78  LEU B O   1 
ATOM   2723  C CB  . LEU B  1 78  ? 27.129  63.449 -2.751  1.00 46.93  ? 78  LEU B CB  1 
ATOM   2724  C CG  . LEU B  1 78  ? 26.019  62.665 -3.448  1.00 52.04  ? 78  LEU B CG  1 
ATOM   2725  C CD1 . LEU B  1 78  ? 24.937  62.265 -2.457  1.00 49.97  ? 78  LEU B CD1 1 
ATOM   2726  C CD2 . LEU B  1 78  ? 25.427  63.459 -4.604  1.00 51.77  ? 78  LEU B CD2 1 
ATOM   2727  N N   . GLY B  1 79  ? 30.593  64.184 -2.906  1.00 49.90  ? 79  GLY B N   1 
ATOM   2728  C CA  . GLY B  1 79  ? 31.699  64.634 -2.038  1.00 49.24  ? 79  GLY B CA  1 
ATOM   2729  C C   . GLY B  1 79  ? 32.551  65.710 -2.689  1.00 51.08  ? 79  GLY B C   1 
ATOM   2730  O O   . GLY B  1 79  ? 33.289  66.399 -1.956  1.00 52.47  ? 79  GLY B O   1 
ATOM   2731  N N   . TYR B  1 80  ? 32.473  65.849 -4.015  1.00 51.89  ? 80  TYR B N   1 
ATOM   2732  C CA  . TYR B  1 80  ? 33.305  66.788 -4.812  1.00 51.15  ? 80  TYR B CA  1 
ATOM   2733  C C   . TYR B  1 80  ? 32.415  67.561 -5.789  1.00 50.22  ? 80  TYR B C   1 
ATOM   2734  O O   . TYR B  1 80  ? 31.419  66.992 -6.276  1.00 57.78  ? 80  TYR B O   1 
ATOM   2735  C CB  . TYR B  1 80  ? 34.406  66.028 -5.556  1.00 51.11  ? 80  TYR B CB  1 
ATOM   2736  C CG  . TYR B  1 80  ? 35.497  65.475 -4.673  1.00 48.87  ? 80  TYR B CG  1 
ATOM   2737  C CD1 . TYR B  1 80  ? 36.633  66.215 -4.395  1.00 49.44  ? 80  TYR B CD1 1 
ATOM   2738  C CD2 . TYR B  1 80  ? 35.395  64.213 -4.113  1.00 51.09  ? 80  TYR B CD2 1 
ATOM   2739  C CE1 . TYR B  1 80  ? 37.637  65.718 -3.580  1.00 53.10  ? 80  TYR B CE1 1 
ATOM   2740  C CE2 . TYR B  1 80  ? 36.389  63.701 -3.296  1.00 52.67  ? 80  TYR B CE2 1 
ATOM   2741  C CZ  . TYR B  1 80  ? 37.515  64.456 -3.028  1.00 54.57  ? 80  TYR B CZ  1 
ATOM   2742  O OH  . TYR B  1 80  ? 38.494  63.950 -2.221  1.00 57.94  ? 80  TYR B OH  1 
ATOM   2743  N N   . ASP B  1 81  ? 32.778  68.817 -6.064  1.00 51.60  ? 81  ASP B N   1 
ATOM   2744  C CA  . ASP B  1 81  ? 32.104  69.698 -7.054  1.00 51.74  ? 81  ASP B CA  1 
ATOM   2745  C C   . ASP B  1 81  ? 33.111  70.028 -8.162  1.00 54.96  ? 81  ASP B C   1 
ATOM   2746  O O   . ASP B  1 81  ? 34.248  70.427 -7.822  1.00 55.68  ? 81  ASP B O   1 
ATOM   2747  C CB  . ASP B  1 81  ? 31.545  70.952 -6.380  1.00 49.49  ? 81  ASP B CB  1 
ATOM   2748  C CG  . ASP B  1 81  ? 30.868  70.667 -5.050  1.00 55.36  ? 81  ASP B CG  1 
ATOM   2749  O OD1 . ASP B  1 81  ? 31.555  70.160 -4.142  1.00 70.53  ? 81  ASP B OD1 1 
ATOM   2750  O OD2 . ASP B  1 81  ? 29.659  70.938 -4.936  1.00 61.69  ? 81  ASP B OD2 1 
ATOM   2751  N N   . SER B  1 82  ? 32.713  69.843 -9.426  1.00 53.15  ? 82  SER B N   1 
ATOM   2752  C CA  . SER B  1 82  ? 33.578  70.020 -10.622 1.00 57.73  ? 82  SER B CA  1 
ATOM   2753  C C   . SER B  1 82  ? 33.927  71.501 -10.798 1.00 64.42  ? 82  SER B C   1 
ATOM   2754  O O   . SER B  1 82  ? 33.016  72.343 -10.660 1.00 65.24  ? 82  SER B O   1 
ATOM   2755  C CB  . SER B  1 82  ? 32.920  69.469 -11.857 1.00 62.00  ? 82  SER B CB  1 
ATOM   2756  O OG  . SER B  1 82  ? 33.765  69.607 -12.993 1.00 75.29  ? 82  SER B OG  1 
ATOM   2757  N N   . THR B  1 83  ? 35.197  71.795 -11.093 1.00 68.80  ? 83  THR B N   1 
ATOM   2758  C CA  . THR B  1 83  ? 35.715  73.177 -11.274 1.00 73.45  ? 83  THR B CA  1 
ATOM   2759  C C   . THR B  1 83  ? 36.697  73.245 -12.450 1.00 83.52  ? 83  THR B C   1 
ATOM   2760  O O   . THR B  1 83  ? 37.882  73.549 -12.207 1.00 90.68  ? 83  THR B O   1 
ATOM   2761  C CB  . THR B  1 83  ? 36.395  73.693 -10.000 1.00 80.89  ? 83  THR B CB  1 
ATOM   2762  O OG1 . THR B  1 83  ? 37.488  72.831 -9.678  1.00 104.72 ? 83  THR B OG1 1 
ATOM   2763  C CG2 . THR B  1 83  ? 35.444  73.791 -8.827  1.00 80.64  ? 83  THR B CG2 1 
ATOM   2764  N N   . ALA B  1 84  ? 36.220  72.987 -13.673 1.00 93.03  ? 84  ALA B N   1 
ATOM   2765  C CA  . ALA B  1 84  ? 36.951  73.232 -14.941 1.00 96.83  ? 84  ALA B CA  1 
ATOM   2766  C C   . ALA B  1 84  ? 38.289  72.482 -14.956 1.00 97.23  ? 84  ALA B C   1 
ATOM   2767  O O   . ALA B  1 84  ? 39.341  73.157 -15.002 1.00 105.16 ? 84  ALA B O   1 
ATOM   2768  C CB  . ALA B  1 84  ? 37.175  74.715 -15.116 1.00 97.26  ? 84  ALA B CB  1 
ATOM   2769  N N   . GLY B  1 85  ? 38.250  71.146 -14.930 1.00 90.52  ? 85  GLY B N   1 
ATOM   2770  C CA  . GLY B  1 85  ? 39.447  70.282 -14.975 1.00 91.22  ? 85  GLY B CA  1 
ATOM   2771  C C   . GLY B  1 85  ? 39.899  69.853 -13.588 1.00 91.23  ? 85  GLY B C   1 
ATOM   2772  O O   . GLY B  1 85  ? 40.903  69.118 -13.496 1.00 67.37  ? 85  GLY B O   1 
ATOM   2773  N N   . GLY B  1 86  ? 39.186  70.300 -12.550 1.00 102.51 ? 86  GLY B N   1 
ATOM   2774  C CA  . GLY B  1 86  ? 39.471  69.987 -11.138 1.00 93.24  ? 86  GLY B CA  1 
ATOM   2775  C C   . GLY B  1 86  ? 38.194  69.716 -10.366 1.00 77.56  ? 86  GLY B C   1 
ATOM   2776  O O   . GLY B  1 86  ? 37.126  70.211 -10.782 1.00 86.97  ? 86  GLY B O   1 
ATOM   2777  N N   . TRP B  1 87  ? 38.298  68.933 -9.290  1.00 65.47  ? 87  TRP B N   1 
ATOM   2778  C CA  . TRP B  1 87  ? 37.170  68.552 -8.398  1.00 56.28  ? 87  TRP B CA  1 
ATOM   2779  C C   . TRP B  1 87  ? 37.482  69.015 -6.974  1.00 49.68  ? 87  TRP B C   1 
ATOM   2780  O O   . TRP B  1 87  ? 38.421  68.469 -6.361  1.00 48.70  ? 87  TRP B O   1 
ATOM   2781  C CB  . TRP B  1 87  ? 36.914  67.043 -8.464  1.00 53.18  ? 87  TRP B CB  1 
ATOM   2782  C CG  . TRP B  1 87  ? 36.343  66.601 -9.774  1.00 47.67  ? 87  TRP B CG  1 
ATOM   2783  C CD1 . TRP B  1 87  ? 37.034  66.322 -10.918 1.00 44.66  ? 87  TRP B CD1 1 
ATOM   2784  C CD2 . TRP B  1 87  ? 34.952  66.396 -10.083 1.00 48.36  ? 87  TRP B CD2 1 
ATOM   2785  N NE1 . TRP B  1 87  ? 36.171  65.958 -11.916 1.00 44.49  ? 87  TRP B NE1 1 
ATOM   2786  C CE2 . TRP B  1 87  ? 34.888  65.991 -11.433 1.00 47.00  ? 87  TRP B CE2 1 
ATOM   2787  C CE3 . TRP B  1 87  ? 33.760  66.509 -9.354  1.00 46.48  ? 87  TRP B CE3 1 
ATOM   2788  C CZ2 . TRP B  1 87  ? 33.680  65.696 -12.063 1.00 47.66  ? 87  TRP B CZ2 1 
ATOM   2789  C CZ3 . TRP B  1 87  ? 32.568  66.216 -9.977  1.00 42.58  ? 87  TRP B CZ3 1 
ATOM   2790  C CH2 . TRP B  1 87  ? 32.531  65.816 -11.313 1.00 47.98  ? 87  TRP B CH2 1 
ATOM   2791  N N   . VAL B  1 88  ? 36.720  69.988 -6.475  1.00 48.07  ? 88  VAL B N   1 
ATOM   2792  C CA  . VAL B  1 88  ? 36.982  70.644 -5.161  1.00 50.54  ? 88  VAL B CA  1 
ATOM   2793  C C   . VAL B  1 88  ? 36.186  69.923 -4.079  1.00 46.71  ? 88  VAL B C   1 
ATOM   2794  O O   . VAL B  1 88  ? 34.973  69.764 -4.193  1.00 42.09  ? 88  VAL B O   1 
ATOM   2795  C CB  . VAL B  1 88  ? 36.658  72.149 -5.203  1.00 48.99  ? 88  VAL B CB  1 
ATOM   2796  C CG1 . VAL B  1 88  ? 36.741  72.774 -3.819  1.00 51.62  ? 88  VAL B CG1 1 
ATOM   2797  C CG2 . VAL B  1 88  ? 37.563  72.881 -6.182  1.00 44.52  ? 88  VAL B CG2 1 
ATOM   2798  N N   . PRO B  1 89  ? 36.858  69.476 -2.995  1.00 45.90  ? 89  PRO B N   1 
ATOM   2799  C CA  . PRO B  1 89  ? 36.188  68.783 -1.897  1.00 43.74  ? 89  PRO B CA  1 
ATOM   2800  C C   . PRO B  1 89  ? 35.110  69.666 -1.257  1.00 41.82  ? 89  PRO B C   1 
ATOM   2801  O O   . PRO B  1 89  ? 35.350  70.847 -1.088  1.00 45.01  ? 89  PRO B O   1 
ATOM   2802  C CB  . PRO B  1 89  ? 37.308  68.499 -0.883  1.00 44.95  ? 89  PRO B CB  1 
ATOM   2803  C CG  . PRO B  1 89  ? 38.587  68.595 -1.690  1.00 48.79  ? 89  PRO B CG  1 
ATOM   2804  C CD  . PRO B  1 89  ? 38.303  69.619 -2.768  1.00 49.37  ? 89  PRO B CD  1 
ATOM   2805  N N   . ASN B  1 90  ? 33.956  69.080 -0.934  1.00 45.74  ? 90  ASN B N   1 
ATOM   2806  C CA  . ASN B  1 90  ? 32.881  69.738 -0.145  1.00 45.14  ? 90  ASN B CA  1 
ATOM   2807  C C   . ASN B  1 90  ? 32.860  69.110 1.253   1.00 53.35  ? 90  ASN B C   1 
ATOM   2808  O O   . ASN B  1 90  ? 33.780  68.326 1.561   1.00 56.66  ? 90  ASN B O   1 
ATOM   2809  C CB  . ASN B  1 90  ? 31.526  69.677 -0.856  1.00 46.71  ? 90  ASN B CB  1 
ATOM   2810  C CG  . ASN B  1 90  ? 30.976  68.276 -1.029  1.00 54.48  ? 90  ASN B CG  1 
ATOM   2811  O OD1 . ASN B  1 90  ? 30.986  67.470 -0.099  1.00 60.58  ? 90  ASN B OD1 1 
ATOM   2812  N ND2 . ASN B  1 90  ? 30.454  67.993 -2.211  1.00 55.70  ? 90  ASN B ND2 1 
ATOM   2813  N N   . ASP B  1 91  ? 31.856  69.447 2.067   1.00 58.65  ? 91  ASP B N   1 
ATOM   2814  C CA  . ASP B  1 91  ? 31.749  69.003 3.482   1.00 64.08  ? 91  ASP B CA  1 
ATOM   2815  C C   . ASP B  1 91  ? 31.596  67.481 3.538   1.00 57.57  ? 91  ASP B C   1 
ATOM   2816  O O   . ASP B  1 91  ? 32.056  66.888 4.528   1.00 61.55  ? 91  ASP B O   1 
ATOM   2817  C CB  . ASP B  1 91  ? 30.589  69.701 4.196   1.00 75.90  ? 91  ASP B CB  1 
ATOM   2818  C CG  . ASP B  1 91  ? 30.827  71.184 4.416   1.00 92.42  ? 91  ASP B CG  1 
ATOM   2819  O OD1 . ASP B  1 91  ? 31.834  71.700 3.889   1.00 98.26  ? 91  ASP B OD1 1 
ATOM   2820  O OD2 . ASP B  1 91  ? 30.007  71.810 5.116   1.00 105.80 ? 91  ASP B OD2 1 
ATOM   2821  N N   . GLY B  1 92  ? 30.984  66.883 2.512   1.00 54.72  ? 92  GLY B N   1 
ATOM   2822  C CA  . GLY B  1 92  ? 30.631  65.450 2.475   1.00 62.45  ? 92  GLY B CA  1 
ATOM   2823  C C   . GLY B  1 92  ? 31.783  64.567 2.023   1.00 61.70  ? 92  GLY B C   1 
ATOM   2824  O O   . GLY B  1 92  ? 31.597  63.336 2.017   1.00 64.06  ? 92  GLY B O   1 
ATOM   2825  N N   . ALA B  1 93  ? 32.924  65.162 1.655   1.00 56.96  ? 93  ALA B N   1 
ATOM   2826  C CA  . ALA B  1 93  ? 34.112  64.457 1.119   1.00 52.37  ? 93  ALA B CA  1 
ATOM   2827  C C   . ALA B  1 93  ? 34.668  63.503 2.180   1.00 50.57  ? 93  ALA B C   1 
ATOM   2828  O O   . ALA B  1 93  ? 35.186  62.437 1.801   1.00 50.54  ? 93  ALA B O   1 
ATOM   2829  C CB  . ALA B  1 93  ? 35.159  65.449 0.677   1.00 51.82  ? 93  ALA B CB  1 
ATOM   2830  N N   . ILE B  1 94  ? 34.569  63.880 3.458   1.00 46.13  ? 94  ILE B N   1 
ATOM   2831  C CA  . ILE B  1 94  ? 35.053  63.061 4.609   1.00 46.77  ? 94  ILE B CA  1 
ATOM   2832  C C   . ILE B  1 94  ? 34.282  61.736 4.626   1.00 49.21  ? 94  ILE B C   1 
ATOM   2833  O O   . ILE B  1 94  ? 34.869  60.720 5.041   1.00 47.81  ? 94  ILE B O   1 
ATOM   2834  C CB  . ILE B  1 94  ? 34.906  63.820 5.944   1.00 42.54  ? 94  ILE B CB  1 
ATOM   2835  C CG1 . ILE B  1 94  ? 35.431  62.996 7.123   1.00 46.44  ? 94  ILE B CG1 1 
ATOM   2836  C CG2 . ILE B  1 94  ? 33.468  64.258 6.161   1.00 39.31  ? 94  ILE B CG2 1 
ATOM   2837  C CD1 . ILE B  1 94  ? 35.328  63.686 8.461   1.00 44.85  ? 94  ILE B CD1 1 
ATOM   2838  N N   . ASN B  1 95  ? 33.020  61.753 4.190   1.00 47.22  ? 95  ASN B N   1 
ATOM   2839  C CA  . ASN B  1 95  ? 32.096  60.588 4.257   1.00 48.68  ? 95  ASN B CA  1 
ATOM   2840  C C   . ASN B  1 95  ? 32.649  59.447 3.395   1.00 46.66  ? 95  ASN B C   1 
ATOM   2841  O O   . ASN B  1 95  ? 32.382  58.277 3.729   1.00 48.77  ? 95  ASN B O   1 
ATOM   2842  C CB  . ASN B  1 95  ? 30.671  60.978 3.858   1.00 51.11  ? 95  ASN B CB  1 
ATOM   2843  C CG  . ASN B  1 95  ? 30.055  61.972 4.819   1.00 52.51  ? 95  ASN B CG  1 
ATOM   2844  O OD1 . ASN B  1 95  ? 30.508  62.111 5.953   1.00 55.18  ? 95  ASN B OD1 1 
ATOM   2845  N ND2 . ASN B  1 95  ? 29.021  62.668 4.377   1.00 58.86  ? 95  ASN B ND2 1 
ATOM   2846  N N   . ILE B  1 96  ? 33.404  59.775 2.341   1.00 45.60  ? 96  ILE B N   1 
ATOM   2847  C CA  . ILE B  1 96  ? 34.055  58.780 1.437   1.00 47.00  ? 96  ILE B CA  1 
ATOM   2848  C C   . ILE B  1 96  ? 34.956  57.873 2.282   1.00 47.81  ? 96  ILE B C   1 
ATOM   2849  O O   . ILE B  1 96  ? 34.976  56.655 2.025   1.00 51.70  ? 96  ILE B O   1 
ATOM   2850  C CB  . ILE B  1 96  ? 34.848  59.469 0.308   1.00 44.63  ? 96  ILE B CB  1 
ATOM   2851  C CG1 . ILE B  1 96  ? 33.958  60.358 -0.565  1.00 49.07  ? 96  ILE B CG1 1 
ATOM   2852  C CG2 . ILE B  1 96  ? 35.589  58.434 -0.522  1.00 42.23  ? 96  ILE B CG2 1 
ATOM   2853  C CD1 . ILE B  1 96  ? 34.717  61.175 -1.590  1.00 53.92  ? 96  ILE B CD1 1 
ATOM   2854  N N   . PHE B  1 97  ? 35.665  58.455 3.254   1.00 46.42  ? 97  PHE B N   1 
ATOM   2855  C CA  . PHE B  1 97  ? 36.592  57.755 4.182   1.00 48.33  ? 97  PHE B CA  1 
ATOM   2856  C C   . PHE B  1 97  ? 35.791  57.168 5.348   1.00 48.86  ? 97  PHE B C   1 
ATOM   2857  O O   . PHE B  1 97  ? 36.023  56.002 5.714   1.00 54.04  ? 97  PHE B O   1 
ATOM   2858  C CB  . PHE B  1 97  ? 37.684  58.714 4.657   1.00 47.24  ? 97  PHE B CB  1 
ATOM   2859  C CG  . PHE B  1 97  ? 38.556  59.228 3.541   1.00 53.86  ? 97  PHE B CG  1 
ATOM   2860  C CD1 . PHE B  1 97  ? 39.775  58.633 3.263   1.00 58.32  ? 97  PHE B CD1 1 
ATOM   2861  C CD2 . PHE B  1 97  ? 38.141  60.285 2.747   1.00 57.63  ? 97  PHE B CD2 1 
ATOM   2862  C CE1 . PHE B  1 97  ? 40.569  59.096 2.225   1.00 61.20  ? 97  PHE B CE1 1 
ATOM   2863  C CE2 . PHE B  1 97  ? 38.935  60.749 1.710   1.00 61.57  ? 97  PHE B CE2 1 
ATOM   2864  C CZ  . PHE B  1 97  ? 40.149  60.155 1.453   1.00 64.51  ? 97  PHE B CZ  1 
ATOM   2865  N N   . SER B  1 98  ? 34.874  57.965 5.903   1.00 48.84  ? 98  SER B N   1 
ATOM   2866  C CA  . SER B  1 98  ? 33.917  57.564 6.966   1.00 47.69  ? 98  SER B CA  1 
ATOM   2867  C C   . SER B  1 98  ? 33.266  56.226 6.597   1.00 48.76  ? 98  SER B C   1 
ATOM   2868  O O   . SER B  1 98  ? 33.305  55.296 7.424   1.00 42.99  ? 98  SER B O   1 
ATOM   2869  C CB  . SER B  1 98  ? 32.885  58.639 7.174   1.00 45.82  ? 98  SER B CB  1 
ATOM   2870  O OG  . SER B  1 98  ? 31.962  58.275 8.188   1.00 56.15  ? 98  SER B OG  1 
ATOM   2871  N N   . THR B  1 99  ? 32.700  56.143 5.389   1.00 52.32  ? 99  THR B N   1 
ATOM   2872  C CA  . THR B  1 99  ? 31.915  54.984 4.888   1.00 55.28  ? 99  THR B CA  1 
ATOM   2873  C C   . THR B  1 99  ? 32.792  53.727 4.836   1.00 51.45  ? 99  THR B C   1 
ATOM   2874  O O   . THR B  1 99  ? 32.256  52.635 5.099   1.00 52.44  ? 99  THR B O   1 
ATOM   2875  C CB  . THR B  1 99  ? 31.301  55.286 3.516   1.00 61.25  ? 99  THR B CB  1 
ATOM   2876  O OG1 . THR B  1 99  ? 30.656  56.556 3.606   1.00 62.58  ? 99  THR B OG1 1 
ATOM   2877  C CG2 . THR B  1 99  ? 30.307  54.238 3.067   1.00 71.42  ? 99  THR B CG2 1 
ATOM   2878  N N   . ARG B  1 100 ? 34.078  53.866 4.504   1.00 44.99  ? 100 ARG B N   1 
ATOM   2879  C CA  . ARG B  1 100 ? 35.001  52.711 4.342   1.00 43.50  ? 100 ARG B CA  1 
ATOM   2880  C C   . ARG B  1 100 ? 35.219  52.048 5.708   1.00 40.71  ? 100 ARG B C   1 
ATOM   2881  O O   . ARG B  1 100 ? 35.287  50.805 5.755   1.00 41.18  ? 100 ARG B O   1 
ATOM   2882  C CB  . ARG B  1 100 ? 36.319  53.137 3.691   1.00 43.98  ? 100 ARG B CB  1 
ATOM   2883  C CG  . ARG B  1 100 ? 37.069  51.982 3.043   1.00 50.75  ? 100 ARG B CG  1 
ATOM   2884  C CD  . ARG B  1 100 ? 38.394  52.382 2.424   1.00 60.03  ? 100 ARG B CD  1 
ATOM   2885  N NE  . ARG B  1 100 ? 38.245  53.034 1.131   1.00 61.30  ? 100 ARG B NE  1 
ATOM   2886  C CZ  . ARG B  1 100 ? 38.129  52.392 -0.025  1.00 59.70  ? 100 ARG B CZ  1 
ATOM   2887  N NH1 . ARG B  1 100 ? 38.134  51.071 -0.055  1.00 60.04  ? 100 ARG B NH1 1 
ATOM   2888  N NH2 . ARG B  1 100 ? 38.005  53.073 -1.150  1.00 59.54  ? 100 ARG B NH2 1 
ATOM   2889  N N   . TYR B  1 101 ? 35.312  52.842 6.778   1.00 40.26  ? 101 TYR B N   1 
ATOM   2890  C CA  . TYR B  1 101 ? 35.428  52.348 8.175   1.00 43.88  ? 101 TYR B CA  1 
ATOM   2891  C C   . TYR B  1 101 ? 34.188  51.511 8.507   1.00 45.37  ? 101 TYR B C   1 
ATOM   2892  O O   . TYR B  1 101 ? 34.339  50.369 8.990   1.00 46.72  ? 101 TYR B O   1 
ATOM   2893  C CB  . TYR B  1 101 ? 35.626  53.512 9.149   1.00 43.76  ? 101 TYR B CB  1 
ATOM   2894  C CG  . TYR B  1 101 ? 37.034  54.053 9.182   1.00 46.59  ? 101 TYR B CG  1 
ATOM   2895  C CD1 . TYR B  1 101 ? 38.008  53.461 9.969   1.00 49.22  ? 101 TYR B CD1 1 
ATOM   2896  C CD2 . TYR B  1 101 ? 37.399  55.144 8.412   1.00 49.79  ? 101 TYR B CD2 1 
ATOM   2897  C CE1 . TYR B  1 101 ? 39.307  53.943 9.997   1.00 49.75  ? 101 TYR B CE1 1 
ATOM   2898  C CE2 . TYR B  1 101 ? 38.692  55.641 8.429   1.00 53.48  ? 101 TYR B CE2 1 
ATOM   2899  C CZ  . TYR B  1 101 ? 39.651  55.038 9.225   1.00 51.34  ? 101 TYR B CZ  1 
ATOM   2900  O OH  . TYR B  1 101 ? 40.928  55.523 9.248   1.00 43.05  ? 101 TYR B OH  1 
ATOM   2901  N N   . ILE B  1 102 ? 33.002  52.061 8.233   1.00 47.86  ? 102 ILE B N   1 
ATOM   2902  C CA  . ILE B  1 102 ? 31.692  51.362 8.397   1.00 51.64  ? 102 ILE B CA  1 
ATOM   2903  C C   . ILE B  1 102 ? 31.802  49.971 7.759   1.00 49.62  ? 102 ILE B C   1 
ATOM   2904  O O   . ILE B  1 102 ? 31.436  48.986 8.425   1.00 48.77  ? 102 ILE B O   1 
ATOM   2905  C CB  . ILE B  1 102 ? 30.536  52.180 7.783   1.00 51.18  ? 102 ILE B CB  1 
ATOM   2906  C CG1 . ILE B  1 102 ? 30.387  53.551 8.447   1.00 53.45  ? 102 ILE B CG1 1 
ATOM   2907  C CG2 . ILE B  1 102 ? 29.238  51.390 7.835   1.00 51.71  ? 102 ILE B CG2 1 
ATOM   2908  C CD1 . ILE B  1 102 ? 29.227  54.364 7.919   1.00 49.85  ? 102 ILE B CD1 1 
ATOM   2909  N N   . GLU B  1 103 ? 32.288  49.901 6.516   1.00 43.92  ? 103 GLU B N   1 
ATOM   2910  C CA  . GLU B  1 103 ? 32.478  48.631 5.768   1.00 41.48  ? 103 GLU B CA  1 
ATOM   2911  C C   . GLU B  1 103 ? 33.308  47.667 6.620   1.00 42.03  ? 103 GLU B C   1 
ATOM   2912  O O   . GLU B  1 103 ? 32.785  46.593 6.981   1.00 40.28  ? 103 GLU B O   1 
ATOM   2913  C CB  . GLU B  1 103 ? 33.180  48.877 4.433   1.00 41.69  ? 103 GLU B CB  1 
ATOM   2914  C CG  . GLU B  1 103 ? 33.595  47.595 3.735   1.00 45.11  ? 103 GLU B CG  1 
ATOM   2915  C CD  . GLU B  1 103 ? 34.834  47.720 2.867   1.00 51.35  ? 103 GLU B CD  1 
ATOM   2916  O OE1 . GLU B  1 103 ? 35.486  46.689 2.620   1.00 63.85  ? 103 GLU B OE1 1 
ATOM   2917  O OE2 . GLU B  1 103 ? 35.143  48.849 2.441   1.00 58.36  ? 103 GLU B OE2 1 
ATOM   2918  N N   . TRP B  1 104 ? 34.555  48.051 6.915   1.00 45.44  ? 104 TRP B N   1 
ATOM   2919  C CA  . TRP B  1 104 ? 35.553  47.230 7.652   1.00 41.11  ? 104 TRP B CA  1 
ATOM   2920  C C   . TRP B  1 104 ? 34.936  46.706 8.950   1.00 34.82  ? 104 TRP B C   1 
ATOM   2921  O O   . TRP B  1 104 ? 35.113  45.509 9.248   1.00 33.85  ? 104 TRP B O   1 
ATOM   2922  C CB  . TRP B  1 104 ? 36.824  48.042 7.925   1.00 42.58  ? 104 TRP B CB  1 
ATOM   2923  C CG  . TRP B  1 104 ? 37.565  48.446 6.688   1.00 42.54  ? 104 TRP B CG  1 
ATOM   2924  C CD1 . TRP B  1 104 ? 37.506  47.850 5.463   1.00 42.71  ? 104 TRP B CD1 1 
ATOM   2925  C CD2 . TRP B  1 104 ? 38.509  49.524 6.563   1.00 44.74  ? 104 TRP B CD2 1 
ATOM   2926  N NE1 . TRP B  1 104 ? 38.334  48.492 4.581   1.00 45.29  ? 104 TRP B NE1 1 
ATOM   2927  C CE2 . TRP B  1 104 ? 38.966  49.519 5.228   1.00 45.24  ? 104 TRP B CE2 1 
ATOM   2928  C CE3 . TRP B  1 104 ? 39.011  50.490 7.443   1.00 48.79  ? 104 TRP B CE3 1 
ATOM   2929  C CZ2 . TRP B  1 104 ? 39.893  50.447 4.756   1.00 47.78  ? 104 TRP B CZ2 1 
ATOM   2930  C CZ3 . TRP B  1 104 ? 39.927  51.405 6.975   1.00 50.62  ? 104 TRP B CZ3 1 
ATOM   2931  C CH2 . TRP B  1 104 ? 40.361  51.382 5.649   1.00 48.48  ? 104 TRP B CH2 1 
ATOM   2932  N N   . THR B  1 105 ? 34.242  47.578 9.684   1.00 35.59  ? 105 THR B N   1 
ATOM   2933  C CA  . THR B  1 105 ? 33.617  47.278 10.999  1.00 39.03  ? 105 THR B CA  1 
ATOM   2934  C C   . THR B  1 105 ? 32.887  45.932 10.921  1.00 38.02  ? 105 THR B C   1 
ATOM   2935  O O   . THR B  1 105 ? 32.988  45.158 11.892  1.00 40.07  ? 105 THR B O   1 
ATOM   2936  C CB  . THR B  1 105 ? 32.679  48.412 11.433  1.00 43.16  ? 105 THR B CB  1 
ATOM   2937  O OG1 . THR B  1 105 ? 33.455  49.610 11.516  1.00 45.84  ? 105 THR B OG1 1 
ATOM   2938  C CG2 . THR B  1 105 ? 31.987  48.137 12.751  1.00 40.06  ? 105 THR B CG2 1 
ATOM   2939  N N   . VAL B  1 106 ? 32.197  45.666 9.807   1.00 40.87  ? 106 VAL B N   1 
ATOM   2940  C CA  . VAL B  1 106 ? 31.334  44.459 9.619   1.00 43.89  ? 106 VAL B CA  1 
ATOM   2941  C C   . VAL B  1 106 ? 32.085  43.415 8.786   1.00 42.33  ? 106 VAL B C   1 
ATOM   2942  O O   . VAL B  1 106 ? 32.080  42.233 9.184   1.00 41.45  ? 106 VAL B O   1 
ATOM   2943  C CB  . VAL B  1 106 ? 29.988  44.811 8.956   1.00 47.37  ? 106 VAL B CB  1 
ATOM   2944  C CG1 . VAL B  1 106 ? 29.032  43.629 8.984   1.00 46.42  ? 106 VAL B CG1 1 
ATOM   2945  C CG2 . VAL B  1 106 ? 29.341  46.037 9.580   1.00 51.76  ? 106 VAL B CG2 1 
ATOM   2946  N N   . SER B  1 107 ? 32.690  43.832 7.669   1.00 41.04  ? 107 SER B N   1 
ATOM   2947  C CA  . SER B  1 107 ? 33.305  42.927 6.663   1.00 45.22  ? 107 SER B CA  1 
ATOM   2948  C C   . SER B  1 107 ? 34.445  42.118 7.298   1.00 49.94  ? 107 SER B C   1 
ATOM   2949  O O   . SER B  1 107 ? 34.550  40.911 6.991   1.00 52.95  ? 107 SER B O   1 
ATOM   2950  C CB  . SER B  1 107 ? 33.772  43.689 5.448   1.00 43.93  ? 107 SER B CB  1 
ATOM   2951  O OG  . SER B  1 107 ? 34.745  44.659 5.799   1.00 50.03  ? 107 SER B OG  1 
ATOM   2952  N N   . VAL B  1 108 ? 35.253  42.748 8.157   1.00 53.67  ? 108 VAL B N   1 
ATOM   2953  C CA  . VAL B  1 108 ? 36.486  42.143 8.750   1.00 53.85  ? 108 VAL B CA  1 
ATOM   2954  C C   . VAL B  1 108 ? 36.097  41.037 9.729   1.00 47.90  ? 108 VAL B C   1 
ATOM   2955  O O   . VAL B  1 108 ? 36.522  39.894 9.575   1.00 53.32  ? 108 VAL B O   1 
ATOM   2956  C CB  . VAL B  1 108 ? 37.377  43.207 9.420   1.00 52.70  ? 108 VAL B CB  1 
ATOM   2957  C CG1 . VAL B  1 108 ? 38.467  42.569 10.268  1.00 55.94  ? 108 VAL B CG1 1 
ATOM   2958  C CG2 . VAL B  1 108 ? 37.984  44.155 8.397   1.00 52.14  ? 108 VAL B CG2 1 
ATOM   2959  N N   . PRO B  1 109 ? 35.295  41.336 10.776  1.00 39.72  ? 109 PRO B N   1 
ATOM   2960  C CA  . PRO B  1 109 ? 34.863  40.307 11.724  1.00 38.17  ? 109 PRO B CA  1 
ATOM   2961  C C   . PRO B  1 109 ? 34.361  39.032 11.029  1.00 40.80  ? 109 PRO B C   1 
ATOM   2962  O O   . PRO B  1 109 ? 34.655  37.947 11.505  1.00 39.51  ? 109 PRO B O   1 
ATOM   2963  C CB  . PRO B  1 109 ? 33.734  41.008 12.491  1.00 35.74  ? 109 PRO B CB  1 
ATOM   2964  C CG  . PRO B  1 109 ? 34.130  42.471 12.468  1.00 36.34  ? 109 PRO B CG  1 
ATOM   2965  C CD  . PRO B  1 109 ? 34.781  42.673 11.115  1.00 37.06  ? 109 PRO B CD  1 
ATOM   2966  N N   . LEU B  1 110 ? 33.624  39.191 9.925   1.00 44.79  ? 110 LEU B N   1 
ATOM   2967  C CA  . LEU B  1 110 ? 33.090  38.065 9.111   1.00 44.76  ? 110 LEU B CA  1 
ATOM   2968  C C   . LEU B  1 110 ? 34.259  37.273 8.519   1.00 44.18  ? 110 LEU B C   1 
ATOM   2969  O O   . LEU B  1 110 ? 34.144  36.037 8.419   1.00 39.33  ? 110 LEU B O   1 
ATOM   2970  C CB  . LEU B  1 110 ? 32.179  38.618 8.012   1.00 45.40  ? 110 LEU B CB  1 
ATOM   2971  C CG  . LEU B  1 110 ? 30.817  39.120 8.490   1.00 47.24  ? 110 LEU B CG  1 
ATOM   2972  C CD1 . LEU B  1 110 ? 30.034  39.734 7.341   1.00 48.46  ? 110 LEU B CD1 1 
ATOM   2973  C CD2 . LEU B  1 110 ? 30.022  37.999 9.143   1.00 46.36  ? 110 LEU B CD2 1 
ATOM   2974  N N   . LEU B  1 111 ? 35.341  37.965 8.149   1.00 42.32  ? 111 LEU B N   1 
ATOM   2975  C CA  . LEU B  1 111 ? 36.577  37.349 7.599   1.00 43.20  ? 111 LEU B CA  1 
ATOM   2976  C C   . LEU B  1 111 ? 37.201  36.431 8.655   1.00 48.08  ? 111 LEU B C   1 
ATOM   2977  O O   . LEU B  1 111 ? 37.632  35.326 8.282   1.00 54.16  ? 111 LEU B O   1 
ATOM   2978  C CB  . LEU B  1 111 ? 37.550  38.452 7.172   1.00 40.80  ? 111 LEU B CB  1 
ATOM   2979  C CG  . LEU B  1 111 ? 37.185  39.172 5.876   1.00 43.60  ? 111 LEU B CG  1 
ATOM   2980  C CD1 . LEU B  1 111 ? 38.123  40.342 5.622   1.00 44.12  ? 111 LEU B CD1 1 
ATOM   2981  C CD2 . LEU B  1 111 ? 37.198  38.210 4.697   1.00 43.50  ? 111 LEU B CD2 1 
ATOM   2982  N N   . THR B  1 112 ? 37.252  36.870 9.917   1.00 49.71  ? 112 THR B N   1 
ATOM   2983  C CA  . THR B  1 112 ? 37.764  36.062 11.057  1.00 52.59  ? 112 THR B CA  1 
ATOM   2984  C C   . THR B  1 112 ? 36.924  34.785 11.168  1.00 51.90  ? 112 THR B C   1 
ATOM   2985  O O   . THR B  1 112 ? 37.504  33.685 11.084  1.00 51.92  ? 112 THR B O   1 
ATOM   2986  C CB  . THR B  1 112 ? 37.748  36.850 12.374  1.00 54.75  ? 112 THR B CB  1 
ATOM   2987  O OG1 . THR B  1 112 ? 36.389  37.004 12.783  1.00 65.70  ? 112 THR B OG1 1 
ATOM   2988  C CG2 . THR B  1 112 ? 38.408  38.207 12.260  1.00 54.58  ? 112 THR B CG2 1 
ATOM   2989  N N   . ILE B  1 113 ? 35.608  34.941 11.331  1.00 49.92  ? 113 ILE B N   1 
ATOM   2990  C CA  . ILE B  1 113 ? 34.623  33.825 11.461  1.00 49.08  ? 113 ILE B CA  1 
ATOM   2991  C C   . ILE B  1 113 ? 34.858  32.816 10.331  1.00 46.58  ? 113 ILE B C   1 
ATOM   2992  O O   . ILE B  1 113 ? 34.874  31.599 10.614  1.00 43.50  ? 113 ILE B O   1 
ATOM   2993  C CB  . ILE B  1 113 ? 33.182  34.373 11.441  1.00 47.25  ? 113 ILE B CB  1 
ATOM   2994  C CG1 . ILE B  1 113 ? 32.897  35.257 12.657  1.00 47.22  ? 113 ILE B CG1 1 
ATOM   2995  C CG2 . ILE B  1 113 ? 32.175  33.239 11.320  1.00 45.89  ? 113 ILE B CG2 1 
ATOM   2996  C CD1 . ILE B  1 113 ? 31.722  36.187 12.478  1.00 48.23  ? 113 ILE B CD1 1 
ATOM   2997  N N   . GLU B  1 114 ? 35.026  33.315 9.103   1.00 46.51  ? 114 GLU B N   1 
ATOM   2998  C CA  . GLU B  1 114 ? 35.191  32.499 7.872   1.00 50.77  ? 114 GLU B CA  1 
ATOM   2999  C C   . GLU B  1 114 ? 36.435  31.617 8.012   1.00 53.52  ? 114 GLU B C   1 
ATOM   3000  O O   . GLU B  1 114 ? 36.356  30.433 7.644   1.00 57.84  ? 114 GLU B O   1 
ATOM   3001  C CB  . GLU B  1 114 ? 35.296  33.402 6.641   1.00 58.81  ? 114 GLU B CB  1 
ATOM   3002  C CG  . GLU B  1 114 ? 35.354  32.639 5.330   1.00 62.80  ? 114 GLU B CG  1 
ATOM   3003  C CD  . GLU B  1 114 ? 35.389  33.516 4.089   1.00 74.07  ? 114 GLU B CD  1 
ATOM   3004  O OE1 . GLU B  1 114 ? 35.752  33.000 3.014   1.00 78.85  ? 114 GLU B OE1 1 
ATOM   3005  O OE2 . GLU B  1 114 ? 35.053  34.715 4.200   1.00 91.09  ? 114 GLU B OE2 1 
ATOM   3006  N N   . LEU B  1 115 ? 37.535  32.178 8.525   1.00 54.00  ? 115 LEU B N   1 
ATOM   3007  C CA  . LEU B  1 115 ? 38.830  31.468 8.710   1.00 50.94  ? 115 LEU B CA  1 
ATOM   3008  C C   . LEU B  1 115 ? 38.684  30.426 9.822   1.00 48.55  ? 115 LEU B C   1 
ATOM   3009  O O   . LEU B  1 115 ? 39.136  29.287 9.619   1.00 49.38  ? 115 LEU B O   1 
ATOM   3010  C CB  . LEU B  1 115 ? 39.926  32.482 9.051   1.00 49.20  ? 115 LEU B CB  1 
ATOM   3011  C CG  . LEU B  1 115 ? 41.327  31.896 9.220   1.00 50.84  ? 115 LEU B CG  1 
ATOM   3012  C CD1 . LEU B  1 115 ? 41.744  31.120 7.980   1.00 51.21  ? 115 LEU B CD1 1 
ATOM   3013  C CD2 . LEU B  1 115 ? 42.339  32.986 9.533   1.00 52.61  ? 115 LEU B CD2 1 
ATOM   3014  N N   . LEU B  1 116 ? 38.078  30.811 10.949  1.00 46.13  ? 116 LEU B N   1 
ATOM   3015  C CA  . LEU B  1 116 ? 37.894  29.941 12.140  1.00 50.13  ? 116 LEU B CA  1 
ATOM   3016  C C   . LEU B  1 116 ? 36.965  28.775 11.787  1.00 53.93  ? 116 LEU B C   1 
ATOM   3017  O O   . LEU B  1 116 ? 37.109  27.700 12.404  1.00 53.47  ? 116 LEU B O   1 
ATOM   3018  C CB  . LEU B  1 116 ? 37.325  30.779 13.288  1.00 52.64  ? 116 LEU B CB  1 
ATOM   3019  C CG  . LEU B  1 116 ? 38.281  31.822 13.863  1.00 63.84  ? 116 LEU B CG  1 
ATOM   3020  C CD1 . LEU B  1 116 ? 37.663  32.531 15.057  1.00 68.13  ? 116 LEU B CD1 1 
ATOM   3021  C CD2 . LEU B  1 116 ? 39.607  31.188 14.253  1.00 71.75  ? 116 LEU B CD2 1 
ATOM   3022  N N   . ALA B  1 117 ? 36.055  28.986 10.833  1.00 56.07  ? 117 ALA B N   1 
ATOM   3023  C CA  . ALA B  1 117 ? 35.047  27.995 10.388  1.00 58.50  ? 117 ALA B CA  1 
ATOM   3024  C C   . ALA B  1 117 ? 35.747  26.822 9.691   1.00 56.66  ? 117 ALA B C   1 
ATOM   3025  O O   . ALA B  1 117 ? 35.308  25.673 9.886   1.00 60.56  ? 117 ALA B O   1 
ATOM   3026  C CB  . ALA B  1 117 ? 34.034  28.657 9.482   1.00 63.35  ? 117 ALA B CB  1 
ATOM   3027  N N   . VAL B  1 118 ? 36.796  27.106 8.912   1.00 56.28  ? 118 VAL B N   1 
ATOM   3028  C CA  . VAL B  1 118 ? 37.559  26.090 8.126   1.00 58.09  ? 118 VAL B CA  1 
ATOM   3029  C C   . VAL B  1 118 ? 38.682  25.521 9.000   1.00 64.01  ? 118 VAL B C   1 
ATOM   3030  O O   . VAL B  1 118 ? 39.309  24.531 8.577   1.00 73.03  ? 118 VAL B O   1 
ATOM   3031  C CB  . VAL B  1 118 ? 38.115  26.677 6.814   1.00 56.27  ? 118 VAL B CB  1 
ATOM   3032  C CG1 . VAL B  1 118 ? 37.012  26.914 5.795   1.00 57.48  ? 118 VAL B CG1 1 
ATOM   3033  C CG2 . VAL B  1 118 ? 38.917  27.947 7.050   1.00 55.04  ? 118 VAL B CG2 1 
ATOM   3034  N N   . CYS B  1 119 ? 38.925  26.129 10.166  1.00 68.62  ? 119 CYS B N   1 
ATOM   3035  C CA  . CYS B  1 119 ? 39.870  25.625 11.199  1.00 71.81  ? 119 CYS B CA  1 
ATOM   3036  C C   . CYS B  1 119 ? 39.224  24.446 11.937  1.00 79.56  ? 119 CYS B C   1 
ATOM   3037  O O   . CYS B  1 119 ? 37.979  24.340 11.905  1.00 66.03  ? 119 CYS B O   1 
ATOM   3038  C CB  . CYS B  1 119 ? 40.269  26.728 12.173  1.00 70.89  ? 119 CYS B CB  1 
ATOM   3039  S SG  . CYS B  1 119 ? 41.527  27.851 11.510  1.00 64.69  ? 119 CYS B SG  1 
ATOM   3040  N N   . ALA B  1 120 ? 40.045  23.596 12.562  1.00 95.56  ? 120 ALA B N   1 
ATOM   3041  C CA  . ALA B  1 120 ? 39.643  22.297 13.153  1.00 103.92 ? 120 ALA B CA  1 
ATOM   3042  C C   . ALA B  1 120 ? 39.271  22.472 14.628  1.00 107.03 ? 120 ALA B C   1 
ATOM   3043  O O   . ALA B  1 120 ? 38.856  21.474 15.245  1.00 119.73 ? 120 ALA B O   1 
ATOM   3044  C CB  . ALA B  1 120 ? 40.752  21.285 12.986  1.00 99.93  ? 120 ALA B CB  1 
ATOM   3045  N N   . THR B  1 121 ? 39.404  23.686 15.170  1.00 101.89 ? 121 THR B N   1 
ATOM   3046  C CA  . THR B  1 121 ? 39.070  24.006 16.584  1.00 100.62 ? 121 THR B CA  1 
ATOM   3047  C C   . THR B  1 121 ? 37.644  23.514 16.861  1.00 105.03 ? 121 THR B C   1 
ATOM   3048  O O   . THR B  1 121 ? 36.783  23.696 15.978  1.00 90.50  ? 121 THR B O   1 
ATOM   3049  C CB  . THR B  1 121 ? 39.255  25.501 16.870  1.00 103.45 ? 121 THR B CB  1 
ATOM   3050  O OG1 . THR B  1 121 ? 38.407  26.227 15.980  1.00 122.09 ? 121 THR B OG1 1 
ATOM   3051  C CG2 . THR B  1 121 ? 40.690  25.955 16.706  1.00 101.74 ? 121 THR B CG2 1 
ATOM   3052  N N   . LEU B  1 122 ? 37.417  22.898 18.028  1.00 114.11 ? 122 LEU B N   1 
ATOM   3053  C CA  . LEU B  1 122 ? 36.130  22.253 18.408  1.00 104.76 ? 122 LEU B CA  1 
ATOM   3054  C C   . LEU B  1 122 ? 35.679  22.749 19.790  1.00 102.53 ? 122 LEU B C   1 
ATOM   3055  O O   . LEU B  1 122 ? 36.546  23.122 20.613  1.00 94.38  ? 122 LEU B O   1 
ATOM   3056  C CB  . LEU B  1 122 ? 36.307  20.729 18.407  1.00 103.93 ? 122 LEU B CB  1 
ATOM   3057  C CG  . LEU B  1 122 ? 36.979  20.131 17.170  1.00 111.01 ? 122 LEU B CG  1 
ATOM   3058  C CD1 . LEU B  1 122 ? 37.239  18.643 17.355  1.00 93.09  ? 122 LEU B CD1 1 
ATOM   3059  C CD2 . LEU B  1 122 ? 36.146  20.368 15.919  1.00 124.76 ? 122 LEU B CD2 1 
ATOM   3060  N N   . GLY B  1 123 ? 34.363  22.756 20.020  1.00 108.02 ? 123 GLY B N   1 
ATOM   3061  C CA  . GLY B  1 123 ? 33.736  23.030 21.328  1.00 112.45 ? 123 GLY B CA  1 
ATOM   3062  C C   . GLY B  1 123 ? 33.792  24.501 21.707  1.00 118.71 ? 123 GLY B C   1 
ATOM   3063  O O   . GLY B  1 123 ? 33.441  25.361 20.866  1.00 122.06 ? 123 GLY B O   1 
ATOM   3064  N N   . VAL B  1 124 ? 34.192  24.785 22.949  1.00 119.72 ? 124 VAL B N   1 
ATOM   3065  C CA  . VAL B  1 124 ? 34.181  26.157 23.541  1.00 129.71 ? 124 VAL B CA  1 
ATOM   3066  C C   . VAL B  1 124 ? 35.460  26.889 23.116  1.00 144.66 ? 124 VAL B C   1 
ATOM   3067  O O   . VAL B  1 124 ? 35.387  28.108 22.892  1.00 162.42 ? 124 VAL B O   1 
ATOM   3068  C CB  . VAL B  1 124 ? 34.022  26.130 25.074  1.00 125.67 ? 124 VAL B CB  1 
ATOM   3069  C CG1 . VAL B  1 124 ? 34.008  27.536 25.654  1.00 129.03 ? 124 VAL B CG1 1 
ATOM   3070  C CG2 . VAL B  1 124 ? 32.776  25.371 25.508  1.00 114.38 ? 124 VAL B CG2 1 
ATOM   3071  N N   . GLN B  1 125 ? 36.585  26.176 22.996  1.00 136.53 ? 125 GLN B N   1 
ATOM   3072  C CA  . GLN B  1 125 ? 37.879  26.730 22.507  1.00 120.20 ? 125 GLN B CA  1 
ATOM   3073  C C   . GLN B  1 125 ? 37.642  27.469 21.182  1.00 115.14 ? 125 GLN B C   1 
ATOM   3074  O O   . GLN B  1 125 ? 38.277  28.521 20.960  1.00 118.02 ? 125 GLN B O   1 
ATOM   3075  C CB  . GLN B  1 125 ? 38.906  25.609 22.333  1.00 105.62 ? 125 GLN B CB  1 
ATOM   3076  N N   . ALA B  1 126 ? 36.753  26.932 20.341  1.00 114.54 ? 126 ALA B N   1 
ATOM   3077  C CA  . ALA B  1 126 ? 36.374  27.493 19.023  1.00 106.19 ? 126 ALA B CA  1 
ATOM   3078  C C   . ALA B  1 126 ? 35.477  28.723 19.218  1.00 92.08  ? 126 ALA B C   1 
ATOM   3079  O O   . ALA B  1 126 ? 35.820  29.788 18.682  1.00 94.39  ? 126 ALA B O   1 
ATOM   3080  C CB  . ALA B  1 126 ? 35.701  26.429 18.189  1.00 102.87 ? 126 ALA B CB  1 
ATOM   3081  N N   . ARG B  1 127 ? 34.373  28.583 19.960  1.00 82.86  ? 127 ARG B N   1 
ATOM   3082  C CA  . ARG B  1 127 ? 33.387  29.670 20.218  1.00 82.55  ? 127 ARG B CA  1 
ATOM   3083  C C   . ARG B  1 127 ? 34.066  30.842 20.944  1.00 85.32  ? 127 ARG B C   1 
ATOM   3084  O O   . ARG B  1 127 ? 33.704  31.997 20.661  1.00 81.17  ? 127 ARG B O   1 
ATOM   3085  C CB  . ARG B  1 127 ? 32.201  29.134 21.028  1.00 78.79  ? 127 ARG B CB  1 
ATOM   3086  N N   . ARG B  1 128 ? 35.005  30.559 21.852  1.00 83.58  ? 128 ARG B N   1 
ATOM   3087  C CA  . ARG B  1 128 ? 35.772  31.586 22.611  1.00 81.61  ? 128 ARG B CA  1 
ATOM   3088  C C   . ARG B  1 128 ? 36.654  32.376 21.637  1.00 82.75  ? 128 ARG B C   1 
ATOM   3089  O O   . ARG B  1 128 ? 36.623  33.618 21.688  1.00 83.64  ? 128 ARG B O   1 
ATOM   3090  C CB  . ARG B  1 128 ? 36.612  30.936 23.715  1.00 73.62  ? 128 ARG B CB  1 
ATOM   3091  N N   . ASN B  1 129 ? 37.408  31.676 20.784  1.00 87.46  ? 129 ASN B N   1 
ATOM   3092  C CA  . ASN B  1 129 ? 38.302  32.277 19.757  1.00 91.15  ? 129 ASN B CA  1 
ATOM   3093  C C   . ASN B  1 129 ? 37.504  33.275 18.910  1.00 89.66  ? 129 ASN B C   1 
ATOM   3094  O O   . ASN B  1 129 ? 37.926  34.444 18.824  1.00 94.55  ? 129 ASN B O   1 
ATOM   3095  C CB  . ASN B  1 129 ? 38.949  31.207 18.874  1.00 93.04  ? 129 ASN B CB  1 
ATOM   3096  C CG  . ASN B  1 129 ? 39.982  30.383 19.610  1.00 96.98  ? 129 ASN B CG  1 
ATOM   3097  O OD1 . ASN B  1 129 ? 40.259  30.633 20.781  1.00 104.05 ? 129 ASN B OD1 1 
ATOM   3098  N ND2 . ASN B  1 129 ? 40.561  29.408 18.930  1.00 101.07 ? 129 ASN B ND2 1 
ATOM   3099  N N   . THR B  1 130 ? 36.399  32.822 18.310  1.00 82.54  ? 130 THR B N   1 
ATOM   3100  C CA  . THR B  1 130 ? 35.483  33.642 17.472  1.00 77.40  ? 130 THR B CA  1 
ATOM   3101  C C   . THR B  1 130 ? 35.127  34.931 18.222  1.00 73.40  ? 130 THR B C   1 
ATOM   3102  O O   . THR B  1 130 ? 35.336  36.021 17.654  1.00 68.38  ? 130 THR B O   1 
ATOM   3103  C CB  . THR B  1 130 ? 34.222  32.854 17.092  1.00 73.26  ? 130 THR B CB  1 
ATOM   3104  O OG1 . THR B  1 130 ? 34.624  31.563 16.636  1.00 83.78  ? 130 THR B OG1 1 
ATOM   3105  C CG2 . THR B  1 130 ? 33.398  33.536 16.021  1.00 74.04  ? 130 THR B CG2 1 
ATOM   3106  N N   . ALA B  1 131 ? 34.617  34.801 19.451  1.00 62.11  ? 131 ALA B N   1 
ATOM   3107  C CA  . ALA B  1 131 ? 34.155  35.915 20.313  1.00 57.23  ? 131 ALA B CA  1 
ATOM   3108  C C   . ALA B  1 131 ? 35.262  36.966 20.448  1.00 55.69  ? 131 ALA B C   1 
ATOM   3109  O O   . ALA B  1 131 ? 34.953  38.166 20.328  1.00 57.12  ? 131 ALA B O   1 
ATOM   3110  C CB  . ALA B  1 131 ? 33.735  35.379 21.659  1.00 54.93  ? 131 ALA B CB  1 
ATOM   3111  N N   . ILE B  1 132 ? 36.500  36.526 20.693  1.00 56.10  ? 132 ILE B N   1 
ATOM   3112  C CA  . ILE B  1 132 ? 37.694  37.407 20.873  1.00 59.36  ? 132 ILE B CA  1 
ATOM   3113  C C   . ILE B  1 132 ? 38.044  38.050 19.525  1.00 59.30  ? 132 ILE B C   1 
ATOM   3114  O O   . ILE B  1 132 ? 38.108  39.292 19.465  1.00 54.79  ? 132 ILE B O   1 
ATOM   3115  C CB  . ILE B  1 132 ? 38.878  36.612 21.457  1.00 62.99  ? 132 ILE B CB  1 
ATOM   3116  C CG1 . ILE B  1 132 ? 38.538  36.020 22.827  1.00 66.95  ? 132 ILE B CG1 1 
ATOM   3117  C CG2 . ILE B  1 132 ? 40.131  37.471 21.511  1.00 65.75  ? 132 ILE B CG2 1 
ATOM   3118  C CD1 . ILE B  1 132 ? 39.621  35.137 23.400  1.00 71.23  ? 132 ILE B CD1 1 
ATOM   3119  N N   . ALA B  1 133 ? 38.254  37.230 18.491  1.00 60.33  ? 133 ALA B N   1 
ATOM   3120  C CA  . ALA B  1 133 ? 38.617  37.659 17.119  1.00 66.04  ? 133 ALA B CA  1 
ATOM   3121  C C   . ALA B  1 133 ? 37.627  38.721 16.624  1.00 67.17  ? 133 ALA B C   1 
ATOM   3122  O O   . ALA B  1 133 ? 38.083  39.757 16.106  1.00 64.74  ? 133 ALA B O   1 
ATOM   3123  C CB  . ALA B  1 133 ? 38.646  36.467 16.195  1.00 69.79  ? 133 ALA B CB  1 
ATOM   3124  N N   . VAL B  1 134 ? 36.324  38.463 16.773  1.00 60.69  ? 134 VAL B N   1 
ATOM   3125  C CA  . VAL B  1 134 ? 35.230  39.366 16.307  1.00 56.00  ? 134 VAL B CA  1 
ATOM   3126  C C   . VAL B  1 134 ? 35.344  40.701 17.050  1.00 51.53  ? 134 VAL B C   1 
ATOM   3127  O O   . VAL B  1 134 ? 35.533  41.734 16.379  1.00 58.17  ? 134 VAL B O   1 
ATOM   3128  C CB  . VAL B  1 134 ? 33.840  38.732 16.503  1.00 59.19  ? 134 VAL B CB  1 
ATOM   3129  C CG1 . VAL B  1 134 ? 32.725  39.755 16.346  1.00 59.87  ? 134 VAL B CG1 1 
ATOM   3130  C CG2 . VAL B  1 134 ? 33.621  37.559 15.562  1.00 62.70  ? 134 VAL B CG2 1 
ATOM   3131  N N   . THR B  1 135 ? 35.236  40.675 18.381  1.00 45.99  ? 135 THR B N   1 
ATOM   3132  C CA  . THR B  1 135 ? 35.244  41.887 19.245  1.00 51.66  ? 135 THR B CA  1 
ATOM   3133  C C   . THR B  1 135 ? 36.576  42.624 19.066  1.00 44.97  ? 135 THR B C   1 
ATOM   3134  O O   . THR B  1 135 ? 36.560  43.870 19.040  1.00 47.54  ? 135 THR B O   1 
ATOM   3135  C CB  . THR B  1 135 ? 34.972  41.533 20.712  1.00 53.15  ? 135 THR B CB  1 
ATOM   3136  O OG1 . THR B  1 135 ? 35.962  40.592 21.128  1.00 58.25  ? 135 THR B OG1 1 
ATOM   3137  C CG2 . THR B  1 135 ? 33.589  40.957 20.931  1.00 52.62  ? 135 THR B CG2 1 
ATOM   3138  N N   . ALA B  1 136 ? 37.677  41.878 18.937  1.00 41.68  ? 136 ALA B N   1 
ATOM   3139  C CA  . ALA B  1 136 ? 39.038  42.414 18.706  1.00 44.34  ? 136 ALA B CA  1 
ATOM   3140  C C   . ALA B  1 136 ? 39.044  43.242 17.417  1.00 47.66  ? 136 ALA B C   1 
ATOM   3141  O O   . ALA B  1 136 ? 39.350  44.447 17.498  1.00 54.96  ? 136 ALA B O   1 
ATOM   3142  C CB  . ALA B  1 136 ? 40.038  41.288 18.643  1.00 47.99  ? 136 ALA B CB  1 
ATOM   3143  N N   . THR B  1 137 ? 38.710  42.616 16.283  1.00 50.23  ? 137 THR B N   1 
ATOM   3144  C CA  . THR B  1 137 ? 38.696  43.240 14.930  1.00 47.55  ? 137 THR B CA  1 
ATOM   3145  C C   . THR B  1 137 ? 37.667  44.377 14.896  1.00 46.01  ? 137 THR B C   1 
ATOM   3146  O O   . THR B  1 137 ? 37.976  45.426 14.298  1.00 41.64  ? 137 THR B O   1 
ATOM   3147  C CB  . THR B  1 137 ? 38.435  42.198 13.835  1.00 43.42  ? 137 THR B CB  1 
ATOM   3148  O OG1 . THR B  1 137 ? 37.291  41.426 14.200  1.00 47.49  ? 137 THR B OG1 1 
ATOM   3149  C CG2 . THR B  1 137 ? 39.618  41.281 13.612  1.00 46.52  ? 137 THR B CG2 1 
ATOM   3150  N N   . GLY B  1 138 ? 36.498  44.176 15.512  1.00 42.79  ? 138 GLY B N   1 
ATOM   3151  C CA  . GLY B  1 138 ? 35.458  45.212 15.654  1.00 42.09  ? 138 GLY B CA  1 
ATOM   3152  C C   . GLY B  1 138 ? 36.020  46.460 16.312  1.00 44.81  ? 138 GLY B C   1 
ATOM   3153  O O   . GLY B  1 138 ? 35.914  47.549 15.712  1.00 47.67  ? 138 GLY B O   1 
ATOM   3154  N N   . ALA B  1 139 ? 36.609  46.299 17.502  1.00 44.88  ? 139 ALA B N   1 
ATOM   3155  C CA  . ALA B  1 139 ? 37.263  47.368 18.291  1.00 45.07  ? 139 ALA B CA  1 
ATOM   3156  C C   . ALA B  1 139 ? 38.407  47.987 17.478  1.00 46.73  ? 139 ALA B C   1 
ATOM   3157  O O   . ALA B  1 139 ? 38.491  49.229 17.422  1.00 44.40  ? 139 ALA B O   1 
ATOM   3158  C CB  . ALA B  1 139 ? 37.761  46.800 19.597  1.00 46.13  ? 139 ALA B CB  1 
ATOM   3159  N N   . MET B  1 140 ? 39.255  47.144 16.879  1.00 45.80  ? 140 MET B N   1 
ATOM   3160  C CA  . MET B  1 140 ? 40.407  47.562 16.036  1.00 50.11  ? 140 MET B CA  1 
ATOM   3161  C C   . MET B  1 140 ? 39.958  48.667 15.074  1.00 52.31  ? 140 MET B C   1 
ATOM   3162  O O   . MET B  1 140 ? 40.610  49.731 15.042  1.00 58.45  ? 140 MET B O   1 
ATOM   3163  C CB  . MET B  1 140 ? 40.951  46.382 15.225  1.00 54.53  ? 140 MET B CB  1 
ATOM   3164  C CG  . MET B  1 140 ? 42.040  46.774 14.243  1.00 61.40  ? 140 MET B CG  1 
ATOM   3165  S SD  . MET B  1 140 ? 42.740  45.348 13.368  1.00 76.77  ? 140 MET B SD  1 
ATOM   3166  C CE  . MET B  1 140 ? 41.336  44.854 12.369  1.00 80.66  ? 140 MET B CE  1 
ATOM   3167  N N   . ILE B  1 141 ? 38.882  48.414 14.323  1.00 52.00  ? 141 ILE B N   1 
ATOM   3168  C CA  . ILE B  1 141 ? 38.326  49.345 13.298  1.00 49.58  ? 141 ILE B CA  1 
ATOM   3169  C C   . ILE B  1 141 ? 37.763  50.579 14.007  1.00 47.17  ? 141 ILE B C   1 
ATOM   3170  O O   . ILE B  1 141 ? 38.161  51.700 13.639  1.00 48.71  ? 141 ILE B O   1 
ATOM   3171  C CB  . ILE B  1 141 ? 37.257  48.643 12.436  1.00 48.16  ? 141 ILE B CB  1 
ATOM   3172  C CG1 . ILE B  1 141 ? 37.816  47.393 11.752  1.00 48.68  ? 141 ILE B CG1 1 
ATOM   3173  C CG2 . ILE B  1 141 ? 36.652  49.612 11.433  1.00 50.08  ? 141 ILE B CG2 1 
ATOM   3174  C CD1 . ILE B  1 141 ? 39.015  47.655 10.865  1.00 48.76  ? 141 ILE B CD1 1 
ATOM   3175  N N   . PHE B  1 142 ? 36.874  50.373 14.984  1.00 48.48  ? 142 PHE B N   1 
ATOM   3176  C CA  . PHE B  1 142 ? 36.153  51.450 15.711  1.00 51.47  ? 142 PHE B CA  1 
ATOM   3177  C C   . PHE B  1 142 ? 37.159  52.463 16.266  1.00 49.38  ? 142 PHE B C   1 
ATOM   3178  O O   . PHE B  1 142 ? 36.846  53.668 16.289  1.00 51.65  ? 142 PHE B O   1 
ATOM   3179  C CB  . PHE B  1 142 ? 35.293  50.884 16.843  1.00 50.67  ? 142 PHE B CB  1 
ATOM   3180  C CG  . PHE B  1 142 ? 34.515  51.938 17.589  1.00 52.01  ? 142 PHE B CG  1 
ATOM   3181  C CD1 . PHE B  1 142 ? 34.834  52.271 18.895  1.00 53.92  ? 142 PHE B CD1 1 
ATOM   3182  C CD2 . PHE B  1 142 ? 33.484  52.622 16.966  1.00 53.18  ? 142 PHE B CD2 1 
ATOM   3183  C CE1 . PHE B  1 142 ? 34.120  53.248 19.570  1.00 58.58  ? 142 PHE B CE1 1 
ATOM   3184  C CE2 . PHE B  1 142 ? 32.773  53.601 17.641  1.00 55.72  ? 142 PHE B CE2 1 
ATOM   3185  C CZ  . PHE B  1 142 ? 33.093  53.913 18.941  1.00 57.99  ? 142 PHE B CZ  1 
ATOM   3186  N N   . CYS B  1 143 ? 38.323  51.982 16.708  1.00 50.77  ? 143 CYS B N   1 
ATOM   3187  C CA  . CYS B  1 143 ? 39.430  52.816 17.244  1.00 53.81  ? 143 CYS B CA  1 
ATOM   3188  C C   . CYS B  1 143 ? 39.966  53.725 16.133  1.00 60.85  ? 143 CYS B C   1 
ATOM   3189  O O   . CYS B  1 143 ? 39.926  54.960 16.309  1.00 69.33  ? 143 CYS B O   1 
ATOM   3190  C CB  . CYS B  1 143 ? 40.549  51.950 17.807  1.00 54.75  ? 143 CYS B CB  1 
ATOM   3191  S SG  . CYS B  1 143 ? 40.142  51.221 19.413  1.00 62.79  ? 143 CYS B SG  1 
ATOM   3192  N N   . GLY B  1 144 ? 40.442  53.129 15.035  1.00 57.42  ? 144 GLY B N   1 
ATOM   3193  C CA  . GLY B  1 144 ? 40.915  53.853 13.841  1.00 54.13  ? 144 GLY B CA  1 
ATOM   3194  C C   . GLY B  1 144 ? 39.917  54.912 13.405  1.00 53.20  ? 144 GLY B C   1 
ATOM   3195  O O   . GLY B  1 144 ? 40.359  55.993 12.967  1.00 55.29  ? 144 GLY B O   1 
ATOM   3196  N N   . PHE B  1 145 ? 38.618  54.614 13.527  1.00 57.32  ? 145 PHE B N   1 
ATOM   3197  C CA  . PHE B  1 145 ? 37.492  55.515 13.164  1.00 57.14  ? 145 PHE B CA  1 
ATOM   3198  C C   . PHE B  1 145 ? 37.524  56.759 14.058  1.00 54.83  ? 145 PHE B C   1 
ATOM   3199  O O   . PHE B  1 145 ? 37.438  57.885 13.525  1.00 50.19  ? 145 PHE B O   1 
ATOM   3200  C CB  . PHE B  1 145 ? 36.152  54.781 13.278  1.00 56.54  ? 145 PHE B CB  1 
ATOM   3201  C CG  . PHE B  1 145 ? 34.947  55.610 12.906  1.00 53.82  ? 145 PHE B CG  1 
ATOM   3202  C CD1 . PHE B  1 145 ? 33.925  55.826 13.816  1.00 58.15  ? 145 PHE B CD1 1 
ATOM   3203  C CD2 . PHE B  1 145 ? 34.840  56.185 11.649  1.00 51.28  ? 145 PHE B CD2 1 
ATOM   3204  C CE1 . PHE B  1 145 ? 32.819  56.590 13.474  1.00 60.21  ? 145 PHE B CE1 1 
ATOM   3205  C CE2 . PHE B  1 145 ? 33.733  56.947 11.307  1.00 49.92  ? 145 PHE B CE2 1 
ATOM   3206  C CZ  . PHE B  1 145 ? 32.725  57.149 12.220  1.00 53.42  ? 145 PHE B CZ  1 
ATOM   3207  N N   . LEU B  1 146 ? 37.648  56.557 15.373  1.00 51.97  ? 146 LEU B N   1 
ATOM   3208  C CA  . LEU B  1 146 ? 37.711  57.646 16.385  1.00 53.75  ? 146 LEU B CA  1 
ATOM   3209  C C   . LEU B  1 146 ? 38.887  58.576 16.061  1.00 51.21  ? 146 LEU B C   1 
ATOM   3210  O O   . LEU B  1 146 ? 38.686  59.808 16.044  1.00 51.87  ? 146 LEU B O   1 
ATOM   3211  C CB  . LEU B  1 146 ? 37.860  57.032 17.781  1.00 55.33  ? 146 LEU B CB  1 
ATOM   3212  C CG  . LEU B  1 146 ? 36.611  56.354 18.345  1.00 57.48  ? 146 LEU B CG  1 
ATOM   3213  C CD1 . LEU B  1 146 ? 36.870  55.823 19.745  1.00 57.82  ? 146 LEU B CD1 1 
ATOM   3214  C CD2 . LEU B  1 146 ? 35.421  57.302 18.351  1.00 58.38  ? 146 LEU B CD2 1 
ATOM   3215  N N   . GLY B  1 147 ? 40.064  57.998 15.803  1.00 43.55  ? 147 GLY B N   1 
ATOM   3216  C CA  . GLY B  1 147 ? 41.314  58.735 15.540  1.00 42.52  ? 147 GLY B CA  1 
ATOM   3217  C C   . GLY B  1 147 ? 41.234  59.572 14.275  1.00 43.67  ? 147 GLY B C   1 
ATOM   3218  O O   . GLY B  1 147 ? 41.503  60.784 14.353  1.00 42.78  ? 147 GLY B O   1 
ATOM   3219  N N   . ALA B  1 148 ? 40.868  58.950 13.151  1.00 47.57  ? 148 ALA B N   1 
ATOM   3220  C CA  . ALA B  1 148 ? 41.011  59.506 11.785  1.00 49.73  ? 148 ALA B CA  1 
ATOM   3221  C C   . ALA B  1 148 ? 39.808  60.380 11.410  1.00 47.64  ? 148 ALA B C   1 
ATOM   3222  O O   . ALA B  1 148 ? 39.978  61.253 10.534  1.00 52.50  ? 148 ALA B O   1 
ATOM   3223  C CB  . ALA B  1 148 ? 41.188  58.380 10.796  1.00 48.50  ? 148 ALA B CB  1 
ATOM   3224  N N   . ILE B  1 149 ? 38.645  60.160 12.034  1.00 44.90  ? 149 ILE B N   1 
ATOM   3225  C CA  . ILE B  1 149 ? 37.347  60.748 11.584  1.00 49.29  ? 149 ILE B CA  1 
ATOM   3226  C C   . ILE B  1 149 ? 36.674  61.512 12.730  1.00 54.37  ? 149 ILE B C   1 
ATOM   3227  O O   . ILE B  1 149 ? 36.505  62.739 12.600  1.00 58.51  ? 149 ILE B O   1 
ATOM   3228  C CB  . ILE B  1 149 ? 36.418  59.651 11.024  1.00 47.77  ? 149 ILE B CB  1 
ATOM   3229  C CG1 . ILE B  1 149 ? 37.023  58.962 9.799   1.00 51.86  ? 149 ILE B CG1 1 
ATOM   3230  C CG2 . ILE B  1 149 ? 35.039  60.215 10.722  1.00 45.49  ? 149 ILE B CG2 1 
ATOM   3231  C CD1 . ILE B  1 149 ? 37.009  59.807 8.542   1.00 56.74  ? 149 ILE B CD1 1 
ATOM   3232  N N   . VAL B  1 150 ? 36.286  60.807 13.796  1.00 60.55  ? 150 VAL B N   1 
ATOM   3233  C CA  . VAL B  1 150 ? 35.319  61.295 14.826  1.00 64.84  ? 150 VAL B CA  1 
ATOM   3234  C C   . VAL B  1 150 ? 35.931  62.462 15.613  1.00 65.84  ? 150 VAL B C   1 
ATOM   3235  O O   . VAL B  1 150 ? 35.308  63.544 15.641  1.00 60.82  ? 150 VAL B O   1 
ATOM   3236  C CB  . VAL B  1 150 ? 34.883  60.154 15.763  1.00 66.26  ? 150 VAL B CB  1 
ATOM   3237  C CG1 . VAL B  1 150 ? 33.934  60.646 16.845  1.00 64.41  ? 150 VAL B CG1 1 
ATOM   3238  C CG2 . VAL B  1 150 ? 34.264  58.998 14.990  1.00 66.92  ? 150 VAL B CG2 1 
ATOM   3239  N N   . ILE B  1 151 ? 37.096  62.245 16.232  1.00 63.80  ? 151 ILE B N   1 
ATOM   3240  C CA  . ILE B  1 151 ? 37.728  63.189 17.204  1.00 59.63  ? 151 ILE B CA  1 
ATOM   3241  C C   . ILE B  1 151 ? 38.270  64.414 16.457  1.00 62.19  ? 151 ILE B C   1 
ATOM   3242  O O   . ILE B  1 151 ? 39.207  64.251 15.650  1.00 59.99  ? 151 ILE B O   1 
ATOM   3243  C CB  . ILE B  1 151 ? 38.831  62.478 18.012  1.00 57.58  ? 151 ILE B CB  1 
ATOM   3244  C CG1 . ILE B  1 151 ? 38.255  61.372 18.898  1.00 52.46  ? 151 ILE B CG1 1 
ATOM   3245  C CG2 . ILE B  1 151 ? 39.638  63.482 18.821  1.00 59.31  ? 151 ILE B CG2 1 
ATOM   3246  C CD1 . ILE B  1 151 ? 39.301  60.554 19.614  1.00 53.28  ? 151 ILE B CD1 1 
ATOM   3247  N N   . ASP B  1 152 ? 37.702  65.592 16.736  1.00 66.99  ? 152 ASP B N   1 
ATOM   3248  C CA  . ASP B  1 152 ? 38.140  66.903 16.185  1.00 68.58  ? 152 ASP B CA  1 
ATOM   3249  C C   . ASP B  1 152 ? 38.285  66.788 14.663  1.00 67.43  ? 152 ASP B C   1 
ATOM   3250  O O   . ASP B  1 152 ? 39.302  67.270 14.125  1.00 76.24  ? 152 ASP B O   1 
ATOM   3251  C CB  . ASP B  1 152 ? 39.439  67.370 16.850  1.00 72.96  ? 152 ASP B CB  1 
ATOM   3252  C CG  . ASP B  1 152 ? 39.336  67.519 18.361  1.00 72.08  ? 152 ASP B CG  1 
ATOM   3253  O OD1 . ASP B  1 152 ? 38.277  67.976 18.836  1.00 66.43  ? 152 ASP B OD1 1 
ATOM   3254  O OD2 . ASP B  1 152 ? 40.314  67.169 19.052  1.00 68.46  ? 152 ASP B OD2 1 
ATOM   3255  N N   . ASN B  1 153 ? 37.302  66.163 14.008  1.00 64.89  ? 153 ASN B N   1 
ATOM   3256  C CA  . ASN B  1 153 ? 37.208  66.029 12.528  1.00 63.53  ? 153 ASN B CA  1 
ATOM   3257  C C   . ASN B  1 153 ? 38.497  65.413 11.975  1.00 58.49  ? 153 ASN B C   1 
ATOM   3258  O O   . ASN B  1 153 ? 38.799  65.655 10.792  1.00 53.68  ? 153 ASN B O   1 
ATOM   3259  C CB  . ASN B  1 153 ? 36.917  67.376 11.864  1.00 66.28  ? 153 ASN B CB  1 
ATOM   3260  C CG  . ASN B  1 153 ? 35.745  68.090 12.497  1.00 71.09  ? 153 ASN B CG  1 
ATOM   3261  O OD1 . ASN B  1 153 ? 34.873  67.455 13.086  1.00 80.73  ? 153 ASN B OD1 1 
ATOM   3262  N ND2 . ASN B  1 153 ? 35.722  69.407 12.390  1.00 80.79  ? 153 ASN B ND2 1 
ATOM   3263  N N   . GLY B  1 154 ? 39.220  64.651 12.803  1.00 59.43  ? 154 GLY B N   1 
ATOM   3264  C CA  . GLY B  1 154 ? 40.419  63.887 12.405  1.00 64.37  ? 154 GLY B CA  1 
ATOM   3265  C C   . GLY B  1 154 ? 41.597  64.788 12.079  1.00 68.29  ? 154 GLY B C   1 
ATOM   3266  O O   . GLY B  1 154 ? 42.427  64.391 11.236  1.00 75.14  ? 154 GLY B O   1 
ATOM   3267  N N   . THR B  1 155 ? 41.673  65.956 12.724  1.00 71.28  ? 155 THR B N   1 
ATOM   3268  C CA  . THR B  1 155 ? 42.751  66.964 12.535  1.00 66.88  ? 155 THR B CA  1 
ATOM   3269  C C   . THR B  1 155 ? 43.744  66.873 13.700  1.00 66.70  ? 155 THR B C   1 
ATOM   3270  O O   . THR B  1 155 ? 44.932  67.195 13.494  1.00 70.81  ? 155 THR B O   1 
ATOM   3271  C CB  . THR B  1 155 ? 42.163  68.373 12.392  1.00 65.59  ? 155 THR B CB  1 
ATOM   3272  O OG1 . THR B  1 155 ? 41.356  68.638 13.541  1.00 76.13  ? 155 THR B OG1 1 
ATOM   3273  C CG2 . THR B  1 155 ? 41.333  68.538 11.138  1.00 63.56  ? 155 THR B CG2 1 
ATOM   3274  N N   . ASN B  1 156 ? 43.268  66.440 14.872  1.00 62.68  ? 156 ASN B N   1 
ATOM   3275  C CA  . ASN B  1 156 ? 44.068  66.295 16.118  1.00 66.21  ? 156 ASN B CA  1 
ATOM   3276  C C   . ASN B  1 156 ? 45.098  65.173 15.930  1.00 63.57  ? 156 ASN B C   1 
ATOM   3277  O O   . ASN B  1 156 ? 44.692  63.993 15.927  1.00 66.54  ? 156 ASN B O   1 
ATOM   3278  C CB  . ASN B  1 156 ? 43.160  66.040 17.324  1.00 66.44  ? 156 ASN B CB  1 
ATOM   3279  C CG  . ASN B  1 156 ? 43.927  65.786 18.604  1.00 65.09  ? 156 ASN B CG  1 
ATOM   3280  O OD1 . ASN B  1 156 ? 45.083  65.369 18.570  1.00 68.85  ? 156 ASN B OD1 1 
ATOM   3281  N ND2 . ASN B  1 156 ? 43.289  66.028 19.736  1.00 64.77  ? 156 ASN B ND2 1 
ATOM   3282  N N   . THR B  1 157 ? 46.379  65.536 15.796  1.00 63.33  ? 157 THR B N   1 
ATOM   3283  C CA  . THR B  1 157 ? 47.517  64.608 15.546  1.00 60.30  ? 157 THR B CA  1 
ATOM   3284  C C   . THR B  1 157 ? 47.729  63.698 16.763  1.00 55.02  ? 157 THR B C   1 
ATOM   3285  O O   . THR B  1 157 ? 48.203  62.560 16.573  1.00 51.18  ? 157 THR B O   1 
ATOM   3286  C CB  . THR B  1 157 ? 48.801  65.378 15.206  1.00 59.00  ? 157 THR B CB  1 
ATOM   3287  O OG1 . THR B  1 157 ? 48.483  66.382 14.239  1.00 51.89  ? 157 THR B OG1 1 
ATOM   3288  C CG2 . THR B  1 157 ? 49.900  64.484 14.671  1.00 56.57  ? 157 THR B CG2 1 
ATOM   3289  N N   . GLY B  1 158 ? 47.406  64.187 17.963  1.00 56.48  ? 158 GLY B N   1 
ATOM   3290  C CA  . GLY B  1 158 ? 47.501  63.418 19.219  1.00 58.17  ? 158 GLY B CA  1 
ATOM   3291  C C   . GLY B  1 158 ? 46.621  62.182 19.175  1.00 59.03  ? 158 GLY B C   1 
ATOM   3292  O O   . GLY B  1 158 ? 47.170  61.063 19.194  1.00 53.30  ? 158 GLY B O   1 
ATOM   3293  N N   . ALA B  1 159 ? 45.301  62.384 19.104  1.00 68.11  ? 159 ALA B N   1 
ATOM   3294  C CA  . ALA B  1 159 ? 44.266  61.325 19.046  1.00 68.86  ? 159 ALA B CA  1 
ATOM   3295  C C   . ALA B  1 159 ? 44.536  60.409 17.847  1.00 62.72  ? 159 ALA B C   1 
ATOM   3296  O O   . ALA B  1 159 ? 44.460  59.172 18.012  1.00 57.36  ? 159 ALA B O   1 
ATOM   3297  C CB  . ALA B  1 159 ? 42.897  61.954 18.958  1.00 73.84  ? 159 ALA B CB  1 
ATOM   3298  N N   . PHE B  1 160 ? 44.835  61.007 16.690  1.00 57.20  ? 160 PHE B N   1 
ATOM   3299  C CA  . PHE B  1 160 ? 45.125  60.309 15.411  1.00 55.52  ? 160 PHE B CA  1 
ATOM   3300  C C   . PHE B  1 160 ? 46.135  59.185 15.665  1.00 58.19  ? 160 PHE B C   1 
ATOM   3301  O O   . PHE B  1 160 ? 45.885  58.044 15.231  1.00 63.99  ? 160 PHE B O   1 
ATOM   3302  C CB  . PHE B  1 160 ? 45.646  61.304 14.371  1.00 54.55  ? 160 PHE B CB  1 
ATOM   3303  C CG  . PHE B  1 160 ? 45.805  60.741 12.982  1.00 56.22  ? 160 PHE B CG  1 
ATOM   3304  C CD1 . PHE B  1 160 ? 47.033  60.275 12.540  1.00 56.18  ? 160 PHE B CD1 1 
ATOM   3305  C CD2 . PHE B  1 160 ? 44.727  60.687 12.111  1.00 57.95  ? 160 PHE B CD2 1 
ATOM   3306  C CE1 . PHE B  1 160 ? 47.178  59.764 11.260  1.00 56.14  ? 160 PHE B CE1 1 
ATOM   3307  C CE2 . PHE B  1 160 ? 44.874  60.173 10.832  1.00 59.76  ? 160 PHE B CE2 1 
ATOM   3308  C CZ  . PHE B  1 160 ? 46.099  59.712 10.409  1.00 56.86  ? 160 PHE B CZ  1 
ATOM   3309  N N   . ILE B  1 161 ? 47.234  59.502 16.358  1.00 56.34  ? 161 ILE B N   1 
ATOM   3310  C CA  . ILE B  1 161 ? 48.349  58.552 16.654  1.00 56.98  ? 161 ILE B CA  1 
ATOM   3311  C C   . ILE B  1 161 ? 47.962  57.680 17.853  1.00 53.98  ? 161 ILE B C   1 
ATOM   3312  O O   . ILE B  1 161 ? 48.186  56.457 17.785  1.00 55.30  ? 161 ILE B O   1 
ATOM   3313  C CB  . ILE B  1 161 ? 49.674  59.303 16.896  1.00 57.42  ? 161 ILE B CB  1 
ATOM   3314  C CG1 . ILE B  1 161 ? 50.135  60.051 15.642  1.00 58.86  ? 161 ILE B CG1 1 
ATOM   3315  C CG2 . ILE B  1 161 ? 50.744  58.349 17.406  1.00 57.80  ? 161 ILE B CG2 1 
ATOM   3316  C CD1 . ILE B  1 161 ? 51.571  60.515 15.695  1.00 57.88  ? 161 ILE B CD1 1 
ATOM   3317  N N   . LEU B  1 162 ? 47.408  58.287 18.906  1.00 52.93  ? 162 LEU B N   1 
ATOM   3318  C CA  . LEU B  1 162 ? 46.992  57.583 20.149  1.00 56.88  ? 162 LEU B CA  1 
ATOM   3319  C C   . LEU B  1 162 ? 46.155  56.353 19.777  1.00 60.05  ? 162 LEU B C   1 
ATOM   3320  O O   . LEU B  1 162 ? 46.616  55.221 20.037  1.00 55.61  ? 162 LEU B O   1 
ATOM   3321  C CB  . LEU B  1 162 ? 46.188  58.542 21.034  1.00 57.03  ? 162 LEU B CB  1 
ATOM   3322  C CG  . LEU B  1 162 ? 46.033  58.122 22.496  1.00 58.94  ? 162 LEU B CG  1 
ATOM   3323  C CD1 . LEU B  1 162 ? 44.803  58.768 23.119  1.00 59.94  ? 162 LEU B CD1 1 
ATOM   3324  C CD2 . LEU B  1 162 ? 45.958  56.608 22.632  1.00 57.91  ? 162 LEU B CD2 1 
ATOM   3325  N N   . TRP B  1 163 ? 44.983  56.581 19.175  1.00 63.11  ? 163 TRP B N   1 
ATOM   3326  C CA  . TRP B  1 163 ? 43.939  55.552 18.917  1.00 63.16  ? 163 TRP B CA  1 
ATOM   3327  C C   . TRP B  1 163 ? 44.424  54.542 17.870  1.00 59.45  ? 163 TRP B C   1 
ATOM   3328  O O   . TRP B  1 163 ? 43.996  53.373 17.940  1.00 55.27  ? 163 TRP B O   1 
ATOM   3329  C CB  . TRP B  1 163 ? 42.621  56.220 18.511  1.00 61.13  ? 163 TRP B CB  1 
ATOM   3330  C CG  . TRP B  1 163 ? 41.927  56.888 19.658  1.00 63.60  ? 163 TRP B CG  1 
ATOM   3331  C CD1 . TRP B  1 163 ? 41.956  58.214 19.980  1.00 64.49  ? 163 TRP B CD1 1 
ATOM   3332  C CD2 . TRP B  1 163 ? 41.118  56.250 20.663  1.00 62.38  ? 163 TRP B CD2 1 
ATOM   3333  N NE1 . TRP B  1 163 ? 41.215  58.446 21.107  1.00 67.31  ? 163 TRP B NE1 1 
ATOM   3334  C CE2 . TRP B  1 163 ? 40.690  57.261 21.550  1.00 62.65  ? 163 TRP B CE2 1 
ATOM   3335  C CE3 . TRP B  1 163 ? 40.714  54.931 20.900  1.00 63.19  ? 163 TRP B CE3 1 
ATOM   3336  C CZ2 . TRP B  1 163 ? 39.875  56.991 22.649  1.00 62.40  ? 163 TRP B CZ2 1 
ATOM   3337  C CZ3 . TRP B  1 163 ? 39.911  54.666 21.988  1.00 66.09  ? 163 TRP B CZ3 1 
ATOM   3338  C CH2 . TRP B  1 163 ? 39.499  55.683 22.849  1.00 62.95  ? 163 TRP B CH2 1 
ATOM   3339  N N   . ALA B  1 164 ? 45.284  54.969 16.942  1.00 55.50  ? 164 ALA B N   1 
ATOM   3340  C CA  . ALA B  1 164 ? 45.960  54.085 15.965  1.00 55.02  ? 164 ALA B CA  1 
ATOM   3341  C C   . ALA B  1 164 ? 46.752  53.016 16.727  1.00 59.11  ? 164 ALA B C   1 
ATOM   3342  O O   . ALA B  1 164 ? 46.786  51.857 16.264  1.00 67.99  ? 164 ALA B O   1 
ATOM   3343  C CB  . ALA B  1 164 ? 46.854  54.896 15.059  1.00 55.53  ? 164 ALA B CB  1 
ATOM   3344  N N   . VAL B  1 165 ? 47.357  53.400 17.856  1.00 56.06  ? 165 VAL B N   1 
ATOM   3345  C CA  . VAL B  1 165 ? 48.173  52.506 18.730  1.00 53.29  ? 165 VAL B CA  1 
ATOM   3346  C C   . VAL B  1 165 ? 47.228  51.568 19.487  1.00 51.03  ? 165 VAL B C   1 
ATOM   3347  O O   . VAL B  1 165 ? 47.437  50.338 19.422  1.00 48.24  ? 165 VAL B O   1 
ATOM   3348  C CB  . VAL B  1 165 ? 49.061  53.319 19.691  1.00 54.23  ? 165 VAL B CB  1 
ATOM   3349  C CG1 . VAL B  1 165 ? 49.653  52.449 20.790  1.00 57.66  ? 165 VAL B CG1 1 
ATOM   3350  C CG2 . VAL B  1 165 ? 50.159  54.061 18.942  1.00 51.15  ? 165 VAL B CG2 1 
ATOM   3351  N N   . ILE B  1 166 ? 46.228  52.133 20.172  1.00 48.58  ? 166 ILE B N   1 
ATOM   3352  C CA  . ILE B  1 166 ? 45.143  51.367 20.855  1.00 51.64  ? 166 ILE B CA  1 
ATOM   3353  C C   . ILE B  1 166 ? 44.597  50.334 19.864  1.00 55.45  ? 166 ILE B C   1 
ATOM   3354  O O   . ILE B  1 166 ? 44.426  49.164 20.259  1.00 53.99  ? 166 ILE B O   1 
ATOM   3355  C CB  . ILE B  1 166 ? 44.033  52.308 21.363  1.00 49.98  ? 166 ILE B CB  1 
ATOM   3356  C CG1 . ILE B  1 166 ? 44.571  53.331 22.366  1.00 54.42  ? 166 ILE B CG1 1 
ATOM   3357  C CG2 . ILE B  1 166 ? 42.872  51.512 21.936  1.00 47.88  ? 166 ILE B CG2 1 
ATOM   3358  C CD1 . ILE B  1 166 ? 43.512  54.239 22.941  1.00 55.86  ? 166 ILE B CD1 1 
ATOM   3359  N N   . SER B  1 167 ? 44.335  50.766 18.626  1.00 56.36  ? 167 SER B N   1 
ATOM   3360  C CA  . SER B  1 167 ? 43.879  49.912 17.499  1.00 54.37  ? 167 SER B CA  1 
ATOM   3361  C C   . SER B  1 167 ? 44.851  48.739 17.323  1.00 50.48  ? 167 SER B C   1 
ATOM   3362  O O   . SER B  1 167 ? 44.394  47.579 17.372  1.00 43.33  ? 167 SER B O   1 
ATOM   3363  C CB  . SER B  1 167 ? 43.741  50.719 16.231  1.00 55.34  ? 167 SER B CB  1 
ATOM   3364  O OG  . SER B  1 167 ? 43.419  49.887 15.126  1.00 60.95  ? 167 SER B OG  1 
ATOM   3365  N N   . CYS B  1 168 ? 46.143  49.039 17.145  1.00 49.83  ? 168 CYS B N   1 
ATOM   3366  C CA  . CYS B  1 168 ? 47.220  48.045 16.886  1.00 53.17  ? 168 CYS B CA  1 
ATOM   3367  C C   . CYS B  1 168 ? 47.258  47.000 18.005  1.00 53.59  ? 168 CYS B C   1 
ATOM   3368  O O   . CYS B  1 168 ? 47.578  45.834 17.706  1.00 58.59  ? 168 CYS B O   1 
ATOM   3369  C CB  . CYS B  1 168 ? 48.579  48.719 16.755  1.00 54.65  ? 168 CYS B CB  1 
ATOM   3370  S SG  . CYS B  1 168 ? 48.759  49.648 15.211  1.00 71.02  ? 168 CYS B SG  1 
ATOM   3371  N N   . VAL B  1 169 ? 46.958  47.405 19.242  1.00 55.12  ? 169 VAL B N   1 
ATOM   3372  C CA  . VAL B  1 169 ? 46.830  46.481 20.408  1.00 58.41  ? 169 VAL B CA  1 
ATOM   3373  C C   . VAL B  1 169 ? 45.841  45.377 20.023  1.00 65.62  ? 169 VAL B C   1 
ATOM   3374  O O   . VAL B  1 169 ? 46.255  44.197 19.982  1.00 71.25  ? 169 VAL B O   1 
ATOM   3375  C CB  . VAL B  1 169 ? 46.381  47.226 21.680  1.00 59.12  ? 169 VAL B CB  1 
ATOM   3376  C CG1 . VAL B  1 169 ? 45.899  46.266 22.758  1.00 55.48  ? 169 VAL B CG1 1 
ATOM   3377  C CG2 . VAL B  1 169 ? 47.479  48.132 22.216  1.00 57.16  ? 169 VAL B CG2 1 
ATOM   3378  N N   . PHE B  1 170 ? 44.593  45.760 19.732  1.00 69.72  ? 170 PHE B N   1 
ATOM   3379  C CA  . PHE B  1 170 ? 43.494  44.855 19.304  1.00 68.96  ? 170 PHE B CA  1 
ATOM   3380  C C   . PHE B  1 170 ? 43.956  44.039 18.090  1.00 65.21  ? 170 PHE B C   1 
ATOM   3381  O O   . PHE B  1 170 ? 43.701  42.817 18.055  1.00 66.07  ? 170 PHE B O   1 
ATOM   3382  C CB  . PHE B  1 170 ? 42.221  45.653 19.003  1.00 68.00  ? 170 PHE B CB  1 
ATOM   3383  C CG  . PHE B  1 170 ? 41.547  46.249 20.216  1.00 68.00  ? 170 PHE B CG  1 
ATOM   3384  C CD1 . PHE B  1 170 ? 40.939  45.437 21.162  1.00 63.11  ? 170 PHE B CD1 1 
ATOM   3385  C CD2 . PHE B  1 170 ? 41.514  47.621 20.412  1.00 65.07  ? 170 PHE B CD2 1 
ATOM   3386  C CE1 . PHE B  1 170 ? 40.317  45.983 22.274  1.00 56.06  ? 170 PHE B CE1 1 
ATOM   3387  C CE2 . PHE B  1 170 ? 40.893  48.166 21.526  1.00 56.67  ? 170 PHE B CE2 1 
ATOM   3388  C CZ  . PHE B  1 170 ? 40.295  47.346 22.454  1.00 53.50  ? 170 PHE B CZ  1 
ATOM   3389  N N   . TRP B  1 171 ? 44.623  44.695 17.133  1.00 56.51  ? 171 TRP B N   1 
ATOM   3390  C CA  . TRP B  1 171 ? 45.159  44.065 15.896  1.00 59.90  ? 171 TRP B CA  1 
ATOM   3391  C C   . TRP B  1 171 ? 45.978  42.824 16.266  1.00 63.61  ? 171 TRP B C   1 
ATOM   3392  O O   . TRP B  1 171 ? 45.694  41.740 15.716  1.00 66.82  ? 171 TRP B O   1 
ATOM   3393  C CB  . TRP B  1 171 ? 45.992  45.067 15.083  1.00 63.15  ? 171 TRP B CB  1 
ATOM   3394  C CG  . TRP B  1 171 ? 46.521  44.514 13.793  1.00 69.13  ? 171 TRP B CG  1 
ATOM   3395  C CD1 . TRP B  1 171 ? 45.920  43.585 12.994  1.00 72.91  ? 171 TRP B CD1 1 
ATOM   3396  C CD2 . TRP B  1 171 ? 47.751  44.870 13.134  1.00 67.58  ? 171 TRP B CD2 1 
ATOM   3397  N NE1 . TRP B  1 171 ? 46.695  43.328 11.895  1.00 70.20  ? 171 TRP B NE1 1 
ATOM   3398  C CE2 . TRP B  1 171 ? 47.823  44.101 11.952  1.00 65.43  ? 171 TRP B CE2 1 
ATOM   3399  C CE3 . TRP B  1 171 ? 48.794  45.757 13.422  1.00 66.01  ? 171 TRP B CE3 1 
ATOM   3400  C CZ2 . TRP B  1 171 ? 48.895  44.192 11.067  1.00 63.01  ? 171 TRP B CZ2 1 
ATOM   3401  C CZ3 . TRP B  1 171 ? 49.853  45.846 12.546  1.00 66.41  ? 171 TRP B CZ3 1 
ATOM   3402  C CH2 . TRP B  1 171 ? 49.901  45.075 11.385  1.00 65.30  ? 171 TRP B CH2 1 
ATOM   3403  N N   . VAL B  1 172 ? 46.955  42.985 17.163  1.00 64.41  ? 172 VAL B N   1 
ATOM   3404  C CA  . VAL B  1 172 ? 47.884  41.902 17.603  1.00 61.17  ? 172 VAL B CA  1 
ATOM   3405  C C   . VAL B  1 172 ? 47.060  40.782 18.246  1.00 56.86  ? 172 VAL B C   1 
ATOM   3406  O O   . VAL B  1 172 ? 47.219  39.614 17.829  1.00 56.22  ? 172 VAL B O   1 
ATOM   3407  C CB  . VAL B  1 172 ? 48.962  42.438 18.563  1.00 57.17  ? 172 VAL B CB  1 
ATOM   3408  C CG1 . VAL B  1 172 ? 49.774  41.310 19.178  1.00 58.47  ? 172 VAL B CG1 1 
ATOM   3409  C CG2 . VAL B  1 172 ? 49.873  43.444 17.875  1.00 55.91  ? 172 VAL B CG2 1 
ATOM   3410  N N   . ILE B  1 173 ? 46.208  41.130 19.214  1.00 52.01  ? 173 ILE B N   1 
ATOM   3411  C CA  . ILE B  1 173 ? 45.313  40.169 19.924  1.00 54.00  ? 173 ILE B CA  1 
ATOM   3412  C C   . ILE B  1 173 ? 44.661  39.252 18.881  1.00 57.34  ? 173 ILE B C   1 
ATOM   3413  O O   . ILE B  1 173 ? 44.678  38.020 19.079  1.00 55.94  ? 173 ILE B O   1 
ATOM   3414  C CB  . ILE B  1 173 ? 44.259  40.908 20.771  1.00 51.80  ? 173 ILE B CB  1 
ATOM   3415  C CG1 . ILE B  1 173 ? 44.904  41.806 21.829  1.00 48.54  ? 173 ILE B CG1 1 
ATOM   3416  C CG2 . ILE B  1 173 ? 43.287  39.916 21.392  1.00 49.19  ? 173 ILE B CG2 1 
ATOM   3417  C CD1 . ILE B  1 173 ? 43.914  42.615 22.632  1.00 50.94  ? 173 ILE B CD1 1 
ATOM   3418  N N   . ALA B  1 174 ? 44.117  39.842 17.812  1.00 60.23  ? 174 ALA B N   1 
ATOM   3419  C CA  . ALA B  1 174 ? 43.450  39.134 16.694  1.00 62.28  ? 174 ALA B CA  1 
ATOM   3420  C C   . ALA B  1 174 ? 44.447  38.185 16.019  1.00 59.99  ? 174 ALA B C   1 
ATOM   3421  O O   . ALA B  1 174 ? 44.184  36.967 16.003  1.00 59.31  ? 174 ALA B O   1 
ATOM   3422  C CB  . ALA B  1 174 ? 42.884  40.133 15.712  1.00 62.26  ? 174 ALA B CB  1 
ATOM   3423  N N   . ASN B  1 175 ? 45.544  38.731 15.484  1.00 54.30  ? 175 ASN B N   1 
ATOM   3424  C CA  . ASN B  1 175 ? 46.613  37.964 14.789  1.00 53.58  ? 175 ASN B CA  1 
ATOM   3425  C C   . ASN B  1 175 ? 46.973  36.733 15.623  1.00 57.92  ? 175 ASN B C   1 
ATOM   3426  O O   . ASN B  1 175 ? 46.994  35.622 15.058  1.00 58.50  ? 175 ASN B O   1 
ATOM   3427  C CB  . ASN B  1 175 ? 47.854  38.819 14.532  1.00 49.47  ? 175 ASN B CB  1 
ATOM   3428  C CG  . ASN B  1 175 ? 47.688  39.736 13.341  1.00 51.20  ? 175 ASN B CG  1 
ATOM   3429  O OD1 . ASN B  1 175 ? 47.496  40.937 13.505  1.00 56.90  ? 175 ASN B OD1 1 
ATOM   3430  N ND2 . ASN B  1 175 ? 47.742  39.175 12.143  1.00 50.84  ? 175 ASN B ND2 1 
ATOM   3431  N N   . VAL B  1 176 ? 47.249  36.935 16.914  1.00 58.72  ? 176 VAL B N   1 
ATOM   3432  C CA  . VAL B  1 176 ? 47.611  35.854 17.877  1.00 63.74  ? 176 VAL B CA  1 
ATOM   3433  C C   . VAL B  1 176 ? 46.526  34.772 17.828  1.00 62.58  ? 176 VAL B C   1 
ATOM   3434  O O   . VAL B  1 176 ? 46.830  33.642 17.388  1.00 57.05  ? 176 VAL B O   1 
ATOM   3435  C CB  . VAL B  1 176 ? 47.789  36.411 19.303  1.00 61.76  ? 176 VAL B CB  1 
ATOM   3436  C CG1 . VAL B  1 176 ? 47.799  35.302 20.344  1.00 60.69  ? 176 VAL B CG1 1 
ATOM   3437  C CG2 . VAL B  1 176 ? 49.038  37.271 19.419  1.00 58.25  ? 176 VAL B CG2 1 
ATOM   3438  N N   . VAL B  1 177 ? 45.308  35.119 18.254  1.00 58.53  ? 177 VAL B N   1 
ATOM   3439  C CA  . VAL B  1 177 ? 44.141  34.192 18.355  1.00 59.81  ? 177 VAL B CA  1 
ATOM   3440  C C   . VAL B  1 177 ? 44.034  33.369 17.065  1.00 60.64  ? 177 VAL B C   1 
ATOM   3441  O O   . VAL B  1 177 ? 43.910  32.134 17.167  1.00 60.48  ? 177 VAL B O   1 
ATOM   3442  C CB  . VAL B  1 177 ? 42.839  34.965 18.636  1.00 61.39  ? 177 VAL B CB  1 
ATOM   3443  C CG1 . VAL B  1 177 ? 41.626  34.052 18.584  1.00 64.34  ? 177 VAL B CG1 1 
ATOM   3444  C CG2 . VAL B  1 177 ? 42.897  35.705 19.963  1.00 64.08  ? 177 VAL B CG2 1 
ATOM   3445  N N   . LEU B  1 178 ? 44.077  34.031 15.905  1.00 63.31  ? 178 LEU B N   1 
ATOM   3446  C CA  . LEU B  1 178 ? 43.914  33.397 14.567  1.00 67.35  ? 178 LEU B CA  1 
ATOM   3447  C C   . LEU B  1 178 ? 45.106  32.477 14.281  1.00 61.07  ? 178 LEU B C   1 
ATOM   3448  O O   . LEU B  1 178 ? 44.872  31.294 13.962  1.00 55.82  ? 178 LEU B O   1 
ATOM   3449  C CB  . LEU B  1 178 ? 43.793  34.490 13.500  1.00 74.42  ? 178 LEU B CB  1 
ATOM   3450  C CG  . LEU B  1 178 ? 42.482  35.275 13.515  1.00 72.84  ? 178 LEU B CG  1 
ATOM   3451  C CD1 . LEU B  1 178 ? 42.513  36.401 12.495  1.00 70.14  ? 178 LEU B CD1 1 
ATOM   3452  C CD2 . LEU B  1 178 ? 41.296  34.360 13.257  1.00 72.33  ? 178 LEU B CD2 1 
ATOM   3453  N N   . ILE B  1 179 ? 46.329  33.005 14.390  1.00 60.02  ? 179 ILE B N   1 
ATOM   3454  C CA  . ILE B  1 179 ? 47.598  32.262 14.123  1.00 59.71  ? 179 ILE B CA  1 
ATOM   3455  C C   . ILE B  1 179 ? 47.625  31.000 14.991  1.00 60.73  ? 179 ILE B C   1 
ATOM   3456  O O   . ILE B  1 179 ? 47.903  29.913 14.445  1.00 57.54  ? 179 ILE B O   1 
ATOM   3457  C CB  . ILE B  1 179 ? 48.828  33.157 14.375  1.00 55.52  ? 179 ILE B CB  1 
ATOM   3458  C CG1 . ILE B  1 179 ? 48.962  34.244 13.306  1.00 54.15  ? 179 ILE B CG1 1 
ATOM   3459  C CG2 . ILE B  1 179 ? 50.090  32.316 14.482  1.00 54.65  ? 179 ILE B CG2 1 
ATOM   3460  C CD1 . ILE B  1 179 ? 49.947  35.333 13.656  1.00 53.40  ? 179 ILE B CD1 1 
ATOM   3461  N N   . ARG B  1 180 ? 47.348  31.143 16.291  1.00 66.79  ? 180 ARG B N   1 
ATOM   3462  C CA  . ARG B  1 180 ? 47.293  30.010 17.252  1.00 74.50  ? 180 ARG B CA  1 
ATOM   3463  C C   . ARG B  1 180 ? 46.304  28.964 16.733  1.00 71.69  ? 180 ARG B C   1 
ATOM   3464  O O   . ARG B  1 180 ? 46.715  27.802 16.572  1.00 69.35  ? 180 ARG B O   1 
ATOM   3465  C CB  . ARG B  1 180 ? 46.896  30.485 18.653  1.00 82.65  ? 180 ARG B CB  1 
ATOM   3466  C CG  . ARG B  1 180 ? 48.010  31.211 19.395  1.00 90.52  ? 180 ARG B CG  1 
ATOM   3467  C CD  . ARG B  1 180 ? 48.379  30.538 20.705  1.00 94.96  ? 180 ARG B CD  1 
ATOM   3468  N NE  . ARG B  1 180 ? 47.215  30.148 21.489  1.00 98.77  ? 180 ARG B NE  1 
ATOM   3469  C CZ  . ARG B  1 180 ? 46.609  30.924 22.382  1.00 103.61 ? 180 ARG B CZ  1 
ATOM   3470  N NH1 . ARG B  1 180 ? 45.557  30.472 23.044  1.00 99.76  ? 180 ARG B NH1 1 
ATOM   3471  N NH2 . ARG B  1 180 ? 47.054  32.147 22.610  1.00 104.40 ? 180 ARG B NH2 1 
ATOM   3472  N N   . ALA B  1 181 ? 45.059  29.375 16.473  1.00 67.69  ? 181 ALA B N   1 
ATOM   3473  C CA  . ALA B  1 181 ? 43.938  28.507 16.041  1.00 63.89  ? 181 ALA B CA  1 
ATOM   3474  C C   . ALA B  1 181 ? 44.306  27.768 14.750  1.00 56.29  ? 181 ALA B C   1 
ATOM   3475  O O   . ALA B  1 181 ? 43.884  26.604 14.602  1.00 59.93  ? 181 ALA B O   1 
ATOM   3476  C CB  . ALA B  1 181 ? 42.688  29.333 15.864  1.00 67.24  ? 181 ALA B CB  1 
ATOM   3477  N N   . VAL B  1 182 ? 45.055  28.419 13.854  1.00 54.08  ? 182 VAL B N   1 
ATOM   3478  C CA  . VAL B  1 182 ? 45.507  27.834 12.555  1.00 61.76  ? 182 VAL B CA  1 
ATOM   3479  C C   . VAL B  1 182 ? 46.612  26.810 12.836  1.00 68.73  ? 182 VAL B C   1 
ATOM   3480  O O   . VAL B  1 182 ? 46.493  25.661 12.364  1.00 71.36  ? 182 VAL B O   1 
ATOM   3481  C CB  . VAL B  1 182 ? 45.996  28.917 11.573  1.00 62.58  ? 182 VAL B CB  1 
ATOM   3482  C CG1 . VAL B  1 182 ? 46.591  28.302 10.315  1.00 59.97  ? 182 VAL B CG1 1 
ATOM   3483  C CG2 . VAL B  1 182 ? 44.892  29.900 11.214  1.00 68.41  ? 182 VAL B CG2 1 
ATOM   3484  N N   . ARG B  1 183 ? 47.643  27.224 13.579  1.00 79.10  ? 183 ARG B N   1 
ATOM   3485  C CA  . ARG B  1 183 ? 48.840  26.404 13.904  1.00 84.35  ? 183 ARG B CA  1 
ATOM   3486  C C   . ARG B  1 183 ? 48.405  25.108 14.602  1.00 83.11  ? 183 ARG B C   1 
ATOM   3487  O O   . ARG B  1 183 ? 49.108  24.094 14.433  1.00 94.97  ? 183 ARG B O   1 
ATOM   3488  C CB  . ARG B  1 183 ? 49.807  27.219 14.768  1.00 93.35  ? 183 ARG B CB  1 
ATOM   3489  C CG  . ARG B  1 183 ? 51.192  26.607 14.921  1.00 100.41 ? 183 ARG B CG  1 
ATOM   3490  C CD  . ARG B  1 183 ? 52.184  27.602 15.495  1.00 100.68 ? 183 ARG B CD  1 
ATOM   3491  N NE  . ARG B  1 183 ? 51.696  28.228 16.718  1.00 113.36 ? 183 ARG B NE  1 
ATOM   3492  C CZ  . ARG B  1 183 ? 52.229  29.307 17.281  1.00 115.71 ? 183 ARG B CZ  1 
ATOM   3493  N NH1 . ARG B  1 183 ? 53.277  29.895 16.729  1.00 118.12 ? 183 ARG B NH1 1 
ATOM   3494  N NH2 . ARG B  1 183 ? 51.710  29.798 18.393  1.00 113.53 ? 183 ARG B NH2 1 
ATOM   3495  N N   . GLN B  1 184 ? 47.296  25.146 15.352  1.00 79.03  ? 184 GLN B N   1 
ATOM   3496  C CA  . GLN B  1 184 ? 46.742  23.985 16.104  1.00 82.10  ? 184 GLN B CA  1 
ATOM   3497  C C   . GLN B  1 184 ? 46.057  23.015 15.137  1.00 86.33  ? 184 GLN B C   1 
ATOM   3498  O O   . GLN B  1 184 ? 46.138  21.789 15.369  1.00 87.31  ? 184 GLN B O   1 
ATOM   3499  C CB  . GLN B  1 184 ? 45.717  24.436 17.145  1.00 81.51  ? 184 GLN B CB  1 
ATOM   3500  C CG  . GLN B  1 184 ? 46.301  25.258 18.283  1.00 87.72  ? 184 GLN B CG  1 
ATOM   3501  C CD  . GLN B  1 184 ? 45.217  25.770 19.199  1.00 93.81  ? 184 GLN B CD  1 
ATOM   3502  O OE1 . GLN B  1 184 ? 44.090  25.280 19.189  1.00 95.49  ? 184 GLN B OE1 1 
ATOM   3503  N NE2 . GLN B  1 184 ? 45.549  26.771 19.998  1.00 101.97 ? 184 GLN B NE2 1 
ATOM   3504  N N   . SER B  1 185 ? 45.391  23.553 14.111  1.00 97.13  ? 185 SER B N   1 
ATOM   3505  C CA  . SER B  1 185 ? 44.585  22.791 13.122  1.00 104.69 ? 185 SER B CA  1 
ATOM   3506  C C   . SER B  1 185 ? 45.509  22.019 12.174  1.00 103.33 ? 185 SER B C   1 
ATOM   3507  O O   . SER B  1 185 ? 45.251  20.818 11.944  1.00 106.49 ? 185 SER B O   1 
ATOM   3508  C CB  . SER B  1 185 ? 43.667  23.706 12.355  1.00 107.56 ? 185 SER B CB  1 
ATOM   3509  O OG  . SER B  1 185 ? 42.711  24.312 13.213  1.00 105.87 ? 185 SER B OG  1 
ATOM   3510  N N   . LEU B  1 186 ? 46.546  22.691 11.664  1.00 94.73  ? 186 LEU B N   1 
ATOM   3511  C CA  . LEU B  1 186 ? 47.435  22.203 10.575  1.00 102.45 ? 186 LEU B CA  1 
ATOM   3512  C C   . LEU B  1 186 ? 47.920  20.786 10.875  1.00 116.41 ? 186 LEU B C   1 
ATOM   3513  O O   . LEU B  1 186 ? 47.958  19.945 9.978   1.00 124.89 ? 186 LEU B O   1 
ATOM   3514  C CB  . LEU B  1 186 ? 48.605  23.180 10.418  1.00 105.86 ? 186 LEU B CB  1 
ATOM   3515  C CG  . LEU B  1 186 ? 48.238  24.552 9.854   1.00 104.95 ? 186 LEU B CG  1 
ATOM   3516  C CD1 . LEU B  1 186 ? 49.458  25.455 9.765   1.00 104.86 ? 186 LEU B CD1 1 
ATOM   3517  C CD2 . LEU B  1 186 ? 47.577  24.421 8.492   1.00 110.22 ? 186 LEU B CD2 1 
ATOM   3518  N N   . PRO B  1 187 ? 48.324  20.473 12.128  1.00 116.17 ? 187 PRO B N   1 
ATOM   3519  C CA  . PRO B  1 187 ? 48.761  19.120 12.479  1.00 101.32 ? 187 PRO B CA  1 
ATOM   3520  C C   . PRO B  1 187 ? 47.705  18.035 12.210  1.00 103.31 ? 187 PRO B C   1 
ATOM   3521  O O   . PRO B  1 187 ? 48.062  16.996 11.686  1.00 102.72 ? 187 PRO B O   1 
ATOM   3522  C CB  . PRO B  1 187 ? 49.039  19.208 13.988  1.00 106.20 ? 187 PRO B CB  1 
ATOM   3523  C CG  . PRO B  1 187 ? 49.320  20.675 14.234  1.00 115.14 ? 187 PRO B CG  1 
ATOM   3524  C CD  . PRO B  1 187 ? 48.421  21.407 13.260  1.00 125.26 ? 187 PRO B CD  1 
ATOM   3525  N N   . THR B  1 188 ? 46.445  18.298 12.572  1.00 106.19 ? 188 THR B N   1 
ATOM   3526  C CA  . THR B  1 188 ? 45.329  17.311 12.555  1.00 100.62 ? 188 THR B CA  1 
ATOM   3527  C C   . THR B  1 188 ? 44.696  17.236 11.159  1.00 84.93  ? 188 THR B C   1 
ATOM   3528  O O   . THR B  1 188 ? 43.848  16.350 10.948  1.00 71.07  ? 188 THR B O   1 
ATOM   3529  C CB  . THR B  1 188 ? 44.278  17.647 13.619  1.00 109.14 ? 188 THR B CB  1 
ATOM   3530  O OG1 . THR B  1 188 ? 43.631  18.862 13.234  1.00 115.38 ? 188 THR B OG1 1 
ATOM   3531  C CG2 . THR B  1 188 ? 44.872  17.771 15.006  1.00 111.66 ? 188 THR B CG2 1 
ATOM   3532  N N   . LEU B  1 189 ? 45.083  18.129 10.242  1.00 85.73  ? 189 LEU B N   1 
ATOM   3533  C CA  . LEU B  1 189 ? 44.592  18.151 8.835   1.00 80.67  ? 189 LEU B CA  1 
ATOM   3534  C C   . LEU B  1 189 ? 45.503  17.279 7.963   1.00 64.85  ? 189 LEU B C   1 
ATOM   3535  O O   . LEU B  1 189 ? 46.581  16.890 8.445   1.00 56.82  ? 189 LEU B O   1 
ATOM   3536  C CB  . LEU B  1 189 ? 44.572  19.595 8.320   1.00 84.47  ? 189 LEU B CB  1 
ATOM   3537  C CG  . LEU B  1 189 ? 43.622  20.545 9.048   1.00 85.51  ? 189 LEU B CG  1 
ATOM   3538  C CD1 . LEU B  1 189 ? 43.638  21.923 8.403   1.00 81.92  ? 189 LEU B CD1 1 
ATOM   3539  C CD2 . LEU B  1 189 ? 42.206  19.988 9.080   1.00 90.75  ? 189 LEU B CD2 1 
ATOM   3540  N N   . THR B  1 190 ? 45.081  16.993 6.727   1.00 59.90  ? 190 THR B N   1 
ATOM   3541  C CA  . THR B  1 190 ? 45.885  16.273 5.703   1.00 60.57  ? 190 THR B CA  1 
ATOM   3542  C C   . THR B  1 190 ? 46.933  17.225 5.134   1.00 61.08  ? 190 THR B C   1 
ATOM   3543  O O   . THR B  1 190 ? 46.918  18.417 5.432   1.00 55.22  ? 190 THR B O   1 
ATOM   3544  C CB  . THR B  1 190 ? 45.000  15.703 4.588   1.00 60.23  ? 190 THR B CB  1 
ATOM   3545  O OG1 . THR B  1 190 ? 44.618  16.778 3.728   1.00 56.06  ? 190 THR B OG1 1 
ATOM   3546  C CG2 . THR B  1 190 ? 43.772  14.994 5.113   1.00 57.61  ? 190 THR B CG2 1 
ATOM   3547  N N   . PRO B  1 191 ? 47.885  16.727 4.313   1.00 73.14  ? 191 PRO B N   1 
ATOM   3548  C CA  . PRO B  1 191 ? 48.880  17.584 3.668   1.00 76.05  ? 191 PRO B CA  1 
ATOM   3549  C C   . PRO B  1 191 ? 48.251  18.642 2.749   1.00 77.67  ? 191 PRO B C   1 
ATOM   3550  O O   . PRO B  1 191 ? 48.666  19.783 2.806   1.00 75.67  ? 191 PRO B O   1 
ATOM   3551  C CB  . PRO B  1 191 ? 49.729  16.608 2.838   1.00 78.34  ? 191 PRO B CB  1 
ATOM   3552  C CG  . PRO B  1 191 ? 49.507  15.262 3.498   1.00 82.37  ? 191 PRO B CG  1 
ATOM   3553  C CD  . PRO B  1 191 ? 48.076  15.305 3.991   1.00 79.29  ? 191 PRO B CD  1 
ATOM   3554  N N   . GLU B  1 192 ? 47.277  18.234 1.931   1.00 81.78  ? 192 GLU B N   1 
ATOM   3555  C CA  . GLU B  1 192 ? 46.608  19.090 0.913   1.00 76.60  ? 192 GLU B CA  1 
ATOM   3556  C C   . GLU B  1 192 ? 45.805  20.196 1.609   1.00 71.32  ? 192 GLU B C   1 
ATOM   3557  O O   . GLU B  1 192 ? 45.908  21.357 1.169   1.00 70.88  ? 192 GLU B O   1 
ATOM   3558  C CB  . GLU B  1 192 ? 45.723  18.224 0.017   1.00 80.87  ? 192 GLU B CB  1 
ATOM   3559  C CG  . GLU B  1 192 ? 44.864  17.252 0.802   1.00 88.98  ? 192 GLU B CG  1 
ATOM   3560  C CD  . GLU B  1 192 ? 44.936  15.812 0.328   1.00 87.67  ? 192 GLU B CD  1 
ATOM   3561  O OE1 . GLU B  1 192 ? 45.186  15.599 -0.875  1.00 100.27 ? 192 GLU B OE1 1 
ATOM   3562  O OE2 . GLU B  1 192 ? 44.752  14.907 1.167   1.00 79.98  ? 192 GLU B OE2 1 
ATOM   3563  N N   . SER B  1 193 ? 45.036  19.851 2.649   1.00 69.58  ? 193 SER B N   1 
ATOM   3564  C CA  . SER B  1 193 ? 44.245  20.804 3.475   1.00 72.11  ? 193 SER B CA  1 
ATOM   3565  C C   . SER B  1 193 ? 45.197  21.750 4.214   1.00 76.57  ? 193 SER B C   1 
ATOM   3566  O O   . SER B  1 193 ? 45.023  22.980 4.101   1.00 82.34  ? 193 SER B O   1 
ATOM   3567  C CB  . SER B  1 193 ? 43.342  20.081 4.442   1.00 72.05  ? 193 SER B CB  1 
ATOM   3568  O OG  . SER B  1 193 ? 42.363  19.320 3.752   1.00 71.47  ? 193 SER B OG  1 
ATOM   3569  N N   . HIS B  1 194 ? 46.160  21.179 4.945   1.00 81.06  ? 194 HIS B N   1 
ATOM   3570  C CA  . HIS B  1 194 ? 47.243  21.895 5.671   1.00 82.63  ? 194 HIS B CA  1 
ATOM   3571  C C   . HIS B  1 194 ? 47.729  23.083 4.833   1.00 74.85  ? 194 HIS B C   1 
ATOM   3572  O O   . HIS B  1 194 ? 47.696  24.213 5.352   1.00 72.37  ? 194 HIS B O   1 
ATOM   3573  C CB  . HIS B  1 194 ? 48.372  20.910 6.011   1.00 97.29  ? 194 HIS B CB  1 
ATOM   3574  C CG  . HIS B  1 194 ? 49.641  21.542 6.476   1.00 105.66 ? 194 HIS B CG  1 
ATOM   3575  N ND1 . HIS B  1 194 ? 50.019  21.550 7.804   1.00 93.24  ? 194 HIS B ND1 1 
ATOM   3576  C CD2 . HIS B  1 194 ? 50.634  22.159 5.799   1.00 106.38 ? 194 HIS B CD2 1 
ATOM   3577  C CE1 . HIS B  1 194 ? 51.180  22.159 7.928   1.00 100.85 ? 194 HIS B CE1 1 
ATOM   3578  N NE2 . HIS B  1 194 ? 51.580  22.543 6.711   1.00 107.18 ? 194 HIS B NE2 1 
ATOM   3579  N N   . THR B  1 195 ? 48.149  22.828 3.589   1.00 68.93  ? 195 THR B N   1 
ATOM   3580  C CA  . THR B  1 195 ? 48.733  23.829 2.654   1.00 70.84  ? 195 THR B CA  1 
ATOM   3581  C C   . THR B  1 195 ? 47.751  24.986 2.435   1.00 74.73  ? 195 THR B C   1 
ATOM   3582  O O   . THR B  1 195 ? 48.172  26.152 2.581   1.00 74.54  ? 195 THR B O   1 
ATOM   3583  C CB  . THR B  1 195 ? 49.110  23.185 1.314   1.00 68.07  ? 195 THR B CB  1 
ATOM   3584  O OG1 . THR B  1 195 ? 49.954  22.067 1.590   1.00 73.44  ? 195 THR B OG1 1 
ATOM   3585  C CG2 . THR B  1 195 ? 49.814  24.142 0.377   1.00 68.19  ? 195 THR B CG2 1 
ATOM   3586  N N   . MET B  1 196 ? 46.500  24.669 2.092   1.00 75.82  ? 196 MET B N   1 
ATOM   3587  C CA  . MET B  1 196 ? 45.451  25.660 1.734   1.00 78.85  ? 196 MET B CA  1 
ATOM   3588  C C   . MET B  1 196 ? 45.179  26.583 2.928   1.00 73.00  ? 196 MET B C   1 
ATOM   3589  O O   . MET B  1 196 ? 45.236  27.814 2.742   1.00 80.22  ? 196 MET B O   1 
ATOM   3590  C CB  . MET B  1 196 ? 44.155  24.959 1.316   1.00 87.17  ? 196 MET B CB  1 
ATOM   3591  C CG  . MET B  1 196 ? 44.216  24.374 -0.083  1.00 94.26  ? 196 MET B CG  1 
ATOM   3592  S SD  . MET B  1 196 ? 44.610  25.621 -1.338  1.00 95.36  ? 196 MET B SD  1 
ATOM   3593  C CE  . MET B  1 196 ? 43.251  26.763 -1.097  1.00 105.11 ? 196 MET B CE  1 
ATOM   3594  N N   . LEU B  1 197 ? 44.902  26.010 4.103   1.00 62.41  ? 197 LEU B N   1 
ATOM   3595  C CA  . LEU B  1 197 ? 44.580  26.770 5.340   1.00 59.53  ? 197 LEU B CA  1 
ATOM   3596  C C   . LEU B  1 197 ? 45.720  27.749 5.640   1.00 55.84  ? 197 LEU B C   1 
ATOM   3597  O O   . LEU B  1 197 ? 45.426  28.921 5.940   1.00 59.96  ? 197 LEU B O   1 
ATOM   3598  C CB  . LEU B  1 197 ? 44.365  25.796 6.502   1.00 61.34  ? 197 LEU B CB  1 
ATOM   3599  C CG  . LEU B  1 197 ? 43.822  26.425 7.786   1.00 61.47  ? 197 LEU B CG  1 
ATOM   3600  C CD1 . LEU B  1 197 ? 42.485  27.103 7.534   1.00 59.83  ? 197 LEU B CD1 1 
ATOM   3601  C CD2 . LEU B  1 197 ? 43.692  25.388 8.889   1.00 62.23  ? 197 LEU B CD2 1 
ATOM   3602  N N   . LYS B  1 198 ? 46.969  27.282 5.559   1.00 56.73  ? 198 LYS B N   1 
ATOM   3603  C CA  . LYS B  1 198 ? 48.185  28.120 5.740   1.00 57.54  ? 198 LYS B CA  1 
ATOM   3604  C C   . LYS B  1 198 ? 48.135  29.272 4.731   1.00 56.67  ? 198 LYS B C   1 
ATOM   3605  O O   . LYS B  1 198 ? 48.281  30.433 5.156   1.00 59.90  ? 198 LYS B O   1 
ATOM   3606  C CB  . LYS B  1 198 ? 49.457  27.285 5.564   1.00 55.49  ? 198 LYS B CB  1 
ATOM   3607  N N   . SER B  1 199 ? 47.918  28.955 3.451   1.00 54.53  ? 199 SER B N   1 
ATOM   3608  C CA  . SER B  1 199 ? 47.815  29.935 2.338   1.00 60.68  ? 199 SER B CA  1 
ATOM   3609  C C   . SER B  1 199 ? 46.759  30.996 2.671   1.00 64.42  ? 199 SER B C   1 
ATOM   3610  O O   . SER B  1 199 ? 47.112  32.190 2.702   1.00 69.47  ? 199 SER B O   1 
ATOM   3611  C CB  . SER B  1 199 ? 47.507  29.252 1.036   1.00 59.16  ? 199 SER B CB  1 
ATOM   3612  O OG  . SER B  1 199 ? 47.205  30.207 0.032   1.00 71.81  ? 199 SER B OG  1 
ATOM   3613  N N   . ALA B  1 200 ? 45.514  30.569 2.904   1.00 60.97  ? 200 ALA B N   1 
ATOM   3614  C CA  . ALA B  1 200 ? 44.362  31.436 3.248   1.00 63.42  ? 200 ALA B CA  1 
ATOM   3615  C C   . ALA B  1 200 ? 44.746  32.379 4.394   1.00 61.51  ? 200 ALA B C   1 
ATOM   3616  O O   . ALA B  1 200 ? 44.527  33.596 4.257   1.00 62.68  ? 200 ALA B O   1 
ATOM   3617  C CB  . ALA B  1 200 ? 43.169  30.587 3.614   1.00 65.55  ? 200 ALA B CB  1 
ATOM   3618  N N   . ALA B  1 201 ? 45.294  31.826 5.481   1.00 58.93  ? 201 ALA B N   1 
ATOM   3619  C CA  . ALA B  1 201 ? 45.685  32.553 6.712   1.00 59.41  ? 201 ALA B CA  1 
ATOM   3620  C C   . ALA B  1 201 ? 46.682  33.665 6.364   1.00 59.01  ? 201 ALA B C   1 
ATOM   3621  O O   . ALA B  1 201 ? 46.526  34.786 6.887   1.00 59.71  ? 201 ALA B O   1 
ATOM   3622  C CB  . ALA B  1 201 ? 46.265  31.588 7.717   1.00 56.46  ? 201 ALA B CB  1 
ATOM   3623  N N   . ILE B  1 202 ? 47.666  33.358 5.514   1.00 55.15  ? 202 ILE B N   1 
ATOM   3624  C CA  . ILE B  1 202 ? 48.715  34.318 5.058   1.00 58.84  ? 202 ILE B CA  1 
ATOM   3625  C C   . ILE B  1 202 ? 48.036  35.470 4.311   1.00 60.31  ? 202 ILE B C   1 
ATOM   3626  O O   . ILE B  1 202 ? 48.229  36.630 4.720   1.00 66.40  ? 202 ILE B O   1 
ATOM   3627  C CB  . ILE B  1 202 ? 49.771  33.612 4.186   1.00 59.50  ? 202 ILE B CB  1 
ATOM   3628  C CG1 . ILE B  1 202 ? 50.581  32.596 4.995   1.00 61.51  ? 202 ILE B CG1 1 
ATOM   3629  C CG2 . ILE B  1 202 ? 50.670  34.629 3.499   1.00 57.74  ? 202 ILE B CG2 1 
ATOM   3630  C CD1 . ILE B  1 202 ? 51.482  31.719 4.155   1.00 67.27  ? 202 ILE B CD1 1 
ATOM   3631  N N   . VAL B  1 203 ? 47.264  35.151 3.265   1.00 54.34  ? 203 VAL B N   1 
ATOM   3632  C CA  . VAL B  1 203 ? 46.566  36.141 2.390   1.00 48.24  ? 203 VAL B CA  1 
ATOM   3633  C C   . VAL B  1 203 ? 45.854  37.169 3.275   1.00 49.85  ? 203 VAL B C   1 
ATOM   3634  O O   . VAL B  1 203 ? 45.997  38.378 3.004   1.00 49.50  ? 203 VAL B O   1 
ATOM   3635  C CB  . VAL B  1 203 ? 45.573  35.459 1.429   1.00 43.42  ? 203 VAL B CB  1 
ATOM   3636  C CG1 . VAL B  1 203 ? 44.823  36.477 0.584   1.00 42.77  ? 203 VAL B CG1 1 
ATOM   3637  C CG2 . VAL B  1 203 ? 46.256  34.431 0.541   1.00 43.44  ? 203 VAL B CG2 1 
ATOM   3638  N N   . LEU B  1 204 ? 45.117  36.704 4.288   1.00 47.47  ? 204 LEU B N   1 
ATOM   3639  C CA  . LEU B  1 204 ? 44.328  37.567 5.207   1.00 51.95  ? 204 LEU B CA  1 
ATOM   3640  C C   . LEU B  1 204 ? 45.282  38.363 6.104   1.00 53.36  ? 204 LEU B C   1 
ATOM   3641  O O   . LEU B  1 204 ? 45.290  39.604 6.009   1.00 60.59  ? 204 LEU B O   1 
ATOM   3642  C CB  . LEU B  1 204 ? 43.389  36.695 6.048   1.00 53.42  ? 204 LEU B CB  1 
ATOM   3643  C CG  . LEU B  1 204 ? 42.517  37.459 7.045   1.00 56.08  ? 204 LEU B CG  1 
ATOM   3644  C CD1 . LEU B  1 204 ? 41.522  38.353 6.320   1.00 58.30  ? 204 LEU B CD1 1 
ATOM   3645  C CD2 . LEU B  1 204 ? 41.794  36.505 7.982   1.00 56.50  ? 204 LEU B CD2 1 
ATOM   3646  N N   . LEU B  1 205 ? 46.060  37.659 6.929   1.00 55.50  ? 205 LEU B N   1 
ATOM   3647  C CA  . LEU B  1 205 ? 46.902  38.240 8.007   1.00 53.02  ? 205 LEU B CA  1 
ATOM   3648  C C   . LEU B  1 205 ? 48.012  39.103 7.396   1.00 49.39  ? 205 LEU B C   1 
ATOM   3649  O O   . LEU B  1 205 ? 48.303  40.170 7.969   1.00 51.31  ? 205 LEU B O   1 
ATOM   3650  C CB  . LEU B  1 205 ? 47.465  37.092 8.848   1.00 54.80  ? 205 LEU B CB  1 
ATOM   3651  C CG  . LEU B  1 205 ? 46.405  36.223 9.525   1.00 54.92  ? 205 LEU B CG  1 
ATOM   3652  C CD1 . LEU B  1 205 ? 47.032  35.022 10.212  1.00 59.19  ? 205 LEU B CD1 1 
ATOM   3653  C CD2 . LEU B  1 205 ? 45.594  37.043 10.516  1.00 58.42  ? 205 LEU B CD2 1 
ATOM   3654  N N   . ALA B  1 206 ? 48.593  38.664 6.276   1.00 48.44  ? 206 ALA B N   1 
ATOM   3655  C CA  . ALA B  1 206 ? 49.633  39.398 5.517   1.00 48.84  ? 206 ALA B CA  1 
ATOM   3656  C C   . ALA B  1 206 ? 49.051  40.717 4.995   1.00 53.13  ? 206 ALA B C   1 
ATOM   3657  O O   . ALA B  1 206 ? 49.591  41.780 5.355   1.00 60.06  ? 206 ALA B O   1 
ATOM   3658  C CB  . ALA B  1 206 ? 50.156  38.545 4.388   1.00 49.22  ? 206 ALA B CB  1 
ATOM   3659  N N   . GLY B  1 207 ? 47.990  40.641 4.182   1.00 50.34  ? 207 GLY B N   1 
ATOM   3660  C CA  . GLY B  1 207 ? 47.320  41.802 3.563   1.00 51.50  ? 207 GLY B CA  1 
ATOM   3661  C C   . GLY B  1 207 ? 46.968  42.869 4.586   1.00 56.57  ? 207 GLY B C   1 
ATOM   3662  O O   . GLY B  1 207 ? 47.131  44.064 4.271   1.00 63.63  ? 207 GLY B O   1 
ATOM   3663  N N   . TRP B  1 208 ? 46.510  42.449 5.770   1.00 61.01  ? 208 TRP B N   1 
ATOM   3664  C CA  . TRP B  1 208 ? 46.080  43.323 6.896   1.00 64.41  ? 208 TRP B CA  1 
ATOM   3665  C C   . TRP B  1 208 ? 47.078  44.468 7.112   1.00 60.70  ? 208 TRP B C   1 
ATOM   3666  O O   . TRP B  1 208 ? 46.637  45.561 7.508   1.00 58.35  ? 208 TRP B O   1 
ATOM   3667  C CB  . TRP B  1 208 ? 45.903  42.488 8.170   1.00 66.94  ? 208 TRP B CB  1 
ATOM   3668  C CG  . TRP B  1 208 ? 44.544  41.875 8.295   1.00 70.66  ? 208 TRP B CG  1 
ATOM   3669  C CD1 . TRP B  1 208 ? 43.621  41.722 7.301   1.00 75.94  ? 208 TRP B CD1 1 
ATOM   3670  C CD2 . TRP B  1 208 ? 43.953  41.316 9.481   1.00 71.69  ? 208 TRP B CD2 1 
ATOM   3671  N NE1 . TRP B  1 208 ? 42.493  41.119 7.788   1.00 85.03  ? 208 TRP B NE1 1 
ATOM   3672  C CE2 . TRP B  1 208 ? 42.668  40.857 9.122   1.00 78.61  ? 208 TRP B CE2 1 
ATOM   3673  C CE3 . TRP B  1 208 ? 44.379  41.160 10.803  1.00 74.02  ? 208 TRP B CE3 1 
ATOM   3674  C CZ2 . TRP B  1 208 ? 41.808  40.259 10.041  1.00 77.63  ? 208 TRP B CZ2 1 
ATOM   3675  C CZ3 . TRP B  1 208 ? 43.530  40.568 11.711  1.00 77.52  ? 208 TRP B CZ3 1 
ATOM   3676  C CH2 . TRP B  1 208 ? 42.263  40.124 11.332  1.00 77.28  ? 208 TRP B CH2 1 
ATOM   3677  N N   . VAL B  1 209 ? 48.366  44.217 6.862   1.00 58.66  ? 209 VAL B N   1 
ATOM   3678  C CA  . VAL B  1 209 ? 49.491  45.160 7.139   1.00 56.71  ? 209 VAL B CA  1 
ATOM   3679  C C   . VAL B  1 209 ? 49.291  46.448 6.331   1.00 52.60  ? 209 VAL B C   1 
ATOM   3680  O O   . VAL B  1 209 ? 49.579  47.534 6.874   1.00 54.61  ? 209 VAL B O   1 
ATOM   3681  C CB  . VAL B  1 209 ? 50.848  44.502 6.825   1.00 57.20  ? 209 VAL B CB  1 
ATOM   3682  C CG1 . VAL B  1 209 ? 51.992  45.503 6.880   1.00 55.23  ? 209 VAL B CG1 1 
ATOM   3683  C CG2 . VAL B  1 209 ? 51.121  43.320 7.743   1.00 57.02  ? 209 VAL B CG2 1 
ATOM   3684  N N   . VAL B  1 210 ? 48.814  46.322 5.089   1.00 51.19  ? 210 VAL B N   1 
ATOM   3685  C CA  . VAL B  1 210 ? 48.642  47.447 4.120   1.00 48.78  ? 210 VAL B CA  1 
ATOM   3686  C C   . VAL B  1 210 ? 47.876  48.588 4.796   1.00 49.40  ? 210 VAL B C   1 
ATOM   3687  O O   . VAL B  1 210 ? 48.230  49.760 4.558   1.00 46.77  ? 210 VAL B O   1 
ATOM   3688  C CB  . VAL B  1 210 ? 47.912  46.982 2.845   1.00 47.58  ? 210 VAL B CB  1 
ATOM   3689  C CG1 . VAL B  1 210 ? 47.558  48.150 1.938   1.00 45.00  ? 210 VAL B CG1 1 
ATOM   3690  C CG2 . VAL B  1 210 ? 48.714  45.936 2.087   1.00 55.00  ? 210 VAL B CG2 1 
ATOM   3691  N N   . TYR B  1 211 ? 46.866  48.248 5.600   1.00 50.20  ? 211 TYR B N   1 
ATOM   3692  C CA  . TYR B  1 211 ? 45.842  49.191 6.120   1.00 51.86  ? 211 TYR B CA  1 
ATOM   3693  C C   . TYR B  1 211 ? 46.479  50.145 7.129   1.00 50.44  ? 211 TYR B C   1 
ATOM   3694  O O   . TYR B  1 211 ? 46.381  51.359 6.966   1.00 53.88  ? 211 TYR B O   1 
ATOM   3695  C CB  . TYR B  1 211 ? 44.638  48.405 6.645   1.00 54.61  ? 211 TYR B CB  1 
ATOM   3696  C CG  . TYR B  1 211 ? 43.870  47.692 5.559   1.00 56.40  ? 211 TYR B CG  1 
ATOM   3697  C CD1 . TYR B  1 211 ? 42.776  48.283 4.945   1.00 57.86  ? 211 TYR B CD1 1 
ATOM   3698  C CD2 . TYR B  1 211 ? 44.257  46.439 5.115   1.00 55.04  ? 211 TYR B CD2 1 
ATOM   3699  C CE1 . TYR B  1 211 ? 42.076  47.641 3.935   1.00 58.13  ? 211 TYR B CE1 1 
ATOM   3700  C CE2 . TYR B  1 211 ? 43.568  45.782 4.108   1.00 57.33  ? 211 TYR B CE2 1 
ATOM   3701  C CZ  . TYR B  1 211 ? 42.474  46.385 3.513   1.00 58.75  ? 211 TYR B CZ  1 
ATOM   3702  O OH  . TYR B  1 211 ? 41.793  45.740 2.518   1.00 55.83  ? 211 TYR B OH  1 
ATOM   3703  N N   . PRO B  1 212 ? 47.158  49.653 8.191   1.00 52.93  ? 212 PRO B N   1 
ATOM   3704  C CA  . PRO B  1 212 ? 47.824  50.537 9.148   1.00 52.94  ? 212 PRO B CA  1 
ATOM   3705  C C   . PRO B  1 212 ? 48.818  51.487 8.463   1.00 54.19  ? 212 PRO B C   1 
ATOM   3706  O O   . PRO B  1 212 ? 48.924  52.627 8.880   1.00 53.68  ? 212 PRO B O   1 
ATOM   3707  C CB  . PRO B  1 212 ? 48.565  49.580 10.095  1.00 50.24  ? 212 PRO B CB  1 
ATOM   3708  C CG  . PRO B  1 212 ? 47.817  48.269 9.967   1.00 55.55  ? 212 PRO B CG  1 
ATOM   3709  C CD  . PRO B  1 212 ? 47.315  48.233 8.537   1.00 58.78  ? 212 PRO B CD  1 
ATOM   3710  N N   . ILE B  1 213 ? 49.516  50.994 7.436   1.00 46.93  ? 213 ILE B N   1 
ATOM   3711  C CA  . ILE B  1 213 ? 50.528  51.764 6.652   1.00 45.45  ? 213 ILE B CA  1 
ATOM   3712  C C   . ILE B  1 213 ? 49.829  52.941 5.964   1.00 49.98  ? 213 ILE B C   1 
ATOM   3713  O O   . ILE B  1 213 ? 50.332  54.073 6.079   1.00 50.96  ? 213 ILE B O   1 
ATOM   3714  C CB  . ILE B  1 213 ? 51.244  50.847 5.642   1.00 44.40  ? 213 ILE B CB  1 
ATOM   3715  C CG1 . ILE B  1 213 ? 52.086  49.783 6.352   1.00 44.07  ? 213 ILE B CG1 1 
ATOM   3716  C CG2 . ILE B  1 213 ? 52.073  51.665 4.663   1.00 40.52  ? 213 ILE B CG2 1 
ATOM   3717  C CD1 . ILE B  1 213 ? 52.585  48.685 5.443   1.00 44.41  ? 213 ILE B CD1 1 
ATOM   3718  N N   . VAL B  1 214 ? 48.711  52.674 5.284   1.00 52.40  ? 214 VAL B N   1 
ATOM   3719  C CA  . VAL B  1 214 ? 47.924  53.680 4.509   1.00 52.92  ? 214 VAL B CA  1 
ATOM   3720  C C   . VAL B  1 214 ? 47.300  54.689 5.484   1.00 49.32  ? 214 VAL B C   1 
ATOM   3721  O O   . VAL B  1 214 ? 47.130  55.859 5.094   1.00 49.89  ? 214 VAL B O   1 
ATOM   3722  C CB  . VAL B  1 214 ? 46.853  52.997 3.635   1.00 53.54  ? 214 VAL B CB  1 
ATOM   3723  C CG1 . VAL B  1 214 ? 46.007  54.008 2.873   1.00 55.42  ? 214 VAL B CG1 1 
ATOM   3724  C CG2 . VAL B  1 214 ? 47.475  51.991 2.678   1.00 51.34  ? 214 VAL B CG2 1 
ATOM   3725  N N   . TYR B  1 215 ? 46.978  54.251 6.704   1.00 43.62  ? 215 TYR B N   1 
ATOM   3726  C CA  . TYR B  1 215 ? 46.324  55.075 7.755   1.00 43.44  ? 215 TYR B CA  1 
ATOM   3727  C C   . TYR B  1 215 ? 47.194  56.291 8.084   1.00 43.18  ? 215 TYR B C   1 
ATOM   3728  O O   . TYR B  1 215 ? 46.627  57.352 8.410   1.00 41.07  ? 215 TYR B O   1 
ATOM   3729  C CB  . TYR B  1 215 ? 46.081  54.253 9.023   1.00 44.96  ? 215 TYR B CB  1 
ATOM   3730  C CG  . TYR B  1 215 ? 45.526  55.038 10.186  1.00 44.72  ? 215 TYR B CG  1 
ATOM   3731  C CD1 . TYR B  1 215 ? 46.336  55.862 10.950  1.00 47.73  ? 215 TYR B CD1 1 
ATOM   3732  C CD2 . TYR B  1 215 ? 44.187  54.953 10.530  1.00 50.11  ? 215 TYR B CD2 1 
ATOM   3733  C CE1 . TYR B  1 215 ? 45.832  56.582 12.020  1.00 52.56  ? 215 TYR B CE1 1 
ATOM   3734  C CE2 . TYR B  1 215 ? 43.666  55.664 11.599  1.00 53.99  ? 215 TYR B CE2 1 
ATOM   3735  C CZ  . TYR B  1 215 ? 44.492  56.483 12.346  1.00 52.82  ? 215 TYR B CZ  1 
ATOM   3736  O OH  . TYR B  1 215 ? 43.980  57.182 13.401  1.00 54.68  ? 215 TYR B OH  1 
ATOM   3737  N N   . PHE B  1 216 ? 48.520  56.129 7.997   1.00 46.30  ? 216 PHE B N   1 
ATOM   3738  C CA  . PHE B  1 216 ? 49.536  57.078 8.528   1.00 44.77  ? 216 PHE B CA  1 
ATOM   3739  C C   . PHE B  1 216 ? 50.048  58.014 7.429   1.00 44.21  ? 216 PHE B C   1 
ATOM   3740  O O   . PHE B  1 216 ? 50.721  59.002 7.770   1.00 48.76  ? 216 PHE B O   1 
ATOM   3741  C CB  . PHE B  1 216 ? 50.707  56.317 9.152   1.00 43.75  ? 216 PHE B CB  1 
ATOM   3742  C CG  . PHE B  1 216 ? 50.441  55.791 10.538  1.00 44.28  ? 216 PHE B CG  1 
ATOM   3743  C CD1 . PHE B  1 216 ? 50.172  56.659 11.584  1.00 43.67  ? 216 PHE B CD1 1 
ATOM   3744  C CD2 . PHE B  1 216 ? 50.473  54.431 10.799  1.00 44.83  ? 216 PHE B CD2 1 
ATOM   3745  C CE1 . PHE B  1 216 ? 49.925  56.176 12.859  1.00 43.83  ? 216 PHE B CE1 1 
ATOM   3746  C CE2 . PHE B  1 216 ? 50.233  53.950 12.077  1.00 45.70  ? 216 PHE B CE2 1 
ATOM   3747  C CZ  . PHE B  1 216 ? 49.957  54.822 13.104  1.00 44.41  ? 216 PHE B CZ  1 
ATOM   3748  N N   . LEU B  1 217 ? 49.744  57.716 6.162   1.00 46.47  ? 217 LEU B N   1 
ATOM   3749  C CA  . LEU B  1 217 ? 50.213  58.506 4.992   1.00 52.99  ? 217 LEU B CA  1 
ATOM   3750  C C   . LEU B  1 217 ? 49.789  59.965 5.148   1.00 55.76  ? 217 LEU B C   1 
ATOM   3751  O O   . LEU B  1 217 ? 50.536  60.862 4.772   1.00 50.44  ? 217 LEU B O   1 
ATOM   3752  C CB  . LEU B  1 217 ? 49.652  57.894 3.704   1.00 58.13  ? 217 LEU B CB  1 
ATOM   3753  C CG  . LEU B  1 217 ? 50.181  56.504 3.357   1.00 65.39  ? 217 LEU B CG  1 
ATOM   3754  C CD1 . LEU B  1 217 ? 49.743  56.086 1.962   1.00 65.51  ? 217 LEU B CD1 1 
ATOM   3755  C CD2 . LEU B  1 217 ? 51.697  56.453 3.474   1.00 67.84  ? 217 LEU B CD2 1 
ATOM   3756  N N   . PRO B  1 218 ? 48.584  60.253 5.691   1.00 62.94  ? 218 PRO B N   1 
ATOM   3757  C CA  . PRO B  1 218 ? 48.141  61.632 5.909   1.00 64.69  ? 218 PRO B CA  1 
ATOM   3758  C C   . PRO B  1 218 ? 49.110  62.488 6.743   1.00 64.64  ? 218 PRO B C   1 
ATOM   3759  O O   . PRO B  1 218 ? 48.943  63.696 6.761   1.00 62.00  ? 218 PRO B O   1 
ATOM   3760  C CB  . PRO B  1 218 ? 46.813  61.462 6.664   1.00 63.04  ? 218 PRO B CB  1 
ATOM   3761  C CG  . PRO B  1 218 ? 46.306  60.113 6.209   1.00 66.11  ? 218 PRO B CG  1 
ATOM   3762  C CD  . PRO B  1 218 ? 47.559  59.272 6.076   1.00 69.67  ? 218 PRO B CD  1 
ATOM   3763  N N   . LEU B  1 219 ? 50.086  61.858 7.406   1.00 60.28  ? 219 LEU B N   1 
ATOM   3764  C CA  . LEU B  1 219 ? 51.085  62.544 8.273   1.00 60.30  ? 219 LEU B CA  1 
ATOM   3765  C C   . LEU B  1 219 ? 52.199  63.139 7.404   1.00 62.95  ? 219 LEU B C   1 
ATOM   3766  O O   . LEU B  1 219 ? 52.763  64.177 7.799   1.00 70.50  ? 219 LEU B O   1 
ATOM   3767  C CB  . LEU B  1 219 ? 51.647  61.548 9.293   1.00 61.02  ? 219 LEU B CB  1 
ATOM   3768  C CG  . LEU B  1 219 ? 50.696  61.170 10.429  1.00 67.14  ? 219 LEU B CG  1 
ATOM   3769  C CD1 . LEU B  1 219 ? 51.327  60.139 11.353  1.00 65.68  ? 219 LEU B CD1 1 
ATOM   3770  C CD2 . LEU B  1 219 ? 50.270  62.401 11.215  1.00 68.81  ? 219 LEU B CD2 1 
ATOM   3771  N N   . PHE B  1 220 ? 52.495  62.510 6.263   1.00 65.61  ? 220 PHE B N   1 
ATOM   3772  C CA  . PHE B  1 220 ? 53.568  62.918 5.318   1.00 66.95  ? 220 PHE B CA  1 
ATOM   3773  C C   . PHE B  1 220 ? 53.024  63.977 4.350   1.00 64.73  ? 220 PHE B C   1 
ATOM   3774  O O   . PHE B  1 220 ? 53.631  64.175 3.280   1.00 76.49  ? 220 PHE B O   1 
ATOM   3775  C CB  . PHE B  1 220 ? 54.125  61.694 4.581   1.00 71.33  ? 220 PHE B CB  1 
ATOM   3776  C CG  . PHE B  1 220 ? 54.669  60.617 5.487   1.00 78.18  ? 220 PHE B CG  1 
ATOM   3777  C CD1 . PHE B  1 220 ? 55.818  60.831 6.232   1.00 80.83  ? 220 PHE B CD1 1 
ATOM   3778  C CD2 . PHE B  1 220 ? 54.030  59.392 5.600   1.00 89.07  ? 220 PHE B CD2 1 
ATOM   3779  C CE1 . PHE B  1 220 ? 56.315  59.844 7.070   1.00 84.73  ? 220 PHE B CE1 1 
ATOM   3780  C CE2 . PHE B  1 220 ? 54.528  58.406 6.439   1.00 93.31  ? 220 PHE B CE2 1 
ATOM   3781  C CZ  . PHE B  1 220 ? 55.670  58.634 7.171   1.00 89.92  ? 220 PHE B CZ  1 
ATOM   3782  N N   . GLY B  1 221 ? 51.913  64.628 4.716   1.00 65.46  ? 221 GLY B N   1 
ATOM   3783  C CA  . GLY B  1 221 ? 51.323  65.757 3.967   1.00 67.01  ? 221 GLY B CA  1 
ATOM   3784  C C   . GLY B  1 221 ? 49.967  65.419 3.364   1.00 70.80  ? 221 GLY B C   1 
ATOM   3785  O O   . GLY B  1 221 ? 49.387  64.386 3.747   1.00 75.96  ? 221 GLY B O   1 
ATOM   3786  N N   . ALA B  1 222 ? 49.481  66.272 2.455   1.00 72.15  ? 222 ALA B N   1 
ATOM   3787  C CA  . ALA B  1 222 ? 48.199  66.132 1.723   1.00 70.07  ? 222 ALA B CA  1 
ATOM   3788  C C   . ALA B  1 222 ? 48.392  66.587 0.271   1.00 69.10  ? 222 ALA B C   1 
ATOM   3789  O O   . ALA B  1 222 ? 49.192  67.512 0.039   1.00 77.17  ? 222 ALA B O   1 
ATOM   3790  C CB  . ALA B  1 222 ? 47.117  66.933 2.406   1.00 66.37  ? 222 ALA B CB  1 
ATOM   3791  N N   . SER B  1 223 ? 47.675  65.964 -0.668  1.00 70.78  ? 223 SER B N   1 
ATOM   3792  C CA  . SER B  1 223 ? 47.822  66.182 -2.130  1.00 68.70  ? 223 SER B CA  1 
ATOM   3793  C C   . SER B  1 223 ? 46.794  65.336 -2.884  1.00 72.38  ? 223 SER B C   1 
ATOM   3794  O O   . SER B  1 223 ? 46.499  64.218 -2.416  1.00 83.08  ? 223 SER B O   1 
ATOM   3795  C CB  . SER B  1 223 ? 49.224  65.853 -2.578  1.00 71.18  ? 223 SER B CB  1 
ATOM   3796  O OG  . SER B  1 223 ? 49.288  65.691 -3.988  1.00 83.68  ? 223 SER B OG  1 
ATOM   3797  N N   . GLY B  1 224 ? 46.278  65.853 -4.003  1.00 65.99  ? 224 GLY B N   1 
ATOM   3798  C CA  . GLY B  1 224 ? 45.405  65.107 -4.929  1.00 59.93  ? 224 GLY B CA  1 
ATOM   3799  C C   . GLY B  1 224 ? 45.970  63.725 -5.209  1.00 57.97  ? 224 GLY B C   1 
ATOM   3800  O O   . GLY B  1 224 ? 45.214  62.738 -5.090  1.00 60.15  ? 224 GLY B O   1 
ATOM   3801  N N   . GLY B  1 225 ? 47.265  63.662 -5.537  1.00 55.98  ? 225 GLY B N   1 
ATOM   3802  C CA  . GLY B  1 225 ? 47.999  62.417 -5.837  1.00 56.42  ? 225 GLY B CA  1 
ATOM   3803  C C   . GLY B  1 225 ? 47.993  61.452 -4.661  1.00 57.56  ? 225 GLY B C   1 
ATOM   3804  O O   . GLY B  1 225 ? 47.722  60.253 -4.885  1.00 59.25  ? 225 GLY B O   1 
ATOM   3805  N N   . LEU B  1 226 ? 48.288  61.946 -3.453  1.00 51.29  ? 226 LEU B N   1 
ATOM   3806  C CA  . LEU B  1 226 ? 48.311  61.130 -2.208  1.00 51.16  ? 226 LEU B CA  1 
ATOM   3807  C C   . LEU B  1 226 ? 46.900  60.596 -1.945  1.00 51.65  ? 226 LEU B C   1 
ATOM   3808  O O   . LEU B  1 226 ? 46.745  59.364 -1.836  1.00 53.41  ? 226 LEU B O   1 
ATOM   3809  C CB  . LEU B  1 226 ? 48.811  61.978 -1.032  1.00 49.72  ? 226 LEU B CB  1 
ATOM   3810  C CG  . LEU B  1 226 ? 48.926  61.242 0.305   1.00 44.46  ? 226 LEU B CG  1 
ATOM   3811  C CD1 . LEU B  1 226 ? 49.843  60.034 0.189   1.00 41.00  ? 226 LEU B CD1 1 
ATOM   3812  C CD2 . LEU B  1 226 ? 49.408  62.171 1.409   1.00 42.86  ? 226 LEU B CD2 1 
ATOM   3813  N N   . THR B  1 227 ? 45.918  61.497 -1.858  1.00 52.88  ? 227 THR B N   1 
ATOM   3814  C CA  . THR B  1 227 ? 44.488  61.176 -1.609  1.00 57.03  ? 227 THR B CA  1 
ATOM   3815  C C   . THR B  1 227 ? 44.045  60.082 -2.589  1.00 57.93  ? 227 THR B C   1 
ATOM   3816  O O   . THR B  1 227 ? 43.436  59.095 -2.126  1.00 58.32  ? 227 THR B O   1 
ATOM   3817  C CB  . THR B  1 227 ? 43.621  62.438 -1.698  1.00 58.32  ? 227 THR B CB  1 
ATOM   3818  O OG1 . THR B  1 227 ? 44.025  63.305 -0.636  1.00 57.66  ? 227 THR B OG1 1 
ATOM   3819  C CG2 . THR B  1 227 ? 42.139  62.147 -1.597  1.00 56.59  ? 227 THR B CG2 1 
ATOM   3820  N N   . THR B  1 228 ? 44.352  60.249 -3.881  1.00 50.69  ? 228 THR B N   1 
ATOM   3821  C CA  . THR B  1 228 ? 44.057  59.260 -4.952  1.00 49.71  ? 228 THR B CA  1 
ATOM   3822  C C   . THR B  1 228 ? 44.683  57.912 -4.580  1.00 49.05  ? 228 THR B C   1 
ATOM   3823  O O   . THR B  1 228 ? 43.968  56.892 -4.640  1.00 55.78  ? 228 THR B O   1 
ATOM   3824  C CB  . THR B  1 228 ? 44.559  59.739 -6.320  1.00 51.82  ? 228 THR B CB  1 
ATOM   3825  O OG1 . THR B  1 228 ? 43.851  60.931 -6.659  1.00 45.52  ? 228 THR B OG1 1 
ATOM   3826  C CG2 . THR B  1 228 ? 44.368  58.707 -7.411  1.00 57.67  ? 228 THR B CG2 1 
ATOM   3827  N N   . THR B  1 229 ? 45.967  57.923 -4.211  1.00 50.16  ? 229 THR B N   1 
ATOM   3828  C CA  . THR B  1 229 ? 46.752  56.726 -3.805  1.00 51.02  ? 229 THR B CA  1 
ATOM   3829  C C   . THR B  1 229 ? 46.041  56.025 -2.644  1.00 49.61  ? 229 THR B C   1 
ATOM   3830  O O   . THR B  1 229 ? 45.769  54.815 -2.759  1.00 48.54  ? 229 THR B O   1 
ATOM   3831  C CB  . THR B  1 229 ? 48.184  57.110 -3.412  1.00 52.04  ? 229 THR B CB  1 
ATOM   3832  O OG1 . THR B  1 229 ? 48.781  57.757 -4.537  1.00 53.54  ? 229 THR B OG1 1 
ATOM   3833  C CG2 . THR B  1 229 ? 49.020  55.923 -2.986  1.00 50.76  ? 229 THR B CG2 1 
ATOM   3834  N N   . ILE B  1 230 ? 45.761  56.768 -1.571  1.00 45.12  ? 230 ILE B N   1 
ATOM   3835  C CA  . ILE B  1 230 ? 45.081  56.262 -0.344  1.00 48.07  ? 230 ILE B CA  1 
ATOM   3836  C C   . ILE B  1 230 ? 43.796  55.537 -0.755  1.00 51.08  ? 230 ILE B C   1 
ATOM   3837  O O   . ILE B  1 230 ? 43.632  54.366 -0.364  1.00 59.70  ? 230 ILE B O   1 
ATOM   3838  C CB  . ILE B  1 230 ? 44.813  57.420 0.636   1.00 49.67  ? 230 ILE B CB  1 
ATOM   3839  C CG1 . ILE B  1 230 ? 46.116  57.911 1.272   1.00 52.65  ? 230 ILE B CG1 1 
ATOM   3840  C CG2 . ILE B  1 230 ? 43.779  57.023 1.680   1.00 50.53  ? 230 ILE B CG2 1 
ATOM   3841  C CD1 . ILE B  1 230 ? 45.995  59.230 1.998   1.00 57.38  ? 230 ILE B CD1 1 
ATOM   3842  N N   . LEU B  1 231 ? 42.935  56.205 -1.529  1.00 48.85  ? 231 LEU B N   1 
ATOM   3843  C CA  . LEU B  1 231 ? 41.603  55.686 -1.942  1.00 45.89  ? 231 LEU B CA  1 
ATOM   3844  C C   . LEU B  1 231 ? 41.773  54.414 -2.782  1.00 41.41  ? 231 LEU B C   1 
ATOM   3845  O O   . LEU B  1 231 ? 41.141  53.396 -2.436  1.00 42.07  ? 231 LEU B O   1 
ATOM   3846  C CB  . LEU B  1 231 ? 40.862  56.773 -2.726  1.00 42.78  ? 231 LEU B CB  1 
ATOM   3847  C CG  . LEU B  1 231 ? 40.367  57.956 -1.894  1.00 44.96  ? 231 LEU B CG  1 
ATOM   3848  C CD1 . LEU B  1 231 ? 39.560  58.919 -2.750  1.00 47.94  ? 231 LEU B CD1 1 
ATOM   3849  C CD2 . LEU B  1 231 ? 39.542  57.481 -0.709  1.00 43.73  ? 231 LEU B CD2 1 
ATOM   3850  N N   . ILE B  1 232 ? 42.594  54.473 -3.836  1.00 38.34  ? 232 ILE B N   1 
ATOM   3851  C CA  . ILE B  1 232 ? 42.771  53.371 -4.830  1.00 41.70  ? 232 ILE B CA  1 
ATOM   3852  C C   . ILE B  1 232 ? 43.406  52.159 -4.140  1.00 44.10  ? 232 ILE B C   1 
ATOM   3853  O O   . ILE B  1 232 ? 42.914  51.038 -4.351  1.00 43.79  ? 232 ILE B O   1 
ATOM   3854  C CB  . ILE B  1 232 ? 43.610  53.832 -6.037  1.00 39.19  ? 232 ILE B CB  1 
ATOM   3855  C CG1 . ILE B  1 232 ? 42.889  54.914 -6.845  1.00 40.62  ? 232 ILE B CG1 1 
ATOM   3856  C CG2 . ILE B  1 232 ? 43.999  52.641 -6.902  1.00 35.53  ? 232 ILE B CG2 1 
ATOM   3857  C CD1 . ILE B  1 232 ? 43.579  55.282 -8.136  1.00 40.63  ? 232 ILE B CD1 1 
ATOM   3858  N N   . THR B  1 233 ? 44.470  52.379 -3.364  1.00 48.56  ? 233 THR B N   1 
ATOM   3859  C CA  . THR B  1 233 ? 45.233  51.311 -2.664  1.00 47.33  ? 233 THR B CA  1 
ATOM   3860  C C   . THR B  1 233 ? 44.270  50.504 -1.789  1.00 47.43  ? 233 THR B C   1 
ATOM   3861  O O   . THR B  1 233 ? 44.249  49.267 -1.928  1.00 48.20  ? 233 THR B O   1 
ATOM   3862  C CB  . THR B  1 233 ? 46.393  51.903 -1.857  1.00 45.45  ? 233 THR B CB  1 
ATOM   3863  O OG1 . THR B  1 233 ? 47.301  52.489 -2.790  1.00 40.78  ? 233 THR B OG1 1 
ATOM   3864  C CG2 . THR B  1 233 ? 47.112  50.878 -1.007  1.00 47.29  ? 233 THR B CG2 1 
ATOM   3865  N N   . LEU B  1 234 ? 43.497  51.188 -0.939  1.00 47.42  ? 234 LEU B N   1 
ATOM   3866  C CA  . LEU B  1 234 ? 42.518  50.571 -0.004  1.00 52.04  ? 234 LEU B CA  1 
ATOM   3867  C C   . LEU B  1 234 ? 41.502  49.740 -0.798  1.00 53.97  ? 234 LEU B C   1 
ATOM   3868  O O   . LEU B  1 234 ? 41.120  48.659 -0.313  1.00 54.78  ? 234 LEU B O   1 
ATOM   3869  C CB  . LEU B  1 234 ? 41.817  51.674 0.795   1.00 57.80  ? 234 LEU B CB  1 
ATOM   3870  C CG  . LEU B  1 234 ? 42.680  52.381 1.838   1.00 62.75  ? 234 LEU B CG  1 
ATOM   3871  C CD1 . LEU B  1 234 ? 41.899  53.496 2.516   1.00 68.51  ? 234 LEU B CD1 1 
ATOM   3872  C CD2 . LEU B  1 234 ? 43.208  51.395 2.870   1.00 64.77  ? 234 LEU B CD2 1 
ATOM   3873  N N   . THR B  1 235 ? 41.075  50.232 -1.966  1.00 48.76  ? 235 THR B N   1 
ATOM   3874  C CA  . THR B  1 235 ? 40.113  49.541 -2.866  1.00 43.48  ? 235 THR B CA  1 
ATOM   3875  C C   . THR B  1 235 ? 40.752  48.247 -3.383  1.00 38.92  ? 235 THR B C   1 
ATOM   3876  O O   . THR B  1 235 ? 40.135  47.180 -3.212  1.00 39.50  ? 235 THR B O   1 
ATOM   3877  C CB  . THR B  1 235 ? 39.664  50.456 -4.013  1.00 44.33  ? 235 THR B CB  1 
ATOM   3878  O OG1 . THR B  1 235 ? 39.103  51.637 -3.439  1.00 43.20  ? 235 THR B OG1 1 
ATOM   3879  C CG2 . THR B  1 235 ? 38.654  49.801 -4.929  1.00 44.05  ? 235 THR B CG2 1 
ATOM   3880  N N   . VAL B  1 236 ? 41.941  48.346 -3.985  1.00 32.50  ? 236 VAL B N   1 
ATOM   3881  C CA  . VAL B  1 236 ? 42.715  47.184 -4.514  1.00 31.43  ? 236 VAL B CA  1 
ATOM   3882  C C   . VAL B  1 236 ? 42.933  46.193 -3.366  1.00 31.80  ? 236 VAL B C   1 
ATOM   3883  O O   . VAL B  1 236 ? 42.745  44.979 -3.585  1.00 27.92  ? 236 VAL B O   1 
ATOM   3884  C CB  . VAL B  1 236 ? 44.051  47.628 -5.141  1.00 30.56  ? 236 VAL B CB  1 
ATOM   3885  C CG1 . VAL B  1 236 ? 44.938  46.441 -5.483  1.00 27.75  ? 236 VAL B CG1 1 
ATOM   3886  C CG2 . VAL B  1 236 ? 43.839  48.504 -6.365  1.00 31.31  ? 236 VAL B CG2 1 
ATOM   3887  N N   . ALA B  1 237 ? 43.308  46.701 -2.188  1.00 32.54  ? 237 ALA B N   1 
ATOM   3888  C CA  . ALA B  1 237 ? 43.525  45.912 -0.953  1.00 35.96  ? 237 ALA B CA  1 
ATOM   3889  C C   . ALA B  1 237 ? 42.245  45.142 -0.616  1.00 40.17  ? 237 ALA B C   1 
ATOM   3890  O O   . ALA B  1 237 ? 42.302  43.901 -0.566  1.00 45.28  ? 237 ALA B O   1 
ATOM   3891  C CB  . ALA B  1 237 ? 43.940  46.820 0.178   1.00 36.51  ? 237 ALA B CB  1 
ATOM   3892  N N   . ASP B  1 238 ? 41.137  45.861 -0.404  1.00 41.44  ? 238 ASP B N   1 
ATOM   3893  C CA  . ASP B  1 238 ? 39.803  45.286 -0.084  1.00 40.46  ? 238 ASP B CA  1 
ATOM   3894  C C   . ASP B  1 238 ? 39.498  44.142 -1.058  1.00 44.59  ? 238 ASP B C   1 
ATOM   3895  O O   . ASP B  1 238 ? 39.232  43.025 -0.585  1.00 46.97  ? 238 ASP B O   1 
ATOM   3896  C CB  . ASP B  1 238 ? 38.705  46.352 -0.140  1.00 40.10  ? 238 ASP B CB  1 
ATOM   3897  C CG  . ASP B  1 238 ? 38.575  47.174 1.130   1.00 41.96  ? 238 ASP B CG  1 
ATOM   3898  O OD1 . ASP B  1 238 ? 37.745  48.106 1.141   1.00 38.84  ? 238 ASP B OD1 1 
ATOM   3899  O OD2 . ASP B  1 238 ? 39.303  46.879 2.094   1.00 49.27  ? 238 ASP B OD2 1 
ATOM   3900  N N   . VAL B  1 239 ? 39.544  44.413 -2.365  1.00 45.81  ? 239 VAL B N   1 
ATOM   3901  C CA  . VAL B  1 239 ? 39.141  43.454 -3.437  1.00 45.39  ? 239 VAL B CA  1 
ATOM   3902  C C   . VAL B  1 239 ? 40.036  42.212 -3.368  1.00 45.34  ? 239 VAL B C   1 
ATOM   3903  O O   . VAL B  1 239 ? 39.488  41.103 -3.267  1.00 44.93  ? 239 VAL B O   1 
ATOM   3904  C CB  . VAL B  1 239 ? 39.195  44.103 -4.832  1.00 43.76  ? 239 VAL B CB  1 
ATOM   3905  C CG1 . VAL B  1 239 ? 39.086  43.067 -5.938  1.00 45.59  ? 239 VAL B CG1 1 
ATOM   3906  C CG2 . VAL B  1 239 ? 38.122  45.165 -4.990  1.00 45.54  ? 239 VAL B CG2 1 
ATOM   3907  N N   . ILE B  1 240 ? 41.358  42.397 -3.424  1.00 45.49  ? 240 ILE B N   1 
ATOM   3908  C CA  . ILE B  1 240 ? 42.357  41.287 -3.467  1.00 46.43  ? 240 ILE B CA  1 
ATOM   3909  C C   . ILE B  1 240 ? 42.199  40.414 -2.217  1.00 48.90  ? 240 ILE B C   1 
ATOM   3910  O O   . ILE B  1 240 ? 42.072  39.187 -2.371  1.00 51.75  ? 240 ILE B O   1 
ATOM   3911  C CB  . ILE B  1 240 ? 43.790  41.832 -3.602  1.00 46.78  ? 240 ILE B CB  1 
ATOM   3912  C CG1 . ILE B  1 240 ? 44.041  42.406 -4.998  1.00 49.44  ? 240 ILE B CG1 1 
ATOM   3913  C CG2 . ILE B  1 240 ? 44.806  40.758 -3.244  1.00 43.70  ? 240 ILE B CG2 1 
ATOM   3914  C CD1 . ILE B  1 240 ? 45.415  43.008 -5.176  1.00 53.44  ? 240 ILE B CD1 1 
ATOM   3915  N N   . VAL B  1 241 ? 42.211  41.022 -1.028  1.00 43.25  ? 241 VAL B N   1 
ATOM   3916  C CA  . VAL B  1 241 ? 42.127  40.302 0.277   1.00 44.53  ? 241 VAL B CA  1 
ATOM   3917  C C   . VAL B  1 241 ? 40.822  39.513 0.330   1.00 47.22  ? 241 VAL B C   1 
ATOM   3918  O O   . VAL B  1 241 ? 40.835  38.312 0.576   1.00 47.75  ? 241 VAL B O   1 
ATOM   3919  C CB  . VAL B  1 241 ? 42.241  41.271 1.468   1.00 45.26  ? 241 VAL B CB  1 
ATOM   3920  C CG1 . VAL B  1 241 ? 41.848  40.604 2.778   1.00 47.84  ? 241 VAL B CG1 1 
ATOM   3921  C CG2 . VAL B  1 241 ? 43.636  41.870 1.568   1.00 46.47  ? 241 VAL B CG2 1 
ATOM   3922  N N   . LYS B  1 242 ? 39.703  40.200 0.083   1.00 51.58  ? 242 LYS B N   1 
ATOM   3923  C CA  . LYS B  1 242 ? 38.382  39.627 0.289   1.00 51.64  ? 242 LYS B CA  1 
ATOM   3924  C C   . LYS B  1 242 ? 38.133  38.493 -0.703  1.00 48.09  ? 242 LYS B C   1 
ATOM   3925  O O   . LYS B  1 242 ? 37.643  37.436 -0.321  1.00 46.21  ? 242 LYS B O   1 
ATOM   3926  C CB  . LYS B  1 242 ? 37.307  40.711 0.160   1.00 53.64  ? 242 LYS B CB  1 
ATOM   3927  C CG  . LYS B  1 242 ? 37.253  41.710 1.310   1.00 57.71  ? 242 LYS B CG  1 
ATOM   3928  C CD  . LYS B  1 242 ? 36.190  42.778 1.137   1.00 63.84  ? 242 LYS B CD  1 
ATOM   3929  C CE  . LYS B  1 242 ? 36.351  43.965 2.075   1.00 66.91  ? 242 LYS B CE  1 
ATOM   3930  N NZ  . LYS B  1 242 ? 36.824  43.564 3.405   1.00 66.24  ? 242 LYS B NZ  1 
ATOM   3931  N N   . LEU B  1 243 ? 38.469  38.723 -1.977  1.00 49.24  ? 243 LEU B N   1 
ATOM   3932  C CA  . LEU B  1 243 ? 38.228  37.741 -3.023  1.00 53.64  ? 243 LEU B CA  1 
ATOM   3933  C C   . LEU B  1 243 ? 39.345  36.693 -3.018  1.00 50.35  ? 243 LEU B C   1 
ATOM   3934  O O   . LEU B  1 243 ? 39.037  35.501 -3.185  1.00 53.75  ? 243 LEU B O   1 
ATOM   3935  C CB  . LEU B  1 243 ? 38.154  38.449 -4.380  1.00 54.63  ? 243 LEU B CB  1 
ATOM   3936  C CG  . LEU B  1 243 ? 36.953  39.372 -4.577  1.00 56.90  ? 243 LEU B CG  1 
ATOM   3937  C CD1 . LEU B  1 243 ? 36.906  39.891 -6.004  1.00 57.89  ? 243 LEU B CD1 1 
ATOM   3938  C CD2 . LEU B  1 243 ? 35.653  38.665 -4.224  1.00 55.50  ? 243 LEU B CD2 1 
ATOM   3939  N N   . GLY B  1 244 ? 40.596  37.131 -2.855  1.00 47.26  ? 244 GLY B N   1 
ATOM   3940  C CA  . GLY B  1 244 ? 41.766  36.242 -2.741  1.00 41.95  ? 244 GLY B CA  1 
ATOM   3941  C C   . GLY B  1 244 ? 41.576  35.248 -1.612  1.00 38.40  ? 244 GLY B C   1 
ATOM   3942  O O   . GLY B  1 244 ? 41.569  34.042 -1.887  1.00 42.02  ? 244 GLY B O   1 
ATOM   3943  N N   . PHE B  1 245 ? 41.404  35.751 -0.389  1.00 38.31  ? 245 PHE B N   1 
ATOM   3944  C CA  . PHE B  1 245 ? 41.179  34.959 0.848   1.00 41.93  ? 245 PHE B CA  1 
ATOM   3945  C C   . PHE B  1 245 ? 39.958  34.049 0.674   1.00 46.94  ? 245 PHE B C   1 
ATOM   3946  O O   . PHE B  1 245 ? 40.094  32.830 0.875   1.00 51.41  ? 245 PHE B O   1 
ATOM   3947  C CB  . PHE B  1 245 ? 41.004  35.896 2.043   1.00 41.59  ? 245 PHE B CB  1 
ATOM   3948  C CG  . PHE B  1 245 ? 40.435  35.241 3.273   1.00 46.61  ? 245 PHE B CG  1 
ATOM   3949  C CD1 . PHE B  1 245 ? 41.258  34.564 4.157   1.00 52.32  ? 245 PHE B CD1 1 
ATOM   3950  C CD2 . PHE B  1 245 ? 39.078  35.306 3.545   1.00 54.91  ? 245 PHE B CD2 1 
ATOM   3951  C CE1 . PHE B  1 245 ? 40.734  33.965 5.290   1.00 62.83  ? 245 PHE B CE1 1 
ATOM   3952  C CE2 . PHE B  1 245 ? 38.555  34.704 4.678   1.00 61.16  ? 245 PHE B CE2 1 
ATOM   3953  C CZ  . PHE B  1 245 ? 39.384  34.036 5.547   1.00 62.51  ? 245 PHE B CZ  1 
ATOM   3954  N N   . SER B  1 246 ? 38.804  34.624 0.319   1.00 51.85  ? 246 SER B N   1 
ATOM   3955  C CA  . SER B  1 246 ? 37.500  33.916 0.197   1.00 55.42  ? 246 SER B CA  1 
ATOM   3956  C C   . SER B  1 246 ? 37.654  32.672 -0.689  1.00 56.63  ? 246 SER B C   1 
ATOM   3957  O O   . SER B  1 246 ? 37.230  31.586 -0.253  1.00 54.59  ? 246 SER B O   1 
ATOM   3958  C CB  . SER B  1 246 ? 36.417  34.832 -0.319  1.00 57.40  ? 246 SER B CB  1 
ATOM   3959  O OG  . SER B  1 246 ? 36.594  35.110 -1.699  1.00 69.12  ? 246 SER B OG  1 
ATOM   3960  N N   . THR B  1 247 ? 38.240  32.824 -1.880  1.00 57.05  ? 247 THR B N   1 
ATOM   3961  C CA  . THR B  1 247 ? 38.489  31.721 -2.847  1.00 61.13  ? 247 THR B CA  1 
ATOM   3962  C C   . THR B  1 247 ? 39.237  30.582 -2.146  1.00 60.48  ? 247 THR B C   1 
ATOM   3963  O O   . THR B  1 247 ? 38.919  29.410 -2.426  1.00 69.95  ? 247 THR B O   1 
ATOM   3964  C CB  . THR B  1 247 ? 39.276  32.207 -4.071  1.00 64.08  ? 247 THR B CB  1 
ATOM   3965  O OG1 . THR B  1 247 ? 38.578  33.316 -4.639  1.00 68.62  ? 247 THR B OG1 1 
ATOM   3966  C CG2 . THR B  1 247 ? 39.462  31.131 -5.118  1.00 71.36  ? 247 THR B CG2 1 
ATOM   3967  N N   . GLN B  1 248 ? 40.190  30.923 -1.272  1.00 58.88  ? 248 GLN B N   1 
ATOM   3968  C CA  . GLN B  1 248 ? 41.078  29.959 -0.566  1.00 51.87  ? 248 GLN B CA  1 
ATOM   3969  C C   . GLN B  1 248 ? 40.257  29.147 0.441   1.00 51.15  ? 248 GLN B C   1 
ATOM   3970  O O   . GLN B  1 248 ? 40.289  27.905 0.352   1.00 48.40  ? 248 GLN B O   1 
ATOM   3971  C CB  . GLN B  1 248 ? 42.223  30.691 0.137   1.00 54.99  ? 248 GLN B CB  1 
ATOM   3972  C CG  . GLN B  1 248 ? 43.218  31.330 -0.820  1.00 59.73  ? 248 GLN B CG  1 
ATOM   3973  C CD  . GLN B  1 248 ? 44.004  30.306 -1.599  1.00 59.11  ? 248 GLN B CD  1 
ATOM   3974  O OE1 . GLN B  1 248 ? 44.673  29.447 -1.033  1.00 67.50  ? 248 GLN B OE1 1 
ATOM   3975  N NE2 . GLN B  1 248 ? 43.935  30.397 -2.916  1.00 65.11  ? 248 GLN B NE2 1 
ATOM   3976  N N   . THR B  1 249 ? 39.555  29.820 1.359   1.00 51.49  ? 249 THR B N   1 
ATOM   3977  C CA  . THR B  1 249 ? 38.744  29.180 2.431   1.00 54.32  ? 249 THR B CA  1 
ATOM   3978  C C   . THR B  1 249 ? 37.700  28.259 1.793   1.00 53.19  ? 249 THR B C   1 
ATOM   3979  O O   . THR B  1 249 ? 37.378  27.228 2.406   1.00 66.11  ? 249 THR B O   1 
ATOM   3980  C CB  . THR B  1 249 ? 38.082  30.219 3.344   1.00 55.85  ? 249 THR B CB  1 
ATOM   3981  O OG1 . THR B  1 249 ? 37.272  31.070 2.534   1.00 51.53  ? 249 THR B OG1 1 
ATOM   3982  C CG2 . THR B  1 249 ? 39.090  31.038 4.121   1.00 58.90  ? 249 THR B CG2 1 
ATOM   3983  N N   . HIS B  1 250 ? 37.192  28.621 0.613   1.00 53.06  ? 250 HIS B N   1 
ATOM   3984  C CA  . HIS B  1 250 ? 36.255  27.783 -0.182  1.00 55.76  ? 250 HIS B CA  1 
ATOM   3985  C C   . HIS B  1 250 ? 36.963  26.478 -0.562  1.00 57.69  ? 250 HIS B C   1 
ATOM   3986  O O   . HIS B  1 250 ? 36.460  25.401 -0.180  1.00 52.99  ? 250 HIS B O   1 
ATOM   3987  C CB  . HIS B  1 250 ? 35.736  28.544 -1.411  1.00 52.65  ? 250 HIS B CB  1 
ATOM   3988  C CG  . HIS B  1 250 ? 34.640  27.825 -2.125  1.00 54.16  ? 250 HIS B CG  1 
ATOM   3989  N ND1 . HIS B  1 250 ? 33.430  27.533 -1.520  1.00 60.17  ? 250 HIS B ND1 1 
ATOM   3990  C CD2 . HIS B  1 250 ? 34.567  27.324 -3.378  1.00 53.96  ? 250 HIS B CD2 1 
ATOM   3991  C CE1 . HIS B  1 250 ? 32.659  26.885 -2.370  1.00 55.18  ? 250 HIS B CE1 1 
ATOM   3992  N NE2 . HIS B  1 250 ? 33.333  26.747 -3.519  1.00 56.27  ? 250 HIS B NE2 1 
ATOM   3993  N N   . ARG B  1 251 ? 38.090  26.579 -1.274  1.00 56.56  ? 251 ARG B N   1 
ATOM   3994  C CA  . ARG B  1 251 ? 38.903  25.416 -1.722  1.00 51.84  ? 251 ARG B CA  1 
ATOM   3995  C C   . ARG B  1 251 ? 39.149  24.494 -0.521  1.00 53.46  ? 251 ARG B C   1 
ATOM   3996  O O   . ARG B  1 251 ? 39.100  23.264 -0.707  1.00 59.24  ? 251 ARG B O   1 
ATOM   3997  C CB  . ARG B  1 251 ? 40.213  25.885 -2.363  1.00 44.08  ? 251 ARG B CB  1 
ATOM   3998  N N   . VAL B  1 252 ? 39.381  25.069 0.664   1.00 53.96  ? 252 VAL B N   1 
ATOM   3999  C CA  . VAL B  1 252 ? 39.597  24.321 1.939   1.00 55.96  ? 252 VAL B CA  1 
ATOM   4000  C C   . VAL B  1 252 ? 38.334  23.513 2.256   1.00 56.13  ? 252 VAL B C   1 
ATOM   4001  O O   . VAL B  1 252 ? 38.421  22.274 2.277   1.00 55.19  ? 252 VAL B O   1 
ATOM   4002  C CB  . VAL B  1 252 ? 39.951  25.264 3.105   1.00 55.37  ? 252 VAL B CB  1 
ATOM   4003  C CG1 . VAL B  1 252 ? 39.994  24.525 4.433   1.00 54.75  ? 252 VAL B CG1 1 
ATOM   4004  C CG2 . VAL B  1 252 ? 41.259  26.000 2.859   1.00 56.82  ? 252 VAL B CG2 1 
ATOM   4005  N N   . ALA B  1 253 ? 37.214  24.202 2.496   1.00 55.49  ? 253 ALA B N   1 
ATOM   4006  C CA  . ALA B  1 253 ? 35.908  23.615 2.879   1.00 58.50  ? 253 ALA B CA  1 
ATOM   4007  C C   . ALA B  1 253 ? 35.583  22.423 1.970   1.00 57.33  ? 253 ALA B C   1 
ATOM   4008  O O   . ALA B  1 253 ? 35.098  21.403 2.492   1.00 56.69  ? 253 ALA B O   1 
ATOM   4009  C CB  . ALA B  1 253 ? 34.827  24.666 2.811   1.00 59.61  ? 253 ALA B CB  1 
ATOM   4010  N N   . LYS B  1 254 ? 35.840  22.553 0.665   1.00 53.32  ? 254 LYS B N   1 
ATOM   4011  C CA  . LYS B  1 254 ? 35.567  21.499 -0.349  1.00 57.08  ? 254 LYS B CA  1 
ATOM   4012  C C   . LYS B  1 254 ? 36.477  20.293 -0.088  1.00 55.52  ? 254 LYS B C   1 
ATOM   4013  O O   . LYS B  1 254 ? 35.956  19.161 -0.038  1.00 51.14  ? 254 LYS B O   1 
ATOM   4014  C CB  . LYS B  1 254 ? 35.773  22.047 -1.764  1.00 57.07  ? 254 LYS B CB  1 
ATOM   4015  C CG  . LYS B  1 254 ? 34.735  23.064 -2.217  1.00 57.26  ? 254 LYS B CG  1 
ATOM   4016  C CD  . LYS B  1 254 ? 35.011  23.622 -3.596  1.00 57.05  ? 254 LYS B CD  1 
ATOM   4017  C CE  . LYS B  1 254 ? 34.769  22.617 -4.702  1.00 57.49  ? 254 LYS B CE  1 
ATOM   4018  N NZ  . LYS B  1 254 ? 35.107  23.175 -6.033  1.00 59.16  ? 254 LYS B NZ  1 
ATOM   4019  N N   . LEU B  1 255 ? 37.783  20.533 0.067   1.00 53.40  ? 255 LEU B N   1 
ATOM   4020  C CA  . LEU B  1 255 ? 38.799  19.492 0.376   1.00 51.06  ? 255 LEU B CA  1 
ATOM   4021  C C   . LEU B  1 255 ? 38.379  18.741 1.642   1.00 47.31  ? 255 LEU B C   1 
ATOM   4022  O O   . LEU B  1 255 ? 38.337  17.500 1.608   1.00 51.29  ? 255 LEU B O   1 
ATOM   4023  C CB  . LEU B  1 255 ? 40.167  20.154 0.570   1.00 55.22  ? 255 LEU B CB  1 
ATOM   4024  C CG  . LEU B  1 255 ? 41.008  20.317 -0.693  1.00 60.48  ? 255 LEU B CG  1 
ATOM   4025  C CD1 . LEU B  1 255 ? 42.265  21.123 -0.405  1.00 66.07  ? 255 LEU B CD1 1 
ATOM   4026  C CD2 . LEU B  1 255 ? 41.367  18.964 -1.288  1.00 63.25  ? 255 LEU B CD2 1 
ATOM   4027  N N   . ARG B  1 256 ? 38.078  19.480 2.712   1.00 44.44  ? 256 ARG B N   1 
ATOM   4028  C CA  . ARG B  1 256 ? 37.682  18.928 4.034   1.00 48.45  ? 256 ARG B CA  1 
ATOM   4029  C C   . ARG B  1 256 ? 36.374  18.147 3.885   1.00 47.59  ? 256 ARG B C   1 
ATOM   4030  O O   . ARG B  1 256 ? 36.239  17.100 4.541   1.00 56.47  ? 256 ARG B O   1 
ATOM   4031  C CB  . ARG B  1 256 ? 37.563  20.065 5.052   1.00 53.16  ? 256 ARG B CB  1 
ATOM   4032  C CG  . ARG B  1 256 ? 38.908  20.633 5.482   1.00 58.63  ? 256 ARG B CG  1 
ATOM   4033  C CD  . ARG B  1 256 ? 39.319  20.172 6.866   1.00 63.75  ? 256 ARG B CD  1 
ATOM   4034  N NE  . ARG B  1 256 ? 38.884  21.132 7.868   1.00 64.46  ? 256 ARG B NE  1 
ATOM   4035  C CZ  . ARG B  1 256 ? 38.709  20.861 9.153   1.00 70.68  ? 256 ARG B CZ  1 
ATOM   4036  N NH1 . ARG B  1 256 ? 38.916  19.638 9.612   1.00 73.01  ? 256 ARG B NH1 1 
ATOM   4037  N NH2 . ARG B  1 256 ? 38.307  21.816 9.970   1.00 76.61  ? 256 ARG B NH2 1 
ATOM   4038  N N   . THR B  1 257 ? 35.454  18.640 3.050   1.00 48.00  ? 257 THR B N   1 
ATOM   4039  C CA  . THR B  1 257 ? 34.155  17.983 2.741   1.00 46.90  ? 257 THR B CA  1 
ATOM   4040  C C   . THR B  1 257 ? 34.418  16.664 2.008   1.00 46.89  ? 257 THR B C   1 
ATOM   4041  O O   . THR B  1 257 ? 33.856  15.635 2.429   1.00 49.40  ? 257 THR B O   1 
ATOM   4042  C CB  . THR B  1 257 ? 33.242  18.893 1.911   1.00 44.34  ? 257 THR B CB  1 
ATOM   4043  O OG1 . THR B  1 257 ? 32.980  20.073 2.671   1.00 46.91  ? 257 THR B OG1 1 
ATOM   4044  C CG2 . THR B  1 257 ? 31.937  18.221 1.543   1.00 44.89  ? 257 THR B CG2 1 
ATOM   4045  N N   . ALA B  1 258 ? 35.237  16.707 0.953   1.00 45.36  ? 258 ALA B N   1 
ATOM   4046  C CA  . ALA B  1 258 ? 35.627  15.542 0.125   1.00 45.26  ? 258 ALA B CA  1 
ATOM   4047  C C   . ALA B  1 258 ? 36.293  14.486 1.015   1.00 48.71  ? 258 ALA B C   1 
ATOM   4048  O O   . ALA B  1 258 ? 35.943  13.297 0.891   1.00 44.29  ? 258 ALA B O   1 
ATOM   4049  C CB  . ALA B  1 258 ? 36.539  15.987 -0.993  1.00 43.45  ? 258 ALA B CB  1 
ATOM   4050  N N   . GLU B  1 259 ? 37.212  14.915 1.883   1.00 54.13  ? 259 GLU B N   1 
ATOM   4051  C CA  . GLU B  1 259 ? 37.949  14.041 2.835   1.00 57.10  ? 259 GLU B CA  1 
ATOM   4052  C C   . GLU B  1 259 ? 36.938  13.276 3.693   1.00 57.07  ? 259 GLU B C   1 
ATOM   4053  O O   . GLU B  1 259 ? 37.025  12.036 3.731   1.00 63.48  ? 259 GLU B O   1 
ATOM   4054  C CB  . GLU B  1 259 ? 38.901  14.872 3.698   1.00 61.07  ? 259 GLU B CB  1 
ATOM   4055  C CG  . GLU B  1 259 ? 40.131  15.344 2.944   1.00 64.20  ? 259 GLU B CG  1 
ATOM   4056  C CD  . GLU B  1 259 ? 41.033  16.296 3.708   1.00 70.68  ? 259 GLU B CD  1 
ATOM   4057  O OE1 . GLU B  1 259 ? 40.725  16.592 4.882   1.00 82.60  ? 259 GLU B OE1 1 
ATOM   4058  O OE2 . GLU B  1 259 ? 42.044  16.739 3.126   1.00 70.55  ? 259 GLU B OE2 1 
ATOM   4059  N N   . ASP B  1 260 ? 36.016  13.993 4.345   1.00 55.47  ? 260 ASP B N   1 
ATOM   4060  C CA  . ASP B  1 260 ? 34.956  13.413 5.213   1.00 58.31  ? 260 ASP B CA  1 
ATOM   4061  C C   . ASP B  1 260 ? 34.197  12.334 4.431   1.00 54.29  ? 260 ASP B C   1 
ATOM   4062  O O   . ASP B  1 260 ? 33.896  11.283 5.022   1.00 48.48  ? 260 ASP B O   1 
ATOM   4063  C CB  . ASP B  1 260 ? 34.007  14.496 5.735   1.00 64.31  ? 260 ASP B CB  1 
ATOM   4064  C CG  . ASP B  1 260 ? 34.624  15.386 6.801   1.00 70.66  ? 260 ASP B CG  1 
ATOM   4065  O OD1 . ASP B  1 260 ? 33.926  16.308 7.269   1.00 70.24  ? 260 ASP B OD1 1 
ATOM   4066  O OD2 . ASP B  1 260 ? 35.797  15.150 7.153   1.00 70.41  ? 260 ASP B OD2 1 
ATOM   4067  N N   . VAL B  1 261 ? 33.904  12.587 3.152   1.00 54.23  ? 261 VAL B N   1 
ATOM   4068  C CA  . VAL B  1 261 ? 33.172  11.642 2.257   1.00 54.13  ? 261 VAL B CA  1 
ATOM   4069  C C   . VAL B  1 261 ? 34.034  10.391 2.053   1.00 52.14  ? 261 VAL B C   1 
ATOM   4070  O O   . VAL B  1 261 ? 33.504  9.280  2.233   1.00 50.01  ? 261 VAL B O   1 
ATOM   4071  C CB  . VAL B  1 261 ? 32.807  12.297 0.910   1.00 55.23  ? 261 VAL B CB  1 
ATOM   4072  C CG1 . VAL B  1 261 ? 32.351  11.270 -0.115  1.00 56.11  ? 261 VAL B CG1 1 
ATOM   4073  C CG2 . VAL B  1 261 ? 31.757  13.384 1.081   1.00 59.45  ? 261 VAL B CG2 1 
ATOM   4074  N N   . ARG B  1 262 ? 35.309  10.577 1.694   1.00 57.49  ? 262 ARG B N   1 
ATOM   4075  C CA  . ARG B  1 262 ? 36.279  9.481  1.420   1.00 59.30  ? 262 ARG B CA  1 
ATOM   4076  C C   . ARG B  1 262 ? 36.500  8.663  2.699   1.00 62.00  ? 262 ARG B C   1 
ATOM   4077  O O   . ARG B  1 262 ? 36.530  7.422  2.607   1.00 64.29  ? 262 ARG B O   1 
ATOM   4078  C CB  . ARG B  1 262 ? 37.605  10.044 0.896   1.00 57.56  ? 262 ARG B CB  1 
ATOM   4079  C CG  . ARG B  1 262 ? 37.531  10.594 -0.522  1.00 59.75  ? 262 ARG B CG  1 
ATOM   4080  C CD  . ARG B  1 262 ? 38.899  10.783 -1.151  1.00 63.43  ? 262 ARG B CD  1 
ATOM   4081  N NE  . ARG B  1 262 ? 39.768  11.644 -0.361  1.00 66.02  ? 262 ARG B NE  1 
ATOM   4082  C CZ  . ARG B  1 262 ? 39.953  12.942 -0.580  1.00 64.89  ? 262 ARG B CZ  1 
ATOM   4083  N NH1 . ARG B  1 262 ? 39.328  13.550 -1.575  1.00 68.47  ? 262 ARG B NH1 1 
ATOM   4084  N NH2 . ARG B  1 262 ? 40.768  13.629 0.199   1.00 69.34  ? 262 ARG B NH2 1 
ATOM   4085  N N   . ALA B  1 263 ? 36.649  9.339  3.842   1.00 57.61  ? 263 ALA B N   1 
ATOM   4086  C CA  . ALA B  1 263 ? 36.868  8.726  5.173   1.00 58.95  ? 263 ALA B CA  1 
ATOM   4087  C C   . ALA B  1 263 ? 35.588  8.021  5.636   1.00 58.07  ? 263 ALA B C   1 
ATOM   4088  O O   . ALA B  1 263 ? 35.633  7.342  6.680   1.00 69.22  ? 263 ALA B O   1 
ATOM   4089  C CB  . ALA B  1 263 ? 37.305  9.781  6.160   1.00 61.56  ? 263 ALA B CB  1 
ATOM   4090  N N   . GLY B  1 264 ? 34.493  8.186  4.886   1.00 58.93  ? 264 GLY B N   1 
ATOM   4091  C CA  . GLY B  1 264 ? 33.176  7.585  5.180   1.00 59.51  ? 264 GLY B CA  1 
ATOM   4092  C C   . GLY B  1 264 ? 32.548  8.172  6.434   1.00 62.04  ? 264 GLY B C   1 
ATOM   4093  O O   . GLY B  1 264 ? 31.720  7.478  7.053   1.00 59.18  ? 264 GLY B O   1 
ATOM   4094  N N   . ASP B  1 265 ? 32.926  9.403  6.796   1.00 71.83  ? 265 ASP B N   1 
ATOM   4095  C CA  . ASP B  1 265 ? 32.407  10.137 7.983   1.00 73.67  ? 265 ASP B CA  1 
ATOM   4096  C C   . ASP B  1 265 ? 31.043  10.747 7.646   1.00 69.07  ? 265 ASP B C   1 
ATOM   4097  O O   . ASP B  1 265 ? 30.219  10.894 8.570   1.00 72.23  ? 265 ASP B O   1 
ATOM   4098  C CB  . ASP B  1 265 ? 33.377  11.231 8.439   1.00 81.90  ? 265 ASP B CB  1 
ATOM   4099  C CG  . ASP B  1 265 ? 34.653  10.703 9.070   1.00 82.02  ? 265 ASP B CG  1 
ATOM   4100  O OD1 . ASP B  1 265 ? 34.602  9.606  9.661   1.00 89.97  ? 265 ASP B OD1 1 
ATOM   4101  O OD2 . ASP B  1 265 ? 35.687  11.392 8.964   1.00 90.25  ? 265 ASP B OD2 1 
ATOM   4102  N N   . ASP B  1 266 ? 30.827  11.097 6.375   1.00 71.84  ? 266 ASP B N   1 
ATOM   4103  C CA  . ASP B  1 266 ? 29.568  11.710 5.874   1.00 69.94  ? 266 ASP B CA  1 
ATOM   4104  C C   . ASP B  1 266 ? 29.412  11.372 4.388   1.00 63.31  ? 266 ASP B C   1 
ATOM   4105  O O   . ASP B  1 266 ? 30.299  10.689 3.837   1.00 64.08  ? 266 ASP B O   1 
ATOM   4106  C CB  . ASP B  1 266 ? 29.563  13.224 6.109   1.00 71.10  ? 266 ASP B CB  1 
ATOM   4107  C CG  . ASP B  1 266 ? 28.189  13.807 6.396   1.00 71.36  ? 266 ASP B CG  1 
ATOM   4108  O OD1 . ASP B  1 266 ? 28.117  14.769 7.183   1.00 67.32  ? 266 ASP B OD1 1 
ATOM   4109  O OD2 . ASP B  1 266 ? 27.203  13.300 5.828   1.00 84.61  ? 266 ASP B OD2 1 
ATOM   4110  N N   . VAL B  1 267 ? 28.324  11.840 3.772   1.00 62.43  ? 267 VAL B N   1 
ATOM   4111  C CA  . VAL B  1 267 ? 28.000  11.624 2.331   1.00 59.90  ? 267 VAL B CA  1 
ATOM   4112  C C   . VAL B  1 267 ? 27.568  12.965 1.727   1.00 59.39  ? 267 VAL B C   1 
ATOM   4113  O O   . VAL B  1 267 ? 26.988  13.790 2.463   1.00 64.40  ? 267 VAL B O   1 
ATOM   4114  C CB  . VAL B  1 267 ? 26.919  10.539 2.165   1.00 58.48  ? 267 VAL B CB  1 
ATOM   4115  C CG1 . VAL B  1 267 ? 25.674  10.855 2.978   1.00 55.35  ? 267 VAL B CG1 1 
ATOM   4116  C CG2 . VAL B  1 267 ? 26.560  10.310 0.705   1.00 65.76  ? 267 VAL B CG2 1 
ATOM   4117  N N   . HIS B  1 268 ? 27.859  13.174 0.440   1.00 58.15  ? 268 HIS B N   1 
ATOM   4118  C CA  . HIS B  1 268 ? 27.540  14.415 -0.315  1.00 56.54  ? 268 HIS B CA  1 
ATOM   4119  C C   . HIS B  1 268 ? 26.829  14.043 -1.612  1.00 58.32  ? 268 HIS B C   1 
ATOM   4120  O O   . HIS B  1 268 ? 27.294  13.180 -2.352  1.00 67.95  ? 268 HIS B O   1 
ATOM   4121  C CB  . HIS B  1 268 ? 28.813  15.235 -0.550  1.00 52.46  ? 268 HIS B CB  1 
ATOM   4122  C CG  . HIS B  1 268 ? 28.554  16.683 -0.791  1.00 55.21  ? 268 HIS B CG  1 
ATOM   4123  N ND1 . HIS B  1 268 ? 28.708  17.266 -2.034  1.00 56.43  ? 268 HIS B ND1 1 
ATOM   4124  C CD2 . HIS B  1 268 ? 28.147  17.666 0.042   1.00 58.21  ? 268 HIS B CD2 1 
ATOM   4125  C CE1 . HIS B  1 268 ? 28.415  18.549 -1.953  1.00 53.23  ? 268 HIS B CE1 1 
ATOM   4126  N NE2 . HIS B  1 268 ? 28.068  18.821 -0.690  1.00 52.72  ? 268 HIS B NE2 1 
ATOM   4127  N N   . PRO B  1 269 ? 25.686  14.693 -1.927  1.00 55.97  ? 269 PRO B N   1 
ATOM   4128  C CA  . PRO B  1 269 ? 24.800  14.230 -2.996  1.00 56.54  ? 269 PRO B CA  1 
ATOM   4129  C C   . PRO B  1 269 ? 25.325  14.488 -4.417  1.00 57.78  ? 269 PRO B C   1 
ATOM   4130  O O   . PRO B  1 269 ? 24.701  14.030 -5.356  1.00 65.18  ? 269 PRO B O   1 
ATOM   4131  C CB  . PRO B  1 269 ? 23.518  15.037 -2.745  1.00 57.80  ? 269 PRO B CB  1 
ATOM   4132  C CG  . PRO B  1 269 ? 24.015  16.327 -2.129  1.00 59.45  ? 269 PRO B CG  1 
ATOM   4133  C CD  . PRO B  1 269 ? 25.194  15.915 -1.272  1.00 58.53  ? 269 PRO B CD  1 
ATOM   4134  N N   . GLU B  1 270 ? 26.444  15.208 -4.538  1.00 59.21  ? 270 GLU B N   1 
ATOM   4135  C CA  . GLU B  1 270 ? 27.097  15.529 -5.834  1.00 56.53  ? 270 GLU B CA  1 
ATOM   4136  C C   . GLU B  1 270 ? 28.599  15.259 -5.715  1.00 53.02  ? 270 GLU B C   1 
ATOM   4137  O O   . GLU B  1 270 ? 29.123  15.302 -4.584  1.00 52.99  ? 270 GLU B O   1 
ATOM   4138  C CB  . GLU B  1 270 ? 26.833  16.986 -6.225  1.00 65.97  ? 270 GLU B CB  1 
ATOM   4139  C CG  . GLU B  1 270 ? 27.686  17.991 -5.469  1.00 80.14  ? 270 GLU B CG  1 
ATOM   4140  C CD  . GLU B  1 270 ? 27.457  19.445 -5.857  1.00 90.09  ? 270 GLU B CD  1 
ATOM   4141  O OE1 . GLU B  1 270 ? 26.428  19.730 -6.503  1.00 79.32  ? 270 GLU B OE1 1 
ATOM   4142  O OE2 . GLU B  1 270 ? 28.312  20.292 -5.513  1.00 93.92  ? 270 GLU B OE2 1 
ATOM   4143  N N   . SER B  1 271 ? 29.257  14.985 -6.843  1.00 55.45  ? 271 SER B N   1 
ATOM   4144  C CA  . SER B  1 271 ? 30.731  14.821 -6.942  1.00 54.89  ? 271 SER B CA  1 
ATOM   4145  C C   . SER B  1 271 ? 31.399  16.182 -6.725  1.00 56.65  ? 271 SER B C   1 
ATOM   4146  O O   . SER B  1 271 ? 30.889  17.187 -7.261  1.00 54.87  ? 271 SER B O   1 
ATOM   4147  C CB  . SER B  1 271 ? 31.130  14.214 -8.260  1.00 54.79  ? 271 SER B CB  1 
ATOM   4148  O OG  . SER B  1 271 ? 30.393  14.792 -9.326  1.00 59.03  ? 271 SER B OG  1 
ATOM   4149  N N   . ILE B  1 272 ? 32.490  16.204 -5.956  1.00 54.39  ? 272 ILE B N   1 
ATOM   4150  C CA  . ILE B  1 272 ? 33.276  17.432 -5.636  1.00 47.91  ? 272 ILE B CA  1 
ATOM   4151  C C   . ILE B  1 272 ? 34.540  17.434 -6.499  1.00 48.55  ? 272 ILE B C   1 
ATOM   4152  O O   . ILE B  1 272 ? 35.230  16.397 -6.542  1.00 49.51  ? 272 ILE B O   1 
ATOM   4153  C CB  . ILE B  1 272 ? 33.597  17.496 -4.131  1.00 47.17  ? 272 ILE B CB  1 
ATOM   4154  C CG1 . ILE B  1 272 ? 32.317  17.553 -3.291  1.00 48.36  ? 272 ILE B CG1 1 
ATOM   4155  C CG2 . ILE B  1 272 ? 34.529  18.659 -3.829  1.00 47.46  ? 272 ILE B CG2 1 
ATOM   4156  C CD1 . ILE B  1 272 ? 32.550  17.467 -1.802  1.00 48.86  ? 272 ILE B CD1 1 
ATOM   4157  N N   . TRP B  1 273 ? 34.813  18.558 -7.168  1.00 56.11  ? 273 TRP B N   1 
ATOM   4158  C CA  . TRP B  1 273 ? 35.964  18.740 -8.092  1.00 57.07  ? 273 TRP B CA  1 
ATOM   4159  C C   . TRP B  1 273 ? 36.811  19.931 -7.632  1.00 58.50  ? 273 TRP B C   1 
ATOM   4160  O O   . TRP B  1 273 ? 36.248  20.866 -7.027  1.00 60.21  ? 273 TRP B O   1 
ATOM   4161  C CB  . TRP B  1 273 ? 35.476  18.930 -9.534  1.00 54.15  ? 273 TRP B CB  1 
ATOM   4162  C CG  . TRP B  1 273 ? 34.665  17.787 -10.060 1.00 58.12  ? 273 TRP B CG  1 
ATOM   4163  C CD1 . TRP B  1 273 ? 33.369  17.489 -9.753  1.00 61.57  ? 273 TRP B CD1 1 
ATOM   4164  C CD2 . TRP B  1 273 ? 35.091  16.787 -11.002 1.00 64.13  ? 273 TRP B CD2 1 
ATOM   4165  N NE1 . TRP B  1 273 ? 32.963  16.374 -10.434 1.00 66.58  ? 273 TRP B NE1 1 
ATOM   4166  C CE2 . TRP B  1 273 ? 33.997  15.920 -11.209 1.00 67.40  ? 273 TRP B CE2 1 
ATOM   4167  C CE3 . TRP B  1 273 ? 36.284  16.539 -11.689 1.00 63.68  ? 273 TRP B CE3 1 
ATOM   4168  C CZ2 . TRP B  1 273 ? 34.066  14.827 -12.071 1.00 67.06  ? 273 TRP B CZ2 1 
ATOM   4169  C CZ3 . TRP B  1 273 ? 36.352  15.458 -12.540 1.00 65.68  ? 273 TRP B CZ3 1 
ATOM   4170  C CH2 . TRP B  1 273 ? 35.256  14.615 -12.727 1.00 64.78  ? 273 TRP B CH2 1 
ATOM   4171  N N   . ILE B  1 274 ? 38.116  19.881 -7.910  1.00 61.82  ? 274 ILE B N   1 
ATOM   4172  C CA  . ILE B  1 274 ? 39.082  20.994 -7.675  1.00 64.83  ? 274 ILE B CA  1 
ATOM   4173  C C   . ILE B  1 274 ? 40.072  21.017 -8.844  1.00 68.03  ? 274 ILE B C   1 
ATOM   4174  O O   . ILE B  1 274 ? 40.819  20.031 -9.010  1.00 64.67  ? 274 ILE B O   1 
ATOM   4175  C CB  . ILE B  1 274 ? 39.783  20.841 -6.310  1.00 63.27  ? 274 ILE B CB  1 
ATOM   4176  C CG1 . ILE B  1 274 ? 38.771  20.846 -5.161  1.00 61.38  ? 274 ILE B CG1 1 
ATOM   4177  C CG2 . ILE B  1 274 ? 40.850  21.910 -6.128  1.00 68.36  ? 274 ILE B CG2 1 
ATOM   4178  C CD1 . ILE B  1 274 ? 39.388  20.705 -3.789  1.00 61.79  ? 274 ILE B CD1 1 
ATOM   4179  N N   . SER B  1 275 ? 40.050  22.095 -9.632  1.00 72.39  ? 275 SER B N   1 
ATOM   4180  C CA  . SER B  1 275 ? 40.888  22.281 -10.844 1.00 79.92  ? 275 SER B CA  1 
ATOM   4181  C C   . SER B  1 275 ? 40.638  21.126 -11.822 1.00 83.62  ? 275 SER B C   1 
ATOM   4182  O O   . SER B  1 275 ? 41.596  20.708 -12.502 1.00 90.50  ? 275 SER B O   1 
ATOM   4183  C CB  . SER B  1 275 ? 42.345  22.390 -10.476 1.00 88.06  ? 275 SER B CB  1 
ATOM   4184  O OG  . SER B  1 275 ? 42.560  23.462 -9.569  1.00 86.35  ? 275 SER B OG  1 
ATOM   4185  N N   . SER B  1 276 ? 39.397  20.627 -11.868 1.00 87.60  ? 276 SER B N   1 
ATOM   4186  C CA  . SER B  1 276 ? 38.911  19.603 -12.831 1.00 97.71  ? 276 SER B CA  1 
ATOM   4187  C C   . SER B  1 276 ? 39.378  18.201 -12.416 1.00 93.00  ? 276 SER B C   1 
ATOM   4188  O O   . SER B  1 276 ? 39.237  17.267 -13.232 1.00 91.84  ? 276 SER B O   1 
ATOM   4189  C CB  . SER B  1 276 ? 39.360  19.932 -14.229 1.00 103.09 ? 276 SER B CB  1 
ATOM   4190  O OG  . SER B  1 276 ? 38.910  21.222 -14.614 1.00 102.89 ? 276 SER B OG  1 
ATOM   4191  N N   . VAL B  1 277 ? 39.910  18.063 -11.198 1.00 79.16  ? 277 VAL B N   1 
ATOM   4192  C CA  . VAL B  1 277 ? 40.331  16.760 -10.601 1.00 69.84  ? 277 VAL B CA  1 
ATOM   4193  C C   . VAL B  1 277 ? 39.291  16.350 -9.552  1.00 64.97  ? 277 VAL B C   1 
ATOM   4194  O O   . VAL B  1 277 ? 39.106  17.104 -8.577  1.00 57.48  ? 277 VAL B O   1 
ATOM   4195  C CB  . VAL B  1 277 ? 41.743  16.852 -9.989  1.00 73.06  ? 277 VAL B CB  1 
ATOM   4196  C CG1 . VAL B  1 277 ? 42.150  15.557 -9.303  1.00 74.08  ? 277 VAL B CG1 1 
ATOM   4197  C CG2 . VAL B  1 277 ? 42.777  17.258 -11.027 1.00 78.47  ? 277 VAL B CG2 1 
ATOM   4198  N N   . LYS B  1 278 ? 38.637  15.203 -9.753  1.00 59.91  ? 278 LYS B N   1 
ATOM   4199  C CA  . LYS B  1 278 ? 37.585  14.674 -8.844  1.00 59.86  ? 278 LYS B CA  1 
ATOM   4200  C C   . LYS B  1 278 ? 38.201  14.408 -7.464  1.00 56.13  ? 278 LYS B C   1 
ATOM   4201  O O   . LYS B  1 278 ? 39.323  13.876 -7.412  1.00 56.55  ? 278 LYS B O   1 
ATOM   4202  C CB  . LYS B  1 278 ? 36.953  13.409 -9.432  1.00 59.64  ? 278 LYS B CB  1 
ATOM   4203  C CG  . LYS B  1 278 ? 35.819  12.818 -8.604  1.00 61.30  ? 278 LYS B CG  1 
ATOM   4204  C CD  . LYS B  1 278 ? 35.199  11.581 -9.212  1.00 62.43  ? 278 LYS B CD  1 
ATOM   4205  C CE  . LYS B  1 278 ? 34.354  11.881 -10.430 1.00 70.07  ? 278 LYS B CE  1 
ATOM   4206  N NZ  . LYS B  1 278 ? 33.548  10.707 -10.842 1.00 79.99  ? 278 LYS B NZ  1 
ATOM   4207  N N   . GLN B  1 279 ? 37.483  14.770 -6.396  1.00 57.32  ? 279 GLN B N   1 
ATOM   4208  C CA  . GLN B  1 279 ? 37.937  14.653 -4.984  1.00 55.86  ? 279 GLN B CA  1 
ATOM   4209  C C   . GLN B  1 279 ? 37.063  13.632 -4.249  1.00 52.19  ? 279 GLN B C   1 
ATOM   4210  O O   . GLN B  1 279 ? 37.620  12.786 -3.526  1.00 61.04  ? 279 GLN B O   1 
ATOM   4211  C CB  . GLN B  1 279 ? 37.861  16.014 -4.290  1.00 61.11  ? 279 GLN B CB  1 
ATOM   4212  C CG  . GLN B  1 279 ? 38.753  17.066 -4.930  1.00 58.93  ? 279 GLN B CG  1 
ATOM   4213  C CD  . GLN B  1 279 ? 40.215  16.742 -4.757  1.00 61.36  ? 279 GLN B CD  1 
ATOM   4214  O OE1 . GLN B  1 279 ? 40.671  16.408 -3.664  1.00 68.21  ? 279 GLN B OE1 1 
ATOM   4215  N NE2 . GLN B  1 279 ? 40.964  16.835 -5.843  1.00 61.85  ? 279 GLN B NE2 1 
ATOM   4216  N N   . SER B  1 280 ? 35.743  13.730 -4.418  1.00 51.56  ? 280 SER B N   1 
ATOM   4217  C CA  . SER B  1 280 ? 34.738  12.800 -3.844  1.00 50.96  ? 280 SER B CA  1 
ATOM   4218  C C   . SER B  1 280 ? 33.744  12.395 -4.936  1.00 49.08  ? 280 SER B C   1 
ATOM   4219  O O   . SER B  1 280 ? 33.696  13.077 -5.977  1.00 48.86  ? 280 SER B O   1 
ATOM   4220  C CB  . SER B  1 280 ? 34.035  13.420 -2.665  1.00 53.48  ? 280 SER B CB  1 
ATOM   4221  O OG  . SER B  1 280 ? 32.892  14.154 -3.080  1.00 52.84  ? 280 SER B OG  1 
ATOM   4222  N N   . ASP B  1 281 ? 32.991  11.320 -4.702  1.00 52.07  ? 281 ASP B N   1 
ATOM   4223  C CA  . ASP B  1 281 ? 31.903  10.850 -5.598  1.00 56.46  ? 281 ASP B CA  1 
ATOM   4224  C C   . ASP B  1 281 ? 30.558  11.182 -4.947  1.00 53.29  ? 281 ASP B C   1 
ATOM   4225  O O   . ASP B  1 281 ? 30.497  11.232 -3.702  1.00 53.91  ? 281 ASP B O   1 
ATOM   4226  C CB  . ASP B  1 281 ? 32.019  9.351  -5.889  1.00 62.22  ? 281 ASP B CB  1 
ATOM   4227  C CG  . ASP B  1 281 ? 33.065  9.007  -6.933  1.00 62.86  ? 281 ASP B CG  1 
ATOM   4228  O OD1 . ASP B  1 281 ? 32.931  7.942  -7.565  1.00 74.08  ? 281 ASP B OD1 1 
ATOM   4229  O OD2 . ASP B  1 281 ? 34.004  9.803  -7.102  1.00 72.25  ? 281 ASP B OD2 1 
ATOM   4230  N N   . ALA B  1 282 ? 29.530  11.406 -5.766  1.00 50.91  ? 282 ALA B N   1 
ATOM   4231  C CA  . ALA B  1 282 ? 28.137  11.630 -5.322  1.00 49.13  ? 282 ALA B CA  1 
ATOM   4232  C C   . ALA B  1 282 ? 27.657  10.386 -4.569  1.00 46.26  ? 282 ALA B C   1 
ATOM   4233  O O   . ALA B  1 282 ? 27.965  9.264  -5.015  1.00 39.65  ? 282 ALA B O   1 
ATOM   4234  C CB  . ALA B  1 282 ? 27.257  11.938 -6.508  1.00 51.97  ? 282 ALA B CB  1 
ATOM   4235  N N   . GLY B  1 283 ? 26.948  10.593 -3.456  1.00 43.59  ? 283 GLY B N   1 
ATOM   4236  C CA  . GLY B  1 283 ? 26.323  9.524  -2.657  1.00 39.63  ? 283 GLY B CA  1 
ATOM   4237  C C   . GLY B  1 283 ? 25.067  10.022 -1.970  1.00 42.60  ? 283 GLY B C   1 
ATOM   4238  O O   . GLY B  1 283 ? 24.999  11.226 -1.662  1.00 48.52  ? 283 GLY B O   1 
ATOM   4239  N N   . LEU B  1 284 ? 24.098  9.133  -1.745  1.00 47.95  ? 284 LEU B N   1 
ATOM   4240  C CA  . LEU B  1 284 ? 22.848  9.443  -1.003  1.00 51.35  ? 284 LEU B CA  1 
ATOM   4241  C C   . LEU B  1 284 ? 22.932  8.814  0.381   1.00 52.99  ? 284 LEU B C   1 
ATOM   4242  O O   . LEU B  1 284 ? 23.603  7.801  0.567   1.00 53.22  ? 284 LEU B O   1 
ATOM   4243  C CB  . LEU B  1 284 ? 21.640  8.897  -1.770  1.00 57.40  ? 284 LEU B CB  1 
ATOM   4244  C CG  . LEU B  1 284 ? 21.401  9.500  -3.152  1.00 63.77  ? 284 LEU B CG  1 
ATOM   4245  C CD1 . LEU B  1 284 ? 20.147  8.916  -3.785  1.00 67.04  ? 284 LEU B CD1 1 
ATOM   4246  C CD2 . LEU B  1 284 ? 21.309  11.017 -3.075  1.00 67.01  ? 284 LEU B CD2 1 
ATOM   4247  N N   . PRO B  1 285 ? 22.269  9.411  1.394   1.00 58.14  ? 285 PRO B N   1 
ATOM   4248  C CA  . PRO B  1 285 ? 22.091  8.758  2.690   1.00 60.38  ? 285 PRO B CA  1 
ATOM   4249  C C   . PRO B  1 285 ? 21.213  7.506  2.544   1.00 61.26  ? 285 PRO B C   1 
ATOM   4250  O O   . PRO B  1 285 ? 20.368  7.496  1.662   1.00 63.29  ? 285 PRO B O   1 
ATOM   4251  C CB  . PRO B  1 285 ? 21.393  9.819  3.557   1.00 63.42  ? 285 PRO B CB  1 
ATOM   4252  C CG  . PRO B  1 285 ? 21.617  11.130 2.821   1.00 64.01  ? 285 PRO B CG  1 
ATOM   4253  C CD  . PRO B  1 285 ? 21.688  10.759 1.355   1.00 60.28  ? 285 PRO B CD  1 
ATOM   4254  N N   . ARG B  1 286 ? 21.442  6.489  3.381   1.00 54.52  ? 286 ARG B N   1 
ATOM   4255  C CA  . ARG B  1 286 ? 20.668  5.219  3.371   1.00 51.08  ? 286 ARG B CA  1 
ATOM   4256  C C   . ARG B  1 286 ? 19.201  5.540  3.673   1.00 52.00  ? 286 ARG B C   1 
ATOM   4257  O O   . ARG B  1 286 ? 18.960  6.331  4.601   1.00 57.62  ? 286 ARG B O   1 
ATOM   4258  C CB  . ARG B  1 286 ? 21.236  4.231  4.395   1.00 46.17  ? 286 ARG B CB  1 
ATOM   4259  N N   . GLU B  1 287 ? 18.265  4.978  2.900   1.00 54.98  ? 287 GLU B N   1 
ATOM   4260  C CA  . GLU B  1 287 ? 16.806  5.076  3.174   1.00 55.12  ? 287 GLU B CA  1 
ATOM   4261  C C   . GLU B  1 287 ? 16.529  4.352  4.493   1.00 56.33  ? 287 GLU B C   1 
ATOM   4262  O O   . GLU B  1 287 ? 17.115  3.275  4.701   1.00 65.41  ? 287 GLU B O   1 
ATOM   4263  C CB  . GLU B  1 287 ? 15.985  4.481  2.031   1.00 60.21  ? 287 GLU B CB  1 
ATOM   4264  C CG  . GLU B  1 287 ? 15.987  5.338  0.782   1.00 66.00  ? 287 GLU B CG  1 
ATOM   4265  C CD  . GLU B  1 287 ? 15.348  4.684  -0.431  1.00 75.26  ? 287 GLU B CD  1 
ATOM   4266  O OE1 . GLU B  1 287 ? 14.778  3.583  -0.281  1.00 76.83  ? 287 GLU B OE1 1 
ATOM   4267  O OE2 . GLU B  1 287 ? 15.426  5.279  -1.522  1.00 79.37  ? 287 GLU B OE2 1 
ATOM   4268  N N   . VAL B  1 288 ? 15.680  4.932  5.345   1.00 55.07  ? 288 VAL B N   1 
ATOM   4269  C CA  . VAL B  1 288 ? 15.480  4.503  6.760   1.00 58.39  ? 288 VAL B CA  1 
ATOM   4270  C C   . VAL B  1 288 ? 13.977  4.415  7.043   1.00 61.23  ? 288 VAL B C   1 
ATOM   4271  O O   . VAL B  1 288 ? 13.211  5.188  6.434   1.00 65.79  ? 288 VAL B O   1 
ATOM   4272  C CB  . VAL B  1 288 ? 16.185  5.475  7.730   1.00 57.96  ? 288 VAL B CB  1 
ATOM   4273  C CG1 . VAL B  1 288 ? 15.749  5.273  9.173   1.00 63.84  ? 288 VAL B CG1 1 
ATOM   4274  C CG2 . VAL B  1 288 ? 17.698  5.377  7.617   1.00 54.77  ? 288 VAL B CG2 1 
ATOM   4275  N N   . TYR B  1 289 ? 13.585  3.512  7.949   1.00 63.67  ? 289 TYR B N   1 
ATOM   4276  C CA  . TYR B  1 289 ? 12.226  3.420  8.543   1.00 64.67  ? 289 TYR B CA  1 
ATOM   4277  C C   . TYR B  1 289 ? 12.157  4.276  9.815   1.00 63.59  ? 289 TYR B C   1 
ATOM   4278  O O   . TYR B  1 289 ? 13.198  4.794  10.264  1.00 58.86  ? 289 TYR B O   1 
ATOM   4279  C CB  . TYR B  1 289 ? 11.875  1.967  8.873   1.00 64.39  ? 289 TYR B CB  1 
ATOM   4280  C CG  . TYR B  1 289 ? 11.722  1.058  7.680   1.00 64.18  ? 289 TYR B CG  1 
ATOM   4281  C CD1 . TYR B  1 289 ? 10.515  0.961  7.006   1.00 68.25  ? 289 TYR B CD1 1 
ATOM   4282  C CD2 . TYR B  1 289 ? 12.776  0.278  7.236   1.00 65.85  ? 289 TYR B CD2 1 
ATOM   4283  C CE1 . TYR B  1 289 ? 10.363  0.123  5.914   1.00 71.04  ? 289 TYR B CE1 1 
ATOM   4284  C CE2 . TYR B  1 289 ? 12.641  -0.566 6.146   1.00 68.56  ? 289 TYR B CE2 1 
ATOM   4285  C CZ  . TYR B  1 289 ? 11.430  -0.643 5.481   1.00 70.78  ? 289 TYR B CZ  1 
ATOM   4286  O OH  . TYR B  1 289 ? 11.287  -1.470 4.405   1.00 74.65  ? 289 TYR B OH  1 
ATOM   4287  N N   . LEU B  1 290 ? 10.955  4.414  10.377  1.00 68.39  ? 290 LEU B N   1 
ATOM   4288  C CA  . LEU B  1 290 ? 10.705  5.104  11.669  1.00 73.33  ? 290 LEU B CA  1 
ATOM   4289  C C   . LEU B  1 290 ? 10.309  4.063  12.722  1.00 81.46  ? 290 LEU B C   1 
ATOM   4290  O O   . LEU B  1 290 ? 9.531   3.149  12.385  1.00 95.62  ? 290 LEU B O   1 
ATOM   4291  C CB  . LEU B  1 290 ? 9.597   6.145  11.478  1.00 71.30  ? 290 LEU B CB  1 
ATOM   4292  C CG  . LEU B  1 290 ? 9.887   7.238  10.451  1.00 69.44  ? 290 LEU B CG  1 
ATOM   4293  C CD1 . LEU B  1 290 ? 8.725   8.215  10.361  1.00 72.28  ? 290 LEU B CD1 1 
ATOM   4294  C CD2 . LEU B  1 290 ? 11.176  7.971  10.786  1.00 71.24  ? 290 LEU B CD2 1 
ATOM   4295  N N   . ALA B  1 291 ? 10.835  4.196  13.943  1.00 74.76  ? 291 ALA B N   1 
ATOM   4296  C CA  . ALA B  1 291 ? 10.474  3.370  15.117  1.00 76.22  ? 291 ALA B CA  1 
ATOM   4297  C C   . ALA B  1 291 ? 8.995   3.596  15.467  1.00 90.27  ? 291 ALA B C   1 
ATOM   4298  O O   . ALA B  1 291 ? 8.398   2.718  16.131  1.00 75.61  ? 291 ALA B O   1 
ATOM   4299  C CB  . ALA B  1 291 ? 11.381  3.709  16.274  1.00 67.57  ? 291 ALA B CB  1 
ATOM   4300  N N   . GLU B  1 292 ? 8.428   4.727  15.024  1.00 99.83  ? 292 GLU B N   1 
ATOM   4301  C CA  . GLU B  1 292 ? 7.026   5.144  15.309  1.00 104.15 ? 292 GLU B CA  1 
ATOM   4302  C C   . GLU B  1 292 ? 6.664   6.373  14.463  1.00 103.16 ? 292 GLU B C   1 
ATOM   4303  O O   . GLU B  1 292 ? 7.485   7.308  14.404  1.00 117.23 ? 292 GLU B O   1 
ATOM   4304  C CB  . GLU B  1 292 ? 6.865   5.456  16.798  1.00 102.12 ? 292 GLU B CB  1 
ATOM   4305  C CG  . GLU B  1 292 ? 5.420   5.599  17.232  1.00 95.38  ? 292 GLU B CG  1 
ATOM   4306  C CD  . GLU B  1 292 ? 4.579   4.360  16.983  1.00 94.05  ? 292 GLU B CD  1 
ATOM   4307  O OE1 . GLU B  1 292 ? 5.147   3.342  16.534  1.00 76.13  ? 292 GLU B OE1 1 
ATOM   4308  O OE2 . GLU B  1 292 ? 3.360   4.417  17.239  1.00 104.00 ? 292 GLU B OE2 1 
ATOM   4309  N N   . GLY B  1 293 ? 5.475   6.373  13.848  1.00 90.93  ? 293 GLY B N   1 
ATOM   4310  C CA  . GLY B  1 293 ? 4.977   7.477  13.003  1.00 84.42  ? 293 GLY B CA  1 
ATOM   4311  C C   . GLY B  1 293 ? 3.473   7.404  12.795  1.00 93.88  ? 293 GLY B C   1 
ATOM   4312  O O   . GLY B  1 293 ? 2.832   6.539  13.423  1.00 105.84 ? 293 GLY B O   1 
ATOM   4313  N N   . ALA B  1 294 ? 2.930   8.287  11.948  1.00 97.85  ? 294 ALA B N   1 
ATOM   4314  C CA  . ALA B  1 294 ? 1.491   8.379  11.599  1.00 82.18  ? 294 ALA B CA  1 
ATOM   4315  C C   . ALA B  1 294 ? 0.868   6.980  11.611  1.00 72.94  ? 294 ALA B C   1 
ATOM   4316  O O   . ALA B  1 294 ? -0.026  6.705  12.407  1.00 72.13  ? 294 ALA B O   1 
ATOM   4317  C CB  . ALA B  1 294 ? 1.326   9.038  10.252  1.00 82.86  ? 294 ALA B CB  1 
ATOM   4318  N N   . THR C  1 4   ? 47.520  67.316 -32.103 1.00 106.45 ? 4   THR C N   1 
ATOM   4319  C CA  . THR C  1 4   ? 46.269  66.604 -31.714 1.00 108.61 ? 4   THR C CA  1 
ATOM   4320  C C   . THR C  1 4   ? 45.479  66.233 -32.974 1.00 110.59 ? 4   THR C C   1 
ATOM   4321  O O   . THR C  1 4   ? 45.442  67.051 -33.913 1.00 105.95 ? 4   THR C O   1 
ATOM   4322  C CB  . THR C  1 4   ? 45.451  67.465 -30.783 1.00 99.83  ? 4   THR C CB  1 
ATOM   4323  N N   . ASN C  1 5   ? 44.886  65.036 -32.987 1.00 115.24 ? 5   ASN C N   1 
ATOM   4324  C CA  . ASN C  1 5   ? 43.996  64.537 -34.070 1.00 109.64 ? 5   ASN C CA  1 
ATOM   4325  C C   . ASN C  1 5   ? 42.743  63.918 -33.438 1.00 111.30 ? 5   ASN C C   1 
ATOM   4326  O O   . ASN C  1 5   ? 41.791  63.621 -34.186 1.00 98.42  ? 5   ASN C O   1 
ATOM   4327  C CB  . ASN C  1 5   ? 44.721  63.544 -34.982 1.00 92.07  ? 5   ASN C CB  1 
ATOM   4328  N N   . VAL C  1 6   ? 42.742  63.759 -32.109 1.00 114.00 ? 6   VAL C N   1 
ATOM   4329  C CA  . VAL C  1 6   ? 41.659  63.078 -31.335 1.00 102.21 ? 6   VAL C CA  1 
ATOM   4330  C C   . VAL C  1 6   ? 40.483  64.043 -31.158 1.00 88.58  ? 6   VAL C C   1 
ATOM   4331  O O   . VAL C  1 6   ? 40.648  65.055 -30.456 1.00 74.88  ? 6   VAL C O   1 
ATOM   4332  C CB  . VAL C  1 6   ? 42.152  62.576 -29.965 1.00 104.72 ? 6   VAL C CB  1 
ATOM   4333  C CG1 . VAL C  1 6   ? 41.084  61.756 -29.259 1.00 103.79 ? 6   VAL C CG1 1 
ATOM   4334  C CG2 . VAL C  1 6   ? 43.447  61.789 -30.080 1.00 115.29 ? 6   VAL C CG2 1 
ATOM   4335  N N   . SER C  1 7   ? 39.348  63.728 -31.786 1.00 82.96  ? 7   SER C N   1 
ATOM   4336  C CA  . SER C  1 7   ? 38.049  64.430 -31.622 1.00 80.13  ? 7   SER C CA  1 
ATOM   4337  C C   . SER C  1 7   ? 37.160  63.609 -30.681 1.00 79.13  ? 7   SER C C   1 
ATOM   4338  O O   . SER C  1 7   ? 36.454  62.706 -31.174 1.00 86.69  ? 7   SER C O   1 
ATOM   4339  C CB  . SER C  1 7   ? 37.390  64.649 -32.958 1.00 84.46  ? 7   SER C CB  1 
ATOM   4340  O OG  . SER C  1 7   ? 38.340  65.078 -33.922 1.00 92.72  ? 7   SER C OG  1 
ATOM   4341  N N   . VAL C  1 8   ? 37.223  63.894 -29.377 1.00 73.73  ? 8   VAL C N   1 
ATOM   4342  C CA  . VAL C  1 8   ? 36.500  63.137 -28.310 1.00 63.38  ? 8   VAL C CA  1 
ATOM   4343  C C   . VAL C  1 8   ? 35.025  63.046 -28.688 1.00 61.26  ? 8   VAL C C   1 
ATOM   4344  O O   . VAL C  1 8   ? 34.411  64.041 -29.069 1.00 54.95  ? 8   VAL C O   1 
ATOM   4345  C CB  . VAL C  1 8   ? 36.692  63.782 -26.925 1.00 64.67  ? 8   VAL C CB  1 
ATOM   4346  C CG1 . VAL C  1 8   ? 38.140  63.706 -26.465 1.00 61.32  ? 8   VAL C CG1 1 
ATOM   4347  C CG2 . VAL C  1 8   ? 36.189  65.218 -26.898 1.00 69.17  ? 8   VAL C CG2 1 
ATOM   4348  N N   . PRO C  1 9   ? 34.421  61.839 -28.597 1.00 60.44  ? 9   PRO C N   1 
ATOM   4349  C CA  . PRO C  1 9   ? 33.048  61.611 -29.046 1.00 58.96  ? 9   PRO C CA  1 
ATOM   4350  C C   . PRO C  1 9   ? 31.991  62.283 -28.156 1.00 57.60  ? 9   PRO C C   1 
ATOM   4351  O O   . PRO C  1 9   ? 30.871  62.457 -28.609 1.00 56.62  ? 9   PRO C O   1 
ATOM   4352  C CB  . PRO C  1 9   ? 32.871  60.083 -28.979 1.00 60.87  ? 9   PRO C CB  1 
ATOM   4353  C CG  . PRO C  1 9   ? 34.269  59.523 -28.770 1.00 58.39  ? 9   PRO C CG  1 
ATOM   4354  C CD  . PRO C  1 9   ? 35.044  60.618 -28.071 1.00 59.46  ? 9   PRO C CD  1 
ATOM   4355  N N   . TRP C  1 10  ? 32.365  62.631 -26.921 1.00 53.26  ? 10  TRP C N   1 
ATOM   4356  C CA  . TRP C  1 10  ? 31.469  63.273 -25.921 1.00 57.45  ? 10  TRP C CA  1 
ATOM   4357  C C   . TRP C  1 10  ? 31.494  64.797 -26.098 1.00 60.55  ? 10  TRP C C   1 
ATOM   4358  O O   . TRP C  1 10  ? 31.013  65.504 -25.193 1.00 61.13  ? 10  TRP C O   1 
ATOM   4359  C CB  . TRP C  1 10  ? 31.858  62.852 -24.497 1.00 56.37  ? 10  TRP C CB  1 
ATOM   4360  C CG  . TRP C  1 10  ? 33.300  63.074 -24.161 1.00 53.20  ? 10  TRP C CG  1 
ATOM   4361  C CD1 . TRP C  1 10  ? 33.876  64.228 -23.716 1.00 56.08  ? 10  TRP C CD1 1 
ATOM   4362  C CD2 . TRP C  1 10  ? 34.356  62.100 -24.230 1.00 52.16  ? 10  TRP C CD2 1 
ATOM   4363  N NE1 . TRP C  1 10  ? 35.216  64.042 -23.508 1.00 56.23  ? 10  TRP C NE1 1 
ATOM   4364  C CE2 . TRP C  1 10  ? 35.539  62.747 -23.815 1.00 56.17  ? 10  TRP C CE2 1 
ATOM   4365  C CE3 . TRP C  1 10  ? 34.418  60.752 -24.598 1.00 51.53  ? 10  TRP C CE3 1 
ATOM   4366  C CZ2 . TRP C  1 10  ? 36.766  62.089 -23.764 1.00 58.20  ? 10  TRP C CZ2 1 
ATOM   4367  C CZ3 . TRP C  1 10  ? 35.630  60.101 -24.544 1.00 53.14  ? 10  TRP C CZ3 1 
ATOM   4368  C CH2 . TRP C  1 10  ? 36.787  60.764 -24.136 1.00 56.97  ? 10  TRP C CH2 1 
ATOM   4369  N N   . GLY C  1 11  ? 32.027  65.276 -27.225 1.00 63.91  ? 11  GLY C N   1 
ATOM   4370  C CA  . GLY C  1 11  ? 32.028  66.703 -27.602 1.00 66.01  ? 11  GLY C CA  1 
ATOM   4371  C C   . GLY C  1 11  ? 30.945  67.006 -28.623 1.00 64.41  ? 11  GLY C C   1 
ATOM   4372  O O   . GLY C  1 11  ? 30.502  68.170 -28.690 1.00 62.59  ? 11  GLY C O   1 
ATOM   4373  N N   . ALA C  1 12  ? 30.525  65.989 -29.381 1.00 67.58  ? 12  ALA C N   1 
ATOM   4374  C CA  . ALA C  1 12  ? 29.538  66.088 -30.482 1.00 68.23  ? 12  ALA C CA  1 
ATOM   4375  C C   . ALA C  1 12  ? 28.121  66.230 -29.914 1.00 63.66  ? 12  ALA C C   1 
ATOM   4376  O O   . ALA C  1 12  ? 27.752  65.439 -29.024 1.00 57.57  ? 12  ALA C O   1 
ATOM   4377  C CB  . ALA C  1 12  ? 29.647  64.877 -31.374 1.00 74.87  ? 12  ALA C CB  1 
ATOM   4378  N N   . THR C  1 13  ? 27.365  67.205 -30.424 1.00 64.75  ? 13  THR C N   1 
ATOM   4379  C CA  . THR C  1 13  ? 25.925  67.427 -30.126 1.00 61.38  ? 13  THR C CA  1 
ATOM   4380  C C   . THR C  1 13  ? 25.100  66.384 -30.889 1.00 60.09  ? 13  THR C C   1 
ATOM   4381  O O   . THR C  1 13  ? 25.460  66.080 -32.041 1.00 66.50  ? 13  THR C O   1 
ATOM   4382  C CB  . THR C  1 13  ? 25.515  68.862 -30.482 1.00 60.68  ? 13  THR C CB  1 
ATOM   4383  O OG1 . THR C  1 13  ? 26.230  69.753 -29.624 1.00 67.22  ? 13  THR C OG1 1 
ATOM   4384  C CG2 . THR C  1 13  ? 24.029  69.110 -30.350 1.00 59.76  ? 13  THR C CG2 1 
ATOM   4385  N N   . LEU C  1 14  ? 24.039  65.860 -30.269 1.00 54.97  ? 14  LEU C N   1 
ATOM   4386  C CA  . LEU C  1 14  ? 23.172  64.794 -30.840 1.00 57.73  ? 14  LEU C CA  1 
ATOM   4387  C C   . LEU C  1 14  ? 21.826  65.391 -31.260 1.00 64.71  ? 14  LEU C C   1 
ATOM   4388  O O   . LEU C  1 14  ? 21.306  66.241 -30.516 1.00 70.25  ? 14  LEU C O   1 
ATOM   4389  C CB  . LEU C  1 14  ? 22.960  63.700 -29.788 1.00 56.53  ? 14  LEU C CB  1 
ATOM   4390  C CG  . LEU C  1 14  ? 24.226  63.027 -29.261 1.00 58.19  ? 14  LEU C CG  1 
ATOM   4391  C CD1 . LEU C  1 14  ? 23.898  62.086 -28.112 1.00 58.96  ? 14  LEU C CD1 1 
ATOM   4392  C CD2 . LEU C  1 14  ? 24.948  62.281 -30.372 1.00 65.83  ? 14  LEU C CD2 1 
ATOM   4393  N N   . SER C  1 15  ? 21.287  64.952 -32.401 1.00 64.55  ? 15  SER C N   1 
ATOM   4394  C CA  . SER C  1 15  ? 19.886  65.211 -32.826 1.00 58.11  ? 15  SER C CA  1 
ATOM   4395  C C   . SER C  1 15  ? 18.944  64.447 -31.888 1.00 57.57  ? 15  SER C C   1 
ATOM   4396  O O   . SER C  1 15  ? 19.444  63.622 -31.099 1.00 61.16  ? 15  SER C O   1 
ATOM   4397  C CB  . SER C  1 15  ? 19.666  64.817 -34.263 1.00 56.94  ? 15  SER C CB  1 
ATOM   4398  O OG  . SER C  1 15  ? 19.714  63.407 -34.417 1.00 54.74  ? 15  SER C OG  1 
ATOM   4399  N N   . ASN C  1 16  ? 17.638  64.716 -31.964 1.00 57.15  ? 16  ASN C N   1 
ATOM   4400  C CA  . ASN C  1 16  ? 16.605  63.999 -31.170 1.00 56.73  ? 16  ASN C CA  1 
ATOM   4401  C C   . ASN C  1 16  ? 16.557  62.539 -31.630 1.00 55.12  ? 16  ASN C C   1 
ATOM   4402  O O   . ASN C  1 16  ? 16.517  61.646 -30.760 1.00 58.68  ? 16  ASN C O   1 
ATOM   4403  C CB  . ASN C  1 16  ? 15.234  64.664 -31.285 1.00 59.54  ? 16  ASN C CB  1 
ATOM   4404  C CG  . ASN C  1 16  ? 15.138  65.933 -30.470 1.00 57.92  ? 16  ASN C CG  1 
ATOM   4405  O OD1 . ASN C  1 16  ? 16.134  66.401 -29.923 1.00 66.64  ? 16  ASN C OD1 1 
ATOM   4406  N ND2 . ASN C  1 16  ? 13.942  66.488 -30.372 1.00 65.47  ? 16  ASN C ND2 1 
ATOM   4407  N N   . ALA C  1 17  ? 16.566  62.318 -32.947 1.00 54.73  ? 17  ALA C N   1 
ATOM   4408  C CA  . ALA C  1 17  ? 16.581  60.982 -33.586 1.00 60.74  ? 17  ALA C CA  1 
ATOM   4409  C C   . ALA C  1 17  ? 17.716  60.144 -32.984 1.00 62.02  ? 17  ALA C C   1 
ATOM   4410  O O   . ALA C  1 17  ? 17.454  58.992 -32.582 1.00 63.57  ? 17  ALA C O   1 
ATOM   4411  C CB  . ALA C  1 17  ? 16.734  61.126 -35.080 1.00 63.59  ? 17  ALA C CB  1 
ATOM   4412  N N   . GLU C  1 18  ? 18.924  60.715 -32.923 1.00 59.21  ? 18  GLU C N   1 
ATOM   4413  C CA  . GLU C  1 18  ? 20.150  60.049 -32.406 1.00 62.38  ? 18  GLU C CA  1 
ATOM   4414  C C   . GLU C  1 18  ? 19.965  59.738 -30.915 1.00 57.60  ? 18  GLU C C   1 
ATOM   4415  O O   . GLU C  1 18  ? 20.144  58.565 -30.528 1.00 60.62  ? 18  GLU C O   1 
ATOM   4416  C CB  . GLU C  1 18  ? 21.375  60.931 -32.658 1.00 66.05  ? 18  GLU C CB  1 
ATOM   4417  C CG  . GLU C  1 18  ? 21.776  61.001 -34.123 1.00 72.92  ? 18  GLU C CG  1 
ATOM   4418  C CD  . GLU C  1 18  ? 22.740  62.122 -34.477 1.00 80.83  ? 18  GLU C CD  1 
ATOM   4419  O OE1 . GLU C  1 18  ? 23.492  61.967 -35.463 1.00 82.64  ? 18  GLU C OE1 1 
ATOM   4420  O OE2 . GLU C  1 18  ? 22.730  63.152 -33.775 1.00 91.47  ? 18  GLU C OE2 1 
ATOM   4421  N N   . HIS C  1 19  ? 19.608  60.750 -30.119 1.00 51.39  ? 19  HIS C N   1 
ATOM   4422  C CA  . HIS C  1 19  ? 19.403  60.651 -28.648 1.00 49.69  ? 19  HIS C CA  1 
ATOM   4423  C C   . HIS C  1 19  ? 18.377  59.556 -28.339 1.00 47.99  ? 19  HIS C C   1 
ATOM   4424  O O   . HIS C  1 19  ? 18.549  58.852 -27.327 1.00 55.32  ? 19  HIS C O   1 
ATOM   4425  C CB  . HIS C  1 19  ? 18.982  62.010 -28.073 1.00 48.49  ? 19  HIS C CB  1 
ATOM   4426  C CG  . HIS C  1 19  ? 18.998  62.066 -26.582 1.00 49.21  ? 19  HIS C CG  1 
ATOM   4427  N ND1 . HIS C  1 19  ? 17.865  61.836 -25.824 1.00 53.81  ? 19  HIS C ND1 1 
ATOM   4428  C CD2 . HIS C  1 19  ? 19.996  62.326 -25.707 1.00 44.66  ? 19  HIS C CD2 1 
ATOM   4429  C CE1 . HIS C  1 19  ? 18.164  61.954 -24.545 1.00 53.25  ? 19  HIS C CE1 1 
ATOM   4430  N NE2 . HIS C  1 19  ? 19.466  62.255 -24.446 1.00 46.81  ? 19  HIS C NE2 1 
ATOM   4431  N N   . GLN C  1 20  ? 17.351  59.421 -29.183 1.00 48.97  ? 20  GLN C N   1 
ATOM   4432  C CA  . GLN C  1 20  ? 16.251  58.435 -29.010 1.00 52.04  ? 20  GLN C CA  1 
ATOM   4433  C C   . GLN C  1 20  ? 16.779  57.030 -29.336 1.00 52.22  ? 20  GLN C C   1 
ATOM   4434  O O   . GLN C  1 20  ? 16.441  56.080 -28.598 1.00 48.56  ? 20  GLN C O   1 
ATOM   4435  C CB  . GLN C  1 20  ? 15.061  58.816 -29.894 1.00 48.24  ? 20  GLN C CB  1 
ATOM   4436  C CG  . GLN C  1 20  ? 13.721  58.332 -29.356 1.00 49.69  ? 20  GLN C CG  1 
ATOM   4437  C CD  . GLN C  1 20  ? 13.210  59.190 -28.224 1.00 50.88  ? 20  GLN C CD  1 
ATOM   4438  O OE1 . GLN C  1 20  ? 13.582  60.353 -28.089 1.00 60.90  ? 20  GLN C OE1 1 
ATOM   4439  N NE2 . GLN C  1 20  ? 12.346  58.619 -27.400 1.00 50.04  ? 20  GLN C NE2 1 
ATOM   4440  N N   . LEU C  1 21  ? 17.583  56.913 -30.397 1.00 52.32  ? 21  LEU C N   1 
ATOM   4441  C CA  . LEU C  1 21  ? 18.155  55.627 -30.880 1.00 55.20  ? 21  LEU C CA  1 
ATOM   4442  C C   . LEU C  1 21  ? 19.112  55.062 -29.825 1.00 54.99  ? 21  LEU C C   1 
ATOM   4443  O O   . LEU C  1 21  ? 18.993  53.864 -29.500 1.00 54.13  ? 21  LEU C O   1 
ATOM   4444  C CB  . LEU C  1 21  ? 18.880  55.856 -32.211 1.00 57.56  ? 21  LEU C CB  1 
ATOM   4445  C CG  . LEU C  1 21  ? 17.990  55.853 -33.455 1.00 56.00  ? 21  LEU C CG  1 
ATOM   4446  C CD1 . LEU C  1 21  ? 18.804  56.140 -34.706 1.00 53.79  ? 21  LEU C CD1 1 
ATOM   4447  C CD2 . LEU C  1 21  ? 17.246  54.533 -33.597 1.00 56.06  ? 21  LEU C CD2 1 
ATOM   4448  N N   . ILE C  1 22  ? 20.025  55.893 -29.317 1.00 48.14  ? 22  ILE C N   1 
ATOM   4449  C CA  . ILE C  1 22  ? 21.052  55.489 -28.312 1.00 46.58  ? 22  ILE C CA  1 
ATOM   4450  C C   . ILE C  1 22  ? 20.335  54.908 -27.088 1.00 47.77  ? 22  ILE C C   1 
ATOM   4451  O O   . ILE C  1 22  ? 20.641  53.760 -26.713 1.00 48.61  ? 22  ILE C O   1 
ATOM   4452  C CB  . ILE C  1 22  ? 21.962  56.678 -27.948 1.00 46.75  ? 22  ILE C CB  1 
ATOM   4453  C CG1 . ILE C  1 22  ? 22.773  57.152 -29.158 1.00 48.67  ? 22  ILE C CG1 1 
ATOM   4454  C CG2 . ILE C  1 22  ? 22.860  56.332 -26.770 1.00 45.25  ? 22  ILE C CG2 1 
ATOM   4455  C CD1 . ILE C  1 22  ? 23.388  58.521 -28.986 1.00 51.28  ? 22  ILE C CD1 1 
ATOM   4456  N N   . PHE C  1 23  ? 19.404  55.668 -26.505 1.00 45.27  ? 23  PHE C N   1 
ATOM   4457  C CA  . PHE C  1 23  ? 18.614  55.268 -25.311 1.00 47.52  ? 23  PHE C CA  1 
ATOM   4458  C C   . PHE C  1 23  ? 17.943  53.914 -25.568 1.00 47.39  ? 23  PHE C C   1 
ATOM   4459  O O   . PHE C  1 23  ? 18.057  53.008 -24.716 1.00 46.66  ? 23  PHE C O   1 
ATOM   4460  C CB  . PHE C  1 23  ? 17.576  56.338 -24.970 1.00 46.94  ? 23  PHE C CB  1 
ATOM   4461  C CG  . PHE C  1 23  ? 16.776  56.047 -23.725 1.00 49.39  ? 23  PHE C CG  1 
ATOM   4462  C CD1 . PHE C  1 23  ? 15.446  55.665 -23.808 1.00 55.36  ? 23  PHE C CD1 1 
ATOM   4463  C CD2 . PHE C  1 23  ? 17.357  56.149 -22.471 1.00 49.43  ? 23  PHE C CD2 1 
ATOM   4464  C CE1 . PHE C  1 23  ? 14.712  55.398 -22.664 1.00 56.16  ? 23  PHE C CE1 1 
ATOM   4465  C CE2 . PHE C  1 23  ? 16.622  55.877 -21.327 1.00 51.77  ? 23  PHE C CE2 1 
ATOM   4466  C CZ  . PHE C  1 23  ? 15.301  55.505 -21.426 1.00 53.32  ? 23  PHE C CZ  1 
ATOM   4467  N N   . TYR C  1 24  ? 17.258  53.793 -26.709 1.00 48.65  ? 24  TYR C N   1 
ATOM   4468  C CA  . TYR C  1 24  ? 16.544  52.568 -27.155 1.00 49.51  ? 24  TYR C CA  1 
ATOM   4469  C C   . TYR C  1 24  ? 17.466  51.351 -27.002 1.00 49.30  ? 24  TYR C C   1 
ATOM   4470  O O   . TYR C  1 24  ? 17.108  50.409 -26.264 1.00 43.16  ? 24  TYR C O   1 
ATOM   4471  C CB  . TYR C  1 24  ? 16.066  52.733 -28.600 1.00 49.40  ? 24  TYR C CB  1 
ATOM   4472  C CG  . TYR C  1 24  ? 15.407  51.513 -29.196 1.00 50.19  ? 24  TYR C CG  1 
ATOM   4473  C CD1 . TYR C  1 24  ? 16.129  50.610 -29.962 1.00 49.04  ? 24  TYR C CD1 1 
ATOM   4474  C CD2 . TYR C  1 24  ? 14.058  51.263 -29.000 1.00 51.58  ? 24  TYR C CD2 1 
ATOM   4475  C CE1 . TYR C  1 24  ? 15.527  49.491 -30.515 1.00 49.32  ? 24  TYR C CE1 1 
ATOM   4476  C CE2 . TYR C  1 24  ? 13.442  50.148 -29.542 1.00 49.57  ? 24  TYR C CE2 1 
ATOM   4477  C CZ  . TYR C  1 24  ? 14.178  49.259 -30.305 1.00 49.63  ? 24  TYR C CZ  1 
ATOM   4478  O OH  . TYR C  1 24  ? 13.569  48.160 -30.839 1.00 45.47  ? 24  TYR C OH  1 
ATOM   4479  N N   . PHE C  1 25  ? 18.622  51.382 -27.674 1.00 46.30  ? 25  PHE C N   1 
ATOM   4480  C CA  . PHE C  1 25  ? 19.603  50.266 -27.735 1.00 49.89  ? 25  PHE C CA  1 
ATOM   4481  C C   . PHE C  1 25  ? 20.191  50.017 -26.341 1.00 53.99  ? 25  PHE C C   1 
ATOM   4482  O O   . PHE C  1 25  ? 20.358  48.840 -25.967 1.00 57.92  ? 25  PHE C O   1 
ATOM   4483  C CB  . PHE C  1 25  ? 20.687  50.560 -28.775 1.00 51.99  ? 25  PHE C CB  1 
ATOM   4484  C CG  . PHE C  1 25  ? 20.272  50.249 -30.190 1.00 60.40  ? 25  PHE C CG  1 
ATOM   4485  C CD1 . PHE C  1 25  ? 20.348  48.955 -30.681 1.00 63.31  ? 25  PHE C CD1 1 
ATOM   4486  C CD2 . PHE C  1 25  ? 19.786  51.242 -31.025 1.00 60.24  ? 25  PHE C CD2 1 
ATOM   4487  C CE1 . PHE C  1 25  ? 19.957  48.663 -31.978 1.00 58.15  ? 25  PHE C CE1 1 
ATOM   4488  C CE2 . PHE C  1 25  ? 19.394  50.948 -32.322 1.00 60.67  ? 25  PHE C CE2 1 
ATOM   4489  C CZ  . PHE C  1 25  ? 19.480  49.660 -32.796 1.00 57.80  ? 25  PHE C CZ  1 
ATOM   4490  N N   . LEU C  1 26  ? 20.488  51.089 -25.600 1.00 53.61  ? 26  LEU C N   1 
ATOM   4491  C CA  . LEU C  1 26  ? 21.034  51.013 -24.218 1.00 50.19  ? 26  LEU C CA  1 
ATOM   4492  C C   . LEU C  1 26  ? 20.092  50.179 -23.345 1.00 46.17  ? 26  LEU C C   1 
ATOM   4493  O O   . LEU C  1 26  ? 20.563  49.193 -22.745 1.00 51.80  ? 26  LEU C O   1 
ATOM   4494  C CB  . LEU C  1 26  ? 21.201  52.426 -23.650 1.00 50.53  ? 26  LEU C CB  1 
ATOM   4495  C CG  . LEU C  1 26  ? 22.510  53.127 -24.009 1.00 50.27  ? 26  LEU C CG  1 
ATOM   4496  C CD1 . LEU C  1 26  ? 22.670  54.408 -23.210 1.00 51.20  ? 26  LEU C CD1 1 
ATOM   4497  C CD2 . LEU C  1 26  ? 23.704  52.210 -23.781 1.00 49.20  ? 26  LEU C CD2 1 
ATOM   4498  N N   . VAL C  1 27  ? 18.813  50.561 -23.285 1.00 39.86  ? 27  VAL C N   1 
ATOM   4499  C CA  . VAL C  1 27  ? 17.799  49.940 -22.382 1.00 39.04  ? 27  VAL C CA  1 
ATOM   4500  C C   . VAL C  1 27  ? 17.470  48.533 -22.893 1.00 40.51  ? 27  VAL C C   1 
ATOM   4501  O O   . VAL C  1 27  ? 17.398  47.608 -22.060 1.00 39.77  ? 27  VAL C O   1 
ATOM   4502  C CB  . VAL C  1 27  ? 16.533  50.807 -22.255 1.00 36.16  ? 27  VAL C CB  1 
ATOM   4503  C CG1 . VAL C  1 27  ? 15.511  50.163 -21.328 1.00 33.93  ? 27  VAL C CG1 1 
ATOM   4504  C CG2 . VAL C  1 27  ? 16.860  52.218 -21.790 1.00 32.86  ? 27  VAL C CG2 1 
ATOM   4505  N N   . VAL C  1 28  ? 17.284  48.378 -24.207 1.00 44.76  ? 28  VAL C N   1 
ATOM   4506  C CA  . VAL C  1 28  ? 17.036  47.056 -24.858 1.00 46.97  ? 28  VAL C CA  1 
ATOM   4507  C C   . VAL C  1 28  ? 18.150  46.100 -24.420 1.00 43.82  ? 28  VAL C C   1 
ATOM   4508  O O   . VAL C  1 28  ? 17.834  44.948 -24.068 1.00 42.48  ? 28  VAL C O   1 
ATOM   4509  C CB  . VAL C  1 28  ? 16.960  47.165 -26.394 1.00 51.17  ? 28  VAL C CB  1 
ATOM   4510  C CG1 . VAL C  1 28  ? 17.011  45.797 -27.058 1.00 50.98  ? 28  VAL C CG1 1 
ATOM   4511  C CG2 . VAL C  1 28  ? 15.728  47.932 -26.849 1.00 49.48  ? 28  VAL C CG2 1 
ATOM   4512  N N   . ALA C  1 29  ? 19.400  46.573 -24.438 1.00 42.64  ? 29  ALA C N   1 
ATOM   4513  C CA  . ALA C  1 29  ? 20.601  45.824 -23.999 1.00 44.11  ? 29  ALA C CA  1 
ATOM   4514  C C   . ALA C  1 29  ? 20.408  45.367 -22.550 1.00 44.87  ? 29  ALA C C   1 
ATOM   4515  O O   . ALA C  1 29  ? 20.416  44.144 -22.308 1.00 47.38  ? 29  ALA C O   1 
ATOM   4516  C CB  . ALA C  1 29  ? 21.832  46.685 -24.145 1.00 42.80  ? 29  ALA C CB  1 
ATOM   4517  N N   . ALA C  1 30  ? 20.228  46.324 -21.635 1.00 44.06  ? 30  ALA C N   1 
ATOM   4518  C CA  . ALA C  1 30  ? 20.036  46.096 -20.183 1.00 43.26  ? 30  ALA C CA  1 
ATOM   4519  C C   . ALA C  1 30  ? 18.994  44.993 -19.963 1.00 40.99  ? 30  ALA C C   1 
ATOM   4520  O O   . ALA C  1 30  ? 19.260  44.079 -19.156 1.00 44.39  ? 30  ALA C O   1 
ATOM   4521  C CB  . ALA C  1 30  ? 19.624  47.384 -19.513 1.00 42.30  ? 30  ALA C CB  1 
ATOM   4522  N N   . LEU C  1 31  ? 17.856  45.081 -20.659 1.00 38.14  ? 31  LEU C N   1 
ATOM   4523  C CA  . LEU C  1 31  ? 16.707  44.147 -20.514 1.00 39.00  ? 31  LEU C CA  1 
ATOM   4524  C C   . LEU C  1 31  ? 17.083  42.776 -21.085 1.00 41.69  ? 31  LEU C C   1 
ATOM   4525  O O   . LEU C  1 31  ? 16.718  41.759 -20.462 1.00 43.42  ? 31  LEU C O   1 
ATOM   4526  C CB  . LEU C  1 31  ? 15.491  44.743 -21.229 1.00 39.56  ? 31  LEU C CB  1 
ATOM   4527  C CG  . LEU C  1 31  ? 14.921  46.006 -20.585 1.00 42.84  ? 31  LEU C CG  1 
ATOM   4528  C CD1 . LEU C  1 31  ? 13.882  46.657 -21.484 1.00 47.68  ? 31  LEU C CD1 1 
ATOM   4529  C CD2 . LEU C  1 31  ? 14.326  45.700 -19.219 1.00 42.41  ? 31  LEU C CD2 1 
ATOM   4530  N N   . ALA C  1 32  ? 17.782  42.753 -22.223 1.00 42.84  ? 32  ALA C N   1 
ATOM   4531  C CA  . ALA C  1 32  ? 18.326  41.527 -22.854 1.00 43.30  ? 32  ALA C CA  1 
ATOM   4532  C C   . ALA C  1 32  ? 19.155  40.761 -21.818 1.00 48.58  ? 32  ALA C C   1 
ATOM   4533  O O   . ALA C  1 32  ? 19.037  39.521 -21.756 1.00 53.76  ? 32  ALA C O   1 
ATOM   4534  C CB  . ALA C  1 32  ? 19.158  41.886 -24.061 1.00 41.74  ? 32  ALA C CB  1 
ATOM   4535  N N   . PHE C  1 33  ? 19.953  41.491 -21.032 1.00 49.26  ? 33  PHE C N   1 
ATOM   4536  C CA  . PHE C  1 33  ? 20.882  40.944 -20.009 1.00 43.96  ? 33  PHE C CA  1 
ATOM   4537  C C   . PHE C  1 33  ? 20.076  40.408 -18.820 1.00 43.47  ? 33  PHE C C   1 
ATOM   4538  O O   . PHE C  1 33  ? 20.445  39.350 -18.274 1.00 48.95  ? 33  PHE C O   1 
ATOM   4539  C CB  . PHE C  1 33  ? 21.893  42.010 -19.583 1.00 41.70  ? 33  PHE C CB  1 
ATOM   4540  C CG  . PHE C  1 33  ? 22.955  42.312 -20.610 1.00 40.37  ? 33  PHE C CG  1 
ATOM   4541  C CD1 . PHE C  1 33  ? 23.595  41.290 -21.293 1.00 42.00  ? 33  PHE C CD1 1 
ATOM   4542  C CD2 . PHE C  1 33  ? 23.329  43.618 -20.880 1.00 45.44  ? 33  PHE C CD2 1 
ATOM   4543  C CE1 . PHE C  1 33  ? 24.577  41.569 -22.230 1.00 42.11  ? 33  PHE C CE1 1 
ATOM   4544  C CE2 . PHE C  1 33  ? 24.316  43.895 -21.813 1.00 44.78  ? 33  PHE C CE2 1 
ATOM   4545  C CZ  . PHE C  1 33  ? 24.938  42.870 -22.486 1.00 43.85  ? 33  PHE C CZ  1 
ATOM   4546  N N   . VAL C  1 34  ? 19.012  41.115 -18.432 1.00 43.49  ? 34  VAL C N   1 
ATOM   4547  C CA  . VAL C  1 34  ? 18.064  40.670 -17.368 1.00 48.87  ? 34  VAL C CA  1 
ATOM   4548  C C   . VAL C  1 34  ? 17.494  39.307 -17.780 1.00 46.04  ? 34  VAL C C   1 
ATOM   4549  O O   . VAL C  1 34  ? 17.581  38.357 -16.975 1.00 49.91  ? 34  VAL C O   1 
ATOM   4550  C CB  . VAL C  1 34  ? 16.951  41.708 -17.126 1.00 55.26  ? 34  VAL C CB  1 
ATOM   4551  C CG1 . VAL C  1 34  ? 15.852  41.622 -18.171 1.00 71.14  ? 34  VAL C CG1 1 
ATOM   4552  C CG2 . VAL C  1 34  ? 16.361  41.579 -15.730 1.00 53.01  ? 34  VAL C CG2 1 
ATOM   4553  N N   . ALA C  1 35  ? 16.952  39.216 -18.999 1.00 43.09  ? 35  ALA C N   1 
ATOM   4554  C CA  . ALA C  1 35  ? 16.372  37.986 -19.585 1.00 43.30  ? 35  ALA C CA  1 
ATOM   4555  C C   . ALA C  1 35  ? 17.433  36.880 -19.599 1.00 40.92  ? 35  ALA C C   1 
ATOM   4556  O O   . ALA C  1 35  ? 17.103  35.739 -19.229 1.00 41.81  ? 35  ALA C O   1 
ATOM   4557  C CB  . ALA C  1 35  ? 15.857  38.271 -20.974 1.00 45.56  ? 35  ALA C CB  1 
ATOM   4558  N N   . GLY C  1 36  ? 18.654  37.217 -20.022 1.00 39.38  ? 36  GLY C N   1 
ATOM   4559  C CA  . GLY C  1 36  ? 19.805  36.295 -20.059 1.00 40.68  ? 36  GLY C CA  1 
ATOM   4560  C C   . GLY C  1 36  ? 20.144  35.781 -18.671 1.00 40.59  ? 36  GLY C C   1 
ATOM   4561  O O   . GLY C  1 36  ? 20.255  34.553 -18.503 1.00 39.21  ? 36  GLY C O   1 
ATOM   4562  N N   . PHE C  1 37  ? 20.302  36.693 -17.708 1.00 46.46  ? 37  PHE C N   1 
ATOM   4563  C CA  . PHE C  1 37  ? 20.621  36.383 -16.291 1.00 45.24  ? 37  PHE C CA  1 
ATOM   4564  C C   . PHE C  1 37  ? 19.603  35.368 -15.759 1.00 48.86  ? 37  PHE C C   1 
ATOM   4565  O O   . PHE C  1 37  ? 20.015  34.339 -15.193 1.00 54.20  ? 37  PHE C O   1 
ATOM   4566  C CB  . PHE C  1 37  ? 20.625  37.657 -15.442 1.00 40.55  ? 37  PHE C CB  1 
ATOM   4567  C CG  . PHE C  1 37  ? 20.994  37.426 -14.000 1.00 41.94  ? 37  PHE C CG  1 
ATOM   4568  C CD1 . PHE C  1 37  ? 22.302  37.584 -13.572 1.00 45.36  ? 37  PHE C CD1 1 
ATOM   4569  C CD2 . PHE C  1 37  ? 20.041  37.027 -13.076 1.00 42.39  ? 37  PHE C CD2 1 
ATOM   4570  C CE1 . PHE C  1 37  ? 22.647  37.362 -12.248 1.00 44.12  ? 37  PHE C CE1 1 
ATOM   4571  C CE2 . PHE C  1 37  ? 20.388  36.802 -11.753 1.00 42.33  ? 37  PHE C CE2 1 
ATOM   4572  C CZ  . PHE C  1 37  ? 21.690  36.971 -11.341 1.00 42.82  ? 37  PHE C CZ  1 
ATOM   4573  N N   . ILE C  1 38  ? 18.311  35.657 -15.942 1.00 47.96  ? 38  ILE C N   1 
ATOM   4574  C CA  . ILE C  1 38  ? 17.181  34.793 -15.488 1.00 46.07  ? 38  ILE C CA  1 
ATOM   4575  C C   . ILE C  1 38  ? 17.326  33.407 -16.130 1.00 47.64  ? 38  ILE C C   1 
ATOM   4576  O O   . ILE C  1 38  ? 17.368  32.412 -15.377 1.00 44.73  ? 38  ILE C O   1 
ATOM   4577  C CB  . ILE C  1 38  ? 15.824  35.448 -15.814 1.00 43.44  ? 38  ILE C CB  1 
ATOM   4578  C CG1 . ILE C  1 38  ? 15.622  36.738 -15.014 1.00 43.18  ? 38  ILE C CG1 1 
ATOM   4579  C CG2 . ILE C  1 38  ? 14.681  34.469 -15.597 1.00 43.78  ? 38  ILE C CG2 1 
ATOM   4580  C CD1 . ILE C  1 38  ? 14.323  37.449 -15.309 1.00 43.43  ? 38  ILE C CD1 1 
ATOM   4581  N N   . ARG C  1 39  ? 17.406  33.344 -17.464 1.00 48.96  ? 39  ARG C N   1 
ATOM   4582  C CA  . ARG C  1 39  ? 17.571  32.074 -18.222 1.00 48.85  ? 39  ARG C CA  1 
ATOM   4583  C C   . ARG C  1 39  ? 18.729  31.285 -17.605 1.00 45.86  ? 39  ARG C C   1 
ATOM   4584  O O   . ARG C  1 39  ? 18.521  30.104 -17.249 1.00 46.99  ? 39  ARG C O   1 
ATOM   4585  C CB  . ARG C  1 39  ? 17.839  32.334 -19.709 1.00 51.93  ? 39  ARG C CB  1 
ATOM   4586  C CG  . ARG C  1 39  ? 18.232  31.092 -20.499 1.00 46.16  ? 39  ARG C CG  1 
ATOM   4587  N N   . THR C  1 40  ? 19.894  31.928 -17.477 1.00 44.48  ? 40  THR C N   1 
ATOM   4588  C CA  . THR C  1 40  ? 21.156  31.314 -16.984 1.00 46.50  ? 40  THR C CA  1 
ATOM   4589  C C   . THR C  1 40  ? 20.930  30.711 -15.595 1.00 50.35  ? 40  THR C C   1 
ATOM   4590  O O   . THR C  1 40  ? 21.364  29.560 -15.381 1.00 52.62  ? 40  THR C O   1 
ATOM   4591  C CB  . THR C  1 40  ? 22.300  32.334 -16.952 1.00 43.69  ? 40  THR C CB  1 
ATOM   4592  O OG1 . THR C  1 40  ? 22.622  32.665 -18.303 1.00 50.33  ? 40  THR C OG1 1 
ATOM   4593  C CG2 . THR C  1 40  ? 23.528  31.814 -16.237 1.00 41.37  ? 40  THR C CG2 1 
ATOM   4594  N N   . TYR C  1 41  ? 20.284  31.465 -14.697 1.00 48.64  ? 41  TYR C N   1 
ATOM   4595  C CA  . TYR C  1 41  ? 20.012  31.067 -13.292 1.00 47.19  ? 41  TYR C CA  1 
ATOM   4596  C C   . TYR C  1 41  ? 19.142  29.806 -13.280 1.00 49.42  ? 41  TYR C C   1 
ATOM   4597  O O   . TYR C  1 41  ? 19.476  28.850 -12.561 1.00 57.85  ? 41  TYR C O   1 
ATOM   4598  C CB  . TYR C  1 41  ? 19.335  32.199 -12.514 1.00 45.51  ? 41  TYR C CB  1 
ATOM   4599  C CG  . TYR C  1 41  ? 19.042  31.861 -11.073 1.00 51.41  ? 41  TYR C CG  1 
ATOM   4600  C CD1 . TYR C  1 41  ? 17.774  31.474 -10.668 1.00 55.24  ? 41  TYR C CD1 1 
ATOM   4601  C CD2 . TYR C  1 41  ? 20.042  31.898 -10.116 1.00 54.84  ? 41  TYR C CD2 1 
ATOM   4602  C CE1 . TYR C  1 41  ? 17.504  31.146 -9.349  1.00 55.75  ? 41  TYR C CE1 1 
ATOM   4603  C CE2 . TYR C  1 41  ? 19.788  31.577 -8.793  1.00 58.68  ? 41  TYR C CE2 1 
ATOM   4604  C CZ  . TYR C  1 41  ? 18.515  31.199 -8.407  1.00 60.16  ? 41  TYR C CZ  1 
ATOM   4605  O OH  . TYR C  1 41  ? 18.258  30.878 -7.104  1.00 69.33  ? 41  TYR C OH  1 
ATOM   4606  N N   . ILE C  1 42  ? 18.061  29.808 -14.061 1.00 50.60  ? 42  ILE C N   1 
ATOM   4607  C CA  . ILE C  1 42  ? 17.018  28.740 -14.054 1.00 53.44  ? 42  ILE C CA  1 
ATOM   4608  C C   . ILE C  1 42  ? 17.608  27.440 -14.615 1.00 54.75  ? 42  ILE C C   1 
ATOM   4609  O O   . ILE C  1 42  ? 17.215  26.359 -14.133 1.00 55.79  ? 42  ILE C O   1 
ATOM   4610  C CB  . ILE C  1 42  ? 15.771  29.201 -14.832 1.00 56.02  ? 42  ILE C CB  1 
ATOM   4611  C CG1 . ILE C  1 42  ? 14.943  30.184 -14.002 1.00 59.74  ? 42  ILE C CG1 1 
ATOM   4612  C CG2 . ILE C  1 42  ? 14.944  28.012 -15.295 1.00 56.66  ? 42  ILE C CG2 1 
ATOM   4613  C CD1 . ILE C  1 42  ? 13.455  30.045 -14.194 1.00 66.79  ? 42  ILE C CD1 1 
ATOM   4614  N N   . THR C  1 43  ? 18.522  27.544 -15.583 1.00 51.28  ? 43  THR C N   1 
ATOM   4615  C CA  . THR C  1 43  ? 19.115  26.390 -16.311 1.00 51.01  ? 43  THR C CA  1 
ATOM   4616  C C   . THR C  1 43  ? 20.484  26.040 -15.719 1.00 56.17  ? 43  THR C C   1 
ATOM   4617  O O   . THR C  1 43  ? 21.275  25.389 -16.426 1.00 62.38  ? 43  THR C O   1 
ATOM   4618  C CB  . THR C  1 43  ? 19.231  26.694 -17.810 1.00 50.92  ? 43  THR C CB  1 
ATOM   4619  O OG1 . THR C  1 43  ? 20.110  27.807 -17.979 1.00 50.02  ? 43  THR C OG1 1 
ATOM   4620  C CG2 . THR C  1 43  ? 17.892  26.999 -18.445 1.00 54.46  ? 43  THR C CG2 1 
ATOM   4621  N N   . ARG C  1 44  ? 20.746  26.440 -14.471 1.00 57.56  ? 44  ARG C N   1 
ATOM   4622  C CA  . ARG C  1 44  ? 22.079  26.304 -13.824 1.00 55.48  ? 44  ARG C CA  1 
ATOM   4623  C C   . ARG C  1 44  ? 22.355  24.826 -13.520 1.00 59.76  ? 44  ARG C C   1 
ATOM   4624  O O   . ARG C  1 44  ? 23.519  24.410 -13.655 1.00 62.46  ? 44  ARG C O   1 
ATOM   4625  C CB  . ARG C  1 44  ? 22.174  27.177 -12.567 1.00 51.13  ? 44  ARG C CB  1 
ATOM   4626  C CG  . ARG C  1 44  ? 21.328  26.719 -11.387 1.00 52.39  ? 44  ARG C CG  1 
ATOM   4627  C CD  . ARG C  1 44  ? 21.368  27.737 -10.259 1.00 56.21  ? 44  ARG C CD  1 
ATOM   4628  N NE  . ARG C  1 44  ? 20.697  27.288 -9.045  1.00 65.02  ? 44  ARG C NE  1 
ATOM   4629  C CZ  . ARG C  1 44  ? 19.406  27.465 -8.779  1.00 70.57  ? 44  ARG C CZ  1 
ATOM   4630  N NH1 . ARG C  1 44  ? 18.625  28.079 -9.651  1.00 75.32  ? 44  ARG C NH1 1 
ATOM   4631  N NH2 . ARG C  1 44  ? 18.898  27.017 -7.644  1.00 75.71  ? 44  ARG C NH2 1 
ATOM   4632  N N   . ASN C  1 45  ? 21.323  24.064 -13.146 1.00 65.33  ? 45  ASN C N   1 
ATOM   4633  C CA  . ASN C  1 45  ? 21.454  22.666 -12.656 1.00 62.78  ? 45  ASN C CA  1 
ATOM   4634  C C   . ASN C  1 45  ? 21.284  21.683 -13.822 1.00 59.01  ? 45  ASN C C   1 
ATOM   4635  O O   . ASN C  1 45  ? 21.044  20.491 -13.555 1.00 62.77  ? 45  ASN C O   1 
ATOM   4636  C CB  . ASN C  1 45  ? 20.473  22.387 -11.517 1.00 66.92  ? 45  ASN C CB  1 
ATOM   4637  C CG  . ASN C  1 45  ? 20.874  23.080 -10.232 1.00 68.76  ? 45  ASN C CG  1 
ATOM   4638  O OD1 . ASN C  1 45  ? 22.060  23.262 -9.964  1.00 58.50  ? 45  ASN C OD1 1 
ATOM   4639  N ND2 . ASN C  1 45  ? 19.894  23.474 -9.433  1.00 75.30  ? 45  ASN C ND2 1 
ATOM   4640  N N   . GLU C  1 46  ? 21.418  22.167 -15.060 1.00 57.95  ? 46  GLU C N   1 
ATOM   4641  C CA  . GLU C  1 46  ? 21.474  21.331 -16.289 1.00 59.39  ? 46  GLU C CA  1 
ATOM   4642  C C   . GLU C  1 46  ? 22.922  20.890 -16.521 1.00 58.77  ? 46  GLU C C   1 
ATOM   4643  O O   . GLU C  1 46  ? 23.185  20.234 -17.545 1.00 62.90  ? 46  GLU C O   1 
ATOM   4644  C CB  . GLU C  1 46  ? 20.976  22.113 -17.506 1.00 60.91  ? 46  GLU C CB  1 
ATOM   4645  C CG  . GLU C  1 46  ? 19.480  22.356 -17.510 1.00 61.17  ? 46  GLU C CG  1 
ATOM   4646  C CD  . GLU C  1 46  ? 18.969  23.059 -18.756 1.00 65.02  ? 46  GLU C CD  1 
ATOM   4647  O OE1 . GLU C  1 46  ? 17.738  23.207 -18.885 1.00 68.83  ? 46  GLU C OE1 1 
ATOM   4648  O OE2 . GLU C  1 46  ? 19.802  23.456 -19.595 1.00 65.49  ? 46  GLU C OE2 1 
ATOM   4649  N N   . VAL C  1 47  ? 23.820  21.254 -15.603 1.00 58.01  ? 47  VAL C N   1 
ATOM   4650  C CA  . VAL C  1 47  ? 25.296  21.093 -15.750 1.00 60.99  ? 47  VAL C CA  1 
ATOM   4651  C C   . VAL C  1 47  ? 25.854  20.420 -14.491 1.00 62.07  ? 47  VAL C C   1 
ATOM   4652  O O   . VAL C  1 47  ? 25.441  20.805 -13.379 1.00 64.36  ? 47  VAL C O   1 
ATOM   4653  C CB  . VAL C  1 47  ? 25.966  22.455 -16.015 1.00 62.80  ? 47  VAL C CB  1 
ATOM   4654  C CG1 . VAL C  1 47  ? 27.464  22.417 -15.763 1.00 67.74  ? 47  VAL C CG1 1 
ATOM   4655  C CG2 . VAL C  1 47  ? 25.668  22.957 -17.419 1.00 56.80  ? 47  VAL C CG2 1 
ATOM   4656  N N   . GLY C  1 48  ? 26.753  19.448 -14.674 1.00 60.30  ? 48  GLY C N   1 
ATOM   4657  C CA  . GLY C  1 48  ? 27.425  18.711 -13.586 1.00 62.27  ? 48  GLY C CA  1 
ATOM   4658  C C   . GLY C  1 48  ? 28.306  19.631 -12.763 1.00 60.06  ? 48  GLY C C   1 
ATOM   4659  O O   . GLY C  1 48  ? 28.756  20.658 -13.306 1.00 57.33  ? 48  GLY C O   1 
ATOM   4660  N N   . SER C  1 49  ? 28.541  19.280 -11.496 1.00 60.04  ? 49  SER C N   1 
ATOM   4661  C CA  . SER C  1 49  ? 29.344  20.076 -10.532 1.00 62.31  ? 49  SER C CA  1 
ATOM   4662  C C   . SER C  1 49  ? 30.724  20.370 -11.132 1.00 59.56  ? 49  SER C C   1 
ATOM   4663  O O   . SER C  1 49  ? 31.351  21.358 -10.708 1.00 59.30  ? 49  SER C O   1 
ATOM   4664  C CB  . SER C  1 49  ? 29.466  19.366 -9.211  1.00 64.53  ? 49  SER C CB  1 
ATOM   4665  O OG  . SER C  1 49  ? 30.098  18.105 -9.372  1.00 62.01  ? 49  SER C OG  1 
ATOM   4666  N N   . ARG C  1 50  ? 31.168  19.544 -12.083 1.00 66.95  ? 50  ARG C N   1 
ATOM   4667  C CA  . ARG C  1 50  ? 32.523  19.622 -12.694 1.00 68.75  ? 50  ARG C CA  1 
ATOM   4668  C C   . ARG C  1 50  ? 32.648  20.888 -13.550 1.00 60.40  ? 50  ARG C C   1 
ATOM   4669  O O   . ARG C  1 50  ? 33.761  21.441 -13.618 1.00 59.08  ? 50  ARG C O   1 
ATOM   4670  C CB  . ARG C  1 50  ? 32.811  18.386 -13.550 1.00 75.49  ? 50  ARG C CB  1 
ATOM   4671  C CG  . ARG C  1 50  ? 34.188  18.402 -14.197 1.00 79.52  ? 50  ARG C CG  1 
ATOM   4672  C CD  . ARG C  1 50  ? 34.444  17.188 -15.068 1.00 91.52  ? 50  ARG C CD  1 
ATOM   4673  N NE  . ARG C  1 50  ? 35.803  17.177 -15.589 1.00 96.78  ? 50  ARG C NE  1 
ATOM   4674  C CZ  . ARG C  1 50  ? 36.274  16.277 -16.444 1.00 90.26  ? 50  ARG C CZ  1 
ATOM   4675  N NH1 . ARG C  1 50  ? 35.490  15.306 -16.882 1.00 82.40  ? 50  ARG C NH1 1 
ATOM   4676  N NH2 . ARG C  1 50  ? 37.525  16.356 -16.861 1.00 96.01  ? 50  ARG C NH2 1 
ATOM   4677  N N   . TYR C  1 51  ? 31.554  21.318 -14.185 1.00 59.28  ? 51  TYR C N   1 
ATOM   4678  C CA  . TYR C  1 51  ? 31.533  22.433 -15.168 1.00 62.46  ? 51  TYR C CA  1 
ATOM   4679  C C   . TYR C  1 51  ? 30.726  23.612 -14.614 1.00 59.23  ? 51  TYR C C   1 
ATOM   4680  O O   . TYR C  1 51  ? 30.280  24.458 -15.410 1.00 55.04  ? 51  TYR C O   1 
ATOM   4681  C CB  . TYR C  1 51  ? 30.964  21.945 -16.503 1.00 64.93  ? 51  TYR C CB  1 
ATOM   4682  C CG  . TYR C  1 51  ? 31.671  20.741 -17.069 1.00 73.46  ? 51  TYR C CG  1 
ATOM   4683  C CD1 . TYR C  1 51  ? 32.937  20.853 -17.619 1.00 78.80  ? 51  TYR C CD1 1 
ATOM   4684  C CD2 . TYR C  1 51  ? 31.084  19.486 -17.044 1.00 77.37  ? 51  TYR C CD2 1 
ATOM   4685  C CE1 . TYR C  1 51  ? 33.602  19.752 -18.134 1.00 77.56  ? 51  TYR C CE1 1 
ATOM   4686  C CE2 . TYR C  1 51  ? 31.734  18.376 -17.557 1.00 81.47  ? 51  TYR C CE2 1 
ATOM   4687  C CZ  . TYR C  1 51  ? 32.998  18.509 -18.104 1.00 79.56  ? 51  TYR C CZ  1 
ATOM   4688  O OH  . TYR C  1 51  ? 33.644  17.420 -18.612 1.00 85.38  ? 51  TYR C OH  1 
ATOM   4689  N N   . ARG C  1 52  ? 30.558  23.675 -13.291 1.00 58.82  ? 52  ARG C N   1 
ATOM   4690  C CA  . ARG C  1 52  ? 29.739  24.717 -12.616 1.00 57.39  ? 52  ARG C CA  1 
ATOM   4691  C C   . ARG C  1 52  ? 30.446  26.075 -12.702 1.00 59.00  ? 52  ARG C C   1 
ATOM   4692  O O   . ARG C  1 52  ? 29.736  27.096 -12.723 1.00 64.27  ? 52  ARG C O   1 
ATOM   4693  C CB  . ARG C  1 52  ? 29.459  24.353 -11.157 1.00 57.44  ? 52  ARG C CB  1 
ATOM   4694  C CG  . ARG C  1 52  ? 28.487  25.308 -10.479 1.00 61.18  ? 52  ARG C CG  1 
ATOM   4695  C CD  . ARG C  1 52  ? 27.838  24.709 -9.249  1.00 66.28  ? 52  ARG C CD  1 
ATOM   4696  N NE  . ARG C  1 52  ? 27.233  23.415 -9.526  1.00 69.39  ? 52  ARG C NE  1 
ATOM   4697  C CZ  . ARG C  1 52  ? 27.091  22.446 -8.629  1.00 77.75  ? 52  ARG C CZ  1 
ATOM   4698  N NH1 . ARG C  1 52  ? 27.506  22.628 -7.387  1.00 74.69  ? 52  ARG C NH1 1 
ATOM   4699  N NH2 . ARG C  1 52  ? 26.525  21.304 -8.973  1.00 87.87  ? 52  ARG C NH2 1 
ATOM   4700  N N   . THR C  1 53  ? 31.782  26.092 -12.746 1.00 58.66  ? 53  THR C N   1 
ATOM   4701  C CA  . THR C  1 53  ? 32.588  27.341 -12.851 1.00 55.75  ? 53  THR C CA  1 
ATOM   4702  C C   . THR C  1 53  ? 32.165  28.101 -14.112 1.00 54.18  ? 53  THR C C   1 
ATOM   4703  O O   . THR C  1 53  ? 32.218  29.344 -14.096 1.00 48.18  ? 53  THR C O   1 
ATOM   4704  C CB  . THR C  1 53  ? 34.097  27.069 -12.867 1.00 58.46  ? 53  THR C CB  1 
ATOM   4705  O OG1 . THR C  1 53  ? 34.400  26.111 -11.853 1.00 70.72  ? 53  THR C OG1 1 
ATOM   4706  C CG2 . THR C  1 53  ? 34.909  28.327 -12.644 1.00 57.70  ? 53  THR C CG2 1 
ATOM   4707  N N   . ALA C  1 54  ? 31.762  27.371 -15.158 1.00 56.61  ? 54  ALA C N   1 
ATOM   4708  C CA  . ALA C  1 54  ? 31.253  27.921 -16.436 1.00 54.67  ? 54  ALA C CA  1 
ATOM   4709  C C   . ALA C  1 54  ? 29.975  28.717 -16.165 1.00 53.27  ? 54  ALA C C   1 
ATOM   4710  O O   . ALA C  1 54  ? 29.809  29.793 -16.763 1.00 62.38  ? 54  ALA C O   1 
ATOM   4711  C CB  . ALA C  1 54  ? 30.999  26.805 -17.419 1.00 57.63  ? 54  ALA C CB  1 
ATOM   4712  N N   . VAL C  1 55  ? 29.119  28.193 -15.284 1.00 49.96  ? 55  VAL C N   1 
ATOM   4713  C CA  . VAL C  1 55  ? 27.779  28.757 -14.949 1.00 47.01  ? 55  VAL C CA  1 
ATOM   4714  C C   . VAL C  1 55  ? 27.961  29.994 -14.062 1.00 43.89  ? 55  VAL C C   1 
ATOM   4715  O O   . VAL C  1 55  ? 27.411  31.052 -14.412 1.00 44.48  ? 55  VAL C O   1 
ATOM   4716  C CB  . VAL C  1 55  ? 26.894  27.696 -14.269 1.00 47.35  ? 55  VAL C CB  1 
ATOM   4717  C CG1 . VAL C  1 55  ? 25.552  28.268 -13.843 1.00 46.52  ? 55  VAL C CG1 1 
ATOM   4718  C CG2 . VAL C  1 55  ? 26.704  26.474 -15.155 1.00 52.43  ? 55  VAL C CG2 1 
ATOM   4719  N N   . SER C  1 56  ? 28.699  29.863 -12.956 1.00 42.14  ? 56  SER C N   1 
ATOM   4720  C CA  . SER C  1 56  ? 28.942  30.953 -11.975 1.00 43.01  ? 56  SER C CA  1 
ATOM   4721  C C   . SER C  1 56  ? 29.575  32.156 -12.686 1.00 44.13  ? 56  SER C C   1 
ATOM   4722  O O   . SER C  1 56  ? 29.211  33.300 -12.353 1.00 46.47  ? 56  SER C O   1 
ATOM   4723  C CB  . SER C  1 56  ? 29.787  30.477 -10.822 1.00 40.71  ? 56  SER C CB  1 
ATOM   4724  O OG  . SER C  1 56  ? 31.025  29.959 -11.280 1.00 44.63  ? 56  SER C OG  1 
ATOM   4725  N N   . ALA C  1 57  ? 30.479  31.904 -13.637 1.00 42.07  ? 57  ALA C N   1 
ATOM   4726  C CA  . ALA C  1 57  ? 31.148  32.937 -14.463 1.00 39.29  ? 57  ALA C CA  1 
ATOM   4727  C C   . ALA C  1 57  ? 30.114  33.622 -15.363 1.00 40.94  ? 57  ALA C C   1 
ATOM   4728  O O   . ALA C  1 57  ? 30.073  34.866 -15.371 1.00 39.66  ? 57  ALA C O   1 
ATOM   4729  C CB  . ALA C  1 57  ? 32.255  32.316 -15.278 1.00 39.04  ? 57  ALA C CB  1 
ATOM   4730  N N   . ARG C  1 58  ? 29.316  32.833 -16.091 1.00 42.71  ? 58  ARG C N   1 
ATOM   4731  C CA  . ARG C  1 58  ? 28.279  33.333 -17.034 1.00 43.38  ? 58  ARG C CA  1 
ATOM   4732  C C   . ARG C  1 58  ? 27.294  34.222 -16.266 1.00 41.48  ? 58  ARG C C   1 
ATOM   4733  O O   . ARG C  1 58  ? 27.043  35.355 -16.720 1.00 42.04  ? 58  ARG C O   1 
ATOM   4734  C CB  . ARG C  1 58  ? 27.556  32.169 -17.721 1.00 45.89  ? 58  ARG C CB  1 
ATOM   4735  C CG  . ARG C  1 58  ? 26.522  32.606 -18.750 1.00 55.00  ? 58  ARG C CG  1 
ATOM   4736  C CD  . ARG C  1 58  ? 26.084  31.496 -19.690 1.00 68.53  ? 58  ARG C CD  1 
ATOM   4737  N NE  . ARG C  1 58  ? 24.880  31.874 -20.420 1.00 86.45  ? 58  ARG C NE  1 
ATOM   4738  C CZ  . ARG C  1 58  ? 23.834  31.080 -20.631 1.00 93.99  ? 58  ARG C CZ  1 
ATOM   4739  N NH1 . ARG C  1 58  ? 23.826  29.845 -20.159 1.00 96.84  ? 58  ARG C NH1 1 
ATOM   4740  N NH2 . ARG C  1 58  ? 22.792  31.529 -21.309 1.00 91.76  ? 58  ARG C NH2 1 
ATOM   4741  N N   . LEU C  1 59  ? 26.767  33.725 -15.144 1.00 40.92  ? 59  LEU C N   1 
ATOM   4742  C CA  . LEU C  1 59  ? 25.789  34.453 -14.295 1.00 41.89  ? 59  LEU C CA  1 
ATOM   4743  C C   . LEU C  1 59  ? 26.468  35.697 -13.712 1.00 46.42  ? 59  LEU C C   1 
ATOM   4744  O O   . LEU C  1 59  ? 25.848  36.780 -13.735 1.00 46.97  ? 59  LEU C O   1 
ATOM   4745  C CB  . LEU C  1 59  ? 25.280  33.523 -13.190 1.00 43.20  ? 59  LEU C CB  1 
ATOM   4746  C CG  . LEU C  1 59  ? 23.927  33.911 -12.597 1.00 48.01  ? 59  LEU C CG  1 
ATOM   4747  C CD1 . LEU C  1 59  ? 22.876  34.025 -13.689 1.00 52.69  ? 59  LEU C CD1 1 
ATOM   4748  C CD2 . LEU C  1 59  ? 23.484  32.916 -11.537 1.00 48.66  ? 59  LEU C CD2 1 
ATOM   4749  N N   . GLY C  1 60  ? 27.700  35.540 -13.220 1.00 43.84  ? 60  GLY C N   1 
ATOM   4750  C CA  . GLY C  1 60  ? 28.534  36.647 -12.716 1.00 41.39  ? 60  GLY C CA  1 
ATOM   4751  C C   . GLY C  1 60  ? 28.640  37.768 -13.734 1.00 41.44  ? 60  GLY C C   1 
ATOM   4752  O O   . GLY C  1 60  ? 28.392  38.926 -13.356 1.00 40.69  ? 60  GLY C O   1 
ATOM   4753  N N   . MET C  1 61  ? 28.977  37.434 -14.986 1.00 49.17  ? 61  MET C N   1 
ATOM   4754  C CA  . MET C  1 61  ? 29.237  38.420 -16.070 1.00 52.09  ? 61  MET C CA  1 
ATOM   4755  C C   . MET C  1 61  ? 27.922  39.097 -16.476 1.00 50.98  ? 61  MET C C   1 
ATOM   4756  O O   . MET C  1 61  ? 27.941  40.321 -16.710 1.00 51.53  ? 61  MET C O   1 
ATOM   4757  C CB  . MET C  1 61  ? 29.873  37.763 -17.299 1.00 53.51  ? 61  MET C CB  1 
ATOM   4758  C CG  . MET C  1 61  ? 28.903  36.948 -18.128 1.00 68.32  ? 61  MET C CG  1 
ATOM   4759  S SD  . MET C  1 61  ? 28.977  37.400 -19.880 1.00 80.46  ? 61  MET C SD  1 
ATOM   4760  C CE  . MET C  1 61  ? 28.213  39.019 -19.826 1.00 75.10  ? 61  MET C CE  1 
ATOM   4761  N N   . LEU C  1 62  ? 26.826  38.336 -16.558 1.00 43.02  ? 62  LEU C N   1 
ATOM   4762  C CA  . LEU C  1 62  ? 25.490  38.862 -16.943 1.00 41.59  ? 62  LEU C CA  1 
ATOM   4763  C C   . LEU C  1 62  ? 25.004  39.830 -15.859 1.00 39.72  ? 62  LEU C C   1 
ATOM   4764  O O   . LEU C  1 62  ? 24.469  40.896 -16.221 1.00 38.65  ? 62  LEU C O   1 
ATOM   4765  C CB  . LEU C  1 62  ? 24.521  37.693 -17.144 1.00 44.11  ? 62  LEU C CB  1 
ATOM   4766  C CG  . LEU C  1 62  ? 24.760  36.860 -18.403 1.00 49.03  ? 62  LEU C CG  1 
ATOM   4767  C CD1 . LEU C  1 62  ? 23.837  35.650 -18.443 1.00 50.41  ? 62  LEU C CD1 1 
ATOM   4768  C CD2 . LEU C  1 62  ? 24.584  37.705 -19.657 1.00 47.84  ? 62  LEU C CD2 1 
ATOM   4769  N N   . GLY C  1 63  ? 25.204  39.473 -14.586 1.00 40.59  ? 63  GLY C N   1 
ATOM   4770  C CA  . GLY C  1 63  ? 24.903  40.337 -13.427 1.00 38.55  ? 63  GLY C CA  1 
ATOM   4771  C C   . GLY C  1 63  ? 25.648  41.658 -13.521 1.00 36.54  ? 63  GLY C C   1 
ATOM   4772  O O   . GLY C  1 63  ? 25.010  42.718 -13.380 1.00 32.32  ? 63  GLY C O   1 
ATOM   4773  N N   . VAL C  1 64  ? 26.957  41.595 -13.767 1.00 37.92  ? 64  VAL C N   1 
ATOM   4774  C CA  . VAL C  1 64  ? 27.853  42.778 -13.931 1.00 43.60  ? 64  VAL C CA  1 
ATOM   4775  C C   . VAL C  1 64  ? 27.338  43.632 -15.098 1.00 43.87  ? 64  VAL C C   1 
ATOM   4776  O O   . VAL C  1 64  ? 27.062  44.829 -14.880 1.00 40.85  ? 64  VAL C O   1 
ATOM   4777  C CB  . VAL C  1 64  ? 29.311  42.330 -14.150 1.00 44.99  ? 64  VAL C CB  1 
ATOM   4778  C CG1 . VAL C  1 64  ? 30.188  43.465 -14.654 1.00 47.45  ? 64  VAL C CG1 1 
ATOM   4779  C CG2 . VAL C  1 64  ? 29.897  41.710 -12.892 1.00 45.47  ? 64  VAL C CG2 1 
ATOM   4780  N N   . ALA C  1 65  ? 27.222  43.033 -16.287 1.00 43.37  ? 65  ALA C N   1 
ATOM   4781  C CA  . ALA C  1 65  ? 26.759  43.686 -17.533 1.00 42.27  ? 65  ALA C CA  1 
ATOM   4782  C C   . ALA C  1 65  ? 25.464  44.451 -17.250 1.00 41.78  ? 65  ALA C C   1 
ATOM   4783  O O   . ALA C  1 65  ? 25.411  45.665 -17.527 1.00 46.70  ? 65  ALA C O   1 
ATOM   4784  C CB  . ALA C  1 65  ? 26.558  42.649 -18.609 1.00 42.73  ? 65  ALA C CB  1 
ATOM   4785  N N   . LEU C  1 66  ? 24.463  43.747 -16.718 1.00 40.82  ? 66  LEU C N   1 
ATOM   4786  C CA  . LEU C  1 66  ? 23.148  44.302 -16.304 1.00 44.90  ? 66  LEU C CA  1 
ATOM   4787  C C   . LEU C  1 66  ? 23.362  45.618 -15.541 1.00 44.92  ? 66  LEU C C   1 
ATOM   4788  O O   . LEU C  1 66  ? 22.870  46.661 -16.011 1.00 50.13  ? 66  LEU C O   1 
ATOM   4789  C CB  . LEU C  1 66  ? 22.454  43.251 -15.432 1.00 47.53  ? 66  LEU C CB  1 
ATOM   4790  C CG  . LEU C  1 66  ? 20.956  43.434 -15.203 1.00 49.69  ? 66  LEU C CG  1 
ATOM   4791  C CD1 . LEU C  1 66  ? 20.439  42.383 -14.233 1.00 50.91  ? 66  LEU C CD1 1 
ATOM   4792  C CD2 . LEU C  1 66  ? 20.645  44.830 -14.689 1.00 50.29  ? 66  LEU C CD2 1 
ATOM   4793  N N   . LEU C  1 67  ? 24.073  45.564 -14.411 1.00 43.57  ? 67  LEU C N   1 
ATOM   4794  C CA  . LEU C  1 67  ? 24.276  46.709 -13.482 1.00 43.22  ? 67  LEU C CA  1 
ATOM   4795  C C   . LEU C  1 67  ? 25.077  47.809 -14.185 1.00 41.33  ? 67  LEU C C   1 
ATOM   4796  O O   . LEU C  1 67  ? 24.669  48.987 -14.105 1.00 39.20  ? 67  LEU C O   1 
ATOM   4797  C CB  . LEU C  1 67  ? 25.000  46.208 -12.229 1.00 45.65  ? 67  LEU C CB  1 
ATOM   4798  C CG  . LEU C  1 67  ? 24.208  45.221 -11.374 1.00 46.86  ? 67  LEU C CG  1 
ATOM   4799  C CD1 . LEU C  1 67  ? 25.036  44.737 -10.195 1.00 52.54  ? 67  LEU C CD1 1 
ATOM   4800  C CD2 . LEU C  1 67  ? 22.908  45.846 -10.892 1.00 46.60  ? 67  LEU C CD2 1 
ATOM   4801  N N   . ALA C  1 68  ? 26.179  47.436 -14.840 1.00 41.59  ? 68  ALA C N   1 
ATOM   4802  C CA  . ALA C  1 68  ? 27.043  48.357 -15.612 1.00 38.99  ? 68  ALA C CA  1 
ATOM   4803  C C   . ALA C  1 68  ? 26.164  49.202 -16.538 1.00 39.74  ? 68  ALA C C   1 
ATOM   4804  O O   . ALA C  1 68  ? 26.320  50.440 -16.540 1.00 44.65  ? 68  ALA C O   1 
ATOM   4805  C CB  . ALA C  1 68  ? 28.074  47.577 -16.388 1.00 38.03  ? 68  ALA C CB  1 
ATOM   4806  N N   . TYR C  1 69  ? 25.258  48.552 -17.274 1.00 38.64  ? 69  TYR C N   1 
ATOM   4807  C CA  . TYR C  1 69  ? 24.406  49.189 -18.312 1.00 41.17  ? 69  TYR C CA  1 
ATOM   4808  C C   . TYR C  1 69  ? 23.413  50.152 -17.656 1.00 39.25  ? 69  TYR C C   1 
ATOM   4809  O O   . TYR C  1 69  ? 23.083  51.176 -18.283 1.00 46.88  ? 69  TYR C O   1 
ATOM   4810  C CB  . TYR C  1 69  ? 23.734  48.135 -19.195 1.00 41.65  ? 69  TYR C CB  1 
ATOM   4811  C CG  . TYR C  1 69  ? 24.470  47.936 -20.494 1.00 44.63  ? 69  TYR C CG  1 
ATOM   4812  C CD1 . TYR C  1 69  ? 24.048  48.560 -21.656 1.00 44.41  ? 69  TYR C CD1 1 
ATOM   4813  C CD2 . TYR C  1 69  ? 25.638  47.194 -20.544 1.00 47.54  ? 69  TYR C CD2 1 
ATOM   4814  C CE1 . TYR C  1 69  ? 24.743  48.416 -22.845 1.00 46.84  ? 69  TYR C CE1 1 
ATOM   4815  C CE2 . TYR C  1 69  ? 26.342  47.036 -21.726 1.00 46.99  ? 69  TYR C CE2 1 
ATOM   4816  C CZ  . TYR C  1 69  ? 25.895  47.652 -22.880 1.00 45.73  ? 69  TYR C CZ  1 
ATOM   4817  O OH  . TYR C  1 69  ? 26.584  47.501 -24.046 1.00 44.28  ? 69  TYR C OH  1 
ATOM   4818  N N   . ILE C  1 70  ? 22.970  49.854 -16.434 1.00 37.43  ? 70  ILE C N   1 
ATOM   4819  C CA  . ILE C  1 70  ? 22.109  50.777 -15.638 1.00 36.96  ? 70  ILE C CA  1 
ATOM   4820  C C   . ILE C  1 70  ? 22.880  52.083 -15.426 1.00 36.61  ? 70  ILE C C   1 
ATOM   4821  O O   . ILE C  1 70  ? 22.286  53.159 -15.629 1.00 36.39  ? 70  ILE C O   1 
ATOM   4822  C CB  . ILE C  1 70  ? 21.669  50.138 -14.308 1.00 36.39  ? 70  ILE C CB  1 
ATOM   4823  C CG1 . ILE C  1 70  ? 20.717  48.964 -14.541 1.00 35.93  ? 70  ILE C CG1 1 
ATOM   4824  C CG2 . ILE C  1 70  ? 21.060  51.187 -13.389 1.00 36.28  ? 70  ILE C CG2 1 
ATOM   4825  C CD1 . ILE C  1 70  ? 20.253  48.288 -13.272 1.00 37.80  ? 70  ILE C CD1 1 
ATOM   4826  N N   . LEU C  1 71  ? 24.159  51.989 -15.051 1.00 37.65  ? 71  LEU C N   1 
ATOM   4827  C CA  . LEU C  1 71  ? 25.044  53.167 -14.848 1.00 45.38  ? 71  LEU C CA  1 
ATOM   4828  C C   . LEU C  1 71  ? 25.177  53.932 -16.169 1.00 46.12  ? 71  LEU C C   1 
ATOM   4829  O O   . LEU C  1 71  ? 24.977  55.163 -16.160 1.00 48.99  ? 71  LEU C O   1 
ATOM   4830  C CB  . LEU C  1 71  ? 26.409  52.703 -14.334 1.00 50.61  ? 71  LEU C CB  1 
ATOM   4831  C CG  . LEU C  1 71  ? 26.435  52.187 -12.896 1.00 56.49  ? 71  LEU C CG  1 
ATOM   4832  C CD1 . LEU C  1 71  ? 27.853  52.210 -12.344 1.00 57.03  ? 71  LEU C CD1 1 
ATOM   4833  C CD2 . LEU C  1 71  ? 25.512  53.004 -12.002 1.00 60.32  ? 71  LEU C CD2 1 
ATOM   4834  N N   . ILE C  1 72  ? 25.495  53.226 -17.258 1.00 47.52  ? 72  ILE C N   1 
ATOM   4835  C CA  . ILE C  1 72  ? 25.661  53.819 -18.619 1.00 46.19  ? 72  ILE C CA  1 
ATOM   4836  C C   . ILE C  1 72  ? 24.390  54.600 -18.967 1.00 44.59  ? 72  ILE C C   1 
ATOM   4837  O O   . ILE C  1 72  ? 24.511  55.757 -19.428 1.00 40.37  ? 72  ILE C O   1 
ATOM   4838  C CB  . ILE C  1 72  ? 25.970  52.736 -19.671 1.00 46.44  ? 72  ILE C CB  1 
ATOM   4839  C CG1 . ILE C  1 72  ? 27.287  52.017 -19.368 1.00 53.11  ? 72  ILE C CG1 1 
ATOM   4840  C CG2 . ILE C  1 72  ? 25.963  53.337 -21.068 1.00 45.23  ? 72  ILE C CG2 1 
ATOM   4841  C CD1 . ILE C  1 72  ? 27.587  50.864 -20.297 1.00 57.88  ? 72  ILE C CD1 1 
ATOM   4842  N N   . ILE C  1 73  ? 23.224  53.984 -18.748 1.00 38.96  ? 73  ILE C N   1 
ATOM   4843  C CA  . ILE C  1 73  ? 21.887  54.596 -19.010 1.00 42.07  ? 73  ILE C CA  1 
ATOM   4844  C C   . ILE C  1 73  ? 21.779  55.891 -18.198 1.00 45.38  ? 73  ILE C C   1 
ATOM   4845  O O   . ILE C  1 73  ? 21.428  56.934 -18.793 1.00 47.25  ? 73  ILE C O   1 
ATOM   4846  C CB  . ILE C  1 73  ? 20.749  53.607 -18.684 1.00 38.44  ? 73  ILE C CB  1 
ATOM   4847  C CG1 . ILE C  1 73  ? 20.752  52.416 -19.646 1.00 40.31  ? 73  ILE C CG1 1 
ATOM   4848  C CG2 . ILE C  1 73  ? 19.401  54.315 -18.669 1.00 35.84  ? 73  ILE C CG2 1 
ATOM   4849  C CD1 . ILE C  1 73  ? 19.869  51.268 -19.208 1.00 38.40  ? 73  ILE C CD1 1 
ATOM   4850  N N   . VAL C  1 74  ? 22.085  55.825 -16.898 1.00 43.59  ? 74  VAL C N   1 
ATOM   4851  C CA  . VAL C  1 74  ? 22.000  56.988 -15.967 1.00 46.43  ? 74  VAL C CA  1 
ATOM   4852  C C   . VAL C  1 74  ? 22.936  58.086 -16.480 1.00 50.33  ? 74  VAL C C   1 
ATOM   4853  O O   . VAL C  1 74  ? 22.488  59.243 -16.577 1.00 54.14  ? 74  VAL C O   1 
ATOM   4854  C CB  . VAL C  1 74  ? 22.336  56.598 -14.515 1.00 46.99  ? 74  VAL C CB  1 
ATOM   4855  C CG1 . VAL C  1 74  ? 22.452  57.828 -13.628 1.00 50.49  ? 74  VAL C CG1 1 
ATOM   4856  C CG2 . VAL C  1 74  ? 21.319  55.626 -13.940 1.00 48.02  ? 74  VAL C CG2 1 
ATOM   4857  N N   . ALA C  1 75  ? 24.182  57.728 -16.804 1.00 49.68  ? 75  ALA C N   1 
ATOM   4858  C CA  . ALA C  1 75  ? 25.220  58.657 -17.309 1.00 46.35  ? 75  ALA C CA  1 
ATOM   4859  C C   . ALA C  1 75  ? 24.702  59.366 -18.564 1.00 42.74  ? 75  ALA C C   1 
ATOM   4860  O O   . ALA C  1 75  ? 24.900  60.592 -18.665 1.00 46.32  ? 75  ALA C O   1 
ATOM   4861  C CB  . ALA C  1 75  ? 26.504  57.916 -17.585 1.00 45.29  ? 75  ALA C CB  1 
ATOM   4862  N N   . PHE C  1 76  ? 24.063  58.620 -19.471 1.00 43.86  ? 76  PHE C N   1 
ATOM   4863  C CA  . PHE C  1 76  ? 23.512  59.137 -20.751 1.00 43.28  ? 76  PHE C CA  1 
ATOM   4864  C C   . PHE C  1 76  ? 22.425  60.173 -20.447 1.00 42.76  ? 76  PHE C C   1 
ATOM   4865  O O   . PHE C  1 76  ? 22.432  61.249 -21.077 1.00 48.93  ? 76  PHE C O   1 
ATOM   4866  C CB  . PHE C  1 76  ? 22.989  57.992 -21.621 1.00 43.27  ? 76  PHE C CB  1 
ATOM   4867  C CG  . PHE C  1 76  ? 22.218  58.425 -22.843 1.00 46.60  ? 76  PHE C CG  1 
ATOM   4868  C CD1 . PHE C  1 76  ? 20.832  58.422 -22.841 1.00 48.72  ? 76  PHE C CD1 1 
ATOM   4869  C CD2 . PHE C  1 76  ? 22.876  58.831 -23.994 1.00 48.01  ? 76  PHE C CD2 1 
ATOM   4870  C CE1 . PHE C  1 76  ? 20.119  58.826 -23.957 1.00 49.14  ? 76  PHE C CE1 1 
ATOM   4871  C CE2 . PHE C  1 76  ? 22.160  59.221 -25.115 1.00 50.99  ? 76  PHE C CE2 1 
ATOM   4872  C CZ  . PHE C  1 76  ? 20.785  59.216 -25.093 1.00 53.03  ? 76  PHE C CZ  1 
ATOM   4873  N N   . LEU C  1 77  ? 21.535  59.865 -19.499 1.00 42.98  ? 77  LEU C N   1 
ATOM   4874  C CA  . LEU C  1 77  ? 20.375  60.724 -19.132 1.00 46.58  ? 77  LEU C CA  1 
ATOM   4875  C C   . LEU C  1 77  ? 20.870  62.030 -18.499 1.00 49.07  ? 77  LEU C C   1 
ATOM   4876  O O   . LEU C  1 77  ? 20.178  63.056 -18.653 1.00 49.31  ? 77  LEU C O   1 
ATOM   4877  C CB  . LEU C  1 77  ? 19.463  59.967 -18.162 1.00 47.18  ? 77  LEU C CB  1 
ATOM   4878  C CG  . LEU C  1 77  ? 18.832  58.688 -18.708 1.00 53.81  ? 77  LEU C CG  1 
ATOM   4879  C CD1 . LEU C  1 77  ? 17.946  58.031 -17.662 1.00 54.14  ? 77  LEU C CD1 1 
ATOM   4880  C CD2 . LEU C  1 77  ? 18.045  58.971 -19.977 1.00 54.27  ? 77  LEU C CD2 1 
ATOM   4881  N N   . LEU C  1 78  ? 22.014  61.989 -17.805 1.00 53.95  ? 78  LEU C N   1 
ATOM   4882  C CA  . LEU C  1 78  ? 22.578  63.152 -17.066 1.00 54.38  ? 78  LEU C CA  1 
ATOM   4883  C C   . LEU C  1 78  ? 23.753  63.750 -17.849 1.00 57.25  ? 78  LEU C C   1 
ATOM   4884  O O   . LEU C  1 78  ? 24.365  64.713 -17.343 1.00 64.57  ? 78  LEU C O   1 
ATOM   4885  C CB  . LEU C  1 78  ? 23.034  62.705 -15.673 1.00 50.18  ? 78  LEU C CB  1 
ATOM   4886  C CG  . LEU C  1 78  ? 21.980  61.995 -14.825 1.00 57.01  ? 78  LEU C CG  1 
ATOM   4887  C CD1 . LEU C  1 78  ? 22.553  61.589 -13.477 1.00 59.30  ? 78  LEU C CD1 1 
ATOM   4888  C CD2 . LEU C  1 78  ? 20.744  62.863 -14.647 1.00 56.49  ? 78  LEU C CD2 1 
ATOM   4889  N N   . GLY C  1 79  ? 24.055  63.210 -19.033 1.00 56.64  ? 79  GLY C N   1 
ATOM   4890  C CA  . GLY C  1 79  ? 25.253  63.572 -19.816 1.00 57.83  ? 79  GLY C CA  1 
ATOM   4891  C C   . GLY C  1 79  ? 24.953  64.591 -20.903 1.00 59.21  ? 79  GLY C C   1 
ATOM   4892  O O   . GLY C  1 79  ? 25.916  65.194 -21.426 1.00 53.26  ? 79  GLY C O   1 
ATOM   4893  N N   . TYR C  1 80  ? 23.676  64.785 -21.244 1.00 60.75  ? 80  TYR C N   1 
ATOM   4894  C CA  . TYR C  1 80  ? 23.228  65.682 -22.341 1.00 60.65  ? 80  TYR C CA  1 
ATOM   4895  C C   . TYR C  1 80  ? 22.074  66.561 -21.855 1.00 60.66  ? 80  TYR C C   1 
ATOM   4896  O O   . TYR C  1 80  ? 21.276  66.098 -21.014 1.00 52.25  ? 80  TYR C O   1 
ATOM   4897  C CB  . TYR C  1 80  ? 22.821  64.860 -23.568 1.00 56.76  ? 80  TYR C CB  1 
ATOM   4898  C CG  . TYR C  1 80  ? 23.978  64.251 -24.318 1.00 52.00  ? 80  TYR C CG  1 
ATOM   4899  C CD1 . TYR C  1 80  ? 24.635  64.950 -25.317 1.00 49.67  ? 80  TYR C CD1 1 
ATOM   4900  C CD2 . TYR C  1 80  ? 24.425  62.975 -24.022 1.00 56.00  ? 80  TYR C CD2 1 
ATOM   4901  C CE1 . TYR C  1 80  ? 25.700  64.394 -26.007 1.00 61.01  ? 80  TYR C CE1 1 
ATOM   4902  C CE2 . TYR C  1 80  ? 25.492  62.406 -24.699 1.00 55.92  ? 80  TYR C CE2 1 
ATOM   4903  C CZ  . TYR C  1 80  ? 26.134  63.116 -25.696 1.00 60.77  ? 80  TYR C CZ  1 
ATOM   4904  O OH  . TYR C  1 80  ? 27.183  62.548 -26.363 1.00 54.24  ? 80  TYR C OH  1 
ATOM   4905  N N   . ASP C  1 81  ? 22.000  67.790 -22.378 1.00 63.94  ? 81  ASP C N   1 
ATOM   4906  C CA  . ASP C  1 81  ? 20.923  68.774 -22.088 1.00 61.35  ? 81  ASP C CA  1 
ATOM   4907  C C   . ASP C  1 81  ? 20.235  69.143 -23.405 1.00 62.78  ? 81  ASP C C   1 
ATOM   4908  O O   . ASP C  1 81  ? 20.956  69.467 -24.363 1.00 57.02  ? 81  ASP C O   1 
ATOM   4909  C CB  . ASP C  1 81  ? 21.489  70.014 -21.394 1.00 60.10  ? 81  ASP C CB  1 
ATOM   4910  C CG  . ASP C  1 81  ? 22.446  69.686 -20.260 1.00 65.99  ? 81  ASP C CG  1 
ATOM   4911  O OD1 . ASP C  1 81  ? 22.230  68.660 -19.588 1.00 78.74  ? 81  ASP C OD1 1 
ATOM   4912  O OD2 . ASP C  1 81  ? 23.406  70.453 -20.066 1.00 77.92  ? 81  ASP C OD2 1 
ATOM   4913  N N   . SER C  1 82  ? 18.900  69.086 -23.456 1.00 66.55  ? 82  SER C N   1 
ATOM   4914  C CA  . SER C  1 82  ? 18.096  69.473 -24.646 1.00 69.28  ? 82  SER C CA  1 
ATOM   4915  C C   . SER C  1 82  ? 18.092  71.003 -24.746 1.00 74.81  ? 82  SER C C   1 
ATOM   4916  O O   . SER C  1 82  ? 17.824  71.651 -23.713 1.00 62.78  ? 82  SER C O   1 
ATOM   4917  C CB  . SER C  1 82  ? 16.699  68.917 -24.578 1.00 64.95  ? 82  SER C CB  1 
ATOM   4918  O OG  . SER C  1 82  ? 16.026  69.102 -25.813 1.00 70.21  ? 82  SER C OG  1 
ATOM   4919  N N   . THR C  1 83  ? 18.389  71.561 -25.925 1.00 87.65  ? 83  THR C N   1 
ATOM   4920  C CA  . THR C  1 83  ? 18.587  73.025 -26.116 1.00 92.41  ? 83  THR C CA  1 
ATOM   4921  C C   . THR C  1 83  ? 17.678  73.560 -27.227 1.00 102.30 ? 83  THR C C   1 
ATOM   4922  O O   . THR C  1 83  ? 17.687  74.789 -27.446 1.00 118.82 ? 83  THR C O   1 
ATOM   4923  C CB  . THR C  1 83  ? 20.051  73.362 -26.426 1.00 91.36  ? 83  THR C CB  1 
ATOM   4924  O OG1 . THR C  1 83  ? 20.391  72.719 -27.656 1.00 75.15  ? 83  THR C OG1 1 
ATOM   4925  C CG2 . THR C  1 83  ? 20.999  72.943 -25.322 1.00 95.87  ? 83  THR C CG2 1 
ATOM   4926  N N   . ALA C  1 84  ? 16.913  72.682 -27.880 1.00 95.74  ? 84  ALA C N   1 
ATOM   4927  C CA  . ALA C  1 84  ? 16.066  73.019 -29.047 1.00 93.63  ? 84  ALA C CA  1 
ATOM   4928  C C   . ALA C  1 84  ? 16.931  73.016 -30.314 1.00 90.58  ? 84  ALA C C   1 
ATOM   4929  O O   . ALA C  1 84  ? 16.361  72.951 -31.418 1.00 88.62  ? 84  ALA C O   1 
ATOM   4930  C CB  . ALA C  1 84  ? 15.399  74.355 -28.827 1.00 88.66  ? 84  ALA C CB  1 
ATOM   4931  N N   . GLY C  1 85  ? 18.259  73.067 -30.155 1.00 82.12  ? 85  GLY C N   1 
ATOM   4932  C CA  . GLY C  1 85  ? 19.236  72.900 -31.250 1.00 74.85  ? 85  GLY C CA  1 
ATOM   4933  C C   . GLY C  1 85  ? 19.831  71.501 -31.256 1.00 77.54  ? 85  GLY C C   1 
ATOM   4934  O O   . GLY C  1 85  ? 20.826  71.280 -31.975 1.00 65.64  ? 85  GLY C O   1 
ATOM   4935  N N   . GLY C  1 86  ? 19.239  70.589 -30.478 1.00 85.26  ? 86  GLY C N   1 
ATOM   4936  C CA  . GLY C  1 86  ? 19.704  69.202 -30.294 1.00 85.46  ? 86  GLY C CA  1 
ATOM   4937  C C   . GLY C  1 86  ? 19.930  68.893 -28.824 1.00 79.86  ? 86  GLY C C   1 
ATOM   4938  O O   . GLY C  1 86  ? 19.368  69.610 -27.965 1.00 86.90  ? 86  GLY C O   1 
ATOM   4939  N N   . TRP C  1 87  ? 20.719  67.854 -28.546 1.00 71.87  ? 87  TRP C N   1 
ATOM   4940  C CA  . TRP C  1 87  ? 21.197  67.490 -27.186 1.00 63.70  ? 87  TRP C CA  1 
ATOM   4941  C C   . TRP C  1 87  ? 22.673  67.872 -27.062 1.00 63.75  ? 87  TRP C C   1 
ATOM   4942  O O   . TRP C  1 87  ? 23.504  67.215 -27.713 1.00 65.10  ? 87  TRP C O   1 
ATOM   4943  C CB  . TRP C  1 87  ? 20.964  66.000 -26.915 1.00 55.23  ? 87  TRP C CB  1 
ATOM   4944  C CG  . TRP C  1 87  ? 19.517  65.648 -26.772 1.00 51.17  ? 87  TRP C CG  1 
ATOM   4945  C CD1 . TRP C  1 87  ? 18.633  65.367 -27.773 1.00 51.07  ? 87  TRP C CD1 1 
ATOM   4946  C CD2 . TRP C  1 87  ? 18.768  65.566 -25.546 1.00 50.28  ? 87  TRP C CD2 1 
ATOM   4947  N NE1 . TRP C  1 87  ? 17.393  65.110 -27.255 1.00 49.61  ? 87  TRP C NE1 1 
ATOM   4948  C CE2 . TRP C  1 87  ? 17.444  65.224 -25.891 1.00 46.92  ? 87  TRP C CE2 1 
ATOM   4949  C CE3 . TRP C  1 87  ? 19.084  65.745 -24.195 1.00 51.75  ? 87  TRP C CE3 1 
ATOM   4950  C CZ2 . TRP C  1 87  ? 16.445  65.055 -24.934 1.00 45.02  ? 87  TRP C CZ2 1 
ATOM   4951  C CZ3 . TRP C  1 87  ? 18.095  65.584 -23.250 1.00 48.40  ? 87  TRP C CZ3 1 
ATOM   4952  C CH2 . TRP C  1 87  ? 16.795  65.241 -23.617 1.00 44.96  ? 87  TRP C CH2 1 
ATOM   4953  N N   . VAL C  1 88  ? 22.973  68.901 -26.263 1.00 61.83  ? 88  VAL C N   1 
ATOM   4954  C CA  . VAL C  1 88  ? 24.347  69.454 -26.085 1.00 55.49  ? 88  VAL C CA  1 
ATOM   4955  C C   . VAL C  1 88  ? 25.060  68.666 -24.992 1.00 50.90  ? 88  VAL C C   1 
ATOM   4956  O O   . VAL C  1 88  ? 24.547  68.514 -23.883 1.00 47.14  ? 88  VAL C O   1 
ATOM   4957  C CB  . VAL C  1 88  ? 24.317  70.960 -25.767 1.00 55.27  ? 88  VAL C CB  1 
ATOM   4958  C CG1 . VAL C  1 88  ? 25.676  71.474 -25.313 1.00 55.20  ? 88  VAL C CG1 1 
ATOM   4959  C CG2 . VAL C  1 88  ? 23.815  71.760 -26.958 1.00 61.22  ? 88  VAL C CG2 1 
ATOM   4960  N N   . PRO C  1 89  ? 26.271  68.146 -25.288 1.00 53.68  ? 89  PRO C N   1 
ATOM   4961  C CA  . PRO C  1 89  ? 27.057  67.417 -24.296 1.00 60.45  ? 89  PRO C CA  1 
ATOM   4962  C C   . PRO C  1 89  ? 27.363  68.318 -23.093 1.00 63.74  ? 89  PRO C C   1 
ATOM   4963  O O   . PRO C  1 89  ? 27.704  69.469 -23.303 1.00 76.91  ? 89  PRO C O   1 
ATOM   4964  C CB  . PRO C  1 89  ? 28.347  67.044 -25.043 1.00 59.33  ? 89  PRO C CB  1 
ATOM   4965  C CG  . PRO C  1 89  ? 27.977  67.133 -26.510 1.00 59.33  ? 89  PRO C CG  1 
ATOM   4966  C CD  . PRO C  1 89  ? 26.950  68.243 -26.590 1.00 58.19  ? 89  PRO C CD  1 
ATOM   4967  N N   . ASN C  1 90  ? 27.223  67.791 -21.876 1.00 65.46  ? 90  ASN C N   1 
ATOM   4968  C CA  . ASN C  1 90  ? 27.685  68.476 -20.642 1.00 64.81  ? 90  ASN C CA  1 
ATOM   4969  C C   . ASN C  1 90  ? 29.000  67.819 -20.209 1.00 75.15  ? 90  ASN C C   1 
ATOM   4970  O O   . ASN C  1 90  ? 29.515  66.971 -20.963 1.00 77.95  ? 90  ASN C O   1 
ATOM   4971  C CB  . ASN C  1 90  ? 26.613  68.500 -19.549 1.00 63.60  ? 90  ASN C CB  1 
ATOM   4972  C CG  . ASN C  1 90  ? 26.250  67.136 -19.005 1.00 72.82  ? 90  ASN C CG  1 
ATOM   4973  O OD1 . ASN C  1 90  ? 27.119  66.312 -18.719 1.00 87.91  ? 90  ASN C OD1 1 
ATOM   4974  N ND2 . ASN C  1 90  ? 24.958  66.911 -18.823 1.00 71.16  ? 90  ASN C ND2 1 
ATOM   4975  N N   . ASP C  1 91  ? 29.535  68.213 -19.054 1.00 77.97  ? 91  ASP C N   1 
ATOM   4976  C CA  . ASP C  1 91  ? 30.860  67.746 -18.568 1.00 77.18  ? 91  ASP C CA  1 
ATOM   4977  C C   . ASP C  1 91  ? 30.798  66.240 -18.289 1.00 75.51  ? 91  ASP C C   1 
ATOM   4978  O O   . ASP C  1 91  ? 31.844  65.580 -18.423 1.00 80.25  ? 91  ASP C O   1 
ATOM   4979  C CB  . ASP C  1 91  ? 31.311  68.543 -17.343 1.00 82.37  ? 91  ASP C CB  1 
ATOM   4980  C CG  . ASP C  1 91  ? 31.640  69.993 -17.653 1.00 95.02  ? 91  ASP C CG  1 
ATOM   4981  O OD1 . ASP C  1 91  ? 31.336  70.437 -18.778 1.00 103.22 ? 91  ASP C OD1 1 
ATOM   4982  O OD2 . ASP C  1 91  ? 32.208  70.665 -16.770 1.00 111.69 ? 91  ASP C OD2 1 
ATOM   4983  N N   . GLY C  1 92  ? 29.616  65.721 -17.943 1.00 71.99  ? 92  GLY C N   1 
ATOM   4984  C CA  . GLY C  1 92  ? 29.406  64.316 -17.538 1.00 68.85  ? 92  GLY C CA  1 
ATOM   4985  C C   . GLY C  1 92  ? 29.205  63.377 -18.720 1.00 62.64  ? 92  GLY C C   1 
ATOM   4986  O O   . GLY C  1 92  ? 29.045  62.165 -18.479 1.00 63.61  ? 92  GLY C O   1 
ATOM   4987  N N   . ALA C  1 93  ? 29.211  63.900 -19.951 1.00 55.27  ? 93  ALA C N   1 
ATOM   4988  C CA  . ALA C  1 93  ? 28.993  63.126 -21.198 1.00 49.83  ? 93  ALA C CA  1 
ATOM   4989  C C   . ALA C  1 93  ? 30.108  62.091 -21.364 1.00 47.55  ? 93  ALA C C   1 
ATOM   4990  O O   . ALA C  1 93  ? 29.826  61.012 -21.915 1.00 48.50  ? 93  ALA C O   1 
ATOM   4991  C CB  . ALA C  1 93  ? 28.933  64.047 -22.390 1.00 46.62  ? 93  ALA C CB  1 
ATOM   4992  N N   . ILE C  1 94  ? 31.324  62.415 -20.916 1.00 45.16  ? 94  ILE C N   1 
ATOM   4993  C CA  . ILE C  1 94  ? 32.511  61.512 -20.995 1.00 48.63  ? 94  ILE C CA  1 
ATOM   4994  C C   . ILE C  1 94  ? 32.213  60.238 -20.198 1.00 45.26  ? 94  ILE C C   1 
ATOM   4995  O O   . ILE C  1 94  ? 32.720  59.172 -20.591 1.00 47.10  ? 94  ILE C O   1 
ATOM   4996  C CB  . ILE C  1 94  ? 33.789  62.213 -20.488 1.00 50.61  ? 94  ILE C CB  1 
ATOM   4997  C CG1 . ILE C  1 94  ? 35.018  61.310 -20.630 1.00 56.44  ? 94  ILE C CG1 1 
ATOM   4998  C CG2 . ILE C  1 94  ? 33.608  62.699 -19.060 1.00 46.52  ? 94  ILE C CG2 1 
ATOM   4999  C CD1 . ILE C  1 94  ? 36.314  61.949 -20.190 1.00 56.05  ? 94  ILE C CD1 1 
ATOM   5000  N N   . ASN C  1 95  ? 31.413  60.349 -19.132 1.00 42.27  ? 95  ASN C N   1 
ATOM   5001  C CA  . ASN C  1 95  ? 31.105  59.235 -18.194 1.00 46.08  ? 95  ASN C CA  1 
ATOM   5002  C C   . ASN C  1 95  ? 30.395  58.104 -18.947 1.00 45.91  ? 95  ASN C C   1 
ATOM   5003  O O   . ASN C  1 95  ? 30.550  56.940 -18.541 1.00 41.34  ? 95  ASN C O   1 
ATOM   5004  C CB  . ASN C  1 95  ? 30.277  59.709 -16.998 1.00 46.78  ? 95  ASN C CB  1 
ATOM   5005  C CG  . ASN C  1 95  ? 31.031  60.686 -16.124 1.00 47.50  ? 95  ASN C CG  1 
ATOM   5006  O OD1 . ASN C  1 95  ? 32.251  60.791 -16.213 1.00 50.63  ? 95  ASN C OD1 1 
ATOM   5007  N ND2 . ASN C  1 95  ? 30.310  61.414 -15.289 1.00 56.67  ? 95  ASN C ND2 1 
ATOM   5008  N N   . ILE C  1 96  ? 29.648  58.434 -20.002 1.00 51.80  ? 96  ILE C N   1 
ATOM   5009  C CA  . ILE C  1 96  ? 28.935  57.445 -20.863 1.00 55.88  ? 96  ILE C CA  1 
ATOM   5010  C C   . ILE C  1 96  ? 29.962  56.449 -21.410 1.00 55.32  ? 96  ILE C C   1 
ATOM   5011  O O   . ILE C  1 96  ? 29.646  55.246 -21.460 1.00 65.88  ? 96  ILE C O   1 
ATOM   5012  C CB  . ILE C  1 96  ? 28.161  58.155 -21.991 1.00 57.36  ? 96  ILE C CB  1 
ATOM   5013  C CG1 . ILE C  1 96  ? 27.073  59.075 -21.433 1.00 59.91  ? 96  ILE C CG1 1 
ATOM   5014  C CG2 . ILE C  1 96  ? 27.594  57.144 -22.976 1.00 58.08  ? 96  ILE C CG2 1 
ATOM   5015  C CD1 . ILE C  1 96  ? 26.388  59.917 -22.481 1.00 66.88  ? 96  ILE C CD1 1 
ATOM   5016  N N   . PHE C  1 97  ? 31.143  56.943 -21.795 1.00 54.80  ? 97  PHE C N   1 
ATOM   5017  C CA  . PHE C  1 97  ? 32.267  56.145 -22.354 1.00 57.80  ? 97  PHE C CA  1 
ATOM   5018  C C   . PHE C  1 97  ? 33.094  55.569 -21.202 1.00 55.05  ? 97  PHE C C   1 
ATOM   5019  O O   . PHE C  1 97  ? 33.436  54.376 -21.247 1.00 60.08  ? 97  PHE C O   1 
ATOM   5020  C CB  . PHE C  1 97  ? 33.102  57.004 -23.305 1.00 56.70  ? 97  PHE C CB  1 
ATOM   5021  C CG  . PHE C  1 97  ? 32.328  57.485 -24.506 1.00 63.97  ? 97  PHE C CG  1 
ATOM   5022  C CD1 . PHE C  1 97  ? 32.376  56.795 -25.706 1.00 63.19  ? 97  PHE C CD1 1 
ATOM   5023  C CD2 . PHE C  1 97  ? 31.515  58.604 -24.421 1.00 66.14  ? 97  PHE C CD2 1 
ATOM   5024  C CE1 . PHE C  1 97  ? 31.652  57.233 -26.804 1.00 62.07  ? 97  PHE C CE1 1 
ATOM   5025  C CE2 . PHE C  1 97  ? 30.790  59.041 -25.519 1.00 62.78  ? 97  PHE C CE2 1 
ATOM   5026  C CZ  . PHE C  1 97  ? 30.858  58.352 -26.707 1.00 60.63  ? 97  PHE C CZ  1 
ATOM   5027  N N   . SER C  1 98  ? 33.386  56.401 -20.200 1.00 53.82  ? 98  SER C N   1 
ATOM   5028  C CA  . SER C  1 98  ? 34.064  56.019 -18.935 1.00 51.05  ? 98  SER C CA  1 
ATOM   5029  C C   . SER C  1 98  ? 33.428  54.743 -18.370 1.00 52.61  ? 98  SER C C   1 
ATOM   5030  O O   . SER C  1 98  ? 34.169  53.780 -18.105 1.00 58.73  ? 98  SER C O   1 
ATOM   5031  C CB  . SER C  1 98  ? 33.995  57.145 -17.939 1.00 51.46  ? 98  SER C CB  1 
ATOM   5032  O OG  . SER C  1 98  ? 34.678  56.807 -16.743 1.00 68.13  ? 98  SER C OG  1 
ATOM   5033  N N   . THR C  1 99  ? 32.102  54.747 -18.204 1.00 54.28  ? 99  THR C N   1 
ATOM   5034  C CA  . THR C  1 99  ? 31.314  53.662 -17.560 1.00 53.15  ? 99  THR C CA  1 
ATOM   5035  C C   . THR C  1 99  ? 31.461  52.355 -18.345 1.00 55.28  ? 99  THR C C   1 
ATOM   5036  O O   . THR C  1 99  ? 31.471  51.286 -17.705 1.00 55.31  ? 99  THR C O   1 
ATOM   5037  C CB  . THR C  1 99  ? 29.835  54.045 -17.429 1.00 57.87  ? 99  THR C CB  1 
ATOM   5038  O OG1 . THR C  1 99  ? 29.771  55.363 -16.887 1.00 66.13  ? 99  THR C OG1 1 
ATOM   5039  C CG2 . THR C  1 99  ? 29.060  53.091 -16.547 1.00 67.98  ? 99  THR C CG2 1 
ATOM   5040  N N   . ARG C  1 100 ? 31.559  52.428 -19.674 1.00 58.30  ? 100 ARG C N   1 
ATOM   5041  C CA  . ARG C  1 100 ? 31.620  51.223 -20.542 1.00 58.52  ? 100 ARG C CA  1 
ATOM   5042  C C   . ARG C  1 100 ? 32.941  50.489 -20.287 1.00 50.64  ? 100 ARG C C   1 
ATOM   5043  O O   . ARG C  1 100 ? 32.927  49.245 -20.268 1.00 48.78  ? 100 ARG C O   1 
ATOM   5044  C CB  . ARG C  1 100 ? 31.459  51.582 -22.022 1.00 58.42  ? 100 ARG C CB  1 
ATOM   5045  C CG  . ARG C  1 100 ? 30.893  50.441 -22.854 1.00 57.27  ? 100 ARG C CG  1 
ATOM   5046  C CD  . ARG C  1 100 ? 30.747  50.803 -24.316 1.00 62.12  ? 100 ARG C CD  1 
ATOM   5047  N NE  . ARG C  1 100 ? 29.521  51.534 -24.601 1.00 57.70  ? 100 ARG C NE  1 
ATOM   5048  C CZ  . ARG C  1 100 ? 28.339  50.967 -24.816 1.00 60.93  ? 100 ARG C CZ  1 
ATOM   5049  N NH1 . ARG C  1 100 ? 28.211  49.652 -24.761 1.00 60.70  ? 100 ARG C NH1 1 
ATOM   5050  N NH2 . ARG C  1 100 ? 27.286  51.720 -25.077 1.00 70.66  ? 100 ARG C NH2 1 
ATOM   5051  N N   . TYR C  1 101 ? 34.034  51.232 -20.088 1.00 46.76  ? 101 TYR C N   1 
ATOM   5052  C CA  . TYR C  1 101 ? 35.369  50.680 -19.740 1.00 50.80  ? 101 TYR C CA  1 
ATOM   5053  C C   . TYR C  1 101 ? 35.253  49.916 -18.417 1.00 49.34  ? 101 TYR C C   1 
ATOM   5054  O O   . TYR C  1 101 ? 35.695  48.750 -18.360 1.00 48.55  ? 101 TYR C O   1 
ATOM   5055  C CB  . TYR C  1 101 ? 36.425  51.789 -19.693 1.00 48.30  ? 101 TYR C CB  1 
ATOM   5056  C CG  . TYR C  1 101 ? 36.913  52.227 -21.051 1.00 49.84  ? 101 TYR C CG  1 
ATOM   5057  C CD1 . TYR C  1 101 ? 37.919  51.537 -21.708 1.00 50.79  ? 101 TYR C CD1 1 
ATOM   5058  C CD2 . TYR C  1 101 ? 36.353  53.318 -21.694 1.00 52.36  ? 101 TYR C CD2 1 
ATOM   5059  C CE1 . TYR C  1 101 ? 38.365  51.929 -22.961 1.00 55.13  ? 101 TYR C CE1 1 
ATOM   5060  C CE2 . TYR C  1 101 ? 36.785  53.723 -22.946 1.00 52.13  ? 101 TYR C CE2 1 
ATOM   5061  C CZ  . TYR C  1 101 ? 37.795  53.025 -23.584 1.00 55.41  ? 101 TYR C CZ  1 
ATOM   5062  O OH  . TYR C  1 101 ? 38.223  53.423 -24.818 1.00 53.08  ? 101 TYR C OH  1 
ATOM   5063  N N   . ILE C  1 102 ? 34.657  50.550 -17.401 1.00 45.59  ? 102 ILE C N   1 
ATOM   5064  C CA  . ILE C  1 102 ? 34.361  49.932 -16.073 1.00 44.28  ? 102 ILE C CA  1 
ATOM   5065  C C   . ILE C  1 102 ? 33.730  48.556 -16.310 1.00 46.38  ? 102 ILE C C   1 
ATOM   5066  O O   . ILE C  1 102 ? 34.203  47.574 -15.707 1.00 50.66  ? 102 ILE C O   1 
ATOM   5067  C CB  . ILE C  1 102 ? 33.441  50.837 -15.227 1.00 41.07  ? 102 ILE C CB  1 
ATOM   5068  C CG1 . ILE C  1 102 ? 34.090  52.189 -14.918 1.00 41.86  ? 102 ILE C CG1 1 
ATOM   5069  C CG2 . ILE C  1 102 ? 33.002  50.124 -13.958 1.00 40.32  ? 102 ILE C CG2 1 
ATOM   5070  C CD1 . ILE C  1 102 ? 33.247  53.090 -14.044 1.00 40.84  ? 102 ILE C CD1 1 
ATOM   5071  N N   . GLU C  1 103 ? 32.697  48.497 -17.154 1.00 51.62  ? 103 GLU C N   1 
ATOM   5072  C CA  . GLU C  1 103 ? 31.977  47.244 -17.500 1.00 52.12  ? 103 GLU C CA  1 
ATOM   5073  C C   . GLU C  1 103 ? 32.988  46.204 -17.989 1.00 50.85  ? 103 GLU C C   1 
ATOM   5074  O O   . GLU C  1 103 ? 33.123  45.156 -17.332 1.00 54.02  ? 103 GLU C O   1 
ATOM   5075  C CB  . GLU C  1 103 ? 30.928  47.494 -18.583 1.00 55.86  ? 103 GLU C CB  1 
ATOM   5076  C CG  . GLU C  1 103 ? 30.318  46.213 -19.119 1.00 62.23  ? 103 GLU C CG  1 
ATOM   5077  C CD  . GLU C  1 103 ? 29.855  46.297 -20.560 1.00 66.82  ? 103 GLU C CD  1 
ATOM   5078  O OE1 . GLU C  1 103 ? 29.752  45.236 -21.208 1.00 68.25  ? 103 GLU C OE1 1 
ATOM   5079  O OE2 . GLU C  1 103 ? 29.606  47.424 -21.032 1.00 72.81  ? 103 GLU C OE2 1 
ATOM   5080  N N   . TRP C  1 104 ? 33.663  46.499 -19.104 1.00 49.77  ? 104 TRP C N   1 
ATOM   5081  C CA  . TRP C  1 104 ? 34.624  45.590 -19.784 1.00 46.71  ? 104 TRP C CA  1 
ATOM   5082  C C   . TRP C  1 104 ? 35.645  45.065 -18.771 1.00 47.32  ? 104 TRP C C   1 
ATOM   5083  O O   . TRP C  1 104 ? 35.916  43.849 -18.779 1.00 48.93  ? 104 TRP C O   1 
ATOM   5084  C CB  . TRP C  1 104 ? 35.309  46.305 -20.955 1.00 46.65  ? 104 TRP C CB  1 
ATOM   5085  C CG  . TRP C  1 104 ? 34.367  46.721 -22.043 1.00 50.71  ? 104 TRP C CG  1 
ATOM   5086  C CD1 . TRP C  1 104 ? 33.140  46.189 -22.317 1.00 50.68  ? 104 TRP C CD1 1 
ATOM   5087  C CD2 . TRP C  1 104 ? 34.588  47.743 -23.032 1.00 53.21  ? 104 TRP C CD2 1 
ATOM   5088  N NE1 . TRP C  1 104 ? 32.576  46.819 -23.393 1.00 51.35  ? 104 TRP C NE1 1 
ATOM   5089  C CE2 . TRP C  1 104 ? 33.440  47.777 -23.854 1.00 50.21  ? 104 TRP C CE2 1 
ATOM   5090  C CE3 . TRP C  1 104 ? 35.632  48.635 -23.297 1.00 56.29  ? 104 TRP C CE3 1 
ATOM   5091  C CZ2 . TRP C  1 104 ? 33.315  48.667 -24.919 1.00 49.03  ? 104 TRP C CZ2 1 
ATOM   5092  C CZ3 . TRP C  1 104 ? 35.506  49.514 -24.351 1.00 55.70  ? 104 TRP C CZ3 1 
ATOM   5093  C CH2 . TRP C  1 104 ? 34.362  49.528 -25.149 1.00 50.85  ? 104 TRP C CH2 1 
ATOM   5094  N N   . THR C  1 105 ? 36.182  45.956 -17.933 1.00 47.27  ? 105 THR C N   1 
ATOM   5095  C CA  . THR C  1 105 ? 37.233  45.651 -16.927 1.00 43.62  ? 105 THR C CA  1 
ATOM   5096  C C   . THR C  1 105 ? 36.865  44.365 -16.180 1.00 44.63  ? 105 THR C C   1 
ATOM   5097  O O   . THR C  1 105 ? 37.775  43.554 -15.926 1.00 50.19  ? 105 THR C O   1 
ATOM   5098  C CB  . THR C  1 105 ? 37.433  46.828 -15.964 1.00 43.11  ? 105 THR C CB  1 
ATOM   5099  O OG1 . THR C  1 105 ? 37.794  47.973 -16.737 1.00 45.27  ? 105 THR C OG1 1 
ATOM   5100  C CG2 . THR C  1 105 ? 38.492  46.561 -14.917 1.00 41.85  ? 105 THR C CG2 1 
ATOM   5101  N N   . VAL C  1 106 ? 35.581  44.187 -15.852 1.00 44.35  ? 106 VAL C N   1 
ATOM   5102  C CA  . VAL C  1 106 ? 35.078  43.054 -15.018 1.00 49.79  ? 106 VAL C CA  1 
ATOM   5103  C C   . VAL C  1 106 ? 34.449  41.989 -15.924 1.00 51.60  ? 106 VAL C C   1 
ATOM   5104  O O   . VAL C  1 106 ? 34.767  40.797 -15.733 1.00 47.90  ? 106 VAL C O   1 
ATOM   5105  C CB  . VAL C  1 106 ? 34.076  43.537 -13.951 1.00 50.64  ? 106 VAL C CB  1 
ATOM   5106  C CG1 . VAL C  1 106 ? 33.723  42.426 -12.975 1.00 52.12  ? 106 VAL C CG1 1 
ATOM   5107  C CG2 . VAL C  1 106 ? 34.588  44.758 -13.203 1.00 51.23  ? 106 VAL C CG2 1 
ATOM   5108  N N   . SER C  1 107 ? 33.590  42.397 -16.865 1.00 54.25  ? 107 SER C N   1 
ATOM   5109  C CA  . SER C  1 107 ? 32.777  41.486 -17.715 1.00 54.94  ? 107 SER C CA  1 
ATOM   5110  C C   . SER C  1 107 ? 33.688  40.584 -18.557 1.00 57.19  ? 107 SER C C   1 
ATOM   5111  O O   . SER C  1 107 ? 33.363  39.388 -18.689 1.00 67.97  ? 107 SER C O   1 
ATOM   5112  C CB  . SER C  1 107 ? 31.806  42.248 -18.585 1.00 52.55  ? 107 SER C CB  1 
ATOM   5113  O OG  . SER C  1 107 ? 32.487  43.143 -19.447 1.00 61.46  ? 107 SER C OG  1 
ATOM   5114  N N   . VAL C  1 108 ? 34.783  41.131 -19.094 1.00 53.06  ? 108 VAL C N   1 
ATOM   5115  C CA  . VAL C  1 108 ? 35.695  40.432 -20.051 1.00 53.55  ? 108 VAL C CA  1 
ATOM   5116  C C   . VAL C  1 108 ? 36.445  39.319 -19.321 1.00 51.36  ? 108 VAL C C   1 
ATOM   5117  O O   . VAL C  1 108 ? 36.362  38.157 -19.715 1.00 41.39  ? 108 VAL C O   1 
ATOM   5118  C CB  . VAL C  1 108 ? 36.660  41.420 -20.735 1.00 53.46  ? 108 VAL C CB  1 
ATOM   5119  C CG1 . VAL C  1 108 ? 37.801  40.705 -21.443 1.00 53.05  ? 108 VAL C CG1 1 
ATOM   5120  C CG2 . VAL C  1 108 ? 35.923  42.338 -21.698 1.00 56.58  ? 108 VAL C CG2 1 
ATOM   5121  N N   . PRO C  1 109 ? 37.212  39.630 -18.250 1.00 52.00  ? 109 PRO C N   1 
ATOM   5122  C CA  . PRO C  1 109 ? 37.922  38.600 -17.492 1.00 51.03  ? 109 PRO C CA  1 
ATOM   5123  C C   . PRO C  1 109 ? 37.032  37.392 -17.161 1.00 52.23  ? 109 PRO C C   1 
ATOM   5124  O O   . PRO C  1 109 ? 37.514  36.278 -17.239 1.00 62.03  ? 109 PRO C O   1 
ATOM   5125  C CB  . PRO C  1 109 ? 38.351  39.341 -16.218 1.00 48.90  ? 109 PRO C CB  1 
ATOM   5126  C CG  . PRO C  1 109 ? 38.531  40.772 -16.679 1.00 51.45  ? 109 PRO C CG  1 
ATOM   5127  C CD  . PRO C  1 109 ? 37.452  40.982 -17.722 1.00 51.24  ? 109 PRO C CD  1 
ATOM   5128  N N   . LEU C  1 110 ? 35.767  37.639 -16.807 1.00 49.71  ? 110 LEU C N   1 
ATOM   5129  C CA  . LEU C  1 110 ? 34.767  36.581 -16.498 1.00 53.05  ? 110 LEU C CA  1 
ATOM   5130  C C   . LEU C  1 110 ? 34.524  35.735 -17.752 1.00 51.29  ? 110 LEU C C   1 
ATOM   5131  O O   . LEU C  1 110 ? 34.323  34.514 -17.610 1.00 47.87  ? 110 LEU C O   1 
ATOM   5132  C CB  . LEU C  1 110 ? 33.472  37.232 -16.003 1.00 57.57  ? 110 LEU C CB  1 
ATOM   5133  C CG  . LEU C  1 110 ? 33.525  37.790 -14.581 1.00 59.17  ? 110 LEU C CG  1 
ATOM   5134  C CD1 . LEU C  1 110 ? 32.236  38.517 -14.232 1.00 60.85  ? 110 LEU C CD1 1 
ATOM   5135  C CD2 . LEU C  1 110 ? 33.800  36.683 -13.575 1.00 55.11  ? 110 LEU C CD2 1 
ATOM   5136  N N   . LEU C  1 111 ? 34.550  36.365 -18.929 1.00 54.19  ? 111 LEU C N   1 
ATOM   5137  C CA  . LEU C  1 111 ? 34.367  35.690 -20.242 1.00 52.92  ? 111 LEU C CA  1 
ATOM   5138  C C   . LEU C  1 111 ? 35.514  34.700 -20.468 1.00 48.35  ? 111 LEU C C   1 
ATOM   5139  O O   . LEU C  1 111 ? 35.236  33.581 -20.936 1.00 42.94  ? 111 LEU C O   1 
ATOM   5140  C CB  . LEU C  1 111 ? 34.310  36.743 -21.353 1.00 55.21  ? 111 LEU C CB  1 
ATOM   5141  C CG  . LEU C  1 111 ? 33.004  37.530 -21.435 1.00 59.60  ? 111 LEU C CG  1 
ATOM   5142  C CD1 . LEU C  1 111 ? 33.100  38.639 -22.472 1.00 63.09  ? 111 LEU C CD1 1 
ATOM   5143  C CD2 . LEU C  1 111 ? 31.832  36.610 -21.742 1.00 58.50  ? 111 LEU C CD2 1 
ATOM   5144  N N   . THR C  1 112 ? 36.750  35.095 -20.148 1.00 48.87  ? 112 THR C N   1 
ATOM   5145  C CA  . THR C  1 112 ? 37.951  34.218 -20.230 1.00 53.48  ? 112 THR C CA  1 
ATOM   5146  C C   . THR C  1 112 ? 37.729  32.994 -19.334 1.00 53.15  ? 112 THR C C   1 
ATOM   5147  O O   . THR C  1 112 ? 37.776  31.862 -19.854 1.00 51.33  ? 112 THR C O   1 
ATOM   5148  C CB  . THR C  1 112 ? 39.233  34.965 -19.841 1.00 52.39  ? 112 THR C CB  1 
ATOM   5149  O OG1 . THR C  1 112 ? 39.209  35.195 -18.431 1.00 53.15  ? 112 THR C OG1 1 
ATOM   5150  C CG2 . THR C  1 112 ? 39.398  36.273 -20.583 1.00 48.93  ? 112 THR C CG2 1 
ATOM   5151  N N   . ILE C  1 113 ? 37.485  33.229 -18.042 1.00 52.81  ? 113 ILE C N   1 
ATOM   5152  C CA  . ILE C  1 113 ? 37.237  32.180 -17.009 1.00 54.49  ? 113 ILE C CA  1 
ATOM   5153  C C   . ILE C  1 113 ? 36.187  31.195 -17.535 1.00 51.22  ? 113 ILE C C   1 
ATOM   5154  O O   . ILE C  1 113 ? 36.393  29.972 -17.393 1.00 45.41  ? 113 ILE C O   1 
ATOM   5155  C CB  . ILE C  1 113 ? 36.793  32.826 -15.682 1.00 58.95  ? 113 ILE C CB  1 
ATOM   5156  C CG1 . ILE C  1 113 ? 37.903  33.687 -15.073 1.00 63.60  ? 113 ILE C CG1 1 
ATOM   5157  C CG2 . ILE C  1 113 ? 36.296  31.769 -14.707 1.00 61.98  ? 113 ILE C CG2 1 
ATOM   5158  C CD1 . ILE C  1 113 ? 37.417  34.683 -14.046 1.00 64.20  ? 113 ILE C CD1 1 
ATOM   5159  N N   . GLU C  1 114 ? 35.102  31.720 -18.111 1.00 53.31  ? 114 GLU C N   1 
ATOM   5160  C CA  . GLU C  1 114 ? 33.945  30.933 -18.613 1.00 54.41  ? 114 GLU C CA  1 
ATOM   5161  C C   . GLU C  1 114 ? 34.421  29.964 -19.700 1.00 50.70  ? 114 GLU C C   1 
ATOM   5162  O O   . GLU C  1 114 ? 33.982  28.799 -19.680 1.00 49.97  ? 114 GLU C O   1 
ATOM   5163  C CB  . GLU C  1 114 ? 32.859  31.870 -19.145 1.00 62.69  ? 114 GLU C CB  1 
ATOM   5164  C CG  . GLU C  1 114 ? 31.597  31.147 -19.576 1.00 73.11  ? 114 GLU C CG  1 
ATOM   5165  C CD  . GLU C  1 114 ? 30.467  32.057 -20.027 1.00 85.25  ? 114 GLU C CD  1 
ATOM   5166  O OE1 . GLU C  1 114 ? 29.534  31.549 -20.677 1.00 91.98  ? 114 GLU C OE1 1 
ATOM   5167  O OE2 . GLU C  1 114 ? 30.520  33.270 -19.725 1.00 79.82  ? 114 GLU C OE2 1 
ATOM   5168  N N   . LEU C  1 115 ? 35.287  30.430 -20.605 1.00 51.62  ? 115 LEU C N   1 
ATOM   5169  C CA  . LEU C  1 115 ? 35.831  29.623 -21.731 1.00 53.09  ? 115 LEU C CA  1 
ATOM   5170  C C   . LEU C  1 115 ? 36.790  28.562 -21.183 1.00 50.19  ? 115 LEU C C   1 
ATOM   5171  O O   . LEU C  1 115 ? 36.687  27.399 -21.612 1.00 52.83  ? 115 LEU C O   1 
ATOM   5172  C CB  . LEU C  1 115 ? 36.543  30.542 -22.727 1.00 55.05  ? 115 LEU C CB  1 
ATOM   5173  C CG  . LEU C  1 115 ? 37.116  29.842 -23.959 1.00 59.58  ? 115 LEU C CG  1 
ATOM   5174  C CD1 . LEU C  1 115 ? 36.029  29.082 -24.704 1.00 65.47  ? 115 LEU C CD1 1 
ATOM   5175  C CD2 . LEU C  1 115 ? 37.805  30.836 -24.882 1.00 64.00  ? 115 LEU C CD2 1 
ATOM   5176  N N   . LEU C  1 116 ? 37.688  28.955 -20.275 1.00 52.97  ? 116 LEU C N   1 
ATOM   5177  C CA  . LEU C  1 116 ? 38.712  28.063 -19.667 1.00 55.73  ? 116 LEU C CA  1 
ATOM   5178  C C   . LEU C  1 116 ? 38.019  26.976 -18.837 1.00 55.15  ? 116 LEU C C   1 
ATOM   5179  O O   . LEU C  1 116 ? 38.594  25.880 -18.699 1.00 57.28  ? 116 LEU C O   1 
ATOM   5180  C CB  . LEU C  1 116 ? 39.658  28.897 -18.797 1.00 57.46  ? 116 LEU C CB  1 
ATOM   5181  C CG  . LEU C  1 116 ? 40.563  29.870 -19.550 1.00 57.68  ? 116 LEU C CG  1 
ATOM   5182  C CD1 . LEU C  1 116 ? 41.514  30.573 -18.592 1.00 63.36  ? 116 LEU C CD1 1 
ATOM   5183  C CD2 . LEU C  1 116 ? 41.339  29.153 -20.644 1.00 54.50  ? 116 LEU C CD2 1 
ATOM   5184  N N   . ALA C  1 117 ? 36.833  27.276 -18.304 1.00 56.52  ? 117 ALA C N   1 
ATOM   5185  C CA  . ALA C  1 117 ? 36.041  26.371 -17.440 1.00 57.52  ? 117 ALA C CA  1 
ATOM   5186  C C   . ALA C  1 117 ? 35.540  25.176 -18.259 1.00 54.84  ? 117 ALA C C   1 
ATOM   5187  O O   . ALA C  1 117 ? 35.510  24.062 -17.710 1.00 55.40  ? 117 ALA C O   1 
ATOM   5188  C CB  . ALA C  1 117 ? 34.902  27.131 -16.807 1.00 58.72  ? 117 ALA C CB  1 
ATOM   5189  N N   . VAL C  1 118 ? 35.164  25.402 -19.522 1.00 60.16  ? 118 VAL C N   1 
ATOM   5190  C CA  . VAL C  1 118 ? 34.621  24.355 -20.440 1.00 63.19  ? 118 VAL C CA  1 
ATOM   5191  C C   . VAL C  1 118 ? 35.786  23.687 -21.180 1.00 66.79  ? 118 VAL C C   1 
ATOM   5192  O O   . VAL C  1 118 ? 35.546  22.678 -21.872 1.00 63.46  ? 118 VAL C O   1 
ATOM   5193  C CB  . VAL C  1 118 ? 33.587  24.937 -21.423 1.00 63.72  ? 118 VAL C CB  1 
ATOM   5194  C CG1 . VAL C  1 118 ? 32.278  25.270 -20.725 1.00 63.55  ? 118 VAL C CG1 1 
ATOM   5195  C CG2 . VAL C  1 118 ? 34.127  26.149 -22.166 1.00 65.05  ? 118 VAL C CG2 1 
ATOM   5196  N N   . CYS C  1 119 ? 36.997  24.235 -21.043 1.00 71.28  ? 119 CYS C N   1 
ATOM   5197  C CA  . CYS C  1 119 ? 38.262  23.633 -21.544 1.00 73.49  ? 119 CYS C CA  1 
ATOM   5198  C C   . CYS C  1 119 ? 38.691  22.497 -20.607 1.00 76.48  ? 119 CYS C C   1 
ATOM   5199  O O   . CYS C  1 119 ? 38.195  22.456 -19.463 1.00 73.77  ? 119 CYS C O   1 
ATOM   5200  C CB  . CYS C  1 119 ? 39.366  24.677 -21.658 1.00 71.57  ? 119 CYS C CB  1 
ATOM   5201  S SG  . CYS C  1 119 ? 39.190  25.749 -23.107 1.00 71.49  ? 119 CYS C SG  1 
ATOM   5202  N N   . ALA C  1 120 ? 39.589  21.624 -21.073 1.00 85.03  ? 120 ALA C N   1 
ATOM   5203  C CA  . ALA C  1 120 ? 39.980  20.362 -20.400 1.00 92.86  ? 120 ALA C CA  1 
ATOM   5204  C C   . ALA C  1 120 ? 41.210  20.577 -19.508 1.00 94.85  ? 120 ALA C C   1 
ATOM   5205  O O   . ALA C  1 120 ? 41.666  19.590 -18.900 1.00 103.98 ? 120 ALA C O   1 
ATOM   5206  C CB  . ALA C  1 120 ? 40.231  19.294 -21.436 1.00 85.65  ? 120 ALA C CB  1 
ATOM   5207  N N   . THR C  1 121 ? 41.720  21.810 -19.429 1.00 99.27  ? 121 THR C N   1 
ATOM   5208  C CA  . THR C  1 121 ? 42.884  22.191 -18.581 1.00 98.35  ? 121 THR C CA  1 
ATOM   5209  C C   . THR C  1 121 ? 42.672  21.631 -17.168 1.00 104.63 ? 121 THR C C   1 
ATOM   5210  O O   . THR C  1 121 ? 41.539  21.744 -16.661 1.00 100.00 ? 121 THR C O   1 
ATOM   5211  C CB  . THR C  1 121 ? 43.087  23.712 -18.578 1.00 98.90  ? 121 THR C CB  1 
ATOM   5212  O OG1 . THR C  1 121 ? 41.876  24.321 -18.130 1.00 100.53 ? 121 THR C OG1 1 
ATOM   5213  C CG2 . THR C  1 121 ? 43.450  24.268 -19.938 1.00 102.74 ? 121 THR C CG2 1 
ATOM   5214  N N   . LEU C  1 122 ? 43.716  21.044 -16.567 1.00 116.65 ? 122 LEU C N   1 
ATOM   5215  C CA  . LEU C  1 122 ? 43.658  20.383 -15.232 1.00 115.58 ? 122 LEU C CA  1 
ATOM   5216  C C   . LEU C  1 122 ? 44.794  20.899 -14.340 1.00 113.12 ? 122 LEU C C   1 
ATOM   5217  O O   . LEU C  1 122 ? 45.903  21.128 -14.870 1.00 120.85 ? 122 LEU C O   1 
ATOM   5218  C CB  . LEU C  1 122 ? 43.773  18.865 -15.405 1.00 110.51 ? 122 LEU C CB  1 
ATOM   5219  C CG  . LEU C  1 122 ? 42.907  18.247 -16.501 1.00 120.88 ? 122 LEU C CG  1 
ATOM   5220  C CD1 . LEU C  1 122 ? 43.272  16.787 -16.718 1.00 119.07 ? 122 LEU C CD1 1 
ATOM   5221  C CD2 . LEU C  1 122 ? 41.429  18.385 -16.170 1.00 131.70 ? 122 LEU C CD2 1 
ATOM   5222  N N   . GLY C  1 123 ? 44.517  21.060 -13.041 1.00 97.29  ? 123 GLY C N   1 
ATOM   5223  C CA  . GLY C  1 123 ? 45.516  21.338 -11.989 1.00 99.00  ? 123 GLY C CA  1 
ATOM   5224  C C   . GLY C  1 123 ? 46.123  22.726 -12.107 1.00 102.53 ? 123 GLY C C   1 
ATOM   5225  O O   . GLY C  1 123 ? 45.359  23.705 -12.064 1.00 110.17 ? 123 GLY C O   1 
ATOM   5226  N N   . VAL C  1 124 ? 47.452  22.797 -12.240 1.00 102.71 ? 124 VAL C N   1 
ATOM   5227  C CA  . VAL C  1 124 ? 48.257  24.056 -12.266 1.00 104.90 ? 124 VAL C CA  1 
ATOM   5228  C C   . VAL C  1 124 ? 48.126  24.718 -13.644 1.00 107.35 ? 124 VAL C C   1 
ATOM   5229  O O   . VAL C  1 124 ? 47.976  25.960 -13.696 1.00 119.56 ? 124 VAL C O   1 
ATOM   5230  C CB  . VAL C  1 124 ? 49.733  23.769 -11.928 1.00 104.67 ? 124 VAL C CB  1 
ATOM   5231  C CG1 . VAL C  1 124 ? 50.601  25.006 -12.097 1.00 115.89 ? 124 VAL C CG1 1 
ATOM   5232  C CG2 . VAL C  1 124 ? 49.891  23.183 -10.532 1.00 91.49  ? 124 VAL C CG2 1 
ATOM   5233  N N   . GLN C  1 125 ? 48.202  23.919 -14.714 1.00 100.69 ? 125 GLN C N   1 
ATOM   5234  C CA  . GLN C  1 125 ? 48.099  24.386 -16.123 1.00 98.82  ? 125 GLN C CA  1 
ATOM   5235  C C   . GLN C  1 125 ? 46.832  25.236 -16.272 1.00 105.55 ? 125 GLN C C   1 
ATOM   5236  O O   . GLN C  1 125 ? 46.876  26.246 -17.006 1.00 111.37 ? 125 GLN C O   1 
ATOM   5237  C CB  . GLN C  1 125 ? 48.080  23.194 -17.083 1.00 83.50  ? 125 GLN C CB  1 
ATOM   5238  N N   . ALA C  1 126 ? 45.754  24.834 -15.589 1.00 103.46 ? 126 ALA C N   1 
ATOM   5239  C CA  . ALA C  1 126 ? 44.431  25.501 -15.593 1.00 94.02  ? 126 ALA C CA  1 
ATOM   5240  C C   . ALA C  1 126 ? 44.508  26.811 -14.801 1.00 95.00  ? 126 ALA C C   1 
ATOM   5241  O O   . ALA C  1 126 ? 44.185  27.864 -15.380 1.00 96.21  ? 126 ALA C O   1 
ATOM   5242  C CB  . ALA C  1 126 ? 43.387  24.573 -15.021 1.00 86.84  ? 126 ALA C CB  1 
ATOM   5243  N N   . ARG C  1 127 ? 44.921  26.737 -13.530 1.00 89.32  ? 127 ARG C N   1 
ATOM   5244  C CA  . ARG C  1 127 ? 44.994  27.892 -12.593 1.00 83.40  ? 127 ARG C CA  1 
ATOM   5245  C C   . ARG C  1 127 ? 45.947  28.955 -13.154 1.00 91.21  ? 127 ARG C C   1 
ATOM   5246  O O   . ARG C  1 127 ? 45.638  30.154 -13.002 1.00 90.85  ? 127 ARG C O   1 
ATOM   5247  C CB  . ARG C  1 127 ? 45.439  27.433 -11.200 1.00 71.81  ? 127 ARG C CB  1 
ATOM   5248  N N   . ARG C  1 128 ? 47.055  28.534 -13.776 1.00 87.62  ? 128 ARG C N   1 
ATOM   5249  C CA  . ARG C  1 128 ? 48.067  29.444 -14.380 1.00 82.85  ? 128 ARG C CA  1 
ATOM   5250  C C   . ARG C  1 128 ? 47.427  30.206 -15.548 1.00 92.73  ? 128 ARG C C   1 
ATOM   5251  O O   . ARG C  1 128 ? 47.539  31.450 -15.577 1.00 108.13 ? 128 ARG C O   1 
ATOM   5252  C CB  . ARG C  1 128 ? 49.298  28.656 -14.838 1.00 74.35  ? 128 ARG C CB  1 
ATOM   5253  N N   . ASN C  1 129 ? 46.777  29.482 -16.467 1.00 87.04  ? 129 ASN C N   1 
ATOM   5254  C CA  . ASN C  1 129 ? 46.108  30.050 -17.669 1.00 82.36  ? 129 ASN C CA  1 
ATOM   5255  C C   . ASN C  1 129 ? 45.135  31.152 -17.235 1.00 74.46  ? 129 ASN C C   1 
ATOM   5256  O O   . ASN C  1 129 ? 45.256  32.285 -17.743 1.00 69.16  ? 129 ASN C O   1 
ATOM   5257  C CB  . ASN C  1 129 ? 45.389  28.970 -18.480 1.00 86.62  ? 129 ASN C CB  1 
ATOM   5258  C CG  . ASN C  1 129 ? 46.343  28.022 -19.175 1.00 95.97  ? 129 ASN C CG  1 
ATOM   5259  O OD1 . ASN C  1 129 ? 47.558  28.178 -19.083 1.00 107.77 ? 129 ASN C OD1 1 
ATOM   5260  N ND2 . ASN C  1 129 ? 45.802  27.039 -19.876 1.00 100.70 ? 129 ASN C ND2 1 
ATOM   5261  N N   . THR C  1 130 ? 44.205  30.822 -16.332 1.00 65.19  ? 130 THR C N   1 
ATOM   5262  C CA  . THR C  1 130 ? 43.182  31.752 -15.785 1.00 67.22  ? 130 THR C CA  1 
ATOM   5263  C C   . THR C  1 130 ? 43.871  33.034 -15.301 1.00 62.85  ? 130 THR C C   1 
ATOM   5264  O O   . THR C  1 130 ? 43.463  34.123 -15.745 1.00 67.54  ? 130 THR C O   1 
ATOM   5265  C CB  . THR C  1 130 ? 42.374  31.089 -14.661 1.00 69.31  ? 130 THR C CB  1 
ATOM   5266  O OG1 . THR C  1 130 ? 41.958  29.802 -15.118 1.00 82.21  ? 130 THR C OG1 1 
ATOM   5267  C CG2 . THR C  1 130 ? 41.161  31.893 -14.247 1.00 70.46  ? 130 THR C CG2 1 
ATOM   5268  N N   . ALA C  1 131 ? 44.880  32.898 -14.436 1.00 56.02  ? 131 ALA C N   1 
ATOM   5269  C CA  . ALA C  1 131 ? 45.628  34.014 -13.811 1.00 55.15  ? 131 ALA C CA  1 
ATOM   5270  C C   . ALA C  1 131 ? 46.159  34.962 -14.892 1.00 55.17  ? 131 ALA C C   1 
ATOM   5271  O O   . ALA C  1 131 ? 46.023  36.191 -14.719 1.00 54.87  ? 131 ALA C O   1 
ATOM   5272  C CB  . ALA C  1 131 ? 46.749  33.468 -12.963 1.00 58.01  ? 131 ALA C CB  1 
ATOM   5273  N N   . ILE C  1 132 ? 46.741  34.408 -15.960 1.00 54.27  ? 132 ILE C N   1 
ATOM   5274  C CA  . ILE C  1 132 ? 47.327  35.178 -17.099 1.00 56.74  ? 132 ILE C CA  1 
ATOM   5275  C C   . ILE C  1 132 ? 46.190  35.846 -17.884 1.00 56.05  ? 132 ILE C C   1 
ATOM   5276  O O   . ILE C  1 132 ? 46.227  37.084 -18.046 1.00 59.70  ? 132 ILE C O   1 
ATOM   5277  C CB  . ILE C  1 132 ? 48.184  34.270 -18.002 1.00 59.26  ? 132 ILE C CB  1 
ATOM   5278  C CG1 . ILE C  1 132 ? 49.325  33.607 -17.226 1.00 66.76  ? 132 ILE C CG1 1 
ATOM   5279  C CG2 . ILE C  1 132 ? 48.700  35.048 -19.202 1.00 59.79  ? 132 ILE C CG2 1 
ATOM   5280  C CD1 . ILE C  1 132 ? 50.134  32.625 -18.042 1.00 67.84  ? 132 ILE C CD1 1 
ATOM   5281  N N   . ALA C  1 133 ? 45.222  35.051 -18.349 1.00 51.98  ? 133 ALA C N   1 
ATOM   5282  C CA  . ALA C  1 133 ? 44.053  35.505 -19.138 1.00 55.13  ? 133 ALA C CA  1 
ATOM   5283  C C   . ALA C  1 133 ? 43.355  36.666 -18.419 1.00 55.72  ? 133 ALA C C   1 
ATOM   5284  O O   . ALA C  1 133 ? 43.070  37.684 -19.077 1.00 57.50  ? 133 ALA C O   1 
ATOM   5285  C CB  . ALA C  1 133 ? 43.106  34.354 -19.364 1.00 55.11  ? 133 ALA C CB  1 
ATOM   5286  N N   . VAL C  1 134 ? 43.085  36.511 -17.119 1.00 54.29  ? 134 VAL C N   1 
ATOM   5287  C CA  . VAL C  1 134 ? 42.363  37.518 -16.286 1.00 57.35  ? 134 VAL C CA  1 
ATOM   5288  C C   . VAL C  1 134 ? 43.187  38.809 -16.250 1.00 57.10  ? 134 VAL C C   1 
ATOM   5289  O O   . VAL C  1 134 ? 42.670  39.845 -16.710 1.00 65.63  ? 134 VAL C O   1 
ATOM   5290  C CB  . VAL C  1 134 ? 42.067  36.985 -14.870 1.00 57.48  ? 134 VAL C CB  1 
ATOM   5291  C CG1 . VAL C  1 134 ? 41.646  38.100 -13.923 1.00 57.97  ? 134 VAL C CG1 1 
ATOM   5292  C CG2 . VAL C  1 134 ? 41.015  35.884 -14.898 1.00 53.25  ? 134 VAL C CG2 1 
ATOM   5293  N N   . THR C  1 135 ? 44.420  38.746 -15.736 1.00 57.63  ? 135 THR C N   1 
ATOM   5294  C CA  . THR C  1 135 ? 45.320  39.920 -15.564 1.00 56.06  ? 135 THR C CA  1 
ATOM   5295  C C   . THR C  1 135 ? 45.589  40.553 -16.933 1.00 55.45  ? 135 THR C C   1 
ATOM   5296  O O   . THR C  1 135 ? 45.625  41.798 -17.008 1.00 58.65  ? 135 THR C O   1 
ATOM   5297  C CB  . THR C  1 135 ? 46.623  39.537 -14.851 1.00 53.50  ? 135 THR C CB  1 
ATOM   5298  O OG1 . THR C  1 135 ? 47.247  38.494 -15.598 1.00 58.17  ? 135 THR C OG1 1 
ATOM   5299  C CG2 . THR C  1 135 ? 46.404  39.076 -13.427 1.00 57.71  ? 135 THR C CG2 1 
ATOM   5300  N N   . ALA C  1 136 ? 45.761  39.726 -17.969 1.00 53.49  ? 136 ALA C N   1 
ATOM   5301  C CA  . ALA C  1 136 ? 45.986  40.158 -19.368 1.00 53.62  ? 136 ALA C CA  1 
ATOM   5302  C C   . ALA C  1 136 ? 44.809  41.028 -19.824 1.00 56.11  ? 136 ALA C C   1 
ATOM   5303  O O   . ALA C  1 136 ? 45.040  42.206 -20.164 1.00 63.64  ? 136 ALA C O   1 
ATOM   5304  C CB  . ALA C  1 136 ? 46.169  38.955 -20.259 1.00 52.22  ? 136 ALA C CB  1 
ATOM   5305  N N   . THR C  1 137 ? 43.594  40.467 -19.818 1.00 53.16  ? 137 THR C N   1 
ATOM   5306  C CA  . THR C  1 137 ? 42.341  41.135 -20.265 1.00 50.30  ? 137 THR C CA  1 
ATOM   5307  C C   . THR C  1 137 ? 42.052  42.346 -19.370 1.00 50.24  ? 137 THR C C   1 
ATOM   5308  O O   . THR C  1 137 ? 41.622  43.387 -19.913 1.00 50.76  ? 137 THR C O   1 
ATOM   5309  C CB  . THR C  1 137 ? 41.161  40.156 -20.287 1.00 48.87  ? 137 THR C CB  1 
ATOM   5310  O OG1 . THR C  1 137 ? 41.112  39.459 -19.042 1.00 48.55  ? 137 THR C OG1 1 
ATOM   5311  C CG2 . THR C  1 137 ? 41.255  39.166 -21.426 1.00 49.27  ? 137 THR C CG2 1 
ATOM   5312  N N   . GLY C  1 138 ? 42.274  42.214 -18.059 1.00 47.66  ? 138 GLY C N   1 
ATOM   5313  C CA  . GLY C  1 138 ? 42.136  43.318 -17.090 1.00 52.87  ? 138 GLY C CA  1 
ATOM   5314  C C   . GLY C  1 138 ? 42.991  44.505 -17.498 1.00 53.33  ? 138 GLY C C   1 
ATOM   5315  O O   . GLY C  1 138 ? 42.438  45.616 -17.654 1.00 51.49  ? 138 GLY C O   1 
ATOM   5316  N N   . ALA C  1 139 ? 44.294  44.266 -17.680 1.00 54.54  ? 139 ALA C N   1 
ATOM   5317  C CA  . ALA C  1 139 ? 45.298  45.259 -18.126 1.00 55.08  ? 139 ALA C CA  1 
ATOM   5318  C C   . ALA C  1 139 ? 44.897  45.817 -19.496 1.00 55.96  ? 139 ALA C C   1 
ATOM   5319  O O   . ALA C  1 139 ? 44.927  47.054 -19.662 1.00 56.10  ? 139 ALA C O   1 
ATOM   5320  C CB  . ALA C  1 139 ? 46.662  44.616 -18.169 1.00 55.74  ? 139 ALA C CB  1 
ATOM   5321  N N   . MET C  1 140 ? 44.537  44.933 -20.433 1.00 52.75  ? 140 MET C N   1 
ATOM   5322  C CA  . MET C  1 140 ? 44.107  45.290 -21.812 1.00 52.78  ? 140 MET C CA  1 
ATOM   5323  C C   . MET C  1 140 ? 43.115  46.456 -21.743 1.00 53.15  ? 140 MET C C   1 
ATOM   5324  O O   . MET C  1 140 ? 43.348  47.476 -22.425 1.00 53.36  ? 140 MET C O   1 
ATOM   5325  C CB  . MET C  1 140 ? 43.437  44.102 -22.510 1.00 55.03  ? 140 MET C CB  1 
ATOM   5326  C CG  . MET C  1 140 ? 42.839  44.457 -23.861 1.00 61.02  ? 140 MET C CG  1 
ATOM   5327  S SD  . MET C  1 140 ? 42.135  43.027 -24.725 1.00 61.94  ? 140 MET C SD  1 
ATOM   5328  C CE  . MET C  1 140 ? 40.746  42.647 -23.658 1.00 70.12  ? 140 MET C CE  1 
ATOM   5329  N N   . ILE C  1 141 ? 42.055  46.301 -20.945 1.00 51.83  ? 141 ILE C N   1 
ATOM   5330  C CA  . ILE C  1 141 ? 40.961  47.305 -20.792 1.00 49.84  ? 141 ILE C CA  1 
ATOM   5331  C C   . ILE C  1 141 ? 41.527  48.554 -20.112 1.00 48.04  ? 141 ILE C C   1 
ATOM   5332  O O   . ILE C  1 141 ? 41.362  49.657 -20.672 1.00 42.64  ? 141 ILE C O   1 
ATOM   5333  C CB  . ILE C  1 141 ? 39.775  46.714 -20.006 1.00 53.12  ? 141 ILE C CB  1 
ATOM   5334  C CG1 . ILE C  1 141 ? 39.236  45.444 -20.670 1.00 53.12  ? 141 ILE C CG1 1 
ATOM   5335  C CG2 . ILE C  1 141 ? 38.684  47.758 -19.811 1.00 54.27  ? 141 ILE C CG2 1 
ATOM   5336  C CD1 . ILE C  1 141 ? 38.761  45.645 -22.091 1.00 50.31  ? 141 ILE C CD1 1 
ATOM   5337  N N   . PHE C  1 142 ? 42.171  48.381 -18.953 1.00 46.78  ? 142 PHE C N   1 
ATOM   5338  C CA  . PHE C  1 142 ? 42.687  49.489 -18.108 1.00 50.51  ? 142 PHE C CA  1 
ATOM   5339  C C   . PHE C  1 142 ? 43.581  50.409 -18.946 1.00 51.34  ? 142 PHE C C   1 
ATOM   5340  O O   . PHE C  1 142 ? 43.573  51.635 -18.712 1.00 52.58  ? 142 PHE C O   1 
ATOM   5341  C CB  . PHE C  1 142 ? 43.460  48.967 -16.896 1.00 51.26  ? 142 PHE C CB  1 
ATOM   5342  C CG  . PHE C  1 142 ? 43.946  50.070 -15.989 1.00 50.74  ? 142 PHE C CG  1 
ATOM   5343  C CD1 . PHE C  1 142 ? 45.297  50.354 -15.871 1.00 49.69  ? 142 PHE C CD1 1 
ATOM   5344  C CD2 . PHE C  1 142 ? 43.044  50.854 -15.287 1.00 50.13  ? 142 PHE C CD2 1 
ATOM   5345  C CE1 . PHE C  1 142 ? 45.735  51.380 -15.049 1.00 48.64  ? 142 PHE C CE1 1 
ATOM   5346  C CE2 . PHE C  1 142 ? 43.483  51.881 -14.469 1.00 49.29  ? 142 PHE C CE2 1 
ATOM   5347  C CZ  . PHE C  1 142 ? 44.827  52.142 -14.351 1.00 49.07  ? 142 PHE C CZ  1 
ATOM   5348  N N   . CYS C  1 143 ? 44.338  49.830 -19.880 1.00 54.06  ? 143 CYS C N   1 
ATOM   5349  C CA  . CYS C  1 143 ? 45.241  50.567 -20.803 1.00 56.00  ? 143 CYS C CA  1 
ATOM   5350  C C   . CYS C  1 143 ? 44.407  51.472 -21.717 1.00 54.92  ? 143 CYS C C   1 
ATOM   5351  O O   . CYS C  1 143 ? 44.632  52.700 -21.700 1.00 50.39  ? 143 CYS C O   1 
ATOM   5352  C CB  . CYS C  1 143 ? 46.099  49.602 -21.612 1.00 60.97  ? 143 CYS C CB  1 
ATOM   5353  S SG  . CYS C  1 143 ? 47.454  48.879 -20.650 1.00 65.23  ? 143 CYS C SG  1 
ATOM   5354  N N   . GLY C  1 144 ? 43.475  50.885 -22.473 1.00 55.92  ? 144 GLY C N   1 
ATOM   5355  C CA  . GLY C  1 144 ? 42.520  51.619 -23.327 1.00 54.23  ? 144 GLY C CA  1 
ATOM   5356  C C   . GLY C  1 144 ? 41.855  52.757 -22.571 1.00 53.49  ? 144 GLY C C   1 
ATOM   5357  O O   . GLY C  1 144 ? 41.627  53.817 -23.186 1.00 54.34  ? 144 GLY C O   1 
ATOM   5358  N N   . PHE C  1 145 ? 41.558  52.546 -21.284 1.00 50.27  ? 145 PHE C N   1 
ATOM   5359  C CA  . PHE C  1 145 ? 40.921  53.537 -20.376 1.00 48.23  ? 145 PHE C CA  1 
ATOM   5360  C C   . PHE C  1 145 ? 41.853  54.742 -20.203 1.00 51.44  ? 145 PHE C C   1 
ATOM   5361  O O   . PHE C  1 145 ? 41.382  55.890 -20.342 1.00 49.32  ? 145 PHE C O   1 
ATOM   5362  C CB  . PHE C  1 145 ? 40.573  52.893 -19.030 1.00 46.32  ? 145 PHE C CB  1 
ATOM   5363  C CG  . PHE C  1 145 ? 39.919  53.819 -18.035 1.00 45.37  ? 145 PHE C CG  1 
ATOM   5364  C CD1 . PHE C  1 145 ? 40.496  54.056 -16.798 1.00 44.68  ? 145 PHE C CD1 1 
ATOM   5365  C CD2 . PHE C  1 145 ? 38.729  54.463 -18.337 1.00 47.94  ? 145 PHE C CD2 1 
ATOM   5366  C CE1 . PHE C  1 145 ? 39.894  54.910 -15.886 1.00 46.00  ? 145 PHE C CE1 1 
ATOM   5367  C CE2 . PHE C  1 145 ? 38.130  55.319 -17.425 1.00 43.64  ? 145 PHE C CE2 1 
ATOM   5368  C CZ  . PHE C  1 145 ? 38.713  55.541 -16.201 1.00 41.93  ? 145 PHE C CZ  1 
ATOM   5369  N N   . LEU C  1 146 ? 43.132  54.486 -19.909 1.00 52.72  ? 146 LEU C N   1 
ATOM   5370  C CA  . LEU C  1 146 ? 44.176  55.531 -19.724 1.00 53.03  ? 146 LEU C CA  1 
ATOM   5371  C C   . LEU C  1 146 ? 44.266  56.391 -20.989 1.00 52.62  ? 146 LEU C C   1 
ATOM   5372  O O   . LEU C  1 146 ? 44.254  57.635 -20.867 1.00 53.63  ? 146 LEU C O   1 
ATOM   5373  C CB  . LEU C  1 146 ? 45.520  54.861 -19.421 1.00 51.48  ? 146 LEU C CB  1 
ATOM   5374  C CG  . LEU C  1 146 ? 45.656  54.272 -18.019 1.00 52.69  ? 146 LEU C CG  1 
ATOM   5375  C CD1 . LEU C  1 146 ? 47.018  53.626 -17.829 1.00 52.26  ? 146 LEU C CD1 1 
ATOM   5376  C CD2 . LEU C  1 146 ? 45.421  55.334 -16.958 1.00 53.96  ? 146 LEU C CD2 1 
ATOM   5377  N N   . GLY C  1 147 ? 44.350  55.744 -22.154 1.00 46.41  ? 147 GLY C N   1 
ATOM   5378  C CA  . GLY C  1 147 ? 44.515  56.408 -23.460 1.00 51.03  ? 147 GLY C CA  1 
ATOM   5379  C C   . GLY C  1 147 ? 43.331  57.294 -23.810 1.00 50.36  ? 147 GLY C C   1 
ATOM   5380  O O   . GLY C  1 147 ? 43.552  58.485 -24.101 1.00 53.74  ? 147 GLY C O   1 
ATOM   5381  N N   . ALA C  1 148 ? 42.117  56.735 -23.771 1.00 53.46  ? 148 ALA C N   1 
ATOM   5382  C CA  . ALA C  1 148 ? 40.887  57.326 -24.351 1.00 53.20  ? 148 ALA C CA  1 
ATOM   5383  C C   . ALA C  1 148 ? 40.225  58.303 -23.373 1.00 51.29  ? 148 ALA C C   1 
ATOM   5384  O O   . ALA C  1 148 ? 39.500  59.192 -23.855 1.00 57.93  ? 148 ALA C O   1 
ATOM   5385  C CB  . ALA C  1 148 ? 39.929  56.227 -24.742 1.00 54.59  ? 148 ALA C CB  1 
ATOM   5386  N N   . ILE C  1 149 ? 40.455  58.147 -22.064 1.00 50.91  ? 149 ILE C N   1 
ATOM   5387  C CA  . ILE C  1 149 ? 39.666  58.835 -20.997 1.00 49.04  ? 149 ILE C CA  1 
ATOM   5388  C C   . ILE C  1 149 ? 40.596  59.595 -20.043 1.00 48.61  ? 149 ILE C C   1 
ATOM   5389  O O   . ILE C  1 149 ? 40.491  60.837 -19.985 1.00 54.97  ? 149 ILE C O   1 
ATOM   5390  C CB  . ILE C  1 149 ? 38.792  57.822 -20.231 1.00 51.06  ? 149 ILE C CB  1 
ATOM   5391  C CG1 . ILE C  1 149 ? 37.781  57.126 -21.146 1.00 55.18  ? 149 ILE C CG1 1 
ATOM   5392  C CG2 . ILE C  1 149 ? 38.107  58.487 -19.047 1.00 52.03  ? 149 ILE C CG2 1 
ATOM   5393  C CD1 . ILE C  1 149 ? 36.619  57.999 -21.559 1.00 55.50  ? 149 ILE C CD1 1 
ATOM   5394  N N   . VAL C  1 150 ? 41.450  58.872 -19.312 1.00 48.50  ? 150 VAL C N   1 
ATOM   5395  C CA  . VAL C  1 150 ? 42.172  59.379 -18.105 1.00 50.64  ? 150 VAL C CA  1 
ATOM   5396  C C   . VAL C  1 150 ? 43.164  60.475 -18.509 1.00 52.93  ? 150 VAL C C   1 
ATOM   5397  O O   . VAL C  1 150 ? 43.062  61.592 -17.961 1.00 58.97  ? 150 VAL C O   1 
ATOM   5398  C CB  . VAL C  1 150 ? 42.885  58.238 -17.354 1.00 50.87  ? 150 VAL C CB  1 
ATOM   5399  C CG1 . VAL C  1 150 ? 43.662  58.756 -16.153 1.00 51.84  ? 150 VAL C CG1 1 
ATOM   5400  C CG2 . VAL C  1 150 ? 41.913  57.146 -16.933 1.00 50.49  ? 150 VAL C CG2 1 
ATOM   5401  N N   . ILE C  1 151 ? 44.090  60.161 -19.421 1.00 56.76  ? 151 ILE C N   1 
ATOM   5402  C CA  . ILE C  1 151 ? 45.253  61.028 -19.779 1.00 58.09  ? 151 ILE C CA  1 
ATOM   5403  C C   . ILE C  1 151 ? 44.765  62.238 -20.586 1.00 61.95  ? 151 ILE C C   1 
ATOM   5404  O O   . ILE C  1 151 ? 44.259  62.041 -21.708 1.00 58.91  ? 151 ILE C O   1 
ATOM   5405  C CB  . ILE C  1 151 ? 46.320  60.219 -20.542 1.00 57.44  ? 151 ILE C CB  1 
ATOM   5406  C CG1 . ILE C  1 151 ? 46.930  59.125 -19.660 1.00 56.89  ? 151 ILE C CG1 1 
ATOM   5407  C CG2 . ILE C  1 151 ? 47.384  61.141 -21.113 1.00 61.38  ? 151 ILE C CG2 1 
ATOM   5408  C CD1 . ILE C  1 151 ? 47.878  58.204 -20.387 1.00 57.46  ? 151 ILE C CD1 1 
ATOM   5409  N N   . ASP C  1 152 ? 44.928  63.441 -20.025 1.00 72.19  ? 152 ASP C N   1 
ATOM   5410  C CA  . ASP C  1 152 ? 44.607  64.739 -20.677 1.00 77.20  ? 152 ASP C CA  1 
ATOM   5411  C C   . ASP C  1 152 ? 43.190  64.680 -21.259 1.00 74.91  ? 152 ASP C C   1 
ATOM   5412  O O   . ASP C  1 152 ? 43.005  65.129 -22.407 1.00 80.75  ? 152 ASP C O   1 
ATOM   5413  C CB  . ASP C  1 152 ? 45.646  65.083 -21.747 1.00 79.57  ? 152 ASP C CB  1 
ATOM   5414  C CG  . ASP C  1 152 ? 47.055  65.220 -21.199 1.00 84.15  ? 152 ASP C CG  1 
ATOM   5415  O OD1 . ASP C  1 152 ? 47.199  65.760 -20.083 1.00 85.12  ? 152 ASP C OD1 1 
ATOM   5416  O OD2 . ASP C  1 152 ? 47.997  64.779 -21.886 1.00 88.30  ? 152 ASP C OD2 1 
ATOM   5417  N N   . ASN C  1 153 ? 42.239  64.140 -20.491 1.00 69.43  ? 153 ASN C N   1 
ATOM   5418  C CA  . ASN C  1 153 ? 40.793  64.084 -20.838 1.00 67.47  ? 153 ASN C CA  1 
ATOM   5419  C C   . ASN C  1 153 ? 40.619  63.433 -22.216 1.00 62.59  ? 153 ASN C C   1 
ATOM   5420  O O   . ASN C  1 153 ? 39.611  63.728 -22.886 1.00 53.05  ? 153 ASN C O   1 
ATOM   5421  C CB  . ASN C  1 153 ? 40.159  65.475 -20.776 1.00 66.25  ? 153 ASN C CB  1 
ATOM   5422  C CG  . ASN C  1 153 ? 40.484  66.198 -19.486 1.00 63.57  ? 153 ASN C CG  1 
ATOM   5423  O OD1 . ASN C  1 153 ? 40.757  65.567 -18.470 1.00 72.86  ? 153 ASN C OD1 1 
ATOM   5424  N ND2 . ASN C  1 153 ? 40.467  67.519 -19.518 1.00 70.07  ? 153 ASN C ND2 1 
ATOM   5425  N N   . GLY C  1 154 ? 41.572  62.580 -22.608 1.00 64.42  ? 154 GLY C N   1 
ATOM   5426  C CA  . GLY C  1 154 ? 41.517  61.753 -23.829 1.00 69.38  ? 154 GLY C CA  1 
ATOM   5427  C C   . GLY C  1 154 ? 41.648  62.581 -25.094 1.00 67.47  ? 154 GLY C C   1 
ATOM   5428  O O   . GLY C  1 154 ? 41.099  62.158 -26.128 1.00 76.72  ? 154 GLY C O   1 
ATOM   5429  N N   . THR C  1 155 ? 42.352  63.715 -25.020 1.00 65.75  ? 155 THR C N   1 
ATOM   5430  C CA  . THR C  1 155 ? 42.577  64.650 -26.156 1.00 70.80  ? 155 THR C CA  1 
ATOM   5431  C C   . THR C  1 155 ? 43.989  64.445 -26.720 1.00 72.40  ? 155 THR C C   1 
ATOM   5432  O O   . THR C  1 155 ? 44.186  64.702 -27.925 1.00 79.41  ? 155 THR C O   1 
ATOM   5433  C CB  . THR C  1 155 ? 42.334  66.103 -25.728 1.00 63.78  ? 155 THR C CB  1 
ATOM   5434  O OG1 . THR C  1 155 ? 43.174  66.385 -24.609 1.00 62.37  ? 155 THR C OG1 1 
ATOM   5435  C CG2 . THR C  1 155 ? 40.891  66.376 -25.364 1.00 62.06  ? 155 THR C CG2 1 
ATOM   5436  N N   . ASN C  1 156 ? 44.925  63.994 -25.880 1.00 70.34  ? 156 ASN C N   1 
ATOM   5437  C CA  . ASN C  1 156 ? 46.344  63.738 -26.249 1.00 73.51  ? 156 ASN C CA  1 
ATOM   5438  C C   . ASN C  1 156 ? 46.410  62.564 -27.235 1.00 74.94  ? 156 ASN C C   1 
ATOM   5439  O O   . ASN C  1 156 ? 46.209  61.412 -26.796 1.00 74.51  ? 156 ASN C O   1 
ATOM   5440  C CB  . ASN C  1 156 ? 47.203  63.471 -25.011 1.00 73.84  ? 156 ASN C CB  1 
ATOM   5441  C CG  . ASN C  1 156 ? 48.644  63.150 -25.348 1.00 81.40  ? 156 ASN C CG  1 
ATOM   5442  O OD1 . ASN C  1 156 ? 48.941  62.666 -26.438 1.00 90.96  ? 156 ASN C OD1 1 
ATOM   5443  N ND2 . ASN C  1 156 ? 49.545  63.410 -24.415 1.00 84.97  ? 156 ASN C ND2 1 
ATOM   5444  N N   . THR C  1 157 ? 46.695  62.850 -28.510 1.00 71.51  ? 157 THR C N   1 
ATOM   5445  C CA  . THR C  1 157 ? 46.740  61.857 -29.619 1.00 75.49  ? 157 THR C CA  1 
ATOM   5446  C C   . THR C  1 157 ? 47.914  60.892 -29.412 1.00 70.57  ? 157 THR C C   1 
ATOM   5447  O O   . THR C  1 157 ? 47.804  59.730 -29.855 1.00 67.78  ? 157 THR C O   1 
ATOM   5448  C CB  . THR C  1 157 ? 46.828  62.548 -30.986 1.00 82.00  ? 157 THR C CB  1 
ATOM   5449  O OG1 . THR C  1 157 ? 45.874  63.611 -31.021 1.00 84.65  ? 157 THR C OG1 1 
ATOM   5450  C CG2 . THR C  1 157 ? 46.571  61.599 -32.137 1.00 83.14  ? 157 THR C CG2 1 
ATOM   5451  N N   . GLY C  1 158 ? 48.993  61.357 -28.775 1.00 65.66  ? 158 GLY C N   1 
ATOM   5452  C CA  . GLY C  1 158 ? 50.170  60.532 -28.439 1.00 68.42  ? 158 GLY C CA  1 
ATOM   5453  C C   . GLY C  1 158 ? 49.789  59.358 -27.553 1.00 71.62  ? 158 GLY C C   1 
ATOM   5454  O O   . GLY C  1 158 ? 49.903  58.203 -28.014 1.00 69.02  ? 158 GLY C O   1 
ATOM   5455  N N   . ALA C  1 159 ? 49.338  59.650 -26.328 1.00 74.52  ? 159 ALA C N   1 
ATOM   5456  C CA  . ALA C  1 159 ? 48.904  58.668 -25.307 1.00 67.99  ? 159 ALA C CA  1 
ATOM   5457  C C   . ALA C  1 159 ? 47.792  57.782 -25.882 1.00 63.03  ? 159 ALA C C   1 
ATOM   5458  O O   . ALA C  1 159 ? 47.858  56.550 -25.696 1.00 53.44  ? 159 ALA C O   1 
ATOM   5459  C CB  . ALA C  1 159 ? 48.441  59.392 -24.066 1.00 63.78  ? 159 ALA C CB  1 
ATOM   5460  N N   . PHE C  1 160 ? 46.812  58.400 -26.549 1.00 62.12  ? 160 PHE C N   1 
ATOM   5461  C CA  . PHE C  1 160 ? 45.645  57.728 -27.179 1.00 63.14  ? 160 PHE C CA  1 
ATOM   5462  C C   . PHE C  1 160 ? 46.127  56.525 -27.995 1.00 65.65  ? 160 PHE C C   1 
ATOM   5463  O O   . PHE C  1 160 ? 45.570  55.422 -27.826 1.00 65.31  ? 160 PHE C O   1 
ATOM   5464  C CB  . PHE C  1 160 ? 44.875  58.712 -28.062 1.00 60.44  ? 160 PHE C CB  1 
ATOM   5465  C CG  . PHE C  1 160 ? 43.568  58.186 -28.601 1.00 62.97  ? 160 PHE C CG  1 
ATOM   5466  C CD1 . PHE C  1 160 ? 43.492  57.633 -29.869 1.00 59.96  ? 160 PHE C CD1 1 
ATOM   5467  C CD2 . PHE C  1 160 ? 42.411  58.253 -27.840 1.00 66.85  ? 160 PHE C CD2 1 
ATOM   5468  C CE1 . PHE C  1 160 ? 42.287  57.158 -30.365 1.00 59.61  ? 160 PHE C CE1 1 
ATOM   5469  C CE2 . PHE C  1 160 ? 41.208  57.778 -28.337 1.00 68.19  ? 160 PHE C CE2 1 
ATOM   5470  C CZ  . PHE C  1 160 ? 41.148  57.231 -29.598 1.00 63.74  ? 160 PHE C CZ  1 
ATOM   5471  N N   . ILE C  1 161 ? 47.134  56.740 -28.848 1.00 67.88  ? 161 ILE C N   1 
ATOM   5472  C CA  . ILE C  1 161 ? 47.693  55.710 -29.773 1.00 63.14  ? 161 ILE C CA  1 
ATOM   5473  C C   . ILE C  1 161 ? 48.671  54.819 -28.999 1.00 60.41  ? 161 ILE C C   1 
ATOM   5474  O O   . ILE C  1 161 ? 48.603  53.586 -29.169 1.00 51.08  ? 161 ILE C O   1 
ATOM   5475  C CB  . ILE C  1 161 ? 48.359  56.367 -30.998 1.00 60.92  ? 161 ILE C CB  1 
ATOM   5476  C CG1 . ILE C  1 161 ? 47.344  57.146 -31.840 1.00 69.08  ? 161 ILE C CG1 1 
ATOM   5477  C CG2 . ILE C  1 161 ? 49.099  55.328 -31.826 1.00 60.07  ? 161 ILE C CG2 1 
ATOM   5478  C CD1 . ILE C  1 161 ? 47.847  57.536 -33.209 1.00 74.80  ? 161 ILE C CD1 1 
ATOM   5479  N N   . LEU C  1 162 ? 49.543  55.423 -28.186 1.00 59.78  ? 162 LEU C N   1 
ATOM   5480  C CA  . LEU C  1 162 ? 50.561  54.701 -27.376 1.00 65.57  ? 162 LEU C CA  1 
ATOM   5481  C C   . LEU C  1 162 ? 49.880  53.551 -26.625 1.00 66.07  ? 162 LEU C C   1 
ATOM   5482  O O   . LEU C  1 162 ? 50.201  52.381 -26.912 1.00 62.21  ? 162 LEU C O   1 
ATOM   5483  C CB  . LEU C  1 162 ? 51.222  55.680 -26.397 1.00 72.72  ? 162 LEU C CB  1 
ATOM   5484  C CG  . LEU C  1 162 ? 52.536  55.208 -25.770 1.00 73.39  ? 162 LEU C CG  1 
ATOM   5485  C CD1 . LEU C  1 162 ? 52.813  55.942 -24.466 1.00 73.25  ? 162 LEU C CD1 1 
ATOM   5486  C CD2 . LEU C  1 162 ? 52.531  53.706 -25.533 1.00 70.58  ? 162 LEU C CD2 1 
ATOM   5487  N N   . TRP C  1 163 ? 48.968  53.885 -25.707 1.00 66.38  ? 163 TRP C N   1 
ATOM   5488  C CA  . TRP C  1 163 ? 48.359  52.943 -24.729 1.00 61.68  ? 163 TRP C CA  1 
ATOM   5489  C C   . TRP C  1 163 ? 47.445  51.942 -25.443 1.00 60.69  ? 163 TRP C C   1 
ATOM   5490  O O   . TRP C  1 163 ? 47.311  50.808 -24.939 1.00 60.58  ? 163 TRP C O   1 
ATOM   5491  C CB  . TRP C  1 163 ? 47.623  53.722 -23.636 1.00 62.36  ? 163 TRP C CB  1 
ATOM   5492  C CG  . TRP C  1 163 ? 48.551  54.389 -22.670 1.00 64.90  ? 163 TRP C CG  1 
ATOM   5493  C CD1 . TRP C  1 163 ? 48.939  55.697 -22.669 1.00 66.96  ? 163 TRP C CD1 1 
ATOM   5494  C CD2 . TRP C  1 163 ? 49.237  53.766 -21.568 1.00 66.35  ? 163 TRP C CD2 1 
ATOM   5495  N NE1 . TRP C  1 163 ? 49.804  55.935 -21.635 1.00 68.53  ? 163 TRP C NE1 1 
ATOM   5496  C CE2 . TRP C  1 163 ? 50.005  54.771 -20.942 1.00 65.78  ? 163 TRP C CE2 1 
ATOM   5497  C CE3 . TRP C  1 163 ? 49.268  52.469 -21.045 1.00 65.03  ? 163 TRP C CE3 1 
ATOM   5498  C CZ2 . TRP C  1 163 ? 50.795  54.512 -19.823 1.00 65.50  ? 163 TRP C CZ2 1 
ATOM   5499  C CZ3 . TRP C  1 163 ? 50.049  52.215 -19.939 1.00 61.58  ? 163 TRP C CZ3 1 
ATOM   5500  C CH2 . TRP C  1 163 ? 50.801  53.224 -19.338 1.00 63.39  ? 163 TRP C CH2 1 
ATOM   5501  N N   . ALA C  1 164 ? 46.846  52.341 -26.568 1.00 58.38  ? 164 ALA C N   1 
ATOM   5502  C CA  . ALA C  1 164 ? 46.068  51.450 -27.458 1.00 62.60  ? 164 ALA C CA  1 
ATOM   5503  C C   . ALA C  1 164 ? 46.968  50.297 -27.919 1.00 69.54  ? 164 ALA C C   1 
ATOM   5504  O O   . ALA C  1 164 ? 46.474  49.156 -28.022 1.00 74.15  ? 164 ALA C O   1 
ATOM   5505  C CB  . ALA C  1 164 ? 45.524  52.231 -28.628 1.00 60.42  ? 164 ALA C CB  1 
ATOM   5506  N N   . VAL C  1 165 ? 48.246  50.594 -28.178 1.00 68.76  ? 165 VAL C N   1 
ATOM   5507  C CA  . VAL C  1 165 ? 49.276  49.611 -28.628 1.00 64.55  ? 165 VAL C CA  1 
ATOM   5508  C C   . VAL C  1 165 ? 49.650  48.722 -27.437 1.00 57.49  ? 165 VAL C C   1 
ATOM   5509  O O   . VAL C  1 165 ? 49.586  47.486 -27.584 1.00 51.58  ? 165 VAL C O   1 
ATOM   5510  C CB  . VAL C  1 165 ? 50.511  50.317 -29.220 1.00 68.24  ? 165 VAL C CB  1 
ATOM   5511  C CG1 . VAL C  1 165 ? 51.683  49.362 -29.391 1.00 67.22  ? 165 VAL C CG1 1 
ATOM   5512  C CG2 . VAL C  1 165 ? 50.186  51.007 -30.537 1.00 63.22  ? 165 VAL C CG2 1 
ATOM   5513  N N   . ILE C  1 166 ? 50.027  49.333 -26.309 1.00 54.88  ? 166 ILE C N   1 
ATOM   5514  C CA  . ILE C  1 166 ? 50.310  48.619 -25.028 1.00 59.06  ? 166 ILE C CA  1 
ATOM   5515  C C   . ILE C  1 166 ? 49.144  47.665 -24.751 1.00 58.42  ? 166 ILE C C   1 
ATOM   5516  O O   . ILE C  1 166 ? 49.401  46.497 -24.407 1.00 63.03  ? 166 ILE C O   1 
ATOM   5517  C CB  . ILE C  1 166 ? 50.525  49.609 -23.867 1.00 59.37  ? 166 ILE C CB  1 
ATOM   5518  C CG1 . ILE C  1 166 ? 51.706  50.545 -24.138 1.00 65.34  ? 166 ILE C CG1 1 
ATOM   5519  C CG2 . ILE C  1 166 ? 50.684  48.862 -22.551 1.00 56.58  ? 166 ILE C CG2 1 
ATOM   5520  C CD1 . ILE C  1 166 ? 52.064  51.444 -22.976 1.00 66.05  ? 166 ILE C CD1 1 
ATOM   5521  N N   . SER C  1 167 ? 47.913  48.158 -24.905 1.00 60.13  ? 167 SER C N   1 
ATOM   5522  C CA  . SER C  1 167 ? 46.658  47.373 -24.776 1.00 58.65  ? 167 SER C CA  1 
ATOM   5523  C C   . SER C  1 167 ? 46.725  46.143 -25.690 1.00 55.81  ? 167 SER C C   1 
ATOM   5524  O O   . SER C  1 167 ? 46.572  45.018 -25.176 1.00 52.91  ? 167 SER C O   1 
ATOM   5525  C CB  . SER C  1 167 ? 45.456  48.231 -25.081 1.00 58.39  ? 167 SER C CB  1 
ATOM   5526  O OG  . SER C  1 167 ? 44.263  47.460 -25.072 1.00 64.37  ? 167 SER C OG  1 
ATOM   5527  N N   . CYS C  1 168 ? 46.964  46.356 -26.989 1.00 57.41  ? 168 CYS C N   1 
ATOM   5528  C CA  . CYS C  1 168 ? 47.004  45.299 -28.039 1.00 59.26  ? 168 CYS C CA  1 
ATOM   5529  C C   . CYS C  1 168 ? 48.023  44.217 -27.667 1.00 53.50  ? 168 CYS C C   1 
ATOM   5530  O O   . CYS C  1 168 ? 47.778  43.041 -28.000 1.00 50.64  ? 168 CYS C O   1 
ATOM   5531  C CB  . CYS C  1 168 ? 47.351  45.880 -29.404 1.00 63.80  ? 168 CYS C CB  1 
ATOM   5532  S SG  . CYS C  1 168 ? 46.025  46.894 -30.106 1.00 73.77  ? 168 CYS C SG  1 
ATOM   5533  N N   . VAL C  1 169 ? 49.128  44.603 -27.023 1.00 50.30  ? 169 VAL C N   1 
ATOM   5534  C CA  . VAL C  1 169 ? 50.149  43.655 -26.489 1.00 57.09  ? 169 VAL C CA  1 
ATOM   5535  C C   . VAL C  1 169 ? 49.422  42.636 -25.607 1.00 59.91  ? 169 VAL C C   1 
ATOM   5536  O O   . VAL C  1 169 ? 49.449  41.433 -25.937 1.00 57.30  ? 169 VAL C O   1 
ATOM   5537  C CB  . VAL C  1 169 ? 51.258  44.388 -25.709 1.00 59.31  ? 169 VAL C CB  1 
ATOM   5538  C CG1 . VAL C  1 169 ? 52.086  43.428 -24.867 1.00 56.91  ? 169 VAL C CG1 1 
ATOM   5539  C CG2 . VAL C  1 169 ? 52.151  45.202 -26.633 1.00 59.78  ? 169 VAL C CG2 1 
ATOM   5540  N N   . PHE C  1 170 ? 48.781  43.117 -24.538 1.00 60.78  ? 170 PHE C N   1 
ATOM   5541  C CA  . PHE C  1 170 ? 47.990  42.306 -23.576 1.00 56.14  ? 170 PHE C CA  1 
ATOM   5542  C C   . PHE C  1 170 ? 46.927  41.509 -24.340 1.00 54.01  ? 170 PHE C C   1 
ATOM   5543  O O   . PHE C  1 170 ? 46.733  40.321 -24.023 1.00 53.17  ? 170 PHE C O   1 
ATOM   5544  C CB  . PHE C  1 170 ? 47.372  43.203 -22.502 1.00 54.47  ? 170 PHE C CB  1 
ATOM   5545  C CG  . PHE C  1 170 ? 48.362  43.792 -21.529 1.00 60.13  ? 170 PHE C CG  1 
ATOM   5546  C CD1 . PHE C  1 170 ? 49.042  42.983 -20.631 1.00 61.72  ? 170 PHE C CD1 1 
ATOM   5547  C CD2 . PHE C  1 170 ? 48.609  45.155 -21.504 1.00 62.57  ? 170 PHE C CD2 1 
ATOM   5548  C CE1 . PHE C  1 170 ? 49.951  43.525 -19.735 1.00 59.39  ? 170 PHE C CE1 1 
ATOM   5549  C CE2 . PHE C  1 170 ? 49.517  45.696 -20.607 1.00 60.67  ? 170 PHE C CE2 1 
ATOM   5550  C CZ  . PHE C  1 170 ? 50.186  44.880 -19.724 1.00 60.00  ? 170 PHE C CZ  1 
ATOM   5551  N N   . TRP C  1 171 ? 46.267  42.142 -25.315 1.00 51.76  ? 171 TRP C N   1 
ATOM   5552  C CA  . TRP C  1 171 ? 45.218  41.515 -26.164 1.00 61.36  ? 171 TRP C CA  1 
ATOM   5553  C C   . TRP C  1 171 ? 45.755  40.204 -26.748 1.00 64.77  ? 171 TRP C C   1 
ATOM   5554  O O   . TRP C  1 171 ? 45.092  39.163 -26.580 1.00 64.38  ? 171 TRP C O   1 
ATOM   5555  C CB  . TRP C  1 171 ? 44.750  42.471 -27.270 1.00 64.74  ? 171 TRP C CB  1 
ATOM   5556  C CG  . TRP C  1 171 ? 43.630  41.930 -28.106 1.00 65.80  ? 171 TRP C CG  1 
ATOM   5557  C CD1 . TRP C  1 171 ? 42.650  41.066 -27.707 1.00 71.53  ? 171 TRP C CD1 1 
ATOM   5558  C CD2 . TRP C  1 171 ? 43.346  42.240 -29.482 1.00 71.61  ? 171 TRP C CD2 1 
ATOM   5559  N NE1 . TRP C  1 171 ? 41.791  40.805 -28.739 1.00 71.48  ? 171 TRP C NE1 1 
ATOM   5560  C CE2 . TRP C  1 171 ? 42.188  41.515 -29.840 1.00 71.92  ? 171 TRP C CE2 1 
ATOM   5561  C CE3 . TRP C  1 171 ? 43.952  43.054 -30.446 1.00 78.02  ? 171 TRP C CE3 1 
ATOM   5562  C CZ2 . TRP C  1 171 ? 41.633  41.577 -31.117 1.00 70.12  ? 171 TRP C CZ2 1 
ATOM   5563  C CZ3 . TRP C  1 171 ? 43.402  43.116 -31.708 1.00 82.89  ? 171 TRP C CZ3 1 
ATOM   5564  C CH2 . TRP C  1 171 ? 42.258  42.386 -32.037 1.00 77.31  ? 171 TRP C CH2 1 
ATOM   5565  N N   . VAL C  1 172 ? 46.917  40.262 -27.403 1.00 67.65  ? 172 VAL C N   1 
ATOM   5566  C CA  . VAL C  1 172 ? 47.569  39.094 -28.064 1.00 64.22  ? 172 VAL C CA  1 
ATOM   5567  C C   . VAL C  1 172 ? 47.871  38.032 -27.000 1.00 60.83  ? 172 VAL C C   1 
ATOM   5568  O O   . VAL C  1 172 ? 47.470  36.871 -27.202 1.00 68.46  ? 172 VAL C O   1 
ATOM   5569  C CB  . VAL C  1 172 ? 48.839  39.517 -28.827 1.00 67.28  ? 172 VAL C CB  1 
ATOM   5570  C CG1 . VAL C  1 172 ? 49.621  38.314 -29.331 1.00 67.88  ? 172 VAL C CG1 1 
ATOM   5571  C CG2 . VAL C  1 172 ? 48.512  40.465 -29.971 1.00 62.09  ? 172 VAL C CG2 1 
ATOM   5572  N N   . ILE C  1 173 ? 48.540  38.420 -25.910 1.00 54.36  ? 173 ILE C N   1 
ATOM   5573  C CA  . ILE C  1 173 ? 48.878  37.516 -24.769 1.00 54.98  ? 173 ILE C CA  1 
ATOM   5574  C C   . ILE C  1 173 ? 47.637  36.683 -24.427 1.00 63.49  ? 173 ILE C C   1 
ATOM   5575  O O   . ILE C  1 173 ? 47.773  35.452 -24.291 1.00 68.98  ? 173 ILE C O   1 
ATOM   5576  C CB  . ILE C  1 173 ? 49.377  38.312 -23.547 1.00 51.56  ? 173 ILE C CB  1 
ATOM   5577  C CG1 . ILE C  1 173 ? 50.636  39.120 -23.869 1.00 51.25  ? 173 ILE C CG1 1 
ATOM   5578  C CG2 . ILE C  1 173 ? 49.590  37.388 -22.357 1.00 47.99  ? 173 ILE C CG2 1 
ATOM   5579  C CD1 . ILE C  1 173 ? 51.122  39.984 -22.727 1.00 52.90  ? 173 ILE C CD1 1 
ATOM   5580  N N   . ALA C  1 174 ? 46.480  37.340 -24.296 1.00 66.65  ? 174 ALA C N   1 
ATOM   5581  C CA  . ALA C  1 174 ? 45.173  36.715 -23.979 1.00 69.60  ? 174 ALA C CA  1 
ATOM   5582  C C   . ALA C  1 174 ? 44.808  35.707 -25.074 1.00 68.50  ? 174 ALA C C   1 
ATOM   5583  O O   . ALA C  1 174 ? 44.660  34.512 -24.750 1.00 66.84  ? 174 ALA C O   1 
ATOM   5584  C CB  . ALA C  1 174 ? 44.111  37.777 -23.833 1.00 70.42  ? 174 ALA C CB  1 
ATOM   5585  N N   . ASN C  1 175 ? 44.673  36.181 -26.318 1.00 63.72  ? 175 ASN C N   1 
ATOM   5586  C CA  . ASN C  1 175 ? 44.325  35.354 -27.506 1.00 65.89  ? 175 ASN C CA  1 
ATOM   5587  C C   . ASN C  1 175 ? 45.175  34.080 -27.498 1.00 65.71  ? 175 ASN C C   1 
ATOM   5588  O O   . ASN C  1 175 ? 44.596  32.986 -27.620 1.00 71.81  ? 175 ASN C O   1 
ATOM   5589  C CB  . ASN C  1 175 ? 44.510  36.129 -28.812 1.00 68.76  ? 175 ASN C CB  1 
ATOM   5590  C CG  . ASN C  1 175 ? 43.381  37.099 -29.088 1.00 74.74  ? 175 ASN C CG  1 
ATOM   5591  O OD1 . ASN C  1 175 ? 42.220  36.801 -28.818 1.00 69.56  ? 175 ASN C OD1 1 
ATOM   5592  N ND2 . ASN C  1 175 ? 43.709  38.259 -29.633 1.00 85.89  ? 175 ASN C ND2 1 
ATOM   5593  N N   . VAL C  1 176 ? 46.495  34.229 -27.356 1.00 64.77  ? 176 VAL C N   1 
ATOM   5594  C CA  . VAL C  1 176 ? 47.475  33.103 -27.311 1.00 66.17  ? 176 VAL C CA  1 
ATOM   5595  C C   . VAL C  1 176 ? 47.036  32.110 -26.229 1.00 72.44  ? 176 VAL C C   1 
ATOM   5596  O O   . VAL C  1 176 ? 46.667  30.974 -26.584 1.00 80.27  ? 176 VAL C O   1 
ATOM   5597  C CB  . VAL C  1 176 ? 48.906  33.616 -27.057 1.00 59.47  ? 176 VAL C CB  1 
ATOM   5598  C CG1 . VAL C  1 176 ? 49.845  32.494 -26.643 1.00 58.15  ? 176 VAL C CG1 1 
ATOM   5599  C CG2 . VAL C  1 176 ? 49.458  34.361 -28.263 1.00 56.63  ? 176 VAL C CG2 1 
ATOM   5600  N N   . VAL C  1 177 ? 47.067  32.535 -24.962 1.00 70.65  ? 177 VAL C N   1 
ATOM   5601  C CA  . VAL C  1 177 ? 46.755  31.688 -23.771 1.00 70.61  ? 177 VAL C CA  1 
ATOM   5602  C C   . VAL C  1 177 ? 45.460  30.909 -24.030 1.00 73.20  ? 177 VAL C C   1 
ATOM   5603  O O   . VAL C  1 177 ? 45.458  29.680 -23.807 1.00 84.15  ? 177 VAL C O   1 
ATOM   5604  C CB  . VAL C  1 177 ? 46.645  32.531 -22.487 1.00 68.53  ? 177 VAL C CB  1 
ATOM   5605  C CG1 . VAL C  1 177 ? 46.215  31.682 -21.298 1.00 68.03  ? 177 VAL C CG1 1 
ATOM   5606  C CG2 . VAL C  1 177 ? 47.941  33.263 -22.182 1.00 68.90  ? 177 VAL C CG2 1 
ATOM   5607  N N   . LEU C  1 178 ? 44.405  31.599 -24.475 1.00 67.64  ? 178 LEU C N   1 
ATOM   5608  C CA  . LEU C  1 178 ? 43.057  31.014 -24.712 1.00 71.65  ? 178 LEU C CA  1 
ATOM   5609  C C   . LEU C  1 178 ? 43.130  30.010 -25.869 1.00 66.29  ? 178 LEU C C   1 
ATOM   5610  O O   . LEU C  1 178 ? 42.705  28.855 -25.675 1.00 63.97  ? 178 LEU C O   1 
ATOM   5611  C CB  . LEU C  1 178 ? 42.060  32.138 -25.018 1.00 76.45  ? 178 LEU C CB  1 
ATOM   5612  C CG  . LEU C  1 178 ? 41.695  33.039 -23.838 1.00 77.51  ? 178 LEU C CG  1 
ATOM   5613  C CD1 . LEU C  1 178 ? 40.792  34.179 -24.282 1.00 82.74  ? 178 LEU C CD1 1 
ATOM   5614  C CD2 . LEU C  1 178 ? 41.032  32.241 -22.726 1.00 74.39  ? 178 LEU C CD2 1 
ATOM   5615  N N   . ILE C  1 179 ? 43.649  30.442 -27.021 1.00 65.36  ? 179 ILE C N   1 
ATOM   5616  C CA  . ILE C  1 179 ? 43.764  29.618 -28.261 1.00 61.76  ? 179 ILE C CA  1 
ATOM   5617  C C   . ILE C  1 179 ? 44.551  28.342 -27.943 1.00 59.04  ? 179 ILE C C   1 
ATOM   5618  O O   . ILE C  1 179 ? 44.079  27.258 -28.320 1.00 54.68  ? 179 ILE C O   1 
ATOM   5619  C CB  . ILE C  1 179 ? 44.406  30.430 -29.403 1.00 58.18  ? 179 ILE C CB  1 
ATOM   5620  C CG1 . ILE C  1 179 ? 43.441  31.492 -29.938 1.00 59.20  ? 179 ILE C CG1 1 
ATOM   5621  C CG2 . ILE C  1 179 ? 44.903  29.509 -30.506 1.00 60.62  ? 179 ILE C CG2 1 
ATOM   5622  C CD1 . ILE C  1 179 ? 44.089  32.523 -30.832 1.00 59.02  ? 179 ILE C CD1 1 
ATOM   5623  N N   . ARG C  1 180 ? 45.701  28.472 -27.273 1.00 58.96  ? 180 ARG C N   1 
ATOM   5624  C CA  . ARG C  1 180 ? 46.547  27.324 -26.846 1.00 63.04  ? 180 ARG C CA  1 
ATOM   5625  C C   . ARG C  1 180 ? 45.689  26.354 -26.024 1.00 73.18  ? 180 ARG C C   1 
ATOM   5626  O O   . ARG C  1 180 ? 45.616  25.167 -26.398 1.00 80.39  ? 180 ARG C O   1 
ATOM   5627  C CB  . ARG C  1 180 ? 47.755  27.809 -26.038 1.00 58.01  ? 180 ARG C CB  1 
ATOM   5628  N N   . ALA C  1 181 ? 45.057  26.853 -24.958 1.00 77.70  ? 181 ALA C N   1 
ATOM   5629  C CA  . ALA C  1 181 ? 44.248  26.070 -23.993 1.00 74.21  ? 181 ALA C CA  1 
ATOM   5630  C C   . ALA C  1 181 ? 43.104  25.352 -24.718 1.00 66.65  ? 181 ALA C C   1 
ATOM   5631  O O   . ALA C  1 181 ? 42.761  24.227 -24.305 1.00 63.94  ? 181 ALA C O   1 
ATOM   5632  C CB  . ALA C  1 181 ? 43.726  26.977 -22.906 1.00 82.61  ? 181 ALA C CB  1 
ATOM   5633  N N   . VAL C  1 182 ? 42.530  25.983 -25.748 1.00 61.53  ? 182 VAL C N   1 
ATOM   5634  C CA  . VAL C  1 182 ? 41.406  25.421 -26.558 1.00 66.54  ? 182 VAL C CA  1 
ATOM   5635  C C   . VAL C  1 182 ? 41.964  24.328 -27.474 1.00 68.18  ? 182 VAL C C   1 
ATOM   5636  O O   . VAL C  1 182 ? 41.406  23.220 -27.477 1.00 72.81  ? 182 VAL C O   1 
ATOM   5637  C CB  . VAL C  1 182 ? 40.680  26.509 -27.374 1.00 70.54  ? 182 VAL C CB  1 
ATOM   5638  C CG1 . VAL C  1 182 ? 39.646  25.907 -28.314 1.00 67.97  ? 182 VAL C CG1 1 
ATOM   5639  C CG2 . VAL C  1 182 ? 40.039  27.559 -26.481 1.00 70.51  ? 182 VAL C CG2 1 
ATOM   5640  N N   . ARG C  1 183 ? 43.025  24.648 -28.220 1.00 76.29  ? 183 ARG C N   1 
ATOM   5641  C CA  . ARG C  1 183 ? 43.690  23.748 -29.201 1.00 80.13  ? 183 ARG C CA  1 
ATOM   5642  C C   . ARG C  1 183 ? 44.114  22.449 -28.503 1.00 79.00  ? 183 ARG C C   1 
ATOM   5643  O O   . ARG C  1 183 ? 44.116  21.403 -29.177 1.00 81.10  ? 183 ARG C O   1 
ATOM   5644  C CB  . ARG C  1 183 ? 44.882  24.479 -29.829 1.00 83.73  ? 183 ARG C CB  1 
ATOM   5645  C CG  . ARG C  1 183 ? 45.553  23.753 -30.985 1.00 94.76  ? 183 ARG C CG  1 
ATOM   5646  C CD  . ARG C  1 183 ? 46.650  24.602 -31.602 1.00 102.68 ? 183 ARG C CD  1 
ATOM   5647  N NE  . ARG C  1 183 ? 47.533  25.181 -30.596 1.00 118.03 ? 183 ARG C NE  1 
ATOM   5648  C CZ  . ARG C  1 183 ? 48.406  26.157 -30.827 1.00 119.26 ? 183 ARG C CZ  1 
ATOM   5649  N NH1 . ARG C  1 183 ? 48.518  26.674 -32.038 1.00 122.21 ? 183 ARG C NH1 1 
ATOM   5650  N NH2 . ARG C  1 183 ? 49.162  26.615 -29.844 1.00 112.54 ? 183 ARG C NH2 1 
ATOM   5651  N N   . GLN C  1 184 ? 44.453  22.518 -27.210 1.00 78.53  ? 184 GLN C N   1 
ATOM   5652  C CA  . GLN C  1 184 ? 44.895  21.358 -26.388 1.00 81.15  ? 184 GLN C CA  1 
ATOM   5653  C C   . GLN C  1 184 ? 43.686  20.492 -26.020 1.00 83.52  ? 184 GLN C C   1 
ATOM   5654  O O   . GLN C  1 184 ? 43.839  19.257 -25.959 1.00 91.55  ? 184 GLN C O   1 
ATOM   5655  C CB  . GLN C  1 184 ? 45.582  21.823 -25.102 1.00 81.92  ? 184 GLN C CB  1 
ATOM   5656  C CG  . GLN C  1 184 ? 46.887  22.570 -25.327 1.00 90.65  ? 184 GLN C CG  1 
ATOM   5657  C CD  . GLN C  1 184 ? 47.477  23.046 -24.022 1.00 99.09  ? 184 GLN C CD  1 
ATOM   5658  O OE1 . GLN C  1 184 ? 47.143  22.545 -22.951 1.00 97.59  ? 184 GLN C OE1 1 
ATOM   5659  N NE2 . GLN C  1 184 ? 48.365  24.025 -24.102 1.00 104.64 ? 184 GLN C NE2 1 
ATOM   5660  N N   . SER C  1 185 ? 42.539  21.126 -25.763 1.00 91.37  ? 185 SER C N   1 
ATOM   5661  C CA  . SER C  1 185 ? 41.289  20.472 -25.294 1.00 101.20 ? 185 SER C CA  1 
ATOM   5662  C C   . SER C  1 185 ? 40.628  19.709 -26.448 1.00 110.40 ? 185 SER C C   1 
ATOM   5663  O O   . SER C  1 185 ? 40.222  18.556 -26.229 1.00 134.66 ? 185 SER C O   1 
ATOM   5664  C CB  . SER C  1 185 ? 40.347  21.480 -24.687 1.00 101.16 ? 185 SER C CB  1 
ATOM   5665  O OG  . SER C  1 185 ? 40.922  22.081 -23.536 1.00 109.49 ? 185 SER C OG  1 
ATOM   5666  N N   . LEU C  1 186 ? 40.545  20.329 -27.630 1.00 112.90 ? 186 LEU C N   1 
ATOM   5667  C CA  . LEU C  1 186 ? 39.788  19.823 -28.810 1.00 106.48 ? 186 LEU C CA  1 
ATOM   5668  C C   . LEU C  1 186 ? 40.144  18.363 -29.090 1.00 111.55 ? 186 LEU C C   1 
ATOM   5669  O O   . LEU C  1 186 ? 39.265  17.555 -29.385 1.00 115.90 ? 186 LEU C O   1 
ATOM   5670  C CB  . LEU C  1 186 ? 40.091  20.721 -30.014 1.00 103.76 ? 186 LEU C CB  1 
ATOM   5671  C CG  . LEU C  1 186 ? 39.504  22.130 -29.935 1.00 105.76 ? 186 LEU C CG  1 
ATOM   5672  C CD1 . LEU C  1 186 ? 39.921  22.965 -31.137 1.00 107.34 ? 186 LEU C CD1 1 
ATOM   5673  C CD2 . LEU C  1 186 ? 37.987  22.079 -29.820 1.00 111.39 ? 186 LEU C CD2 1 
ATOM   5674  N N   . PRO C  1 187 ? 41.438  17.974 -29.029 1.00 113.30 ? 187 PRO C N   1 
ATOM   5675  C CA  . PRO C  1 187 ? 41.833  16.581 -29.237 1.00 108.81 ? 187 PRO C CA  1 
ATOM   5676  C C   . PRO C  1 187 ? 41.187  15.593 -28.253 1.00 103.40 ? 187 PRO C C   1 
ATOM   5677  O O   . PRO C  1 187 ? 40.770  14.538 -28.693 1.00 92.83  ? 187 PRO C O   1 
ATOM   5678  C CB  . PRO C  1 187 ? 43.356  16.596 -29.028 1.00 110.75 ? 187 PRO C CB  1 
ATOM   5679  C CG  . PRO C  1 187 ? 43.758  18.029 -29.302 1.00 111.76 ? 187 PRO C CG  1 
ATOM   5680  C CD  . PRO C  1 187 ? 42.591  18.857 -28.804 1.00 118.99 ? 187 PRO C CD  1 
ATOM   5681  N N   . THR C  1 188 ? 41.120  15.954 -26.965 1.00 106.09 ? 188 THR C N   1 
ATOM   5682  C CA  . THR C  1 188 ? 40.681  15.068 -25.850 1.00 102.14 ? 188 THR C CA  1 
ATOM   5683  C C   . THR C  1 188 ? 39.147  14.996 -25.803 1.00 93.11  ? 188 THR C C   1 
ATOM   5684  O O   . THR C  1 188 ? 38.627  14.105 -25.103 1.00 86.59  ? 188 THR C O   1 
ATOM   5685  C CB  . THR C  1 188 ? 41.248  15.532 -24.499 1.00 98.34  ? 188 THR C CB  1 
ATOM   5686  O OG1 . THR C  1 188 ? 40.541  16.702 -24.084 1.00 106.90 ? 188 THR C OG1 1 
ATOM   5687  C CG2 . THR C  1 188 ? 42.730  15.838 -24.539 1.00 86.33  ? 188 THR C CG2 1 
ATOM   5688  N N   . LEU C  1 189 ? 38.458  15.893 -26.518 1.00 95.22  ? 189 LEU C N   1 
ATOM   5689  C CA  . LEU C  1 189 ? 36.973  15.986 -26.544 1.00 100.04 ? 189 LEU C CA  1 
ATOM   5690  C C   . LEU C  1 189 ? 36.422  15.081 -27.650 1.00 87.29  ? 189 LEU C C   1 
ATOM   5691  O O   . LEU C  1 189 ? 37.213  14.628 -28.497 1.00 76.86  ? 189 LEU C O   1 
ATOM   5692  C CB  . LEU C  1 189 ? 36.553  17.440 -26.783 1.00 111.61 ? 189 LEU C CB  1 
ATOM   5693  C CG  . LEU C  1 189 ? 36.959  18.443 -25.704 1.00 119.89 ? 189 LEU C CG  1 
ATOM   5694  C CD1 . LEU C  1 189 ? 36.380  19.817 -26.001 1.00 118.97 ? 189 LEU C CD1 1 
ATOM   5695  C CD2 . LEU C  1 189 ? 36.523  17.970 -24.327 1.00 120.87 ? 189 LEU C CD2 1 
ATOM   5696  N N   . THR C  1 190 ? 35.108  14.843 -27.632 1.00 86.63  ? 190 THR C N   1 
ATOM   5697  C CA  . THR C  1 190 ? 34.359  14.096 -28.677 1.00 86.85  ? 190 THR C CA  1 
ATOM   5698  C C   . THR C  1 190 ? 34.188  14.991 -29.901 1.00 88.09  ? 190 THR C C   1 
ATOM   5699  O O   . THR C  1 190 ? 34.524  16.171 -29.862 1.00 83.62  ? 190 THR C O   1 
ATOM   5700  C CB  . THR C  1 190 ? 33.003  13.615 -28.146 1.00 86.29  ? 190 THR C CB  1 
ATOM   5701  O OG1 . THR C  1 190 ? 32.113  14.733 -28.120 1.00 88.82  ? 190 THR C OG1 1 
ATOM   5702  C CG2 . THR C  1 190 ? 33.100  12.995 -26.768 1.00 83.23  ? 190 THR C CG2 1 
ATOM   5703  N N   . PRO C  1 191 ? 33.672  14.452 -31.029 1.00 99.76  ? 191 PRO C N   1 
ATOM   5704  C CA  . PRO C  1 191 ? 33.403  15.259 -32.219 1.00 105.23 ? 191 PRO C CA  1 
ATOM   5705  C C   . PRO C  1 191 ? 32.391  16.387 -31.959 1.00 107.84 ? 191 PRO C C   1 
ATOM   5706  O O   . PRO C  1 191 ? 32.635  17.503 -32.394 1.00 105.98 ? 191 PRO C O   1 
ATOM   5707  C CB  . PRO C  1 191 ? 32.819  14.253 -33.223 1.00 101.03 ? 191 PRO C CB  1 
ATOM   5708  C CG  . PRO C  1 191 ? 33.312  12.905 -32.737 1.00 99.99  ? 191 PRO C CG  1 
ATOM   5709  C CD  . PRO C  1 191 ? 33.356  13.031 -31.229 1.00 99.04  ? 191 PRO C CD  1 
ATOM   5710  N N   . GLU C  1 192 ? 31.293  16.067 -31.265 1.00 99.65  ? 192 GLU C N   1 
ATOM   5711  C CA  . GLU C  1 192 ? 30.162  16.994 -30.984 1.00 94.91  ? 192 GLU C CA  1 
ATOM   5712  C C   . GLU C  1 192 ? 30.647  18.138 -30.082 1.00 96.95  ? 192 GLU C C   1 
ATOM   5713  O O   . GLU C  1 192 ? 30.331  19.307 -30.392 1.00 92.95  ? 192 GLU C O   1 
ATOM   5714  C CB  . GLU C  1 192 ? 28.997  16.236 -30.343 1.00 83.41  ? 192 GLU C CB  1 
ATOM   5715  N N   . SER C  1 193 ? 31.377  17.812 -29.009 1.00 96.57  ? 193 SER C N   1 
ATOM   5716  C CA  . SER C  1 193 ? 31.966  18.788 -28.054 1.00 99.47  ? 193 SER C CA  1 
ATOM   5717  C C   . SER C  1 193 ? 33.014  19.643 -28.776 1.00 98.49  ? 193 SER C C   1 
ATOM   5718  O O   . SER C  1 193 ? 32.918  20.883 -28.702 1.00 100.11 ? 193 SER C O   1 
ATOM   5719  C CB  . SER C  1 193 ? 32.558  18.095 -26.855 1.00 104.66 ? 193 SER C CB  1 
ATOM   5720  O OG  . SER C  1 193 ? 31.550  17.438 -26.102 1.00 110.29 ? 193 SER C OG  1 
ATOM   5721  N N   . HIS C  1 194 ? 33.973  18.989 -29.440 1.00 103.36 ? 194 HIS C N   1 
ATOM   5722  C CA  . HIS C  1 194 ? 35.043  19.613 -30.265 1.00 102.87 ? 194 HIS C CA  1 
ATOM   5723  C C   . HIS C  1 194 ? 34.466  20.806 -31.036 1.00 99.03  ? 194 HIS C C   1 
ATOM   5724  O O   . HIS C  1 194 ? 35.002  21.921 -30.883 1.00 102.34 ? 194 HIS C O   1 
ATOM   5725  C CB  . HIS C  1 194 ? 35.666  18.563 -31.201 1.00 107.03 ? 194 HIS C CB  1 
ATOM   5726  C CG  . HIS C  1 194 ? 36.573  19.129 -32.245 1.00 105.76 ? 194 HIS C CG  1 
ATOM   5727  N ND1 . HIS C  1 194 ? 37.952  19.084 -32.137 1.00 100.40 ? 194 HIS C ND1 1 
ATOM   5728  C CD2 . HIS C  1 194 ? 36.306  19.742 -33.419 1.00 106.60 ? 194 HIS C CD2 1 
ATOM   5729  C CE1 . HIS C  1 194 ? 38.493  19.652 -33.196 1.00 99.80  ? 194 HIS C CE1 1 
ATOM   5730  N NE2 . HIS C  1 194 ? 37.505  20.064 -33.998 1.00 106.43 ? 194 HIS C NE2 1 
ATOM   5731  N N   . THR C  1 195 ? 33.409  20.568 -31.820 1.00 96.71  ? 195 THR C N   1 
ATOM   5732  C CA  . THR C  1 195 ? 32.751  21.563 -32.711 1.00 91.05  ? 195 THR C CA  1 
ATOM   5733  C C   . THR C  1 195 ? 32.293  22.781 -31.898 1.00 88.39  ? 195 THR C C   1 
ATOM   5734  O O   . THR C  1 195 ? 32.623  23.915 -32.299 1.00 89.49  ? 195 THR C O   1 
ATOM   5735  C CB  . THR C  1 195 ? 31.569  20.934 -33.459 1.00 91.05  ? 195 THR C CB  1 
ATOM   5736  O OG1 . THR C  1 195 ? 32.045  19.758 -34.115 1.00 97.43  ? 195 THR C OG1 1 
ATOM   5737  C CG2 . THR C  1 195 ? 30.942  21.873 -34.467 1.00 89.35  ? 195 THR C CG2 1 
ATOM   5738  N N   . MET C  1 196 ? 31.558  22.549 -30.808 1.00 87.56  ? 196 MET C N   1 
ATOM   5739  C CA  . MET C  1 196 ? 30.938  23.613 -29.973 1.00 84.40  ? 196 MET C CA  1 
ATOM   5740  C C   . MET C  1 196 ? 32.029  24.504 -29.368 1.00 73.26  ? 196 MET C C   1 
ATOM   5741  O O   . MET C  1 196 ? 31.928  25.734 -29.520 1.00 74.11  ? 196 MET C O   1 
ATOM   5742  C CB  . MET C  1 196 ? 30.090  23.010 -28.851 1.00 89.29  ? 196 MET C CB  1 
ATOM   5743  C CG  . MET C  1 196 ? 28.763  22.470 -29.340 1.00 93.69  ? 196 MET C CG  1 
ATOM   5744  S SD  . MET C  1 196 ? 27.373  23.192 -28.442 1.00 114.82 ? 196 MET C SD  1 
ATOM   5745  C CE  . MET C  1 196 ? 27.613  24.930 -28.807 1.00 109.15 ? 196 MET C CE  1 
ATOM   5746  N N   . LEU C  1 197 ? 33.026  23.908 -28.708 1.00 64.47  ? 197 LEU C N   1 
ATOM   5747  C CA  . LEU C  1 197 ? 34.134  24.644 -28.042 1.00 68.25  ? 197 LEU C CA  1 
ATOM   5748  C C   . LEU C  1 197 ? 34.817  25.555 -29.068 1.00 77.95  ? 197 LEU C C   1 
ATOM   5749  O O   . LEU C  1 197 ? 35.062  26.733 -28.741 1.00 90.71  ? 197 LEU C O   1 
ATOM   5750  C CB  . LEU C  1 197 ? 35.128  23.647 -27.437 1.00 66.91  ? 197 LEU C CB  1 
ATOM   5751  C CG  . LEU C  1 197 ? 36.214  24.266 -26.556 1.00 70.55  ? 197 LEU C CG  1 
ATOM   5752  C CD1 . LEU C  1 197 ? 35.603  25.030 -25.390 1.00 73.02  ? 197 LEU C CD1 1 
ATOM   5753  C CD2 . LEU C  1 197 ? 37.176  23.205 -26.050 1.00 77.13  ? 197 LEU C CD2 1 
ATOM   5754  N N   . LYS C  1 198 ? 35.109  25.024 -30.260 1.00 79.09  ? 198 LYS C N   1 
ATOM   5755  C CA  . LYS C  1 198 ? 35.700  25.789 -31.390 1.00 74.85  ? 198 LYS C CA  1 
ATOM   5756  C C   . LYS C  1 198 ? 34.779  26.974 -31.704 1.00 73.98  ? 198 LYS C C   1 
ATOM   5757  O O   . LYS C  1 198 ? 35.282  28.111 -31.756 1.00 78.28  ? 198 LYS C O   1 
ATOM   5758  C CB  . LYS C  1 198 ? 35.896  24.883 -32.610 1.00 70.27  ? 198 LYS C CB  1 
ATOM   5759  C CG  . LYS C  1 198 ? 36.912  25.378 -33.632 1.00 65.92  ? 198 LYS C CG  1 
ATOM   5760  N N   . SER C  1 199 ? 33.480  26.711 -31.883 1.00 74.77  ? 199 SER C N   1 
ATOM   5761  C CA  . SER C  1 199 ? 32.436  27.730 -32.174 1.00 82.60  ? 199 SER C CA  1 
ATOM   5762  C C   . SER C  1 199 ? 32.474  28.832 -31.111 1.00 81.35  ? 199 SER C C   1 
ATOM   5763  O O   . SER C  1 199 ? 32.662  30.002 -31.487 1.00 78.21  ? 199 SER C O   1 
ATOM   5764  C CB  . SER C  1 199 ? 31.068  27.107 -32.257 1.00 89.47  ? 199 SER C CB  1 
ATOM   5765  O OG  . SER C  1 199 ? 31.053  26.039 -33.193 1.00 115.92 ? 199 SER C OG  1 
ATOM   5766  N N   . ALA C  1 200 ? 32.294  28.463 -29.838 1.00 78.49  ? 200 ALA C N   1 
ATOM   5767  C CA  . ALA C  1 200 ? 32.295  29.379 -28.672 1.00 77.87  ? 200 ALA C CA  1 
ATOM   5768  C C   . ALA C  1 200 ? 33.540  30.271 -28.717 1.00 80.52  ? 200 ALA C C   1 
ATOM   5769  O O   . ALA C  1 200 ? 33.389  31.508 -28.617 1.00 87.57  ? 200 ALA C O   1 
ATOM   5770  C CB  . ALA C  1 200 ? 32.236  28.580 -27.394 1.00 75.41  ? 200 ALA C CB  1 
ATOM   5771  N N   . ALA C  1 201 ? 34.720  29.659 -28.866 1.00 70.14  ? 201 ALA C N   1 
ATOM   5772  C CA  . ALA C  1 201 ? 36.041  30.330 -28.888 1.00 62.45  ? 201 ALA C CA  1 
ATOM   5773  C C   . ALA C  1 201 ? 36.066  31.396 -29.990 1.00 61.16  ? 201 ALA C C   1 
ATOM   5774  O O   . ALA C  1 201 ? 36.550  32.514 -29.725 1.00 63.19  ? 201 ALA C O   1 
ATOM   5775  C CB  . ALA C  1 201 ? 37.131  29.307 -29.088 1.00 59.81  ? 201 ALA C CB  1 
ATOM   5776  N N   . ILE C  1 202 ? 35.559  31.056 -31.178 1.00 61.45  ? 202 ILE C N   1 
ATOM   5777  C CA  . ILE C  1 202 ? 35.494  31.964 -32.362 1.00 65.41  ? 202 ILE C CA  1 
ATOM   5778  C C   . ILE C  1 202 ? 34.616  33.169 -32.013 1.00 66.34  ? 202 ILE C C   1 
ATOM   5779  O O   . ILE C  1 202 ? 35.110  34.305 -32.132 1.00 64.97  ? 202 ILE C O   1 
ATOM   5780  C CB  . ILE C  1 202 ? 34.975  31.211 -33.603 1.00 64.49  ? 202 ILE C CB  1 
ATOM   5781  C CG1 . ILE C  1 202 ? 35.978  30.152 -34.070 1.00 67.76  ? 202 ILE C CG1 1 
ATOM   5782  C CG2 . ILE C  1 202 ? 34.618  32.184 -34.717 1.00 60.05  ? 202 ILE C CG2 1 
ATOM   5783  C CD1 . ILE C  1 202 ? 35.456  29.249 -35.162 1.00 76.98  ? 202 ILE C CD1 1 
ATOM   5784  N N   . VAL C  1 203 ? 33.371  32.923 -31.593 1.00 68.74  ? 203 VAL C N   1 
ATOM   5785  C CA  . VAL C  1 203 ? 32.363  33.978 -31.270 1.00 71.82  ? 203 VAL C CA  1 
ATOM   5786  C C   . VAL C  1 203 ? 33.021  35.029 -30.371 1.00 70.78  ? 203 VAL C C   1 
ATOM   5787  O O   . VAL C  1 203 ? 32.856  36.232 -30.651 1.00 73.55  ? 203 VAL C O   1 
ATOM   5788  C CB  . VAL C  1 203 ? 31.107  33.390 -30.599 1.00 76.33  ? 203 VAL C CB  1 
ATOM   5789  C CG1 . VAL C  1 203 ? 30.117  34.483 -30.225 1.00 74.98  ? 203 VAL C CG1 1 
ATOM   5790  C CG2 . VAL C  1 203 ? 30.436  32.339 -31.469 1.00 79.30  ? 203 VAL C CG2 1 
ATOM   5791  N N   . LEU C  1 204 ? 33.733  34.587 -29.331 1.00 64.91  ? 204 LEU C N   1 
ATOM   5792  C CA  . LEU C  1 204 ? 34.388  35.482 -28.342 1.00 68.07  ? 204 LEU C CA  1 
ATOM   5793  C C   . LEU C  1 204 ? 35.582  36.182 -28.999 1.00 68.30  ? 204 LEU C C   1 
ATOM   5794  O O   . LEU C  1 204 ? 35.552  37.423 -29.101 1.00 72.46  ? 204 LEU C O   1 
ATOM   5795  C CB  . LEU C  1 204 ? 34.827  34.668 -27.122 1.00 66.03  ? 204 LEU C CB  1 
ATOM   5796  C CG  . LEU C  1 204 ? 35.476  35.485 -26.005 1.00 65.75  ? 204 LEU C CG  1 
ATOM   5797  C CD1 . LEU C  1 204 ? 34.856  35.160 -24.655 1.00 66.90  ? 204 LEU C CD1 1 
ATOM   5798  C CD2 . LEU C  1 204 ? 36.981  35.269 -25.979 1.00 72.41  ? 204 LEU C CD2 1 
ATOM   5799  N N   . LEU C  1 205 ? 36.576  35.406 -29.437 1.00 62.67  ? 205 LEU C N   1 
ATOM   5800  C CA  . LEU C  1 205 ? 37.881  35.906 -29.950 1.00 64.61  ? 205 LEU C CA  1 
ATOM   5801  C C   . LEU C  1 205 ? 37.673  36.716 -31.237 1.00 64.38  ? 205 LEU C C   1 
ATOM   5802  O O   . LEU C  1 205 ? 38.359  37.744 -31.398 1.00 65.03  ? 205 LEU C O   1 
ATOM   5803  C CB  . LEU C  1 205 ? 38.805  34.708 -30.185 1.00 68.51  ? 205 LEU C CB  1 
ATOM   5804  C CG  . LEU C  1 205 ? 39.097  33.863 -28.945 1.00 75.07  ? 205 LEU C CG  1 
ATOM   5805  C CD1 . LEU C  1 205 ? 39.918  32.635 -29.306 1.00 81.55  ? 205 LEU C CD1 1 
ATOM   5806  C CD2 . LEU C  1 205 ? 39.805  34.686 -27.878 1.00 79.78  ? 205 LEU C CD2 1 
ATOM   5807  N N   . ALA C  1 206 ? 36.764  36.274 -32.111 1.00 60.18  ? 206 ALA C N   1 
ATOM   5808  C CA  . ALA C  1 206 ? 36.389  36.965 -33.368 1.00 59.18  ? 206 ALA C CA  1 
ATOM   5809  C C   . ALA C  1 206 ? 35.781  38.334 -33.041 1.00 63.89  ? 206 ALA C C   1 
ATOM   5810  O O   . ALA C  1 206 ? 36.339  39.350 -33.496 1.00 67.69  ? 206 ALA C O   1 
ATOM   5811  C CB  . ALA C  1 206 ? 35.428  36.118 -34.164 1.00 55.43  ? 206 ALA C CB  1 
ATOM   5812  N N   . GLY C  1 207 ? 34.682  38.349 -32.278 1.00 60.97  ? 207 GLY C N   1 
ATOM   5813  C CA  . GLY C  1 207 ? 33.950  39.568 -31.882 1.00 59.21  ? 207 GLY C CA  1 
ATOM   5814  C C   . GLY C  1 207 ? 34.870  40.618 -31.281 1.00 61.13  ? 207 GLY C C   1 
ATOM   5815  O O   . GLY C  1 207 ? 34.677  41.811 -31.582 1.00 64.60  ? 207 GLY C O   1 
ATOM   5816  N N   . TRP C  1 208 ? 35.839  40.186 -30.466 1.00 59.52  ? 208 TRP C N   1 
ATOM   5817  C CA  . TRP C  1 208 ? 36.818  41.047 -29.747 1.00 58.69  ? 208 TRP C CA  1 
ATOM   5818  C C   . TRP C  1 208 ? 37.385  42.119 -30.686 1.00 59.25  ? 208 TRP C C   1 
ATOM   5819  O O   . TRP C  1 208 ? 37.688  43.223 -30.198 1.00 60.53  ? 208 TRP C O   1 
ATOM   5820  C CB  . TRP C  1 208 ? 37.932  40.187 -29.136 1.00 61.63  ? 208 TRP C CB  1 
ATOM   5821  C CG  . TRP C  1 208 ? 37.597  39.656 -27.777 1.00 69.43  ? 208 TRP C CG  1 
ATOM   5822  C CD1 . TRP C  1 208 ? 36.356  39.583 -27.214 1.00 85.12  ? 208 TRP C CD1 1 
ATOM   5823  C CD2 . TRP C  1 208 ? 38.509  39.114 -26.804 1.00 75.70  ? 208 TRP C CD2 1 
ATOM   5824  N NE1 . TRP C  1 208 ? 36.432  39.042 -25.959 1.00 91.45  ? 208 TRP C NE1 1 
ATOM   5825  C CE2 . TRP C  1 208 ? 37.739  38.742 -25.681 1.00 82.65  ? 208 TRP C CE2 1 
ATOM   5826  C CE3 . TRP C  1 208 ? 39.892  38.906 -26.767 1.00 79.56  ? 208 TRP C CE3 1 
ATOM   5827  C CZ2 . TRP C  1 208 ? 38.308  38.175 -24.542 1.00 77.20  ? 208 TRP C CZ2 1 
ATOM   5828  C CZ3 . TRP C  1 208 ? 40.454  38.348 -25.640 1.00 80.47  ? 208 TRP C CZ3 1 
ATOM   5829  C CH2 . TRP C  1 208 ? 39.670  37.988 -24.544 1.00 77.73  ? 208 TRP C CH2 1 
ATOM   5830  N N   . VAL C  1 209 ? 37.521  41.799 -31.976 1.00 59.82  ? 209 VAL C N   1 
ATOM   5831  C CA  . VAL C  1 209 ? 38.178  42.662 -33.004 1.00 59.13  ? 209 VAL C CA  1 
ATOM   5832  C C   . VAL C  1 209 ? 37.411  43.983 -33.129 1.00 59.67  ? 209 VAL C C   1 
ATOM   5833  O O   . VAL C  1 209 ? 38.068  45.031 -33.292 1.00 60.51  ? 209 VAL C O   1 
ATOM   5834  C CB  . VAL C  1 209 ? 38.274  41.939 -34.360 1.00 55.91  ? 209 VAL C CB  1 
ATOM   5835  C CG1 . VAL C  1 209 ? 38.762  42.869 -35.459 1.00 54.43  ? 209 VAL C CG1 1 
ATOM   5836  C CG2 . VAL C  1 209 ? 39.154  40.702 -34.271 1.00 59.20  ? 209 VAL C CG2 1 
ATOM   5837  N N   . VAL C  1 210 ? 36.078  43.930 -33.053 1.00 56.26  ? 210 VAL C N   1 
ATOM   5838  C CA  . VAL C  1 210 ? 35.164  45.098 -33.236 1.00 55.84  ? 210 VAL C CA  1 
ATOM   5839  C C   . VAL C  1 210 ? 35.640  46.261 -32.357 1.00 57.19  ? 210 VAL C C   1 
ATOM   5840  O O   . VAL C  1 210 ? 35.579  47.418 -32.821 1.00 57.01  ? 210 VAL C O   1 
ATOM   5841  C CB  . VAL C  1 210 ? 33.705  44.723 -32.908 1.00 56.08  ? 210 VAL C CB  1 
ATOM   5842  C CG1 . VAL C  1 210 ? 32.793  45.940 -32.903 1.00 55.96  ? 210 VAL C CG1 1 
ATOM   5843  C CG2 . VAL C  1 210 ? 33.170  43.659 -33.852 1.00 60.08  ? 210 VAL C CG2 1 
ATOM   5844  N N   . TYR C  1 211 ? 36.096  45.960 -31.139 1.00 54.07  ? 211 TYR C N   1 
ATOM   5845  C CA  . TYR C  1 211 ? 36.336  46.950 -30.056 1.00 53.84  ? 211 TYR C CA  1 
ATOM   5846  C C   . TYR C  1 211 ? 37.537  47.826 -30.407 1.00 54.41  ? 211 TYR C C   1 
ATOM   5847  O O   . TYR C  1 211 ? 37.416  49.049 -30.426 1.00 54.39  ? 211 TYR C O   1 
ATOM   5848  C CB  . TYR C  1 211 ? 36.443  46.222 -28.714 1.00 54.18  ? 211 TYR C CB  1 
ATOM   5849  C CG  . TYR C  1 211 ? 35.136  45.607 -28.278 1.00 55.14  ? 211 TYR C CG  1 
ATOM   5850  C CD1 . TYR C  1 211 ? 34.260  46.295 -27.456 1.00 52.90  ? 211 TYR C CD1 1 
ATOM   5851  C CD2 . TYR C  1 211 ? 34.747  44.358 -28.731 1.00 55.15  ? 211 TYR C CD2 1 
ATOM   5852  C CE1 . TYR C  1 211 ? 33.049  45.748 -27.070 1.00 50.15  ? 211 TYR C CE1 1 
ATOM   5853  C CE2 . TYR C  1 211 ? 33.538  43.796 -28.354 1.00 55.95  ? 211 TYR C CE2 1 
ATOM   5854  C CZ  . TYR C  1 211 ? 32.685  44.494 -27.520 1.00 52.92  ? 211 TYR C CZ  1 
ATOM   5855  O OH  . TYR C  1 211 ? 31.492  43.948 -27.143 1.00 57.83  ? 211 TYR C OH  1 
ATOM   5856  N N   . PRO C  1 212 ? 38.722  47.249 -30.706 1.00 59.77  ? 212 PRO C N   1 
ATOM   5857  C CA  . PRO C  1 212 ? 39.884  48.048 -31.100 1.00 60.37  ? 212 PRO C CA  1 
ATOM   5858  C C   . PRO C  1 212 ? 39.582  48.951 -32.306 1.00 59.97  ? 212 PRO C C   1 
ATOM   5859  O O   . PRO C  1 212 ? 40.080  50.062 -32.346 1.00 63.49  ? 212 PRO C O   1 
ATOM   5860  C CB  . PRO C  1 212 ? 40.950  47.004 -31.466 1.00 58.43  ? 212 PRO C CB  1 
ATOM   5861  C CG  . PRO C  1 212 ? 40.530  45.759 -30.713 1.00 60.33  ? 212 PRO C CG  1 
ATOM   5862  C CD  . PRO C  1 212 ? 39.016  45.810 -30.669 1.00 59.18  ? 212 PRO C CD  1 
ATOM   5863  N N   . ILE C  1 213 ? 38.778  48.450 -33.250 1.00 55.96  ? 213 ILE C N   1 
ATOM   5864  C CA  . ILE C  1 213 ? 38.371  49.173 -34.492 1.00 60.27  ? 213 ILE C CA  1 
ATOM   5865  C C   . ILE C  1 213 ? 37.590  50.430 -34.098 1.00 61.46  ? 213 ILE C C   1 
ATOM   5866  O O   . ILE C  1 213 ? 37.923  51.522 -34.605 1.00 65.20  ? 213 ILE C O   1 
ATOM   5867  C CB  . ILE C  1 213 ? 37.544  48.255 -35.414 1.00 61.99  ? 213 ILE C CB  1 
ATOM   5868  C CG1 . ILE C  1 213 ? 38.379  47.085 -35.942 1.00 62.73  ? 213 ILE C CG1 1 
ATOM   5869  C CG2 . ILE C  1 213 ? 36.909  49.054 -36.543 1.00 59.03  ? 213 ILE C CG2 1 
ATOM   5870  C CD1 . ILE C  1 213 ? 37.568  46.012 -36.632 1.00 65.09  ? 213 ILE C CD1 1 
ATOM   5871  N N   . VAL C  1 214 ? 36.591  50.271 -33.225 1.00 57.69  ? 214 VAL C N   1 
ATOM   5872  C CA  . VAL C  1 214 ? 35.677  51.360 -32.771 1.00 57.82  ? 214 VAL C CA  1 
ATOM   5873  C C   . VAL C  1 214 ? 36.479  52.373 -31.943 1.00 57.01  ? 214 VAL C C   1 
ATOM   5874  O O   . VAL C  1 214 ? 36.129  53.569 -31.973 1.00 59.40  ? 214 VAL C O   1 
ATOM   5875  C CB  . VAL C  1 214 ? 34.487  50.789 -31.974 1.00 59.58  ? 214 VAL C CB  1 
ATOM   5876  C CG1 . VAL C  1 214 ? 33.560  51.885 -31.473 1.00 62.78  ? 214 VAL C CG1 1 
ATOM   5877  C CG2 . VAL C  1 214 ? 33.708  49.763 -32.784 1.00 60.72  ? 214 VAL C CG2 1 
ATOM   5878  N N   . TYR C  1 215 ? 37.517  51.909 -31.239 1.00 54.34  ? 215 TYR C N   1 
ATOM   5879  C CA  . TYR C  1 215 ? 38.373  52.730 -30.342 1.00 53.69  ? 215 TYR C CA  1 
ATOM   5880  C C   . TYR C  1 215 ? 39.017  53.873 -31.135 1.00 55.64  ? 215 TYR C C   1 
ATOM   5881  O O   . TYR C  1 215 ? 39.225  54.956 -30.553 1.00 53.89  ? 215 TYR C O   1 
ATOM   5882  C CB  . TYR C  1 215 ? 39.452  51.868 -29.681 1.00 52.85  ? 215 TYR C CB  1 
ATOM   5883  C CG  . TYR C  1 215 ? 40.449  52.633 -28.847 1.00 53.40  ? 215 TYR C CG  1 
ATOM   5884  C CD1 . TYR C  1 215 ? 41.471  53.358 -29.437 1.00 55.49  ? 215 TYR C CD1 1 
ATOM   5885  C CD2 . TYR C  1 215 ? 40.377  52.630 -27.465 1.00 59.10  ? 215 TYR C CD2 1 
ATOM   5886  C CE1 . TYR C  1 215 ? 42.391  54.064 -28.678 1.00 60.96  ? 215 TYR C CE1 1 
ATOM   5887  C CE2 . TYR C  1 215 ? 41.289  53.328 -26.690 1.00 62.14  ? 215 TYR C CE2 1 
ATOM   5888  C CZ  . TYR C  1 215 ? 42.300  54.050 -27.299 1.00 62.17  ? 215 TYR C CZ  1 
ATOM   5889  O OH  . TYR C  1 215 ? 43.203  54.743 -26.544 1.00 63.72  ? 215 TYR C OH  1 
ATOM   5890  N N   . PHE C  1 216 ? 39.315  53.632 -32.417 1.00 58.98  ? 216 PHE C N   1 
ATOM   5891  C CA  . PHE C  1 216 ? 40.183  54.489 -33.269 1.00 61.76  ? 216 PHE C CA  1 
ATOM   5892  C C   . PHE C  1 216 ? 39.350  55.439 -34.137 1.00 64.76  ? 216 PHE C C   1 
ATOM   5893  O O   . PHE C  1 216 ? 39.939  56.371 -34.716 1.00 75.72  ? 216 PHE C O   1 
ATOM   5894  C CB  . PHE C  1 216 ? 41.090  53.619 -34.143 1.00 63.35  ? 216 PHE C CB  1 
ATOM   5895  C CG  . PHE C  1 216 ? 42.302  53.080 -33.428 1.00 65.82  ? 216 PHE C CG  1 
ATOM   5896  C CD1 . PHE C  1 216 ? 43.274  53.940 -32.942 1.00 67.64  ? 216 PHE C CD1 1 
ATOM   5897  C CD2 . PHE C  1 216 ? 42.471  51.718 -33.235 1.00 60.07  ? 216 PHE C CD2 1 
ATOM   5898  C CE1 . PHE C  1 216 ? 44.390  53.450 -32.283 1.00 63.40  ? 216 PHE C CE1 1 
ATOM   5899  C CE2 . PHE C  1 216 ? 43.586  51.230 -32.573 1.00 62.11  ? 216 PHE C CE2 1 
ATOM   5900  C CZ  . PHE C  1 216 ? 44.544  52.096 -32.101 1.00 64.83  ? 216 PHE C CZ  1 
ATOM   5901  N N   . LEU C  1 217 ? 38.035  55.218 -34.222 1.00 66.16  ? 217 LEU C N   1 
ATOM   5902  C CA  . LEU C  1 217 ? 37.112  56.025 -35.067 1.00 71.12  ? 217 LEU C CA  1 
ATOM   5903  C C   . LEU C  1 217 ? 37.220  57.503 -34.695 1.00 80.34  ? 217 LEU C C   1 
ATOM   5904  O O   . LEU C  1 217 ? 37.150  58.366 -35.568 1.00 90.79  ? 217 LEU C O   1 
ATOM   5905  C CB  . LEU C  1 217 ? 35.680  55.508 -34.892 1.00 72.42  ? 217 LEU C CB  1 
ATOM   5906  C CG  . LEU C  1 217 ? 35.426  54.096 -35.417 1.00 74.05  ? 217 LEU C CG  1 
ATOM   5907  C CD1 . LEU C  1 217 ? 33.940  53.768 -35.396 1.00 69.12  ? 217 LEU C CD1 1 
ATOM   5908  C CD2 . LEU C  1 217 ? 35.989  53.925 -36.821 1.00 71.72  ? 217 LEU C CD2 1 
ATOM   5909  N N   . PRO C  1 218 ? 37.379  57.849 -33.397 1.00 85.39  ? 218 PRO C N   1 
ATOM   5910  C CA  . PRO C  1 218 ? 37.512  59.248 -32.985 1.00 85.36  ? 218 PRO C CA  1 
ATOM   5911  C C   . PRO C  1 218 ? 38.656  60.004 -33.680 1.00 82.97  ? 218 PRO C C   1 
ATOM   5912  O O   . PRO C  1 218 ? 38.677  61.220 -33.591 1.00 81.97  ? 218 PRO C O   1 
ATOM   5913  C CB  . PRO C  1 218 ? 37.783  59.156 -31.475 1.00 85.52  ? 218 PRO C CB  1 
ATOM   5914  C CG  . PRO C  1 218 ? 37.171  57.832 -31.065 1.00 83.81  ? 218 PRO C CG  1 
ATOM   5915  C CD  . PRO C  1 218 ? 37.392  56.921 -32.255 1.00 89.77  ? 218 PRO C CD  1 
ATOM   5916  N N   . LEU C  1 219 ? 39.566  59.281 -34.347 1.00 79.12  ? 219 LEU C N   1 
ATOM   5917  C CA  . LEU C  1 219 ? 40.743  59.857 -35.057 1.00 77.99  ? 219 LEU C CA  1 
ATOM   5918  C C   . LEU C  1 219 ? 40.306  60.434 -36.409 1.00 84.40  ? 219 LEU C C   1 
ATOM   5919  O O   . LEU C  1 219 ? 40.931  61.416 -36.859 1.00 95.67  ? 219 LEU C O   1 
ATOM   5920  C CB  . LEU C  1 219 ? 41.807  58.772 -35.250 1.00 69.04  ? 219 LEU C CB  1 
ATOM   5921  C CG  . LEU C  1 219 ? 42.611  58.409 -34.002 1.00 72.84  ? 219 LEU C CG  1 
ATOM   5922  C CD1 . LEU C  1 219 ? 43.631  57.324 -34.310 1.00 71.34  ? 219 LEU C CD1 1 
ATOM   5923  C CD2 . LEU C  1 219 ? 43.298  59.636 -33.423 1.00 73.20  ? 219 LEU C CD2 1 
ATOM   5924  N N   . PHE C  1 220 ? 39.280  59.842 -37.028 1.00 86.62  ? 220 PHE C N   1 
ATOM   5925  C CA  . PHE C  1 220 ? 38.767  60.218 -38.372 1.00 87.86  ? 220 PHE C CA  1 
ATOM   5926  C C   . PHE C  1 220 ? 37.765  61.372 -38.237 1.00 84.08  ? 220 PHE C C   1 
ATOM   5927  O O   . PHE C  1 220 ? 37.010  61.620 -39.197 1.00 85.17  ? 220 PHE C O   1 
ATOM   5928  C CB  . PHE C  1 220 ? 38.152  59.001 -39.069 1.00 88.89  ? 220 PHE C CB  1 
ATOM   5929  C CG  . PHE C  1 220 ? 39.094  57.833 -39.229 1.00 97.40  ? 220 PHE C CG  1 
ATOM   5930  C CD1 . PHE C  1 220 ? 40.204  57.925 -40.055 1.00 102.35 ? 220 PHE C CD1 1 
ATOM   5931  C CD2 . PHE C  1 220 ? 38.873  56.641 -38.556 1.00 105.78 ? 220 PHE C CD2 1 
ATOM   5932  C CE1 . PHE C  1 220 ? 41.072  56.854 -40.199 1.00 103.17 ? 220 PHE C CE1 1 
ATOM   5933  C CE2 . PHE C  1 220 ? 39.742  55.571 -38.703 1.00 112.60 ? 220 PHE C CE2 1 
ATOM   5934  C CZ  . PHE C  1 220 ? 40.840  55.679 -39.524 1.00 106.30 ? 220 PHE C CZ  1 
ATOM   5935  N N   . GLY C  1 221 ? 37.766  62.056 -37.087 1.00 84.65  ? 221 GLY C N   1 
ATOM   5936  C CA  . GLY C  1 221 ? 36.945  63.259 -36.840 1.00 88.33  ? 221 GLY C CA  1 
ATOM   5937  C C   . GLY C  1 221 ? 35.908  63.044 -35.748 1.00 87.19  ? 221 GLY C C   1 
ATOM   5938  O O   . GLY C  1 221 ? 36.018  62.040 -35.015 1.00 95.47  ? 221 GLY C O   1 
ATOM   5939  N N   . ALA C  1 222 ? 34.939  63.963 -35.648 1.00 81.73  ? 222 ALA C N   1 
ATOM   5940  C CA  . ALA C  1 222 ? 33.843  63.969 -34.648 1.00 81.35  ? 222 ALA C CA  1 
ATOM   5941  C C   . ALA C  1 222 ? 32.534  64.411 -35.313 1.00 78.08  ? 222 ALA C C   1 
ATOM   5942  O O   . ALA C  1 222 ? 32.590  65.238 -36.244 1.00 86.15  ? 222 ALA C O   1 
ATOM   5943  C CB  . ALA C  1 222 ? 34.201  64.878 -33.498 1.00 79.98  ? 222 ALA C CB  1 
ATOM   5944  N N   . SER C  1 223 ? 31.401  63.892 -34.831 1.00 72.26  ? 223 SER C N   1 
ATOM   5945  C CA  . SER C  1 223 ? 30.043  64.132 -35.386 1.00 65.58  ? 223 SER C CA  1 
ATOM   5946  C C   . SER C  1 223 ? 29.000  63.380 -34.554 1.00 65.29  ? 223 SER C C   1 
ATOM   5947  O O   . SER C  1 223 ? 29.312  62.271 -34.075 1.00 73.69  ? 223 SER C O   1 
ATOM   5948  C CB  . SER C  1 223 ? 29.975  63.720 -36.834 1.00 66.10  ? 223 SER C CB  1 
ATOM   5949  O OG  . SER C  1 223 ? 28.628  63.640 -37.276 1.00 71.06  ? 223 SER C OG  1 
ATOM   5950  N N   . GLY C  1 224 ? 27.810  63.967 -34.395 1.00 63.10  ? 224 GLY C N   1 
ATOM   5951  C CA  . GLY C  1 224 ? 26.647  63.308 -33.772 1.00 62.81  ? 224 GLY C CA  1 
ATOM   5952  C C   . GLY C  1 224 ? 26.454  61.911 -34.335 1.00 62.63  ? 224 GLY C C   1 
ATOM   5953  O O   . GLY C  1 224 ? 26.275  60.971 -33.539 1.00 60.20  ? 224 GLY C O   1 
ATOM   5954  N N   . GLY C  1 225 ? 26.513  61.784 -35.664 1.00 68.12  ? 225 GLY C N   1 
ATOM   5955  C CA  . GLY C  1 225 ? 26.368  60.512 -36.399 1.00 72.80  ? 225 GLY C CA  1 
ATOM   5956  C C   . GLY C  1 225 ? 27.437  59.503 -36.011 1.00 70.46  ? 225 GLY C C   1 
ATOM   5957  O O   . GLY C  1 225 ? 27.080  58.332 -35.772 1.00 70.33  ? 225 GLY C O   1 
ATOM   5958  N N   . LEU C  1 226 ? 28.703  59.931 -35.957 1.00 64.97  ? 226 LEU C N   1 
ATOM   5959  C CA  . LEU C  1 226 ? 29.852  59.069 -35.567 1.00 63.49  ? 226 LEU C CA  1 
ATOM   5960  C C   . LEU C  1 226 ? 29.648  58.602 -34.122 1.00 61.72  ? 226 LEU C C   1 
ATOM   5961  O O   . LEU C  1 226 ? 29.629  57.376 -33.890 1.00 59.58  ? 226 LEU C O   1 
ATOM   5962  C CB  . LEU C  1 226 ? 31.163  59.850 -35.719 1.00 61.23  ? 226 LEU C CB  1 
ATOM   5963  C CG  . LEU C  1 226 ? 32.435  59.062 -35.398 1.00 69.94  ? 226 LEU C CG  1 
ATOM   5964  C CD1 . LEU C  1 226 ? 32.536  57.811 -36.259 1.00 68.99  ? 226 LEU C CD1 1 
ATOM   5965  C CD2 . LEU C  1 226 ? 33.677  59.925 -35.569 1.00 75.29  ? 226 LEU C CD2 1 
ATOM   5966  N N   . THR C  1 227 ? 29.491  59.552 -33.196 1.00 62.02  ? 227 THR C N   1 
ATOM   5967  C CA  . THR C  1 227 ? 29.271  59.300 -31.747 1.00 58.05  ? 227 THR C CA  1 
ATOM   5968  C C   . THR C  1 227 ? 28.141  58.278 -31.581 1.00 57.10  ? 227 THR C C   1 
ATOM   5969  O O   . THR C  1 227 ? 28.330  57.316 -30.814 1.00 60.98  ? 227 THR C O   1 
ATOM   5970  C CB  . THR C  1 227 ? 28.986  60.609 -31.001 1.00 55.16  ? 227 THR C CB  1 
ATOM   5971  O OG1 . THR C  1 227 ? 30.146  61.436 -31.112 1.00 50.89  ? 227 THR C OG1 1 
ATOM   5972  C CG2 . THR C  1 227 ? 28.644  60.391 -29.543 1.00 56.81  ? 227 THR C CG2 1 
ATOM   5973  N N   . THR C  1 228 ? 27.016  58.478 -32.274 1.00 56.06  ? 228 THR C N   1 
ATOM   5974  C CA  . THR C  1 228 ? 25.847  57.556 -32.271 1.00 58.49  ? 228 THR C CA  1 
ATOM   5975  C C   . THR C  1 228 ? 26.308  56.161 -32.704 1.00 54.53  ? 228 THR C C   1 
ATOM   5976  O O   . THR C  1 228 ? 25.971  55.186 -32.006 1.00 57.58  ? 228 THR C O   1 
ATOM   5977  C CB  . THR C  1 228 ? 24.716  58.071 -33.170 1.00 57.94  ? 228 THR C CB  1 
ATOM   5978  O OG1 . THR C  1 228 ? 24.260  59.311 -32.628 1.00 59.50  ? 228 THR C OG1 1 
ATOM   5979  C CG2 . THR C  1 228 ? 23.557  57.103 -33.269 1.00 60.08  ? 228 THR C CG2 1 
ATOM   5980  N N   . THR C  1 229 ? 27.052  56.081 -33.811 1.00 51.93  ? 229 THR C N   1 
ATOM   5981  C CA  . THR C  1 229 ? 27.606  54.822 -34.374 1.00 55.65  ? 229 THR C CA  1 
ATOM   5982  C C   . THR C  1 229 ? 28.455  54.120 -33.309 1.00 61.64  ? 229 THR C C   1 
ATOM   5983  O O   . THR C  1 229 ? 28.187  52.936 -33.027 1.00 61.97  ? 229 THR C O   1 
ATOM   5984  C CB  . THR C  1 229 ? 28.433  55.095 -35.635 1.00 52.50  ? 229 THR C CB  1 
ATOM   5985  O OG1 . THR C  1 229 ? 27.586  55.761 -36.572 1.00 48.78  ? 229 THR C OG1 1 
ATOM   5986  C CG2 . THR C  1 229 ? 29.004  53.834 -36.247 1.00 51.35  ? 229 THR C CG2 1 
ATOM   5987  N N   . ILE C  1 230 ? 29.436  54.834 -32.750 1.00 61.66  ? 230 ILE C N   1 
ATOM   5988  C CA  . ILE C  1 230 ? 30.363  54.328 -31.694 1.00 57.43  ? 230 ILE C CA  1 
ATOM   5989  C C   . ILE C  1 230 ? 29.533  53.701 -30.567 1.00 56.19  ? 230 ILE C C   1 
ATOM   5990  O O   . ILE C  1 230 ? 29.785  52.530 -30.231 1.00 62.77  ? 230 ILE C O   1 
ATOM   5991  C CB  . ILE C  1 230 ? 31.273  55.463 -31.181 1.00 54.89  ? 230 ILE C CB  1 
ATOM   5992  C CG1 . ILE C  1 230 ? 32.301  55.878 -32.236 1.00 62.25  ? 230 ILE C CG1 1 
ATOM   5993  C CG2 . ILE C  1 230 ? 31.938  55.073 -29.872 1.00 52.63  ? 230 ILE C CG2 1 
ATOM   5994  C CD1 . ILE C  1 230 ? 32.997  57.187 -31.937 1.00 67.60  ? 230 ILE C CD1 1 
ATOM   5995  N N   . LEU C  1 231 ? 28.574  54.452 -30.021 1.00 51.25  ? 231 LEU C N   1 
ATOM   5996  C CA  . LEU C  1 231 ? 27.741  54.037 -28.861 1.00 52.23  ? 231 LEU C CA  1 
ATOM   5997  C C   . LEU C  1 231 ? 26.920  52.793 -29.221 1.00 57.56  ? 231 LEU C C   1 
ATOM   5998  O O   . LEU C  1 231 ? 26.989  51.807 -28.461 1.00 63.38  ? 231 LEU C O   1 
ATOM   5999  C CB  . LEU C  1 231 ? 26.833  55.201 -28.452 1.00 51.01  ? 231 LEU C CB  1 
ATOM   6000  C CG  . LEU C  1 231 ? 27.537  56.372 -27.769 1.00 49.66  ? 231 LEU C CG  1 
ATOM   6001  C CD1 . LEU C  1 231 ? 26.529  57.396 -27.270 1.00 47.48  ? 231 LEU C CD1 1 
ATOM   6002  C CD2 . LEU C  1 231 ? 28.413  55.887 -26.624 1.00 51.71  ? 231 LEU C CD2 1 
ATOM   6003  N N   . ILE C  1 232 ? 26.176  52.839 -30.332 1.00 54.68  ? 232 ILE C N   1 
ATOM   6004  C CA  . ILE C  1 232 ? 25.215  51.771 -30.744 1.00 51.55  ? 232 ILE C CA  1 
ATOM   6005  C C   . ILE C  1 232 ? 25.988  50.492 -31.084 1.00 47.19  ? 232 ILE C C   1 
ATOM   6006  O O   . ILE C  1 232 ? 25.572  49.413 -30.619 1.00 52.88  ? 232 ILE C O   1 
ATOM   6007  C CB  . ILE C  1 232 ? 24.333  52.234 -31.920 1.00 49.72  ? 232 ILE C CB  1 
ATOM   6008  C CG1 . ILE C  1 232 ? 23.432  53.404 -31.514 1.00 51.06  ? 232 ILE C CG1 1 
ATOM   6009  C CG2 . ILE C  1 232 ? 23.532  51.065 -32.476 1.00 46.56  ? 232 ILE C CG2 1 
ATOM   6010  C CD1 . ILE C  1 232 ? 22.392  53.779 -32.545 1.00 51.25  ? 232 ILE C CD1 1 
ATOM   6011  N N   . THR C  1 233 ? 27.062  50.612 -31.868 1.00 41.84  ? 233 THR C N   1 
ATOM   6012  C CA  . THR C  1 233 ? 27.914  49.474 -32.305 1.00 41.04  ? 233 THR C CA  1 
ATOM   6013  C C   . THR C  1 233 ? 28.384  48.699 -31.071 1.00 44.01  ? 233 THR C C   1 
ATOM   6014  O O   . THR C  1 233 ? 28.172  47.472 -31.032 1.00 46.27  ? 233 THR C O   1 
ATOM   6015  C CB  . THR C  1 233 ? 29.102  49.952 -33.148 1.00 38.41  ? 233 THR C CB  1 
ATOM   6016  O OG1 . THR C  1 233 ? 28.578  50.540 -34.338 1.00 37.97  ? 233 THR C OG1 1 
ATOM   6017  C CG2 . THR C  1 233 ? 30.060  48.838 -33.509 1.00 37.93  ? 233 THR C CG2 1 
ATOM   6018  N N   . LEU C  1 234 ? 28.989  49.400 -30.106 1.00 45.47  ? 234 LEU C N   1 
ATOM   6019  C CA  . LEU C  1 234 ? 29.550  48.813 -28.859 1.00 45.82  ? 234 LEU C CA  1 
ATOM   6020  C C   . LEU C  1 234 ? 28.441  48.086 -28.093 1.00 42.39  ? 234 LEU C C   1 
ATOM   6021  O O   . LEU C  1 234 ? 28.727  47.015 -27.528 1.00 42.53  ? 234 LEU C O   1 
ATOM   6022  C CB  . LEU C  1 234 ? 30.175  49.924 -28.010 1.00 49.81  ? 234 LEU C CB  1 
ATOM   6023  C CG  . LEU C  1 234 ? 31.480  50.510 -28.551 1.00 52.42  ? 234 LEU C CG  1 
ATOM   6024  C CD1 . LEU C  1 234 ? 31.971  51.647 -27.670 1.00 53.50  ? 234 LEU C CD1 1 
ATOM   6025  C CD2 . LEU C  1 234 ? 32.550  49.437 -28.684 1.00 49.92  ? 234 LEU C CD2 1 
ATOM   6026  N N   . THR C  1 235 ? 27.229  48.647 -28.077 1.00 41.38  ? 235 THR C N   1 
ATOM   6027  C CA  . THR C  1 235 ? 26.040  48.053 -27.406 1.00 43.65  ? 235 THR C CA  1 
ATOM   6028  C C   . THR C  1 235 ? 25.676  46.736 -28.100 1.00 42.10  ? 235 THR C C   1 
ATOM   6029  O O   . THR C  1 235 ? 25.600  45.702 -27.403 1.00 43.55  ? 235 THR C O   1 
ATOM   6030  C CB  . THR C  1 235 ? 24.865  49.037 -27.382 1.00 42.81  ? 235 THR C CB  1 
ATOM   6031  O OG1 . THR C  1 235 ? 25.320  50.233 -26.748 1.00 42.75  ? 235 THR C OG1 1 
ATOM   6032  C CG2 . THR C  1 235 ? 23.656  48.494 -26.651 1.00 43.55  ? 235 THR C CG2 1 
ATOM   6033  N N   . VAL C  1 236 ? 25.470  46.775 -29.418 1.00 41.78  ? 236 VAL C N   1 
ATOM   6034  C CA  . VAL C  1 236 ? 25.152  45.579 -30.255 1.00 43.58  ? 236 VAL C CA  1 
ATOM   6035  C C   . VAL C  1 236 ? 26.270  44.545 -30.070 1.00 43.56  ? 236 VAL C C   1 
ATOM   6036  O O   . VAL C  1 236 ? 25.949  43.353 -29.900 1.00 41.13  ? 236 VAL C O   1 
ATOM   6037  C CB  . VAL C  1 236 ? 24.966  45.959 -31.737 1.00 40.82  ? 236 VAL C CB  1 
ATOM   6038  C CG1 . VAL C  1 236 ? 24.873  44.730 -32.629 1.00 38.62  ? 236 VAL C CG1 1 
ATOM   6039  C CG2 . VAL C  1 236 ? 23.754  46.858 -31.934 1.00 39.81  ? 236 VAL C CG2 1 
ATOM   6040  N N   . ALA C  1 237 ? 27.529  44.992 -30.091 1.00 42.94  ? 237 ALA C N   1 
ATOM   6041  C CA  . ALA C  1 237 ? 28.731  44.153 -29.875 1.00 47.76  ? 237 ALA C CA  1 
ATOM   6042  C C   . ALA C  1 237 ? 28.625  43.454 -28.516 1.00 51.48  ? 237 ALA C C   1 
ATOM   6043  O O   . ALA C  1 237 ? 28.647  42.209 -28.490 1.00 54.62  ? 237 ALA C O   1 
ATOM   6044  C CB  . ALA C  1 237 ? 29.981  44.995 -29.962 1.00 50.02  ? 237 ALA C CB  1 
ATOM   6045  N N   . ASP C  1 238 ? 28.513  44.232 -27.434 1.00 51.95  ? 238 ASP C N   1 
ATOM   6046  C CA  . ASP C  1 238 ? 28.387  43.721 -26.042 1.00 50.42  ? 238 ASP C CA  1 
ATOM   6047  C C   . ASP C  1 238 ? 27.314  42.628 -25.998 1.00 52.60  ? 238 ASP C C   1 
ATOM   6048  O O   . ASP C  1 238 ? 27.634  41.513 -25.547 1.00 54.53  ? 238 ASP C O   1 
ATOM   6049  C CB  . ASP C  1 238 ? 28.062  44.845 -25.054 1.00 50.20  ? 238 ASP C CB  1 
ATOM   6050  C CG  . ASP C  1 238 ? 29.278  45.636 -24.604 1.00 51.34  ? 238 ASP C CG  1 
ATOM   6051  O OD1 . ASP C  1 238 ? 29.093  46.625 -23.867 1.00 48.97  ? 238 ASP C OD1 1 
ATOM   6052  O OD2 . ASP C  1 238 ? 30.400  45.255 -24.990 1.00 51.11  ? 238 ASP C OD2 1 
ATOM   6053  N N   . VAL C  1 239 ? 26.096  42.935 -26.455 1.00 50.61  ? 239 VAL C N   1 
ATOM   6054  C CA  . VAL C  1 239 ? 24.913  42.026 -26.367 1.00 51.09  ? 239 VAL C CA  1 
ATOM   6055  C C   . VAL C  1 239 ? 25.210  40.729 -27.131 1.00 54.47  ? 239 VAL C C   1 
ATOM   6056  O O   . VAL C  1 239 ? 25.087  39.648 -26.524 1.00 51.06  ? 239 VAL C O   1 
ATOM   6057  C CB  . VAL C  1 239 ? 23.633  42.704 -26.891 1.00 50.50  ? 239 VAL C CB  1 
ATOM   6058  C CG1 . VAL C  1 239 ? 22.504  41.699 -27.061 1.00 50.91  ? 239 VAL C CG1 1 
ATOM   6059  C CG2 . VAL C  1 239 ? 23.196  43.855 -25.998 1.00 50.53  ? 239 VAL C CG2 1 
ATOM   6060  N N   . ILE C  1 240 ? 25.578  40.836 -28.412 1.00 58.72  ? 240 ILE C N   1 
ATOM   6061  C CA  . ILE C  1 240 ? 25.814  39.675 -29.323 1.00 58.49  ? 240 ILE C CA  1 
ATOM   6062  C C   . ILE C  1 240 ? 26.906  38.776 -28.731 1.00 57.74  ? 240 ILE C C   1 
ATOM   6063  O O   . ILE C  1 240 ? 26.661  37.564 -28.604 1.00 57.13  ? 240 ILE C O   1 
ATOM   6064  C CB  . ILE C  1 240 ? 26.175  40.149 -30.744 1.00 59.21  ? 240 ILE C CB  1 
ATOM   6065  C CG1 . ILE C  1 240 ? 24.951  40.713 -31.470 1.00 64.59  ? 240 ILE C CG1 1 
ATOM   6066  C CG2 . ILE C  1 240 ? 26.834  39.030 -31.536 1.00 58.65  ? 240 ILE C CG2 1 
ATOM   6067  C CD1 . ILE C  1 240 ? 25.253  41.265 -32.843 1.00 70.65  ? 240 ILE C CD1 1 
ATOM   6068  N N   . VAL C  1 241 ? 28.066  39.347 -28.396 1.00 52.06  ? 241 VAL C N   1 
ATOM   6069  C CA  . VAL C  1 241 ? 29.245  38.592 -27.876 1.00 57.23  ? 241 VAL C CA  1 
ATOM   6070  C C   . VAL C  1 241 ? 28.849  37.874 -26.590 1.00 59.30  ? 241 VAL C C   1 
ATOM   6071  O O   . VAL C  1 241 ? 29.035  36.666 -26.467 1.00 69.22  ? 241 VAL C O   1 
ATOM   6072  C CB  . VAL C  1 241 ? 30.455  39.516 -27.646 1.00 62.95  ? 241 VAL C CB  1 
ATOM   6073  C CG1 . VAL C  1 241 ? 31.549  38.816 -26.851 1.00 64.45  ? 241 VAL C CG1 1 
ATOM   6074  C CG2 . VAL C  1 241 ? 31.008  40.061 -28.954 1.00 64.80  ? 241 VAL C CG2 1 
ATOM   6075  N N   . LYS C  1 242 ? 28.292  38.633 -25.641 1.00 58.07  ? 242 LYS C N   1 
ATOM   6076  C CA  . LYS C  1 242 ? 28.049  38.138 -24.296 1.00 55.06  ? 242 LYS C CA  1 
ATOM   6077  C C   . LYS C  1 242 ? 26.990  37.038 -24.321 1.00 52.28  ? 242 LYS C C   1 
ATOM   6078  O O   . LYS C  1 242 ? 27.171  35.993 -23.701 1.00 54.22  ? 242 LYS C O   1 
ATOM   6079  C CB  . LYS C  1 242 ? 27.631  39.289 -23.376 1.00 55.12  ? 242 LYS C CB  1 
ATOM   6080  C CG  . LYS C  1 242 ? 28.750  40.257 -23.012 1.00 56.27  ? 242 LYS C CG  1 
ATOM   6081  C CD  . LYS C  1 242 ? 28.309  41.417 -22.135 1.00 60.03  ? 242 LYS C CD  1 
ATOM   6082  C CE  . LYS C  1 242 ? 29.384  42.477 -21.941 1.00 60.19  ? 242 LYS C CE  1 
ATOM   6083  N NZ  . LYS C  1 242 ? 30.705  41.915 -22.164 1.00 63.33  ? 242 LYS C NZ  1 
ATOM   6084  N N   . LEU C  1 243 ? 25.888  37.286 -25.038 1.00 49.57  ? 243 LEU C N   1 
ATOM   6085  C CA  . LEU C  1 243 ? 24.782  36.345 -25.098 1.00 49.28  ? 243 LEU C CA  1 
ATOM   6086  C C   . LEU C  1 243 ? 25.090  35.239 -26.113 1.00 50.78  ? 243 LEU C C   1 
ATOM   6087  O O   . LEU C  1 243 ? 24.791  34.067 -25.816 1.00 55.31  ? 243 LEU C O   1 
ATOM   6088  C CB  . LEU C  1 243 ? 23.503  37.099 -25.472 1.00 46.18  ? 243 LEU C CB  1 
ATOM   6089  C CG  . LEU C  1 243 ? 22.959  38.024 -24.385 1.00 49.76  ? 243 LEU C CG  1 
ATOM   6090  C CD1 . LEU C  1 243 ? 21.651  38.667 -24.820 1.00 48.88  ? 243 LEU C CD1 1 
ATOM   6091  C CD2 . LEU C  1 243 ? 22.774  37.270 -23.077 1.00 53.01  ? 243 LEU C CD2 1 
ATOM   6092  N N   . GLY C  1 244 ? 25.649  35.604 -27.270 1.00 48.77  ? 244 GLY C N   1 
ATOM   6093  C CA  . GLY C  1 244 ? 26.084  34.651 -28.309 1.00 48.58  ? 244 GLY C CA  1 
ATOM   6094  C C   . GLY C  1 244 ? 27.047  33.627 -27.736 1.00 50.71  ? 244 GLY C C   1 
ATOM   6095  O O   . GLY C  1 244 ? 26.721  32.425 -27.761 1.00 52.29  ? 244 GLY C O   1 
ATOM   6096  N N   . PHE C  1 245 ? 28.186  34.097 -27.222 1.00 50.18  ? 245 PHE C N   1 
ATOM   6097  C CA  . PHE C  1 245 ? 29.254  33.275 -26.598 1.00 52.56  ? 245 PHE C CA  1 
ATOM   6098  C C   . PHE C  1 245 ? 28.668  32.437 -25.457 1.00 53.14  ? 245 PHE C C   1 
ATOM   6099  O O   . PHE C  1 245 ? 28.835  31.202 -25.475 1.00 58.97  ? 245 PHE C O   1 
ATOM   6100  C CB  . PHE C  1 245 ? 30.387  34.174 -26.097 1.00 56.79  ? 245 PHE C CB  1 
ATOM   6101  C CG  . PHE C  1 245 ? 31.341  33.507 -25.140 1.00 59.60  ? 245 PHE C CG  1 
ATOM   6102  C CD1 . PHE C  1 245 ? 32.396  32.740 -25.608 1.00 66.31  ? 245 PHE C CD1 1 
ATOM   6103  C CD2 . PHE C  1 245 ? 31.181  33.643 -23.771 1.00 57.82  ? 245 PHE C CD2 1 
ATOM   6104  C CE1 . PHE C  1 245 ? 33.272  32.125 -24.728 1.00 66.83  ? 245 PHE C CE1 1 
ATOM   6105  C CE2 . PHE C  1 245 ? 32.057  33.028 -22.893 1.00 63.70  ? 245 PHE C CE2 1 
ATOM   6106  C CZ  . PHE C  1 245 ? 33.100  32.271 -23.373 1.00 67.34  ? 245 PHE C CZ  1 
ATOM   6107  N N   . SER C  1 246 ? 28.010  33.092 -24.494 1.00 57.56  ? 246 SER C N   1 
ATOM   6108  C CA  . SER C  1 246 ? 27.469  32.466 -23.257 1.00 65.29  ? 246 SER C CA  1 
ATOM   6109  C C   . SER C  1 246 ? 26.611  31.245 -23.616 1.00 70.61  ? 246 SER C C   1 
ATOM   6110  O O   . SER C  1 246 ? 26.843  30.169 -23.028 1.00 73.62  ? 246 SER C O   1 
ATOM   6111  C CB  . SER C  1 246 ? 26.701  33.462 -22.425 1.00 63.60  ? 246 SER C CB  1 
ATOM   6112  O OG  . SER C  1 246 ? 25.451  33.773 -23.022 1.00 68.54  ? 246 SER C OG  1 
ATOM   6113  N N   . THR C  1 247 ? 25.663  31.399 -24.547 1.00 64.36  ? 247 THR C N   1 
ATOM   6114  C CA  . THR C  1 247 ? 24.758  30.310 -25.007 1.00 63.08  ? 247 THR C CA  1 
ATOM   6115  C C   . THR C  1 247 ? 25.591  29.103 -25.454 1.00 64.58  ? 247 THR C C   1 
ATOM   6116  O O   . THR C  1 247 ? 25.170  27.962 -25.175 1.00 67.79  ? 247 THR C O   1 
ATOM   6117  C CB  . THR C  1 247 ? 23.835  30.771 -26.143 1.00 59.63  ? 247 THR C CB  1 
ATOM   6118  O OG1 . THR C  1 247 ? 23.159  31.955 -25.719 1.00 62.63  ? 247 THR C OG1 1 
ATOM   6119  C CG2 . THR C  1 247 ? 22.822  29.716 -26.531 1.00 58.28  ? 247 THR C CG2 1 
ATOM   6120  N N   . GLN C  1 248 ? 26.722  29.354 -26.122 1.00 59.71  ? 248 GLN C N   1 
ATOM   6121  C CA  . GLN C  1 248 ? 27.614  28.311 -26.700 1.00 55.87  ? 248 GLN C CA  1 
ATOM   6122  C C   . GLN C  1 248 ? 28.280  27.515 -25.571 1.00 57.82  ? 248 GLN C C   1 
ATOM   6123  O O   . GLN C  1 248 ? 28.137  26.277 -25.570 1.00 59.42  ? 248 GLN C O   1 
ATOM   6124  C CB  . GLN C  1 248 ? 28.659  28.953 -27.612 1.00 63.25  ? 248 GLN C CB  1 
ATOM   6125  C CG  . GLN C  1 248 ? 28.074  29.532 -28.892 1.00 72.75  ? 248 GLN C CG  1 
ATOM   6126  C CD  . GLN C  1 248 ? 27.549  28.462 -29.818 1.00 77.08  ? 248 GLN C CD  1 
ATOM   6127  O OE1 . GLN C  1 248 ? 28.269  27.553 -30.221 1.00 86.01  ? 248 GLN C OE1 1 
ATOM   6128  N NE2 . GLN C  1 248 ? 26.279  28.568 -30.170 1.00 81.21  ? 248 GLN C NE2 1 
ATOM   6129  N N   . THR C  1 249 ? 28.977  28.194 -24.653 1.00 60.36  ? 249 THR C N   1 
ATOM   6130  C CA  . THR C  1 249 ? 29.715  27.567 -23.521 1.00 55.05  ? 249 THR C CA  1 
ATOM   6131  C C   . THR C  1 249 ? 28.744  26.733 -22.679 1.00 51.19  ? 249 THR C C   1 
ATOM   6132  O O   . THR C  1 249 ? 29.176  25.698 -22.142 1.00 52.21  ? 249 THR C O   1 
ATOM   6133  C CB  . THR C  1 249 ? 30.436  28.613 -22.661 1.00 53.60  ? 249 THR C CB  1 
ATOM   6134  O OG1 . THR C  1 249 ? 29.464  29.541 -22.181 1.00 56.84  ? 249 THR C OG1 1 
ATOM   6135  C CG2 . THR C  1 249 ? 31.524  29.342 -23.417 1.00 51.95  ? 249 THR C CG2 1 
ATOM   6136  N N   . HIS C  1 250 ? 27.487  27.168 -22.568 1.00 50.56  ? 250 HIS C N   1 
ATOM   6137  C CA  . HIS C  1 250 ? 26.403  26.416 -21.880 1.00 54.06  ? 250 HIS C CA  1 
ATOM   6138  C C   . HIS C  1 250 ? 26.182  25.086 -22.610 1.00 55.81  ? 250 HIS C C   1 
ATOM   6139  O O   . HIS C  1 250 ? 26.333  24.026 -21.970 1.00 52.09  ? 250 HIS C O   1 
ATOM   6140  C CB  . HIS C  1 250 ? 25.120  27.255 -21.790 1.00 53.81  ? 250 HIS C CB  1 
ATOM   6141  C CG  . HIS C  1 250 ? 24.056  26.628 -20.949 1.00 51.52  ? 250 HIS C CG  1 
ATOM   6142  N ND1 . HIS C  1 250 ? 24.228  26.384 -19.600 1.00 51.44  ? 250 HIS C ND1 1 
ATOM   6143  C CD2 . HIS C  1 250 ? 22.812  26.199 -21.254 1.00 51.04  ? 250 HIS C CD2 1 
ATOM   6144  C CE1 . HIS C  1 250 ? 23.138  25.825 -19.112 1.00 47.04  ? 250 HIS C CE1 1 
ATOM   6145  N NE2 . HIS C  1 250 ? 22.253  25.702 -20.107 1.00 47.57  ? 250 HIS C NE2 1 
ATOM   6146  N N   . ARG C  1 251 ? 25.853  25.145 -23.905 1.00 59.69  ? 251 ARG C N   1 
ATOM   6147  C CA  . ARG C  1 251 ? 25.611  23.950 -24.758 1.00 58.72  ? 251 ARG C CA  1 
ATOM   6148  C C   . ARG C  1 251 ? 26.782  22.972 -24.586 1.00 53.11  ? 251 ARG C C   1 
ATOM   6149  O O   . ARG C  1 251 ? 26.525  21.753 -24.546 1.00 47.40  ? 251 ARG C O   1 
ATOM   6150  C CB  . ARG C  1 251 ? 25.409  24.358 -26.222 1.00 59.35  ? 251 ARG C CB  1 
ATOM   6151  C CG  . ARG C  1 251 ? 24.054  24.992 -26.508 1.00 61.18  ? 251 ARG C CG  1 
ATOM   6152  C CD  . ARG C  1 251 ? 23.788  25.201 -27.989 1.00 60.42  ? 251 ARG C CD  1 
ATOM   6153  N N   . VAL C  1 252 ? 28.010  23.490 -24.467 1.00 46.53  ? 252 VAL C N   1 
ATOM   6154  C CA  . VAL C  1 252 ? 29.252  22.685 -24.258 1.00 46.97  ? 252 VAL C CA  1 
ATOM   6155  C C   . VAL C  1 252 ? 29.132  21.938 -22.926 1.00 45.00  ? 252 VAL C C   1 
ATOM   6156  O O   . VAL C  1 252 ? 29.119  20.696 -22.945 1.00 44.71  ? 252 VAL C O   1 
ATOM   6157  C CB  . VAL C  1 252 ? 30.518  23.565 -24.284 1.00 45.92  ? 252 VAL C CB  1 
ATOM   6158  C CG1 . VAL C  1 252 ? 31.759  22.779 -23.889 1.00 43.53  ? 252 VAL C CG1 1 
ATOM   6159  C CG2 . VAL C  1 252 ? 30.720  24.230 -25.637 1.00 48.47  ? 252 VAL C CG2 1 
ATOM   6160  N N   . ALA C  1 253 ? 29.052  22.681 -21.819 1.00 48.02  ? 253 ALA C N   1 
ATOM   6161  C CA  . ALA C  1 253 ? 28.980  22.159 -20.434 1.00 50.58  ? 253 ALA C CA  1 
ATOM   6162  C C   . ALA C  1 253 ? 27.965  21.013 -20.357 1.00 53.07  ? 253 ALA C C   1 
ATOM   6163  O O   . ALA C  1 253 ? 28.266  20.003 -19.692 1.00 55.82  ? 253 ALA C O   1 
ATOM   6164  C CB  . ALA C  1 253 ? 28.622  23.276 -19.485 1.00 48.50  ? 253 ALA C CB  1 
ATOM   6165  N N   . LYS C  1 254 ? 26.808  21.171 -21.009 1.00 52.91  ? 254 LYS C N   1 
ATOM   6166  C CA  . LYS C  1 254 ? 25.703  20.173 -21.012 1.00 56.45  ? 254 LYS C CA  1 
ATOM   6167  C C   . LYS C  1 254 ? 26.169  18.908 -21.741 1.00 59.61  ? 254 LYS C C   1 
ATOM   6168  O O   . LYS C  1 254 ? 26.001  17.807 -21.183 1.00 63.02  ? 254 LYS C O   1 
ATOM   6169  C CB  . LYS C  1 254 ? 24.450  20.758 -21.669 1.00 56.35  ? 254 LYS C CB  1 
ATOM   6170  C CG  . LYS C  1 254 ? 23.753  21.846 -20.863 1.00 62.41  ? 254 LYS C CG  1 
ATOM   6171  C CD  . LYS C  1 254 ? 22.571  22.472 -21.572 1.00 62.53  ? 254 LYS C CD  1 
ATOM   6172  C CE  . LYS C  1 254 ? 21.387  21.537 -21.693 1.00 63.03  ? 254 LYS C CE  1 
ATOM   6173  N NZ  . LYS C  1 254 ? 20.286  22.148 -22.474 1.00 65.43  ? 254 LYS C NZ  1 
ATOM   6174  N N   . LEU C  1 255 ? 26.728  19.070 -22.944 1.00 64.76  ? 255 LEU C N   1 
ATOM   6175  C CA  . LEU C  1 255 ? 27.279  17.962 -23.768 1.00 66.16  ? 255 LEU C CA  1 
ATOM   6176  C C   . LEU C  1 255 ? 28.316  17.187 -22.949 1.00 57.62  ? 255 LEU C C   1 
ATOM   6177  O O   . LEU C  1 255 ? 28.198  15.950 -22.865 1.00 60.44  ? 255 LEU C O   1 
ATOM   6178  C CB  . LEU C  1 255 ? 27.901  18.542 -25.041 1.00 75.42  ? 255 LEU C CB  1 
ATOM   6179  C CG  . LEU C  1 255 ? 27.085  18.323 -26.311 1.00 79.49  ? 255 LEU C CG  1 
ATOM   6180  C CD1 . LEU C  1 255 ? 27.892  18.699 -27.545 1.00 79.40  ? 255 LEU C CD1 1 
ATOM   6181  C CD2 . LEU C  1 255 ? 26.614  16.879 -26.396 1.00 93.24  ? 255 LEU C CD2 1 
ATOM   6182  N N   . ARG C  1 256 ? 29.285  17.900 -22.370 1.00 52.62  ? 256 ARG C N   1 
ATOM   6183  C CA  . ARG C  1 256 ? 30.390  17.323 -21.560 1.00 54.49  ? 256 ARG C CA  1 
ATOM   6184  C C   . ARG C  1 256 ? 29.804  16.623 -20.329 1.00 48.74  ? 256 ARG C C   1 
ATOM   6185  O O   . ARG C  1 256 ? 30.332  15.562 -19.953 1.00 47.03  ? 256 ARG C O   1 
ATOM   6186  C CB  . ARG C  1 256 ? 31.379  18.425 -21.173 1.00 61.85  ? 256 ARG C CB  1 
ATOM   6187  C CG  . ARG C  1 256 ? 32.251  18.896 -22.328 1.00 73.10  ? 256 ARG C CG  1 
ATOM   6188  C CD  . ARG C  1 256 ? 33.669  18.372 -22.230 1.00 83.14  ? 256 ARG C CD  1 
ATOM   6189  N NE  . ARG C  1 256 ? 34.549  19.325 -21.568 1.00 93.02  ? 256 ARG C NE  1 
ATOM   6190  C CZ  . ARG C  1 256 ? 35.712  19.016 -21.004 1.00 103.78 ? 256 ARG C CZ  1 
ATOM   6191  N NH1 . ARG C  1 256 ? 36.142  17.766 -21.010 1.00 105.14 ? 256 ARG C NH1 1 
ATOM   6192  N NH2 . ARG C  1 256 ? 36.437  19.957 -20.429 1.00 114.11 ? 256 ARG C NH2 1 
ATOM   6193  N N   . THR C  1 257 ? 28.757  17.198 -19.730 1.00 46.81  ? 257 THR C N   1 
ATOM   6194  C CA  . THR C  1 257 ? 28.037  16.628 -18.559 1.00 45.50  ? 257 THR C CA  1 
ATOM   6195  C C   . THR C  1 257 ? 27.348  15.324 -18.974 1.00 48.89  ? 257 THR C C   1 
ATOM   6196  O O   . THR C  1 257 ? 27.517  14.317 -18.264 1.00 53.66  ? 257 THR C O   1 
ATOM   6197  C CB  . THR C  1 257 ? 27.013  17.613 -17.983 1.00 40.40  ? 257 THR C CB  1 
ATOM   6198  O OG1 . THR C  1 257 ? 27.710  18.784 -17.556 1.00 36.60  ? 257 THR C OG1 1 
ATOM   6199  C CG2 . THR C  1 257 ? 26.229  17.026 -16.829 1.00 39.08  ? 257 THR C CG2 1 
ATOM   6200  N N   . ALA C  1 258 ? 26.596  15.359 -20.077 1.00 53.30  ? 258 ALA C N   1 
ATOM   6201  C CA  . ALA C  1 258 ? 25.862  14.206 -20.647 1.00 57.13  ? 258 ALA C CA  1 
ATOM   6202  C C   . ALA C  1 258 ? 26.853  13.078 -20.957 1.00 63.73  ? 258 ALA C C   1 
ATOM   6203  O O   . ALA C  1 258 ? 26.563  11.917 -20.602 1.00 62.42  ? 258 ALA C O   1 
ATOM   6204  C CB  . ALA C  1 258 ? 25.107  14.638 -21.880 1.00 54.27  ? 258 ALA C CB  1 
ATOM   6205  N N   . GLU C  1 259 ? 27.980  13.418 -21.589 1.00 65.04  ? 259 GLU C N   1 
ATOM   6206  C CA  . GLU C  1 259 ? 29.062  12.465 -21.955 1.00 63.56  ? 259 GLU C CA  1 
ATOM   6207  C C   . GLU C  1 259 ? 29.533  11.735 -20.694 1.00 68.21  ? 259 GLU C C   1 
ATOM   6208  O O   . GLU C  1 259 ? 29.527  10.492 -20.704 1.00 75.63  ? 259 GLU C O   1 
ATOM   6209  C CB  . GLU C  1 259 ? 30.215  13.203 -22.634 1.00 68.40  ? 259 GLU C CB  1 
ATOM   6210  C CG  . GLU C  1 259 ? 29.892  13.636 -24.052 1.00 79.07  ? 259 GLU C CG  1 
ATOM   6211  C CD  . GLU C  1 259 ? 30.948  14.502 -24.715 1.00 85.35  ? 259 GLU C CD  1 
ATOM   6212  O OE1 . GLU C  1 259 ? 31.981  14.777 -24.067 1.00 90.91  ? 259 GLU C OE1 1 
ATOM   6213  O OE2 . GLU C  1 259 ? 30.735  14.896 -25.880 1.00 83.69  ? 259 GLU C OE2 1 
ATOM   6214  N N   . ASP C  1 260 ? 29.914  12.483 -19.654 1.00 66.32  ? 260 ASP C N   1 
ATOM   6215  C CA  . ASP C  1 260 ? 30.385  11.940 -18.351 1.00 68.01  ? 260 ASP C CA  1 
ATOM   6216  C C   . ASP C  1 260 ? 29.354  10.936 -17.820 1.00 61.14  ? 260 ASP C C   1 
ATOM   6217  O O   . ASP C  1 260 ? 29.774  9.882  -17.308 1.00 58.19  ? 260 ASP C O   1 
ATOM   6218  C CB  . ASP C  1 260 ? 30.646  13.060 -17.340 1.00 79.21  ? 260 ASP C CB  1 
ATOM   6219  C CG  . ASP C  1 260 ? 31.893  13.877 -17.637 1.00 81.53  ? 260 ASP C CG  1 
ATOM   6220  O OD1 . ASP C  1 260 ? 32.167  14.827 -16.874 1.00 82.11  ? 260 ASP C OD1 1 
ATOM   6221  O OD2 . ASP C  1 260 ? 32.580  13.558 -18.628 1.00 78.42  ? 260 ASP C OD2 1 
ATOM   6222  N N   . VAL C  1 261 ? 28.062  11.254 -17.942 1.00 55.85  ? 261 VAL C N   1 
ATOM   6223  C CA  . VAL C  1 261 ? 26.937  10.389 -17.474 1.00 56.25  ? 261 VAL C CA  1 
ATOM   6224  C C   . VAL C  1 261 ? 26.937  9.097  -18.298 1.00 52.51  ? 261 VAL C C   1 
ATOM   6225  O O   . VAL C  1 261 ? 26.891  8.010  -17.687 1.00 49.99  ? 261 VAL C O   1 
ATOM   6226  C CB  . VAL C  1 261 ? 25.580  11.113 -17.567 1.00 58.97  ? 261 VAL C CB  1 
ATOM   6227  C CG1 . VAL C  1 261 ? 24.410  10.156 -17.390 1.00 56.91  ? 261 VAL C CG1 1 
ATOM   6228  C CG2 . VAL C  1 261 ? 25.485  12.258 -16.572 1.00 67.84  ? 261 VAL C CG2 1 
ATOM   6229  N N   . ARG C  1 262 ? 26.991  9.219  -19.628 1.00 49.57  ? 262 ARG C N   1 
ATOM   6230  C CA  . ARG C  1 262 ? 26.966  8.076  -20.580 1.00 54.59  ? 262 ARG C CA  1 
ATOM   6231  C C   . ARG C  1 262 ? 28.206  7.200  -20.365 1.00 55.86  ? 262 ARG C C   1 
ATOM   6232  O O   . ARG C  1 262 ? 28.062  5.964  -20.368 1.00 51.29  ? 262 ARG C O   1 
ATOM   6233  C CB  . ARG C  1 262 ? 26.893  8.574  -22.027 1.00 60.25  ? 262 ARG C CB  1 
ATOM   6234  C CG  . ARG C  1 262 ? 25.544  9.162  -22.418 1.00 65.99  ? 262 ARG C CG  1 
ATOM   6235  C CD  . ARG C  1 262 ? 25.369  9.285  -23.922 1.00 68.46  ? 262 ARG C CD  1 
ATOM   6236  N NE  . ARG C  1 262 ? 26.430  10.062 -24.551 1.00 72.53  ? 262 ARG C NE  1 
ATOM   6237  C CZ  . ARG C  1 262 ? 26.352  11.356 -24.846 1.00 73.67  ? 262 ARG C CZ  1 
ATOM   6238  N NH1 . ARG C  1 262 ? 25.253  12.039 -24.574 1.00 75.75  ? 262 ARG C NH1 1 
ATOM   6239  N NH2 . ARG C  1 262 ? 27.376  11.964 -25.416 1.00 79.49  ? 262 ARG C NH2 1 
ATOM   6240  N N   . ALA C  1 263 ? 29.377  7.821  -20.187 1.00 65.36  ? 263 ALA C N   1 
ATOM   6241  C CA  . ALA C  1 263 ? 30.678  7.146  -19.964 1.00 68.02  ? 263 ALA C CA  1 
ATOM   6242  C C   . ALA C  1 263 ? 30.697  6.502  -18.572 1.00 64.14  ? 263 ALA C C   1 
ATOM   6243  O O   . ALA C  1 263 ? 31.672  5.790  -18.263 1.00 60.21  ? 263 ALA C O   1 
ATOM   6244  C CB  . ALA C  1 263 ? 31.806  8.135  -20.127 1.00 72.45  ? 263 ALA C CB  1 
ATOM   6245  N N   . GLY C  1 264 ? 29.658  6.753  -17.768 1.00 62.01  ? 264 GLY C N   1 
ATOM   6246  C CA  . GLY C  1 264 ? 29.513  6.222  -16.399 1.00 60.58  ? 264 GLY C CA  1 
ATOM   6247  C C   . GLY C  1 264 ? 30.552  6.803  -15.454 1.00 59.93  ? 264 GLY C C   1 
ATOM   6248  O O   . GLY C  1 264 ? 30.863  6.139  -14.445 1.00 55.72  ? 264 GLY C O   1 
ATOM   6249  N N   . ASP C  1 265 ? 31.069  7.996  -15.766 1.00 65.64  ? 265 ASP C N   1 
ATOM   6250  C CA  . ASP C  1 265 ? 32.083  8.720  -14.952 1.00 72.23  ? 265 ASP C CA  1 
ATOM   6251  C C   . ASP C  1 265 ? 31.386  9.430  -13.788 1.00 73.91  ? 265 ASP C C   1 
ATOM   6252  O O   . ASP C  1 265 ? 32.028  9.606  -12.735 1.00 79.62  ? 265 ASP C O   1 
ATOM   6253  C CB  . ASP C  1 265 ? 32.866  9.728  -15.798 1.00 75.40  ? 265 ASP C CB  1 
ATOM   6254  C CG  . ASP C  1 265 ? 33.846  9.084  -16.761 1.00 82.64  ? 265 ASP C CG  1 
ATOM   6255  O OD1 . ASP C  1 265 ? 34.336  7.980  -16.447 1.00 91.86  ? 265 ASP C OD1 1 
ATOM   6256  O OD2 . ASP C  1 265 ? 34.113  9.693  -17.817 1.00 85.38  ? 265 ASP C OD2 1 
ATOM   6257  N N   . ASP C  1 266 ? 30.125  9.824  -13.985 1.00 71.78  ? 266 ASP C N   1 
ATOM   6258  C CA  . ASP C  1 266 ? 29.311  10.569 -12.989 1.00 69.67  ? 266 ASP C CA  1 
ATOM   6259  C C   . ASP C  1 266 ? 27.829  10.293 -13.260 1.00 57.97  ? 266 ASP C C   1 
ATOM   6260  O O   . ASP C  1 266 ? 27.531  9.559  -14.221 1.00 51.71  ? 266 ASP C O   1 
ATOM   6261  C CB  . ASP C  1 266 ? 29.624  12.068 -13.040 1.00 74.92  ? 266 ASP C CB  1 
ATOM   6262  C CG  . ASP C  1 266 ? 29.531  12.770 -11.695 1.00 72.05  ? 266 ASP C CG  1 
ATOM   6263  O OD1 . ASP C  1 266 ? 30.324  13.706 -11.473 1.00 70.59  ? 266 ASP C OD1 1 
ATOM   6264  O OD2 . ASP C  1 266 ? 28.667  12.377 -10.882 1.00 66.01  ? 266 ASP C OD2 1 
ATOM   6265  N N   . VAL C  1 267 ? 26.945  10.870 -12.441 1.00 57.35  ? 267 VAL C N   1 
ATOM   6266  C CA  . VAL C  1 267 ? 25.463  10.726 -12.546 1.00 55.26  ? 267 VAL C CA  1 
ATOM   6267  C C   . VAL C  1 267 ? 24.828  12.116 -12.396 1.00 54.37  ? 267 VAL C C   1 
ATOM   6268  O O   . VAL C  1 267 ? 25.414  12.958 -11.689 1.00 55.39  ? 267 VAL C O   1 
ATOM   6269  C CB  . VAL C  1 267 ? 24.933  9.728  -11.497 1.00 54.60  ? 267 VAL C CB  1 
ATOM   6270  C CG1 . VAL C  1 267 ? 25.357  10.109 -10.089 1.00 53.46  ? 267 VAL C CG1 1 
ATOM   6271  C CG2 . VAL C  1 267 ? 23.423  9.565  -11.576 1.00 65.00  ? 267 VAL C CG2 1 
ATOM   6272  N N   . HIS C  1 268 ? 23.688  12.347 -13.058 1.00 54.93  ? 268 HIS C N   1 
ATOM   6273  C CA  . HIS C  1 268 ? 22.936  13.632 -13.043 1.00 55.37  ? 268 HIS C CA  1 
ATOM   6274  C C   . HIS C  1 268 ? 21.466  13.353 -12.744 1.00 56.63  ? 268 HIS C C   1 
ATOM   6275  O O   . HIS C  1 268 ? 20.852  12.497 -13.377 1.00 54.83  ? 268 HIS C O   1 
ATOM   6276  C CB  . HIS C  1 268 ? 23.137  14.386 -14.365 1.00 57.70  ? 268 HIS C CB  1 
ATOM   6277  C CG  . HIS C  1 268 ? 22.881  15.853 -14.266 1.00 57.02  ? 268 HIS C CG  1 
ATOM   6278  N ND1 . HIS C  1 268 ? 21.769  16.449 -14.828 1.00 54.48  ? 268 HIS C ND1 1 
ATOM   6279  C CD2 . HIS C  1 268 ? 23.580  16.843 -13.670 1.00 62.55  ? 268 HIS C CD2 1 
ATOM   6280  C CE1 . HIS C  1 268 ? 21.795  17.744 -14.584 1.00 56.70  ? 268 HIS C CE1 1 
ATOM   6281  N NE2 . HIS C  1 268 ? 22.895  18.010 -13.874 1.00 62.97  ? 268 HIS C NE2 1 
ATOM   6282  N N   . PRO C  1 269 ? 20.855  14.082 -11.781 1.00 58.05  ? 269 PRO C N   1 
ATOM   6283  C CA  . PRO C  1 269 ? 19.540  13.719 -11.249 1.00 54.92  ? 269 PRO C CA  1 
ATOM   6284  C C   . PRO C  1 269 ? 18.360  14.015 -12.191 1.00 58.47  ? 269 PRO C C   1 
ATOM   6285  O O   . PRO C  1 269 ? 17.246  13.649 -11.854 1.00 56.01  ? 269 PRO C O   1 
ATOM   6286  C CB  . PRO C  1 269 ? 19.444  14.578 -9.980  1.00 53.81  ? 269 PRO C CB  1 
ATOM   6287  C CG  . PRO C  1 269 ? 20.255  15.811 -10.311 1.00 54.16  ? 269 PRO C CG  1 
ATOM   6288  C CD  . PRO C  1 269 ? 21.400  15.300 -11.161 1.00 57.20  ? 269 PRO C CD  1 
ATOM   6289  N N   . GLU C  1 270 ? 18.625  14.659 -13.332 1.00 56.96  ? 270 GLU C N   1 
ATOM   6290  C CA  . GLU C  1 270 ? 17.604  14.973 -14.369 1.00 54.05  ? 270 GLU C CA  1 
ATOM   6291  C C   . GLU C  1 270 ? 18.154  14.600 -15.751 1.00 52.74  ? 270 GLU C C   1 
ATOM   6292  O O   . GLU C  1 270 ? 19.392  14.565 -15.908 1.00 48.67  ? 270 GLU C O   1 
ATOM   6293  C CB  . GLU C  1 270 ? 17.222  16.454 -14.317 1.00 59.90  ? 270 GLU C CB  1 
ATOM   6294  C CG  . GLU C  1 270 ? 18.239  17.371 -14.973 1.00 68.66  ? 270 GLU C CG  1 
ATOM   6295  C CD  . GLU C  1 270 ? 17.838  18.837 -15.021 1.00 73.34  ? 270 GLU C CD  1 
ATOM   6296  O OE1 . GLU C  1 270 ? 16.875  19.208 -14.321 1.00 70.22  ? 270 GLU C OE1 1 
ATOM   6297  O OE2 . GLU C  1 270 ? 18.489  19.603 -15.760 1.00 77.12  ? 270 GLU C OE2 1 
ATOM   6298  N N   . SER C  1 271 ? 17.263  14.325 -16.708 1.00 51.63  ? 271 SER C N   1 
ATOM   6299  C CA  . SER C  1 271 ? 17.603  14.069 -18.132 1.00 49.01  ? 271 SER C CA  1 
ATOM   6300  C C   . SER C  1 271 ? 18.079  15.374 -18.776 1.00 49.10  ? 271 SER C C   1 
ATOM   6301  O O   . SER C  1 271 ? 17.466  16.424 -18.509 1.00 47.74  ? 271 SER C O   1 
ATOM   6302  C CB  . SER C  1 271 ? 16.438  13.477 -18.879 1.00 47.62  ? 271 SER C CB  1 
ATOM   6303  O OG  . SER C  1 271 ? 15.232  14.143 -18.542 1.00 48.40  ? 271 SER C OG  1 
ATOM   6304  N N   . ILE C  1 272 ? 19.144  15.303 -19.579 1.00 51.99  ? 272 ILE C N   1 
ATOM   6305  C CA  . ILE C  1 272 ? 19.753  16.471 -20.281 1.00 52.48  ? 272 ILE C CA  1 
ATOM   6306  C C   . ILE C  1 272 ? 19.319  16.438 -21.750 1.00 55.07  ? 272 ILE C C   1 
ATOM   6307  O O   . ILE C  1 272 ? 19.425  15.362 -22.370 1.00 48.84  ? 272 ILE C O   1 
ATOM   6308  C CB  . ILE C  1 272 ? 21.286  16.460 -20.129 1.00 52.01  ? 272 ILE C CB  1 
ATOM   6309  C CG1 . ILE C  1 272 ? 21.701  16.556 -18.659 1.00 54.11  ? 272 ILE C CG1 1 
ATOM   6310  C CG2 . ILE C  1 272 ? 21.921  17.557 -20.971 1.00 53.42  ? 272 ILE C CG2 1 
ATOM   6311  C CD1 . ILE C  1 272 ? 23.187  16.419 -18.427 1.00 58.38  ? 272 ILE C CD1 1 
ATOM   6312  N N   . TRP C  1 273 ? 18.842  17.575 -22.267 1.00 59.90  ? 273 TRP C N   1 
ATOM   6313  C CA  . TRP C  1 273 ? 18.313  17.729 -23.648 1.00 57.19  ? 273 TRP C CA  1 
ATOM   6314  C C   . TRP C  1 273 ? 19.073  18.840 -24.376 1.00 57.00  ? 273 TRP C C   1 
ATOM   6315  O O   . TRP C  1 273 ? 19.524  19.787 -23.706 1.00 53.75  ? 273 TRP C O   1 
ATOM   6316  C CB  . TRP C  1 273 ? 16.808  18.019 -23.617 1.00 53.86  ? 273 TRP C CB  1 
ATOM   6317  C CG  . TRP C  1 273 ? 15.998  16.940 -22.968 1.00 54.39  ? 273 TRP C CG  1 
ATOM   6318  C CD1 . TRP C  1 273 ? 15.870  16.703 -21.630 1.00 53.19  ? 273 TRP C CD1 1 
ATOM   6319  C CD2 . TRP C  1 273 ? 15.204  15.940 -23.630 1.00 55.20  ? 273 TRP C CD2 1 
ATOM   6320  N NE1 . TRP C  1 273 ? 15.047  15.632 -21.414 1.00 56.84  ? 273 TRP C NE1 1 
ATOM   6321  C CE2 . TRP C  1 273 ? 14.622  15.143 -22.621 1.00 56.08  ? 273 TRP C CE2 1 
ATOM   6322  C CE3 . TRP C  1 273 ? 14.922  15.644 -24.969 1.00 54.82  ? 273 TRP C CE3 1 
ATOM   6323  C CZ2 . TRP C  1 273 ? 13.780  14.072 -22.913 1.00 58.46  ? 273 TRP C CZ2 1 
ATOM   6324  C CZ3 . TRP C  1 273 ? 14.087  14.587 -25.255 1.00 57.66  ? 273 TRP C CZ3 1 
ATOM   6325  C CH2 . TRP C  1 273 ? 13.527  13.812 -24.239 1.00 57.94  ? 273 TRP C CH2 1 
ATOM   6326  N N   . ILE C  1 274 ? 19.202  18.711 -25.699 1.00 70.96  ? 274 ILE C N   1 
ATOM   6327  C CA  . ILE C  1 274 ? 19.782  19.745 -26.607 1.00 79.14  ? 274 ILE C CA  1 
ATOM   6328  C C   . ILE C  1 274 ? 18.988  19.728 -27.918 1.00 78.71  ? 274 ILE C C   1 
ATOM   6329  O O   . ILE C  1 274 ? 19.037  18.705 -28.629 1.00 70.14  ? 274 ILE C O   1 
ATOM   6330  C CB  . ILE C  1 274 ? 21.291  19.510 -26.833 1.00 74.95  ? 274 ILE C CB  1 
ATOM   6331  C CG1 . ILE C  1 274 ? 22.069  19.545 -25.514 1.00 70.77  ? 274 ILE C CG1 1 
ATOM   6332  C CG2 . ILE C  1 274 ? 21.846  20.507 -27.840 1.00 79.13  ? 274 ILE C CG2 1 
ATOM   6333  C CD1 . ILE C  1 274 ? 23.557  19.322 -25.666 1.00 71.50  ? 274 ILE C CD1 1 
ATOM   6334  N N   . SER C  1 275 ? 18.269  20.816 -28.204 1.00 83.41  ? 275 SER C N   1 
ATOM   6335  C CA  . SER C  1 275 ? 17.413  20.979 -29.407 1.00 90.19  ? 275 SER C CA  1 
ATOM   6336  C C   . SER C  1 275 ? 16.361  19.865 -29.444 1.00 94.15  ? 275 SER C C   1 
ATOM   6337  O O   . SER C  1 275 ? 16.027  19.403 -30.552 1.00 116.38 ? 275 SER C O   1 
ATOM   6338  C CB  . SER C  1 275 ? 18.248  20.994 -30.661 1.00 95.44  ? 275 SER C CB  1 
ATOM   6339  O OG  . SER C  1 275 ? 19.199  22.047 -30.621 1.00 106.67 ? 275 SER C OG  1 
ATOM   6340  N N   . SER C  1 276 ? 15.876  19.449 -28.269 1.00 96.78  ? 276 SER C N   1 
ATOM   6341  C CA  . SER C  1 276 ? 14.766  18.476 -28.086 1.00 97.11  ? 276 SER C CA  1 
ATOM   6342  C C   . SER C  1 276 ? 15.267  17.040 -28.283 1.00 87.66  ? 276 SER C C   1 
ATOM   6343  O O   . SER C  1 276 ? 14.419  16.129 -28.344 1.00 81.92  ? 276 SER C O   1 
ATOM   6344  C CB  . SER C  1 276 ? 13.624  18.783 -29.019 1.00 104.16 ? 276 SER C CB  1 
ATOM   6345  O OG  . SER C  1 276 ? 13.144  20.103 -28.813 1.00 111.95 ? 276 SER C OG  1 
ATOM   6346  N N   . VAL C  1 277 ? 16.587  16.850 -28.375 1.00 79.26  ? 277 VAL C N   1 
ATOM   6347  C CA  . VAL C  1 277 ? 17.241  15.513 -28.505 1.00 75.97  ? 277 VAL C CA  1 
ATOM   6348  C C   . VAL C  1 277 ? 17.873  15.150 -27.156 1.00 69.06  ? 277 VAL C C   1 
ATOM   6349  O O   . VAL C  1 277 ? 18.773  15.888 -26.708 1.00 66.97  ? 277 VAL C O   1 
ATOM   6350  C CB  . VAL C  1 277 ? 18.284  15.502 -29.639 1.00 72.76  ? 277 VAL C CB  1 
ATOM   6351  C CG1 . VAL C  1 277 ? 19.001  14.164 -29.735 1.00 71.32  ? 277 VAL C CG1 1 
ATOM   6352  C CG2 . VAL C  1 277 ? 17.666  15.875 -30.977 1.00 69.91  ? 277 VAL C CG2 1 
ATOM   6353  N N   . LYS C  1 278 ? 17.412  14.059 -26.535 1.00 62.35  ? 278 LYS C N   1 
ATOM   6354  C CA  . LYS C  1 278 ? 17.911  13.576 -25.220 1.00 60.30  ? 278 LYS C CA  1 
ATOM   6355  C C   . LYS C  1 278 ? 19.397  13.219 -25.352 1.00 56.47  ? 278 LYS C C   1 
ATOM   6356  O O   . LYS C  1 278 ? 19.771  12.616 -26.373 1.00 55.60  ? 278 LYS C O   1 
ATOM   6357  C CB  . LYS C  1 278 ? 17.090  12.378 -24.732 1.00 59.04  ? 278 LYS C CB  1 
ATOM   6358  C CG  . LYS C  1 278 ? 17.486  11.845 -23.361 1.00 60.89  ? 278 LYS C CG  1 
ATOM   6359  C CD  . LYS C  1 278 ? 16.667  10.660 -22.900 1.00 63.79  ? 278 LYS C CD  1 
ATOM   6360  C CE  . LYS C  1 278 ? 15.260  11.038 -22.489 1.00 68.00  ? 278 LYS C CE  1 
ATOM   6361  N NZ  . LYS C  1 278 ? 14.568  9.912  -21.818 1.00 70.01  ? 278 LYS C NZ  1 
ATOM   6362  N N   . GLN C  1 279 ? 20.202  13.587 -24.351 1.00 58.46  ? 279 GLN C N   1 
ATOM   6363  C CA  . GLN C  1 279 ? 21.677  13.392 -24.329 1.00 56.90  ? 279 GLN C CA  1 
ATOM   6364  C C   . GLN C  1 279 ? 22.043  12.387 -23.233 1.00 56.96  ? 279 GLN C C   1 
ATOM   6365  O O   . GLN C  1 279 ? 22.848  11.477 -23.505 1.00 52.51  ? 279 GLN C O   1 
ATOM   6366  C CB  . GLN C  1 279 ? 22.376  14.731 -24.093 1.00 57.89  ? 279 GLN C CB  1 
ATOM   6367  C CG  . GLN C  1 279 ? 22.110  15.751 -25.188 1.00 61.13  ? 279 GLN C CG  1 
ATOM   6368  C CD  . GLN C  1 279 ? 22.729  15.329 -26.497 1.00 72.39  ? 279 GLN C CD  1 
ATOM   6369  O OE1 . GLN C  1 279 ? 23.895  14.941 -26.556 1.00 80.58  ? 279 GLN C OE1 1 
ATOM   6370  N NE2 . GLN C  1 279 ? 21.946  15.402 -27.562 1.00 78.94  ? 279 GLN C NE2 1 
ATOM   6371  N N   . SER C  1 280 ? 21.481  12.565 -22.036 1.00 59.79  ? 280 SER C N   1 
ATOM   6372  C CA  . SER C  1 280 ? 21.670  11.672 -20.864 1.00 62.74  ? 280 SER C CA  1 
ATOM   6373  C C   . SER C  1 280 ? 20.307  11.375 -20.233 1.00 62.82  ? 280 SER C C   1 
ATOM   6374  O O   . SER C  1 280 ? 19.342  12.101 -20.543 1.00 62.45  ? 280 SER C O   1 
ATOM   6375  C CB  . SER C  1 280 ? 22.611  12.288 -19.862 1.00 70.53  ? 280 SER C CB  1 
ATOM   6376  O OG  . SER C  1 280 ? 21.910  13.124 -18.951 1.00 75.34  ? 280 SER C OG  1 
ATOM   6377  N N   . ASP C  1 281 ? 20.242  10.346 -19.386 1.00 65.62  ? 281 ASP C N   1 
ATOM   6378  C CA  . ASP C  1 281 ? 19.031  9.978  -18.606 1.00 63.30  ? 281 ASP C CA  1 
ATOM   6379  C C   . ASP C  1 281 ? 19.251  10.386 -17.148 1.00 53.43  ? 281 ASP C C   1 
ATOM   6380  O O   . ASP C  1 281 ? 20.418  10.412 -16.712 1.00 48.59  ? 281 ASP C O   1 
ATOM   6381  C CB  . ASP C  1 281 ? 18.722  8.483  -18.721 1.00 67.00  ? 281 ASP C CB  1 
ATOM   6382  C CG  . ASP C  1 281 ? 18.060  8.092  -20.030 1.00 75.70  ? 281 ASP C CG  1 
ATOM   6383  O OD1 . ASP C  1 281 ? 17.426  7.020  -20.064 1.00 101.14 ? 281 ASP C OD1 1 
ATOM   6384  O OD2 . ASP C  1 281 ? 18.186  8.859  -21.004 1.00 91.91  ? 281 ASP C OD2 1 
ATOM   6385  N N   . ALA C  1 282 ? 18.169  10.702 -16.435 1.00 47.99  ? 282 ALA C N   1 
ATOM   6386  C CA  . ALA C  1 282 ? 18.181  11.007 -14.988 1.00 48.06  ? 282 ALA C CA  1 
ATOM   6387  C C   . ALA C  1 282 ? 18.679  9.773  -14.230 1.00 47.91  ? 282 ALA C C   1 
ATOM   6388  O O   . ALA C  1 282 ? 18.272  8.651  -14.593 1.00 39.33  ? 282 ALA C O   1 
ATOM   6389  C CB  . ALA C  1 282 ? 16.805  11.422 -14.529 1.00 51.08  ? 282 ALA C CB  1 
ATOM   6390  N N   . GLY C  1 283 ? 19.543  9.983  -13.235 1.00 47.02  ? 283 GLY C N   1 
ATOM   6391  C CA  . GLY C  1 283 ? 20.081  8.927  -12.359 1.00 47.71  ? 283 GLY C CA  1 
ATOM   6392  C C   . GLY C  1 283 ? 20.398  9.469  -10.977 1.00 51.16  ? 283 GLY C C   1 
ATOM   6393  O O   . GLY C  1 283 ? 20.755  10.658 -10.875 1.00 56.05  ? 283 GLY C O   1 
ATOM   6394  N N   . LEU C  1 284 ? 20.266  8.630  -9.948  1.00 52.49  ? 284 LEU C N   1 
ATOM   6395  C CA  . LEU C  1 284 ? 20.643  8.964  -8.552  1.00 51.15  ? 284 LEU C CA  1 
ATOM   6396  C C   . LEU C  1 284 ? 21.928  8.227  -8.196  1.00 51.93  ? 284 LEU C C   1 
ATOM   6397  O O   . LEU C  1 284 ? 22.224  7.172  -8.755  1.00 45.03  ? 284 LEU C O   1 
ATOM   6398  C CB  . LEU C  1 284 ? 19.506  8.566  -7.606  1.00 53.90  ? 284 LEU C CB  1 
ATOM   6399  C CG  . LEU C  1 284 ? 18.222  9.384  -7.732  1.00 51.43  ? 284 LEU C CG  1 
ATOM   6400  C CD1 . LEU C  1 284 ? 17.235  9.002  -6.642  1.00 52.20  ? 284 LEU C CD1 1 
ATOM   6401  C CD2 . LEU C  1 284 ? 18.515  10.874 -7.679  1.00 55.12  ? 284 LEU C CD2 1 
ATOM   6402  N N   . PRO C  1 285 ? 22.739  8.777  -7.268  1.00 56.87  ? 285 PRO C N   1 
ATOM   6403  C CA  . PRO C  1 285 ? 23.866  8.043  -6.698  1.00 61.99  ? 285 PRO C CA  1 
ATOM   6404  C C   . PRO C  1 285 ? 23.376  6.854  -5.858  1.00 66.84  ? 285 PRO C C   1 
ATOM   6405  O O   . PRO C  1 285 ? 22.264  6.900  -5.365  1.00 75.98  ? 285 PRO C O   1 
ATOM   6406  C CB  . PRO C  1 285 ? 24.583  9.071  -5.808  1.00 56.52  ? 285 PRO C CB  1 
ATOM   6407  C CG  . PRO C  1 285 ? 24.036  10.417 -6.245  1.00 57.17  ? 285 PRO C CG  1 
ATOM   6408  C CD  . PRO C  1 285 ? 22.631  10.142 -6.738  1.00 55.88  ? 285 PRO C CD  1 
ATOM   6409  N N   . ARG C  1 286 ? 24.215  5.825  -5.723  1.00 66.17  ? 286 ARG C N   1 
ATOM   6410  C CA  . ARG C  1 286 ? 24.000  4.669  -4.814  1.00 66.44  ? 286 ARG C CA  1 
ATOM   6411  C C   . ARG C  1 286 ? 23.821  5.179  -3.379  1.00 60.31  ? 286 ARG C C   1 
ATOM   6412  O O   . ARG C  1 286 ? 24.599  6.060  -2.967  1.00 66.03  ? 286 ARG C O   1 
ATOM   6413  C CB  . ARG C  1 286 ? 25.204  3.725  -4.892  1.00 73.88  ? 286 ARG C CB  1 
ATOM   6414  C CG  . ARG C  1 286 ? 26.538  4.417  -4.649  1.00 75.32  ? 286 ARG C CG  1 
ATOM   6415  C CD  . ARG C  1 286 ? 27.710  3.458  -4.617  1.00 81.14  ? 286 ARG C CD  1 
ATOM   6416  N NE  . ARG C  1 286 ? 27.794  2.718  -3.365  1.00 85.84  ? 286 ARG C NE  1 
ATOM   6417  C CZ  . ARG C  1 286 ? 28.662  2.976  -2.393  1.00 91.79  ? 286 ARG C CZ  1 
ATOM   6418  N NH1 . ARG C  1 286 ? 29.533  3.962  -2.526  1.00 93.24  ? 286 ARG C NH1 1 
ATOM   6419  N NH2 . ARG C  1 286 ? 28.661  2.246  -1.292  1.00 100.98 ? 286 ARG C NH2 1 
ATOM   6420  N N   . GLU C  1 287 ? 22.840  4.645  -2.646  1.00 56.97  ? 287 GLU C N   1 
ATOM   6421  C CA  . GLU C  1 287 ? 22.697  4.860  -1.180  1.00 56.63  ? 287 GLU C CA  1 
ATOM   6422  C C   . GLU C  1 287 ? 23.946  4.301  -0.489  1.00 60.78  ? 287 GLU C C   1 
ATOM   6423  O O   . GLU C  1 287 ? 24.430  3.239  -0.925  1.00 71.79  ? 287 GLU C O   1 
ATOM   6424  C CB  . GLU C  1 287 ? 21.435  4.183  -0.647  1.00 54.49  ? 287 GLU C CB  1 
ATOM   6425  C CG  . GLU C  1 287 ? 20.153  4.852  -1.099  1.00 58.18  ? 287 GLU C CG  1 
ATOM   6426  C CD  . GLU C  1 287 ? 18.895  4.143  -0.632  1.00 65.48  ? 287 GLU C CD  1 
ATOM   6427  O OE1 . GLU C  1 287 ? 18.958  3.470  0.414   1.00 72.63  ? 287 GLU C OE1 1 
ATOM   6428  O OE2 . GLU C  1 287 ? 17.861  4.258  -1.317  1.00 80.00  ? 287 GLU C OE2 1 
ATOM   6429  N N   . VAL C  1 288 ? 24.438  4.981  0.549   1.00 61.82  ? 288 VAL C N   1 
ATOM   6430  C CA  . VAL C  1 288 ? 25.759  4.689  1.181   1.00 63.87  ? 288 VAL C CA  1 
ATOM   6431  C C   . VAL C  1 288 ? 25.564  4.386  2.671   1.00 66.98  ? 288 VAL C C   1 
ATOM   6432  O O   . VAL C  1 288 ? 24.771  5.088  3.326   1.00 73.03  ? 288 VAL C O   1 
ATOM   6433  C CB  . VAL C  1 288 ? 26.744  5.851  0.958   1.00 58.79  ? 288 VAL C CB  1 
ATOM   6434  C CG1 . VAL C  1 288 ? 28.043  5.653  1.725   1.00 60.78  ? 288 VAL C CG1 1 
ATOM   6435  C CG2 . VAL C  1 288 ? 27.022  6.065  -0.521  1.00 54.39  ? 288 VAL C CG2 1 
ATOM   6436  N N   . TYR C  1 289 ? 26.260  3.358  3.164   1.00 71.16  ? 289 TYR C N   1 
ATOM   6437  C CA  . TYR C  1 289 ? 26.273  2.925  4.584   1.00 71.49  ? 289 TYR C CA  1 
ATOM   6438  C C   . TYR C  1 289 ? 27.537  3.479  5.251   1.00 69.22  ? 289 TYR C C   1 
ATOM   6439  O O   . TYR C  1 289 ? 28.582  3.558  4.574   1.00 64.20  ? 289 TYR C O   1 
ATOM   6440  C CB  . TYR C  1 289 ? 26.222  1.397  4.684   1.00 77.92  ? 289 TYR C CB  1 
ATOM   6441  C CG  . TYR C  1 289 ? 24.984  0.750  4.114   1.00 85.25  ? 289 TYR C CG  1 
ATOM   6442  C CD1 . TYR C  1 289 ? 23.856  0.554  4.893   1.00 88.67  ? 289 TYR C CD1 1 
ATOM   6443  C CD2 . TYR C  1 289 ? 24.943  0.315  2.799   1.00 88.90  ? 289 TYR C CD2 1 
ATOM   6444  C CE1 . TYR C  1 289 ? 22.717  -0.047 4.381   1.00 88.00  ? 289 TYR C CE1 1 
ATOM   6445  C CE2 . TYR C  1 289 ? 23.813  -0.286 2.270   1.00 90.37  ? 289 TYR C CE2 1 
ATOM   6446  C CZ  . TYR C  1 289 ? 22.696  -0.469 3.064   1.00 89.08  ? 289 TYR C CZ  1 
ATOM   6447  O OH  . TYR C  1 289 ? 21.578  -1.061 2.552   1.00 94.80  ? 289 TYR C OH  1 
ATOM   6448  N N   . LEU C  1 290 ? 27.435  3.855  6.530   1.00 66.13  ? 290 LEU C N   1 
ATOM   6449  C CA  . LEU C  1 290 ? 28.579  4.300  7.372   1.00 68.35  ? 290 LEU C CA  1 
ATOM   6450  C C   . LEU C  1 290 ? 28.756  3.319  8.538   1.00 69.83  ? 290 LEU C C   1 
ATOM   6451  O O   . LEU C  1 290 ? 28.817  3.698  9.709   1.00 70.22  ? 290 LEU C O   1 
ATOM   6452  C CB  . LEU C  1 290 ? 28.318  5.724  7.876   1.00 75.26  ? 290 LEU C CB  1 
ATOM   6453  C CG  . LEU C  1 290 ? 27.960  6.755  6.804   1.00 76.64  ? 290 LEU C CG  1 
ATOM   6454  C CD1 . LEU C  1 290 ? 28.159  8.172  7.325   1.00 68.02  ? 290 LEU C CD1 1 
ATOM   6455  C CD2 . LEU C  1 290 ? 28.774  6.539  5.537   1.00 80.21  ? 290 LEU C CD2 1 
ATOM   6456  N N   . LEU D  1 3   ? 0.949   65.049 -45.390 1.00 92.48  ? 3   LEU D N   1 
ATOM   6457  C CA  . LEU D  1 3   ? 1.882   66.085 -44.858 1.00 95.43  ? 3   LEU D CA  1 
ATOM   6458  C C   . LEU D  1 3   ? 2.317   65.704 -43.438 1.00 105.31 ? 3   LEU D C   1 
ATOM   6459  O O   . LEU D  1 3   ? 3.116   64.755 -43.303 1.00 117.32 ? 3   LEU D O   1 
ATOM   6460  C CB  . LEU D  1 3   ? 1.217   67.438 -44.893 1.00 91.80  ? 3   LEU D CB  1 
ATOM   6461  N N   . THR D  1 4   ? 1.819   66.423 -42.427 1.00 100.69 ? 4   THR D N   1 
ATOM   6462  C CA  . THR D  1 4   ? 2.036   66.121 -40.986 1.00 97.25  ? 4   THR D CA  1 
ATOM   6463  C C   . THR D  1 4   ? 0.703   65.677 -40.370 1.00 102.46 ? 4   THR D C   1 
ATOM   6464  O O   . THR D  1 4   ? 0.432   66.055 -39.214 1.00 92.91  ? 4   THR D O   1 
ATOM   6465  C CB  . THR D  1 4   ? 2.657   67.319 -40.255 1.00 95.18  ? 4   THR D CB  1 
ATOM   6466  O OG1 . THR D  1 4   ? 3.719   67.816 -41.070 1.00 99.77  ? 4   THR D OG1 1 
ATOM   6467  C CG2 . THR D  1 4   ? 3.186   66.963 -38.883 1.00 96.82  ? 4   THR D CG2 1 
ATOM   6468  N N   . ASN D  1 5   ? -0.084  64.897 -41.121 1.00 118.27 ? 5   ASN D N   1 
ATOM   6469  C CA  . ASN D  1 5   ? -1.430  64.407 -40.714 1.00 112.40 ? 5   ASN D CA  1 
ATOM   6470  C C   . ASN D  1 5   ? -1.306  63.579 -39.432 1.00 110.44 ? 5   ASN D C   1 
ATOM   6471  O O   . ASN D  1 5   ? -2.324  63.443 -38.720 1.00 102.09 ? 5   ASN D O   1 
ATOM   6472  C CB  . ASN D  1 5   ? -2.104  63.575 -41.808 1.00 103.69 ? 5   ASN D CB  1 
ATOM   6473  C CG  . ASN D  1 5   ? -2.343  64.346 -43.089 1.00 105.23 ? 5   ASN D CG  1 
ATOM   6474  O OD1 . ASN D  1 5   ? -2.913  63.813 -44.037 1.00 93.13  ? 5   ASN D OD1 1 
ATOM   6475  N ND2 . ASN D  1 5   ? -1.917  65.599 -43.128 1.00 110.12 ? 5   ASN D ND2 1 
ATOM   6476  N N   . VAL D  1 6   ? -0.115  63.031 -39.163 1.00 103.55 ? 6   VAL D N   1 
ATOM   6477  C CA  . VAL D  1 6   ? 0.198   62.315 -37.890 1.00 94.36  ? 6   VAL D CA  1 
ATOM   6478  C C   . VAL D  1 6   ? 0.075   63.319 -36.742 1.00 80.04  ? 6   VAL D C   1 
ATOM   6479  O O   . VAL D  1 6   ? 0.827   64.316 -36.746 1.00 71.73  ? 6   VAL D O   1 
ATOM   6480  C CB  . VAL D  1 6   ? 1.597   61.670 -37.888 1.00 91.96  ? 6   VAL D CB  1 
ATOM   6481  C CG1 . VAL D  1 6   ? 1.886   61.010 -36.549 1.00 91.89  ? 6   VAL D CG1 1 
ATOM   6482  C CG2 . VAL D  1 6   ? 1.774   60.680 -39.028 1.00 101.22 ? 6   VAL D CG2 1 
ATOM   6483  N N   . SER D  1 7   ? -0.836  63.057 -35.802 1.00 81.08  ? 7   SER D N   1 
ATOM   6484  C CA  . SER D  1 7   ? -1.046  63.878 -34.584 1.00 73.62  ? 7   SER D CA  1 
ATOM   6485  C C   . SER D  1 7   ? -0.441  63.143 -33.393 1.00 78.22  ? 7   SER D C   1 
ATOM   6486  O O   . SER D  1 7   ? -1.132  62.255 -32.855 1.00 74.05  ? 7   SER D O   1 
ATOM   6487  C CB  . SER D  1 7   ? -2.502  64.167 -34.350 1.00 66.28  ? 7   SER D CB  1 
ATOM   6488  O OG  . SER D  1 7   ? -3.083  64.744 -35.507 1.00 70.67  ? 7   SER D OG  1 
ATOM   6489  N N   . VAL D  1 8   ? 0.789   63.505 -33.009 1.00 70.40  ? 8   VAL D N   1 
ATOM   6490  C CA  . VAL D  1 8   ? 1.555   62.821 -31.926 1.00 60.50  ? 8   VAL D CA  1 
ATOM   6491  C C   . VAL D  1 8   ? 0.672   62.764 -30.683 1.00 61.94  ? 8   VAL D C   1 
ATOM   6492  O O   . VAL D  1 8   ? 0.097   63.773 -30.274 1.00 58.88  ? 8   VAL D O   1 
ATOM   6493  C CB  . VAL D  1 8   ? 2.903   63.511 -31.642 1.00 59.78  ? 8   VAL D CB  1 
ATOM   6494  C CG1 . VAL D  1 8   ? 3.808   63.504 -32.865 1.00 56.50  ? 8   VAL D CG1 1 
ATOM   6495  C CG2 . VAL D  1 8   ? 2.728   64.926 -31.110 1.00 64.82  ? 8   VAL D CG2 1 
ATOM   6496  N N   . PRO D  1 9   ? 0.523   61.573 -30.061 1.00 59.06  ? 9   PRO D N   1 
ATOM   6497  C CA  . PRO D  1 9   ? -0.341  61.412 -28.893 1.00 58.79  ? 9   PRO D CA  1 
ATOM   6498  C C   . PRO D  1 9   ? 0.236   62.108 -27.651 1.00 58.53  ? 9   PRO D C   1 
ATOM   6499  O O   . PRO D  1 9   ? -0.513  62.372 -26.731 1.00 55.10  ? 9   PRO D O   1 
ATOM   6500  C CB  . PRO D  1 9   ? -0.409  59.893 -28.674 1.00 60.35  ? 9   PRO D CB  1 
ATOM   6501  C CG  . PRO D  1 9   ? 0.181   59.282 -29.938 1.00 63.45  ? 9   PRO D CG  1 
ATOM   6502  C CD  . PRO D  1 9   ? 1.155   60.311 -30.470 1.00 60.53  ? 9   PRO D CD  1 
ATOM   6503  N N   . TRP D  1 10  ? 1.544   62.387 -27.662 1.00 62.33  ? 10  TRP D N   1 
ATOM   6504  C CA  . TRP D  1 10  ? 2.278   63.011 -26.530 1.00 67.72  ? 10  TRP D CA  1 
ATOM   6505  C C   . TRP D  1 10  ? 2.204   64.538 -26.633 1.00 74.38  ? 10  TRP D C   1 
ATOM   6506  O O   . TRP D  1 10  ? 2.957   65.216 -25.907 1.00 87.69  ? 10  TRP D O   1 
ATOM   6507  C CB  . TRP D  1 10  ? 3.731   62.525 -26.482 1.00 66.41  ? 10  TRP D CB  1 
ATOM   6508  C CG  . TRP D  1 10  ? 4.478   62.664 -27.772 1.00 58.84  ? 10  TRP D CG  1 
ATOM   6509  C CD1 . TRP D  1 10  ? 5.117   63.773 -28.248 1.00 56.37  ? 10  TRP D CD1 1 
ATOM   6510  C CD2 . TRP D  1 10  ? 4.686   61.633 -28.752 1.00 55.93  ? 10  TRP D CD2 1 
ATOM   6511  N NE1 . TRP D  1 10  ? 5.696   63.507 -29.459 1.00 57.58  ? 10  TRP D NE1 1 
ATOM   6512  C CE2 . TRP D  1 10  ? 5.449   62.201 -29.794 1.00 57.63  ? 10  TRP D CE2 1 
ATOM   6513  C CE3 . TRP D  1 10  ? 4.291   60.297 -28.856 1.00 53.02  ? 10  TRP D CE3 1 
ATOM   6514  C CZ2 . TRP D  1 10  ? 5.824   61.473 -30.922 1.00 54.76  ? 10  TRP D CZ2 1 
ATOM   6515  C CZ3 . TRP D  1 10  ? 4.663   59.577 -29.968 1.00 55.49  ? 10  TRP D CZ3 1 
ATOM   6516  C CH2 . TRP D  1 10  ? 5.418   60.160 -30.985 1.00 57.67  ? 10  TRP D CH2 1 
ATOM   6517  N N   . GLY D  1 11  ? 1.340   65.056 -27.511 1.00 75.81  ? 11  GLY D N   1 
ATOM   6518  C CA  . GLY D  1 11  ? 1.115   66.504 -27.675 1.00 72.75  ? 11  GLY D CA  1 
ATOM   6519  C C   . GLY D  1 11  ? -0.196  66.941 -27.043 1.00 66.16  ? 11  GLY D C   1 
ATOM   6520  O O   . GLY D  1 11  ? -0.412  68.163 -26.921 1.00 69.76  ? 11  GLY D O   1 
ATOM   6521  N N   . ALA D  1 12  ? -1.038  65.980 -26.648 1.00 64.74  ? 12  ALA D N   1 
ATOM   6522  C CA  . ALA D  1 12  ? -2.404  66.221 -26.123 1.00 67.23  ? 12  ALA D CA  1 
ATOM   6523  C C   . ALA D  1 12  ? -2.346  66.422 -24.606 1.00 65.20  ? 12  ALA D C   1 
ATOM   6524  O O   . ALA D  1 12  ? -1.723  65.584 -23.927 1.00 72.82  ? 12  ALA D O   1 
ATOM   6525  C CB  . ALA D  1 12  ? -3.314  65.071 -26.495 1.00 70.85  ? 12  ALA D CB  1 
ATOM   6526  N N   . THR D  1 13  ? -2.965  67.499 -24.106 1.00 68.48  ? 13  THR D N   1 
ATOM   6527  C CA  . THR D  1 13  ? -3.147  67.781 -22.656 1.00 69.74  ? 13  THR D CA  1 
ATOM   6528  C C   . THR D  1 13  ? -4.208  66.826 -22.099 1.00 68.70  ? 13  THR D C   1 
ATOM   6529  O O   . THR D  1 13  ? -5.209  66.574 -22.808 1.00 68.79  ? 13  THR D O   1 
ATOM   6530  C CB  . THR D  1 13  ? -3.551  69.239 -22.396 1.00 69.20  ? 13  THR D CB  1 
ATOM   6531  O OG1 . THR D  1 13  ? -2.516  70.080 -22.908 1.00 67.00  ? 13  THR D OG1 1 
ATOM   6532  C CG2 . THR D  1 13  ? -3.771  69.529 -20.928 1.00 74.69  ? 13  THR D CG2 1 
ATOM   6533  N N   . LEU D  1 14  ? -3.990  66.315 -20.882 1.00 68.20  ? 14  LEU D N   1 
ATOM   6534  C CA  . LEU D  1 14  ? -4.848  65.282 -20.246 1.00 65.14  ? 14  LEU D CA  1 
ATOM   6535  C C   . LEU D  1 14  ? -5.617  65.916 -19.085 1.00 55.12  ? 14  LEU D C   1 
ATOM   6536  O O   . LEU D  1 14  ? -5.040  66.779 -18.388 1.00 49.14  ? 14  LEU D O   1 
ATOM   6537  C CB  . LEU D  1 14  ? -3.970  64.116 -19.776 1.00 69.10  ? 14  LEU D CB  1 
ATOM   6538  C CG  . LEU D  1 14  ? -3.135  63.443 -20.868 1.00 75.99  ? 14  LEU D CG  1 
ATOM   6539  C CD1 . LEU D  1 14  ? -2.203  62.399 -20.278 1.00 75.07  ? 14  LEU D CD1 1 
ATOM   6540  C CD2 . LEU D  1 14  ? -4.022  62.818 -21.937 1.00 80.76  ? 14  LEU D CD2 1 
ATOM   6541  N N   . SER D  1 15  ? -6.880  65.516 -18.910 1.00 55.31  ? 15  SER D N   1 
ATOM   6542  C CA  . SER D  1 15  ? -7.721  65.876 -17.741 1.00 59.67  ? 15  SER D CA  1 
ATOM   6543  C C   . SER D  1 15  ? -7.160  65.153 -16.516 1.00 71.57  ? 15  SER D C   1 
ATOM   6544  O O   . SER D  1 15  ? -6.285  64.294 -16.709 1.00 84.09  ? 15  SER D O   1 
ATOM   6545  C CB  . SER D  1 15  ? -9.177  65.559 -17.972 1.00 51.18  ? 15  SER D CB  1 
ATOM   6546  O OG  . SER D  1 15  ? -9.405  64.165 -17.974 1.00 48.03  ? 15  SER D OG  1 
ATOM   6547  N N   . ASN D  1 16  ? -7.623  65.501 -15.314 1.00 73.68  ? 16  ASN D N   1 
ATOM   6548  C CA  . ASN D  1 16  ? -7.222  64.814 -14.057 1.00 73.46  ? 16  ASN D CA  1 
ATOM   6549  C C   . ASN D  1 16  ? -7.742  63.374 -14.110 1.00 74.56  ? 16  ASN D C   1 
ATOM   6550  O O   . ASN D  1 16  ? -6.964  62.453 -13.799 1.00 73.93  ? 16  ASN D O   1 
ATOM   6551  C CB  . ASN D  1 16  ? -7.719  65.553 -12.814 1.00 69.20  ? 16  ASN D CB  1 
ATOM   6552  C CG  . ASN D  1 16  ? -7.046  66.895 -12.626 1.00 71.90  ? 16  ASN D CG  1 
ATOM   6553  O OD1 . ASN D  1 16  ? -6.081  67.213 -13.317 1.00 77.37  ? 16  ASN D OD1 1 
ATOM   6554  N ND2 . ASN D  1 16  ? -7.552  67.688 -11.698 1.00 78.46  ? 16  ASN D ND2 1 
ATOM   6555  N N   . ALA D  1 17  ? -9.007  63.200 -14.508 1.00 72.82  ? 17  ALA D N   1 
ATOM   6556  C CA  . ALA D  1 17  ? -9.674  61.889 -14.682 1.00 76.85  ? 17  ALA D CA  1 
ATOM   6557  C C   . ALA D  1 17  ? -8.804  60.986 -15.565 1.00 78.26  ? 17  ALA D C   1 
ATOM   6558  O O   . ALA D  1 17  ? -8.571  59.828 -15.181 1.00 72.98  ? 17  ALA D O   1 
ATOM   6559  C CB  . ALA D  1 17  ? -11.048 62.086 -15.275 1.00 72.20  ? 17  ALA D CB  1 
ATOM   6560  N N   . GLU D  1 18  ? -8.340  61.508 -16.703 1.00 74.17  ? 18  GLU D N   1 
ATOM   6561  C CA  . GLU D  1 18  ? -7.517  60.768 -17.697 1.00 72.92  ? 18  GLU D CA  1 
ATOM   6562  C C   . GLU D  1 18  ? -6.161  60.420 -17.075 1.00 72.97  ? 18  GLU D C   1 
ATOM   6563  O O   . GLU D  1 18  ? -5.785  59.236 -17.108 1.00 77.76  ? 18  GLU D O   1 
ATOM   6564  C CB  . GLU D  1 18  ? -7.351  61.599 -18.970 1.00 78.13  ? 18  GLU D CB  1 
ATOM   6565  C CG  . GLU D  1 18  ? -8.623  61.700 -19.794 1.00 78.35  ? 18  GLU D CG  1 
ATOM   6566  C CD  . GLU D  1 18  ? -8.613  62.788 -20.853 1.00 79.04  ? 18  GLU D CD  1 
ATOM   6567  O OE1 . GLU D  1 18  ? -9.334  62.638 -21.857 1.00 80.37  ? 18  GLU D OE1 1 
ATOM   6568  O OE2 . GLU D  1 18  ? -7.884  63.784 -20.671 1.00 85.80  ? 18  GLU D OE2 1 
ATOM   6569  N N   . HIS D  1 19  ? -5.463  61.416 -16.524 1.00 66.16  ? 19  HIS D N   1 
ATOM   6570  C CA  . HIS D  1 19  ? -4.124  61.273 -15.890 1.00 59.28  ? 19  HIS D CA  1 
ATOM   6571  C C   . HIS D  1 19  ? -4.189  60.213 -14.784 1.00 59.44  ? 19  HIS D C   1 
ATOM   6572  O O   . HIS D  1 19  ? -3.205  59.468 -14.615 1.00 56.56  ? 19  HIS D O   1 
ATOM   6573  C CB  . HIS D  1 19  ? -3.644  62.633 -15.365 1.00 53.35  ? 19  HIS D CB  1 
ATOM   6574  C CG  . HIS D  1 19  ? -2.220  62.636 -14.925 1.00 50.08  ? 19  HIS D CG  1 
ATOM   6575  N ND1 . HIS D  1 19  ? -1.855  62.422 -13.612 1.00 54.29  ? 19  HIS D ND1 1 
ATOM   6576  C CD2 . HIS D  1 19  ? -1.075  62.822 -15.615 1.00 48.79  ? 19  HIS D CD2 1 
ATOM   6577  C CE1 . HIS D  1 19  ? -0.542  62.478 -13.511 1.00 56.59  ? 19  HIS D CE1 1 
ATOM   6578  N NE2 . HIS D  1 19  ? -0.039  62.723 -14.728 1.00 48.40  ? 19  HIS D NE2 1 
ATOM   6579  N N   . GLN D  1 20  ? -5.315  60.152 -14.066 1.00 56.93  ? 20  GLN D N   1 
ATOM   6580  C CA  . GLN D  1 20  ? -5.552  59.208 -12.942 1.00 57.11  ? 20  GLN D CA  1 
ATOM   6581  C C   . GLN D  1 20  ? -5.778  57.800 -13.508 1.00 58.20  ? 20  GLN D C   1 
ATOM   6582  O O   . GLN D  1 20  ? -5.236  56.842 -12.929 1.00 57.79  ? 20  GLN D O   1 
ATOM   6583  C CB  . GLN D  1 20  ? -6.748  59.672 -12.107 1.00 54.96  ? 20  GLN D CB  1 
ATOM   6584  C CG  . GLN D  1 20  ? -6.684  59.241 -10.649 1.00 59.10  ? 20  GLN D CG  1 
ATOM   6585  C CD  . GLN D  1 20  ? -5.760  60.109 -9.831  1.00 62.16  ? 20  GLN D CD  1 
ATOM   6586  O OE1 . GLN D  1 20  ? -5.442  61.236 -10.202 1.00 63.26  ? 20  GLN D OE1 1 
ATOM   6587  N NE2 . GLN D  1 20  ? -5.322  59.589 -8.696  1.00 66.58  ? 20  GLN D NE2 1 
ATOM   6588  N N   . LEU D  1 21  ? -6.548  57.692 -14.596 1.00 58.33  ? 21  LEU D N   1 
ATOM   6589  C CA  . LEU D  1 21  ? -6.892  56.414 -15.281 1.00 55.03  ? 21  LEU D CA  1 
ATOM   6590  C C   . LEU D  1 21  ? -5.615  55.761 -15.812 1.00 54.09  ? 21  LEU D C   1 
ATOM   6591  O O   . LEU D  1 21  ? -5.412  54.560 -15.555 1.00 55.07  ? 21  LEU D O   1 
ATOM   6592  C CB  . LEU D  1 21  ? -7.860  56.697 -16.434 1.00 54.40  ? 21  LEU D CB  1 
ATOM   6593  C CG  . LEU D  1 21  ? -9.342  56.717 -16.070 1.00 51.92  ? 21  LEU D CG  1 
ATOM   6594  C CD1 . LEU D  1 21  ? -10.184 57.113 -17.273 1.00 49.38  ? 21  LEU D CD1 1 
ATOM   6595  C CD2 . LEU D  1 21  ? -9.779  55.364 -15.533 1.00 51.61  ? 21  LEU D CD2 1 
ATOM   6596  N N   . ILE D  1 22  ? -4.804  56.528 -16.544 1.00 54.60  ? 22  ILE D N   1 
ATOM   6597  C CA  . ILE D  1 22  ? -3.549  56.043 -17.189 1.00 60.61  ? 22  ILE D CA  1 
ATOM   6598  C C   . ILE D  1 22  ? -2.652  55.435 -16.106 1.00 59.50  ? 22  ILE D C   1 
ATOM   6599  O O   . ILE D  1 22  ? -2.280  54.251 -16.242 1.00 69.50  ? 22  ILE D O   1 
ATOM   6600  C CB  . ILE D  1 22  ? -2.849  57.184 -17.954 1.00 58.12  ? 22  ILE D CB  1 
ATOM   6601  C CG1 . ILE D  1 22  ? -3.717  57.704 -19.102 1.00 57.72  ? 22  ILE D CG1 1 
ATOM   6602  C CG2 . ILE D  1 22  ? -1.478  56.741 -18.439 1.00 59.19  ? 22  ILE D CG2 1 
ATOM   6603  C CD1 . ILE D  1 22  ? -3.268  59.032 -19.657 1.00 60.65  ? 22  ILE D CD1 1 
ATOM   6604  N N   . PHE D  1 23  ? -2.338  56.215 -15.067 1.00 52.34  ? 23  PHE D N   1 
ATOM   6605  C CA  . PHE D  1 23  ? -1.481  55.807 -13.925 1.00 50.57  ? 23  PHE D CA  1 
ATOM   6606  C C   . PHE D  1 23  ? -2.017  54.503 -13.322 1.00 49.60  ? 23  PHE D C   1 
ATOM   6607  O O   . PHE D  1 23  ? -1.229  53.556 -13.136 1.00 54.28  ? 23  PHE D O   1 
ATOM   6608  C CB  . PHE D  1 23  ? -1.423  56.916 -12.873 1.00 50.95  ? 23  PHE D CB  1 
ATOM   6609  C CG  . PHE D  1 23  ? -0.511  56.621 -11.709 1.00 49.51  ? 23  PHE D CG  1 
ATOM   6610  C CD1 . PHE D  1 23  ? -1.026  56.293 -10.465 1.00 51.69  ? 23  PHE D CD1 1 
ATOM   6611  C CD2 . PHE D  1 23  ? 0.865   56.667 -11.861 1.00 49.22  ? 23  PHE D CD2 1 
ATOM   6612  C CE1 . PHE D  1 23  ? -0.184  56.022 -9.398  1.00 51.44  ? 23  PHE D CE1 1 
ATOM   6613  C CE2 . PHE D  1 23  ? 1.706   56.400 -10.793 1.00 49.03  ? 23  PHE D CE2 1 
ATOM   6614  C CZ  . PHE D  1 23  ? 1.180   56.073 -9.565  1.00 50.92  ? 23  PHE D CZ  1 
ATOM   6615  N N   . TYR D  1 24  ? -3.320  54.465 -13.028 1.00 48.99  ? 24  TYR D N   1 
ATOM   6616  C CA  . TYR D  1 24  ? -4.032  53.302 -12.436 1.00 51.77  ? 24  TYR D CA  1 
ATOM   6617  C C   . TYR D  1 24  ? -3.675  52.032 -13.217 1.00 53.22  ? 24  TYR D C   1 
ATOM   6618  O O   . TYR D  1 24  ? -3.149  51.074 -12.611 1.00 54.10  ? 24  TYR D O   1 
ATOM   6619  C CB  . TYR D  1 24  ? -5.544  53.547 -12.433 1.00 49.34  ? 24  TYR D CB  1 
ATOM   6620  C CG  . TYR D  1 24  ? -6.378  52.390 -11.940 1.00 47.44  ? 24  TYR D CG  1 
ATOM   6621  C CD1 . TYR D  1 24  ? -6.919  51.470 -12.822 1.00 48.78  ? 24  TYR D CD1 1 
ATOM   6622  C CD2 . TYR D  1 24  ? -6.641  52.221 -10.591 1.00 50.15  ? 24  TYR D CD2 1 
ATOM   6623  C CE1 . TYR D  1 24  ? -7.690  50.408 -12.380 1.00 50.98  ? 24  TYR D CE1 1 
ATOM   6624  C CE2 . TYR D  1 24  ? -7.411  51.165 -10.130 1.00 49.77  ? 24  TYR D CE2 1 
ATOM   6625  C CZ  . TYR D  1 24  ? -7.939  50.255 -11.027 1.00 49.92  ? 24  TYR D CZ  1 
ATOM   6626  O OH  . TYR D  1 24  ? -8.698  49.212 -10.582 1.00 44.07  ? 24  TYR D OH  1 
ATOM   6627  N N   . PHE D  1 25  ? -3.947  52.033 -14.525 1.00 51.94  ? 25  PHE D N   1 
ATOM   6628  C CA  . PHE D  1 25  ? -3.773  50.864 -15.426 1.00 53.98  ? 25  PHE D CA  1 
ATOM   6629  C C   . PHE D  1 25  ? -2.285  50.522 -15.538 1.00 53.03  ? 25  PHE D C   1 
ATOM   6630  O O   . PHE D  1 25  ? -1.946  49.321 -15.517 1.00 56.71  ? 25  PHE D O   1 
ATOM   6631  C CB  . PHE D  1 25  ? -4.430  51.128 -16.783 1.00 53.81  ? 25  PHE D CB  1 
ATOM   6632  C CG  . PHE D  1 25  ? -5.922  50.906 -16.779 1.00 57.10  ? 25  PHE D CG  1 
ATOM   6633  C CD1 . PHE D  1 25  ? -6.448  49.627 -16.875 1.00 58.46  ? 25  PHE D CD1 1 
ATOM   6634  C CD2 . PHE D  1 25  ? -6.801  51.968 -16.639 1.00 59.04  ? 25  PHE D CD2 1 
ATOM   6635  C CE1 . PHE D  1 25  ? -7.818  49.419 -16.852 1.00 60.31  ? 25  PHE D CE1 1 
ATOM   6636  C CE2 . PHE D  1 25  ? -8.171  51.758 -16.617 1.00 57.92  ? 25  PHE D CE2 1 
ATOM   6637  C CZ  . PHE D  1 25  ? -8.677  50.485 -16.724 1.00 58.83  ? 25  PHE D CZ  1 
ATOM   6638  N N   . LEU D  1 26  ? -1.428  51.542 -15.643 1.00 48.67  ? 26  LEU D N   1 
ATOM   6639  C CA  . LEU D  1 26  ? 0.049   51.378 -15.723 1.00 48.79  ? 26  LEU D CA  1 
ATOM   6640  C C   . LEU D  1 26  ? 0.535   50.559 -14.521 1.00 48.28  ? 26  LEU D C   1 
ATOM   6641  O O   . LEU D  1 26  ? 1.181   49.515 -14.738 1.00 47.22  ? 26  LEU D O   1 
ATOM   6642  C CB  . LEU D  1 26  ? 0.716   52.757 -15.758 1.00 48.12  ? 26  LEU D CB  1 
ATOM   6643  C CG  . LEU D  1 26  ? 0.829   53.402 -17.139 1.00 48.19  ? 26  LEU D CG  1 
ATOM   6644  C CD1 . LEU D  1 26  ? 1.692   54.655 -17.087 1.00 49.38  ? 26  LEU D CD1 1 
ATOM   6645  C CD2 . LEU D  1 26  ? 1.388   52.416 -18.152 1.00 46.24  ? 26  LEU D CD2 1 
ATOM   6646  N N   . VAL D  1 27  ? 0.223   51.013 -13.304 1.00 45.27  ? 27  VAL D N   1 
ATOM   6647  C CA  . VAL D  1 27  ? 0.717   50.411 -12.029 1.00 43.84  ? 27  VAL D CA  1 
ATOM   6648  C C   . VAL D  1 27  ? 0.050   49.045 -11.825 1.00 47.07  ? 27  VAL D C   1 
ATOM   6649  O O   . VAL D  1 27  ? 0.766   48.093 -11.451 1.00 50.74  ? 27  VAL D O   1 
ATOM   6650  C CB  . VAL D  1 27  ? 0.475   51.349 -10.830 1.00 42.88  ? 27  VAL D CB  1 
ATOM   6651  C CG1 . VAL D  1 27  ? 0.949   50.725 -9.527  1.00 42.99  ? 27  VAL D CG1 1 
ATOM   6652  C CG2 . VAL D  1 27  ? 1.124   52.710 -11.039 1.00 43.93  ? 27  VAL D CG2 1 
ATOM   6653  N N   . VAL D  1 28  ? -1.263  48.949 -12.057 1.00 49.12  ? 28  VAL D N   1 
ATOM   6654  C CA  . VAL D  1 28  ? -2.030  47.669 -11.960 1.00 48.10  ? 28  VAL D CA  1 
ATOM   6655  C C   . VAL D  1 28  ? -1.334  46.628 -12.844 1.00 46.33  ? 28  VAL D C   1 
ATOM   6656  O O   . VAL D  1 28  ? -1.169  45.478 -12.391 1.00 45.77  ? 28  VAL D O   1 
ATOM   6657  C CB  . VAL D  1 28  ? -3.506  47.847 -12.360 1.00 48.18  ? 28  VAL D CB  1 
ATOM   6658  C CG1 . VAL D  1 28  ? -4.206  46.506 -12.520 1.00 45.65  ? 28  VAL D CG1 1 
ATOM   6659  C CG2 . VAL D  1 28  ? -4.255  48.724 -11.369 1.00 52.07  ? 28  VAL D CG2 1 
ATOM   6660  N N   . ALA D  1 29  ? -0.936  47.029 -14.054 1.00 46.28  ? 29  ALA D N   1 
ATOM   6661  C CA  . ALA D  1 29  ? -0.178  46.196 -15.017 1.00 47.30  ? 29  ALA D CA  1 
ATOM   6662  C C   . ALA D  1 29  ? 1.107   45.692 -14.351 1.00 49.01  ? 29  ALA D C   1 
ATOM   6663  O O   . ALA D  1 29  ? 1.273   44.461 -14.231 1.00 55.12  ? 29  ALA D O   1 
ATOM   6664  C CB  . ALA D  1 29  ? 0.128   46.993 -16.261 1.00 45.75  ? 29  ALA D CB  1 
ATOM   6665  N N   . ALA D  1 30  ? 1.972   46.622 -13.935 1.00 47.19  ? 30  ALA D N   1 
ATOM   6666  C CA  . ALA D  1 30  ? 3.277   46.353 -13.288 1.00 44.83  ? 30  ALA D CA  1 
ATOM   6667  C C   . ALA D  1 30  ? 3.100   45.302 -12.185 1.00 46.00  ? 30  ALA D C   1 
ATOM   6668  O O   . ALA D  1 30  ? 3.898   44.343 -12.148 1.00 50.84  ? 30  ALA D O   1 
ATOM   6669  C CB  . ALA D  1 30  ? 3.852   47.638 -12.744 1.00 43.70  ? 30  ALA D CB  1 
ATOM   6670  N N   . LEU D  1 31  ? 2.087   45.477 -11.329 1.00 42.17  ? 31  LEU D N   1 
ATOM   6671  C CA  . LEU D  1 31  ? 1.809   44.601 -10.158 1.00 43.12  ? 31  LEU D CA  1 
ATOM   6672  C C   . LEU D  1 31  ? 1.330   43.227 -10.641 1.00 40.59  ? 31  LEU D C   1 
ATOM   6673  O O   . LEU D  1 31  ? 1.759   42.210 -10.059 1.00 34.94  ? 31  LEU D O   1 
ATOM   6674  C CB  . LEU D  1 31  ? 0.762   45.276 -9.269  1.00 48.42  ? 31  LEU D CB  1 
ATOM   6675  C CG  . LEU D  1 31  ? 1.233   46.554 -8.575  1.00 57.85  ? 31  LEU D CG  1 
ATOM   6676  C CD1 . LEU D  1 31  ? 0.069   47.279 -7.918  1.00 63.02  ? 31  LEU D CD1 1 
ATOM   6677  C CD2 . LEU D  1 31  ? 2.321   46.249 -7.556  1.00 59.47  ? 31  LEU D CD2 1 
ATOM   6678  N N   . ALA D  1 32  ? 0.469   43.203 -11.662 1.00 42.15  ? 32  ALA D N   1 
ATOM   6679  C CA  . ALA D  1 32  ? -0.015  41.972 -12.326 1.00 42.43  ? 32  ALA D CA  1 
ATOM   6680  C C   . ALA D  1 32  ? 1.193   41.131 -12.755 1.00 46.83  ? 32  ALA D C   1 
ATOM   6681  O O   . ALA D  1 32  ? 1.154   39.896 -12.579 1.00 44.70  ? 32  ALA D O   1 
ATOM   6682  C CB  . ALA D  1 32  ? -0.887  42.329 -13.504 1.00 40.31  ? 32  ALA D CB  1 
ATOM   6683  N N   . PHE D  1 33  ? 2.227   41.793 -13.284 1.00 50.63  ? 33  PHE D N   1 
ATOM   6684  C CA  . PHE D  1 33  ? 3.463   41.162 -13.816 1.00 52.74  ? 33  PHE D CA  1 
ATOM   6685  C C   . PHE D  1 33  ? 4.310   40.633 -12.653 1.00 50.88  ? 33  PHE D C   1 
ATOM   6686  O O   . PHE D  1 33  ? 4.891   39.540 -12.787 1.00 58.63  ? 33  PHE D O   1 
ATOM   6687  C CB  . PHE D  1 33  ? 4.237   42.148 -14.696 1.00 55.04  ? 33  PHE D CB  1 
ATOM   6688  C CG  . PHE D  1 33  ? 3.596   42.426 -16.033 1.00 60.85  ? 33  PHE D CG  1 
ATOM   6689  C CD1 . PHE D  1 33  ? 3.076   41.395 -16.800 1.00 62.27  ? 33  PHE D CD1 1 
ATOM   6690  C CD2 . PHE D  1 33  ? 3.517   43.719 -16.527 1.00 66.08  ? 33  PHE D CD2 1 
ATOM   6691  C CE1 . PHE D  1 33  ? 2.481   41.653 -18.025 1.00 60.64  ? 33  PHE D CE1 1 
ATOM   6692  C CE2 . PHE D  1 33  ? 2.930   43.973 -17.757 1.00 61.24  ? 33  PHE D CE2 1 
ATOM   6693  C CZ  . PHE D  1 33  ? 2.413   42.941 -18.503 1.00 59.20  ? 33  PHE D CZ  1 
ATOM   6694  N N   . VAL D  1 34  ? 4.373   41.381 -11.547 1.00 49.79  ? 34  VAL D N   1 
ATOM   6695  C CA  . VAL D  1 34  ? 5.037   40.947 -10.281 1.00 48.32  ? 34  VAL D CA  1 
ATOM   6696  C C   . VAL D  1 34  ? 4.408   39.619 -9.843  1.00 46.65  ? 34  VAL D C   1 
ATOM   6697  O O   . VAL D  1 34  ? 5.158   38.640 -9.652  1.00 45.63  ? 34  VAL D O   1 
ATOM   6698  C CB  . VAL D  1 34  ? 4.915   42.015 -9.176  1.00 46.73  ? 34  VAL D CB  1 
ATOM   6699  C CG1 . VAL D  1 34  ? 5.147   41.429 -7.793  1.00 46.92  ? 34  VAL D CG1 1 
ATOM   6700  C CG2 . VAL D  1 34  ? 5.846   43.191 -9.421  1.00 48.26  ? 34  VAL D CG2 1 
ATOM   6701  N N   . ALA D  1 35  ? 3.079   39.597 -9.700  1.00 42.20  ? 35  ALA D N   1 
ATOM   6702  C CA  . ALA D  1 35  ? 2.282   38.414 -9.302  1.00 42.16  ? 35  ALA D CA  1 
ATOM   6703  C C   . ALA D  1 35  ? 2.561   37.260 -10.271 1.00 43.27  ? 35  ALA D C   1 
ATOM   6704  O O   . ALA D  1 35  ? 2.760   36.122 -9.801  1.00 40.79  ? 35  ALA D O   1 
ATOM   6705  C CB  . ALA D  1 35  ? 0.816   38.769 -9.276  1.00 43.25  ? 35  ALA D CB  1 
ATOM   6706  N N   . GLY D  1 36  ? 2.564   37.555 -11.575 1.00 46.30  ? 36  GLY D N   1 
ATOM   6707  C CA  . GLY D  1 36  ? 2.847   36.584 -12.649 1.00 45.52  ? 36  GLY D CA  1 
ATOM   6708  C C   . GLY D  1 36  ? 4.245   36.008 -12.518 1.00 44.24  ? 36  GLY D C   1 
ATOM   6709  O O   . GLY D  1 36  ? 4.378   34.768 -12.520 1.00 41.43  ? 36  GLY D O   1 
ATOM   6710  N N   . PHE D  1 37  ? 5.251   36.879 -12.400 1.00 44.78  ? 37  PHE D N   1 
ATOM   6711  C CA  . PHE D  1 37  ? 6.683   36.509 -12.253 1.00 42.10  ? 37  PHE D CA  1 
ATOM   6712  C C   . PHE D  1 37  ? 6.835   35.535 -11.082 1.00 37.70  ? 37  PHE D C   1 
ATOM   6713  O O   . PHE D  1 37  ? 7.458   34.472 -11.252 1.00 38.46  ? 37  PHE D O   1 
ATOM   6714  C CB  . PHE D  1 37  ? 7.545   37.754 -12.039 1.00 41.93  ? 37  PHE D CB  1 
ATOM   6715  C CG  . PHE D  1 37  ? 9.021   37.468 -11.950 1.00 45.00  ? 37  PHE D CG  1 
ATOM   6716  C CD1 . PHE D  1 37  ? 9.828   37.554 -13.072 1.00 46.61  ? 37  PHE D CD1 1 
ATOM   6717  C CD2 . PHE D  1 37  ? 9.601   37.099 -10.746 1.00 49.02  ? 37  PHE D CD2 1 
ATOM   6718  C CE1 . PHE D  1 37  ? 11.186  37.290 -12.990 1.00 49.56  ? 37  PHE D CE1 1 
ATOM   6719  C CE2 . PHE D  1 37  ? 10.960  36.835 -10.665 1.00 48.48  ? 37  PHE D CE2 1 
ATOM   6720  C CZ  . PHE D  1 37  ? 11.749  36.930 -11.787 1.00 48.52  ? 37  PHE D CZ  1 
ATOM   6721  N N   . ILE D  1 38  ? 6.271   35.895 -9.927  1.00 35.57  ? 38  ILE D N   1 
ATOM   6722  C CA  . ILE D  1 38  ? 6.315   35.077 -8.679  1.00 38.32  ? 38  ILE D CA  1 
ATOM   6723  C C   . ILE D  1 38  ? 5.690   33.706 -8.963  1.00 40.04  ? 38  ILE D C   1 
ATOM   6724  O O   . ILE D  1 38  ? 6.376   32.691 -8.734  1.00 37.35  ? 38  ILE D O   1 
ATOM   6725  C CB  . ILE D  1 38  ? 5.617   35.807 -7.516  1.00 37.97  ? 38  ILE D CB  1 
ATOM   6726  C CG1 . ILE D  1 38  ? 6.358   37.093 -7.141  1.00 39.65  ? 38  ILE D CG1 1 
ATOM   6727  C CG2 . ILE D  1 38  ? 5.457   34.879 -6.322  1.00 37.52  ? 38  ILE D CG2 1 
ATOM   6728  C CD1 . ILE D  1 38  ? 5.707   37.881 -6.030  1.00 40.11  ? 38  ILE D CD1 1 
ATOM   6729  N N   . ARG D  1 39  ? 4.444   33.678 -9.447  1.00 44.71  ? 39  ARG D N   1 
ATOM   6730  C CA  . ARG D  1 39  ? 3.725   32.418 -9.780  1.00 45.91  ? 39  ARG D CA  1 
ATOM   6731  C C   . ARG D  1 39  ? 4.625   31.563 -10.677 1.00 43.42  ? 39  ARG D C   1 
ATOM   6732  O O   . ARG D  1 39  ? 4.845   30.387 -10.338 1.00 48.38  ? 39  ARG D O   1 
ATOM   6733  C CB  . ARG D  1 39  ? 2.388   32.689 -10.477 1.00 49.43  ? 39  ARG D CB  1 
ATOM   6734  C CG  . ARG D  1 39  ? 1.641   31.423 -10.875 1.00 44.76  ? 39  ARG D CG  1 
ATOM   6735  N N   . THR D  1 40  ? 5.134   32.147 -11.766 1.00 40.89  ? 40  THR D N   1 
ATOM   6736  C CA  . THR D  1 40  ? 5.969   31.460 -12.787 1.00 41.77  ? 40  THR D CA  1 
ATOM   6737  C C   . THR D  1 40  ? 7.190   30.821 -12.115 1.00 48.10  ? 40  THR D C   1 
ATOM   6738  O O   . THR D  1 40  ? 7.478   29.642 -12.416 1.00 55.32  ? 40  THR D O   1 
ATOM   6739  C CB  . THR D  1 40  ? 6.407   32.427 -13.894 1.00 41.31  ? 40  THR D CB  1 
ATOM   6740  O OG1 . THR D  1 40  ? 5.257   32.797 -14.653 1.00 45.07  ? 40  THR D OG1 1 
ATOM   6741  C CG2 . THR D  1 40  ? 7.447   31.825 -14.813 1.00 43.37  ? 40  THR D CG2 1 
ATOM   6742  N N   . TYR D  1 41  ? 7.878   31.571 -11.248 1.00 49.45  ? 41  TYR D N   1 
ATOM   6743  C CA  . TYR D  1 41  ? 9.106   31.125 -10.540 1.00 50.82  ? 41  TYR D CA  1 
ATOM   6744  C C   . TYR D  1 41  ? 8.778   29.920 -9.651  1.00 50.91  ? 41  TYR D C   1 
ATOM   6745  O O   . TYR D  1 41  ? 9.514   28.917 -9.700  1.00 54.71  ? 41  TYR D O   1 
ATOM   6746  C CB  . TYR D  1 41  ? 9.712   32.258 -9.706  1.00 55.48  ? 41  TYR D CB  1 
ATOM   6747  C CG  . TYR D  1 41  ? 10.984  31.873 -8.991  1.00 62.95  ? 41  TYR D CG  1 
ATOM   6748  C CD1 . TYR D  1 41  ? 10.982  31.557 -7.642  1.00 61.35  ? 41  TYR D CD1 1 
ATOM   6749  C CD2 . TYR D  1 41  ? 12.188  31.794 -9.671  1.00 67.51  ? 41  TYR D CD2 1 
ATOM   6750  C CE1 . TYR D  1 41  ? 12.146  31.193 -6.984  1.00 66.65  ? 41  TYR D CE1 1 
ATOM   6751  C CE2 . TYR D  1 41  ? 13.360  31.427 -9.029  1.00 68.90  ? 41  TYR D CE2 1 
ATOM   6752  C CZ  . TYR D  1 41  ? 13.340  31.126 -7.680  1.00 69.51  ? 41  TYR D CZ  1 
ATOM   6753  O OH  . TYR D  1 41  ? 14.493  30.765 -7.042  1.00 69.85  ? 41  TYR D OH  1 
ATOM   6754  N N   . ILE D  1 42  ? 7.700   30.020 -8.869  1.00 48.13  ? 42  ILE D N   1 
ATOM   6755  C CA  . ILE D  1 42  ? 7.307   29.012 -7.840  1.00 48.70  ? 42  ILE D CA  1 
ATOM   6756  C C   . ILE D  1 42  ? 6.905   27.701 -8.527  1.00 46.23  ? 42  ILE D C   1 
ATOM   6757  O O   . ILE D  1 42  ? 7.174   26.629 -7.951  1.00 43.20  ? 42  ILE D O   1 
ATOM   6758  C CB  . ILE D  1 42  ? 6.182   29.562 -6.939  1.00 47.45  ? 42  ILE D CB  1 
ATOM   6759  C CG1 . ILE D  1 42  ? 6.729   30.577 -5.932  1.00 52.67  ? 42  ILE D CG1 1 
ATOM   6760  C CG2 . ILE D  1 42  ? 5.430   28.432 -6.252  1.00 44.75  ? 42  ILE D CG2 1 
ATOM   6761  C CD1 . ILE D  1 42  ? 6.152   30.441 -4.544  1.00 60.37  ? 42  ILE D CD1 1 
ATOM   6762  N N   . THR D  1 43  ? 6.292   27.787 -9.710  1.00 48.28  ? 43  THR D N   1 
ATOM   6763  C CA  . THR D  1 43  ? 5.731   26.629 -10.456 1.00 51.47  ? 43  THR D CA  1 
ATOM   6764  C C   . THR D  1 43  ? 6.710   26.174 -11.545 1.00 56.58  ? 43  THR D C   1 
ATOM   6765  O O   . THR D  1 43  ? 6.261   25.499 -12.490 1.00 63.04  ? 43  THR D O   1 
ATOM   6766  C CB  . THR D  1 43  ? 4.368   26.981 -11.066 1.00 51.58  ? 43  THR D CB  1 
ATOM   6767  O OG1 . THR D  1 43  ? 4.559   28.043 -12.002 1.00 44.41  ? 43  THR D OG1 1 
ATOM   6768  C CG2 . THR D  1 43  ? 3.350   27.386 -10.023 1.00 53.58  ? 43  THR D CG2 1 
ATOM   6769  N N   . ARG D  1 44  ? 7.996   26.509 -11.410 1.00 53.37  ? 44  ARG D N   1 
ATOM   6770  C CA  . ARG D  1 44  ? 9.017   26.270 -12.465 1.00 55.11  ? 44  ARG D CA  1 
ATOM   6771  C C   . ARG D  1 44  ? 9.315   24.768 -12.568 1.00 57.19  ? 44  ARG D C   1 
ATOM   6772  O O   . ARG D  1 44  ? 9.538   24.291 -13.699 1.00 57.96  ? 44  ARG D O   1 
ATOM   6773  C CB  . ARG D  1 44  ? 10.283  27.089 -12.189 1.00 57.59  ? 44  ARG D CB  1 
ATOM   6774  C CG  . ARG D  1 44  ? 11.099  26.632 -10.988 1.00 59.15  ? 44  ARG D CG  1 
ATOM   6775  C CD  . ARG D  1 44  ? 12.245  27.590 -10.712 1.00 64.43  ? 44  ARG D CD  1 
ATOM   6776  N NE  . ARG D  1 44  ? 13.147  27.125 -9.666  1.00 72.94  ? 44  ARG D NE  1 
ATOM   6777  C CZ  . ARG D  1 44  ? 12.992  27.365 -8.368  1.00 77.52  ? 44  ARG D CZ  1 
ATOM   6778  N NH1 . ARG D  1 44  ? 11.959  28.070 -7.940  1.00 82.83  ? 44  ARG D NH1 1 
ATOM   6779  N NH2 . ARG D  1 44  ? 13.875  26.901 -7.501  1.00 84.48  ? 44  ARG D NH2 1 
ATOM   6780  N N   . ASN D  1 45  ? 9.297   24.050 -11.441 1.00 56.80  ? 45  ASN D N   1 
ATOM   6781  C CA  . ASN D  1 45  ? 9.736   22.632 -11.347 1.00 53.70  ? 45  ASN D CA  1 
ATOM   6782  C C   . ASN D  1 45  ? 8.545   21.691 -11.555 1.00 56.62  ? 45  ASN D C   1 
ATOM   6783  O O   . ASN D  1 45  ? 8.677   20.499 -11.215 1.00 48.39  ? 45  ASN D O   1 
ATOM   6784  C CB  . ASN D  1 45  ? 10.447  22.365 -10.021 1.00 56.30  ? 45  ASN D CB  1 
ATOM   6785  C CG  . ASN D  1 45  ? 11.825  22.989 -9.979  1.00 59.76  ? 45  ASN D CG  1 
ATOM   6786  O OD1 . ASN D  1 45  ? 12.487  23.103 -11.009 1.00 56.74  ? 45  ASN D OD1 1 
ATOM   6787  N ND2 . ASN D  1 45  ? 12.262  23.397 -8.798  1.00 65.34  ? 45  ASN D ND2 1 
ATOM   6788  N N   . GLU D  1 46  ? 7.439   22.210 -12.098 1.00 64.62  ? 46  GLU D N   1 
ATOM   6789  C CA  . GLU D  1 46  ? 6.251   21.416 -12.515 1.00 61.06  ? 46  GLU D CA  1 
ATOM   6790  C C   . GLU D  1 46  ? 6.470   20.914 -13.946 1.00 62.46  ? 46  GLU D C   1 
ATOM   6791  O O   . GLU D  1 46  ? 5.552   20.273 -14.493 1.00 67.40  ? 46  GLU D O   1 
ATOM   6792  C CB  . GLU D  1 46  ? 4.977   22.262 -12.449 1.00 59.50  ? 46  GLU D CB  1 
ATOM   6793  C CG  . GLU D  1 46  ? 4.521   22.589 -11.039 1.00 62.29  ? 46  GLU D CG  1 
ATOM   6794  C CD  . GLU D  1 46  ? 3.227   23.385 -10.965 1.00 69.47  ? 46  GLU D CD  1 
ATOM   6795  O OE1 . GLU D  1 46  ? 2.745   23.625 -9.841  1.00 72.23  ? 46  GLU D OE1 1 
ATOM   6796  O OE2 . GLU D  1 46  ? 2.700   23.763 -12.032 1.00 77.11  ? 46  GLU D OE2 1 
ATOM   6797  N N   . VAL D  1 47  ? 7.643   21.200 -14.521 1.00 57.11  ? 47  VAL D N   1 
ATOM   6798  C CA  . VAL D  1 47  ? 7.956   20.976 -15.965 1.00 51.74  ? 47  VAL D CA  1 
ATOM   6799  C C   . VAL D  1 47  ? 9.289   20.229 -16.081 1.00 51.06  ? 47  VAL D C   1 
ATOM   6800  O O   . VAL D  1 47  ? 10.231  20.585 -15.351 1.00 52.76  ? 47  VAL D O   1 
ATOM   6801  C CB  . VAL D  1 47  ? 7.985   22.313 -16.730 1.00 49.15  ? 47  VAL D CB  1 
ATOM   6802  C CG1 . VAL D  1 47  ? 8.675   22.189 -18.079 1.00 48.60  ? 47  VAL D CG1 1 
ATOM   6803  C CG2 . VAL D  1 47  ? 6.588   22.891 -16.893 1.00 52.33  ? 47  VAL D CG2 1 
ATOM   6804  N N   . GLY D  1 48  ? 9.351   19.233 -16.972 1.00 51.02  ? 48  GLY D N   1 
ATOM   6805  C CA  . GLY D  1 48  ? 10.560  18.432 -17.245 1.00 57.64  ? 48  GLY D CA  1 
ATOM   6806  C C   . GLY D  1 48  ? 11.671  19.281 -17.838 1.00 57.88  ? 48  GLY D C   1 
ATOM   6807  O O   . GLY D  1 48  ? 11.356  20.313 -18.461 1.00 55.30  ? 48  GLY D O   1 
ATOM   6808  N N   . SER D  1 49  ? 12.927  18.864 -17.653 1.00 60.90  ? 49  SER D N   1 
ATOM   6809  C CA  . SER D  1 49  ? 14.138  19.559 -18.161 1.00 63.53  ? 49  SER D CA  1 
ATOM   6810  C C   . SER D  1 49  ? 13.999  19.808 -19.667 1.00 64.87  ? 49  SER D C   1 
ATOM   6811  O O   . SER D  1 49  ? 14.647  20.743 -20.176 1.00 66.42  ? 49  SER D O   1 
ATOM   6812  C CB  . SER D  1 49  ? 15.386  18.773 -17.853 1.00 59.11  ? 49  SER D CB  1 
ATOM   6813  O OG  . SER D  1 49  ? 15.335  17.489 -18.455 1.00 62.64  ? 49  SER D OG  1 
ATOM   6814  N N   . ARG D  1 50  ? 13.183  18.998 -20.346 1.00 63.02  ? 50  ARG D N   1 
ATOM   6815  C CA  . ARG D  1 50  ? 13.026  19.019 -21.824 1.00 67.41  ? 50  ARG D CA  1 
ATOM   6816  C C   . ARG D  1 50  ? 12.319  20.306 -22.260 1.00 62.10  ? 50  ARG D C   1 
ATOM   6817  O O   . ARG D  1 50  ? 12.634  20.804 -23.357 1.00 64.39  ? 50  ARG D O   1 
ATOM   6818  C CB  . ARG D  1 50  ? 12.234  17.800 -22.304 1.00 75.06  ? 50  ARG D CB  1 
ATOM   6819  C CG  . ARG D  1 50  ? 12.039  17.754 -23.813 1.00 78.40  ? 50  ARG D CG  1 
ATOM   6820  C CD  . ARG D  1 50  ? 11.236  16.550 -24.262 1.00 83.87  ? 50  ARG D CD  1 
ATOM   6821  N NE  . ARG D  1 50  ? 11.190  16.444 -25.713 1.00 85.59  ? 50  ARG D NE  1 
ATOM   6822  C CZ  . ARG D  1 50  ? 10.500  15.527 -26.380 1.00 79.24  ? 50  ARG D CZ  1 
ATOM   6823  N NH1 . ARG D  1 50  ? 9.787   14.628 -25.725 1.00 77.39  ? 50  ARG D NH1 1 
ATOM   6824  N NH2 . ARG D  1 50  ? 10.526  15.512 -27.700 1.00 77.93  ? 50  ARG D NH2 1 
ATOM   6825  N N   . TYR D  1 51  ? 11.395  20.812 -21.439 1.00 62.80  ? 51  TYR D N   1 
ATOM   6826  C CA  . TYR D  1 51  ? 10.497  21.949 -21.775 1.00 65.92  ? 51  TYR D CA  1 
ATOM   6827  C C   . TYR D  1 51  ? 10.824  23.157 -20.891 1.00 60.27  ? 51  TYR D C   1 
ATOM   6828  O O   . TYR D  1 51  ? 9.960   24.042 -20.737 1.00 58.59  ? 51  TYR D O   1 
ATOM   6829  C CB  . TYR D  1 51  ? 9.034   21.523 -21.625 1.00 63.91  ? 51  TYR D CB  1 
ATOM   6830  C CG  . TYR D  1 51  ? 8.663   20.298 -22.420 1.00 66.96  ? 51  TYR D CG  1 
ATOM   6831  C CD1 . TYR D  1 51  ? 8.545   20.350 -23.799 1.00 68.79  ? 51  TYR D CD1 1 
ATOM   6832  C CD2 . TYR D  1 51  ? 8.435   19.082 -21.798 1.00 67.70  ? 51  TYR D CD2 1 
ATOM   6833  C CE1 . TYR D  1 51  ? 8.206   19.230 -24.540 1.00 71.02  ? 51  TYR D CE1 1 
ATOM   6834  C CE2 . TYR D  1 51  ? 8.093   17.951 -22.523 1.00 72.36  ? 51  TYR D CE2 1 
ATOM   6835  C CZ  . TYR D  1 51  ? 7.980   18.025 -23.900 1.00 73.81  ? 51  TYR D CZ  1 
ATOM   6836  O OH  . TYR D  1 51  ? 7.649   16.916 -24.625 1.00 73.23  ? 51  TYR D OH  1 
ATOM   6837  N N   . ARG D  1 52  ? 12.040  23.196 -20.340 1.00 52.85  ? 52  ARG D N   1 
ATOM   6838  C CA  . ARG D  1 52  ? 12.492  24.257 -19.403 1.00 51.46  ? 52  ARG D CA  1 
ATOM   6839  C C   . ARG D  1 52  ? 12.636  25.591 -20.145 1.00 49.99  ? 52  ARG D C   1 
ATOM   6840  O O   . ARG D  1 52  ? 12.433  26.641 -19.501 1.00 42.89  ? 52  ARG D O   1 
ATOM   6841  C CB  . ARG D  1 52  ? 13.814  23.864 -18.741 1.00 51.33  ? 52  ARG D CB  1 
ATOM   6842  C CG  . ARG D  1 52  ? 14.291  24.855 -17.690 1.00 54.51  ? 52  ARG D CG  1 
ATOM   6843  C CD  . ARG D  1 52  ? 15.315  24.225 -16.772 1.00 57.69  ? 52  ARG D CD  1 
ATOM   6844  N NE  . ARG D  1 52  ? 14.780  23.044 -16.110 1.00 60.52  ? 52  ARG D NE  1 
ATOM   6845  C CZ  . ARG D  1 52  ? 15.508  22.003 -15.727 1.00 63.65  ? 52  ARG D CZ  1 
ATOM   6846  N NH1 . ARG D  1 52  ? 16.811  21.985 -15.953 1.00 70.36  ? 52  ARG D NH1 1 
ATOM   6847  N NH2 . ARG D  1 52  ? 14.929  20.975 -15.133 1.00 66.80  ? 52  ARG D NH2 1 
ATOM   6848  N N   . THR D  1 53  ? 12.981  25.556 -21.437 1.00 49.75  ? 53  THR D N   1 
ATOM   6849  C CA  . THR D  1 53  ? 13.163  26.769 -22.279 1.00 48.81  ? 53  THR D CA  1 
ATOM   6850  C C   . THR D  1 53  ? 11.858  27.572 -22.272 1.00 51.41  ? 53  THR D C   1 
ATOM   6851  O O   . THR D  1 53  ? 11.930  28.812 -22.367 1.00 55.09  ? 53  THR D O   1 
ATOM   6852  C CB  . THR D  1 53  ? 13.610  26.420 -23.704 1.00 47.26  ? 53  THR D CB  1 
ATOM   6853  O OG1 . THR D  1 53  ? 14.702  25.507 -23.611 1.00 58.40  ? 53  THR D OG1 1 
ATOM   6854  C CG2 . THR D  1 53  ? 14.033  27.634 -24.502 1.00 44.13  ? 53  THR D CG2 1 
ATOM   6855  N N   . ALA D  1 54  ? 10.716  26.886 -22.155 1.00 48.28  ? 54  ALA D N   1 
ATOM   6856  C CA  . ALA D  1 54  ? 9.367   27.492 -22.063 1.00 45.17  ? 54  ALA D CA  1 
ATOM   6857  C C   . ALA D  1 54  ? 9.288   28.356 -20.801 1.00 42.66  ? 54  ALA D C   1 
ATOM   6858  O O   . ALA D  1 54  ? 8.727   29.469 -20.871 1.00 45.11  ? 54  ALA D O   1 
ATOM   6859  C CB  . ALA D  1 54  ? 8.314   26.412 -22.053 1.00 45.69  ? 54  ALA D CB  1 
ATOM   6860  N N   . VAL D  1 55  ? 9.846   27.851 -19.698 1.00 47.72  ? 55  VAL D N   1 
ATOM   6861  C CA  . VAL D  1 55  ? 9.794   28.480 -18.345 1.00 47.60  ? 55  VAL D CA  1 
ATOM   6862  C C   . VAL D  1 55  ? 10.750  29.678 -18.312 1.00 45.92  ? 55  VAL D C   1 
ATOM   6863  O O   . VAL D  1 55  ? 10.297  30.784 -17.946 1.00 48.82  ? 55  VAL D O   1 
ATOM   6864  C CB  . VAL D  1 55  ? 10.133  27.459 -17.242 1.00 49.00  ? 55  VAL D CB  1 
ATOM   6865  C CG1 . VAL D  1 55  ? 10.115  28.099 -15.863 1.00 48.39  ? 55  VAL D CG1 1 
ATOM   6866  C CG2 . VAL D  1 55  ? 9.209   26.250 -17.286 1.00 52.28  ? 55  VAL D CG2 1 
ATOM   6867  N N   . SER D  1 56  ? 12.020  29.464 -18.676 1.00 39.09  ? 56  SER D N   1 
ATOM   6868  C CA  . SER D  1 56  ? 13.085  30.501 -18.665 1.00 41.17  ? 56  SER D CA  1 
ATOM   6869  C C   . SER D  1 56  ? 12.646  31.701 -19.512 1.00 40.67  ? 56  SER D C   1 
ATOM   6870  O O   . SER D  1 56  ? 12.912  32.849 -19.095 1.00 45.78  ? 56  SER D O   1 
ATOM   6871  C CB  . SER D  1 56  ? 14.405  29.946 -19.135 1.00 42.96  ? 56  SER D CB  1 
ATOM   6872  O OG  . SER D  1 56  ? 14.298  29.411 -20.442 1.00 45.86  ? 56  SER D OG  1 
ATOM   6873  N N   . ALA D  1 57  ? 11.997  31.439 -20.650 1.00 38.57  ? 57  ALA D N   1 
ATOM   6874  C CA  . ALA D  1 57  ? 11.471  32.463 -21.581 1.00 38.10  ? 57  ALA D CA  1 
ATOM   6875  C C   . ALA D  1 57  ? 10.351  33.246 -20.892 1.00 40.20  ? 57  ALA D C   1 
ATOM   6876  O O   . ALA D  1 57  ? 10.407  34.492 -20.897 1.00 38.83  ? 57  ALA D O   1 
ATOM   6877  C CB  . ALA D  1 57  ? 10.978  31.811 -22.846 1.00 39.25  ? 57  ALA D CB  1 
ATOM   6878  N N   . ARG D  1 58  ? 9.376   32.536 -20.318 1.00 44.04  ? 58  ARG D N   1 
ATOM   6879  C CA  . ARG D  1 58  ? 8.196   33.149 -19.654 1.00 49.02  ? 58  ARG D CA  1 
ATOM   6880  C C   . ARG D  1 58  ? 8.672   34.041 -18.506 1.00 47.84  ? 58  ARG D C   1 
ATOM   6881  O O   . ARG D  1 58  ? 8.225   35.200 -18.444 1.00 43.93  ? 58  ARG D O   1 
ATOM   6882  C CB  . ARG D  1 58  ? 7.234   32.077 -19.139 1.00 52.30  ? 58  ARG D CB  1 
ATOM   6883  C CG  . ARG D  1 58  ? 5.967   32.637 -18.510 1.00 60.80  ? 58  ARG D CG  1 
ATOM   6884  C CD  . ARG D  1 58  ? 4.864   31.598 -18.495 1.00 67.49  ? 58  ARG D CD  1 
ATOM   6885  N NE  . ARG D  1 58  ? 5.045   30.554 -17.498 1.00 74.53  ? 58  ARG D NE  1 
ATOM   6886  C CZ  . ARG D  1 58  ? 4.334   30.451 -16.379 1.00 75.74  ? 58  ARG D CZ  1 
ATOM   6887  N NH1 . ARG D  1 58  ? 4.568   29.459 -15.537 1.00 78.87  ? 58  ARG D NH1 1 
ATOM   6888  N NH2 . ARG D  1 58  ? 3.391   31.338 -16.108 1.00 60.87  ? 58  ARG D NH2 1 
ATOM   6889  N N   . LEU D  1 59  ? 9.546   33.520 -17.641 1.00 46.95  ? 59  LEU D N   1 
ATOM   6890  C CA  . LEU D  1 59  ? 10.092  34.268 -16.478 1.00 44.95  ? 59  LEU D CA  1 
ATOM   6891  C C   . LEU D  1 59  ? 10.908  35.455 -16.996 1.00 43.57  ? 59  LEU D C   1 
ATOM   6892  O O   . LEU D  1 59  ? 10.735  36.571 -16.461 1.00 45.84  ? 59  LEU D O   1 
ATOM   6893  C CB  . LEU D  1 59  ? 10.947  33.335 -15.617 1.00 47.02  ? 59  LEU D CB  1 
ATOM   6894  C CG  . LEU D  1 59  ? 11.118  33.779 -14.166 1.00 53.67  ? 59  LEU D CG  1 
ATOM   6895  C CD1 . LEU D  1 59  ? 9.764   33.964 -13.496 1.00 55.48  ? 59  LEU D CD1 1 
ATOM   6896  C CD2 . LEU D  1 59  ? 11.968  32.790 -13.385 1.00 55.72  ? 59  LEU D CD2 1 
ATOM   6897  N N   . GLY D  1 60  ? 11.748  35.215 -18.007 1.00 40.11  ? 60  GLY D N   1 
ATOM   6898  C CA  . GLY D  1 60  ? 12.529  36.257 -18.699 1.00 42.68  ? 60  GLY D CA  1 
ATOM   6899  C C   . GLY D  1 60  ? 11.644  37.406 -19.151 1.00 45.96  ? 60  GLY D C   1 
ATOM   6900  O O   . GLY D  1 60  ? 11.978  38.566 -18.844 1.00 44.38  ? 60  GLY D O   1 
ATOM   6901  N N   . MET D  1 61  ? 10.544  37.097 -19.845 1.00 47.96  ? 61  MET D N   1 
ATOM   6902  C CA  . MET D  1 61  ? 9.645   38.106 -20.467 1.00 53.06  ? 61  MET D CA  1 
ATOM   6903  C C   . MET D  1 61  ? 8.889   38.872 -19.375 1.00 48.31  ? 61  MET D C   1 
ATOM   6904  O O   . MET D  1 61  ? 8.736   40.101 -19.519 1.00 52.59  ? 61  MET D O   1 
ATOM   6905  C CB  . MET D  1 61  ? 8.640   37.453 -21.420 1.00 59.53  ? 61  MET D CB  1 
ATOM   6906  C CG  . MET D  1 61  ? 7.525   36.709 -20.720 1.00 70.46  ? 61  MET D CG  1 
ATOM   6907  S SD  . MET D  1 61  ? 5.902   37.178 -21.355 1.00 72.67  ? 61  MET D SD  1 
ATOM   6908  C CE  . MET D  1 61  ? 5.879   38.911 -20.903 1.00 70.01  ? 61  MET D CE  1 
ATOM   6909  N N   . LEU D  1 62  ? 8.430   38.177 -18.330 1.00 43.32  ? 62  LEU D N   1 
ATOM   6910  C CA  . LEU D  1 62  ? 7.670   38.785 -17.205 1.00 44.47  ? 62  LEU D CA  1 
ATOM   6911  C C   . LEU D  1 62  ? 8.598   39.739 -16.444 1.00 44.39  ? 62  LEU D C   1 
ATOM   6912  O O   . LEU D  1 62  ? 8.148   40.845 -16.089 1.00 43.03  ? 62  LEU D O   1 
ATOM   6913  C CB  . LEU D  1 62  ? 7.125   37.680 -16.294 1.00 46.37  ? 62  LEU D CB  1 
ATOM   6914  C CG  . LEU D  1 62  ? 5.999   36.832 -16.887 1.00 50.95  ? 62  LEU D CG  1 
ATOM   6915  C CD1 . LEU D  1 62  ? 5.616   35.701 -15.945 1.00 51.87  ? 62  LEU D CD1 1 
ATOM   6916  C CD2 . LEU D  1 62  ? 4.783   37.686 -17.218 1.00 50.31  ? 62  LEU D CD2 1 
ATOM   6917  N N   . GLY D  1 63  ? 9.847   39.322 -16.219 1.00 44.36  ? 63  GLY D N   1 
ATOM   6918  C CA  . GLY D  1 63  ? 10.895  40.158 -15.604 1.00 41.53  ? 63  GLY D CA  1 
ATOM   6919  C C   . GLY D  1 63  ? 11.112  41.434 -16.398 1.00 40.82  ? 63  GLY D C   1 
ATOM   6920  O O   . GLY D  1 63  ? 11.117  42.517 -15.790 1.00 40.05  ? 63  GLY D O   1 
ATOM   6921  N N   . VAL D  1 64  ? 11.275  41.308 -17.717 1.00 41.09  ? 64  VAL D N   1 
ATOM   6922  C CA  . VAL D  1 64  ? 11.475  42.448 -18.660 1.00 45.61  ? 64  VAL D CA  1 
ATOM   6923  C C   . VAL D  1 64  ? 10.258  43.375 -18.576 1.00 47.88  ? 64  VAL D C   1 
ATOM   6924  O O   . VAL D  1 64  ? 10.447  44.573 -18.286 1.00 57.04  ? 64  VAL D O   1 
ATOM   6925  C CB  . VAL D  1 64  ? 11.708  41.945 -20.097 1.00 46.90  ? 64  VAL D CB  1 
ATOM   6926  C CG1 . VAL D  1 64  ? 11.585  43.069 -21.116 1.00 49.80  ? 64  VAL D CG1 1 
ATOM   6927  C CG2 . VAL D  1 64  ? 13.049  41.239 -20.230 1.00 44.87  ? 64  VAL D CG2 1 
ATOM   6928  N N   . ALA D  1 65  ? 9.060   42.834 -18.821 1.00 49.41  ? 65  ALA D N   1 
ATOM   6929  C CA  . ALA D  1 65  ? 7.771   43.565 -18.780 1.00 48.67  ? 65  ALA D CA  1 
ATOM   6930  C C   . ALA D  1 65  ? 7.695   44.383 -17.485 1.00 46.00  ? 65  ALA D C   1 
ATOM   6931  O O   . ALA D  1 65  ? 7.490   45.606 -17.562 1.00 46.47  ? 65  ALA D O   1 
ATOM   6932  C CB  . ALA D  1 65  ? 6.625   42.589 -18.887 1.00 47.56  ? 65  ALA D CB  1 
ATOM   6933  N N   . LEU D  1 66  ? 7.861   43.713 -16.344 1.00 47.84  ? 66  LEU D N   1 
ATOM   6934  C CA  . LEU D  1 66  ? 7.877   44.321 -14.987 1.00 54.37  ? 66  LEU D CA  1 
ATOM   6935  C C   . LEU D  1 66  ? 8.746   45.584 -14.996 1.00 53.09  ? 66  LEU D C   1 
ATOM   6936  O O   . LEU D  1 66  ? 8.210   46.670 -14.710 1.00 59.51  ? 66  LEU D O   1 
ATOM   6937  C CB  . LEU D  1 66  ? 8.422   43.283 -14.001 1.00 61.40  ? 66  LEU D CB  1 
ATOM   6938  C CG  . LEU D  1 66  ? 8.099   43.538 -12.532 1.00 67.22  ? 66  LEU D CG  1 
ATOM   6939  C CD1 . LEU D  1 66  ? 8.680   42.440 -11.656 1.00 69.41  ? 66  LEU D CD1 1 
ATOM   6940  C CD2 . LEU D  1 66  ? 8.606   44.904 -12.097 1.00 72.41  ? 66  LEU D CD2 1 
ATOM   6941  N N   . LEU D  1 67  ? 10.036  45.438 -15.314 1.00 50.19  ? 67  LEU D N   1 
ATOM   6942  C CA  . LEU D  1 67  ? 11.047  46.530 -15.268 1.00 49.45  ? 67  LEU D CA  1 
ATOM   6943  C C   . LEU D  1 67  ? 10.678  47.614 -16.284 1.00 48.91  ? 67  LEU D C   1 
ATOM   6944  O O   . LEU D  1 67  ? 10.685  48.801 -15.910 1.00 57.34  ? 67  LEU D O   1 
ATOM   6945  C CB  . LEU D  1 67  ? 12.433  45.950 -15.565 1.00 49.81  ? 67  LEU D CB  1 
ATOM   6946  C CG  . LEU D  1 67  ? 12.946  44.923 -14.557 1.00 52.92  ? 67  LEU D CG  1 
ATOM   6947  C CD1 . LEU D  1 67  ? 14.314  44.404 -14.969 1.00 60.74  ? 67  LEU D CD1 1 
ATOM   6948  C CD2 . LEU D  1 67  ? 12.998  45.506 -13.153 1.00 51.10  ? 67  LEU D CD2 1 
ATOM   6949  N N   . ALA D  1 68  ? 10.377  47.215 -17.522 1.00 48.98  ? 68  ALA D N   1 
ATOM   6950  C CA  . ALA D  1 68  ? 9.963   48.123 -18.616 1.00 45.62  ? 68  ALA D CA  1 
ATOM   6951  C C   . ALA D  1 68  ? 8.851   49.044 -18.105 1.00 45.39  ? 68  ALA D C   1 
ATOM   6952  O O   . ALA D  1 68  ? 8.960   50.266 -18.306 1.00 53.08  ? 68  ALA D O   1 
ATOM   6953  C CB  . ALA D  1 68  ? 9.513   47.327 -19.814 1.00 44.45  ? 68  ALA D CB  1 
ATOM   6954  N N   . TYR D  1 69  ? 7.835   48.475 -17.450 1.00 38.87  ? 69  TYR D N   1 
ATOM   6955  C CA  . TYR D  1 69  ? 6.626   49.201 -16.981 1.00 39.01  ? 69  TYR D CA  1 
ATOM   6956  C C   . TYR D  1 69  ? 7.004   50.190 -15.873 1.00 39.40  ? 69  TYR D C   1 
ATOM   6957  O O   . TYR D  1 69  ? 6.368   51.259 -15.796 1.00 45.33  ? 69  TYR D O   1 
ATOM   6958  C CB  . TYR D  1 69  ? 5.528   48.220 -16.566 1.00 38.18  ? 69  TYR D CB  1 
ATOM   6959  C CG  . TYR D  1 69  ? 4.498   48.011 -17.646 1.00 42.67  ? 69  TYR D CG  1 
ATOM   6960  C CD1 . TYR D  1 69  ? 3.297   48.701 -17.634 1.00 45.21  ? 69  TYR D CD1 1 
ATOM   6961  C CD2 . TYR D  1 69  ? 4.748   47.168 -18.713 1.00 50.37  ? 69  TYR D CD2 1 
ATOM   6962  C CE1 . TYR D  1 69  ? 2.357   48.533 -18.637 1.00 45.80  ? 69  TYR D CE1 1 
ATOM   6963  C CE2 . TYR D  1 69  ? 3.820   46.990 -19.726 1.00 52.69  ? 69  TYR D CE2 1 
ATOM   6964  C CZ  . TYR D  1 69  ? 2.618   47.673 -19.687 1.00 49.25  ? 69  TYR D CZ  1 
ATOM   6965  O OH  . TYR D  1 69  ? 1.698   47.502 -20.680 1.00 56.18  ? 69  TYR D OH  1 
ATOM   6966  N N   . ILE D  1 70  ? 8.011   49.865 -15.060 1.00 39.33  ? 70  ILE D N   1 
ATOM   6967  C CA  . ILE D  1 70  ? 8.556   50.797 -14.028 1.00 41.25  ? 70  ILE D CA  1 
ATOM   6968  C C   . ILE D  1 70  ? 9.072   52.048 -14.745 1.00 42.92  ? 70  ILE D C   1 
ATOM   6969  O O   . ILE D  1 70  ? 8.754   53.163 -14.287 1.00 49.52  ? 70  ILE D O   1 
ATOM   6970  C CB  . ILE D  1 70  ? 9.653   50.131 -13.174 1.00 41.95  ? 70  ILE D CB  1 
ATOM   6971  C CG1 . ILE D  1 70  ? 9.085   49.006 -12.305 1.00 44.37  ? 70  ILE D CG1 1 
ATOM   6972  C CG2 . ILE D  1 70  ? 10.381  51.173 -12.339 1.00 39.18  ? 70  ILE D CG2 1 
ATOM   6973  C CD1 . ILE D  1 70  ? 10.120  48.304 -11.458 1.00 48.23  ? 70  ILE D CD1 1 
ATOM   6974  N N   . LEU D  1 71  ? 9.820   51.862 -15.837 1.00 43.29  ? 71  LEU D N   1 
ATOM   6975  C CA  . LEU D  1 71  ? 10.367  52.971 -16.664 1.00 49.48  ? 71  LEU D CA  1 
ATOM   6976  C C   . LEU D  1 71  ? 9.203   53.787 -17.237 1.00 49.45  ? 71  LEU D C   1 
ATOM   6977  O O   . LEU D  1 71  ? 9.226   55.023 -17.093 1.00 52.99  ? 71  LEU D O   1 
ATOM   6978  C CB  . LEU D  1 71  ? 11.247  52.403 -17.781 1.00 52.79  ? 71  LEU D CB  1 
ATOM   6979  C CG  . LEU D  1 71  ? 12.497  51.654 -17.321 1.00 60.24  ? 71  LEU D CG  1 
ATOM   6980  C CD1 . LEU D  1 71  ? 13.417  51.368 -18.499 1.00 62.16  ? 71  LEU D CD1 1 
ATOM   6981  C CD2 . LEU D  1 71  ? 13.234  52.429 -16.239 1.00 59.80  ? 71  LEU D CD2 1 
ATOM   6982  N N   . ILE D  1 72  ? 8.225   53.115 -17.855 1.00 48.07  ? 72  ILE D N   1 
ATOM   6983  C CA  . ILE D  1 72  ? 7.021   53.758 -18.464 1.00 48.24  ? 72  ILE D CA  1 
ATOM   6984  C C   . ILE D  1 72  ? 6.356   54.632 -17.398 1.00 51.09  ? 72  ILE D C   1 
ATOM   6985  O O   . ILE D  1 72  ? 6.028   55.793 -17.705 1.00 51.93  ? 72  ILE D O   1 
ATOM   6986  C CB  . ILE D  1 72  ? 6.040   52.709 -19.024 1.00 50.34  ? 72  ILE D CB  1 
ATOM   6987  C CG1 . ILE D  1 72  ? 6.662   51.898 -20.163 1.00 52.76  ? 72  ILE D CG1 1 
ATOM   6988  C CG2 . ILE D  1 72  ? 4.735   53.368 -19.450 1.00 51.79  ? 72  ILE D CG2 1 
ATOM   6989  C CD1 . ILE D  1 72  ? 5.786   50.777 -20.672 1.00 52.12  ? 72  ILE D CD1 1 
ATOM   6990  N N   . ILE D  1 73  ? 6.166   54.085 -16.196 1.00 50.62  ? 73  ILE D N   1 
ATOM   6991  C CA  . ILE D  1 73  ? 5.514   54.790 -15.054 1.00 49.97  ? 73  ILE D CA  1 
ATOM   6992  C C   . ILE D  1 73  ? 6.343   56.034 -14.716 1.00 47.45  ? 73  ILE D C   1 
ATOM   6993  O O   . ILE D  1 73  ? 5.750   57.120 -14.587 1.00 44.70  ? 73  ILE D O   1 
ATOM   6994  C CB  . ILE D  1 73  ? 5.344   53.849 -13.847 1.00 49.52  ? 73  ILE D CB  1 
ATOM   6995  C CG1 . ILE D  1 73  ? 4.381   52.702 -14.167 1.00 51.52  ? 73  ILE D CG1 1 
ATOM   6996  C CG2 . ILE D  1 73  ? 4.896   54.633 -12.624 1.00 52.97  ? 73  ILE D CG2 1 
ATOM   6997  C CD1 . ILE D  1 73  ? 4.394   51.577 -13.157 1.00 53.67  ? 73  ILE D CD1 1 
ATOM   6998  N N   . VAL D  1 74  ? 7.664   55.883 -14.600 1.00 45.40  ? 74  VAL D N   1 
ATOM   6999  C CA  . VAL D  1 74  ? 8.602   57.002 -14.288 1.00 45.16  ? 74  VAL D CA  1 
ATOM   7000  C C   . VAL D  1 74  ? 8.482   58.067 -15.383 1.00 50.61  ? 74  VAL D C   1 
ATOM   7001  O O   . VAL D  1 74  ? 8.335   59.252 -15.033 1.00 56.62  ? 74  VAL D O   1 
ATOM   7002  C CB  . VAL D  1 74  ? 10.051  56.503 -14.141 1.00 43.73  ? 74  VAL D CB  1 
ATOM   7003  C CG1 . VAL D  1 74  ? 11.042  57.656 -14.114 1.00 42.90  ? 74  VAL D CG1 1 
ATOM   7004  C CG2 . VAL D  1 74  ? 10.211  55.622 -12.912 1.00 46.48  ? 74  VAL D CG2 1 
ATOM   7005  N N   . ALA D  1 75  ? 8.538   57.657 -16.655 1.00 51.90  ? 75  ALA D N   1 
ATOM   7006  C CA  . ALA D  1 75  ? 8.420   58.543 -17.838 1.00 47.93  ? 75  ALA D CA  1 
ATOM   7007  C C   . ALA D  1 75  ? 7.103   59.322 -17.763 1.00 46.04  ? 75  ALA D C   1 
ATOM   7008  O O   . ALA D  1 75  ? 7.113   60.531 -18.058 1.00 43.28  ? 75  ALA D O   1 
ATOM   7009  C CB  . ALA D  1 75  ? 8.505   57.735 -19.110 1.00 47.73  ? 75  ALA D CB  1 
ATOM   7010  N N   . PHE D  1 76  ? 6.016   58.645 -17.382 1.00 45.03  ? 76  PHE D N   1 
ATOM   7011  C CA  . PHE D  1 76  ? 4.653   59.223 -17.248 1.00 48.37  ? 76  PHE D CA  1 
ATOM   7012  C C   . PHE D  1 76  ? 4.672   60.324 -16.183 1.00 52.27  ? 76  PHE D C   1 
ATOM   7013  O O   . PHE D  1 76  ? 4.113   61.409 -16.428 1.00 64.89  ? 76  PHE D O   1 
ATOM   7014  C CB  . PHE D  1 76  ? 3.630   58.135 -16.905 1.00 48.92  ? 76  PHE D CB  1 
ATOM   7015  C CG  . PHE D  1 76  ? 2.244   58.650 -16.603 1.00 49.58  ? 76  PHE D CG  1 
ATOM   7016  C CD1 . PHE D  1 76  ? 1.799   58.774 -15.295 1.00 48.79  ? 76  PHE D CD1 1 
ATOM   7017  C CD2 . PHE D  1 76  ? 1.386   59.022 -17.626 1.00 48.35  ? 76  PHE D CD2 1 
ATOM   7018  C CE1 . PHE D  1 76  ? 0.526   59.249 -15.020 1.00 48.86  ? 76  PHE D CE1 1 
ATOM   7019  C CE2 . PHE D  1 76  ? 0.116   59.502 -17.348 1.00 50.54  ? 76  PHE D CE2 1 
ATOM   7020  C CZ  . PHE D  1 76  ? -0.314  59.615 -16.046 1.00 50.97  ? 76  PHE D CZ  1 
ATOM   7021  N N   . LEU D  1 77  ? 5.302   60.050 -15.038 1.00 52.53  ? 77  LEU D N   1 
ATOM   7022  C CA  . LEU D  1 77  ? 5.355   60.975 -13.874 1.00 51.08  ? 77  LEU D CA  1 
ATOM   7023  C C   . LEU D  1 77  ? 6.212   62.200 -14.221 1.00 48.57  ? 77  LEU D C   1 
ATOM   7024  O O   . LEU D  1 77  ? 5.945   63.274 -13.654 1.00 49.37  ? 77  LEU D O   1 
ATOM   7025  C CB  . LEU D  1 77  ? 5.902   60.218 -12.659 1.00 50.36  ? 77  LEU D CB  1 
ATOM   7026  C CG  . LEU D  1 77  ? 4.989   59.115 -12.120 1.00 53.55  ? 77  LEU D CG  1 
ATOM   7027  C CD1 . LEU D  1 77  ? 5.617   58.414 -10.925 1.00 55.04  ? 77  LEU D CD1 1 
ATOM   7028  C CD2 . LEU D  1 77  ? 3.619   59.667 -11.751 1.00 49.73  ? 77  LEU D CD2 1 
ATOM   7029  N N   . LEU D  1 78  ? 7.176   62.054 -15.135 1.00 53.06  ? 78  LEU D N   1 
ATOM   7030  C CA  . LEU D  1 78  ? 8.107   63.142 -15.550 1.00 59.75  ? 78  LEU D CA  1 
ATOM   7031  C C   . LEU D  1 78  ? 7.677   63.730 -16.899 1.00 62.96  ? 78  LEU D C   1 
ATOM   7032  O O   . LEU D  1 78  ? 8.373   64.639 -17.388 1.00 62.10  ? 78  LEU D O   1 
ATOM   7033  C CB  . LEU D  1 78  ? 9.529   62.581 -15.650 1.00 57.86  ? 78  LEU D CB  1 
ATOM   7034  C CG  . LEU D  1 78  ? 10.108  61.987 -14.368 1.00 57.54  ? 78  LEU D CG  1 
ATOM   7035  C CD1 . LEU D  1 78  ? 11.580  61.657 -14.556 1.00 52.98  ? 78  LEU D CD1 1 
ATOM   7036  C CD2 . LEU D  1 78  ? 9.922   62.931 -13.189 1.00 59.29  ? 78  LEU D CD2 1 
ATOM   7037  N N   . GLY D  1 79  ? 6.580   63.231 -17.475 1.00 67.47  ? 79  GLY D N   1 
ATOM   7038  C CA  . GLY D  1 79  ? 6.161   63.547 -18.853 1.00 67.57  ? 79  GLY D CA  1 
ATOM   7039  C C   . GLY D  1 79  ? 5.136   64.665 -18.909 1.00 64.44  ? 79  GLY D C   1 
ATOM   7040  O O   . GLY D  1 79  ? 5.021   65.300 -19.975 1.00 70.95  ? 79  GLY D O   1 
ATOM   7041  N N   . TYR D  1 80  ? 4.414   64.896 -17.810 1.00 64.45  ? 80  TYR D N   1 
ATOM   7042  C CA  . TYR D  1 80  ? 3.306   65.883 -17.728 1.00 70.97  ? 80  TYR D CA  1 
ATOM   7043  C C   . TYR D  1 80  ? 3.513   66.792 -16.513 1.00 72.97  ? 80  TYR D C   1 
ATOM   7044  O O   . TYR D  1 80  ? 4.011   66.318 -15.474 1.00 76.34  ? 80  TYR D O   1 
ATOM   7045  C CB  . TYR D  1 80  ? 1.952   65.170 -17.681 1.00 72.37  ? 80  TYR D CB  1 
ATOM   7046  C CG  . TYR D  1 80  ? 1.577   64.479 -18.967 1.00 82.82  ? 80  TYR D CG  1 
ATOM   7047  C CD1 . TYR D  1 80  ? 0.887   65.149 -19.963 1.00 84.39  ? 80  TYR D CD1 1 
ATOM   7048  C CD2 . TYR D  1 80  ? 1.928   63.159 -19.199 1.00 92.10  ? 80  TYR D CD2 1 
ATOM   7049  C CE1 . TYR D  1 80  ? 0.552   64.526 -21.153 1.00 87.26  ? 80  TYR D CE1 1 
ATOM   7050  C CE2 . TYR D  1 80  ? 1.597   62.520 -20.382 1.00 89.84  ? 80  TYR D CE2 1 
ATOM   7051  C CZ  . TYR D  1 80  ? 0.908   63.206 -21.365 1.00 86.54  ? 80  TYR D CZ  1 
ATOM   7052  O OH  . TYR D  1 80  ? 0.581   62.581 -22.534 1.00 81.94  ? 80  TYR D OH  1 
ATOM   7053  N N   . ASP D  1 81  ? 3.154   68.068 -16.669 1.00 73.50  ? 81  ASP D N   1 
ATOM   7054  C CA  . ASP D  1 81  ? 3.164   69.093 -15.594 1.00 62.17  ? 81  ASP D CA  1 
ATOM   7055  C C   . ASP D  1 81  ? 1.718   69.530 -15.348 1.00 64.89  ? 81  ASP D C   1 
ATOM   7056  O O   . ASP D  1 81  ? 1.023   69.858 -16.331 1.00 62.55  ? 81  ASP D O   1 
ATOM   7057  C CB  . ASP D  1 81  ? 4.051   70.280 -15.969 1.00 56.78  ? 81  ASP D CB  1 
ATOM   7058  C CG  . ASP D  1 81  ? 5.369   69.877 -16.604 1.00 59.82  ? 81  ASP D CG  1 
ATOM   7059  O OD1 . ASP D  1 81  ? 5.775   70.538 -17.580 1.00 64.04  ? 81  ASP D OD1 1 
ATOM   7060  O OD2 . ASP D  1 81  ? 5.981   68.909 -16.117 1.00 70.35  ? 81  ASP D OD2 1 
ATOM   7061  N N   . SER D  1 82  ? 1.279   69.510 -14.088 1.00 72.38  ? 82  SER D N   1 
ATOM   7062  C CA  . SER D  1 82  ? -0.085  69.929 -13.678 1.00 74.11  ? 82  SER D CA  1 
ATOM   7063  C C   . SER D  1 82  ? -0.190  71.453 -13.784 1.00 77.39  ? 82  SER D C   1 
ATOM   7064  O O   . SER D  1 82  ? 0.731   72.147 -13.309 1.00 62.26  ? 82  SER D O   1 
ATOM   7065  C CB  . SER D  1 82  ? -0.422  69.449 -12.293 1.00 74.42  ? 82  SER D CB  1 
ATOM   7066  O OG  . SER D  1 82  ? -1.808  69.609 -12.031 1.00 74.52  ? 82  SER D OG  1 
ATOM   7067  N N   . THR D  1 83  ? -1.267  71.942 -14.403 1.00 87.70  ? 83  THR D N   1 
ATOM   7068  C CA  . THR D  1 83  ? -1.535  73.384 -14.638 1.00 91.11  ? 83  THR D CA  1 
ATOM   7069  C C   . THR D  1 83  ? -3.011  73.666 -14.344 1.00 90.17  ? 83  THR D C   1 
ATOM   7070  O O   . THR D  1 83  ? -3.717  72.731 -13.909 1.00 79.86  ? 83  THR D O   1 
ATOM   7071  C CB  . THR D  1 83  ? -1.164  73.789 -16.071 1.00 89.52  ? 83  THR D CB  1 
ATOM   7072  O OG1 . THR D  1 83  ? -2.048  73.106 -16.960 1.00 97.05  ? 83  THR D OG1 1 
ATOM   7073  C CG2 . THR D  1 83  ? 0.270   73.467 -16.431 1.00 85.37  ? 83  THR D CG2 1 
ATOM   7074  N N   . ALA D  1 84  ? -3.447  74.909 -14.571 1.00 88.98  ? 84  ALA D N   1 
ATOM   7075  C CA  . ALA D  1 84  ? -4.859  75.344 -14.475 1.00 86.45  ? 84  ALA D CA  1 
ATOM   7076  C C   . ALA D  1 84  ? -5.676  74.638 -15.563 1.00 89.62  ? 84  ALA D C   1 
ATOM   7077  O O   . ALA D  1 84  ? -6.905  74.515 -15.394 1.00 101.04 ? 84  ALA D O   1 
ATOM   7078  C CB  . ALA D  1 84  ? -4.942  76.846 -14.604 1.00 80.52  ? 84  ALA D CB  1 
ATOM   7079  N N   . GLY D  1 85  ? -5.005  74.181 -16.627 1.00 84.97  ? 85  GLY D N   1 
ATOM   7080  C CA  . GLY D  1 85  ? -5.637  73.614 -17.834 1.00 83.45  ? 85  GLY D CA  1 
ATOM   7081  C C   . GLY D  1 85  ? -5.591  72.095 -17.858 1.00 91.52  ? 85  GLY D C   1 
ATOM   7082  O O   . GLY D  1 85  ? -5.974  71.522 -18.895 1.00 95.64  ? 85  GLY D O   1 
ATOM   7083  N N   . GLY D  1 86  ? -5.139  71.464 -16.766 1.00 103.91 ? 86  GLY D N   1 
ATOM   7084  C CA  . GLY D  1 86  ? -5.088  69.994 -16.617 1.00 98.08  ? 86  GLY D CA  1 
ATOM   7085  C C   . GLY D  1 86  ? -3.670  69.478 -16.421 1.00 92.69  ? 86  GLY D C   1 
ATOM   7086  O O   . GLY D  1 86  ? -3.003  69.946 -15.480 1.00 102.02 ? 86  GLY D O   1 
ATOM   7087  N N   . TRP D  1 87  ? -3.232  68.536 -17.267 1.00 76.43  ? 87  TRP D N   1 
ATOM   7088  C CA  . TRP D  1 87  ? -1.845  67.992 -17.293 1.00 69.38  ? 87  TRP D CA  1 
ATOM   7089  C C   . TRP D  1 87  ? -1.220  68.236 -18.670 1.00 63.17  ? 87  TRP D C   1 
ATOM   7090  O O   . TRP D  1 87  ? -1.607  67.528 -19.618 1.00 60.69  ? 87  TRP D O   1 
ATOM   7091  C CB  . TRP D  1 87  ? -1.836  66.498 -16.947 1.00 65.28  ? 87  TRP D CB  1 
ATOM   7092  C CG  . TRP D  1 87  ? -2.121  66.207 -15.508 1.00 60.01  ? 87  TRP D CG  1 
ATOM   7093  C CD1 . TRP D  1 87  ? -3.343  66.002 -14.938 1.00 59.34  ? 87  TRP D CD1 1 
ATOM   7094  C CD2 . TRP D  1 87  ? -1.157  66.096 -14.447 1.00 56.74  ? 87  TRP D CD2 1 
ATOM   7095  N NE1 . TRP D  1 87  ? -3.207  65.764 -13.597 1.00 62.59  ? 87  TRP D NE1 1 
ATOM   7096  C CE2 . TRP D  1 87  ? -1.878  65.817 -13.267 1.00 56.32  ? 87  TRP D CE2 1 
ATOM   7097  C CE3 . TRP D  1 87  ? 0.238   66.204 -14.380 1.00 53.18  ? 87  TRP D CE3 1 
ATOM   7098  C CZ2 . TRP D  1 87  ? -1.247  65.647 -12.036 1.00 53.45  ? 87  TRP D CZ2 1 
ATOM   7099  C CZ3 . TRP D  1 87  ? 0.859   66.032 -13.163 1.00 51.10  ? 87  TRP D CZ3 1 
ATOM   7100  C CH2 . TRP D  1 87  ? 0.124   65.758 -12.010 1.00 54.33  ? 87  TRP D CH2 1 
ATOM   7101  N N   . VAL D  1 88  ? -0.277  69.180 -18.761 1.00 61.29  ? 88  VAL D N   1 
ATOM   7102  C CA  . VAL D  1 88  ? 0.313   69.652 -20.050 1.00 63.39  ? 88  VAL D CA  1 
ATOM   7103  C C   . VAL D  1 88  ? 1.561   68.834 -20.362 1.00 59.12  ? 88  VAL D C   1 
ATOM   7104  O O   . VAL D  1 88  ? 2.469   68.731 -19.543 1.00 57.17  ? 88  VAL D O   1 
ATOM   7105  C CB  . VAL D  1 88  ? 0.633   71.158 -20.010 1.00 65.98  ? 88  VAL D CB  1 
ATOM   7106  C CG1 . VAL D  1 88  ? 1.380   71.605 -21.258 1.00 61.82  ? 88  VAL D CG1 1 
ATOM   7107  C CG2 . VAL D  1 88  ? -0.620  71.995 -19.803 1.00 71.49  ? 88  VAL D CG2 1 
ATOM   7108  N N   . PRO D  1 89  ? 1.642   68.241 -21.572 1.00 63.55  ? 89  PRO D N   1 
ATOM   7109  C CA  . PRO D  1 89  ? 2.829   67.501 -21.997 1.00 65.77  ? 89  PRO D CA  1 
ATOM   7110  C C   . PRO D  1 89  ? 4.089   68.376 -21.969 1.00 62.07  ? 89  PRO D C   1 
ATOM   7111  O O   . PRO D  1 89  ? 4.010   69.515 -22.381 1.00 75.52  ? 89  PRO D O   1 
ATOM   7112  C CB  . PRO D  1 89  ? 2.515   67.088 -23.445 1.00 68.35  ? 89  PRO D CB  1 
ATOM   7113  C CG  . PRO D  1 89  ? 1.003   67.155 -23.546 1.00 70.88  ? 89  PRO D CG  1 
ATOM   7114  C CD  . PRO D  1 89  ? 0.589   68.260 -22.597 1.00 67.18  ? 89  PRO D CD  1 
ATOM   7115  N N   . ASN D  1 90  ? 5.203   67.829 -21.475 1.00 61.45  ? 90  ASN D N   1 
ATOM   7116  C CA  . ASN D  1 90  ? 6.553   68.449 -21.570 1.00 67.10  ? 90  ASN D CA  1 
ATOM   7117  C C   . ASN D  1 90  ? 7.359   67.664 -22.613 1.00 71.41  ? 90  ASN D C   1 
ATOM   7118  O O   . ASN D  1 90  ? 6.753   66.809 -23.291 1.00 76.14  ? 90  ASN D O   1 
ATOM   7119  C CB  . ASN D  1 90  ? 7.240   68.529 -20.201 1.00 71.82  ? 90  ASN D CB  1 
ATOM   7120  C CG  . ASN D  1 90  ? 7.541   67.174 -19.596 1.00 76.36  ? 90  ASN D CG  1 
ATOM   7121  O OD1 . ASN D  1 90  ? 8.122   66.309 -20.250 1.00 89.99  ? 90  ASN D OD1 1 
ATOM   7122  N ND2 . ASN D  1 90  ? 7.160   66.977 -18.346 1.00 73.02  ? 90  ASN D ND2 1 
ATOM   7123  N N   . ASP D  1 91  ? 8.661   67.945 -22.727 1.00 78.90  ? 91  ASP D N   1 
ATOM   7124  C CA  . ASP D  1 91  ? 9.589   67.342 -23.725 1.00 82.09  ? 91  ASP D CA  1 
ATOM   7125  C C   . ASP D  1 91  ? 9.599   65.816 -23.582 1.00 78.50  ? 91  ASP D C   1 
ATOM   7126  O O   . ASP D  1 91  ? 9.723   65.122 -24.614 1.00 90.71  ? 91  ASP D O   1 
ATOM   7127  C CB  . ASP D  1 91  ? 11.019  67.861 -23.546 1.00 82.12  ? 91  ASP D CB  1 
ATOM   7128  C CG  . ASP D  1 91  ? 11.164  69.362 -23.711 1.00 90.87  ? 91  ASP D CG  1 
ATOM   7129  O OD1 . ASP D  1 91  ? 10.145  70.020 -24.000 1.00 98.85  ? 91  ASP D OD1 1 
ATOM   7130  O OD2 . ASP D  1 91  ? 12.295  69.858 -23.545 1.00 95.92  ? 91  ASP D OD2 1 
ATOM   7131  N N   . GLY D  1 92  ? 9.484   65.323 -22.346 1.00 71.83  ? 92  GLY D N   1 
ATOM   7132  C CA  . GLY D  1 92  ? 9.707   63.908 -21.992 1.00 70.58  ? 92  GLY D CA  1 
ATOM   7133  C C   . GLY D  1 92  ? 8.463   63.056 -22.167 1.00 72.44  ? 92  GLY D C   1 
ATOM   7134  O O   . GLY D  1 92  ? 8.555   61.839 -21.912 1.00 79.34  ? 92  GLY D O   1 
ATOM   7135  N N   . ALA D  1 93  ? 7.342   63.657 -22.583 1.00 68.63  ? 93  ALA D N   1 
ATOM   7136  C CA  . ALA D  1 93  ? 6.033   62.979 -22.741 1.00 61.49  ? 93  ALA D CA  1 
ATOM   7137  C C   . ALA D  1 93  ? 6.140   61.885 -23.810 1.00 55.66  ? 93  ALA D C   1 
ATOM   7138  O O   . ALA D  1 93  ? 5.466   60.846 -23.667 1.00 52.07  ? 93  ALA D O   1 
ATOM   7139  C CB  . ALA D  1 93  ? 4.965   63.986 -23.085 1.00 63.54  ? 93  ALA D CB  1 
ATOM   7140  N N   . ILE D  1 94  ? 6.961   62.118 -24.839 1.00 54.29  ? 94  ILE D N   1 
ATOM   7141  C CA  . ILE D  1 94  ? 7.201   61.166 -25.966 1.00 57.12  ? 94  ILE D CA  1 
ATOM   7142  C C   . ILE D  1 94  ? 7.773   59.859 -25.402 1.00 55.18  ? 94  ILE D C   1 
ATOM   7143  O O   . ILE D  1 94  ? 7.476   58.785 -25.969 1.00 59.75  ? 94  ILE D O   1 
ATOM   7144  C CB  . ILE D  1 94  ? 8.132   61.795 -27.023 1.00 56.49  ? 94  ILE D CB  1 
ATOM   7145  C CG1 . ILE D  1 94  ? 8.302   60.885 -28.242 1.00 58.50  ? 94  ILE D CG1 1 
ATOM   7146  C CG2 . ILE D  1 94  ? 9.475   62.169 -26.410 1.00 52.81  ? 94  ILE D CG2 1 
ATOM   7147  C CD1 . ILE D  1 94  ? 9.162   61.481 -29.334 1.00 61.52  ? 94  ILE D CD1 1 
ATOM   7148  N N   . ASN D  1 95  ? 8.554   59.955 -24.322 1.00 54.55  ? 95  ASN D N   1 
ATOM   7149  C CA  . ASN D  1 95  ? 9.296   58.819 -23.711 1.00 55.88  ? 95  ASN D CA  1 
ATOM   7150  C C   . ASN D  1 95  ? 8.307   57.758 -23.221 1.00 53.71  ? 95  ASN D C   1 
ATOM   7151  O O   . ASN D  1 95  ? 8.683   56.571 -23.203 1.00 54.78  ? 95  ASN D O   1 
ATOM   7152  C CB  . ASN D  1 95  ? 10.213  59.288 -22.580 1.00 58.71  ? 95  ASN D CB  1 
ATOM   7153  C CG  . ASN D  1 95  ? 11.333  60.178 -23.074 1.00 66.42  ? 95  ASN D CG  1 
ATOM   7154  O OD1 . ASN D  1 95  ? 11.635  60.201 -24.265 1.00 76.00  ? 95  ASN D OD1 1 
ATOM   7155  N ND2 . ASN D  1 95  ? 11.951  60.917 -22.169 1.00 72.20  ? 95  ASN D ND2 1 
ATOM   7156  N N   . ILE D  1 96  ? 7.095   58.170 -22.838 1.00 51.65  ? 96  ILE D N   1 
ATOM   7157  C CA  . ILE D  1 96  ? 6.009   57.255 -22.375 1.00 54.20  ? 96  ILE D CA  1 
ATOM   7158  C C   . ILE D  1 96  ? 5.742   56.219 -23.473 1.00 59.03  ? 96  ILE D C   1 
ATOM   7159  O O   . ILE D  1 96  ? 5.538   55.034 -23.135 1.00 62.21  ? 96  ILE D O   1 
ATOM   7160  C CB  . ILE D  1 96  ? 4.741   58.050 -22.010 1.00 50.80  ? 96  ILE D CB  1 
ATOM   7161  C CG1 . ILE D  1 96  ? 4.999   58.995 -20.835 1.00 55.33  ? 96  ILE D CG1 1 
ATOM   7162  C CG2 . ILE D  1 96  ? 3.571   57.116 -21.739 1.00 47.39  ? 96  ILE D CG2 1 
ATOM   7163  C CD1 . ILE D  1 96  ? 3.852   59.928 -20.536 1.00 61.77  ? 96  ILE D CD1 1 
ATOM   7164  N N   . PHE D  1 97  ? 5.753   56.657 -24.735 1.00 54.91  ? 97  PHE D N   1 
ATOM   7165  C CA  . PHE D  1 97  ? 5.511   55.810 -25.932 1.00 55.69  ? 97  PHE D CA  1 
ATOM   7166  C C   . PHE D  1 97  ? 6.822   55.143 -26.349 1.00 50.71  ? 97  PHE D C   1 
ATOM   7167  O O   . PHE D  1 97  ? 6.818   53.930 -26.636 1.00 54.46  ? 97  PHE D O   1 
ATOM   7168  C CB  . PHE D  1 97  ? 4.898   56.649 -27.053 1.00 60.08  ? 97  PHE D CB  1 
ATOM   7169  C CG  . PHE D  1 97  ? 3.550   57.217 -26.695 1.00 66.41  ? 97  PHE D CG  1 
ATOM   7170  C CD1 . PHE D  1 97  ? 2.385   56.576 -27.082 1.00 65.10  ? 97  PHE D CD1 1 
ATOM   7171  C CD2 . PHE D  1 97  ? 3.448   58.374 -25.938 1.00 71.32  ? 97  PHE D CD2 1 
ATOM   7172  C CE1 . PHE D  1 97  ? 1.146   57.092 -26.737 1.00 70.20  ? 97  PHE D CE1 1 
ATOM   7173  C CE2 . PHE D  1 97  ? 2.209   58.886 -25.589 1.00 74.05  ? 97  PHE D CE2 1 
ATOM   7174  C CZ  . PHE D  1 97  ? 1.061   58.246 -25.993 1.00 76.40  ? 97  PHE D CZ  1 
ATOM   7175  N N   . SER D  1 98  ? 7.906   55.922 -26.364 1.00 48.04  ? 98  SER D N   1 
ATOM   7176  C CA  . SER D  1 98  ? 9.291   55.451 -26.623 1.00 51.56  ? 98  SER D CA  1 
ATOM   7177  C C   . SER D  1 98  ? 9.575   54.189 -25.796 1.00 48.37  ? 98  SER D C   1 
ATOM   7178  O O   . SER D  1 98  ? 9.997   53.173 -26.386 1.00 38.83  ? 98  SER D O   1 
ATOM   7179  C CB  . SER D  1 98  ? 10.281  56.541 -26.317 1.00 51.81  ? 98  SER D CB  1 
ATOM   7180  O OG  . SER D  1 98  ? 11.603  56.121 -26.612 1.00 61.34  ? 98  SER D OG  1 
ATOM   7181  N N   . THR D  1 99  ? 9.340   54.259 -24.482 1.00 54.71  ? 99  THR D N   1 
ATOM   7182  C CA  . THR D  1 99  ? 9.667   53.195 -23.494 1.00 57.87  ? 99  THR D CA  1 
ATOM   7183  C C   . THR D  1 99  ? 8.900   51.907 -23.816 1.00 57.67  ? 99  THR D C   1 
ATOM   7184  O O   . THR D  1 99  ? 9.468   50.817 -23.597 1.00 58.56  ? 99  THR D O   1 
ATOM   7185  C CB  . THR D  1 99  ? 9.367   53.649 -22.060 1.00 55.27  ? 99  THR D CB  1 
ATOM   7186  O OG1 . THR D  1 99  ? 9.891   54.964 -21.880 1.00 48.35  ? 99  THR D OG1 1 
ATOM   7187  C CG2 . THR D  1 99  ? 9.961   52.721 -21.022 1.00 59.76  ? 99  THR D CG2 1 
ATOM   7188  N N   . ARG D  1 100 ? 7.661   52.020 -24.304 1.00 56.20  ? 100 ARG D N   1 
ATOM   7189  C CA  . ARG D  1 100 ? 6.792   50.844 -24.573 1.00 55.73  ? 100 ARG D CA  1 
ATOM   7190  C C   . ARG D  1 100 ? 7.384   50.030 -25.730 1.00 51.92  ? 100 ARG D C   1 
ATOM   7191  O O   . ARG D  1 100 ? 7.333   48.788 -25.659 1.00 54.28  ? 100 ARG D O   1 
ATOM   7192  C CB  . ARG D  1 100 ? 5.348   51.263 -24.861 1.00 52.73  ? 100 ARG D CB  1 
ATOM   7193  C CG  . ARG D  1 100 ? 4.338   50.172 -24.534 1.00 53.88  ? 100 ARG D CG  1 
ATOM   7194  C CD  . ARG D  1 100 ? 2.914   50.566 -24.861 1.00 58.63  ? 100 ARG D CD  1 
ATOM   7195  N NE  . ARG D  1 100 ? 2.297   51.376 -23.822 1.00 53.00  ? 100 ARG D NE  1 
ATOM   7196  C CZ  . ARG D  1 100 ? 1.685   50.884 -22.753 1.00 53.27  ? 100 ARG D CZ  1 
ATOM   7197  N NH1 . ARG D  1 100 ? 1.627   49.576 -22.565 1.00 53.95  ? 100 ARG D NH1 1 
ATOM   7198  N NH2 . ARG D  1 100 ? 1.138   51.703 -21.874 1.00 63.47  ? 100 ARG D NH2 1 
ATOM   7199  N N   . TYR D  1 101 ? 7.930   50.701 -26.747 1.00 51.52  ? 101 TYR D N   1 
ATOM   7200  C CA  . TYR D  1 101 ? 8.631   50.062 -27.892 1.00 55.55  ? 101 TYR D CA  1 
ATOM   7201  C C   . TYR D  1 101 ? 9.812   49.248 -27.352 1.00 53.74  ? 101 TYR D C   1 
ATOM   7202  O O   . TYR D  1 101 ? 9.935   48.057 -27.702 1.00 52.30  ? 101 TYR D O   1 
ATOM   7203  C CB  . TYR D  1 101 ? 9.064   51.108 -28.924 1.00 60.88  ? 101 TYR D CB  1 
ATOM   7204  C CG  . TYR D  1 101 ? 7.945   51.582 -29.817 1.00 67.08  ? 101 TYR D CG  1 
ATOM   7205  C CD1 . TYR D  1 101 ? 7.575   50.863 -30.942 1.00 65.46  ? 101 TYR D CD1 1 
ATOM   7206  C CD2 . TYR D  1 101 ? 7.236   52.735 -29.524 1.00 70.10  ? 101 TYR D CD2 1 
ATOM   7207  C CE1 . TYR D  1 101 ? 6.537   51.282 -31.759 1.00 66.42  ? 101 TYR D CE1 1 
ATOM   7208  C CE2 . TYR D  1 101 ? 6.196   53.168 -30.329 1.00 70.87  ? 101 TYR D CE2 1 
ATOM   7209  C CZ  . TYR D  1 101 ? 5.845   52.439 -31.451 1.00 71.08  ? 101 TYR D CZ  1 
ATOM   7210  O OH  . TYR D  1 101 ? 4.821   52.862 -32.249 1.00 71.11  ? 101 TYR D OH  1 
ATOM   7211  N N   . ILE D  1 102 ? 10.641  49.875 -26.513 1.00 53.56  ? 102 ILE D N   1 
ATOM   7212  C CA  . ILE D  1 102 ? 11.793  49.225 -25.820 1.00 51.22  ? 102 ILE D CA  1 
ATOM   7213  C C   . ILE D  1 102 ? 11.314  47.900 -25.218 1.00 47.18  ? 102 ILE D C   1 
ATOM   7214  O O   . ILE D  1 102 ? 11.974  46.868 -25.455 1.00 46.98  ? 102 ILE D O   1 
ATOM   7215  C CB  . ILE D  1 102 ? 12.389  50.161 -24.749 1.00 49.47  ? 102 ILE D CB  1 
ATOM   7216  C CG1 . ILE D  1 102 ? 12.935  51.450 -25.369 1.00 52.91  ? 102 ILE D CG1 1 
ATOM   7217  C CG2 . ILE D  1 102 ? 13.443  49.436 -23.926 1.00 49.11  ? 102 ILE D CG2 1 
ATOM   7218  C CD1 . ILE D  1 102 ? 13.576  52.393 -24.376 1.00 54.08  ? 102 ILE D CD1 1 
ATOM   7219  N N   . GLU D  1 103 ? 10.207  47.937 -24.470 1.00 44.65  ? 103 GLU D N   1 
ATOM   7220  C CA  . GLU D  1 103 ? 9.589   46.743 -23.834 1.00 47.96  ? 103 GLU D CA  1 
ATOM   7221  C C   . GLU D  1 103 ? 9.369   45.665 -24.900 1.00 47.26  ? 103 GLU D C   1 
ATOM   7222  O O   . GLU D  1 103 ? 9.982   44.585 -24.791 1.00 41.11  ? 103 GLU D O   1 
ATOM   7223  C CB  . GLU D  1 103 ? 8.255   47.096 -23.175 1.00 47.59  ? 103 GLU D CB  1 
ATOM   7224  C CG  . GLU D  1 103 ? 7.488   45.875 -22.696 1.00 49.49  ? 103 GLU D CG  1 
ATOM   7225  C CD  . GLU D  1 103 ? 5.979   46.035 -22.687 1.00 55.24  ? 103 GLU D CD  1 
ATOM   7226  O OE1 . GLU D  1 103 ? 5.277   45.005 -22.731 1.00 62.23  ? 103 GLU D OE1 1 
ATOM   7227  O OE2 . GLU D  1 103 ? 5.508   47.191 -22.638 1.00 59.47  ? 103 GLU D OE2 1 
ATOM   7228  N N   . TRP D  1 104 ? 8.519   45.961 -25.886 1.00 47.84  ? 104 TRP D N   1 
ATOM   7229  C CA  . TRP D  1 104 ? 8.102   45.023 -26.961 1.00 47.27  ? 104 TRP D CA  1 
ATOM   7230  C C   . TRP D  1 104 ? 9.339   44.403 -27.616 1.00 47.96  ? 104 TRP D C   1 
ATOM   7231  O O   . TRP D  1 104 ? 9.338   43.174 -27.833 1.00 48.05  ? 104 TRP D O   1 
ATOM   7232  C CB  . TRP D  1 104 ? 7.226   45.740 -27.993 1.00 49.10  ? 104 TRP D CB  1 
ATOM   7233  C CG  . TRP D  1 104 ? 5.928   46.245 -27.443 1.00 51.27  ? 104 TRP D CG  1 
ATOM   7234  C CD1 . TRP D  1 104 ? 5.269   45.794 -26.335 1.00 51.76  ? 104 TRP D CD1 1 
ATOM   7235  C CD2 . TRP D  1 104 ? 5.109   47.286 -28.000 1.00 54.67  ? 104 TRP D CD2 1 
ATOM   7236  N NE1 . TRP D  1 104 ? 4.106   46.494 -26.155 1.00 49.33  ? 104 TRP D NE1 1 
ATOM   7237  C CE2 . TRP D  1 104 ? 3.980   47.415 -27.162 1.00 54.45  ? 104 TRP D CE2 1 
ATOM   7238  C CE3 . TRP D  1 104 ? 5.223   48.124 -29.116 1.00 53.97  ? 104 TRP D CE3 1 
ATOM   7239  C CZ2 . TRP D  1 104 ? 2.976   48.349 -27.409 1.00 56.15  ? 104 TRP D CZ2 1 
ATOM   7240  C CZ3 . TRP D  1 104 ? 4.230   49.047 -29.358 1.00 55.66  ? 104 TRP D CZ3 1 
ATOM   7241  C CH2 . TRP D  1 104 ? 3.122   49.155 -28.516 1.00 56.19  ? 104 TRP D CH2 1 
ATOM   7242  N N   . THR D  1 105 ? 10.345  45.228 -27.922 1.00 40.83  ? 105 THR D N   1 
ATOM   7243  C CA  . THR D  1 105 ? 11.582  44.814 -28.631 1.00 37.94  ? 105 THR D CA  1 
ATOM   7244  C C   . THR D  1 105 ? 12.127  43.530 -27.997 1.00 42.89  ? 105 THR D C   1 
ATOM   7245  O O   . THR D  1 105 ? 12.594  42.657 -28.752 1.00 47.27  ? 105 THR D O   1 
ATOM   7246  C CB  . THR D  1 105 ? 12.636  45.926 -28.626 1.00 35.45  ? 105 THR D CB  1 
ATOM   7247  O OG1 . THR D  1 105 ? 12.059  47.102 -29.193 1.00 35.36  ? 105 THR D OG1 1 
ATOM   7248  C CG2 . THR D  1 105 ? 13.874  45.547 -29.410 1.00 34.08  ? 105 THR D CG2 1 
ATOM   7249  N N   . VAL D  1 106 ? 12.054  43.415 -26.667 1.00 47.11  ? 106 VAL D N   1 
ATOM   7250  C CA  . VAL D  1 106 ? 12.634  42.278 -25.888 1.00 49.50  ? 106 VAL D CA  1 
ATOM   7251  C C   . VAL D  1 106 ? 11.523  41.290 -25.510 1.00 50.86  ? 106 VAL D C   1 
ATOM   7252  O O   . VAL D  1 106 ? 11.732  40.076 -25.697 1.00 53.07  ? 106 VAL D O   1 
ATOM   7253  C CB  . VAL D  1 106 ? 13.388  42.775 -24.639 1.00 49.60  ? 106 VAL D CB  1 
ATOM   7254  C CG1 . VAL D  1 106 ? 14.121  41.642 -23.936 1.00 46.32  ? 106 VAL D CG1 1 
ATOM   7255  C CG2 . VAL D  1 106 ? 14.350  43.906 -24.974 1.00 49.40  ? 106 VAL D CG2 1 
ATOM   7256  N N   . SER D  1 107 ? 10.396  41.785 -24.990 1.00 49.43  ? 107 SER D N   1 
ATOM   7257  C CA  . SER D  1 107 ? 9.300   40.954 -24.422 1.00 50.51  ? 107 SER D CA  1 
ATOM   7258  C C   . SER D  1 107 ? 8.707   40.038 -25.501 1.00 51.03  ? 107 SER D C   1 
ATOM   7259  O O   . SER D  1 107 ? 8.415   38.869 -25.182 1.00 52.55  ? 107 SER D O   1 
ATOM   7260  C CB  . SER D  1 107 ? 8.238   41.809 -23.777 1.00 53.92  ? 107 SER D CB  1 
ATOM   7261  O OG  . SER D  1 107 ? 7.658   42.700 -24.716 1.00 57.92  ? 107 SER D OG  1 
ATOM   7262  N N   . VAL D  1 108 ? 8.548   40.542 -26.729 1.00 53.05  ? 108 VAL D N   1 
ATOM   7263  C CA  . VAL D  1 108 ? 7.869   39.822 -27.850 1.00 54.39  ? 108 VAL D CA  1 
ATOM   7264  C C   . VAL D  1 108 ? 8.734   38.647 -28.304 1.00 48.80  ? 108 VAL D C   1 
ATOM   7265  O O   . VAL D  1 108 ? 8.278   37.506 -28.302 1.00 45.28  ? 108 VAL D O   1 
ATOM   7266  C CB  . VAL D  1 108 ? 7.543   40.771 -29.020 1.00 55.87  ? 108 VAL D CB  1 
ATOM   7267  C CG1 . VAL D  1 108 ? 7.123   40.007 -30.266 1.00 55.96  ? 108 VAL D CG1 1 
ATOM   7268  C CG2 . VAL D  1 108 ? 6.480   41.787 -28.634 1.00 54.00  ? 108 VAL D CG2 1 
ATOM   7269  N N   . PRO D  1 109 ? 9.997   38.880 -28.727 1.00 43.49  ? 109 PRO D N   1 
ATOM   7270  C CA  . PRO D  1 109 ? 10.885  37.790 -29.129 1.00 43.37  ? 109 PRO D CA  1 
ATOM   7271  C C   . PRO D  1 109 ? 10.879  36.620 -28.134 1.00 44.27  ? 109 PRO D C   1 
ATOM   7272  O O   . PRO D  1 109 ? 10.910  35.485 -28.566 1.00 45.26  ? 109 PRO D O   1 
ATOM   7273  C CB  . PRO D  1 109 ? 12.260  38.467 -29.179 1.00 42.33  ? 109 PRO D CB  1 
ATOM   7274  C CG  . PRO D  1 109 ? 11.943  39.895 -29.559 1.00 41.75  ? 109 PRO D CG  1 
ATOM   7275  C CD  . PRO D  1 109 ? 10.631  40.200 -28.864 1.00 42.80  ? 109 PRO D CD  1 
ATOM   7276  N N   . LEU D  1 110 ? 10.837  36.921 -26.834 1.00 46.40  ? 110 LEU D N   1 
ATOM   7277  C CA  . LEU D  1 110 ? 10.780  35.906 -25.749 1.00 47.48  ? 110 LEU D CA  1 
ATOM   7278  C C   . LEU D  1 110 ? 9.466   35.124 -25.858 1.00 49.46  ? 110 LEU D C   1 
ATOM   7279  O O   . LEU D  1 110 ? 9.476   33.913 -25.576 1.00 55.82  ? 110 LEU D O   1 
ATOM   7280  C CB  . LEU D  1 110 ? 10.912  36.607 -24.395 1.00 44.41  ? 110 LEU D CB  1 
ATOM   7281  C CG  . LEU D  1 110 ? 12.318  37.102 -24.054 1.00 41.91  ? 110 LEU D CG  1 
ATOM   7282  C CD1 . LEU D  1 110 ? 12.322  37.882 -22.750 1.00 42.75  ? 110 LEU D CD1 1 
ATOM   7283  C CD2 . LEU D  1 110 ? 13.298  35.942 -23.983 1.00 39.18  ? 110 LEU D CD2 1 
ATOM   7284  N N   . LEU D  1 111 ? 8.385   35.794 -26.266 1.00 48.76  ? 111 LEU D N   1 
ATOM   7285  C CA  . LEU D  1 111 ? 7.050   35.173 -26.472 1.00 52.67  ? 111 LEU D CA  1 
ATOM   7286  C C   . LEU D  1 111 ? 7.136   34.137 -27.600 1.00 50.99  ? 111 LEU D C   1 
ATOM   7287  O O   . LEU D  1 111 ? 6.546   33.049 -27.443 1.00 54.80  ? 111 LEU D O   1 
ATOM   7288  C CB  . LEU D  1 111 ? 6.025   36.265 -26.788 1.00 58.23  ? 111 LEU D CB  1 
ATOM   7289  C CG  . LEU D  1 111 ? 5.587   37.106 -25.589 1.00 63.34  ? 111 LEU D CG  1 
ATOM   7290  C CD1 . LEU D  1 111 ? 4.696   38.258 -26.024 1.00 64.62  ? 111 LEU D CD1 1 
ATOM   7291  C CD2 . LEU D  1 111 ? 4.874   36.247 -24.557 1.00 61.34  ? 111 LEU D CD2 1 
ATOM   7292  N N   . THR D  1 112 ? 7.842   34.457 -28.690 1.00 48.45  ? 112 THR D N   1 
ATOM   7293  C CA  . THR D  1 112 ? 8.092   33.519 -29.819 1.00 53.18  ? 112 THR D CA  1 
ATOM   7294  C C   . THR D  1 112 ? 8.810   32.279 -29.278 1.00 50.74  ? 112 THR D C   1 
ATOM   7295  O O   . THR D  1 112 ? 8.267   31.168 -29.432 1.00 49.48  ? 112 THR D O   1 
ATOM   7296  C CB  . THR D  1 112 ? 8.900   34.171 -30.949 1.00 54.06  ? 112 THR D CB  1 
ATOM   7297  O OG1 . THR D  1 112 ? 10.245  34.346 -30.504 1.00 62.09  ? 112 THR D OG1 1 
ATOM   7298  C CG2 . THR D  1 112 ? 8.326   35.497 -31.392 1.00 57.00  ? 112 THR D CG2 1 
ATOM   7299  N N   . ILE D  1 113 ? 9.977   32.481 -28.658 1.00 54.57  ? 113 ILE D N   1 
ATOM   7300  C CA  . ILE D  1 113 ? 10.834  31.409 -28.068 1.00 58.83  ? 113 ILE D CA  1 
ATOM   7301  C C   . ILE D  1 113 ? 9.967   30.501 -27.191 1.00 58.35  ? 113 ILE D C   1 
ATOM   7302  O O   . ILE D  1 113 ? 10.106  29.268 -27.296 1.00 51.93  ? 113 ILE D O   1 
ATOM   7303  C CB  . ILE D  1 113 ? 11.999  32.026 -27.269 1.00 55.38  ? 113 ILE D CB  1 
ATOM   7304  C CG1 . ILE D  1 113 ? 12.956  32.803 -28.176 1.00 55.30  ? 113 ILE D CG1 1 
ATOM   7305  C CG2 . ILE D  1 113 ? 12.727  30.956 -26.471 1.00 57.25  ? 113 ILE D CG2 1 
ATOM   7306  C CD1 . ILE D  1 113 ? 13.841  33.781 -27.445 1.00 55.87  ? 113 ILE D CD1 1 
ATOM   7307  N N   . GLU D  1 114 ? 9.112   31.100 -26.359 1.00 58.24  ? 114 GLU D N   1 
ATOM   7308  C CA  . GLU D  1 114 ? 8.240   30.392 -25.386 1.00 59.35  ? 114 GLU D CA  1 
ATOM   7309  C C   . GLU D  1 114 ? 7.312   29.431 -26.138 1.00 59.96  ? 114 GLU D C   1 
ATOM   7310  O O   . GLU D  1 114 ? 7.152   28.284 -25.674 1.00 61.79  ? 114 GLU D O   1 
ATOM   7311  C CB  . GLU D  1 114 ? 7.443   31.406 -24.565 1.00 65.24  ? 114 GLU D CB  1 
ATOM   7312  C CG  . GLU D  1 114 ? 6.605   30.775 -23.470 1.00 72.41  ? 114 GLU D CG  1 
ATOM   7313  C CD  . GLU D  1 114 ? 5.892   31.770 -22.571 1.00 81.15  ? 114 GLU D CD  1 
ATOM   7314  O OE1 . GLU D  1 114 ? 4.961   31.350 -21.856 1.00 89.70  ? 114 GLU D OE1 1 
ATOM   7315  O OE2 . GLU D  1 114 ? 6.267   32.962 -22.588 1.00 76.14  ? 114 GLU D OE2 1 
ATOM   7316  N N   . LEU D  1 115 ? 6.727   29.882 -27.253 1.00 58.43  ? 115 LEU D N   1 
ATOM   7317  C CA  . LEU D  1 115 ? 5.791   29.077 -28.083 1.00 58.60  ? 115 LEU D CA  1 
ATOM   7318  C C   . LEU D  1 115 ? 6.567   27.963 -28.797 1.00 55.47  ? 115 LEU D C   1 
ATOM   7319  O O   . LEU D  1 115 ? 6.086   26.814 -28.790 1.00 52.53  ? 115 LEU D O   1 
ATOM   7320  C CB  . LEU D  1 115 ? 5.084   29.988 -29.091 1.00 62.83  ? 115 LEU D CB  1 
ATOM   7321  C CG  . LEU D  1 115 ? 4.030   29.301 -29.960 1.00 62.30  ? 115 LEU D CG  1 
ATOM   7322  C CD1 . LEU D  1 115 ? 2.990   28.598 -29.103 1.00 61.12  ? 115 LEU D CD1 1 
ATOM   7323  C CD2 . LEU D  1 115 ? 3.358   30.295 -30.895 1.00 66.72  ? 115 LEU D CD2 1 
ATOM   7324  N N   . LEU D  1 116 ? 7.719   28.294 -29.386 1.00 51.94  ? 116 LEU D N   1 
ATOM   7325  C CA  . LEU D  1 116 ? 8.580   27.346 -30.144 1.00 54.08  ? 116 LEU D CA  1 
ATOM   7326  C C   . LEU D  1 116 ? 9.122   26.267 -29.202 1.00 59.36  ? 116 LEU D C   1 
ATOM   7327  O O   . LEU D  1 116 ? 9.396   25.148 -29.683 1.00 60.64  ? 116 LEU D O   1 
ATOM   7328  C CB  . LEU D  1 116 ? 9.727   28.121 -30.798 1.00 58.42  ? 116 LEU D CB  1 
ATOM   7329  C CG  . LEU D  1 116 ? 9.318   29.049 -31.939 1.00 64.36  ? 116 LEU D CG  1 
ATOM   7330  C CD1 . LEU D  1 116 ? 10.537  29.706 -32.564 1.00 67.36  ? 116 LEU D CD1 1 
ATOM   7331  C CD2 . LEU D  1 116 ? 8.521   28.295 -32.992 1.00 63.38  ? 116 LEU D CD2 1 
ATOM   7332  N N   . ALA D  1 117 ? 9.278   26.599 -27.918 1.00 62.40  ? 117 ALA D N   1 
ATOM   7333  C CA  . ALA D  1 117 ? 9.831   25.705 -26.873 1.00 60.18  ? 117 ALA D CA  1 
ATOM   7334  C C   . ALA D  1 117 ? 8.862   24.546 -26.616 1.00 60.60  ? 117 ALA D C   1 
ATOM   7335  O O   . ALA D  1 117 ? 9.343   23.417 -26.397 1.00 64.51  ? 117 ALA D O   1 
ATOM   7336  C CB  . ALA D  1 117 ? 10.100  26.490 -25.615 1.00 57.47  ? 117 ALA D CB  1 
ATOM   7337  N N   . VAL D  1 118 ? 7.554   24.821 -26.643 1.00 60.46  ? 118 VAL D N   1 
ATOM   7338  C CA  . VAL D  1 118 ? 6.475   23.822 -26.374 1.00 62.60  ? 118 VAL D CA  1 
ATOM   7339  C C   . VAL D  1 118 ? 6.107   23.121 -27.686 1.00 64.51  ? 118 VAL D C   1 
ATOM   7340  O O   . VAL D  1 118 ? 5.339   22.144 -27.638 1.00 63.68  ? 118 VAL D O   1 
ATOM   7341  C CB  . VAL D  1 118 ? 5.242   24.474 -25.718 1.00 65.81  ? 118 VAL D CB  1 
ATOM   7342  C CG1 . VAL D  1 118 ? 5.514   24.862 -24.274 1.00 73.32  ? 118 VAL D CG1 1 
ATOM   7343  C CG2 . VAL D  1 118 ? 4.741   25.672 -26.509 1.00 68.42  ? 118 VAL D CG2 1 
ATOM   7344  N N   . CYS D  1 119 ? 6.633   23.611 -28.811 1.00 70.26  ? 119 CYS D N   1 
ATOM   7345  C CA  . CYS D  1 119 ? 6.505   22.976 -30.150 1.00 73.96  ? 119 CYS D CA  1 
ATOM   7346  C C   . CYS D  1 119 ? 7.491   21.806 -30.254 1.00 77.76  ? 119 CYS D C   1 
ATOM   7347  O O   . CYS D  1 119 ? 8.439   21.762 -29.449 1.00 71.82  ? 119 CYS D O   1 
ATOM   7348  C CB  . CYS D  1 119 ? 6.725   23.992 -31.263 1.00 75.35  ? 119 CYS D CB  1 
ATOM   7349  S SG  . CYS D  1 119 ? 5.296   25.077 -31.516 1.00 75.72  ? 119 CYS D SG  1 
ATOM   7350  N N   . ALA D  1 120 ? 7.265   20.897 -31.209 1.00 93.66  ? 120 ALA D N   1 
ATOM   7351  C CA  . ALA D  1 120 ? 7.964   19.595 -31.332 1.00 104.20 ? 120 ALA D CA  1 
ATOM   7352  C C   . ALA D  1 120 ? 9.153   19.706 -32.294 1.00 107.33 ? 120 ALA D C   1 
ATOM   7353  O O   . ALA D  1 120 ? 9.809   18.673 -32.532 1.00 120.68 ? 120 ALA D O   1 
ATOM   7354  C CB  . ALA D  1 120 ? 6.988   18.535 -31.788 1.00 108.31 ? 120 ALA D CB  1 
ATOM   7355  N N   . THR D  1 121 ? 9.418   20.903 -32.829 1.00 106.93 ? 121 THR D N   1 
ATOM   7356  C CA  . THR D  1 121 ? 10.545  21.181 -33.764 1.00 111.77 ? 121 THR D CA  1 
ATOM   7357  C C   . THR D  1 121 ? 11.834  20.581 -33.186 1.00 113.42 ? 121 THR D C   1 
ATOM   7358  O O   . THR D  1 121 ? 12.044  20.719 -31.963 1.00 102.88 ? 121 THR D O   1 
ATOM   7359  C CB  . THR D  1 121 ? 10.677  22.685 -34.034 1.00 108.22 ? 121 THR D CB  1 
ATOM   7360  O OG1 . THR D  1 121 ? 10.788  23.348 -32.774 1.00 122.70 ? 121 THR D OG1 1 
ATOM   7361  C CG2 . THR D  1 121 ? 9.505   23.247 -34.808 1.00 105.35 ? 121 THR D CG2 1 
ATOM   7362  N N   . LEU D  1 122 ? 12.655  19.941 -34.029 1.00 111.52 ? 122 LEU D N   1 
ATOM   7363  C CA  . LEU D  1 122 ? 13.884  19.206 -33.615 1.00 109.00 ? 122 LEU D CA  1 
ATOM   7364  C C   . LEU D  1 122 ? 15.082  19.636 -34.472 1.00 117.04 ? 122 LEU D C   1 
ATOM   7365  O O   . LEU D  1 122 ? 14.893  19.871 -35.681 1.00 121.90 ? 122 LEU D O   1 
ATOM   7366  C CB  . LEU D  1 122 ? 13.643  17.700 -33.763 1.00 103.61 ? 122 LEU D CB  1 
ATOM   7367  C CG  . LEU D  1 122 ? 12.346  17.170 -33.152 1.00 105.32 ? 122 LEU D CG  1 
ATOM   7368  C CD1 . LEU D  1 122 ? 12.135  15.708 -33.513 1.00 97.48  ? 122 LEU D CD1 1 
ATOM   7369  C CD2 . LEU D  1 122 ? 12.339  17.354 -31.643 1.00 108.38 ? 122 LEU D CD2 1 
ATOM   7370  N N   . GLY D  1 123 ? 16.268  19.709 -33.858 1.00 114.36 ? 123 GLY D N   1 
ATOM   7371  C CA  . GLY D  1 123 ? 17.564  19.912 -34.538 1.00 112.78 ? 123 GLY D CA  1 
ATOM   7372  C C   . GLY D  1 123 ? 17.714  21.316 -35.099 1.00 112.47 ? 123 GLY D C   1 
ATOM   7373  O O   . GLY D  1 123 ? 17.582  22.283 -34.320 1.00 103.86 ? 123 GLY D O   1 
ATOM   7374  N N   . VAL D  1 124 ? 17.988  21.420 -36.404 1.00 114.87 ? 124 VAL D N   1 
ATOM   7375  C CA  . VAL D  1 124 ? 18.247  22.704 -37.124 1.00 113.21 ? 124 VAL D CA  1 
ATOM   7376  C C   . VAL D  1 124 ? 16.910  23.406 -37.392 1.00 112.18 ? 124 VAL D C   1 
ATOM   7377  O O   . VAL D  1 124 ? 16.857  24.638 -37.235 1.00 126.66 ? 124 VAL D O   1 
ATOM   7378  C CB  . VAL D  1 124 ? 19.032  22.474 -38.430 1.00 106.09 ? 124 VAL D CB  1 
ATOM   7379  C CG1 . VAL D  1 124 ? 19.155  23.752 -39.245 1.00 109.80 ? 124 VAL D CG1 1 
ATOM   7380  C CG2 . VAL D  1 124 ? 20.405  21.874 -38.165 1.00 96.58  ? 124 VAL D CG2 1 
ATOM   7381  N N   . GLN D  1 125 ? 15.880  22.648 -37.785 1.00 103.96 ? 125 GLN D N   1 
ATOM   7382  C CA  . GLN D  1 125 ? 14.514  23.170 -38.066 1.00 98.57  ? 125 GLN D CA  1 
ATOM   7383  C C   . GLN D  1 125 ? 14.045  24.021 -36.879 1.00 101.97 ? 125 GLN D C   1 
ATOM   7384  O O   . GLN D  1 125 ? 13.387  25.049 -37.120 1.00 106.98 ? 125 GLN D O   1 
ATOM   7385  C CB  . GLN D  1 125 ? 13.542  22.020 -38.339 1.00 79.76  ? 125 GLN D CB  1 
ATOM   7386  N N   . ALA D  1 126 ? 14.382  23.607 -35.653 1.00 102.38 ? 126 ALA D N   1 
ATOM   7387  C CA  . ALA D  1 126 ? 14.027  24.290 -34.385 1.00 91.11  ? 126 ALA D CA  1 
ATOM   7388  C C   . ALA D  1 126 ? 14.857  25.568 -34.229 1.00 87.39  ? 126 ALA D C   1 
ATOM   7389  O O   . ALA D  1 126 ? 14.256  26.656 -34.092 1.00 95.17  ? 126 ALA D O   1 
ATOM   7390  C CB  . ALA D  1 126 ? 14.247  23.358 -33.220 1.00 85.49  ? 126 ALA D CB  1 
ATOM   7391  N N   . ARG D  1 127 ? 16.187  25.428 -34.249 1.00 79.04  ? 127 ARG D N   1 
ATOM   7392  C CA  . ARG D  1 127 ? 17.161  26.535 -34.049 1.00 76.63  ? 127 ARG D CA  1 
ATOM   7393  C C   . ARG D  1 127 ? 16.951  27.605 -35.129 1.00 77.68  ? 127 ARG D C   1 
ATOM   7394  O O   . ARG D  1 127 ? 17.052  28.803 -34.798 1.00 75.69  ? 127 ARG D O   1 
ATOM   7395  C CB  . ARG D  1 127 ? 18.593  25.989 -34.069 1.00 67.79  ? 127 ARG D CB  1 
ATOM   7396  N N   . ARG D  1 128 ? 16.667  27.184 -36.367 1.00 77.20  ? 128 ARG D N   1 
ATOM   7397  C CA  . ARG D  1 128 ? 16.436  28.085 -37.528 1.00 76.40  ? 128 ARG D CA  1 
ATOM   7398  C C   . ARG D  1 128 ? 15.166  28.907 -37.280 1.00 78.50  ? 128 ARG D C   1 
ATOM   7399  O O   . ARG D  1 128 ? 15.233  30.140 -37.419 1.00 85.44  ? 128 ARG D O   1 
ATOM   7400  C CB  . ARG D  1 128 ? 16.320  27.283 -38.829 1.00 69.46  ? 128 ARG D CB  1 
ATOM   7401  N N   . ASN D  1 129 ? 14.063  28.241 -36.924 1.00 79.57  ? 129 ASN D N   1 
ATOM   7402  C CA  . ASN D  1 129 ? 12.745  28.878 -36.653 1.00 88.35  ? 129 ASN D CA  1 
ATOM   7403  C C   . ASN D  1 129 ? 12.926  29.999 -35.626 1.00 82.59  ? 129 ASN D C   1 
ATOM   7404  O O   . ASN D  1 129 ? 12.535  31.145 -35.926 1.00 90.44  ? 129 ASN D O   1 
ATOM   7405  C CB  . ASN D  1 129 ? 11.710  27.861 -36.167 1.00 95.94  ? 129 ASN D CB  1 
ATOM   7406  C CG  . ASN D  1 129 ? 11.257  26.922 -37.263 1.00 107.99 ? 129 ASN D CG  1 
ATOM   7407  O OD1 . ASN D  1 129 ? 11.703  27.032 -38.403 1.00 128.50 ? 129 ASN D OD1 1 
ATOM   7408  N ND2 . ASN D  1 129 ? 10.371  25.998 -36.930 1.00 114.32 ? 129 ASN D ND2 1 
ATOM   7409  N N   . THR D  1 130 ? 13.492  29.670 -34.461 1.00 74.69  ? 130 THR D N   1 
ATOM   7410  C CA  . THR D  1 130 ? 13.746  30.619 -33.345 1.00 74.95  ? 130 THR D CA  1 
ATOM   7411  C C   . THR D  1 130 ? 14.476  31.854 -33.887 1.00 75.19  ? 130 THR D C   1 
ATOM   7412  O O   . THR D  1 130 ? 13.979  32.979 -33.668 1.00 78.14  ? 130 THR D O   1 
ATOM   7413  C CB  . THR D  1 130 ? 14.529  29.941 -32.214 1.00 73.42  ? 130 THR D CB  1 
ATOM   7414  O OG1 . THR D  1 130 ? 13.913  28.682 -31.942 1.00 76.10  ? 130 THR D OG1 1 
ATOM   7415  C CG2 . THR D  1 130 ? 14.573  30.774 -30.952 1.00 76.33  ? 130 THR D CG2 1 
ATOM   7416  N N   . ALA D  1 131 ? 15.601  31.643 -34.579 1.00 63.93  ? 131 ALA D N   1 
ATOM   7417  C CA  . ALA D  1 131 ? 16.480  32.700 -35.132 1.00 57.45  ? 131 ALA D CA  1 
ATOM   7418  C C   . ALA D  1 131 ? 15.662  33.666 -35.998 1.00 62.35  ? 131 ALA D C   1 
ATOM   7419  O O   . ALA D  1 131 ? 15.849  34.890 -35.854 1.00 71.50  ? 131 ALA D O   1 
ATOM   7420  C CB  . ALA D  1 131 ? 17.601  32.071 -35.921 1.00 53.05  ? 131 ALA D CB  1 
ATOM   7421  N N   . ILE D  1 132 ? 14.796  33.130 -36.863 1.00 61.83  ? 132 ILE D N   1 
ATOM   7422  C CA  . ILE D  1 132 ? 13.930  33.913 -37.794 1.00 59.96  ? 132 ILE D CA  1 
ATOM   7423  C C   . ILE D  1 132 ? 12.872  34.659 -36.974 1.00 59.53  ? 132 ILE D C   1 
ATOM   7424  O O   . ILE D  1 132 ? 12.787  35.892 -37.105 1.00 60.34  ? 132 ILE D O   1 
ATOM   7425  C CB  . ILE D  1 132 ? 13.287  32.994 -38.852 1.00 68.26  ? 132 ILE D CB  1 
ATOM   7426  C CG1 . ILE D  1 132 ? 14.346  32.292 -39.707 1.00 72.87  ? 132 ILE D CG1 1 
ATOM   7427  C CG2 . ILE D  1 132 ? 12.291  33.763 -39.708 1.00 69.24  ? 132 ILE D CG2 1 
ATOM   7428  C CD1 . ILE D  1 132 ? 13.778  31.286 -40.681 1.00 75.33  ? 132 ILE D CD1 1 
ATOM   7429  N N   . ALA D  1 133 ? 12.102  33.930 -36.162 1.00 60.36  ? 133 ALA D N   1 
ATOM   7430  C CA  . ALA D  1 133 ? 11.006  34.468 -35.322 1.00 68.81  ? 133 ALA D CA  1 
ATOM   7431  C C   . ALA D  1 133 ? 11.527  35.629 -34.468 1.00 66.65  ? 133 ALA D C   1 
ATOM   7432  O O   . ALA D  1 133 ? 10.861  36.683 -34.436 1.00 73.81  ? 133 ALA D O   1 
ATOM   7433  C CB  . ALA D  1 133 ? 10.431  33.369 -34.467 1.00 76.94  ? 133 ALA D CB  1 
ATOM   7434  N N   . VAL D  1 134 ? 12.671  35.439 -33.804 1.00 62.53  ? 134 VAL D N   1 
ATOM   7435  C CA  . VAL D  1 134 ? 13.298  36.453 -32.904 1.00 68.51  ? 134 VAL D CA  1 
ATOM   7436  C C   . VAL D  1 134 ? 13.638  37.702 -33.727 1.00 67.44  ? 134 VAL D C   1 
ATOM   7437  O O   . VAL D  1 134 ? 13.090  38.777 -33.417 1.00 74.37  ? 134 VAL D O   1 
ATOM   7438  C CB  . VAL D  1 134 ? 14.542  35.887 -32.188 1.00 64.65  ? 134 VAL D CB  1 
ATOM   7439  C CG1 . VAL D  1 134 ? 15.375  36.986 -31.545 1.00 60.48  ? 134 VAL D CG1 1 
ATOM   7440  C CG2 . VAL D  1 134 ? 14.164  34.832 -31.159 1.00 59.86  ? 134 VAL D CG2 1 
ATOM   7441  N N   . THR D  1 135 ? 14.499  37.560 -34.740 1.00 63.32  ? 135 THR D N   1 
ATOM   7442  C CA  . THR D  1 135 ? 14.993  38.680 -35.587 1.00 61.96  ? 135 THR D CA  1 
ATOM   7443  C C   . THR D  1 135 ? 13.806  39.335 -36.305 1.00 58.41  ? 135 THR D C   1 
ATOM   7444  O O   . THR D  1 135 ? 13.809  40.573 -36.439 1.00 55.62  ? 135 THR D O   1 
ATOM   7445  C CB  . THR D  1 135 ? 16.069  38.204 -36.571 1.00 58.05  ? 135 THR D CB  1 
ATOM   7446  O OG1 . THR D  1 135 ? 15.510  37.159 -37.364 1.00 66.81  ? 135 THR D OG1 1 
ATOM   7447  C CG2 . THR D  1 135 ? 17.319  37.702 -35.883 1.00 59.28  ? 135 THR D CG2 1 
ATOM   7448  N N   . ALA D  1 136 ? 12.829  38.533 -36.741 1.00 55.03  ? 136 ALA D N   1 
ATOM   7449  C CA  . ALA D  1 136 ? 11.590  38.998 -37.408 1.00 56.69  ? 136 ALA D CA  1 
ATOM   7450  C C   . ALA D  1 136 ? 10.836  39.949 -36.472 1.00 61.77  ? 136 ALA D C   1 
ATOM   7451  O O   . ALA D  1 136 ? 10.632  41.119 -36.857 1.00 75.40  ? 136 ALA D O   1 
ATOM   7452  C CB  . ALA D  1 136 ? 10.736  37.818 -37.803 1.00 56.69  ? 136 ALA D CB  1 
ATOM   7453  N N   . THR D  1 137 ? 10.447  39.461 -35.288 1.00 58.72  ? 137 THR D N   1 
ATOM   7454  C CA  . THR D  1 137 ? 9.680   40.221 -34.261 1.00 57.76  ? 137 THR D CA  1 
ATOM   7455  C C   . THR D  1 137 ? 10.510  41.418 -33.776 1.00 55.37  ? 137 THR D C   1 
ATOM   7456  O O   . THR D  1 137 ? 9.924   42.501 -33.584 1.00 52.05  ? 137 THR D O   1 
ATOM   7457  C CB  . THR D  1 137 ? 9.257   39.317 -33.096 1.00 57.99  ? 137 THR D CB  1 
ATOM   7458  O OG1 . THR D  1 137 ? 10.395  38.572 -32.663 1.00 66.86  ? 137 THR D OG1 1 
ATOM   7459  C CG2 . THR D  1 137 ? 8.142   38.367 -33.471 1.00 60.66  ? 137 THR D CG2 1 
ATOM   7460  N N   . GLY D  1 138 ? 11.818  41.225 -33.584 1.00 46.82  ? 138 GLY D N   1 
ATOM   7461  C CA  . GLY D  1 138 ? 12.760  42.303 -33.228 1.00 46.02  ? 138 GLY D CA  1 
ATOM   7462  C C   . GLY D  1 138 ? 12.687  43.442 -34.228 1.00 48.55  ? 138 GLY D C   1 
ATOM   7463  O O   . GLY D  1 138 ? 12.439  44.588 -33.803 1.00 48.55  ? 138 GLY D O   1 
ATOM   7464  N N   . ALA D  1 139 ? 12.882  43.130 -35.514 1.00 51.20  ? 139 ALA D N   1 
ATOM   7465  C CA  . ALA D  1 139 ? 12.807  44.073 -36.655 1.00 51.89  ? 139 ALA D CA  1 
ATOM   7466  C C   . ALA D  1 139 ? 11.413  44.709 -36.704 1.00 51.14  ? 139 ALA D C   1 
ATOM   7467  O O   . ALA D  1 139 ? 11.331  45.946 -36.836 1.00 49.93  ? 139 ALA D O   1 
ATOM   7468  C CB  . ALA D  1 139 ? 13.129  43.350 -37.940 1.00 52.94  ? 139 ALA D CB  1 
ATOM   7469  N N   . MET D  1 140 ? 10.365  43.886 -36.598 1.00 50.23  ? 140 MET D N   1 
ATOM   7470  C CA  . MET D  1 140 ? 8.942   44.322 -36.611 1.00 50.61  ? 140 MET D CA  1 
ATOM   7471  C C   . MET D  1 140 ? 8.776   45.539 -35.694 1.00 54.22  ? 140 MET D C   1 
ATOM   7472  O O   . MET D  1 140 ? 8.241   46.567 -36.156 1.00 49.49  ? 140 MET D O   1 
ATOM   7473  C CB  . MET D  1 140 ? 8.020   43.198 -36.131 1.00 50.05  ? 140 MET D CB  1 
ATOM   7474  C CG  . MET D  1 140 ? 6.578   43.636 -35.971 1.00 58.33  ? 140 MET D CG  1 
ATOM   7475  S SD  . MET D  1 140 ? 5.482   42.291 -35.460 1.00 75.99  ? 140 MET D SD  1 
ATOM   7476  C CE  . MET D  1 140 ? 6.084   41.978 -33.802 1.00 76.96  ? 140 MET D CE  1 
ATOM   7477  N N   . ILE D  1 141 ? 9.222   45.416 -34.440 1.00 55.35  ? 141 ILE D N   1 
ATOM   7478  C CA  . ILE D  1 141 ? 9.108   46.475 -33.394 1.00 53.81  ? 141 ILE D CA  1 
ATOM   7479  C C   . ILE D  1 141 ? 10.000  47.658 -33.786 1.00 53.47  ? 141 ILE D C   1 
ATOM   7480  O O   . ILE D  1 141 ? 9.481   48.787 -33.839 1.00 55.10  ? 141 ILE D O   1 
ATOM   7481  C CB  . ILE D  1 141 ? 9.475   45.919 -32.005 1.00 51.42  ? 141 ILE D CB  1 
ATOM   7482  C CG1 . ILE D  1 141 ? 8.604   44.717 -31.631 1.00 50.00  ? 141 ILE D CG1 1 
ATOM   7483  C CG2 . ILE D  1 141 ? 9.404   47.013 -30.951 1.00 50.95  ? 141 ILE D CG2 1 
ATOM   7484  C CD1 . ILE D  1 141 ? 7.125   45.025 -31.585 1.00 48.67  ? 141 ILE D CD1 1 
ATOM   7485  N N   . PHE D  1 142 ? 11.284  47.403 -34.054 1.00 49.09  ? 142 PHE D N   1 
ATOM   7486  C CA  . PHE D  1 142 ? 12.300  48.447 -34.353 1.00 53.19  ? 142 PHE D CA  1 
ATOM   7487  C C   . PHE D  1 142 ? 11.807  49.335 -35.499 1.00 57.99  ? 142 PHE D C   1 
ATOM   7488  O O   . PHE D  1 142 ? 12.095  50.548 -35.482 1.00 60.84  ? 142 PHE D O   1 
ATOM   7489  C CB  . PHE D  1 142 ? 13.658  47.838 -34.705 1.00 54.82  ? 142 PHE D CB  1 
ATOM   7490  C CG  . PHE D  1 142 ? 14.721  48.869 -34.994 1.00 58.75  ? 142 PHE D CG  1 
ATOM   7491  C CD1 . PHE D  1 142 ? 15.243  49.011 -36.269 1.00 61.43  ? 142 PHE D CD1 1 
ATOM   7492  C CD2 . PHE D  1 142 ? 15.173  49.722 -33.998 1.00 60.28  ? 142 PHE D CD2 1 
ATOM   7493  C CE1 . PHE D  1 142 ? 16.212  49.967 -36.535 1.00 64.95  ? 142 PHE D CE1 1 
ATOM   7494  C CE2 . PHE D  1 142 ? 16.136  50.681 -34.267 1.00 59.07  ? 142 PHE D CE2 1 
ATOM   7495  C CZ  . PHE D  1 142 ? 16.657  50.799 -35.534 1.00 63.52  ? 142 PHE D CZ  1 
ATOM   7496  N N   . CYS D  1 143 ? 11.101  48.747 -36.468 1.00 61.93  ? 143 CYS D N   1 
ATOM   7497  C CA  . CYS D  1 143 ? 10.516  49.463 -37.633 1.00 62.78  ? 143 CYS D CA  1 
ATOM   7498  C C   . CYS D  1 143 ? 9.450   50.448 -37.139 1.00 63.45  ? 143 CYS D C   1 
ATOM   7499  O O   . CYS D  1 143 ? 9.598   51.659 -37.401 1.00 65.51  ? 143 CYS D O   1 
ATOM   7500  C CB  . CYS D  1 143 ? 9.932   48.486 -38.647 1.00 63.17  ? 143 CYS D CB  1 
ATOM   7501  S SG  . CYS D  1 143 ? 11.199  47.649 -39.636 1.00 62.07  ? 143 CYS D SG  1 
ATOM   7502  N N   . GLY D  1 144 ? 8.428   49.944 -36.441 1.00 60.54  ? 144 GLY D N   1 
ATOM   7503  C CA  . GLY D  1 144 ? 7.372   50.763 -35.814 1.00 56.82  ? 144 GLY D CA  1 
ATOM   7504  C C   . GLY D  1 144 ? 7.963   51.909 -35.009 1.00 57.56  ? 144 GLY D C   1 
ATOM   7505  O O   . GLY D  1 144 ? 7.370   53.003 -35.019 1.00 58.08  ? 144 GLY D O   1 
ATOM   7506  N N   . PHE D  1 145 ? 9.093   51.666 -34.337 1.00 58.41  ? 145 PHE D N   1 
ATOM   7507  C CA  . PHE D  1 145 ? 9.827   52.658 -33.507 1.00 58.57  ? 145 PHE D CA  1 
ATOM   7508  C C   . PHE D  1 145 ? 10.333  53.797 -34.401 1.00 56.91  ? 145 PHE D C   1 
ATOM   7509  O O   . PHE D  1 145 ? 10.127  54.974 -34.045 1.00 56.52  ? 145 PHE D O   1 
ATOM   7510  C CB  . PHE D  1 145 ? 10.976  51.984 -32.749 1.00 57.37  ? 145 PHE D CB  1 
ATOM   7511  C CG  . PHE D  1 145 ? 11.775  52.909 -31.865 1.00 53.88  ? 145 PHE D CG  1 
ATOM   7512  C CD1 . PHE D  1 145 ? 13.137  53.079 -32.060 1.00 50.90  ? 145 PHE D CD1 1 
ATOM   7513  C CD2 . PHE D  1 145 ? 11.165  53.617 -30.841 1.00 53.51  ? 145 PHE D CD2 1 
ATOM   7514  C CE1 . PHE D  1 145 ? 13.869  53.933 -31.250 1.00 49.75  ? 145 PHE D CE1 1 
ATOM   7515  C CE2 . PHE D  1 145 ? 11.899  54.470 -30.032 1.00 50.33  ? 145 PHE D CE2 1 
ATOM   7516  C CZ  . PHE D  1 145 ? 13.250  54.628 -30.238 1.00 48.07  ? 145 PHE D CZ  1 
ATOM   7517  N N   . LEU D  1 146 ? 10.975  53.454 -35.522 1.00 51.25  ? 146 LEU D N   1 
ATOM   7518  C CA  . LEU D  1 146 ? 11.512  54.429 -36.511 1.00 53.48  ? 146 LEU D CA  1 
ATOM   7519  C C   . LEU D  1 146 ? 10.375  55.332 -37.005 1.00 58.49  ? 146 LEU D C   1 
ATOM   7520  O O   . LEU D  1 146 ? 10.555  56.567 -37.011 1.00 52.97  ? 146 LEU D O   1 
ATOM   7521  C CB  . LEU D  1 146 ? 12.149  53.667 -37.677 1.00 53.26  ? 146 LEU D CB  1 
ATOM   7522  C CG  . LEU D  1 146 ? 13.502  53.023 -37.382 1.00 55.21  ? 146 LEU D CG  1 
ATOM   7523  C CD1 . LEU D  1 146 ? 14.033  52.293 -38.607 1.00 53.96  ? 146 LEU D CD1 1 
ATOM   7524  C CD2 . LEU D  1 146 ? 14.502  54.064 -36.904 1.00 57.93  ? 146 LEU D CD2 1 
ATOM   7525  N N   . GLY D  1 147 ? 9.252   54.728 -37.402 1.00 63.68  ? 147 GLY D N   1 
ATOM   7526  C CA  . GLY D  1 147 ? 8.090   55.433 -37.974 1.00 67.10  ? 147 GLY D CA  1 
ATOM   7527  C C   . GLY D  1 147 ? 7.454   56.394 -36.983 1.00 62.79  ? 147 GLY D C   1 
ATOM   7528  O O   . GLY D  1 147 ? 7.304   57.584 -37.326 1.00 65.40  ? 147 GLY D O   1 
ATOM   7529  N N   . ALA D  1 148 ? 7.106   55.899 -35.792 1.00 57.93  ? 148 ALA D N   1 
ATOM   7530  C CA  . ALA D  1 148 ? 6.227   56.580 -34.812 1.00 59.41  ? 148 ALA D CA  1 
ATOM   7531  C C   . ALA D  1 148 ? 7.023   57.549 -33.930 1.00 63.79  ? 148 ALA D C   1 
ATOM   7532  O O   . ALA D  1 148 ? 6.401   58.490 -33.413 1.00 72.76  ? 148 ALA D O   1 
ATOM   7533  C CB  . ALA D  1 148 ? 5.510   55.550 -33.975 1.00 58.02  ? 148 ALA D CB  1 
ATOM   7534  N N   . ILE D  1 149 ? 8.334   57.334 -33.763 1.00 62.14  ? 149 ILE D N   1 
ATOM   7535  C CA  . ILE D  1 149 ? 9.164   58.030 -32.730 1.00 54.07  ? 149 ILE D CA  1 
ATOM   7536  C C   . ILE D  1 149 ? 10.391  58.691 -33.371 1.00 49.97  ? 149 ILE D C   1 
ATOM   7537  O O   . ILE D  1 149 ? 10.492  59.929 -33.302 1.00 51.77  ? 149 ILE D O   1 
ATOM   7538  C CB  . ILE D  1 149 ? 9.584   57.045 -31.620 1.00 55.19  ? 149 ILE D CB  1 
ATOM   7539  C CG1 . ILE D  1 149 ? 8.377   56.445 -30.893 1.00 52.56  ? 149 ILE D CG1 1 
ATOM   7540  C CG2 . ILE D  1 149 ? 10.548  57.711 -30.652 1.00 58.46  ? 149 ILE D CG2 1 
ATOM   7541  C CD1 . ILE D  1 149 ? 7.707   57.394 -29.932 1.00 51.60  ? 149 ILE D CD1 1 
ATOM   7542  N N   . VAL D  1 150 ? 11.301  57.892 -33.936 1.00 50.09  ? 150 VAL D N   1 
ATOM   7543  C CA  . VAL D  1 150 ? 12.692  58.312 -34.293 1.00 54.38  ? 150 VAL D CA  1 
ATOM   7544  C C   . VAL D  1 150 ? 12.660  59.357 -35.415 1.00 54.89  ? 150 VAL D C   1 
ATOM   7545  O O   . VAL D  1 150 ? 13.228  60.449 -35.217 1.00 53.54  ? 150 VAL D O   1 
ATOM   7546  C CB  . VAL D  1 150 ? 13.562  57.103 -34.691 1.00 52.95  ? 150 VAL D CB  1 
ATOM   7547  C CG1 . VAL D  1 150 ? 14.970  57.528 -35.079 1.00 49.02  ? 150 VAL D CG1 1 
ATOM   7548  C CG2 . VAL D  1 150 ? 13.607  56.055 -33.592 1.00 52.21  ? 150 VAL D CG2 1 
ATOM   7549  N N   . ILE D  1 151 ? 12.038  59.024 -36.550 1.00 63.07  ? 151 ILE D N   1 
ATOM   7550  C CA  . ILE D  1 151 ? 12.071  59.834 -37.806 1.00 64.62  ? 151 ILE D CA  1 
ATOM   7551  C C   . ILE D  1 151 ? 11.226  61.102 -37.624 1.00 64.22  ? 151 ILE D C   1 
ATOM   7552  O O   . ILE D  1 151 ? 9.994   60.981 -37.448 1.00 65.15  ? 151 ILE D O   1 
ATOM   7553  C CB  . ILE D  1 151 ? 11.599  58.994 -39.010 1.00 64.12  ? 151 ILE D CB  1 
ATOM   7554  C CG1 . ILE D  1 151 ? 12.563  57.840 -39.299 1.00 61.08  ? 151 ILE D CG1 1 
ATOM   7555  C CG2 . ILE D  1 151 ? 11.388  59.877 -40.231 1.00 64.78  ? 151 ILE D CG2 1 
ATOM   7556  C CD1 . ILE D  1 151 ? 12.087  56.884 -40.370 1.00 62.67  ? 151 ILE D CD1 1 
ATOM   7557  N N   . ASP D  1 152 ? 11.878  62.269 -37.674 1.00 59.28  ? 152 ASP D N   1 
ATOM   7558  C CA  . ASP D  1 152 ? 11.237  63.610 -37.604 1.00 61.48  ? 152 ASP D CA  1 
ATOM   7559  C C   . ASP D  1 152 ? 10.268  63.647 -36.417 1.00 62.22  ? 152 ASP D C   1 
ATOM   7560  O O   . ASP D  1 152 ? 9.142   64.155 -36.583 1.00 67.39  ? 152 ASP D O   1 
ATOM   7561  C CB  . ASP D  1 152 ? 10.542  63.948 -38.924 1.00 65.52  ? 152 ASP D CB  1 
ATOM   7562  C CG  . ASP D  1 152 ? 11.487  63.980 -40.114 1.00 68.74  ? 152 ASP D CG  1 
ATOM   7563  O OD1 . ASP D  1 152 ? 12.623  64.472 -39.946 1.00 63.57  ? 152 ASP D OD1 1 
ATOM   7564  O OD2 . ASP D  1 152 ? 11.081  63.507 -41.196 1.00 73.12  ? 152 ASP D OD2 1 
ATOM   7565  N N   . ASN D  1 153 ? 10.704  63.119 -35.270 1.00 62.67  ? 153 ASN D N   1 
ATOM   7566  C CA  . ASN D  1 153 ? 9.977   63.163 -33.973 1.00 62.81  ? 153 ASN D CA  1 
ATOM   7567  C C   . ASN D  1 153 ? 8.562   62.604 -34.160 1.00 63.74  ? 153 ASN D C   1 
ATOM   7568  O O   . ASN D  1 153 ? 7.658   63.006 -33.395 1.00 56.30  ? 153 ASN D O   1 
ATOM   7569  C CB  . ASN D  1 153 ? 9.978   64.581 -33.401 1.00 67.05  ? 153 ASN D CB  1 
ATOM   7570  C CG  . ASN D  1 153 ? 11.365  65.190 -33.382 1.00 65.93  ? 153 ASN D CG  1 
ATOM   7571  O OD1 . ASN D  1 153 ? 12.366  64.476 -33.373 1.00 75.62  ? 153 ASN D OD1 1 
ATOM   7572  N ND2 . ASN D  1 153 ? 11.438  66.509 -33.380 1.00 63.95  ? 153 ASN D ND2 1 
ATOM   7573  N N   . GLY D  1 154 ? 8.394   61.709 -35.141 1.00 70.76  ? 154 GLY D N   1 
ATOM   7574  C CA  . GLY D  1 154 ? 7.156   60.943 -35.387 1.00 72.51  ? 154 GLY D CA  1 
ATOM   7575  C C   . GLY D  1 154 ? 6.026   61.824 -35.886 1.00 75.51  ? 154 GLY D C   1 
ATOM   7576  O O   . GLY D  1 154 ? 4.853   61.514 -35.587 1.00 74.83  ? 154 GLY D O   1 
ATOM   7577  N N   . THR D  1 155 ? 6.365   62.885 -36.624 1.00 80.92  ? 155 THR D N   1 
ATOM   7578  C CA  . THR D  1 155 ? 5.396   63.841 -37.224 1.00 80.71  ? 155 THR D CA  1 
ATOM   7579  C C   . THR D  1 155 ? 5.243   63.535 -38.718 1.00 71.26  ? 155 THR D C   1 
ATOM   7580  O O   . THR D  1 155 ? 4.149   63.791 -39.256 1.00 70.58  ? 155 THR D O   1 
ATOM   7581  C CB  . THR D  1 155 ? 5.822   65.292 -36.970 1.00 75.63  ? 155 THR D CB  1 
ATOM   7582  O OG1 . THR D  1 155 ? 7.145   65.463 -37.479 1.00 70.61  ? 155 THR D OG1 1 
ATOM   7583  C CG2 . THR D  1 155 ? 5.779   65.663 -35.504 1.00 76.29  ? 155 THR D CG2 1 
ATOM   7584  N N   . ASN D  1 156 ? 6.297   63.000 -39.344 1.00 60.54  ? 156 ASN D N   1 
ATOM   7585  C CA  . ASN D  1 156 ? 6.349   62.678 -40.796 1.00 60.54  ? 156 ASN D CA  1 
ATOM   7586  C C   . ASN D  1 156 ? 5.369   61.538 -41.098 1.00 57.50  ? 156 ASN D C   1 
ATOM   7587  O O   . ASN D  1 156 ? 5.675   60.385 -40.738 1.00 55.98  ? 156 ASN D O   1 
ATOM   7588  C CB  . ASN D  1 156 ? 7.770   62.323 -41.241 1.00 59.67  ? 156 ASN D CB  1 
ATOM   7589  C CG  . ASN D  1 156 ? 7.848   61.935 -42.702 1.00 63.24  ? 156 ASN D CG  1 
ATOM   7590  O OD1 . ASN D  1 156 ? 6.863   61.484 -43.283 1.00 68.59  ? 156 ASN D OD1 1 
ATOM   7591  N ND2 . ASN D  1 156 ? 9.014   62.102 -43.303 1.00 68.50  ? 156 ASN D ND2 1 
ATOM   7592  N N   . THR D  1 157 ? 4.242   61.855 -41.745 1.00 57.04  ? 157 THR D N   1 
ATOM   7593  C CA  . THR D  1 157 ? 3.147   60.899 -42.069 1.00 56.36  ? 157 THR D CA  1 
ATOM   7594  C C   . THR D  1 157 ? 3.627   59.883 -43.111 1.00 56.18  ? 157 THR D C   1 
ATOM   7595  O O   . THR D  1 157 ? 3.105   58.753 -43.106 1.00 52.71  ? 157 THR D O   1 
ATOM   7596  C CB  . THR D  1 157 ? 1.892   61.625 -42.567 1.00 58.16  ? 157 THR D CB  1 
ATOM   7597  O OG1 . THR D  1 157 ? 1.660   62.753 -41.725 1.00 56.50  ? 157 THR D OG1 1 
ATOM   7598  C CG2 . THR D  1 157 ? 0.674   60.728 -42.580 1.00 59.18  ? 157 THR D CG2 1 
ATOM   7599  N N   . GLY D  1 158 ? 4.572   60.273 -43.972 1.00 56.70  ? 158 GLY D N   1 
ATOM   7600  C CA  . GLY D  1 158 ? 5.185   59.382 -44.975 1.00 55.43  ? 158 GLY D CA  1 
ATOM   7601  C C   . GLY D  1 158 ? 5.857   58.191 -44.314 1.00 60.20  ? 158 GLY D C   1 
ATOM   7602  O O   . GLY D  1 158 ? 5.384   57.053 -44.518 1.00 57.68  ? 158 GLY D O   1 
ATOM   7603  N N   . ALA D  1 159 ? 6.914   58.453 -43.538 1.00 64.87  ? 159 ALA D N   1 
ATOM   7604  C CA  . ALA D  1 159 ? 7.706   57.450 -42.787 1.00 62.96  ? 159 ALA D CA  1 
ATOM   7605  C C   . ALA D  1 159 ? 6.783   56.651 -41.859 1.00 58.28  ? 159 ALA D C   1 
ATOM   7606  O O   . ALA D  1 159 ? 6.906   55.411 -41.821 1.00 57.39  ? 159 ALA D O   1 
ATOM   7607  C CB  . ALA D  1 159 ? 8.798   58.143 -42.012 1.00 63.97  ? 159 ALA D CB  1 
ATOM   7608  N N   . PHE D  1 160 ? 5.898   57.346 -41.139 1.00 51.50  ? 160 PHE D N   1 
ATOM   7609  C CA  . PHE D  1 160 ? 4.915   56.761 -40.190 1.00 57.38  ? 160 PHE D CA  1 
ATOM   7610  C C   . PHE D  1 160 ? 4.204   55.573 -40.848 1.00 58.16  ? 160 PHE D C   1 
ATOM   7611  O O   . PHE D  1 160 ? 4.135   54.497 -40.226 1.00 63.27  ? 160 PHE D O   1 
ATOM   7612  C CB  . PHE D  1 160 ? 3.909   57.824 -39.747 1.00 56.86  ? 160 PHE D CB  1 
ATOM   7613  C CG  . PHE D  1 160 ? 2.978   57.397 -38.642 1.00 57.83  ? 160 PHE D CG  1 
ATOM   7614  C CD1 . PHE D  1 160 ? 1.708   56.920 -38.926 1.00 58.74  ? 160 PHE D CD1 1 
ATOM   7615  C CD2 . PHE D  1 160 ? 3.371   57.480 -37.316 1.00 61.98  ? 160 PHE D CD2 1 
ATOM   7616  C CE1 . PHE D  1 160 ? 0.852   56.535 -37.905 1.00 60.69  ? 160 PHE D CE1 1 
ATOM   7617  C CE2 . PHE D  1 160 ? 2.513   57.097 -36.298 1.00 67.26  ? 160 PHE D CE2 1 
ATOM   7618  C CZ  . PHE D  1 160 ? 1.256   56.625 -36.594 1.00 61.47  ? 160 PHE D CZ  1 
ATOM   7619  N N   . ILE D  1 161 ? 3.695   55.772 -42.068 1.00 54.91  ? 161 ILE D N   1 
ATOM   7620  C CA  . ILE D  1 161 ? 2.917   54.756 -42.839 1.00 55.38  ? 161 ILE D CA  1 
ATOM   7621  C C   . ILE D  1 161 ? 3.893   53.782 -43.507 1.00 52.80  ? 161 ILE D C   1 
ATOM   7622  O O   . ILE D  1 161 ? 3.643   52.561 -43.450 1.00 51.06  ? 161 ILE D O   1 
ATOM   7623  C CB  . ILE D  1 161 ? 1.991   55.439 -43.867 1.00 61.21  ? 161 ILE D CB  1 
ATOM   7624  C CG1 . ILE D  1 161 ? 0.909   56.277 -43.180 1.00 65.46  ? 161 ILE D CG1 1 
ATOM   7625  C CG2 . ILE D  1 161 ? 1.390   54.417 -44.821 1.00 61.66  ? 161 ILE D CG2 1 
ATOM   7626  C CD1 . ILE D  1 161 ? -0.207  56.716 -44.100 1.00 62.08  ? 161 ILE D CD1 1 
ATOM   7627  N N   . LEU D  1 162 ? 4.959   54.306 -44.118 1.00 51.69  ? 162 LEU D N   1 
ATOM   7628  C CA  . LEU D  1 162 ? 5.988   53.501 -44.828 1.00 50.28  ? 162 LEU D CA  1 
ATOM   7629  C C   . LEU D  1 162 ? 6.449   52.359 -43.916 1.00 55.51  ? 162 LEU D C   1 
ATOM   7630  O O   . LEU D  1 162 ? 6.201   51.185 -44.260 1.00 58.24  ? 162 LEU D O   1 
ATOM   7631  C CB  . LEU D  1 162 ? 7.161   54.408 -45.208 1.00 48.62  ? 162 LEU D CB  1 
ATOM   7632  C CG  . LEU D  1 162 ? 8.100   53.857 -46.281 1.00 50.65  ? 162 LEU D CG  1 
ATOM   7633  C CD1 . LEU D  1 162 ? 9.461   54.536 -46.204 1.00 53.71  ? 162 LEU D CD1 1 
ATOM   7634  C CD2 . LEU D  1 162 ? 8.250   52.347 -46.161 1.00 47.76  ? 162 LEU D CD2 1 
ATOM   7635  N N   . TRP D  1 163 ? 7.078   52.704 -42.788 1.00 63.95  ? 163 TRP D N   1 
ATOM   7636  C CA  . TRP D  1 163 ? 7.779   51.761 -41.874 1.00 65.21  ? 163 TRP D CA  1 
ATOM   7637  C C   . TRP D  1 163 ? 6.772   50.840 -41.179 1.00 62.46  ? 163 TRP D C   1 
ATOM   7638  O O   . TRP D  1 163 ? 7.152   49.698 -40.861 1.00 68.30  ? 163 TRP D O   1 
ATOM   7639  C CB  . TRP D  1 163 ? 8.649   52.530 -40.872 1.00 62.08  ? 163 TRP D CB  1 
ATOM   7640  C CG  . TRP D  1 163 ? 9.881   53.106 -41.500 1.00 60.74  ? 163 TRP D CG  1 
ATOM   7641  C CD1 . TRP D  1 163 ? 10.066  54.390 -41.922 1.00 63.42  ? 163 TRP D CD1 1 
ATOM   7642  C CD2 . TRP D  1 163 ? 11.096  52.404 -41.816 1.00 60.01  ? 163 TRP D CD2 1 
ATOM   7643  N NE1 . TRP D  1 163 ? 11.313  54.540 -42.465 1.00 61.91  ? 163 TRP D NE1 1 
ATOM   7644  C CE2 . TRP D  1 163 ? 11.970  53.339 -42.412 1.00 57.97  ? 163 TRP D CE2 1 
ATOM   7645  C CE3 . TRP D  1 163 ? 11.534  51.087 -41.643 1.00 64.07  ? 163 TRP D CE3 1 
ATOM   7646  C CZ2 . TRP D  1 163 ? 13.251  52.993 -42.836 1.00 60.54  ? 163 TRP D CZ2 1 
ATOM   7647  C CZ3 . TRP D  1 163 ? 12.802  50.747 -42.059 1.00 67.14  ? 163 TRP D CZ3 1 
ATOM   7648  C CH2 . TRP D  1 163 ? 13.647  51.688 -42.648 1.00 64.87  ? 163 TRP D CH2 1 
ATOM   7649  N N   . ALA D  1 164 ? 5.543   51.313 -40.956 1.00 57.26  ? 164 ALA D N   1 
ATOM   7650  C CA  . ALA D  1 164 ? 4.418   50.502 -40.434 1.00 57.79  ? 164 ALA D CA  1 
ATOM   7651  C C   . ALA D  1 164 ? 4.178   49.320 -41.381 1.00 59.91  ? 164 ALA D C   1 
ATOM   7652  O O   . ALA D  1 164 ? 3.876   48.215 -40.888 1.00 55.02  ? 164 ALA D O   1 
ATOM   7653  C CB  . ALA D  1 164 ? 3.183   51.355 -40.282 1.00 54.75  ? 164 ALA D CB  1 
ATOM   7654  N N   . VAL D  1 165 ? 4.323   49.553 -42.690 1.00 62.51  ? 165 VAL D N   1 
ATOM   7655  C CA  . VAL D  1 165 ? 4.144   48.530 -43.764 1.00 61.45  ? 165 VAL D CA  1 
ATOM   7656  C C   . VAL D  1 165 ? 5.342   47.574 -43.729 1.00 59.73  ? 165 VAL D C   1 
ATOM   7657  O O   . VAL D  1 165 ? 5.121   46.347 -43.650 1.00 58.55  ? 165 VAL D O   1 
ATOM   7658  C CB  . VAL D  1 165 ? 3.985   49.187 -45.148 1.00 58.09  ? 165 VAL D CB  1 
ATOM   7659  C CG1 . VAL D  1 165 ? 4.133   48.178 -46.277 1.00 57.00  ? 165 VAL D CG1 1 
ATOM   7660  C CG2 . VAL D  1 165 ? 2.666   49.935 -45.265 1.00 53.55  ? 165 VAL D CG2 1 
ATOM   7661  N N   . ILE D  1 166 ? 6.560   48.122 -43.786 1.00 52.50  ? 166 ILE D N   1 
ATOM   7662  C CA  . ILE D  1 166 ? 7.829   47.348 -43.653 1.00 53.06  ? 166 ILE D CA  1 
ATOM   7663  C C   . ILE D  1 166 ? 7.709   46.462 -42.409 1.00 51.96  ? 166 ILE D C   1 
ATOM   7664  O O   . ILE D  1 166 ? 8.054   45.271 -42.496 1.00 58.77  ? 166 ILE D O   1 
ATOM   7665  C CB  . ILE D  1 166 ? 9.052   48.281 -43.573 1.00 54.38  ? 166 ILE D CB  1 
ATOM   7666  C CG1 . ILE D  1 166 ? 9.175   49.164 -44.818 1.00 56.20  ? 166 ILE D CG1 1 
ATOM   7667  C CG2 . ILE D  1 166 ? 10.319  47.476 -43.323 1.00 52.76  ? 166 ILE D CG2 1 
ATOM   7668  C CD1 . ILE D  1 166 ? 10.425  50.014 -44.849 1.00 57.28  ? 166 ILE D CD1 1 
ATOM   7669  N N   . SER D  1 167 ? 7.233   47.037 -41.301 1.00 52.00  ? 167 SER D N   1 
ATOM   7670  C CA  . SER D  1 167 ? 6.957   46.330 -40.023 1.00 58.71  ? 167 SER D CA  1 
ATOM   7671  C C   . SER D  1 167 ? 6.043   45.128 -40.290 1.00 64.18  ? 167 SER D C   1 
ATOM   7672  O O   . SER D  1 167 ? 6.435   43.999 -39.932 1.00 65.41  ? 167 SER D O   1 
ATOM   7673  C CB  . SER D  1 167 ? 6.358   47.268 -39.004 1.00 59.38  ? 167 SER D CB  1 
ATOM   7674  O OG  . SER D  1 167 ? 5.978   46.572 -37.825 1.00 57.70  ? 167 SER D OG  1 
ATOM   7675  N N   . CYS D  1 168 ? 4.881   45.366 -40.908 1.00 62.10  ? 168 CYS D N   1 
ATOM   7676  C CA  . CYS D  1 168 ? 3.838   44.343 -41.193 1.00 59.79  ? 168 CYS D CA  1 
ATOM   7677  C C   . CYS D  1 168 ? 4.434   43.186 -42.001 1.00 56.93  ? 168 CYS D C   1 
ATOM   7678  O O   . CYS D  1 168 ? 3.988   42.040 -41.799 1.00 54.94  ? 168 CYS D O   1 
ATOM   7679  C CB  . CYS D  1 168 ? 2.660   44.946 -41.945 1.00 59.41  ? 168 CYS D CB  1 
ATOM   7680  S SG  . CYS D  1 168 ? 1.647   46.032 -40.909 1.00 68.46  ? 168 CYS D SG  1 
ATOM   7681  N N   . VAL D  1 169 ? 5.388   43.479 -42.889 1.00 51.32  ? 169 VAL D N   1 
ATOM   7682  C CA  . VAL D  1 169 ? 6.150   42.448 -43.654 1.00 57.45  ? 169 VAL D CA  1 
ATOM   7683  C C   . VAL D  1 169 ? 6.728   41.453 -42.644 1.00 57.77  ? 169 VAL D C   1 
ATOM   7684  O O   . VAL D  1 169 ? 6.362   40.264 -42.700 1.00 59.33  ? 169 VAL D O   1 
ATOM   7685  C CB  . VAL D  1 169 ? 7.258   43.081 -44.519 1.00 64.29  ? 169 VAL D CB  1 
ATOM   7686  C CG1 . VAL D  1 169 ? 8.269   42.047 -44.998 1.00 61.18  ? 169 VAL D CG1 1 
ATOM   7687  C CG2 . VAL D  1 169 ? 6.680   43.854 -45.694 1.00 65.38  ? 169 VAL D CG2 1 
ATOM   7688  N N   . PHE D  1 170 ? 7.585   41.941 -41.745 1.00 57.78  ? 170 PHE D N   1 
ATOM   7689  C CA  . PHE D  1 170 ? 8.237   41.148 -40.672 1.00 60.68  ? 170 PHE D CA  1 
ATOM   7690  C C   . PHE D  1 170 ? 7.163   40.448 -39.831 1.00 58.59  ? 170 PHE D C   1 
ATOM   7691  O O   . PHE D  1 170 ? 7.347   39.263 -39.490 1.00 68.18  ? 170 PHE D O   1 
ATOM   7692  C CB  . PHE D  1 170 ? 9.133   42.047 -39.817 1.00 60.65  ? 170 PHE D CB  1 
ATOM   7693  C CG  . PHE D  1 170 ? 10.373  42.546 -40.514 1.00 54.03  ? 170 PHE D CG  1 
ATOM   7694  C CD1 . PHE D  1 170 ? 11.386  41.671 -40.871 1.00 55.01  ? 170 PHE D CD1 1 
ATOM   7695  C CD2 . PHE D  1 170 ? 10.532  43.892 -40.802 1.00 54.16  ? 170 PHE D CD2 1 
ATOM   7696  C CE1 . PHE D  1 170 ? 12.527  42.131 -41.509 1.00 57.12  ? 170 PHE D CE1 1 
ATOM   7697  C CE2 . PHE D  1 170 ? 11.675  44.350 -41.437 1.00 56.35  ? 170 PHE D CE2 1 
ATOM   7698  C CZ  . PHE D  1 170 ? 12.670  43.470 -41.790 1.00 58.30  ? 170 PHE D CZ  1 
ATOM   7699  N N   . TRP D  1 171 ? 6.075   41.156 -39.516 1.00 50.37  ? 171 TRP D N   1 
ATOM   7700  C CA  . TRP D  1 171 ? 4.928   40.625 -38.730 1.00 53.28  ? 171 TRP D CA  1 
ATOM   7701  C C   . TRP D  1 171 ? 4.457   39.302 -39.345 1.00 58.38  ? 171 TRP D C   1 
ATOM   7702  O O   . TRP D  1 171 ? 4.368   38.301 -38.608 1.00 55.51  ? 171 TRP D O   1 
ATOM   7703  C CB  . TRP D  1 171 ? 3.791   41.652 -38.660 1.00 57.24  ? 171 TRP D CB  1 
ATOM   7704  C CG  . TRP D  1 171 ? 2.621   41.208 -37.836 1.00 59.94  ? 171 TRP D CG  1 
ATOM   7705  C CD1 . TRP D  1 171 ? 2.652   40.394 -36.742 1.00 64.15  ? 171 TRP D CD1 1 
ATOM   7706  C CD2 . TRP D  1 171 ? 1.242   41.576 -38.020 1.00 70.09  ? 171 TRP D CD2 1 
ATOM   7707  N NE1 . TRP D  1 171 ? 1.389   40.215 -36.245 1.00 71.66  ? 171 TRP D NE1 1 
ATOM   7708  C CE2 . TRP D  1 171 ? 0.504   40.931 -37.004 1.00 71.15  ? 171 TRP D CE2 1 
ATOM   7709  C CE3 . TRP D  1 171 ? 0.559   42.382 -38.938 1.00 69.71  ? 171 TRP D CE3 1 
ATOM   7710  C CZ2 . TRP D  1 171 ? -0.879  41.067 -36.886 1.00 67.19  ? 171 TRP D CZ2 1 
ATOM   7711  C CZ3 . TRP D  1 171 ? -0.807  42.517 -38.819 1.00 67.15  ? 171 TRP D CZ3 1 
ATOM   7712  C CH2 . TRP D  1 171 ? -1.514  41.867 -37.806 1.00 64.62  ? 171 TRP D CH2 1 
ATOM   7713  N N   . VAL D  1 172 ? 4.172   39.308 -40.649 1.00 70.49  ? 172 VAL D N   1 
ATOM   7714  C CA  . VAL D  1 172 ? 3.664   38.126 -41.407 1.00 67.35  ? 172 VAL D CA  1 
ATOM   7715  C C   . VAL D  1 172 ? 4.712   37.011 -41.332 1.00 65.85  ? 172 VAL D C   1 
ATOM   7716  O O   . VAL D  1 172 ? 4.341   35.883 -40.957 1.00 65.14  ? 172 VAL D O   1 
ATOM   7717  C CB  . VAL D  1 172 ? 3.326   38.497 -42.864 1.00 61.62  ? 172 VAL D CB  1 
ATOM   7718  C CG1 . VAL D  1 172 ? 3.027   37.265 -43.705 1.00 61.03  ? 172 VAL D CG1 1 
ATOM   7719  C CG2 . VAL D  1 172 ? 2.175   39.490 -42.931 1.00 53.35  ? 172 VAL D CG2 1 
ATOM   7720  N N   . ILE D  1 173 ? 5.969   37.321 -41.666 1.00 60.13  ? 173 ILE D N   1 
ATOM   7721  C CA  . ILE D  1 173 ? 7.112   36.359 -41.611 1.00 66.46  ? 173 ILE D CA  1 
ATOM   7722  C C   . ILE D  1 173 ? 7.029   35.586 -40.291 1.00 67.83  ? 173 ILE D C   1 
ATOM   7723  O O   . ILE D  1 173 ? 7.129   34.345 -40.326 1.00 71.61  ? 173 ILE D O   1 
ATOM   7724  C CB  . ILE D  1 173 ? 8.464   37.085 -41.766 1.00 67.02  ? 173 ILE D CB  1 
ATOM   7725  C CG1 . ILE D  1 173 ? 8.567   37.810 -43.111 1.00 72.62  ? 173 ILE D CG1 1 
ATOM   7726  C CG2 . ILE D  1 173 ? 9.620   36.119 -41.554 1.00 62.65  ? 173 ILE D CG2 1 
ATOM   7727  C CD1 . ILE D  1 173 ? 9.846   38.594 -43.295 1.00 72.12  ? 173 ILE D CD1 1 
ATOM   7728  N N   . ALA D  1 174 ? 6.845   36.302 -39.178 1.00 70.99  ? 174 ALA D N   1 
ATOM   7729  C CA  . ALA D  1 174 ? 6.735   35.742 -37.811 1.00 69.60  ? 174 ALA D CA  1 
ATOM   7730  C C   . ALA D  1 174 ? 5.527   34.801 -37.738 1.00 61.30  ? 174 ALA D C   1 
ATOM   7731  O O   . ALA D  1 174 ? 5.728   33.605 -37.441 1.00 62.28  ? 174 ALA D O   1 
ATOM   7732  C CB  . ALA D  1 174 ? 6.624   36.860 -36.805 1.00 68.85  ? 174 ALA D CB  1 
ATOM   7733  N N   . ASN D  1 175 ? 4.327   35.331 -37.999 1.00 53.79  ? 175 ASN D N   1 
ATOM   7734  C CA  . ASN D  1 175 ? 3.046   34.575 -37.978 1.00 58.02  ? 175 ASN D CA  1 
ATOM   7735  C C   . ASN D  1 175 ? 3.234   33.249 -38.724 1.00 59.64  ? 175 ASN D C   1 
ATOM   7736  O O   . ASN D  1 175 ? 2.887   32.193 -38.158 1.00 59.10  ? 175 ASN D O   1 
ATOM   7737  C CB  . ASN D  1 175 ? 1.899   35.386 -38.586 1.00 58.91  ? 175 ASN D CB  1 
ATOM   7738  C CG  . ASN D  1 175 ? 1.352   36.435 -37.642 1.00 63.20  ? 175 ASN D CG  1 
ATOM   7739  O OD1 . ASN D  1 175 ? 1.627   37.623 -37.796 1.00 78.64  ? 175 ASN D OD1 1 
ATOM   7740  N ND2 . ASN D  1 175 ? 0.580   36.004 -36.659 1.00 59.31  ? 175 ASN D ND2 1 
ATOM   7741  N N   . VAL D  1 176 ? 3.765   33.316 -39.948 1.00 60.16  ? 176 VAL D N   1 
ATOM   7742  C CA  . VAL D  1 176 ? 4.032   32.135 -40.821 1.00 62.52  ? 176 VAL D CA  1 
ATOM   7743  C C   . VAL D  1 176 ? 4.889   31.133 -40.041 1.00 59.38  ? 176 VAL D C   1 
ATOM   7744  O O   . VAL D  1 176 ? 4.381   30.038 -39.746 1.00 57.20  ? 176 VAL D O   1 
ATOM   7745  C CB  . VAL D  1 176 ? 4.709   32.555 -42.140 1.00 65.38  ? 176 VAL D CB  1 
ATOM   7746  C CG1 . VAL D  1 176 ? 5.336   31.370 -42.860 1.00 62.08  ? 176 VAL D CG1 1 
ATOM   7747  C CG2 . VAL D  1 176 ? 3.740   33.289 -43.054 1.00 66.51  ? 176 VAL D CG2 1 
ATOM   7748  N N   . VAL D  1 177 ? 6.130   31.509 -39.715 1.00 60.84  ? 177 VAL D N   1 
ATOM   7749  C CA  . VAL D  1 177 ? 7.133   30.641 -39.028 1.00 62.95  ? 177 VAL D CA  1 
ATOM   7750  C C   . VAL D  1 177 ? 6.462   29.933 -37.846 1.00 65.95  ? 177 VAL D C   1 
ATOM   7751  O O   . VAL D  1 177 ? 6.620   28.701 -37.737 1.00 60.12  ? 177 VAL D O   1 
ATOM   7752  C CB  . VAL D  1 177 ? 8.361   31.448 -38.563 1.00 72.11  ? 177 VAL D CB  1 
ATOM   7753  C CG1 . VAL D  1 177 ? 9.312   30.595 -37.734 1.00 76.59  ? 177 VAL D CG1 1 
ATOM   7754  C CG2 . VAL D  1 177 ? 9.096   32.085 -39.731 1.00 76.83  ? 177 VAL D CG2 1 
ATOM   7755  N N   . LEU D  1 178 ? 5.751   30.685 -36.999 1.00 70.72  ? 178 LEU D N   1 
ATOM   7756  C CA  . LEU D  1 178 ? 5.099   30.173 -35.761 1.00 64.56  ? 178 LEU D CA  1 
ATOM   7757  C C   . LEU D  1 178 ? 3.965   29.213 -36.138 1.00 64.87  ? 178 LEU D C   1 
ATOM   7758  O O   . LEU D  1 178 ? 3.972   28.072 -35.641 1.00 69.56  ? 178 LEU D O   1 
ATOM   7759  C CB  . LEU D  1 178 ? 4.570   31.350 -34.937 1.00 62.77  ? 178 LEU D CB  1 
ATOM   7760  C CG  . LEU D  1 178 ? 5.638   32.226 -34.283 1.00 65.29  ? 178 LEU D CG  1 
ATOM   7761  C CD1 . LEU D  1 178 ? 5.008   33.421 -33.587 1.00 66.91  ? 178 LEU D CD1 1 
ATOM   7762  C CD2 . LEU D  1 178 ? 6.478   31.422 -33.304 1.00 62.93  ? 178 LEU D CD2 1 
ATOM   7763  N N   . ILE D  1 179 ? 3.036   29.665 -36.984 1.00 65.03  ? 179 ILE D N   1 
ATOM   7764  C CA  . ILE D  1 179 ? 1.845   28.881 -37.432 1.00 62.93  ? 179 ILE D CA  1 
ATOM   7765  C C   . ILE D  1 179 ? 2.321   27.563 -38.053 1.00 63.31  ? 179 ILE D C   1 
ATOM   7766  O O   . ILE D  1 179 ? 1.768   26.506 -37.690 1.00 64.55  ? 179 ILE D O   1 
ATOM   7767  C CB  . ILE D  1 179 ? 0.984   29.703 -38.411 1.00 62.32  ? 179 ILE D CB  1 
ATOM   7768  C CG1 . ILE D  1 179 ? 0.258   30.845 -37.695 1.00 63.35  ? 179 ILE D CG1 1 
ATOM   7769  C CG2 . ILE D  1 179 ? 0.014   28.802 -39.160 1.00 62.37  ? 179 ILE D CG2 1 
ATOM   7770  C CD1 . ILE D  1 179 ? -0.350  31.870 -38.623 1.00 63.01  ? 179 ILE D CD1 1 
ATOM   7771  N N   . ARG D  1 180 ? 3.305   27.626 -38.956 1.00 58.33  ? 180 ARG D N   1 
ATOM   7772  C CA  . ARG D  1 180 ? 3.911   26.438 -39.615 1.00 65.35  ? 180 ARG D CA  1 
ATOM   7773  C C   . ARG D  1 180 ? 4.396   25.467 -38.532 1.00 74.33  ? 180 ARG D C   1 
ATOM   7774  O O   . ARG D  1 180 ? 3.953   24.299 -38.539 1.00 69.82  ? 180 ARG D O   1 
ATOM   7775  C CB  . ARG D  1 180 ? 5.062   26.853 -40.537 1.00 59.27  ? 180 ARG D CB  1 
ATOM   7776  N N   . ALA D  1 181 ? 5.260   25.950 -37.632 1.00 78.78  ? 181 ALA D N   1 
ATOM   7777  C CA  . ALA D  1 181 ? 5.909   25.169 -36.552 1.00 79.00  ? 181 ALA D CA  1 
ATOM   7778  C C   . ALA D  1 181 ? 4.849   24.528 -35.649 1.00 73.61  ? 181 ALA D C   1 
ATOM   7779  O O   . ALA D  1 181 ? 5.093   23.404 -35.176 1.00 74.69  ? 181 ALA D O   1 
ATOM   7780  C CB  . ALA D  1 181 ? 6.839   26.059 -35.764 1.00 81.16  ? 181 ALA D CB  1 
ATOM   7781  N N   . VAL D  1 182 ? 3.726   25.218 -35.417 1.00 66.35  ? 182 VAL D N   1 
ATOM   7782  C CA  . VAL D  1 182 ? 2.594   24.730 -34.572 1.00 75.32  ? 182 VAL D CA  1 
ATOM   7783  C C   . VAL D  1 182 ? 1.851   23.632 -35.339 1.00 88.75  ? 182 VAL D C   1 
ATOM   7784  O O   . VAL D  1 182 ? 1.658   22.541 -34.768 1.00 89.22  ? 182 VAL D O   1 
ATOM   7785  C CB  . VAL D  1 182 ? 1.636   25.871 -34.177 1.00 81.33  ? 182 VAL D CB  1 
ATOM   7786  C CG1 . VAL D  1 182 ? 0.378   25.348 -33.496 1.00 73.69  ? 182 VAL D CG1 1 
ATOM   7787  C CG2 . VAL D  1 182 ? 2.323   26.909 -33.305 1.00 95.46  ? 182 VAL D CG2 1 
ATOM   7788  N N   . ARG D  1 183 ? 1.453   23.921 -36.581 1.00 107.19 ? 183 ARG D N   1 
ATOM   7789  C CA  . ARG D  1 183 ? 0.650   23.008 -37.436 1.00 103.22 ? 183 ARG D CA  1 
ATOM   7790  C C   . ARG D  1 183 ? 1.406   21.688 -37.636 1.00 101.43 ? 183 ARG D C   1 
ATOM   7791  O O   . ARG D  1 183 ? 0.736   20.654 -37.819 1.00 109.28 ? 183 ARG D O   1 
ATOM   7792  C CB  . ARG D  1 183 ? 0.324   23.670 -38.778 1.00 97.88  ? 183 ARG D CB  1 
ATOM   7793  C CG  . ARG D  1 183 ? -0.864  23.042 -39.492 1.00 90.26  ? 183 ARG D CG  1 
ATOM   7794  N N   . GLN D  1 184 ? 2.743   21.723 -37.595 1.00 83.32  ? 184 GLN D N   1 
ATOM   7795  C CA  . GLN D  1 184 ? 3.621   20.532 -37.761 1.00 80.39  ? 184 GLN D CA  1 
ATOM   7796  C C   . GLN D  1 184 ? 3.623   19.701 -36.474 1.00 84.43  ? 184 GLN D C   1 
ATOM   7797  O O   . GLN D  1 184 ? 3.705   18.461 -36.575 1.00 94.49  ? 184 GLN D O   1 
ATOM   7798  C CB  . GLN D  1 184 ? 5.051   20.953 -38.101 1.00 79.84  ? 184 GLN D CB  1 
ATOM   7799  C CG  . GLN D  1 184 ? 5.181   21.624 -39.458 1.00 93.02  ? 184 GLN D CG  1 
ATOM   7800  C CD  . GLN D  1 184 ? 6.609   22.006 -39.756 1.00 113.75 ? 184 GLN D CD  1 
ATOM   7801  O OE1 . GLN D  1 184 ? 7.539   21.584 -39.070 1.00 118.71 ? 184 GLN D OE1 1 
ATOM   7802  N NE2 . GLN D  1 184 ? 6.796   22.807 -40.792 1.00 129.26 ? 184 GLN D NE2 1 
ATOM   7803  N N   . SER D  1 185 ? 3.552   20.363 -35.315 1.00 94.90  ? 185 SER D N   1 
ATOM   7804  C CA  . SER D  1 185 ? 3.618   19.731 -33.970 1.00 99.07  ? 185 SER D CA  1 
ATOM   7805  C C   . SER D  1 185 ? 2.300   19.012 -33.663 1.00 105.18 ? 185 SER D C   1 
ATOM   7806  O O   . SER D  1 185 ? 2.358   17.866 -33.182 1.00 120.33 ? 185 SER D O   1 
ATOM   7807  C CB  . SER D  1 185 ? 3.950   20.746 -32.905 1.00 92.92  ? 185 SER D CB  1 
ATOM   7808  O OG  . SER D  1 185 ? 5.229   21.317 -33.132 1.00 105.29 ? 185 SER D OG  1 
ATOM   7809  N N   . LEU D  1 186 ? 1.166   19.661 -33.951 1.00 106.97 ? 186 LEU D N   1 
ATOM   7810  C CA  . LEU D  1 186 ? -0.203  19.215 -33.566 1.00 115.72 ? 186 LEU D CA  1 
ATOM   7811  C C   . LEU D  1 186 ? -0.416  17.748 -33.943 1.00 120.89 ? 186 LEU D C   1 
ATOM   7812  O O   . LEU D  1 186 ? -1.004  16.993 -33.173 1.00 118.58 ? 186 LEU D O   1 
ATOM   7813  C CB  . LEU D  1 186 ? -1.233  20.126 -34.244 1.00 118.59 ? 186 LEU D CB  1 
ATOM   7814  C CG  . LEU D  1 186 ? -1.263  21.570 -33.743 1.00 117.92 ? 186 LEU D CG  1 
ATOM   7815  C CD1 . LEU D  1 186 ? -2.269  22.403 -34.523 1.00 121.95 ? 186 LEU D CD1 1 
ATOM   7816  C CD2 . LEU D  1 186 ? -1.570  21.625 -32.256 1.00 117.56 ? 186 LEU D CD2 1 
ATOM   7817  N N   . PRO D  1 187 ? 0.027   17.297 -35.139 1.00 122.06 ? 187 PRO D N   1 
ATOM   7818  C CA  . PRO D  1 187 ? -0.091  15.890 -35.526 1.00 114.85 ? 187 PRO D CA  1 
ATOM   7819  C C   . PRO D  1 187 ? 0.608   14.911 -34.569 1.00 109.29 ? 187 PRO D C   1 
ATOM   7820  O O   . PRO D  1 187 ? 0.016   13.892 -34.264 1.00 102.44 ? 187 PRO D O   1 
ATOM   7821  C CB  . PRO D  1 187 ? 0.585   15.831 -36.905 1.00 117.68 ? 187 PRO D CB  1 
ATOM   7822  C CG  . PRO D  1 187 ? 0.480   17.246 -37.432 1.00 118.91 ? 187 PRO D CG  1 
ATOM   7823  C CD  . PRO D  1 187 ? 0.614   18.123 -36.204 1.00 125.67 ? 187 PRO D CD  1 
ATOM   7824  N N   . THR D  1 188 ? 1.828   15.236 -34.123 1.00 109.19 ? 188 THR D N   1 
ATOM   7825  C CA  . THR D  1 188 ? 2.703   14.340 -33.313 1.00 103.45 ? 188 THR D CA  1 
ATOM   7826  C C   . THR D  1 188 ? 2.287   14.374 -31.837 1.00 94.77  ? 188 THR D C   1 
ATOM   7827  O O   . THR D  1 188 ? 2.763   13.510 -31.077 1.00 86.78  ? 188 THR D O   1 
ATOM   7828  C CB  . THR D  1 188 ? 4.188   14.707 -33.452 1.00 104.70 ? 188 THR D CB  1 
ATOM   7829  O OG1 . THR D  1 188 ? 4.421   15.953 -32.794 1.00 102.79 ? 188 THR D OG1 1 
ATOM   7830  C CG2 . THR D  1 188 ? 4.642   14.797 -34.892 1.00 103.51 ? 188 THR D CG2 1 
ATOM   7831  N N   . LEU D  1 189 ? 1.441   15.334 -31.449 1.00 98.44  ? 189 LEU D N   1 
ATOM   7832  C CA  . LEU D  1 189 ? 0.973   15.523 -30.048 1.00 96.55  ? 189 LEU D CA  1 
ATOM   7833  C C   . LEU D  1 189 ? -0.298  14.699 -29.824 1.00 87.46  ? 189 LEU D C   1 
ATOM   7834  O O   . LEU D  1 189 ? -0.876  14.218 -30.815 1.00 85.64  ? 189 LEU D O   1 
ATOM   7835  C CB  . LEU D  1 189 ? 0.706   17.010 -29.790 1.00 103.16 ? 189 LEU D CB  1 
ATOM   7836  C CG  . LEU D  1 189 ? 1.918   17.934 -29.900 1.00 103.49 ? 189 LEU D CG  1 
ATOM   7837  C CD1 . LEU D  1 189 ? 1.557   19.353 -29.488 1.00 100.90 ? 189 LEU D CD1 1 
ATOM   7838  C CD2 . LEU D  1 189 ? 3.080   17.418 -29.065 1.00 107.92 ? 189 LEU D CD2 1 
ATOM   7839  N N   . THR D  1 190 ? -0.712  14.554 -28.564 1.00 91.27  ? 190 THR D N   1 
ATOM   7840  C CA  . THR D  1 190 ? -1.975  13.882 -28.161 1.00 92.84  ? 190 THR D CA  1 
ATOM   7841  C C   . THR D  1 190 ? -3.142  14.830 -28.416 1.00 88.86  ? 190 THR D C   1 
ATOM   7842  O O   . THR D  1 190 ? -2.938  15.986 -28.778 1.00 74.58  ? 190 THR D O   1 
ATOM   7843  C CB  . THR D  1 190 ? -1.924  13.444 -26.692 1.00 93.01  ? 190 THR D CB  1 
ATOM   7844  O OG1 . THR D  1 190 ? -2.082  14.613 -25.886 1.00 89.55  ? 190 THR D OG1 1 
ATOM   7845  C CG2 . THR D  1 190 ? -0.638  12.729 -26.339 1.00 88.80  ? 190 THR D CG2 1 
ATOM   7846  N N   . PRO D  1 191 ? -4.400  14.363 -28.248 1.00 99.15  ? 191 PRO D N   1 
ATOM   7847  C CA  . PRO D  1 191 ? -5.572  15.230 -28.379 1.00 103.83 ? 191 PRO D CA  1 
ATOM   7848  C C   . PRO D  1 191 ? -5.562  16.394 -27.377 1.00 103.71 ? 191 PRO D C   1 
ATOM   7849  O O   . PRO D  1 191 ? -5.844  17.509 -27.782 1.00 108.38 ? 191 PRO D O   1 
ATOM   7850  C CB  . PRO D  1 191 ? -6.758  14.294 -28.092 1.00 94.26  ? 191 PRO D CB  1 
ATOM   7851  C CG  . PRO D  1 191 ? -6.220  12.908 -28.373 1.00 95.83  ? 191 PRO D CG  1 
ATOM   7852  C CD  . PRO D  1 191 ? -4.764  12.969 -27.959 1.00 99.12  ? 191 PRO D CD  1 
ATOM   7853  N N   . GLU D  1 192 ? -5.243  16.105 -26.111 1.00 93.44  ? 192 GLU D N   1 
ATOM   7854  C CA  . GLU D  1 192 ? -5.266  17.079 -24.984 1.00 91.43  ? 192 GLU D CA  1 
ATOM   7855  C C   . GLU D  1 192 ? -4.203  18.162 -25.216 1.00 98.23  ? 192 GLU D C   1 
ATOM   7856  O O   . GLU D  1 192 ? -4.535  19.354 -25.044 1.00 85.82  ? 192 GLU D O   1 
ATOM   7857  C CB  . GLU D  1 192 ? -5.046  16.359 -23.651 1.00 84.73  ? 192 GLU D CB  1 
ATOM   7858  N N   . SER D  1 193 ? -2.979  17.763 -25.585 1.00 100.86 ? 193 SER D N   1 
ATOM   7859  C CA  . SER D  1 193 ? -1.846  18.674 -25.902 1.00 88.66  ? 193 SER D CA  1 
ATOM   7860  C C   . SER D  1 193 ? -2.191  19.506 -27.141 1.00 89.66  ? 193 SER D C   1 
ATOM   7861  O O   . SER D  1 193 ? -2.100  20.746 -27.071 1.00 90.24  ? 193 SER D O   1 
ATOM   7862  C CB  . SER D  1 193 ? -0.564  17.910 -26.110 1.00 79.93  ? 193 SER D CB  1 
ATOM   7863  O OG  . SER D  1 193 ? -0.155  17.270 -24.913 1.00 78.19  ? 193 SER D OG  1 
ATOM   7864  N N   . HIS D  1 194 ? -2.559  18.827 -28.231 1.00 102.33 ? 194 HIS D N   1 
ATOM   7865  C CA  . HIS D  1 194 ? -3.005  19.422 -29.519 1.00 106.77 ? 194 HIS D CA  1 
ATOM   7866  C C   . HIS D  1 194 ? -3.869  20.660 -29.248 1.00 95.05  ? 194 HIS D C   1 
ATOM   7867  O O   . HIS D  1 194 ? -3.527  21.744 -29.761 1.00 89.18  ? 194 HIS D O   1 
ATOM   7868  C CB  . HIS D  1 194 ? -3.738  18.353 -30.342 1.00 123.26 ? 194 HIS D CB  1 
ATOM   7869  C CG  . HIS D  1 194 ? -4.459  18.872 -31.539 1.00 132.93 ? 194 HIS D CG  1 
ATOM   7870  N ND1 . HIS D  1 194 ? -3.970  18.707 -32.821 1.00 125.94 ? 194 HIS D ND1 1 
ATOM   7871  C CD2 . HIS D  1 194 ? -5.636  19.526 -31.661 1.00 130.23 ? 194 HIS D CD2 1 
ATOM   7872  C CE1 . HIS D  1 194 ? -4.810  19.247 -33.682 1.00 123.06 ? 194 HIS D CE1 1 
ATOM   7873  N NE2 . HIS D  1 194 ? -5.840  19.756 -32.995 1.00 127.75 ? 194 HIS D NE2 1 
ATOM   7874  N N   . THR D  1 195 ? -4.937  20.497 -28.461 1.00 88.28  ? 195 THR D N   1 
ATOM   7875  C CA  . THR D  1 195 ? -5.937  21.551 -28.135 1.00 93.82  ? 195 THR D CA  1 
ATOM   7876  C C   . THR D  1 195 ? -5.248  22.763 -27.494 1.00 106.02 ? 195 THR D C   1 
ATOM   7877  O O   . THR D  1 195 ? -5.487  23.895 -27.967 1.00 111.22 ? 195 THR D O   1 
ATOM   7878  C CB  . THR D  1 195 ? -7.032  21.003 -27.211 1.00 91.35  ? 195 THR D CB  1 
ATOM   7879  O OG1 . THR D  1 195 ? -7.571  19.830 -27.821 1.00 96.71  ? 195 THR D OG1 1 
ATOM   7880  C CG2 . THR D  1 195 ? -8.137  22.002 -26.947 1.00 88.93  ? 195 THR D CG2 1 
ATOM   7881  N N   . MET D  1 196 ? -4.440  22.533 -26.452 1.00 103.08 ? 196 MET D N   1 
ATOM   7882  C CA  . MET D  1 196 ? -3.776  23.595 -25.649 1.00 88.08  ? 196 MET D CA  1 
ATOM   7883  C C   . MET D  1 196 ? -2.856  24.427 -26.550 1.00 76.65  ? 196 MET D C   1 
ATOM   7884  O O   . MET D  1 196 ? -2.988  25.666 -26.539 1.00 71.79  ? 196 MET D O   1 
ATOM   7885  C CB  . MET D  1 196 ? -2.955  22.992 -24.505 1.00 91.81  ? 196 MET D CB  1 
ATOM   7886  C CG  . MET D  1 196 ? -3.800  22.523 -23.338 1.00 102.97 ? 196 MET D CG  1 
ATOM   7887  S SD  . MET D  1 196 ? -4.655  23.890 -22.514 1.00 107.68 ? 196 MET D SD  1 
ATOM   7888  C CE  . MET D  1 196 ? -6.031  24.155 -23.632 1.00 103.46 ? 196 MET D CE  1 
ATOM   7889  N N   . LEU D  1 197 ? -1.962  23.767 -27.292 1.00 72.81  ? 197 LEU D N   1 
ATOM   7890  C CA  . LEU D  1 197 ? -0.965  24.424 -28.179 1.00 78.33  ? 197 LEU D CA  1 
ATOM   7891  C C   . LEU D  1 197 ? -1.699  25.340 -29.164 1.00 82.51  ? 197 LEU D C   1 
ATOM   7892  O O   . LEU D  1 197 ? -1.264  26.498 -29.333 1.00 104.45 ? 197 LEU D O   1 
ATOM   7893  C CB  . LEU D  1 197 ? -0.150  23.354 -28.912 1.00 74.10  ? 197 LEU D CB  1 
ATOM   7894  C CG  . LEU D  1 197 ? 1.063   23.867 -29.686 1.00 72.15  ? 197 LEU D CG  1 
ATOM   7895  C CD1 . LEU D  1 197 ? 2.007   24.638 -28.777 1.00 74.78  ? 197 LEU D CD1 1 
ATOM   7896  C CD2 . LEU D  1 197 ? 1.801   22.721 -30.361 1.00 72.47  ? 197 LEU D CD2 1 
ATOM   7897  N N   . LYS D  1 198 ? -2.772  24.836 -29.780 1.00 78.45  ? 198 LYS D N   1 
ATOM   7898  C CA  . LYS D  1 198 ? -3.645  25.611 -30.701 1.00 78.39  ? 198 LYS D CA  1 
ATOM   7899  C C   . LYS D  1 198 ? -4.169  26.844 -29.953 1.00 81.10  ? 198 LYS D C   1 
ATOM   7900  O O   . LYS D  1 198 ? -4.022  27.961 -30.484 1.00 81.85  ? 198 LYS D O   1 
ATOM   7901  C CB  . LYS D  1 198 ? -4.791  24.738 -31.223 1.00 74.54  ? 198 LYS D CB  1 
ATOM   7902  C CG  . LYS D  1 198 ? -5.432  25.213 -32.521 1.00 64.89  ? 198 LYS D CG  1 
ATOM   7903  N N   . SER D  1 199 ? -4.743  26.643 -28.762 1.00 74.56  ? 199 SER D N   1 
ATOM   7904  C CA  . SER D  1 199 ? -5.289  27.716 -27.889 1.00 71.61  ? 199 SER D CA  1 
ATOM   7905  C C   . SER D  1 199 ? -4.219  28.785 -27.640 1.00 75.91  ? 199 SER D C   1 
ATOM   7906  O O   . SER D  1 199 ? -4.474  29.959 -27.965 1.00 88.40  ? 199 SER D O   1 
ATOM   7907  C CB  . SER D  1 199 ? -5.805  27.157 -26.590 1.00 72.84  ? 199 SER D CB  1 
ATOM   7908  O OG  . SER D  1 199 ? -6.129  28.205 -25.687 1.00 70.51  ? 199 SER D OG  1 
ATOM   7909  N N   . ALA D  1 200 ? -3.075  28.387 -27.075 1.00 73.79  ? 200 ALA D N   1 
ATOM   7910  C CA  . ALA D  1 200 ? -1.928  29.270 -26.758 1.00 72.28  ? 200 ALA D CA  1 
ATOM   7911  C C   . ALA D  1 200 ? -1.561  30.106 -27.990 1.00 72.99  ? 200 ALA D C   1 
ATOM   7912  O O   . ALA D  1 200 ? -1.457  31.342 -27.858 1.00 71.06  ? 200 ALA D O   1 
ATOM   7913  C CB  . ALA D  1 200 ? -0.757  28.441 -26.289 1.00 74.64  ? 200 ALA D CB  1 
ATOM   7914  N N   . ALA D  1 201 ? -1.379  29.445 -29.138 1.00 71.41  ? 201 ALA D N   1 
ATOM   7915  C CA  . ALA D  1 201 ? -0.977  30.060 -30.425 1.00 75.00  ? 201 ALA D CA  1 
ATOM   7916  C C   . ALA D  1 201 ? -1.984  31.147 -30.821 1.00 73.39  ? 201 ALA D C   1 
ATOM   7917  O O   . ALA D  1 201 ? -1.545  32.226 -31.260 1.00 74.68  ? 201 ALA D O   1 
ATOM   7918  C CB  . ALA D  1 201 ? -0.862  28.995 -31.487 1.00 74.59  ? 201 ALA D CB  1 
ATOM   7919  N N   . ILE D  1 202 ? -3.282  30.868 -30.673 1.00 65.83  ? 202 ILE D N   1 
ATOM   7920  C CA  . ILE D  1 202 ? -4.393  31.816 -30.990 1.00 67.51  ? 202 ILE D CA  1 
ATOM   7921  C C   . ILE D  1 202 ? -4.253  33.058 -30.103 1.00 67.93  ? 202 ILE D C   1 
ATOM   7922  O O   . ILE D  1 202 ? -4.165  34.169 -30.657 1.00 76.91  ? 202 ILE D O   1 
ATOM   7923  C CB  . ILE D  1 202 ? -5.765  31.138 -30.809 1.00 69.93  ? 202 ILE D CB  1 
ATOM   7924  C CG1 . ILE D  1 202 ? -5.988  30.029 -31.840 1.00 72.13  ? 202 ILE D CG1 1 
ATOM   7925  C CG2 . ILE D  1 202 ? -6.885  32.168 -30.837 1.00 70.05  ? 202 ILE D CG2 1 
ATOM   7926  C CD1 . ILE D  1 202 ? -7.215  29.185 -31.577 1.00 75.73  ? 202 ILE D CD1 1 
ATOM   7927  N N   . VAL D  1 203 ? -4.230  32.865 -28.780 1.00 65.80  ? 203 VAL D N   1 
ATOM   7928  C CA  . VAL D  1 203 ? -4.166  33.958 -27.762 1.00 61.48  ? 203 VAL D CA  1 
ATOM   7929  C C   . VAL D  1 203 ? -3.059  34.941 -28.162 1.00 55.59  ? 203 VAL D C   1 
ATOM   7930  O O   . VAL D  1 203 ? -3.316  36.161 -28.140 1.00 55.64  ? 203 VAL D O   1 
ATOM   7931  C CB  . VAL D  1 203 ? -3.933  33.407 -26.342 1.00 63.15  ? 203 VAL D CB  1 
ATOM   7932  C CG1 . VAL D  1 203 ? -3.851  34.525 -25.312 1.00 60.56  ? 203 VAL D CG1 1 
ATOM   7933  C CG2 . VAL D  1 203 ? -4.997  32.394 -25.944 1.00 60.64  ? 203 VAL D CG2 1 
ATOM   7934  N N   . LEU D  1 204 ? -1.879  34.423 -28.514 1.00 52.64  ? 204 LEU D N   1 
ATOM   7935  C CA  . LEU D  1 204 ? -0.692  35.234 -28.895 1.00 56.57  ? 204 LEU D CA  1 
ATOM   7936  C C   . LEU D  1 204 ? -0.942  35.905 -30.249 1.00 57.74  ? 204 LEU D C   1 
ATOM   7937  O O   . LEU D  1 204 ? -0.981  37.148 -30.297 1.00 57.78  ? 204 LEU D O   1 
ATOM   7938  C CB  . LEU D  1 204 ? 0.541   34.327 -28.959 1.00 59.49  ? 204 LEU D CB  1 
ATOM   7939  C CG  . LEU D  1 204 ? 1.849   35.029 -29.316 1.00 64.35  ? 204 LEU D CG  1 
ATOM   7940  C CD1 . LEU D  1 204 ? 2.228   36.045 -28.249 1.00 67.04  ? 204 LEU D CD1 1 
ATOM   7941  C CD2 . LEU D  1 204 ? 2.970   34.021 -29.517 1.00 68.42  ? 204 LEU D CD2 1 
ATOM   7942  N N   . LEU D  1 205 ? -1.113  35.098 -31.300 1.00 62.23  ? 205 LEU D N   1 
ATOM   7943  C CA  . LEU D  1 205 ? -1.169  35.546 -32.716 1.00 64.50  ? 205 LEU D CA  1 
ATOM   7944  C C   . LEU D  1 205 ? -2.418  36.405 -32.947 1.00 65.13  ? 205 LEU D C   1 
ATOM   7945  O O   . LEU D  1 205 ? -2.312  37.403 -33.687 1.00 66.90  ? 205 LEU D O   1 
ATOM   7946  C CB  . LEU D  1 205 ? -1.142  34.307 -33.615 1.00 65.50  ? 205 LEU D CB  1 
ATOM   7947  C CG  . LEU D  1 205 ? 0.106   33.438 -33.461 1.00 67.73  ? 205 LEU D CG  1 
ATOM   7948  C CD1 . LEU D  1 205 ? -0.012  32.148 -34.255 1.00 73.14  ? 205 LEU D CD1 1 
ATOM   7949  C CD2 . LEU D  1 205 ? 1.351   34.206 -33.876 1.00 66.08  ? 205 LEU D CD2 1 
ATOM   7950  N N   . ALA D  1 206 ? -3.545  36.043 -32.325 1.00 62.77  ? 206 ALA D N   1 
ATOM   7951  C CA  . ALA D  1 206 ? -4.820  36.800 -32.372 1.00 61.64  ? 206 ALA D CA  1 
ATOM   7952  C C   . ALA D  1 206 ? -4.617  38.188 -31.752 1.00 64.73  ? 206 ALA D C   1 
ATOM   7953  O O   . ALA D  1 206 ? -4.828  39.188 -32.465 1.00 79.24  ? 206 ALA D O   1 
ATOM   7954  C CB  . ALA D  1 206 ? -5.908  36.035 -31.658 1.00 60.79  ? 206 ALA D CB  1 
ATOM   7955  N N   . GLY D  1 207 ? -4.218  38.237 -30.476 1.00 59.35  ? 207 GLY D N   1 
ATOM   7956  C CA  . GLY D  1 207 ? -4.005  39.483 -29.713 1.00 60.36  ? 207 GLY D CA  1 
ATOM   7957  C C   . GLY D  1 207 ? -3.098  40.458 -30.449 1.00 62.44  ? 207 GLY D C   1 
ATOM   7958  O O   . GLY D  1 207 ? -3.375  41.671 -30.400 1.00 72.76  ? 207 GLY D O   1 
ATOM   7959  N N   . TRP D  1 208 ? -2.054  39.944 -31.107 1.00 60.22  ? 208 TRP D N   1 
ATOM   7960  C CA  . TRP D  1 208 ? -1.029  40.724 -31.854 1.00 64.93  ? 208 TRP D CA  1 
ATOM   7961  C C   . TRP D  1 208 ? -1.691  41.801 -32.722 1.00 63.47  ? 208 TRP D C   1 
ATOM   7962  O O   . TRP D  1 208 ? -1.072  42.865 -32.916 1.00 68.51  ? 208 TRP D O   1 
ATOM   7963  C CB  . TRP D  1 208 ? -0.165  39.780 -32.699 1.00 73.85  ? 208 TRP D CB  1 
ATOM   7964  C CG  . TRP D  1 208 ? 1.002   39.211 -31.954 1.00 81.79  ? 208 TRP D CG  1 
ATOM   7965  C CD1 . TRP D  1 208 ? 1.173   39.184 -30.600 1.00 86.21  ? 208 TRP D CD1 1 
ATOM   7966  C CD2 . TRP D  1 208 ? 2.158   38.565 -32.516 1.00 85.71  ? 208 TRP D CD2 1 
ATOM   7967  N NE1 . TRP D  1 208 ? 2.360   38.581 -30.282 1.00 90.68  ? 208 TRP D NE1 1 
ATOM   7968  C CE2 . TRP D  1 208 ? 2.986   38.190 -31.437 1.00 91.53  ? 208 TRP D CE2 1 
ATOM   7969  C CE3 . TRP D  1 208 ? 2.577   38.271 -33.818 1.00 87.20  ? 208 TRP D CE3 1 
ATOM   7970  C CZ2 . TRP D  1 208 ? 4.205   37.540 -31.625 1.00 92.07  ? 208 TRP D CZ2 1 
ATOM   7971  C CZ3 . TRP D  1 208 ? 3.781   37.628 -34.002 1.00 87.11  ? 208 TRP D CZ3 1 
ATOM   7972  C CH2 . TRP D  1 208 ? 4.584   37.271 -32.919 1.00 87.70  ? 208 TRP D CH2 1 
ATOM   7973  N N   . VAL D  1 209 ? -2.896  41.524 -33.226 1.00 63.08  ? 209 VAL D N   1 
ATOM   7974  C CA  . VAL D  1 209 ? -3.636  42.390 -34.193 1.00 61.32  ? 209 VAL D CA  1 
ATOM   7975  C C   . VAL D  1 209 ? -3.898  43.758 -33.555 1.00 61.02  ? 209 VAL D C   1 
ATOM   7976  O O   . VAL D  1 209 ? -3.802  44.772 -34.274 1.00 62.48  ? 209 VAL D O   1 
ATOM   7977  C CB  . VAL D  1 209 ? -4.945  41.715 -34.643 1.00 57.72  ? 209 VAL D CB  1 
ATOM   7978  C CG1 . VAL D  1 209 ? -5.830  42.663 -35.437 1.00 56.24  ? 209 VAL D CG1 1 
ATOM   7979  C CG2 . VAL D  1 209 ? -4.669  40.443 -35.431 1.00 56.63  ? 209 VAL D CG2 1 
ATOM   7980  N N   . VAL D  1 210 ? -4.215  43.776 -32.257 1.00 55.11  ? 210 VAL D N   1 
ATOM   7981  C CA  . VAL D  1 210 ? -4.607  44.998 -31.492 1.00 54.56  ? 210 VAL D CA  1 
ATOM   7982  C C   . VAL D  1 210 ? -3.563  46.098 -31.718 1.00 51.30  ? 210 VAL D C   1 
ATOM   7983  O O   . VAL D  1 210 ? -3.958  47.274 -31.833 1.00 49.93  ? 210 VAL D O   1 
ATOM   7984  C CB  . VAL D  1 210 ? -4.770  44.684 -29.992 1.00 53.94  ? 210 VAL D CB  1 
ATOM   7985  C CG1 . VAL D  1 210 ? -4.979  45.945 -29.169 1.00 54.74  ? 210 VAL D CG1 1 
ATOM   7986  C CG2 . VAL D  1 210 ? -5.894  43.690 -29.745 1.00 53.21  ? 210 VAL D CG2 1 
ATOM   7987  N N   . TYR D  1 211 ? -2.283  45.727 -31.786 1.00 47.39  ? 211 TYR D N   1 
ATOM   7988  C CA  . TYR D  1 211 ? -1.131  46.666 -31.738 1.00 56.37  ? 211 TYR D CA  1 
ATOM   7989  C C   . TYR D  1 211 ? -1.073  47.493 -33.021 1.00 56.96  ? 211 TYR D C   1 
ATOM   7990  O O   . TYR D  1 211 ? -1.061  48.719 -32.959 1.00 60.98  ? 211 TYR D O   1 
ATOM   7991  C CB  . TYR D  1 211 ? 0.149   45.891 -31.413 1.00 59.86  ? 211 TYR D CB  1 
ATOM   7992  C CG  . TYR D  1 211 ? 0.149   45.323 -30.015 1.00 63.02  ? 211 TYR D CG  1 
ATOM   7993  C CD1 . TYR D  1 211 ? 0.704   46.024 -28.957 1.00 62.55  ? 211 TYR D CD1 1 
ATOM   7994  C CD2 . TYR D  1 211 ? -0.457  44.109 -29.739 1.00 62.70  ? 211 TYR D CD2 1 
ATOM   7995  C CE1 . TYR D  1 211 ? 0.683   45.521 -27.667 1.00 61.17  ? 211 TYR D CE1 1 
ATOM   7996  C CE2 . TYR D  1 211 ? -0.486  43.590 -28.456 1.00 61.92  ? 211 TYR D CE2 1 
ATOM   7997  C CZ  . TYR D  1 211 ? 0.086   44.299 -27.415 1.00 61.09  ? 211 TYR D CZ  1 
ATOM   7998  O OH  . TYR D  1 211 ? 0.059   43.790 -26.149 1.00 56.72  ? 211 TYR D OH  1 
ATOM   7999  N N   . PRO D  1 212 ? -1.043  46.869 -34.220 1.00 59.31  ? 212 PRO D N   1 
ATOM   8000  C CA  . PRO D  1 212 ? -1.039  47.625 -35.473 1.00 55.47  ? 212 PRO D CA  1 
ATOM   8001  C C   . PRO D  1 212 ? -2.235  48.585 -35.575 1.00 56.18  ? 212 PRO D C   1 
ATOM   8002  O O   . PRO D  1 212 ? -2.072  49.669 -36.108 1.00 54.55  ? 212 PRO D O   1 
ATOM   8003  C CB  . PRO D  1 212 ? -1.122  46.545 -36.560 1.00 56.65  ? 212 PRO D CB  1 
ATOM   8004  C CG  . PRO D  1 212 ? -0.587  45.295 -35.889 1.00 61.46  ? 212 PRO D CG  1 
ATOM   8005  C CD  . PRO D  1 212 ? -0.997  45.416 -34.435 1.00 61.43  ? 212 PRO D CD  1 
ATOM   8006  N N   . ILE D  1 213 ? -3.396  48.160 -35.063 1.00 54.40  ? 213 ILE D N   1 
ATOM   8007  C CA  . ILE D  1 213 ? -4.668  48.945 -35.050 1.00 48.89  ? 213 ILE D CA  1 
ATOM   8008  C C   . ILE D  1 213 ? -4.454  50.226 -34.237 1.00 49.86  ? 213 ILE D C   1 
ATOM   8009  O O   . ILE D  1 213 ? -4.794  51.318 -34.738 1.00 55.03  ? 213 ILE D O   1 
ATOM   8010  C CB  . ILE D  1 213 ? -5.823  48.100 -34.476 1.00 44.62  ? 213 ILE D CB  1 
ATOM   8011  C CG1 . ILE D  1 213 ? -6.155  46.908 -35.377 1.00 43.35  ? 213 ILE D CG1 1 
ATOM   8012  C CG2 . ILE D  1 213 ? -7.045  48.965 -34.207 1.00 44.91  ? 213 ILE D CG2 1 
ATOM   8013  C CD1 . ILE D  1 213 ? -7.093  45.907 -34.744 1.00 44.56  ? 213 ILE D CD1 1 
ATOM   8014  N N   . VAL D  1 214 ? -3.909  50.087 -33.027 1.00 50.92  ? 214 VAL D N   1 
ATOM   8015  C CA  . VAL D  1 214 ? -3.681  51.206 -32.066 1.00 51.41  ? 214 VAL D CA  1 
ATOM   8016  C C   . VAL D  1 214 ? -2.604  52.141 -32.630 1.00 44.60  ? 214 VAL D C   1 
ATOM   8017  O O   . VAL D  1 214 ? -2.666  53.352 -32.344 1.00 43.95  ? 214 VAL D O   1 
ATOM   8018  C CB  . VAL D  1 214 ? -3.288  50.674 -30.675 1.00 55.28  ? 214 VAL D CB  1 
ATOM   8019  C CG1 . VAL D  1 214 ? -3.041  51.809 -29.696 1.00 57.41  ? 214 VAL D CG1 1 
ATOM   8020  C CG2 . VAL D  1 214 ? -4.324  49.707 -30.123 1.00 57.19  ? 214 VAL D CG2 1 
ATOM   8021  N N   . TYR D  1 215 ? -1.658  51.597 -33.400 1.00 39.26  ? 215 TYR D N   1 
ATOM   8022  C CA  . TYR D  1 215 ? -0.508  52.337 -33.983 1.00 39.92  ? 215 TYR D CA  1 
ATOM   8023  C C   . TYR D  1 215 ? -1.017  53.474 -34.871 1.00 44.52  ? 215 TYR D C   1 
ATOM   8024  O O   . TYR D  1 215 ? -0.341  54.515 -34.948 1.00 47.73  ? 215 TYR D O   1 
ATOM   8025  C CB  . TYR D  1 215 ? 0.391   51.398 -34.790 1.00 40.44  ? 215 TYR D CB  1 
ATOM   8026  C CG  . TYR D  1 215 ? 1.526   52.076 -35.518 1.00 40.48  ? 215 TYR D CG  1 
ATOM   8027  C CD1 . TYR D  1 215 ? 1.310   52.757 -36.702 1.00 45.02  ? 215 TYR D CD1 1 
ATOM   8028  C CD2 . TYR D  1 215 ? 2.823   52.024 -35.034 1.00 45.46  ? 215 TYR D CD2 1 
ATOM   8029  C CE1 . TYR D  1 215 ? 2.348   53.373 -37.384 1.00 47.55  ? 215 TYR D CE1 1 
ATOM   8030  C CE2 . TYR D  1 215 ? 3.872   52.635 -35.702 1.00 46.40  ? 215 TYR D CE2 1 
ATOM   8031  C CZ  . TYR D  1 215 ? 3.635   53.311 -36.885 1.00 46.72  ? 215 TYR D CZ  1 
ATOM   8032  O OH  . TYR D  1 215 ? 4.664   53.918 -37.548 1.00 48.62  ? 215 TYR D OH  1 
ATOM   8033  N N   . PHE D  1 216 ? -2.175  53.272 -35.510 1.00 54.00  ? 216 PHE D N   1 
ATOM   8034  C CA  . PHE D  1 216 ? -2.702  54.121 -36.613 1.00 54.57  ? 216 PHE D CA  1 
ATOM   8035  C C   . PHE D  1 216 ? -3.728  55.136 -36.096 1.00 55.50  ? 216 PHE D C   1 
ATOM   8036  O O   . PHE D  1 216 ? -4.088  56.048 -36.864 1.00 60.71  ? 216 PHE D O   1 
ATOM   8037  C CB  . PHE D  1 216 ? -3.311  53.247 -37.712 1.00 46.77  ? 216 PHE D CB  1 
ATOM   8038  C CG  . PHE D  1 216 ? -2.293  52.636 -38.640 1.00 44.25  ? 216 PHE D CG  1 
ATOM   8039  C CD1 . PHE D  1 216 ? -1.496  53.439 -39.440 1.00 42.41  ? 216 PHE D CD1 1 
ATOM   8040  C CD2 . PHE D  1 216 ? -2.124  51.262 -38.707 1.00 47.01  ? 216 PHE D CD2 1 
ATOM   8041  C CE1 . PHE D  1 216 ? -0.558  52.883 -40.295 1.00 44.60  ? 216 PHE D CE1 1 
ATOM   8042  C CE2 . PHE D  1 216 ? -1.183  50.707 -39.560 1.00 50.29  ? 216 PHE D CE2 1 
ATOM   8043  C CZ  . PHE D  1 216 ? -0.403  51.517 -40.353 1.00 47.49  ? 216 PHE D CZ  1 
ATOM   8044  N N   . LEU D  1 217 ? -4.179  54.994 -34.847 1.00 52.36  ? 217 LEU D N   1 
ATOM   8045  C CA  . LEU D  1 217 ? -5.207  55.881 -34.236 1.00 56.90  ? 217 LEU D CA  1 
ATOM   8046  C C   . LEU D  1 217 ? -4.740  57.334 -34.286 1.00 57.23  ? 217 LEU D C   1 
ATOM   8047  O O   . LEU D  1 217 ? -5.548  58.237 -34.491 1.00 57.04  ? 217 LEU D O   1 
ATOM   8048  C CB  . LEU D  1 217 ? -5.477  55.426 -32.799 1.00 60.34  ? 217 LEU D CB  1 
ATOM   8049  C CG  . LEU D  1 217 ? -6.141  54.056 -32.670 1.00 67.76  ? 217 LEU D CG  1 
ATOM   8050  C CD1 . LEU D  1 217 ? -6.579  53.799 -31.236 1.00 68.73  ? 217 LEU D CD1 1 
ATOM   8051  C CD2 . LEU D  1 217 ? -7.324  53.933 -33.618 1.00 67.10  ? 217 LEU D CD2 1 
ATOM   8052  N N   . PRO D  1 218 ? -3.430  57.616 -34.100 1.00 61.82  ? 218 PRO D N   1 
ATOM   8053  C CA  . PRO D  1 218 ? -2.919  58.985 -34.194 1.00 68.34  ? 218 PRO D CA  1 
ATOM   8054  C C   . PRO D  1 218 ? -3.247  59.694 -35.520 1.00 71.19  ? 218 PRO D C   1 
ATOM   8055  O O   . PRO D  1 218 ? -3.074  60.894 -35.595 1.00 67.27  ? 218 PRO D O   1 
ATOM   8056  C CB  . PRO D  1 218 ? -1.397  58.806 -34.061 1.00 66.56  ? 218 PRO D CB  1 
ATOM   8057  C CG  . PRO D  1 218 ? -1.238  57.516 -33.286 1.00 64.15  ? 218 PRO D CG  1 
ATOM   8058  C CD  . PRO D  1 218 ? -2.384  56.643 -33.752 1.00 62.71  ? 218 PRO D CD  1 
ATOM   8059  N N   . LEU D  1 219 ? -3.700  58.945 -36.530 1.00 71.24  ? 219 LEU D N   1 
ATOM   8060  C CA  . LEU D  1 219 ? -4.019  59.474 -37.884 1.00 65.16  ? 219 LEU D CA  1 
ATOM   8061  C C   . LEU D  1 219 ? -5.421  60.092 -37.884 1.00 62.19  ? 219 LEU D C   1 
ATOM   8062  O O   . LEU D  1 219 ? -5.641  61.023 -38.681 1.00 62.40  ? 219 LEU D O   1 
ATOM   8063  C CB  . LEU D  1 219 ? -3.919  58.344 -38.913 1.00 62.19  ? 219 LEU D CB  1 
ATOM   8064  C CG  . LEU D  1 219 ? -2.501  57.908 -39.278 1.00 63.66  ? 219 LEU D CG  1 
ATOM   8065  C CD1 . LEU D  1 219 ? -2.531  56.809 -40.326 1.00 61.83  ? 219 LEU D CD1 1 
ATOM   8066  C CD2 . LEU D  1 219 ? -1.674  59.087 -39.768 1.00 62.45  ? 219 LEU D CD2 1 
ATOM   8067  N N   . PHE D  1 220 ? -6.319  59.594 -37.024 1.00 60.77  ? 220 PHE D N   1 
ATOM   8068  C CA  . PHE D  1 220 ? -7.724  60.063 -36.879 1.00 64.44  ? 220 PHE D CA  1 
ATOM   8069  C C   . PHE D  1 220 ? -7.768  61.403 -36.131 1.00 63.57  ? 220 PHE D C   1 
ATOM   8070  O O   . PHE D  1 220 ? -8.876  61.894 -35.867 1.00 67.66  ? 220 PHE D O   1 
ATOM   8071  C CB  . PHE D  1 220 ? -8.575  59.040 -36.121 1.00 68.74  ? 220 PHE D CB  1 
ATOM   8072  C CG  . PHE D  1 220 ? -8.856  57.749 -36.848 1.00 78.37  ? 220 PHE D CG  1 
ATOM   8073  C CD1 . PHE D  1 220 ? -9.500  57.745 -38.075 1.00 82.29  ? 220 PHE D CD1 1 
ATOM   8074  C CD2 . PHE D  1 220 ? -8.512  56.532 -36.281 1.00 88.46  ? 220 PHE D CD2 1 
ATOM   8075  C CE1 . PHE D  1 220 ? -9.769  56.553 -38.730 1.00 93.26  ? 220 PHE D CE1 1 
ATOM   8076  C CE2 . PHE D  1 220 ? -8.782  55.341 -36.937 1.00 90.65  ? 220 PHE D CE2 1 
ATOM   8077  C CZ  . PHE D  1 220 ? -9.410  55.353 -38.159 1.00 95.43  ? 220 PHE D CZ  1 
ATOM   8078  N N   . GLY D  1 221 ? -6.602  61.964 -35.799 1.00 74.54  ? 221 GLY D N   1 
ATOM   8079  C CA  . GLY D  1 221 ? -6.473  63.240 -35.069 1.00 84.00  ? 221 GLY D CA  1 
ATOM   8080  C C   . GLY D  1 221 ? -5.785  63.048 -33.729 1.00 97.40  ? 221 GLY D C   1 
ATOM   8081  O O   . GLY D  1 221 ? -5.142  61.990 -33.540 1.00 116.34 ? 221 GLY D O   1 
ATOM   8082  N N   . ALA D  1 222 ? -5.908  64.036 -32.835 1.00 98.24  ? 222 ALA D N   1 
ATOM   8083  C CA  . ALA D  1 222 ? -5.291  64.059 -31.488 1.00 97.30  ? 222 ALA D CA  1 
ATOM   8084  C C   . ALA D  1 222 ? -6.295  64.594 -30.461 1.00 89.75  ? 222 ALA D C   1 
ATOM   8085  O O   . ALA D  1 222 ? -7.122  65.450 -30.827 1.00 94.39  ? 222 ALA D O   1 
ATOM   8086  C CB  . ALA D  1 222 ? -4.036  64.895 -31.514 1.00 91.45  ? 222 ALA D CB  1 
ATOM   8087  N N   . SER D  1 223 ? -6.205  64.110 -29.219 1.00 90.10  ? 223 SER D N   1 
ATOM   8088  C CA  . SER D  1 223 ? -7.129  64.436 -28.103 1.00 81.68  ? 223 SER D CA  1 
ATOM   8089  C C   . SER D  1 223 ? -6.676  63.714 -26.829 1.00 81.38  ? 223 SER D C   1 
ATOM   8090  O O   . SER D  1 223 ? -6.176  62.573 -26.932 1.00 87.37  ? 223 SER D O   1 
ATOM   8091  C CB  . SER D  1 223 ? -8.548  64.072 -28.458 1.00 83.64  ? 223 SER D CB  1 
ATOM   8092  O OG  . SER D  1 223 ? -9.378  64.089 -27.306 1.00 92.64  ? 223 SER D OG  1 
ATOM   8093  N N   . GLY D  1 224 ? -6.845  64.362 -25.673 1.00 77.80  ? 224 GLY D N   1 
ATOM   8094  C CA  . GLY D  1 224 ? -6.641  63.740 -24.353 1.00 74.34  ? 224 GLY D CA  1 
ATOM   8095  C C   . GLY D  1 224 ? -7.310  62.378 -24.291 1.00 70.77  ? 224 GLY D C   1 
ATOM   8096  O O   . GLY D  1 224 ? -6.658  61.417 -23.837 1.00 81.31  ? 224 GLY D O   1 
ATOM   8097  N N   . GLY D  1 225 ? -8.565  62.298 -24.745 1.00 69.26  ? 225 GLY D N   1 
ATOM   8098  C CA  . GLY D  1 225 ? -9.379  61.067 -24.760 1.00 66.75  ? 225 GLY D CA  1 
ATOM   8099  C C   . GLY D  1 225 ? -8.742  59.982 -25.610 1.00 62.29  ? 225 GLY D C   1 
ATOM   8100  O O   . GLY D  1 225 ? -8.687  58.826 -25.149 1.00 56.51  ? 225 GLY D O   1 
ATOM   8101  N N   . LEU D  1 226 ? -8.279  60.339 -26.810 1.00 65.12  ? 226 LEU D N   1 
ATOM   8102  C CA  . LEU D  1 226 ? -7.610  59.402 -27.749 1.00 73.06  ? 226 LEU D CA  1 
ATOM   8103  C C   . LEU D  1 226 ? -6.321  58.888 -27.101 1.00 69.91  ? 226 LEU D C   1 
ATOM   8104  O O   . LEU D  1 226 ? -6.175  57.654 -26.969 1.00 67.98  ? 226 LEU D O   1 
ATOM   8105  C CB  . LEU D  1 226 ? -7.316  60.123 -29.068 1.00 73.25  ? 226 LEU D CB  1 
ATOM   8106  C CG  . LEU D  1 226 ? -6.706  59.250 -30.162 1.00 74.50  ? 226 LEU D CG  1 
ATOM   8107  C CD1 . LEU D  1 226 ? -7.602  58.058 -30.464 1.00 72.36  ? 226 LEU D CD1 1 
ATOM   8108  C CD2 . LEU D  1 226 ? -6.454  60.065 -31.420 1.00 72.12  ? 226 LEU D CD2 1 
ATOM   8109  N N   . THR D  1 227 ? -5.434  59.808 -26.708 1.00 60.86  ? 227 THR D N   1 
ATOM   8110  C CA  . THR D  1 227 ? -4.136  59.510 -26.047 1.00 56.20  ? 227 THR D CA  1 
ATOM   8111  C C   . THR D  1 227 ? -4.371  58.534 -24.888 1.00 58.62  ? 227 THR D C   1 
ATOM   8112  O O   . THR D  1 227 ? -3.643  57.525 -24.806 1.00 55.61  ? 227 THR D O   1 
ATOM   8113  C CB  . THR D  1 227 ? -3.453  60.798 -25.574 1.00 50.14  ? 227 THR D CB  1 
ATOM   8114  O OG1 . THR D  1 227 ? -3.171  61.588 -26.729 1.00 49.72  ? 227 THR D OG1 1 
ATOM   8115  C CG2 . THR D  1 227 ? -2.180  60.533 -24.803 1.00 54.05  ? 227 THR D CG2 1 
ATOM   8116  N N   . THR D  1 228 ? -5.353  58.828 -24.029 1.00 58.20  ? 228 THR D N   1 
ATOM   8117  C CA  . THR D  1 228 ? -5.764  57.969 -22.886 1.00 55.93  ? 228 THR D CA  1 
ATOM   8118  C C   . THR D  1 228 ? -6.111  56.570 -23.406 1.00 58.08  ? 228 THR D C   1 
ATOM   8119  O O   . THR D  1 228 ? -5.607  55.585 -22.833 1.00 67.67  ? 228 THR D O   1 
ATOM   8120  C CB  . THR D  1 228 ? -6.943  58.584 -22.123 1.00 48.66  ? 228 THR D CB  1 
ATOM   8121  O OG1 . THR D  1 228 ? -6.496  59.829 -21.587 1.00 46.43  ? 228 THR D OG1 1 
ATOM   8122  C CG2 . THR D  1 228 ? -7.462  57.687 -21.020 1.00 46.90  ? 228 THR D CG2 1 
ATOM   8123  N N   . THR D  1 229 ? -6.942  56.497 -24.450 1.00 54.44  ? 229 THR D N   1 
ATOM   8124  C CA  . THR D  1 229 ? -7.393  55.237 -25.097 1.00 53.40  ? 229 THR D CA  1 
ATOM   8125  C C   . THR D  1 229 ? -6.170  54.437 -25.552 1.00 52.50  ? 229 THR D C   1 
ATOM   8126  O O   . THR D  1 229 ? -6.061  53.252 -25.181 1.00 49.94  ? 229 THR D O   1 
ATOM   8127  C CB  . THR D  1 229 ? -8.321  55.532 -26.280 1.00 54.07  ? 229 THR D CB  1 
ATOM   8128  O OG1 . THR D  1 229 ? -9.433  56.270 -25.774 1.00 55.03  ? 229 THR D OG1 1 
ATOM   8129  C CG2 . THR D  1 229 ? -8.798  54.281 -26.985 1.00 55.11  ? 229 THR D CG2 1 
ATOM   8130  N N   . ILE D  1 230 ? -5.296  55.071 -26.335 1.00 55.29  ? 230 ILE D N   1 
ATOM   8131  C CA  . ILE D  1 230 ? -4.046  54.462 -26.876 1.00 58.74  ? 230 ILE D CA  1 
ATOM   8132  C C   . ILE D  1 230 ? -3.269  53.824 -25.718 1.00 59.31  ? 230 ILE D C   1 
ATOM   8133  O O   . ILE D  1 230 ? -2.945  52.624 -25.811 1.00 64.38  ? 230 ILE D O   1 
ATOM   8134  C CB  . ILE D  1 230 ? -3.213  55.518 -27.629 1.00 60.11  ? 230 ILE D CB  1 
ATOM   8135  C CG1 . ILE D  1 230 ? -3.882  55.915 -28.948 1.00 63.05  ? 230 ILE D CG1 1 
ATOM   8136  C CG2 . ILE D  1 230 ? -1.787  55.034 -27.840 1.00 57.25  ? 230 ILE D CG2 1 
ATOM   8137  C CD1 . ILE D  1 230 ? -3.333  57.177 -29.570 1.00 65.06  ? 230 ILE D CD1 1 
ATOM   8138  N N   . LEU D  1 231 ? -3.001  54.598 -24.664 1.00 57.40  ? 231 LEU D N   1 
ATOM   8139  C CA  . LEU D  1 231 ? -2.176  54.174 -23.502 1.00 56.43  ? 231 LEU D CA  1 
ATOM   8140  C C   . LEU D  1 231 ? -2.846  52.996 -22.783 1.00 53.87  ? 231 LEU D C   1 
ATOM   8141  O O   . LEU D  1 231 ? -2.161  51.973 -22.584 1.00 63.58  ? 231 LEU D O   1 
ATOM   8142  C CB  . LEU D  1 231 ? -1.974  55.372 -22.568 1.00 57.16  ? 231 LEU D CB  1 
ATOM   8143  C CG  . LEU D  1 231 ? -1.051  56.462 -23.112 1.00 62.90  ? 231 LEU D CG  1 
ATOM   8144  C CD1 . LEU D  1 231 ? -0.829  57.561 -22.085 1.00 68.01  ? 231 LEU D CD1 1 
ATOM   8145  C CD2 . LEU D  1 231 ? 0.283   55.879 -23.556 1.00 60.27  ? 231 LEU D CD2 1 
ATOM   8146  N N   . ILE D  1 232 ? -4.128  53.130 -22.423 1.00 50.83  ? 232 ILE D N   1 
ATOM   8147  C CA  . ILE D  1 232 ? -4.891  52.126 -21.617 1.00 50.92  ? 232 ILE D CA  1 
ATOM   8148  C C   . ILE D  1 232 ? -5.020  50.822 -22.412 1.00 52.70  ? 232 ILE D C   1 
ATOM   8149  O O   . ILE D  1 232 ? -4.760  49.746 -21.832 1.00 61.31  ? 232 ILE D O   1 
ATOM   8150  C CB  . ILE D  1 232 ? -6.276  52.665 -21.205 1.00 49.14  ? 232 ILE D CB  1 
ATOM   8151  C CG1 . ILE D  1 232 ? -6.163  53.863 -20.260 1.00 53.80  ? 232 ILE D CG1 1 
ATOM   8152  C CG2 . ILE D  1 232 ? -7.122  51.553 -20.603 1.00 48.43  ? 232 ILE D CG2 1 
ATOM   8153  C CD1 . ILE D  1 232 ? -7.489  54.339 -19.714 1.00 52.91  ? 232 ILE D CD1 1 
ATOM   8154  N N   . THR D  1 233 ? -5.429  50.916 -23.679 1.00 52.37  ? 233 THR D N   1 
ATOM   8155  C CA  . THR D  1 233 ? -5.660  49.750 -24.573 1.00 55.63  ? 233 THR D CA  1 
ATOM   8156  C C   . THR D  1 233 ? -4.386  48.900 -24.617 1.00 52.13  ? 233 THR D C   1 
ATOM   8157  O O   . THR D  1 233 ? -4.480  47.685 -24.356 1.00 52.52  ? 233 THR D O   1 
ATOM   8158  C CB  . THR D  1 233 ? -6.090  50.194 -25.976 1.00 60.81  ? 233 THR D CB  1 
ATOM   8159  O OG1 . THR D  1 233 ? -7.328  50.898 -25.865 1.00 57.15  ? 233 THR D OG1 1 
ATOM   8160  C CG2 . THR D  1 233 ? -6.254  49.031 -26.930 1.00 60.74  ? 233 THR D CG2 1 
ATOM   8161  N N   . LEU D  1 234 ? -3.247  49.528 -24.924 1.00 52.33  ? 234 LEU D N   1 
ATOM   8162  C CA  . LEU D  1 234 ? -1.921  48.865 -25.050 1.00 53.92  ? 234 LEU D CA  1 
ATOM   8163  C C   . LEU D  1 234 ? -1.566  48.157 -23.738 1.00 51.32  ? 234 LEU D C   1 
ATOM   8164  O O   . LEU D  1 234 ? -0.992  47.049 -23.800 1.00 56.30  ? 234 LEU D O   1 
ATOM   8165  C CB  . LEU D  1 234 ? -0.867  49.915 -25.410 1.00 51.37  ? 234 LEU D CB  1 
ATOM   8166  C CG  . LEU D  1 234 ? -0.934  50.442 -26.841 1.00 52.15  ? 234 LEU D CG  1 
ATOM   8167  C CD1 . LEU D  1 234 ? 0.124   51.509 -27.076 1.00 52.80  ? 234 LEU D CD1 1 
ATOM   8168  C CD2 . LEU D  1 234 ? -0.783  49.307 -27.844 1.00 52.52  ? 234 LEU D CD2 1 
ATOM   8169  N N   . THR D  1 235 ? -1.884  48.777 -22.600 1.00 45.31  ? 235 THR D N   1 
ATOM   8170  C CA  . THR D  1 235 ? -1.634  48.219 -21.245 1.00 45.37  ? 235 THR D CA  1 
ATOM   8171  C C   . THR D  1 235 ? -2.482  46.955 -21.061 1.00 48.58  ? 235 THR D C   1 
ATOM   8172  O O   . THR D  1 235 ? -1.902  45.898 -20.737 1.00 45.72  ? 235 THR D O   1 
ATOM   8173  C CB  . THR D  1 235 ? -1.910  49.265 -20.160 1.00 44.20  ? 235 THR D CB  1 
ATOM   8174  O OG1 . THR D  1 235 ? -1.096  50.406 -20.432 1.00 40.13  ? 235 THR D OG1 1 
ATOM   8175  C CG2 . THR D  1 235 ? -1.620  48.750 -18.769 1.00 44.17  ? 235 THR D CG2 1 
ATOM   8176  N N   . VAL D  1 236 ? -3.797  47.063 -21.268 1.00 51.39  ? 236 VAL D N   1 
ATOM   8177  C CA  . VAL D  1 236 ? -4.759  45.924 -21.176 1.00 53.27  ? 236 VAL D CA  1 
ATOM   8178  C C   . VAL D  1 236 ? -4.302  44.822 -22.140 1.00 53.25  ? 236 VAL D C   1 
ATOM   8179  O O   . VAL D  1 236 ? -4.309  43.643 -21.736 1.00 54.22  ? 236 VAL D O   1 
ATOM   8180  C CB  . VAL D  1 236 ? -6.201  46.376 -21.473 1.00 52.63  ? 236 VAL D CB  1 
ATOM   8181  C CG1 . VAL D  1 236 ? -7.149  45.193 -21.591 1.00 49.64  ? 236 VAL D CG1 1 
ATOM   8182  C CG2 . VAL D  1 236 ? -6.705  47.363 -20.431 1.00 54.29  ? 236 VAL D CG2 1 
ATOM   8183  N N   . ALA D  1 237 ? -3.911  45.200 -23.361 1.00 51.10  ? 237 ALA D N   1 
ATOM   8184  C CA  . ALA D  1 237 ? -3.378  44.291 -24.403 1.00 54.38  ? 237 ALA D CA  1 
ATOM   8185  C C   . ALA D  1 237 ? -2.162  43.537 -23.851 1.00 58.80  ? 237 ALA D C   1 
ATOM   8186  O O   . ALA D  1 237 ? -2.206  42.289 -23.814 1.00 61.41  ? 237 ALA D O   1 
ATOM   8187  C CB  . ALA D  1 237 ? -3.023  45.073 -25.643 1.00 53.13  ? 237 ALA D CB  1 
ATOM   8188  N N   . ASP D  1 238 ? -1.124  44.273 -23.437 1.00 53.05  ? 238 ASP D N   1 
ATOM   8189  C CA  . ASP D  1 238 ? 0.132   43.717 -22.864 1.00 48.32  ? 238 ASP D CA  1 
ATOM   8190  C C   . ASP D  1 238 ? -0.222  42.676 -21.796 1.00 47.66  ? 238 ASP D C   1 
ATOM   8191  O O   . ASP D  1 238 ? 0.237   41.525 -21.921 1.00 47.43  ? 238 ASP D O   1 
ATOM   8192  C CB  . ASP D  1 238 ? 1.027   44.822 -22.295 1.00 48.78  ? 238 ASP D CB  1 
ATOM   8193  C CG  . ASP D  1 238 ? 1.895   45.509 -23.337 1.00 53.82  ? 238 ASP D CG  1 
ATOM   8194  O OD1 . ASP D  1 238 ? 2.600   46.474 -22.975 1.00 55.49  ? 238 ASP D OD1 1 
ATOM   8195  O OD2 . ASP D  1 238 ? 1.861   45.073 -24.504 1.00 53.61  ? 238 ASP D OD2 1 
ATOM   8196  N N   . VAL D  1 239 ? -1.018  43.066 -20.796 1.00 44.31  ? 239 VAL D N   1 
ATOM   8197  C CA  . VAL D  1 239 ? -1.352  42.223 -19.608 1.00 45.02  ? 239 VAL D CA  1 
ATOM   8198  C C   . VAL D  1 239 ? -2.059  40.944 -20.075 1.00 49.26  ? 239 VAL D C   1 
ATOM   8199  O O   . VAL D  1 239 ? -1.587  39.848 -19.720 1.00 48.63  ? 239 VAL D O   1 
ATOM   8200  C CB  . VAL D  1 239 ? -2.210  42.994 -18.586 1.00 43.11  ? 239 VAL D CB  1 
ATOM   8201  C CG1 . VAL D  1 239 ? -2.795  42.066 -17.531 1.00 43.20  ? 239 VAL D CG1 1 
ATOM   8202  C CG2 . VAL D  1 239 ? -1.428  44.120 -17.930 1.00 44.71  ? 239 VAL D CG2 1 
ATOM   8203  N N   . ILE D  1 240 ? -3.150  41.081 -20.833 1.00 51.96  ? 240 ILE D N   1 
ATOM   8204  C CA  . ILE D  1 240 ? -4.011  39.946 -21.282 1.00 52.41  ? 240 ILE D CA  1 
ATOM   8205  C C   . ILE D  1 240 ? -3.167  38.955 -22.093 1.00 50.50  ? 240 ILE D C   1 
ATOM   8206  O O   . ILE D  1 240 ? -3.189  37.751 -21.765 1.00 48.60  ? 240 ILE D O   1 
ATOM   8207  C CB  . ILE D  1 240 ? -5.219  40.457 -22.089 1.00 52.08  ? 240 ILE D CB  1 
ATOM   8208  C CG1 . ILE D  1 240 ? -6.244  41.143 -21.183 1.00 52.76  ? 240 ILE D CG1 1 
ATOM   8209  C CG2 . ILE D  1 240 ? -5.843  39.328 -22.896 1.00 48.60  ? 240 ILE D CG2 1 
ATOM   8210  C CD1 . ILE D  1 240 ? -7.415  41.743 -21.924 1.00 56.88  ? 240 ILE D CD1 1 
ATOM   8211  N N   . VAL D  1 241 ? -2.461  39.443 -23.116 1.00 50.02  ? 241 VAL D N   1 
ATOM   8212  C CA  . VAL D  1 241 ? -1.646  38.603 -24.043 1.00 51.43  ? 241 VAL D CA  1 
ATOM   8213  C C   . VAL D  1 241 ? -0.597  37.851 -23.231 1.00 51.90  ? 241 VAL D C   1 
ATOM   8214  O O   . VAL D  1 241 ? -0.501  36.627 -23.312 1.00 56.21  ? 241 VAL D O   1 
ATOM   8215  C CB  . VAL D  1 241 ? -0.990  39.451 -25.149 1.00 54.77  ? 241 VAL D CB  1 
ATOM   8216  C CG1 . VAL D  1 241 ? 0.067   38.664 -25.907 1.00 58.73  ? 241 VAL D CG1 1 
ATOM   8217  C CG2 . VAL D  1 241 ? -2.021  40.022 -26.108 1.00 59.74  ? 241 VAL D CG2 1 
ATOM   8218  N N   . LYS D  1 242 ? 0.178   38.604 -22.444 1.00 53.02  ? 242 LYS D N   1 
ATOM   8219  C CA  . LYS D  1 242 ? 1.352   38.071 -21.773 1.00 50.65  ? 242 LYS D CA  1 
ATOM   8220  C C   . LYS D  1 242 ? 0.936   37.044 -20.722 1.00 49.78  ? 242 LYS D C   1 
ATOM   8221  O O   . LYS D  1 242 ? 1.520   35.967 -20.658 1.00 49.67  ? 242 LYS D O   1 
ATOM   8222  C CB  . LYS D  1 242 ? 2.174   39.211 -21.163 1.00 50.02  ? 242 LYS D CB  1 
ATOM   8223  C CG  . LYS D  1 242 ? 2.901   40.096 -22.170 1.00 52.66  ? 242 LYS D CG  1 
ATOM   8224  C CD  . LYS D  1 242 ? 3.688   41.228 -21.530 1.00 56.95  ? 242 LYS D CD  1 
ATOM   8225  C CE  . LYS D  1 242 ? 4.171   42.295 -22.502 1.00 60.44  ? 242 LYS D CE  1 
ATOM   8226  N NZ  . LYS D  1 242 ? 4.555   41.739 -23.805 1.00 58.63  ? 242 LYS D NZ  1 
ATOM   8227  N N   . LEU D  1 243 ? -0.072  37.380 -19.906 1.00 51.94  ? 243 LEU D N   1 
ATOM   8228  C CA  . LEU D  1 243 ? -0.534  36.512 -18.832 1.00 52.71  ? 243 LEU D CA  1 
ATOM   8229  C C   . LEU D  1 243 ? -1.438  35.408 -19.396 1.00 54.34  ? 243 LEU D C   1 
ATOM   8230  O O   . LEU D  1 243 ? -1.291  34.242 -18.968 1.00 63.84  ? 243 LEU D O   1 
ATOM   8231  C CB  . LEU D  1 243 ? -1.294  37.352 -17.799 1.00 53.39  ? 243 LEU D CB  1 
ATOM   8232  C CG  . LEU D  1 243 ? -0.530  37.727 -16.527 1.00 55.15  ? 243 LEU D CG  1 
ATOM   8233  C CD1 . LEU D  1 243 ? 0.948   37.957 -16.807 1.00 54.45  ? 243 LEU D CD1 1 
ATOM   8234  C CD2 . LEU D  1 243 ? -1.144  38.961 -15.879 1.00 54.34  ? 243 LEU D CD2 1 
ATOM   8235  N N   . GLY D  1 244 ? -2.355  35.773 -20.296 1.00 53.63  ? 244 GLY D N   1 
ATOM   8236  C CA  . GLY D  1 244 ? -3.251  34.823 -20.982 1.00 51.20  ? 244 GLY D CA  1 
ATOM   8237  C C   . GLY D  1 244 ? -2.455  33.734 -21.679 1.00 53.15  ? 244 GLY D C   1 
ATOM   8238  O O   . GLY D  1 244 ? -2.617  32.552 -21.314 1.00 53.01  ? 244 GLY D O   1 
ATOM   8239  N N   . PHE D  1 245 ? -1.607  34.127 -22.633 1.00 54.26  ? 245 PHE D N   1 
ATOM   8240  C CA  . PHE D  1 245 ? -0.731  33.230 -23.432 1.00 56.99  ? 245 PHE D CA  1 
ATOM   8241  C C   . PHE D  1 245 ? 0.154   32.398 -22.498 1.00 57.76  ? 245 PHE D C   1 
ATOM   8242  O O   . PHE D  1 245 ? 0.148   31.158 -22.614 1.00 64.67  ? 245 PHE D O   1 
ATOM   8243  C CB  . PHE D  1 245 ? 0.120   34.047 -24.407 1.00 60.01  ? 245 PHE D CB  1 
ATOM   8244  C CG  . PHE D  1 245 ? 1.288   33.307 -25.009 1.00 63.97  ? 245 PHE D CG  1 
ATOM   8245  C CD1 . PHE D  1 245 ? 2.576   33.533 -24.553 1.00 63.59  ? 245 PHE D CD1 1 
ATOM   8246  C CD2 . PHE D  1 245 ? 1.105   32.392 -26.035 1.00 67.00  ? 245 PHE D CD2 1 
ATOM   8247  C CE1 . PHE D  1 245 ? 3.654   32.864 -25.112 1.00 66.34  ? 245 PHE D CE1 1 
ATOM   8248  C CE2 . PHE D  1 245 ? 2.184   31.720 -26.589 1.00 68.21  ? 245 PHE D CE2 1 
ATOM   8249  C CZ  . PHE D  1 245 ? 3.458   31.958 -26.129 1.00 65.44  ? 245 PHE D CZ  1 
ATOM   8250  N N   . SER D  1 246 ? 0.896   33.064 -21.609 1.00 56.30  ? 246 SER D N   1 
ATOM   8251  C CA  . SER D  1 246 ? 1.893   32.437 -20.702 1.00 57.18  ? 246 SER D CA  1 
ATOM   8252  C C   . SER D  1 246 ? 1.256   31.265 -19.944 1.00 59.80  ? 246 SER D C   1 
ATOM   8253  O O   . SER D  1 246 ? 1.850   30.166 -19.956 1.00 63.25  ? 246 SER D O   1 
ATOM   8254  C CB  . SER D  1 246 ? 2.486   33.450 -19.757 1.00 57.04  ? 246 SER D CB  1 
ATOM   8255  O OG  . SER D  1 246 ? 1.549   33.832 -18.761 1.00 63.84  ? 246 SER D OG  1 
ATOM   8256  N N   . THR D  1 247 ? 0.100   31.485 -19.311 1.00 59.75  ? 247 THR D N   1 
ATOM   8257  C CA  . THR D  1 247 ? -0.640  30.448 -18.540 1.00 65.55  ? 247 THR D CA  1 
ATOM   8258  C C   . THR D  1 247 ? -0.856  29.213 -19.423 1.00 66.22  ? 247 THR D C   1 
ATOM   8259  O O   . THR D  1 247 ? -0.757  28.087 -18.899 1.00 62.72  ? 247 THR D O   1 
ATOM   8260  C CB  . THR D  1 247 ? -1.987  30.965 -18.020 1.00 65.06  ? 247 THR D CB  1 
ATOM   8261  O OG1 . THR D  1 247 ? -1.767  32.192 -17.324 1.00 70.19  ? 247 THR D OG1 1 
ATOM   8262  C CG2 . THR D  1 247 ? -2.668  29.972 -17.102 1.00 63.56  ? 247 THR D CG2 1 
ATOM   8263  N N   . GLN D  1 248 ? -1.137  29.430 -20.711 1.00 69.12  ? 248 GLN D N   1 
ATOM   8264  C CA  . GLN D  1 248 ? -1.474  28.367 -21.695 1.00 67.31  ? 248 GLN D CA  1 
ATOM   8265  C C   . GLN D  1 248 ? -0.234  27.516 -21.993 1.00 62.65  ? 248 GLN D C   1 
ATOM   8266  O O   . GLN D  1 248 ? -0.323  26.284 -21.837 1.00 57.16  ? 248 GLN D O   1 
ATOM   8267  C CB  . GLN D  1 248 ? -2.044  28.994 -22.967 1.00 72.31  ? 248 GLN D CB  1 
ATOM   8268  C CG  . GLN D  1 248 ? -3.419  29.613 -22.764 1.00 72.41  ? 248 GLN D CG  1 
ATOM   8269  C CD  . GLN D  1 248 ? -4.472  28.567 -22.493 1.00 79.34  ? 248 GLN D CD  1 
ATOM   8270  O OE1 . GLN D  1 248 ? -4.684  27.652 -23.286 1.00 100.15 ? 248 GLN D OE1 1 
ATOM   8271  N NE2 . GLN D  1 248 ? -5.147  28.697 -21.361 1.00 82.72  ? 248 GLN D NE2 1 
ATOM   8272  N N   . THR D  1 249 ? 0.873   28.141 -22.409 1.00 62.19  ? 249 THR D N   1 
ATOM   8273  C CA  . THR D  1 249 ? 2.145   27.451 -22.759 1.00 69.97  ? 249 THR D CA  1 
ATOM   8274  C C   . THR D  1 249 ? 2.627   26.629 -21.559 1.00 64.94  ? 249 THR D C   1 
ATOM   8275  O O   . THR D  1 249 ? 3.235   25.561 -21.775 1.00 56.83  ? 249 THR D O   1 
ATOM   8276  C CB  . THR D  1 249 ? 3.228   28.439 -23.206 1.00 78.60  ? 249 THR D CB  1 
ATOM   8277  O OG1 . THR D  1 249 ? 3.419   29.395 -22.162 1.00 76.82  ? 249 THR D OG1 1 
ATOM   8278  C CG2 . THR D  1 249 ? 2.877   29.141 -24.499 1.00 80.14  ? 249 THR D CG2 1 
ATOM   8279  N N   . HIS D  1 250 ? 2.370   27.116 -20.343 1.00 60.65  ? 250 HIS D N   1 
ATOM   8280  C CA  . HIS D  1 250 ? 2.671   26.397 -19.079 1.00 65.06  ? 250 HIS D CA  1 
ATOM   8281  C C   . HIS D  1 250 ? 1.859   25.097 -19.042 1.00 65.50  ? 250 HIS D C   1 
ATOM   8282  O O   . HIS D  1 250 ? 2.479   24.016 -18.966 1.00 65.86  ? 250 HIS D O   1 
ATOM   8283  C CB  . HIS D  1 250 ? 2.398   27.300 -17.870 1.00 63.09  ? 250 HIS D CB  1 
ATOM   8284  C CG  . HIS D  1 250 ? 2.871   26.719 -16.583 1.00 60.78  ? 250 HIS D CG  1 
ATOM   8285  N ND1 . HIS D  1 250 ? 4.206   26.467 -16.339 1.00 53.62  ? 250 HIS D ND1 1 
ATOM   8286  C CD2 . HIS D  1 250 ? 2.198   26.339 -15.475 1.00 63.27  ? 250 HIS D CD2 1 
ATOM   8287  C CE1 . HIS D  1 250 ? 4.336   25.951 -15.134 1.00 59.79  ? 250 HIS D CE1 1 
ATOM   8288  N NE2 . HIS D  1 250 ? 3.117   25.861 -14.584 1.00 58.46  ? 250 HIS D NE2 1 
ATOM   8289  N N   . ARG D  1 251 ? 0.528   25.207 -19.114 1.00 57.53  ? 251 ARG D N   1 
ATOM   8290  C CA  . ARG D  1 251 ? -0.414  24.054 -19.123 1.00 52.10  ? 251 ARG D CA  1 
ATOM   8291  C C   . ARG D  1 251 ? 0.070   23.018 -20.146 1.00 50.10  ? 251 ARG D C   1 
ATOM   8292  O O   . ARG D  1 251 ? -0.022  21.812 -19.853 1.00 50.61  ? 251 ARG D O   1 
ATOM   8293  C CB  . ARG D  1 251 ? -1.840  24.528 -19.427 1.00 44.60  ? 251 ARG D CB  1 
ATOM   8294  N N   . VAL D  1 252 ? 0.579   23.473 -21.296 1.00 48.93  ? 252 VAL D N   1 
ATOM   8295  C CA  . VAL D  1 252 ? 1.117   22.602 -22.385 1.00 53.76  ? 252 VAL D CA  1 
ATOM   8296  C C   . VAL D  1 252 ? 2.315   21.818 -21.843 1.00 51.78  ? 252 VAL D C   1 
ATOM   8297  O O   . VAL D  1 252 ? 2.239   20.572 -21.801 1.00 53.45  ? 252 VAL D O   1 
ATOM   8298  C CB  . VAL D  1 252 ? 1.516   23.422 -23.627 1.00 62.50  ? 252 VAL D CB  1 
ATOM   8299  C CG1 . VAL D  1 252 ? 2.218   22.561 -24.666 1.00 59.76  ? 252 VAL D CG1 1 
ATOM   8300  C CG2 . VAL D  1 252 ? 0.321   24.134 -24.240 1.00 68.06  ? 252 VAL D CG2 1 
ATOM   8301  N N   . ALA D  1 253 ? 3.377   22.530 -21.454 1.00 57.00  ? 253 ALA D N   1 
ATOM   8302  C CA  . ALA D  1 253 ? 4.655   21.967 -20.956 1.00 59.15  ? 253 ALA D CA  1 
ATOM   8303  C C   . ALA D  1 253 ? 4.375   20.869 -19.923 1.00 59.31  ? 253 ALA D C   1 
ATOM   8304  O O   . ALA D  1 253 ? 5.054   19.827 -19.972 1.00 59.26  ? 253 ALA D O   1 
ATOM   8305  C CB  . ALA D  1 253 ? 5.509   23.065 -20.371 1.00 60.71  ? 253 ALA D CB  1 
ATOM   8306  N N   . LYS D  1 254 ? 3.414   21.104 -19.024 1.00 58.43  ? 254 LYS D N   1 
ATOM   8307  C CA  . LYS D  1 254 ? 3.030   20.164 -17.937 1.00 54.74  ? 254 LYS D CA  1 
ATOM   8308  C C   . LYS D  1 254 ? 2.423   18.898 -18.552 1.00 57.56  ? 254 LYS D C   1 
ATOM   8309  O O   . LYS D  1 254 ? 2.858   17.792 -18.175 1.00 59.57  ? 254 LYS D O   1 
ATOM   8310  C CB  . LYS D  1 254 ? 2.053   20.838 -16.970 1.00 52.58  ? 254 LYS D CB  1 
ATOM   8311  C CG  . LYS D  1 254 ? 2.659   21.943 -16.115 1.00 53.20  ? 254 LYS D CG  1 
ATOM   8312  C CD  . LYS D  1 254 ? 1.653   22.658 -15.239 1.00 53.55  ? 254 LYS D CD  1 
ATOM   8313  C CE  . LYS D  1 254 ? 1.128   21.799 -14.109 1.00 48.79  ? 254 LYS D CE  1 
ATOM   8314  N NZ  . LYS D  1 254 ? 0.062   22.495 -13.350 1.00 46.35  ? 254 LYS D NZ  1 
ATOM   8315  N N   . LEU D  1 255 ? 1.455   19.062 -19.459 1.00 65.09  ? 255 LEU D N   1 
ATOM   8316  C CA  . LEU D  1 255 ? 0.788   17.948 -20.186 1.00 63.08  ? 255 LEU D CA  1 
ATOM   8317  C C   . LEU D  1 255 ? 1.849   17.103 -20.900 1.00 57.19  ? 255 LEU D C   1 
ATOM   8318  O O   . LEU D  1 255 ? 1.846   15.872 -20.713 1.00 58.35  ? 255 LEU D O   1 
ATOM   8319  C CB  . LEU D  1 255 ? -0.225  18.524 -21.179 1.00 68.71  ? 255 LEU D CB  1 
ATOM   8320  C CG  . LEU D  1 255 ? -1.687  18.446 -20.739 1.00 74.36  ? 255 LEU D CG  1 
ATOM   8321  C CD1 . LEU D  1 255 ? -2.559  19.358 -21.589 1.00 73.93  ? 255 LEU D CD1 1 
ATOM   8322  C CD2 . LEU D  1 255 ? -2.196  17.012 -20.795 1.00 83.18  ? 255 LEU D CD2 1 
ATOM   8323  N N   . ARG D  1 256 ? 2.724   17.751 -21.674 1.00 50.44  ? 256 ARG D N   1 
ATOM   8324  C CA  . ARG D  1 256 ? 3.809   17.094 -22.450 1.00 52.15  ? 256 ARG D CA  1 
ATOM   8325  C C   . ARG D  1 256 ? 4.774   16.389 -21.489 1.00 52.99  ? 256 ARG D C   1 
ATOM   8326  O O   . ARG D  1 256 ? 5.246   15.286 -21.832 1.00 58.84  ? 256 ARG D O   1 
ATOM   8327  C CB  . ARG D  1 256 ? 4.535   18.130 -23.311 1.00 56.85  ? 256 ARG D CB  1 
ATOM   8328  C CG  . ARG D  1 256 ? 3.735   18.583 -24.523 1.00 59.58  ? 256 ARG D CG  1 
ATOM   8329  C CD  . ARG D  1 256 ? 4.265   17.970 -25.804 1.00 62.02  ? 256 ARG D CD  1 
ATOM   8330  N NE  . ARG D  1 256 ? 5.204   18.858 -26.474 1.00 65.10  ? 256 ARG D NE  1 
ATOM   8331  C CZ  . ARG D  1 256 ? 6.084   18.475 -27.392 1.00 74.31  ? 256 ARG D CZ  1 
ATOM   8332  N NH1 . ARG D  1 256 ? 6.164   17.204 -27.750 1.00 71.27  ? 256 ARG D NH1 1 
ATOM   8333  N NH2 . ARG D  1 256 ? 6.892   19.364 -27.940 1.00 82.76  ? 256 ARG D NH2 1 
ATOM   8334  N N   . THR D  1 257 ? 5.053   17.002 -20.334 1.00 54.55  ? 257 THR D N   1 
ATOM   8335  C CA  . THR D  1 257 ? 5.922   16.440 -19.265 1.00 53.31  ? 257 THR D CA  1 
ATOM   8336  C C   . THR D  1 257 ? 5.262   15.181 -18.693 1.00 54.19  ? 257 THR D C   1 
ATOM   8337  O O   . THR D  1 257 ? 5.945   14.142 -18.616 1.00 51.44  ? 257 THR D O   1 
ATOM   8338  C CB  . THR D  1 257 ? 6.194   17.464 -18.156 1.00 51.34  ? 257 THR D CB  1 
ATOM   8339  O OG1 . THR D  1 257 ? 6.876   18.580 -18.729 1.00 57.45  ? 257 THR D OG1 1 
ATOM   8340  C CG2 . THR D  1 257 ? 7.019   16.896 -17.023 1.00 50.31  ? 257 THR D CG2 1 
ATOM   8341  N N   . ALA D  1 258 ? 3.986   15.287 -18.307 1.00 55.62  ? 258 ALA D N   1 
ATOM   8342  C CA  . ALA D  1 258 ? 3.169   14.190 -17.738 1.00 56.73  ? 258 ALA D CA  1 
ATOM   8343  C C   . ALA D  1 258 ? 3.120   13.022 -18.731 1.00 59.96  ? 258 ALA D C   1 
ATOM   8344  O O   . ALA D  1 258 ? 3.305   11.866 -18.299 1.00 56.65  ? 258 ALA D O   1 
ATOM   8345  C CB  . ALA D  1 258 ? 1.787   14.697 -17.409 1.00 52.78  ? 258 ALA D CB  1 
ATOM   8346  N N   . GLU D  1 259 ? 2.882   13.321 -20.011 1.00 61.71  ? 259 GLU D N   1 
ATOM   8347  C CA  . GLU D  1 259 ? 2.811   12.321 -21.109 1.00 62.04  ? 259 GLU D CA  1 
ATOM   8348  C C   . GLU D  1 259 ? 4.113   11.516 -21.141 1.00 60.60  ? 259 GLU D C   1 
ATOM   8349  O O   . GLU D  1 259 ? 4.035   10.273 -21.075 1.00 64.65  ? 259 GLU D O   1 
ATOM   8350  C CB  . GLU D  1 259 ? 2.551   13.016 -22.445 1.00 65.81  ? 259 GLU D CB  1 
ATOM   8351  C CG  . GLU D  1 259 ? 1.120   13.499 -22.587 1.00 74.79  ? 259 GLU D CG  1 
ATOM   8352  C CD  . GLU D  1 259 ? 0.844   14.333 -23.824 1.00 84.75  ? 259 GLU D CD  1 
ATOM   8353  O OE1 . GLU D  1 259 ? 1.775   14.525 -24.632 1.00 95.74  ? 259 GLU D OE1 1 
ATOM   8354  O OE2 . GLU D  1 259 ? -0.308  14.785 -23.976 1.00 87.86  ? 259 GLU D OE2 1 
ATOM   8355  N N   . ASP D  1 260 ? 5.255   12.204 -21.227 1.00 57.33  ? 260 ASP D N   1 
ATOM   8356  C CA  . ASP D  1 260 ? 6.608   11.586 -21.260 1.00 65.89  ? 260 ASP D CA  1 
ATOM   8357  C C   . ASP D  1 260 ? 6.753   10.628 -20.070 1.00 66.27  ? 260 ASP D C   1 
ATOM   8358  O O   . ASP D  1 260 ? 7.312   9.528  -20.260 1.00 73.69  ? 260 ASP D O   1 
ATOM   8359  C CB  . ASP D  1 260 ? 7.707   12.652 -21.250 1.00 78.78  ? 260 ASP D CB  1 
ATOM   8360  C CG  . ASP D  1 260 ? 7.829   13.427 -22.552 1.00 86.87  ? 260 ASP D CG  1 
ATOM   8361  O OD1 . ASP D  1 260 ? 8.680   14.338 -22.612 1.00 84.52  ? 260 ASP D OD1 1 
ATOM   8362  O OD2 . ASP D  1 260 ? 7.074   13.113 -23.494 1.00 94.90  ? 260 ASP D OD2 1 
ATOM   8363  N N   . VAL D  1 261 ? 6.267   11.033 -18.892 1.00 60.26  ? 261 VAL D N   1 
ATOM   8364  C CA  . VAL D  1 261 ? 6.329   10.231 -17.634 1.00 57.24  ? 261 VAL D CA  1 
ATOM   8365  C C   . VAL D  1 261 ? 5.482   8.966  -17.816 1.00 55.73  ? 261 VAL D C   1 
ATOM   8366  O O   . VAL D  1 261 ? 5.998   7.868  -17.533 1.00 55.44  ? 261 VAL D O   1 
ATOM   8367  C CB  . VAL D  1 261 ? 5.866   11.049 -16.413 1.00 56.88  ? 261 VAL D CB  1 
ATOM   8368  C CG1 . VAL D  1 261 ? 5.632   10.170 -15.194 1.00 56.49  ? 261 VAL D CG1 1 
ATOM   8369  C CG2 . VAL D  1 261 ? 6.841   12.168 -16.084 1.00 58.42  ? 261 VAL D CG2 1 
ATOM   8370  N N   . ARG D  1 262 ? 4.235   9.121  -18.273 1.00 55.96  ? 262 ARG D N   1 
ATOM   8371  C CA  . ARG D  1 262 ? 3.269   8.005  -18.466 1.00 55.80  ? 262 ARG D CA  1 
ATOM   8372  C C   . ARG D  1 262 ? 3.801   7.048  -19.540 1.00 60.71  ? 262 ARG D C   1 
ATOM   8373  O O   . ARG D  1 262 ? 3.697   5.825  -19.337 1.00 62.81  ? 262 ARG D O   1 
ATOM   8374  C CB  . ARG D  1 262 ? 1.885   8.534  -18.853 1.00 54.19  ? 262 ARG D CB  1 
ATOM   8375  C CG  . ARG D  1 262 ? 1.126   9.196  -17.711 1.00 55.94  ? 262 ARG D CG  1 
ATOM   8376  C CD  . ARG D  1 262 ? -0.349  9.378  -18.022 1.00 59.32  ? 262 ARG D CD  1 
ATOM   8377  N NE  . ARG D  1 262 ? -0.575  10.093 -19.272 1.00 67.12  ? 262 ARG D NE  1 
ATOM   8378  C CZ  . ARG D  1 262 ? -0.811  11.399 -19.373 1.00 72.78  ? 262 ARG D CZ  1 
ATOM   8379  N NH1 . ARG D  1 262 ? -0.860  12.156 -18.290 1.00 81.51  ? 262 ARG D NH1 1 
ATOM   8380  N NH2 . ARG D  1 262 ? -0.997  11.944 -20.562 1.00 78.92  ? 262 ARG D NH2 1 
ATOM   8381  N N   . ALA D  1 263 ? 4.342   7.590  -20.635 1.00 60.40  ? 263 ALA D N   1 
ATOM   8382  C CA  . ALA D  1 263 ? 4.906   6.826  -21.773 1.00 55.17  ? 263 ALA D CA  1 
ATOM   8383  C C   . ALA D  1 263 ? 6.204   6.136  -21.338 1.00 62.07  ? 263 ALA D C   1 
ATOM   8384  O O   . ALA D  1 263 ? 6.749   5.344  -22.134 1.00 67.98  ? 263 ALA D O   1 
ATOM   8385  C CB  . ALA D  1 263 ? 5.136   7.746  -22.946 1.00 55.85  ? 263 ALA D CB  1 
ATOM   8386  N N   . GLY D  1 264 ? 6.675   6.432  -20.122 1.00 64.98  ? 264 GLY D N   1 
ATOM   8387  C CA  . GLY D  1 264 ? 7.898   5.853  -19.532 1.00 64.18  ? 264 GLY D CA  1 
ATOM   8388  C C   . GLY D  1 264 ? 9.149   6.323  -20.255 1.00 65.33  ? 264 GLY D C   1 
ATOM   8389  O O   . GLY D  1 264 ? 10.162  5.600  -20.206 1.00 64.31  ? 264 GLY D O   1 
ATOM   8390  N N   . ASP D  1 265 ? 9.082   7.490  -20.903 1.00 73.67  ? 265 ASP D N   1 
ATOM   8391  C CA  . ASP D  1 265 ? 10.213  8.110  -21.647 1.00 77.78  ? 265 ASP D CA  1 
ATOM   8392  C C   . ASP D  1 265 ? 11.138  8.822  -20.654 1.00 74.84  ? 265 ASP D C   1 
ATOM   8393  O O   . ASP D  1 265 ? 12.348  8.913  -20.935 1.00 79.12  ? 265 ASP D O   1 
ATOM   8394  C CB  . ASP D  1 265 ? 9.716   9.092  -22.712 1.00 81.43  ? 265 ASP D CB  1 
ATOM   8395  C CG  . ASP D  1 265 ? 9.023   8.432  -23.891 1.00 82.90  ? 265 ASP D CG  1 
ATOM   8396  O OD1 . ASP D  1 265 ? 9.384   7.283  -24.213 1.00 91.95  ? 265 ASP D OD1 1 
ATOM   8397  O OD2 . ASP D  1 265 ? 8.130   9.075  -24.480 1.00 78.78  ? 265 ASP D OD2 1 
ATOM   8398  N N   . ASP D  1 266 ? 10.579  9.312  -19.544 1.00 70.42  ? 266 ASP D N   1 
ATOM   8399  C CA  . ASP D  1 266 ? 11.305  10.097 -18.510 1.00 69.98  ? 266 ASP D CA  1 
ATOM   8400  C C   . ASP D  1 266 ? 10.572  9.947  -17.174 1.00 61.40  ? 266 ASP D C   1 
ATOM   8401  O O   . ASP D  1 266 ? 9.547   9.241  -17.142 1.00 55.56  ? 266 ASP D O   1 
ATOM   8402  C CB  . ASP D  1 266 ? 11.426  11.568 -18.922 1.00 76.77  ? 266 ASP D CB  1 
ATOM   8403  C CG  . ASP D  1 266 ? 12.707  12.242 -18.455 1.00 78.50  ? 266 ASP D CG  1 
ATOM   8404  O OD1 . ASP D  1 266 ? 13.244  13.069 -19.221 1.00 74.09  ? 266 ASP D OD1 1 
ATOM   8405  O OD2 . ASP D  1 266 ? 13.160  11.934 -17.335 1.00 69.84  ? 266 ASP D OD2 1 
ATOM   8406  N N   . VAL D  1 267 ? 11.086  10.588 -16.121 1.00 60.80  ? 267 VAL D N   1 
ATOM   8407  C CA  . VAL D  1 267 ? 10.535  10.527 -14.734 1.00 58.27  ? 267 VAL D CA  1 
ATOM   8408  C C   . VAL D  1 267 ? 10.533  11.945 -14.147 1.00 51.52  ? 267 VAL D C   1 
ATOM   8409  O O   . VAL D  1 267 ? 11.399  12.746 -14.544 1.00 43.29  ? 267 VAL D O   1 
ATOM   8410  C CB  . VAL D  1 267 ? 11.339  9.537  -13.867 1.00 55.03  ? 267 VAL D CB  1 
ATOM   8411  C CG1 . VAL D  1 267 ? 12.823  9.874  -13.837 1.00 49.59  ? 267 VAL D CG1 1 
ATOM   8412  C CG2 . VAL D  1 267 ? 10.781  9.441  -12.458 1.00 62.97  ? 267 VAL D CG2 1 
ATOM   8413  N N   . HIS D  1 268 ? 9.581   12.244 -13.256 1.00 50.07  ? 268 HIS D N   1 
ATOM   8414  C CA  . HIS D  1 268 ? 9.420   13.562 -12.583 1.00 49.14  ? 268 HIS D CA  1 
ATOM   8415  C C   . HIS D  1 268 ? 9.241   13.343 -11.083 1.00 51.78  ? 268 HIS D C   1 
ATOM   8416  O O   . HIS D  1 268 ? 8.414   12.535 -10.665 1.00 52.56  ? 268 HIS D O   1 
ATOM   8417  C CB  . HIS D  1 268 ? 8.255   14.345 -13.204 1.00 50.16  ? 268 HIS D CB  1 
ATOM   8418  C CG  . HIS D  1 268 ? 8.343   15.818 -12.989 1.00 50.56  ? 268 HIS D CG  1 
ATOM   8419  N ND1 . HIS D  1 268 ? 7.501   16.490 -12.125 1.00 45.97  ? 268 HIS D ND1 1 
ATOM   8420  C CD2 . HIS D  1 268 ? 9.171   16.747 -13.514 1.00 55.52  ? 268 HIS D CD2 1 
ATOM   8421  C CE1 . HIS D  1 268 ? 7.803   17.772 -12.131 1.00 50.68  ? 268 HIS D CE1 1 
ATOM   8422  N NE2 . HIS D  1 268 ? 8.826   17.956 -12.974 1.00 55.19  ? 268 HIS D NE2 1 
ATOM   8423  N N   . PRO D  1 269 ? 9.999   14.069 -10.230 1.00 54.54  ? 269 PRO D N   1 
ATOM   8424  C CA  . PRO D  1 269 ? 10.081  13.750 -8.803  1.00 53.93  ? 269 PRO D CA  1 
ATOM   8425  C C   . PRO D  1 269 ? 8.841   14.135 -7.979  1.00 51.59  ? 269 PRO D C   1 
ATOM   8426  O O   . PRO D  1 269 ? 8.800   13.802 -6.808  1.00 53.04  ? 269 PRO D O   1 
ATOM   8427  C CB  . PRO D  1 269 ? 11.304  14.559 -8.350  1.00 55.15  ? 269 PRO D CB  1 
ATOM   8428  C CG  . PRO D  1 269 ? 11.303  15.765 -9.266  1.00 58.05  ? 269 PRO D CG  1 
ATOM   8429  C CD  . PRO D  1 269 ? 10.813  15.238 -10.598 1.00 57.11  ? 269 PRO D CD  1 
ATOM   8430  N N   . GLU D  1 270 ? 7.870   14.811 -8.598  1.00 53.21  ? 270 GLU D N   1 
ATOM   8431  C CA  . GLU D  1 270 ? 6.585   15.208 -7.958  1.00 51.38  ? 270 GLU D CA  1 
ATOM   8432  C C   . GLU D  1 270 ? 5.424   14.853 -8.894  1.00 47.45  ? 270 GLU D C   1 
ATOM   8433  O O   . GLU D  1 270 ? 5.654   14.762 -10.118 1.00 45.75  ? 270 GLU D O   1 
ATOM   8434  C CB  . GLU D  1 270 ? 6.578   16.705 -7.634  1.00 55.13  ? 270 GLU D CB  1 
ATOM   8435  C CG  . GLU D  1 270 ? 6.327   17.589 -8.845  1.00 63.14  ? 270 GLU D CG  1 
ATOM   8436  C CD  . GLU D  1 270 ? 6.213   19.076 -8.547  1.00 70.15  ? 270 GLU D CD  1 
ATOM   8437  O OE1 . GLU D  1 270 ? 6.591   19.484 -7.430  1.00 71.53  ? 270 GLU D OE1 1 
ATOM   8438  O OE2 . GLU D  1 270 ? 5.744   19.825 -9.433  1.00 65.75  ? 270 GLU D OE2 1 
ATOM   8439  N N   . SER D  1 271 ? 4.227   14.657 -8.336  1.00 48.86  ? 271 SER D N   1 
ATOM   8440  C CA  . SER D  1 271 ? 2.970   14.427 -9.094  1.00 53.58  ? 271 SER D CA  1 
ATOM   8441  C C   . SER D  1 271 ? 2.573   15.721 -9.814  1.00 56.43  ? 271 SER D C   1 
ATOM   8442  O O   . SER D  1 271 ? 2.682   16.800 -9.195  1.00 57.39  ? 271 SER D O   1 
ATOM   8443  C CB  . SER D  1 271 ? 1.867   13.938 -8.192  1.00 54.24  ? 271 SER D CB  1 
ATOM   8444  O OG  . SER D  1 271 ? 1.848   14.670 -6.974  1.00 54.77  ? 271 SER D OG  1 
ATOM   8445  N N   . ILE D  1 272 ? 2.143   15.614 -11.074 1.00 55.93  ? 272 ILE D N   1 
ATOM   8446  C CA  . ILE D  1 272 ? 1.720   16.769 -11.920 1.00 53.16  ? 272 ILE D CA  1 
ATOM   8447  C C   . ILE D  1 272 ? 0.189   16.804 -11.970 1.00 57.38  ? 272 ILE D C   1 
ATOM   8448  O O   . ILE D  1 272 ? -0.417  15.750 -12.246 1.00 66.00  ? 272 ILE D O   1 
ATOM   8449  C CB  . ILE D  1 272 ? 2.341   16.680 -13.328 1.00 51.15  ? 272 ILE D CB  1 
ATOM   8450  C CG1 . ILE D  1 272 ? 3.870   16.699 -13.269 1.00 50.59  ? 272 ILE D CG1 1 
ATOM   8451  C CG2 . ILE D  1 272 ? 1.795   17.781 -14.224 1.00 52.15  ? 272 ILE D CG2 1 
ATOM   8452  C CD1 . ILE D  1 272 ? 4.543   16.471 -14.603 1.00 49.75  ? 272 ILE D CD1 1 
ATOM   8453  N N   . TRP D  1 273 ? -0.399  17.975 -11.708 1.00 61.78  ? 273 TRP D N   1 
ATOM   8454  C CA  . TRP D  1 273 ? -1.869  18.200 -11.664 1.00 63.82  ? 273 TRP D CA  1 
ATOM   8455  C C   . TRP D  1 273 ? -2.252  19.309 -12.649 1.00 70.62  ? 273 TRP D C   1 
ATOM   8456  O O   . TRP D  1 273 ? -1.410  20.190 -12.912 1.00 70.85  ? 273 TRP D O   1 
ATOM   8457  C CB  . TRP D  1 273 ? -2.320  18.542 -10.238 1.00 61.48  ? 273 TRP D CB  1 
ATOM   8458  C CG  . TRP D  1 273 ? -2.001  17.487 -9.224  1.00 64.83  ? 273 TRP D CG  1 
ATOM   8459  C CD1 . TRP D  1 273 ? -0.780  17.218 -8.677  1.00 69.82  ? 273 TRP D CD1 1 
ATOM   8460  C CD2 . TRP D  1 273 ? -2.922  16.560 -8.621  1.00 70.40  ? 273 TRP D CD2 1 
ATOM   8461  N NE1 . TRP D  1 273 ? -0.877  16.188 -7.781  1.00 79.38  ? 273 TRP D NE1 1 
ATOM   8462  C CE2 . TRP D  1 273 ? -2.177  15.762 -7.727  1.00 77.05  ? 273 TRP D CE2 1 
ATOM   8463  C CE3 . TRP D  1 273 ? -4.294  16.323 -8.752  1.00 72.49  ? 273 TRP D CE3 1 
ATOM   8464  C CZ2 . TRP D  1 273 ? -2.763  14.748 -6.971  1.00 82.37  ? 273 TRP D CZ2 1 
ATOM   8465  C CZ3 . TRP D  1 273 ? -4.871  15.320 -8.005  1.00 75.38  ? 273 TRP D CZ3 1 
ATOM   8466  C CH2 . TRP D  1 273 ? -4.114  14.544 -7.128  1.00 79.38  ? 273 TRP D CH2 1 
ATOM   8467  N N   . ILE D  1 274 ? -3.478  19.249 -13.174 1.00 81.84  ? 274 ILE D N   1 
ATOM   8468  C CA  . ILE D  1 274 ? -4.101  20.310 -14.019 1.00 83.94  ? 274 ILE D CA  1 
ATOM   8469  C C   . ILE D  1 274 ? -5.586  20.394 -13.653 1.00 82.83  ? 274 ILE D C   1 
ATOM   8470  O O   . ILE D  1 274 ? -6.307  19.403 -13.883 1.00 78.24  ? 274 ILE D O   1 
ATOM   8471  C CB  . ILE D  1 274 ? -3.893  20.028 -15.520 1.00 85.76  ? 274 ILE D CB  1 
ATOM   8472  C CG1 . ILE D  1 274 ? -2.408  19.909 -15.876 1.00 85.08  ? 274 ILE D CG1 1 
ATOM   8473  C CG2 . ILE D  1 274 ? -4.594  21.081 -16.365 1.00 84.08  ? 274 ILE D CG2 1 
ATOM   8474  C CD1 . ILE D  1 274 ? -2.148  19.597 -17.331 1.00 82.59  ? 274 ILE D CD1 1 
ATOM   8475  N N   . SER D  1 275 ? -6.011  21.527 -13.088 1.00 89.25  ? 275 SER D N   1 
ATOM   8476  C CA  . SER D  1 275 ? -7.401  21.780 -12.628 1.00 97.09  ? 275 SER D CA  1 
ATOM   8477  C C   . SER D  1 275 ? -7.800  20.722 -11.594 1.00 89.96  ? 275 SER D C   1 
ATOM   8478  O O   . SER D  1 275 ? -8.983  20.330 -11.577 1.00 98.86  ? 275 SER D O   1 
ATOM   8479  C CB  . SER D  1 275 ? -8.359  21.800 -13.793 1.00 103.67 ? 275 SER D CB  1 
ATOM   8480  O OG  . SER D  1 275 ? -7.991  22.795 -14.737 1.00 103.33 ? 275 SER D OG  1 
ATOM   8481  N N   . SER D  1 276 ? -6.838  20.267 -10.784 1.00 86.96  ? 276 SER D N   1 
ATOM   8482  C CA  . SER D  1 276 ? -7.042  19.330 -9.647  1.00 99.51  ? 276 SER D CA  1 
ATOM   8483  C C   . SER D  1 276 ? -7.204  17.890 -10.151 1.00 98.68  ? 276 SER D C   1 
ATOM   8484  O O   . SER D  1 276 ? -7.597  17.025 -9.342  1.00 98.10  ? 276 SER D O   1 
ATOM   8485  C CB  . SER D  1 276 ? -8.227  19.750 -8.816  1.00 99.23  ? 276 SER D CB  1 
ATOM   8486  O OG  . SER D  1 276 ? -8.065  21.077 -8.339  1.00 101.74 ? 276 SER D OG  1 
ATOM   8487  N N   . VAL D  1 277 ? -6.911  17.647 -11.433 1.00 91.34  ? 277 VAL D N   1 
ATOM   8488  C CA  . VAL D  1 277 ? -6.918  16.289 -12.057 1.00 87.44  ? 277 VAL D CA  1 
ATOM   8489  C C   . VAL D  1 277 ? -5.467  15.834 -12.246 1.00 82.17  ? 277 VAL D C   1 
ATOM   8490  O O   . VAL D  1 277 ? -4.732  16.498 -13.011 1.00 67.15  ? 277 VAL D O   1 
ATOM   8491  C CB  . VAL D  1 277 ? -7.687  16.281 -13.392 1.00 92.01  ? 277 VAL D CB  1 
ATOM   8492  C CG1 . VAL D  1 277 ? -7.641  14.914 -14.060 1.00 87.68  ? 277 VAL D CG1 1 
ATOM   8493  C CG2 . VAL D  1 277 ? -9.124  16.748 -13.216 1.00 94.74  ? 277 VAL D CG2 1 
ATOM   8494  N N   . LYS D  1 278 ? -5.077  14.746 -11.573 1.00 78.21  ? 278 LYS D N   1 
ATOM   8495  C CA  . LYS D  1 278 ? -3.705  14.175 -11.623 1.00 71.99  ? 278 LYS D CA  1 
ATOM   8496  C C   . LYS D  1 278 ? -3.397  13.748 -13.062 1.00 65.13  ? 278 LYS D C   1 
ATOM   8497  O O   . LYS D  1 278 ? -4.289  13.167 -13.711 1.00 75.34  ? 278 LYS D O   1 
ATOM   8498  C CB  . LYS D  1 278 ? -3.568  12.998 -10.652 1.00 70.12  ? 278 LYS D CB  1 
ATOM   8499  C CG  . LYS D  1 278 ? -2.189  12.353 -10.618 1.00 73.43  ? 278 LYS D CG  1 
ATOM   8500  C CD  . LYS D  1 278 ? -2.080  11.203 -9.644  1.00 78.39  ? 278 LYS D CD  1 
ATOM   8501  C CE  . LYS D  1 278 ? -2.022  11.657 -8.201  1.00 82.87  ? 278 LYS D CE  1 
ATOM   8502  N NZ  . LYS D  1 278 ? -1.377  10.639 -7.338  1.00 86.41  ? 278 LYS D NZ  1 
ATOM   8503  N N   . GLN D  1 279 ? -2.177  14.030 -13.528 1.00 62.15  ? 279 GLN D N   1 
ATOM   8504  C CA  . GLN D  1 279 ? -1.707  13.736 -14.908 1.00 66.00  ? 279 GLN D CA  1 
ATOM   8505  C C   . GLN D  1 279 ? -0.610  12.668 -14.852 1.00 68.95  ? 279 GLN D C   1 
ATOM   8506  O O   . GLN D  1 279 ? -0.684  11.705 -15.635 1.00 85.65  ? 279 GLN D O   1 
ATOM   8507  C CB  . GLN D  1 279 ? -1.194  15.015 -15.569 1.00 68.68  ? 279 GLN D CB  1 
ATOM   8508  C CG  . GLN D  1 279 ? -2.263  16.088 -15.712 1.00 70.31  ? 279 GLN D CG  1 
ATOM   8509  C CD  . GLN D  1 279 ? -3.342  15.677 -16.683 1.00 66.62  ? 279 GLN D CD  1 
ATOM   8510  O OE1 . GLN D  1 279 ? -3.064  15.213 -17.788 1.00 59.14  ? 279 GLN D OE1 1 
ATOM   8511  N NE2 . GLN D  1 279 ? -4.589  15.844 -16.272 1.00 67.21  ? 279 GLN D NE2 1 
ATOM   8512  N N   . SER D  1 280 ? 0.369   12.843 -13.961 1.00 66.81  ? 280 SER D N   1 
ATOM   8513  C CA  . SER D  1 280 ? 1.488   11.894 -13.729 1.00 62.60  ? 280 SER D CA  1 
ATOM   8514  C C   . SER D  1 280 ? 1.650   11.655 -12.225 1.00 58.96  ? 280 SER D C   1 
ATOM   8515  O O   . SER D  1 280 ? 1.097   12.447 -11.435 1.00 56.18  ? 280 SER D O   1 
ATOM   8516  C CB  . SER D  1 280 ? 2.765   12.408 -14.339 1.00 69.57  ? 280 SER D CB  1 
ATOM   8517  O OG  . SER D  1 280 ? 3.447   13.269 -13.436 1.00 77.79  ? 280 SER D OG  1 
ATOM   8518  N N   . ASP D  1 281 ? 2.380   10.599 -11.853 1.00 59.27  ? 281 ASP D N   1 
ATOM   8519  C CA  . ASP D  1 281 ? 2.740   10.283 -10.446 1.00 64.90  ? 281 ASP D CA  1 
ATOM   8520  C C   . ASP D  1 281 ? 4.223   10.601 -10.234 1.00 58.06  ? 281 ASP D C   1 
ATOM   8521  O O   . ASP D  1 281 ? 4.992   10.507 -11.210 1.00 60.83  ? 281 ASP D O   1 
ATOM   8522  C CB  . ASP D  1 281 ? 2.417   8.827  -10.099 1.00 70.04  ? 281 ASP D CB  1 
ATOM   8523  C CG  . ASP D  1 281 ? 0.955   8.601  -9.751  1.00 76.52  ? 281 ASP D CG  1 
ATOM   8524  O OD1 . ASP D  1 281 ? 0.457   9.288  -8.835  1.00 68.40  ? 281 ASP D OD1 1 
ATOM   8525  O OD2 . ASP D  1 281 ? 0.324   7.748  -10.405 1.00 100.75 ? 281 ASP D OD2 1 
ATOM   8526  N N   . ALA D  1 282 ? 4.594   10.979 -9.008  1.00 53.65  ? 282 ALA D N   1 
ATOM   8527  C CA  . ALA D  1 282 ? 5.989   11.240 -8.586  1.00 50.63  ? 282 ALA D CA  1 
ATOM   8528  C C   . ALA D  1 282 ? 6.814   9.962  -8.769  1.00 48.94  ? 282 ALA D C   1 
ATOM   8529  O O   . ALA D  1 282 ? 6.302   8.876  -8.433  1.00 45.42  ? 282 ALA D O   1 
ATOM   8530  C CB  . ALA D  1 282 ? 6.016   11.711 -7.153  1.00 53.57  ? 282 ALA D CB  1 
ATOM   8531  N N   . GLY D  1 283 ? 8.037   10.096 -9.290  1.00 46.22  ? 283 GLY D N   1 
ATOM   8532  C CA  . GLY D  1 283 ? 8.980   8.981  -9.500  1.00 45.54  ? 283 GLY D CA  1 
ATOM   8533  C C   . GLY D  1 283 ? 10.423  9.445  -9.409  1.00 45.71  ? 283 GLY D C   1 
ATOM   8534  O O   . GLY D  1 283 ? 10.691  10.616 -9.739  1.00 50.80  ? 283 GLY D O   1 
ATOM   8535  N N   . LEU D  1 284 ? 11.321  8.561  -8.965  1.00 47.03  ? 284 LEU D N   1 
ATOM   8536  C CA  . LEU D  1 284 ? 12.781  8.826  -8.880  1.00 51.01  ? 284 LEU D CA  1 
ATOM   8537  C C   . LEU D  1 284 ? 13.495  8.038  -9.972  1.00 50.01  ? 284 LEU D C   1 
ATOM   8538  O O   . LEU D  1 284 ? 13.009  6.999  -10.411 1.00 60.29  ? 284 LEU D O   1 
ATOM   8539  C CB  . LEU D  1 284 ? 13.293  8.421  -7.494  1.00 54.10  ? 284 LEU D CB  1 
ATOM   8540  C CG  . LEU D  1 284 ? 12.749  9.239  -6.325  1.00 54.86  ? 284 LEU D CG  1 
ATOM   8541  C CD1 . LEU D  1 284 ? 13.366  8.786  -5.012  1.00 58.04  ? 284 LEU D CD1 1 
ATOM   8542  C CD2 . LEU D  1 284 ? 12.991  10.723 -6.547  1.00 56.40  ? 284 LEU D CD2 1 
ATOM   8543  N N   . PRO D  1 285 ? 14.663  8.516  -10.451 1.00 46.99  ? 285 PRO D N   1 
ATOM   8544  C CA  . PRO D  1 285 ? 15.529  7.715  -11.314 1.00 51.05  ? 285 PRO D CA  1 
ATOM   8545  C C   . PRO D  1 285 ? 16.097  6.509  -10.552 1.00 51.62  ? 285 PRO D C   1 
ATOM   8546  O O   . PRO D  1 285 ? 16.215  6.589  -9.342  1.00 51.23  ? 285 PRO D O   1 
ATOM   8547  C CB  . PRO D  1 285 ? 16.662  8.675  -11.711 1.00 50.69  ? 285 PRO D CB  1 
ATOM   8548  C CG  . PRO D  1 285 ? 16.126  10.059 -11.390 1.00 48.84  ? 285 PRO D CG  1 
ATOM   8549  C CD  . PRO D  1 285 ? 15.201  9.861  -10.208 1.00 46.84  ? 285 PRO D CD  1 
ATOM   8550  N N   . ARG D  1 286 ? 16.437  5.432  -11.265 1.00 51.12  ? 286 ARG D N   1 
ATOM   8551  C CA  . ARG D  1 286 ? 17.114  4.243  -10.681 1.00 54.36  ? 286 ARG D CA  1 
ATOM   8552  C C   . ARG D  1 286 ? 18.468  4.681  -10.108 1.00 58.82  ? 286 ARG D C   1 
ATOM   8553  O O   . ARG D  1 286 ? 19.176  5.448  -10.794 1.00 64.00  ? 286 ARG D O   1 
ATOM   8554  C CB  . ARG D  1 286 ? 17.293  3.148  -11.739 1.00 49.68  ? 286 ARG D CB  1 
ATOM   8555  N N   . GLU D  1 287 ? 18.800  4.230  -8.893  1.00 53.79  ? 287 GLU D N   1 
ATOM   8556  C CA  . GLU D  1 287 ? 20.138  4.420  -8.270  1.00 53.42  ? 287 GLU D CA  1 
ATOM   8557  C C   . GLU D  1 287 ? 21.179  3.723  -9.150  1.00 56.71  ? 287 GLU D C   1 
ATOM   8558  O O   . GLU D  1 287 ? 20.865  2.638  -9.672  1.00 74.36  ? 287 GLU D O   1 
ATOM   8559  C CB  . GLU D  1 287 ? 20.173  3.839  -6.857  1.00 55.66  ? 287 GLU D CB  1 
ATOM   8560  C CG  . GLU D  1 287 ? 19.336  4.612  -5.859  1.00 63.97  ? 287 GLU D CG  1 
ATOM   8561  C CD  . GLU D  1 287 ? 19.339  4.030  -4.457  1.00 72.69  ? 287 GLU D CD  1 
ATOM   8562  O OE1 . GLU D  1 287 ? 20.162  3.129  -4.189  1.00 81.87  ? 287 GLU D OE1 1 
ATOM   8563  O OE2 . GLU D  1 287 ? 18.518  4.480  -3.637  1.00 85.10  ? 287 GLU D OE2 1 
ATOM   8564  N N   . VAL D  1 288 ? 22.361  4.322  -9.311  1.00 61.45  ? 288 VAL D N   1 
ATOM   8565  C CA  . VAL D  1 288 ? 23.446  3.786  -10.188 1.00 62.10  ? 288 VAL D CA  1 
ATOM   8566  C C   . VAL D  1 288 ? 24.743  3.681  -9.379  1.00 64.39  ? 288 VAL D C   1 
ATOM   8567  O O   . VAL D  1 288 ? 25.067  4.637  -8.652  1.00 71.19  ? 288 VAL D O   1 
ATOM   8568  C CB  . VAL D  1 288 ? 23.641  4.652  -11.447 1.00 64.02  ? 288 VAL D CB  1 
ATOM   8569  C CG1 . VAL D  1 288 ? 24.766  4.113  -12.317 1.00 62.16  ? 288 VAL D CG1 1 
ATOM   8570  C CG2 . VAL D  1 288 ? 22.354  4.791  -12.251 1.00 59.51  ? 288 VAL D CG2 1 
ATOM   8571  N N   . TYR D  1 289 ? 25.441  2.547  -9.505  1.00 70.72  ? 289 TYR D N   1 
ATOM   8572  C CA  . TYR D  1 289 ? 26.791  2.289  -8.939  1.00 74.59  ? 289 TYR D CA  1 
ATOM   8573  C C   . TYR D  1 289 ? 27.824  2.516  -10.050 1.00 77.46  ? 289 TYR D C   1 
ATOM   8574  O O   . TYR D  1 289 ? 27.542  2.140  -11.204 1.00 82.21  ? 289 TYR D O   1 
ATOM   8575  C CB  . TYR D  1 289 ? 26.857  0.873  -8.357  1.00 79.99  ? 289 TYR D CB  1 
ATOM   8576  C CG  . TYR D  1 289 ? 28.106  0.558  -7.572  1.00 89.32  ? 289 TYR D CG  1 
ATOM   8577  C CD1 . TYR D  1 289 ? 29.183  -0.078 -8.166  1.00 87.51  ? 289 TYR D CD1 1 
ATOM   8578  C CD2 . TYR D  1 289 ? 28.209  0.883  -6.229  1.00 91.98  ? 289 TYR D CD2 1 
ATOM   8579  C CE1 . TYR D  1 289 ? 30.332  -0.373 -7.451  1.00 87.43  ? 289 TYR D CE1 1 
ATOM   8580  C CE2 . TYR D  1 289 ? 29.351  0.597  -5.500  1.00 91.38  ? 289 TYR D CE2 1 
ATOM   8581  C CZ  . TYR D  1 289 ? 30.417  -0.034 -6.113  1.00 91.82  ? 289 TYR D CZ  1 
ATOM   8582  O OH  . TYR D  1 289 ? 31.543  -0.318 -5.395  1.00 103.17 ? 289 TYR D OH  1 
ATOM   8583  N N   . LEU D  1 290 ? 28.966  3.129  -9.718  1.00 77.94  ? 290 LEU D N   1 
ATOM   8584  C CA  . LEU D  1 290 ? 30.044  3.484  -10.683 1.00 79.27  ? 290 LEU D CA  1 
ATOM   8585  C C   . LEU D  1 290 ? 31.342  2.751  -10.316 1.00 88.63  ? 290 LEU D C   1 
ATOM   8586  O O   . LEU D  1 290 ? 31.460  2.282  -9.166  1.00 93.81  ? 290 LEU D O   1 
ATOM   8587  C CB  . LEU D  1 290 ? 30.255  5.002  -10.664 1.00 74.85  ? 290 LEU D CB  1 
ATOM   8588  C CG  . LEU D  1 290 ? 29.045  5.846  -11.063 1.00 67.58  ? 290 LEU D CG  1 
ATOM   8589  C CD1 . LEU D  1 290 ? 29.390  7.327  -11.045 1.00 61.45  ? 290 LEU D CD1 1 
ATOM   8590  C CD2 . LEU D  1 290 ? 28.521  5.439  -12.432 1.00 69.66  ? 290 LEU D CD2 1 
ATOM   8591  N N   . ALA D  1 291 ? 32.283  2.676  -11.265 1.00 95.68  ? 291 ALA D N   1 
ATOM   8592  C CA  . ALA D  1 291 ? 33.640  2.104  -11.089 1.00 90.50  ? 291 ALA D CA  1 
ATOM   8593  C C   . ALA D  1 291 ? 34.513  3.085  -10.296 1.00 85.39  ? 291 ALA D C   1 
ATOM   8594  O O   . ALA D  1 291 ? 34.851  2.849  -9.135  1.00 74.86  ? 291 ALA D O   1 
ATOM   8595  C CB  . ALA D  1 291 ? 34.246  1.795  -12.437 1.00 89.60  ? 291 ALA D CB  1 
ATOM   8596  N N   . ASN E  1 5   ? -20.336 68.103 -3.698  1.00 84.06  ? 5   ASN E N   1 
ATOM   8597  C CA  . ASN E  1 5   ? -21.390 67.715 -2.714  1.00 91.74  ? 5   ASN E CA  1 
ATOM   8598  C C   . ASN E  1 5   ? -20.788 66.722 -1.710  1.00 99.20  ? 5   ASN E C   1 
ATOM   8599  O O   . ASN E  1 5   ? -21.198 66.746 -0.531  1.00 104.56 ? 5   ASN E O   1 
ATOM   8600  C CB  . ASN E  1 5   ? -22.620 67.125 -3.411  1.00 95.55  ? 5   ASN E CB  1 
ATOM   8601  C CG  . ASN E  1 5   ? -22.866 67.714 -4.785  1.00 98.41  ? 5   ASN E CG  1 
ATOM   8602  O OD1 . ASN E  1 5   ? -23.081 66.983 -5.751  1.00 82.76  ? 5   ASN E OD1 1 
ATOM   8603  N ND2 . ASN E  1 5   ? -22.826 69.032 -4.885  1.00 101.20 ? 5   ASN E ND2 1 
ATOM   8604  N N   . VAL E  1 6   ? -19.856 65.883 -2.175  1.00 95.66  ? 6   VAL E N   1 
ATOM   8605  C CA  . VAL E  1 6   ? -19.138 64.854 -1.365  1.00 85.02  ? 6   VAL E CA  1 
ATOM   8606  C C   . VAL E  1 6   ? -17.872 65.489 -0.779  1.00 79.50  ? 6   VAL E C   1 
ATOM   8607  O O   . VAL E  1 6   ? -17.075 66.041 -1.564  1.00 78.48  ? 6   VAL E O   1 
ATOM   8608  C CB  . VAL E  1 6   ? -18.791 63.614 -2.214  1.00 84.07  ? 6   VAL E CB  1 
ATOM   8609  C CG1 . VAL E  1 6   ? -17.916 62.627 -1.456  1.00 84.84  ? 6   VAL E CG1 1 
ATOM   8610  C CG2 . VAL E  1 6   ? -20.034 62.916 -2.739  1.00 89.83  ? 6   VAL E CG2 1 
ATOM   8611  N N   . SER E  1 7   ? -17.686 65.385 0.540   1.00 74.54  ? 7   SER E N   1 
ATOM   8612  C CA  . SER E  1 7   ? -16.505 65.906 1.279   1.00 73.44  ? 7   SER E CA  1 
ATOM   8613  C C   . SER E  1 7   ? -15.308 64.957 1.117   1.00 70.07  ? 7   SER E C   1 
ATOM   8614  O O   . SER E  1 7   ? -15.097 64.100 2.003   1.00 71.64  ? 7   SER E O   1 
ATOM   8615  C CB  . SER E  1 7   ? -16.834 66.125 2.731   1.00 76.23  ? 7   SER E CB  1 
ATOM   8616  O OG  . SER E  1 7   ? -18.139 66.662 2.886   1.00 76.47  ? 7   SER E OG  1 
ATOM   8617  N N   . VAL E  1 8   ? -14.543 65.120 0.031   1.00 62.92  ? 8   VAL E N   1 
ATOM   8618  C CA  . VAL E  1 8   ? -13.336 64.300 -0.288  1.00 57.13  ? 8   VAL E CA  1 
ATOM   8619  C C   . VAL E  1 8   ? -12.406 64.308 0.922   1.00 60.60  ? 8   VAL E C   1 
ATOM   8620  O O   . VAL E  1 8   ? -12.130 65.359 1.497   1.00 63.85  ? 8   VAL E O   1 
ATOM   8621  C CB  . VAL E  1 8   ? -12.617 64.806 -1.553  1.00 55.79  ? 8   VAL E CB  1 
ATOM   8622  C CG1 . VAL E  1 8   ? -13.485 64.646 -2.789  1.00 53.01  ? 8   VAL E CG1 1 
ATOM   8623  C CG2 . VAL E  1 8   ? -12.152 66.248 -1.405  1.00 58.53  ? 8   VAL E CG2 1 
ATOM   8624  N N   . PRO E  1 9   ? -11.899 63.127 1.340   1.00 59.14  ? 9   PRO E N   1 
ATOM   8625  C CA  . PRO E  1 9   ? -11.086 63.011 2.551   1.00 57.30  ? 9   PRO E CA  1 
ATOM   8626  C C   . PRO E  1 9   ? -9.683  63.623 2.406   1.00 52.94  ? 9   PRO E C   1 
ATOM   8627  O O   . PRO E  1 9   ? -9.056  63.872 3.422   1.00 52.19  ? 9   PRO E O   1 
ATOM   8628  C CB  . PRO E  1 9   ? -10.968 61.494 2.787   1.00 58.09  ? 9   PRO E CB  1 
ATOM   8629  C CG  . PRO E  1 9   ? -11.962 60.857 1.827   1.00 55.68  ? 9   PRO E CG  1 
ATOM   8630  C CD  . PRO E  1 9   ? -12.098 61.832 0.677   1.00 54.91  ? 9   PRO E CD  1 
ATOM   8631  N N   . TRP E  1 10  ? -9.225  63.838 1.168   1.00 47.84  ? 10  TRP E N   1 
ATOM   8632  C CA  . TRP E  1 10  ? -7.884  64.410 0.858   1.00 52.06  ? 10  TRP E CA  1 
ATOM   8633  C C   . TRP E  1 10  ? -7.966  65.941 0.829   1.00 56.08  ? 10  TRP E C   1 
ATOM   8634  O O   . TRP E  1 10  ? -7.013  66.580 0.335   1.00 70.56  ? 10  TRP E O   1 
ATOM   8635  C CB  . TRP E  1 10  ? -7.328  63.841 -0.455  1.00 50.97  ? 10  TRP E CB  1 
ATOM   8636  C CG  . TRP E  1 10  ? -8.251  63.980 -1.626  1.00 49.43  ? 10  TRP E CG  1 
ATOM   8637  C CD1 . TRP E  1 10  ? -8.396  65.066 -2.440  1.00 49.57  ? 10  TRP E CD1 1 
ATOM   8638  C CD2 . TRP E  1 10  ? -9.162  62.985 -2.123  1.00 49.84  ? 10  TRP E CD2 1 
ATOM   8639  N NE1 . TRP E  1 10  ? -9.337  64.818 -3.402  1.00 49.02  ? 10  TRP E NE1 1 
ATOM   8640  C CE2 . TRP E  1 10  ? -9.824  63.549 -3.234  1.00 47.02  ? 10  TRP E CE2 1 
ATOM   8641  C CE3 . TRP E  1 10  ? -9.486  61.680 -1.734  1.00 54.85  ? 10  TRP E CE3 1 
ATOM   8642  C CZ2 . TRP E  1 10  ? -10.787 62.851 -3.959  1.00 47.06  ? 10  TRP E CZ2 1 
ATOM   8643  C CZ3 . TRP E  1 10  ? -10.440 60.992 -2.450  1.00 56.79  ? 10  TRP E CZ3 1 
ATOM   8644  C CH2 . TRP E  1 10  ? -11.079 61.571 -3.547  1.00 52.52  ? 10  TRP E CH2 1 
ATOM   8645  N N   . GLY E  1 11  ? -9.066  66.500 1.343   1.00 52.60  ? 11  GLY E N   1 
ATOM   8646  C CA  . GLY E  1 11  ? -9.259  67.952 1.515   1.00 50.81  ? 11  GLY E CA  1 
ATOM   8647  C C   . GLY E  1 11  ? -8.949  68.380 2.937   1.00 50.12  ? 11  GLY E C   1 
ATOM   8648  O O   . GLY E  1 11  ? -8.569  69.550 3.132   1.00 58.78  ? 11  GLY E O   1 
ATOM   8649  N N   . ALA E  1 12  ? -9.084  67.452 3.890   1.00 49.49  ? 12  ALA E N   1 
ATOM   8650  C CA  . ALA E  1 12  ? -8.945  67.689 5.346   1.00 53.61  ? 12  ALA E CA  1 
ATOM   8651  C C   . ALA E  1 12  ? -7.466  67.830 5.721   1.00 53.88  ? 12  ALA E C   1 
ATOM   8652  O O   . ALA E  1 12  ? -6.661  66.965 5.326   1.00 60.75  ? 12  ALA E O   1 
ATOM   8653  C CB  . ALA E  1 12  ? -9.595  66.567 6.117   1.00 55.47  ? 12  ALA E CB  1 
ATOM   8654  N N   . THR E  1 13  ? -7.144  68.886 6.472   1.00 55.02  ? 13  THR E N   1 
ATOM   8655  C CA  . THR E  1 13  ? -5.813  69.137 7.085   1.00 52.62  ? 13  THR E CA  1 
ATOM   8656  C C   . THR E  1 13  ? -5.658  68.222 8.304   1.00 52.07  ? 13  THR E C   1 
ATOM   8657  O O   . THR E  1 13  ? -6.661  68.024 9.021   1.00 50.05  ? 13  THR E O   1 
ATOM   8658  C CB  . THR E  1 13  ? -5.657  70.618 7.455   1.00 50.91  ? 13  THR E CB  1 
ATOM   8659  O OG1 . THR E  1 13  ? -5.682  71.379 6.247   1.00 48.52  ? 13  THR E OG1 1 
ATOM   8660  C CG2 . THR E  1 13  ? -4.383  70.905 8.219   1.00 48.67  ? 13  THR E CG2 1 
ATOM   8661  N N   . LEU E  1 14  ? -4.454  67.686 8.522   1.00 52.78  ? 14  LEU E N   1 
ATOM   8662  C CA  . LEU E  1 14  ? -4.150  66.720 9.613   1.00 54.28  ? 14  LEU E CA  1 
ATOM   8663  C C   . LEU E  1 14  ? -3.318  67.407 10.701  1.00 48.37  ? 14  LEU E C   1 
ATOM   8664  O O   . LEU E  1 14  ? -2.428  68.203 10.351  1.00 52.12  ? 14  LEU E O   1 
ATOM   8665  C CB  . LEU E  1 14  ? -3.383  65.530 9.027   1.00 55.23  ? 14  LEU E CB  1 
ATOM   8666  C CG  . LEU E  1 14  ? -4.085  64.773 7.902   1.00 59.66  ? 14  LEU E CG  1 
ATOM   8667  C CD1 . LEU E  1 14  ? -3.152  63.740 7.288   1.00 61.86  ? 14  LEU E CD1 1 
ATOM   8668  C CD2 . LEU E  1 14  ? -5.359  64.111 8.405   1.00 65.56  ? 14  LEU E CD2 1 
ATOM   8669  N N   . SER E  1 15  ? -3.597  67.100 11.971  1.00 45.83  ? 15  SER E N   1 
ATOM   8670  C CA  . SER E  1 15  ? -2.723  67.434 13.125  1.00 52.02  ? 15  SER E CA  1 
ATOM   8671  C C   . SER E  1 15  ? -1.433  66.613 13.017  1.00 54.33  ? 15  SER E C   1 
ATOM   8672  O O   . SER E  1 15  ? -1.378  65.706 12.163  1.00 59.84  ? 15  SER E O   1 
ATOM   8673  C CB  . SER E  1 15  ? -3.425  67.185 14.438  1.00 50.14  ? 15  SER E CB  1 
ATOM   8674  O OG  . SER E  1 15  ? -3.595  65.794 14.670  1.00 50.29  ? 15  SER E OG  1 
ATOM   8675  N N   . ASN E  1 16  ? -0.434  66.919 13.847  1.00 56.35  ? 16  ASN E N   1 
ATOM   8676  C CA  . ASN E  1 16  ? 0.847   66.168 13.909  1.00 55.32  ? 16  ASN E CA  1 
ATOM   8677  C C   . ASN E  1 16  ? 0.560   64.752 14.420  1.00 55.10  ? 16  ASN E C   1 
ATOM   8678  O O   . ASN E  1 16  ? 1.082   63.786 13.820  1.00 51.52  ? 16  ASN E O   1 
ATOM   8679  C CB  . ASN E  1 16  ? 1.884   66.892 14.770  1.00 51.94  ? 16  ASN E CB  1 
ATOM   8680  C CG  . ASN E  1 16  ? 2.317   68.211 14.168  1.00 50.07  ? 16  ASN E CG  1 
ATOM   8681  O OD1 . ASN E  1 16  ? 2.075   68.471 12.992  1.00 57.42  ? 16  ASN E OD1 1 
ATOM   8682  N ND2 . ASN E  1 16  ? 2.947   69.053 14.970  1.00 51.29  ? 16  ASN E ND2 1 
ATOM   8683  N N   . ALA E  1 17  ? -0.245  64.645 15.482  1.00 53.69  ? 17  ALA E N   1 
ATOM   8684  C CA  . ALA E  1 17  ? -0.681  63.371 16.100  1.00 49.71  ? 17  ALA E CA  1 
ATOM   8685  C C   . ALA E  1 17  ? -1.256  62.453 15.016  1.00 51.71  ? 17  ALA E C   1 
ATOM   8686  O O   . ALA E  1 17  ? -0.852  61.272 14.963  1.00 51.37  ? 17  ALA E O   1 
ATOM   8687  C CB  . ALA E  1 17  ? -1.696  63.641 17.182  1.00 49.87  ? 17  ALA E CB  1 
ATOM   8688  N N   . GLU E  1 18  ? -2.157  62.989 14.186  1.00 48.78  ? 18  GLU E N   1 
ATOM   8689  C CA  . GLU E  1 18  ? -2.850  62.246 13.100  1.00 48.20  ? 18  GLU E CA  1 
ATOM   8690  C C   . GLU E  1 18  ? -1.820  61.800 12.054  1.00 49.25  ? 18  GLU E C   1 
ATOM   8691  O O   . GLU E  1 18  ? -1.771  60.590 11.747  1.00 48.72  ? 18  GLU E O   1 
ATOM   8692  C CB  . GLU E  1 18  ? -3.950  63.115 12.488  1.00 48.64  ? 18  GLU E CB  1 
ATOM   8693  C CG  . GLU E  1 18  ? -5.144  63.306 13.407  1.00 56.11  ? 18  GLU E CG  1 
ATOM   8694  C CD  . GLU E  1 18  ? -6.091  64.428 13.016  1.00 58.08  ? 18  GLU E CD  1 
ATOM   8695  O OE1 . GLU E  1 18  ? -7.286  64.339 13.363  1.00 58.39  ? 18  GLU E OE1 1 
ATOM   8696  O OE2 . GLU E  1 18  ? -5.632  65.392 12.372  1.00 63.11  ? 18  GLU E OE2 1 
ATOM   8697  N N   . HIS E  1 19  ? -1.024  62.743 11.538  1.00 49.01  ? 19  HIS E N   1 
ATOM   8698  C CA  . HIS E  1 19  ? 0.018   62.506 10.503  1.00 46.36  ? 19  HIS E CA  1 
ATOM   8699  C C   . HIS E  1 19  ? 0.977   61.405 10.974  1.00 43.22  ? 19  HIS E C   1 
ATOM   8700  O O   . HIS E  1 19  ? 1.417   60.599 10.129  1.00 41.96  ? 19  HIS E O   1 
ATOM   8701  C CB  . HIS E  1 19  ? 0.759   63.811 10.183  1.00 42.98  ? 19  HIS E CB  1 
ATOM   8702  C CG  . HIS E  1 19  ? 1.665   63.712 9.002   1.00 43.88  ? 19  HIS E CG  1 
ATOM   8703  N ND1 . HIS E  1 19  ? 3.013   63.428 9.125   1.00 47.68  ? 19  HIS E ND1 1 
ATOM   8704  C CD2 . HIS E  1 19  ? 1.425   63.855 7.681   1.00 43.65  ? 19  HIS E CD2 1 
ATOM   8705  C CE1 . HIS E  1 19  ? 3.564   63.400 7.929   1.00 47.89  ? 19  HIS E CE1 1 
ATOM   8706  N NE2 . HIS E  1 19  ? 2.611   63.660 7.025   1.00 47.11  ? 19  HIS E NE2 1 
ATOM   8707  N N   . GLN E  1 20  ? 1.285   61.378 12.273  1.00 41.34  ? 20  GLN E N   1 
ATOM   8708  C CA  . GLN E  1 20  ? 2.242   60.418 12.882  1.00 45.26  ? 20  GLN E CA  1 
ATOM   8709  C C   . GLN E  1 20  ? 1.580   59.036 12.972  1.00 45.69  ? 20  GLN E C   1 
ATOM   8710  O O   . GLN E  1 20  ? 2.263   58.034 12.683  1.00 42.08  ? 20  GLN E O   1 
ATOM   8711  C CB  . GLN E  1 20  ? 2.691   60.923 14.254  1.00 48.64  ? 20  GLN E CB  1 
ATOM   8712  C CG  . GLN E  1 20  ? 4.092   60.469 14.638  1.00 56.51  ? 20  GLN E CG  1 
ATOM   8713  C CD  . GLN E  1 20  ? 5.169   61.267 13.944  1.00 63.60  ? 20  GLN E CD  1 
ATOM   8714  O OE1 . GLN E  1 20  ? 4.947   62.388 13.492  1.00 79.01  ? 20  GLN E OE1 1 
ATOM   8715  N NE2 . GLN E  1 20  ? 6.358   60.693 13.860  1.00 70.20  ? 20  GLN E NE2 1 
ATOM   8716  N N   . LEU E  1 21  ? 0.297   58.997 13.349  1.00 45.93  ? 21  LEU E N   1 
ATOM   8717  C CA  . LEU E  1 21  ? -0.509  57.753 13.493  1.00 44.62  ? 21  LEU E CA  1 
ATOM   8718  C C   . LEU E  1 21  ? -0.635  57.058 12.135  1.00 40.27  ? 21  LEU E C   1 
ATOM   8719  O O   . LEU E  1 21  ? -0.383  55.839 12.065  1.00 38.31  ? 21  LEU E O   1 
ATOM   8720  C CB  . LEU E  1 21  ? -1.894  58.107 14.043  1.00 47.29  ? 21  LEU E CB  1 
ATOM   8721  C CG  . LEU E  1 21  ? -1.999  58.205 15.564  1.00 48.13  ? 21  LEU E CG  1 
ATOM   8722  C CD1 . LEU E  1 21  ? -3.399  58.629 15.979  1.00 49.73  ? 21  LEU E CD1 1 
ATOM   8723  C CD2 . LEU E  1 21  ? -1.625  56.885 16.220  1.00 46.61  ? 21  LEU E CD2 1 
ATOM   8724  N N   . ILE E  1 22  ? -1.033  57.807 11.105  1.00 37.74  ? 22  ILE E N   1 
ATOM   8725  C CA  . ILE E  1 22  ? -1.258  57.281 9.727   1.00 40.17  ? 22  ILE E CA  1 
ATOM   8726  C C   . ILE E  1 22  ? 0.031   56.603 9.250   1.00 43.47  ? 22  ILE E C   1 
ATOM   8727  O O   . ILE E  1 22  ? -0.027  55.414 8.883   1.00 52.93  ? 22  ILE E O   1 
ATOM   8728  C CB  . ILE E  1 22  ? -1.711  58.405 8.775   1.00 40.75  ? 22  ILE E CB  1 
ATOM   8729  C CG1 . ILE E  1 22  ? -3.051  59.006 9.206   1.00 39.14  ? 22  ILE E CG1 1 
ATOM   8730  C CG2 . ILE E  1 22  ? -1.753  57.906 7.339   1.00 40.05  ? 22  ILE E CG2 1 
ATOM   8731  C CD1 . ILE E  1 22  ? -3.370  60.330 8.554   1.00 39.28  ? 22  ILE E CD1 1 
ATOM   8732  N N   . PHE E  1 23  ? 1.149   57.335 9.270   1.00 44.01  ? 23  PHE E N   1 
ATOM   8733  C CA  . PHE E  1 23  ? 2.488   56.854 8.840   1.00 45.06  ? 23  PHE E CA  1 
ATOM   8734  C C   . PHE E  1 23  ? 2.830   55.556 9.583   1.00 43.68  ? 23  PHE E C   1 
ATOM   8735  O O   . PHE E  1 23  ? 3.219   54.571 8.927   1.00 39.50  ? 23  PHE E O   1 
ATOM   8736  C CB  . PHE E  1 23  ? 3.545   57.931 9.085   1.00 46.43  ? 23  PHE E CB  1 
ATOM   8737  C CG  . PHE E  1 23  ? 4.928   57.558 8.616   1.00 54.79  ? 23  PHE E CG  1 
ATOM   8738  C CD1 . PHE E  1 23  ? 5.926   57.244 9.525   1.00 59.52  ? 23  PHE E CD1 1 
ATOM   8739  C CD2 . PHE E  1 23  ? 5.230   57.509 7.263   1.00 53.29  ? 23  PHE E CD2 1 
ATOM   8740  C CE1 . PHE E  1 23  ? 7.197   56.898 9.093   1.00 56.20  ? 23  PHE E CE1 1 
ATOM   8741  C CE2 . PHE E  1 23  ? 6.500   57.163 6.833   1.00 50.45  ? 23  PHE E CE2 1 
ATOM   8742  C CZ  . PHE E  1 23  ? 7.480   56.856 7.748   1.00 54.91  ? 23  PHE E CZ  1 
ATOM   8743  N N   . TYR E  1 24  ? 2.688   55.566 10.913  1.00 43.24  ? 24  TYR E N   1 
ATOM   8744  C CA  . TYR E  1 24  ? 2.945   54.413 11.815  1.00 46.59  ? 24  TYR E CA  1 
ATOM   8745  C C   . TYR E  1 24  ? 2.271   53.155 11.253  1.00 45.70  ? 24  TYR E C   1 
ATOM   8746  O O   . TYR E  1 24  ? 2.971   52.160 10.982  1.00 46.47  ? 24  TYR E O   1 
ATOM   8747  C CB  . TYR E  1 24  ? 2.440   54.719 13.229  1.00 46.63  ? 24  TYR E CB  1 
ATOM   8748  C CG  . TYR E  1 24  ? 2.593   53.590 14.217  1.00 46.07  ? 24  TYR E CG  1 
ATOM   8749  C CD1 . TYR E  1 24  ? 1.552   52.710 14.472  1.00 44.39  ? 24  TYR E CD1 1 
ATOM   8750  C CD2 . TYR E  1 24  ? 3.780   53.406 14.908  1.00 47.64  ? 24  TYR E CD2 1 
ATOM   8751  C CE1 . TYR E  1 24  ? 1.691   51.675 15.384  1.00 44.39  ? 24  TYR E CE1 1 
ATOM   8752  C CE2 . TYR E  1 24  ? 3.936   52.378 15.823  1.00 42.79  ? 24  TYR E CE2 1 
ATOM   8753  C CZ  . TYR E  1 24  ? 2.888   51.507 16.059  1.00 43.22  ? 24  TYR E CZ  1 
ATOM   8754  O OH  . TYR E  1 24  ? 3.046   50.495 16.960  1.00 40.88  ? 24  TYR E OH  1 
ATOM   8755  N N   . PHE E  1 25  ? 0.947   53.206 11.083  1.00 43.56  ? 25  PHE E N   1 
ATOM   8756  C CA  . PHE E  1 25  ? 0.101   52.065 10.646  1.00 44.70  ? 25  PHE E CA  1 
ATOM   8757  C C   . PHE E  1 25  ? 0.462   51.669 9.210   1.00 43.02  ? 25  PHE E C   1 
ATOM   8758  O O   . PHE E  1 25  ? 0.524   50.458 8.922   1.00 42.95  ? 25  PHE E O   1 
ATOM   8759  C CB  . PHE E  1 25  ? -1.382  52.411 10.798  1.00 45.76  ? 25  PHE E CB  1 
ATOM   8760  C CG  . PHE E  1 25  ? -1.898  52.251 12.206  1.00 50.27  ? 25  PHE E CG  1 
ATOM   8761  C CD1 . PHE E  1 25  ? -2.258  51.003 12.688  1.00 51.63  ? 25  PHE E CD1 1 
ATOM   8762  C CD2 . PHE E  1 25  ? -1.996  53.340 13.056  1.00 51.60  ? 25  PHE E CD2 1 
ATOM   8763  C CE1 . PHE E  1 25  ? -2.720  50.851 13.986  1.00 51.81  ? 25  PHE E CE1 1 
ATOM   8764  C CE2 . PHE E  1 25  ? -2.460  53.187 14.353  1.00 52.53  ? 25  PHE E CE2 1 
ATOM   8765  C CZ  . PHE E  1 25  ? -2.822  51.944 14.815  1.00 52.38  ? 25  PHE E CZ  1 
ATOM   8766  N N   . LEU E  1 26  ? 0.698   52.656 8.342   1.00 38.25  ? 26  LEU E N   1 
ATOM   8767  C CA  . LEU E  1 26  ? 1.087   52.433 6.924   1.00 35.22  ? 26  LEU E CA  1 
ATOM   8768  C C   . LEU E  1 26  ? 2.345   51.560 6.875   1.00 33.19  ? 26  LEU E C   1 
ATOM   8769  O O   . LEU E  1 26  ? 2.303   50.500 6.216   1.00 28.90  ? 26  LEU E O   1 
ATOM   8770  C CB  . LEU E  1 26  ? 1.325   53.783 6.241   1.00 36.14  ? 26  LEU E CB  1 
ATOM   8771  C CG  . LEU E  1 26  ? 0.074   54.458 5.679   1.00 36.09  ? 26  LEU E CG  1 
ATOM   8772  C CD1 . LEU E  1 26  ? 0.443   55.673 4.842   1.00 38.88  ? 26  LEU E CD1 1 
ATOM   8773  C CD2 . LEU E  1 26  ? -0.745  53.480 4.853   1.00 33.30  ? 26  LEU E CD2 1 
ATOM   8774  N N   . VAL E  1 27  ? 3.411   51.987 7.559   1.00 33.71  ? 27  VAL E N   1 
ATOM   8775  C CA  . VAL E  1 27  ? 4.748   51.322 7.536   1.00 36.59  ? 27  VAL E CA  1 
ATOM   8776  C C   . VAL E  1 27  ? 4.652   49.975 8.262   1.00 38.84  ? 27  VAL E C   1 
ATOM   8777  O O   . VAL E  1 27  ? 5.186   48.983 7.731   1.00 36.51  ? 27  VAL E O   1 
ATOM   8778  C CB  . VAL E  1 27  ? 5.842   52.220 8.147   1.00 37.75  ? 27  VAL E CB  1 
ATOM   8779  C CG1 . VAL E  1 27  ? 7.198   51.533 8.143   1.00 38.25  ? 27  VAL E CG1 1 
ATOM   8780  C CG2 . VAL E  1 27  ? 5.924   53.563 7.439   1.00 39.92  ? 27  VAL E CG2 1 
ATOM   8781  N N   . VAL E  1 28  ? 4.001   49.944 9.430   1.00 39.58  ? 28  VAL E N   1 
ATOM   8782  C CA  . VAL E  1 28  ? 3.776   48.697 10.221  1.00 40.52  ? 28  VAL E CA  1 
ATOM   8783  C C   . VAL E  1 28  ? 3.120   47.661 9.300   1.00 42.89  ? 28  VAL E C   1 
ATOM   8784  O O   . VAL E  1 28  ? 3.539   46.488 9.327   1.00 42.05  ? 28  VAL E O   1 
ATOM   8785  C CB  . VAL E  1 28  ? 2.925   48.962 11.477  1.00 39.02  ? 28  VAL E CB  1 
ATOM   8786  C CG1 . VAL E  1 28  ? 2.441   47.668 12.114  1.00 38.02  ? 28  VAL E CG1 1 
ATOM   8787  C CG2 . VAL E  1 28  ? 3.677   49.808 12.492  1.00 41.27  ? 28  VAL E CG2 1 
ATOM   8788  N N   . ALA E  1 29  ? 2.134   48.090 8.508   1.00 42.62  ? 29  ALA E N   1 
ATOM   8789  C CA  . ALA E  1 29  ? 1.431   47.257 7.507   1.00 44.56  ? 29  ALA E CA  1 
ATOM   8790  C C   . ALA E  1 29  ? 2.456   46.670 6.532   1.00 45.12  ? 29  ALA E C   1 
ATOM   8791  O O   . ALA E  1 29  ? 2.573   45.429 6.459   1.00 47.12  ? 29  ALA E O   1 
ATOM   8792  C CB  . ALA E  1 29  ? 0.396   48.088 6.789   1.00 46.64  ? 29  ALA E CB  1 
ATOM   8793  N N   . ALA E  1 30  ? 3.175   47.542 5.820   1.00 46.00  ? 30  ALA E N   1 
ATOM   8794  C CA  . ALA E  1 30  ? 4.201   47.185 4.813   1.00 43.18  ? 30  ALA E CA  1 
ATOM   8795  C C   . ALA E  1 30  ? 5.145   46.120 5.387   1.00 40.16  ? 30  ALA E C   1 
ATOM   8796  O O   . ALA E  1 30  ? 5.411   45.126 4.684   1.00 39.07  ? 30  ALA E O   1 
ATOM   8797  C CB  . ALA E  1 30  ? 4.951   48.424 4.391   1.00 43.29  ? 30  ALA E CB  1 
ATOM   8798  N N   . LEU E  1 31  ? 5.624   46.323 6.618   1.00 37.28  ? 31  LEU E N   1 
ATOM   8799  C CA  . LEU E  1 31  ? 6.601   45.433 7.304   1.00 37.88  ? 31  LEU E CA  1 
ATOM   8800  C C   . LEU E  1 31  ? 5.934   44.094 7.638   1.00 39.35  ? 31  LEU E C   1 
ATOM   8801  O O   . LEU E  1 31  ? 6.591   43.047 7.467   1.00 39.69  ? 31  LEU E O   1 
ATOM   8802  C CB  . LEU E  1 31  ? 7.110   46.132 8.568   1.00 37.68  ? 31  LEU E CB  1 
ATOM   8803  C CG  . LEU E  1 31  ? 7.982   47.362 8.323   1.00 39.71  ? 31  LEU E CG  1 
ATOM   8804  C CD1 . LEU E  1 31  ? 8.240   48.114 9.619   1.00 39.86  ? 31  LEU E CD1 1 
ATOM   8805  C CD2 . LEU E  1 31  ? 9.295   46.972 7.660   1.00 41.95  ? 31  LEU E CD2 1 
ATOM   8806  N N   . ALA E  1 32  ? 4.682   44.134 8.106   1.00 38.17  ? 32  ALA E N   1 
ATOM   8807  C CA  . ALA E  1 32  ? 3.848   42.942 8.379   1.00 35.81  ? 32  ALA E CA  1 
ATOM   8808  C C   . ALA E  1 32  ? 3.813   42.063 7.125   1.00 37.78  ? 32  ALA E C   1 
ATOM   8809  O O   . ALA E  1 32  ? 3.912   40.827 7.257   1.00 38.08  ? 32  ALA E O   1 
ATOM   8810  C CB  . ALA E  1 32  ? 2.462   43.365 8.796   1.00 35.33  ? 32  ALA E CB  1 
ATOM   8811  N N   . PHE E  1 33  ? 3.688   42.694 5.954   1.00 41.78  ? 33  PHE E N   1 
ATOM   8812  C CA  . PHE E  1 33  ? 3.577   42.028 4.629   1.00 45.28  ? 33  PHE E CA  1 
ATOM   8813  C C   . PHE E  1 33  ? 4.936   41.430 4.245   1.00 44.19  ? 33  PHE E C   1 
ATOM   8814  O O   . PHE E  1 33  ? 4.959   40.314 3.694   1.00 48.00  ? 33  PHE E O   1 
ATOM   8815  C CB  . PHE E  1 33  ? 3.042   43.005 3.578   1.00 46.52  ? 33  PHE E CB  1 
ATOM   8816  C CG  . PHE E  1 33  ? 1.576   43.332 3.722   1.00 47.07  ? 33  PHE E CG  1 
ATOM   8817  C CD1 . PHE E  1 33  ? 0.645   42.329 3.939   1.00 48.11  ? 33  PHE E CD1 1 
ATOM   8818  C CD2 . PHE E  1 33  ? 1.121   44.638 3.627   1.00 52.60  ? 33  PHE E CD2 1 
ATOM   8819  C CE1 . PHE E  1 33  ? -0.702  42.625 4.073   1.00 49.02  ? 33  PHE E CE1 1 
ATOM   8820  C CE2 . PHE E  1 33  ? -0.228  44.932 3.759   1.00 52.34  ? 33  PHE E CE2 1 
ATOM   8821  C CZ  . PHE E  1 33  ? -1.136  43.926 3.985   1.00 50.88  ? 33  PHE E CZ  1 
ATOM   8822  N N   . VAL E  1 34  ? 6.027   42.145 4.533   1.00 41.91  ? 34  VAL E N   1 
ATOM   8823  C CA  . VAL E  1 34  ? 7.424   41.646 4.349   1.00 40.08  ? 34  VAL E CA  1 
ATOM   8824  C C   . VAL E  1 34  ? 7.570   40.336 5.132   1.00 39.92  ? 34  VAL E C   1 
ATOM   8825  O O   . VAL E  1 34  ? 7.961   39.320 4.521   1.00 39.90  ? 34  VAL E O   1 
ATOM   8826  C CB  . VAL E  1 34  ? 8.472   42.684 4.798   1.00 34.00  ? 34  VAL E CB  1 
ATOM   8827  C CG1 . VAL E  1 34  ? 9.825   42.041 5.057   1.00 32.77  ? 34  VAL E CG1 1 
ATOM   8828  C CG2 . VAL E  1 34  ? 8.608   43.821 3.801   1.00 31.62  ? 34  VAL E CG2 1 
ATOM   8829  N N   . ALA E  1 35  ? 7.258   40.370 6.431   1.00 38.77  ? 35  ALA E N   1 
ATOM   8830  C CA  . ALA E  1 35  ? 7.315   39.214 7.356   1.00 41.46  ? 35  ALA E CA  1 
ATOM   8831  C C   . ALA E  1 35  ? 6.460   38.070 6.799   1.00 41.47  ? 35  ALA E C   1 
ATOM   8832  O O   . ALA E  1 35  ? 6.936   36.914 6.802   1.00 36.50  ? 35  ALA E O   1 
ATOM   8833  C CB  . ALA E  1 35  ? 6.848   39.633 8.728   1.00 43.17  ? 35  ALA E CB  1 
ATOM   8834  N N   . GLY E  1 36  ? 5.242   38.393 6.350   1.00 42.56  ? 36  GLY E N   1 
ATOM   8835  C CA  . GLY E  1 36  ? 4.292   37.433 5.758   1.00 42.45  ? 36  GLY E CA  1 
ATOM   8836  C C   . GLY E  1 36  ? 4.859   36.801 4.500   1.00 43.05  ? 36  GLY E C   1 
ATOM   8837  O O   . GLY E  1 36  ? 4.861   35.558 4.407   1.00 39.63  ? 36  GLY E O   1 
ATOM   8838  N N   . PHE E  1 37  ? 5.334   37.631 3.566   1.00 45.45  ? 37  PHE E N   1 
ATOM   8839  C CA  . PHE E  1 37  ? 5.927   37.200 2.274   1.00 41.84  ? 37  PHE E CA  1 
ATOM   8840  C C   . PHE E  1 37  ? 7.049   36.194 2.548   1.00 39.55  ? 37  PHE E C   1 
ATOM   8841  O O   . PHE E  1 37  ? 7.049   35.109 1.935   1.00 35.43  ? 37  PHE E O   1 
ATOM   8842  C CB  . PHE E  1 37  ? 6.449   38.401 1.482   1.00 41.17  ? 37  PHE E CB  1 
ATOM   8843  C CG  . PHE E  1 37  ? 7.018   38.037 0.135   1.00 45.88  ? 37  PHE E CG  1 
ATOM   8844  C CD1 . PHE E  1 37  ? 6.230   38.085 -1.004  1.00 49.42  ? 37  PHE E CD1 1 
ATOM   8845  C CD2 . PHE E  1 37  ? 8.335   37.622 0.011   1.00 49.13  ? 37  PHE E CD2 1 
ATOM   8846  C CE1 . PHE E  1 37  ? 6.752   37.741 -2.240  1.00 51.21  ? 37  PHE E CE1 1 
ATOM   8847  C CE2 . PHE E  1 37  ? 8.855   37.276 -1.226  1.00 49.53  ? 37  PHE E CE2 1 
ATOM   8848  C CZ  . PHE E  1 37  ? 8.062   37.334 -2.348  1.00 51.26  ? 37  PHE E CZ  1 
ATOM   8849  N N   . ILE E  1 38  ? 7.969   36.554 3.448   1.00 39.82  ? 38  ILE E N   1 
ATOM   8850  C CA  . ILE E  1 38  ? 9.136   35.711 3.846   1.00 43.16  ? 38  ILE E CA  1 
ATOM   8851  C C   . ILE E  1 38  ? 8.616   34.370 4.374   1.00 43.26  ? 38  ILE E C   1 
ATOM   8852  O O   . ILE E  1 38  ? 9.016   33.325 3.817   1.00 41.88  ? 38  ILE E O   1 
ATOM   8853  C CB  . ILE E  1 38  ? 10.019  36.440 4.877   1.00 44.07  ? 38  ILE E CB  1 
ATOM   8854  C CG1 . ILE E  1 38  ? 10.675  37.684 4.272   1.00 51.52  ? 38  ILE E CG1 1 
ATOM   8855  C CG2 . ILE E  1 38  ? 11.050  35.495 5.474   1.00 41.58  ? 38  ILE E CG2 1 
ATOM   8856  C CD1 . ILE E  1 38  ? 11.541  38.457 5.240   1.00 55.20  ? 38  ILE E CD1 1 
ATOM   8857  N N   . ARG E  1 39  ? 7.756   34.400 5.399   1.00 45.59  ? 39  ARG E N   1 
ATOM   8858  C CA  . ARG E  1 39  ? 7.151   33.181 5.999   1.00 49.35  ? 39  ARG E CA  1 
ATOM   8859  C C   . ARG E  1 39  ? 6.586   32.313 4.872   1.00 49.29  ? 39  ARG E C   1 
ATOM   8860  O O   . ARG E  1 39  ? 6.952   31.124 4.806   1.00 50.19  ? 39  ARG E O   1 
ATOM   8861  C CB  . ARG E  1 39  ? 6.051   33.526 7.010   1.00 58.00  ? 39  ARG E CB  1 
ATOM   8862  C CG  . ARG E  1 39  ? 5.206   32.331 7.437   1.00 65.46  ? 39  ARG E CG  1 
ATOM   8863  C CD  . ARG E  1 39  ? 4.326   32.600 8.643   1.00 73.55  ? 39  ARG E CD  1 
ATOM   8864  N NE  . ARG E  1 39  ? 5.060   32.489 9.896   1.00 90.79  ? 39  ARG E NE  1 
ATOM   8865  C CZ  . ARG E  1 39  ? 5.653   33.503 10.521  1.00 106.22 ? 39  ARG E CZ  1 
ATOM   8866  N NH1 . ARG E  1 39  ? 5.602   34.722 10.011  1.00 117.62 ? 39  ARG E NH1 1 
ATOM   8867  N NH2 . ARG E  1 39  ? 6.296   33.293 11.656  1.00 100.96 ? 39  ARG E NH2 1 
ATOM   8868  N N   . THR E  1 40  ? 5.739   32.899 4.018   1.00 46.09  ? 40  THR E N   1 
ATOM   8869  C CA  . THR E  1 40  ? 5.015   32.198 2.926   1.00 46.66  ? 40  THR E CA  1 
ATOM   8870  C C   . THR E  1 40  ? 6.019   31.496 2.006   1.00 48.19  ? 40  THR E C   1 
ATOM   8871  O O   . THR E  1 40  ? 5.782   30.315 1.677   1.00 53.17  ? 40  THR E O   1 
ATOM   8872  C CB  . THR E  1 40  ? 4.129   33.162 2.130   1.00 45.85  ? 40  THR E CB  1 
ATOM   8873  O OG1 . THR E  1 40  ? 3.052   33.555 2.981   1.00 45.71  ? 40  THR E OG1 1 
ATOM   8874  C CG2 . THR E  1 40  ? 3.582   32.549 0.859   1.00 47.73  ? 40  THR E CG2 1 
ATOM   8875  N N   . TYR E  1 41  ? 7.087   32.196 1.611   1.00 45.38  ? 41  TYR E N   1 
ATOM   8876  C CA  . TYR E  1 41  ? 8.130   31.687 0.684   1.00 52.28  ? 41  TYR E CA  1 
ATOM   8877  C C   . TYR E  1 41  ? 8.817   30.468 1.307   1.00 55.70  ? 41  TYR E C   1 
ATOM   8878  O O   . TYR E  1 41  ? 8.965   29.436 0.621   1.00 75.13  ? 41  TYR E O   1 
ATOM   8879  C CB  . TYR E  1 41  ? 9.164   32.766 0.354   1.00 55.83  ? 41  TYR E CB  1 
ATOM   8880  C CG  . TYR E  1 41  ? 10.227  32.313 -0.617  1.00 58.87  ? 41  TYR E CG  1 
ATOM   8881  C CD1 . TYR E  1 41  ? 11.486  31.934 -0.182  1.00 59.76  ? 41  TYR E CD1 1 
ATOM   8882  C CD2 . TYR E  1 41  ? 9.963   32.232 -1.974  1.00 62.91  ? 41  TYR E CD2 1 
ATOM   8883  C CE1 . TYR E  1 41  ? 12.459  31.503 -1.069  1.00 64.03  ? 41  TYR E CE1 1 
ATOM   8884  C CE2 . TYR E  1 41  ? 10.924  31.805 -2.875  1.00 66.02  ? 41  TYR E CE2 1 
ATOM   8885  C CZ  . TYR E  1 41  ? 12.178  31.439 -2.421  1.00 68.34  ? 41  TYR E CZ  1 
ATOM   8886  O OH  . TYR E  1 41  ? 13.132  31.020 -3.303  1.00 82.17  ? 41  TYR E OH  1 
ATOM   8887  N N   . ILE E  1 42  ? 9.220   30.591 2.573   1.00 54.98  ? 42  ILE E N   1 
ATOM   8888  C CA  . ILE E  1 42  ? 10.046  29.581 3.297   1.00 56.31  ? 42  ILE E CA  1 
ATOM   8889  C C   . ILE E  1 42  ? 9.218   28.310 3.519   1.00 56.57  ? 42  ILE E C   1 
ATOM   8890  O O   . ILE E  1 42  ? 9.806   27.212 3.485   1.00 63.90  ? 42  ILE E O   1 
ATOM   8891  C CB  . ILE E  1 42  ? 10.581  30.173 4.616   1.00 57.30  ? 42  ILE E CB  1 
ATOM   8892  C CG1 . ILE E  1 42  ? 11.749  31.126 4.352   1.00 58.15  ? 42  ILE E CG1 1 
ATOM   8893  C CG2 . ILE E  1 42  ? 10.954  29.075 5.600   1.00 59.23  ? 42  ILE E CG2 1 
ATOM   8894  C CD1 . ILE E  1 42  ? 12.836  31.072 5.392   1.00 64.13  ? 42  ILE E CD1 1 
ATOM   8895  N N   . THR E  1 43  ? 7.907   28.455 3.724   1.00 55.78  ? 43  THR E N   1 
ATOM   8896  C CA  . THR E  1 43  ? 6.975   27.344 4.059   1.00 56.02  ? 43  THR E CA  1 
ATOM   8897  C C   . THR E  1 43  ? 6.224   26.887 2.803   1.00 60.10  ? 43  THR E C   1 
ATOM   8898  O O   . THR E  1 43  ? 5.148   26.275 2.956   1.00 63.48  ? 43  THR E O   1 
ATOM   8899  C CB  . THR E  1 43  ? 5.996   27.769 5.160   1.00 54.32  ? 43  THR E CB  1 
ATOM   8900  O OG1 . THR E  1 43  ? 5.202   28.847 4.661   1.00 53.62  ? 43  THR E OG1 1 
ATOM   8901  C CG2 . THR E  1 43  ? 6.695   28.190 6.434   1.00 54.66  ? 43  THR E CG2 1 
ATOM   8902  N N   . ARG E  1 44  ? 6.770   27.155 1.613   1.00 57.76  ? 44  ARG E N   1 
ATOM   8903  C CA  . ARG E  1 44  ? 6.073   26.910 0.321   1.00 57.16  ? 44  ARG E CA  1 
ATOM   8904  C C   . ARG E  1 44  ? 6.014   25.403 0.044   1.00 57.19  ? 44  ARG E C   1 
ATOM   8905  O O   . ARG E  1 44  ? 4.990   24.948 -0.502  1.00 62.53  ? 44  ARG E O   1 
ATOM   8906  C CB  . ARG E  1 44  ? 6.745   27.673 -0.825  1.00 54.63  ? 44  ARG E CB  1 
ATOM   8907  C CG  . ARG E  1 44  ? 8.106   27.144 -1.251  1.00 54.69  ? 44  ARG E CG  1 
ATOM   8908  C CD  . ARG E  1 44  ? 8.741   28.061 -2.282  1.00 60.17  ? 44  ARG E CD  1 
ATOM   8909  N NE  . ARG E  1 44  ? 9.987   27.538 -2.825  1.00 68.91  ? 44  ARG E NE  1 
ATOM   8910  C CZ  . ARG E  1 44  ? 11.188  27.732 -2.290  1.00 79.31  ? 44  ARG E CZ  1 
ATOM   8911  N NH1 . ARG E  1 44  ? 11.316  28.438 -1.179  1.00 76.87  ? 44  ARG E NH1 1 
ATOM   8912  N NH2 . ARG E  1 44  ? 12.258  27.212 -2.867  1.00 89.27  ? 44  ARG E NH2 1 
ATOM   8913  N N   . ASN E  1 45  ? 7.057   24.659 0.426   1.00 56.65  ? 45  ASN E N   1 
ATOM   8914  C CA  . ASN E  1 45  ? 7.220   23.220 0.083   1.00 56.08  ? 45  ASN E CA  1 
ATOM   8915  C C   . ASN E  1 45  ? 6.639   22.346 1.201   1.00 54.80  ? 45  ASN E C   1 
ATOM   8916  O O   . ASN E  1 45  ? 6.964   21.144 1.236   1.00 61.18  ? 45  ASN E O   1 
ATOM   8917  C CB  . ASN E  1 45  ? 8.683   22.882 -0.208  1.00 61.41  ? 45  ASN E CB  1 
ATOM   8918  C CG  . ASN E  1 45  ? 9.155   23.455 -1.527  1.00 62.46  ? 45  ASN E CG  1 
ATOM   8919  O OD1 . ASN E  1 45  ? 8.376   23.573 -2.471  1.00 64.71  ? 45  ASN E OD1 1 
ATOM   8920  N ND2 . ASN E  1 45  ? 10.425  23.814 -1.603  1.00 67.71  ? 45  ASN E ND2 1 
ATOM   8921  N N   . GLU E  1 46  ? 5.809   22.931 2.069   1.00 57.32  ? 46  GLU E N   1 
ATOM   8922  C CA  . GLU E  1 46  ? 5.021   22.207 3.103   1.00 57.13  ? 46  GLU E CA  1 
ATOM   8923  C C   . GLU E  1 46  ? 3.696   21.746 2.486   1.00 55.27  ? 46  GLU E C   1 
ATOM   8924  O O   . GLU E  1 46  ? 2.863   21.184 3.222   1.00 56.04  ? 46  GLU E O   1 
ATOM   8925  C CB  . GLU E  1 46  ? 4.737   23.107 4.306   1.00 58.34  ? 46  GLU E CB  1 
ATOM   8926  C CG  . GLU E  1 46  ? 5.960   23.420 5.145   1.00 60.07  ? 46  GLU E CG  1 
ATOM   8927  C CD  . GLU E  1 46  ? 5.657   24.239 6.387   1.00 64.19  ? 46  GLU E CD  1 
ATOM   8928  O OE1 . GLU E  1 46  ? 6.585   24.456 7.191   1.00 69.29  ? 46  GLU E OE1 1 
ATOM   8929  O OE2 . GLU E  1 46  ? 4.490   24.659 6.546   1.00 72.19  ? 46  GLU E OE2 1 
ATOM   8930  N N   . VAL E  1 47  ? 3.518   21.982 1.184   1.00 54.15  ? 47  VAL E N   1 
ATOM   8931  C CA  . VAL E  1 47  ? 2.237   21.762 0.451   1.00 56.95  ? 47  VAL E CA  1 
ATOM   8932  C C   . VAL E  1 47  ? 2.521   20.949 -0.816  1.00 61.31  ? 47  VAL E C   1 
ATOM   8933  O O   . VAL E  1 47  ? 3.517   21.250 -1.504  1.00 64.78  ? 47  VAL E O   1 
ATOM   8934  C CB  . VAL E  1 47  ? 1.556   23.105 0.126   1.00 58.30  ? 47  VAL E CB  1 
ATOM   8935  C CG1 . VAL E  1 47  ? 0.485   22.959 -0.942  1.00 57.05  ? 47  VAL E CG1 1 
ATOM   8936  C CG2 . VAL E  1 47  ? 0.984   23.756 1.376   1.00 62.18  ? 47  VAL E CG2 1 
ATOM   8937  N N   . GLY E  1 48  ? 1.673   19.955 -1.101  1.00 58.81  ? 48  GLY E N   1 
ATOM   8938  C CA  . GLY E  1 48  ? 1.775   19.088 -2.289  1.00 57.01  ? 48  GLY E CA  1 
ATOM   8939  C C   . GLY E  1 48  ? 1.565   19.880 -3.565  1.00 58.30  ? 48  GLY E C   1 
ATOM   8940  O O   . GLY E  1 48  ? 0.898   20.934 -3.503  1.00 69.08  ? 48  GLY E O   1 
ATOM   8941  N N   . SER E  1 49  ? 2.114   19.392 -4.680  1.00 55.88  ? 49  SER E N   1 
ATOM   8942  C CA  . SER E  1 49  ? 2.037   20.033 -6.018  1.00 57.11  ? 49  SER E CA  1 
ATOM   8943  C C   . SER E  1 49  ? 0.575   20.337 -6.364  1.00 54.81  ? 49  SER E C   1 
ATOM   8944  O O   . SER E  1 49  ? 0.336   21.253 -7.174  1.00 46.85  ? 49  SER E O   1 
ATOM   8945  C CB  . SER E  1 49  ? 2.675   19.164 -7.070  1.00 59.80  ? 49  SER E CB  1 
ATOM   8946  O OG  . SER E  1 49  ? 2.012   17.910 -7.162  1.00 55.54  ? 49  SER E OG  1 
ATOM   8947  N N   . ARG E  1 50  ? -0.359  19.595 -5.761  1.00 55.82  ? 50  ARG E N   1 
ATOM   8948  C CA  . ARG E  1 50  ? -1.809  19.658 -6.080  1.00 60.65  ? 50  ARG E CA  1 
ATOM   8949  C C   . ARG E  1 50  ? -2.393  20.994 -5.612  1.00 58.70  ? 50  ARG E C   1 
ATOM   8950  O O   . ARG E  1 50  ? -3.311  21.499 -6.284  1.00 68.16  ? 50  ARG E O   1 
ATOM   8951  C CB  . ARG E  1 50  ? -2.561  18.497 -5.426  1.00 68.53  ? 50  ARG E CB  1 
ATOM   8952  C CG  . ARG E  1 50  ? -4.048  18.490 -5.746  1.00 76.86  ? 50  ARG E CG  1 
ATOM   8953  C CD  . ARG E  1 50  ? -4.794  17.359 -5.072  1.00 82.65  ? 50  ARG E CD  1 
ATOM   8954  N NE  . ARG E  1 50  ? -6.188  17.311 -5.487  1.00 85.08  ? 50  ARG E NE  1 
ATOM   8955  C CZ  . ARG E  1 50  ? -7.084  16.456 -5.011  1.00 90.97  ? 50  ARG E CZ  1 
ATOM   8956  N NH1 . ARG E  1 50  ? -6.731  15.571 -4.095  1.00 96.41  ? 50  ARG E NH1 1 
ATOM   8957  N NH2 . ARG E  1 50  ? -8.328  16.489 -5.451  1.00 102.38 ? 50  ARG E NH2 1 
ATOM   8958  N N   . TYR E  1 51  ? -1.888  21.537 -4.501  1.00 57.07  ? 51  TYR E N   1 
ATOM   8959  C CA  . TYR E  1 51  ? -2.440  22.742 -3.828  1.00 57.89  ? 51  TYR E CA  1 
ATOM   8960  C C   . TYR E  1 51  ? -1.435  23.897 -3.906  1.00 57.17  ? 51  TYR E C   1 
ATOM   8961  O O   . TYR E  1 51  ? -1.535  24.833 -3.092  1.00 60.21  ? 51  TYR E O   1 
ATOM   8962  C CB  . TYR E  1 51  ? -2.806  22.415 -2.377  1.00 62.21  ? 51  TYR E CB  1 
ATOM   8963  C CG  . TYR E  1 51  ? -3.735  21.238 -2.223  1.00 70.64  ? 51  TYR E CG  1 
ATOM   8964  C CD1 . TYR E  1 51  ? -5.076  21.335 -2.554  1.00 76.88  ? 51  TYR E CD1 1 
ATOM   8965  C CD2 . TYR E  1 51  ? -3.273  20.020 -1.754  1.00 77.29  ? 51  TYR E CD2 1 
ATOM   8966  C CE1 . TYR E  1 51  ? -5.935  20.256 -2.422  1.00 80.35  ? 51  TYR E CE1 1 
ATOM   8967  C CE2 . TYR E  1 51  ? -4.117  18.930 -1.616  1.00 83.44  ? 51  TYR E CE2 1 
ATOM   8968  C CZ  . TYR E  1 51  ? -5.453  19.047 -1.953  1.00 86.44  ? 51  TYR E CZ  1 
ATOM   8969  O OH  . TYR E  1 51  ? -6.289  17.975 -1.819  1.00 96.54  ? 51  TYR E OH  1 
ATOM   8970  N N   . ARG E  1 52  ? -0.506  23.842 -4.864  1.00 57.68  ? 52  ARG E N   1 
ATOM   8971  C CA  . ARG E  1 52  ? 0.576   24.852 -5.023  1.00 59.56  ? 52  ARG E CA  1 
ATOM   8972  C C   . ARG E  1 52  ? -0.015  26.183 -5.505  1.00 63.52  ? 52  ARG E C   1 
ATOM   8973  O O   . ARG E  1 52  ? 0.563   27.235 -5.174  1.00 69.25  ? 52  ARG E O   1 
ATOM   8974  C CB  . ARG E  1 52  ? 1.645   24.355 -5.998  1.00 60.73  ? 52  ARG E CB  1 
ATOM   8975  C CG  . ARG E  1 52  ? 2.846   25.283 -6.113  1.00 62.06  ? 52  ARG E CG  1 
ATOM   8976  C CD  . ARG E  1 52  ? 4.047   24.577 -6.712  1.00 62.30  ? 52  ARG E CD  1 
ATOM   8977  N NE  . ARG E  1 52  ? 4.398   23.376 -5.967  1.00 62.24  ? 52  ARG E NE  1 
ATOM   8978  C CZ  . ARG E  1 52  ? 4.938   22.287 -6.503  1.00 70.92  ? 52  ARG E CZ  1 
ATOM   8979  N NH1 . ARG E  1 52  ? 5.183   22.237 -7.801  1.00 75.88  ? 52  ARG E NH1 1 
ATOM   8980  N NH2 . ARG E  1 52  ? 5.224   21.248 -5.740  1.00 76.26  ? 52  ARG E NH2 1 
ATOM   8981  N N   . THR E  1 53  ? -1.114  26.140 -6.264  1.00 63.17  ? 53  THR E N   1 
ATOM   8982  C CA  . THR E  1 53  ? -1.819  27.341 -6.788  1.00 58.03  ? 53  THR E CA  1 
ATOM   8983  C C   . THR E  1 53  ? -2.207  28.242 -5.609  1.00 51.54  ? 53  THR E C   1 
ATOM   8984  O O   . THR E  1 53  ? -2.214  29.478 -5.782  1.00 52.53  ? 53  THR E O   1 
ATOM   8985  C CB  . THR E  1 53  ? -3.043  26.954 -7.628  1.00 62.38  ? 53  THR E CB  1 
ATOM   8986  O OG1 . THR E  1 53  ? -2.652  25.934 -8.548  1.00 65.42  ? 53  THR E OG1 1 
ATOM   8987  C CG2 . THR E  1 53  ? -3.625  28.124 -8.390  1.00 68.42  ? 53  THR E CG2 1 
ATOM   8988  N N   . ALA E  1 54  ? -2.515  27.637 -4.458  1.00 50.90  ? 54  ALA E N   1 
ATOM   8989  C CA  . ALA E  1 54  ? -2.855  28.334 -3.196  1.00 54.96  ? 54  ALA E CA  1 
ATOM   8990  C C   . ALA E  1 54  ? -1.652  29.162 -2.738  1.00 53.85  ? 54  ALA E C   1 
ATOM   8991  O O   . ALA E  1 54  ? -1.855  30.296 -2.273  1.00 57.95  ? 54  ALA E O   1 
ATOM   8992  C CB  . ALA E  1 54  ? -3.262  27.334 -2.140  1.00 52.53  ? 54  ALA E CB  1 
ATOM   8993  N N   . VAL E  1 55  ? -0.449  28.597 -2.876  1.00 53.97  ? 55  VAL E N   1 
ATOM   8994  C CA  . VAL E  1 55  ? 0.836   29.188 -2.399  1.00 48.45  ? 55  VAL E CA  1 
ATOM   8995  C C   . VAL E  1 55  ? 1.239   30.329 -3.339  1.00 46.54  ? 55  VAL E C   1 
ATOM   8996  O O   . VAL E  1 55  ? 1.492   31.438 -2.835  1.00 47.52  ? 55  VAL E O   1 
ATOM   8997  C CB  . VAL E  1 55  ? 1.939   28.117 -2.307  1.00 48.06  ? 55  VAL E CB  1 
ATOM   8998  C CG1 . VAL E  1 55  ? 3.266   28.716 -1.872  1.00 48.33  ? 55  VAL E CG1 1 
ATOM   8999  C CG2 . VAL E  1 55  ? 1.541   26.974 -1.385  1.00 49.96  ? 55  VAL E CG2 1 
ATOM   9000  N N   . SER E  1 56  ? 1.302   30.065 -4.648  1.00 47.28  ? 56  SER E N   1 
ATOM   9001  C CA  . SER E  1 56  ? 1.705   31.052 -5.686  1.00 51.34  ? 56  SER E CA  1 
ATOM   9002  C C   . SER E  1 56  ? 0.804   32.291 -5.602  1.00 50.77  ? 56  SER E C   1 
ATOM   9003  O O   . SER E  1 56  ? 1.325   33.415 -5.756  1.00 47.09  ? 56  SER E O   1 
ATOM   9004  C CB  . SER E  1 56  ? 1.687   30.447 -7.065  1.00 53.64  ? 56  SER E CB  1 
ATOM   9005  O OG  . SER E  1 56  ? 0.410   29.911 -7.369  1.00 69.37  ? 56  SER E OG  1 
ATOM   9006  N N   . ALA E  1 57  ? -0.494  32.089 -5.358  1.00 49.28  ? 57  ALA E N   1 
ATOM   9007  C CA  . ALA E  1 57  ? -1.500  33.163 -5.194  1.00 47.71  ? 57  ALA E CA  1 
ATOM   9008  C C   . ALA E  1 57  ? -1.190  33.969 -3.927  1.00 46.98  ? 57  ALA E C   1 
ATOM   9009  O O   . ALA E  1 57  ? -1.131  35.211 -4.016  1.00 45.89  ? 57  ALA E O   1 
ATOM   9010  C CB  . ALA E  1 57  ? -2.885  32.569 -5.145  1.00 49.45  ? 57  ALA E CB  1 
ATOM   9011  N N   . ARG E  1 58  ? -1.000  33.281 -2.796  1.00 46.36  ? 58  ARG E N   1 
ATOM   9012  C CA  . ARG E  1 58  ? -0.710  33.904 -1.476  1.00 49.04  ? 58  ARG E CA  1 
ATOM   9013  C C   . ARG E  1 58  ? 0.560   34.754 -1.590  1.00 47.10  ? 58  ARG E C   1 
ATOM   9014  O O   . ARG E  1 58  ? 0.522   35.927 -1.177  1.00 43.03  ? 58  ARG E O   1 
ATOM   9015  C CB  . ARG E  1 58  ? -0.556  32.841 -0.383  1.00 54.45  ? 58  ARG E CB  1 
ATOM   9016  C CG  . ARG E  1 58  ? -0.316  33.411 1.008   1.00 63.74  ? 58  ARG E CG  1 
ATOM   9017  C CD  . ARG E  1 58  ? -0.687  32.443 2.117   1.00 79.84  ? 58  ARG E CD  1 
ATOM   9018  N NE  . ARG E  1 58  ? 0.272   31.359 2.274   1.00 93.66  ? 58  ARG E NE  1 
ATOM   9019  C CZ  . ARG E  1 58  ? 1.096   31.226 3.309   1.00 100.40 ? 58  ARG E CZ  1 
ATOM   9020  N NH1 . ARG E  1 58  ? 1.939   30.208 3.355   1.00 100.77 ? 58  ARG E NH1 1 
ATOM   9021  N NH2 . ARG E  1 58  ? 1.071   32.104 4.297   1.00 86.76  ? 58  ARG E NH2 1 
ATOM   9022  N N   . LEU E  1 59  ? 1.640   34.182 -2.129  1.00 45.77  ? 59  LEU E N   1 
ATOM   9023  C CA  . LEU E  1 59  ? 2.945   34.875 -2.284  1.00 46.51  ? 59  LEU E CA  1 
ATOM   9024  C C   . LEU E  1 59  ? 2.772   36.039 -3.264  1.00 48.38  ? 59  LEU E C   1 
ATOM   9025  O O   . LEU E  1 59  ? 3.280   37.141 -2.969  1.00 51.18  ? 59  LEU E O   1 
ATOM   9026  C CB  . LEU E  1 59  ? 4.001   33.882 -2.775  1.00 48.58  ? 59  LEU E CB  1 
ATOM   9027  C CG  . LEU E  1 59  ? 5.445   34.278 -2.475  1.00 54.44  ? 59  LEU E CG  1 
ATOM   9028  C CD1 . LEU E  1 59  ? 5.645   34.525 -0.985  1.00 62.57  ? 59  LEU E CD1 1 
ATOM   9029  C CD2 . LEU E  1 59  ? 6.410   33.216 -2.974  1.00 51.91  ? 59  LEU E CD2 1 
ATOM   9030  N N   . GLY E  1 60  ? 2.072   35.796 -4.375  1.00 47.67  ? 60  GLY E N   1 
ATOM   9031  C CA  . GLY E  1 60  ? 1.715   36.828 -5.367  1.00 48.03  ? 60  GLY E CA  1 
ATOM   9032  C C   . GLY E  1 60  ? 1.048   38.025 -4.708  1.00 47.72  ? 60  GLY E C   1 
ATOM   9033  O O   . GLY E  1 60  ? 1.496   39.162 -4.957  1.00 46.73  ? 60  GLY E O   1 
ATOM   9034  N N   . MET E  1 61  ? 0.025   37.782 -3.881  1.00 43.26  ? 61  MET E N   1 
ATOM   9035  C CA  . MET E  1 61  ? -0.810  38.842 -3.256  1.00 48.15  ? 61  MET E CA  1 
ATOM   9036  C C   . MET E  1 61  ? 0.020   39.601 -2.215  1.00 46.18  ? 61  MET E C   1 
ATOM   9037  O O   . MET E  1 61  ? -0.109  40.838 -2.154  1.00 56.14  ? 61  MET E O   1 
ATOM   9038  C CB  . MET E  1 61  ? -2.062  38.254 -2.595  1.00 55.67  ? 61  MET E CB  1 
ATOM   9039  C CG  . MET E  1 61  ? -1.798  37.539 -1.282  1.00 68.87  ? 61  MET E CG  1 
ATOM   9040  S SD  . MET E  1 61  ? -2.161  38.547 0.184   1.00 61.83  ? 61  MET E SD  1 
ATOM   9041  C CE  . MET E  1 61  ? -3.519  39.546 -0.421  1.00 66.51  ? 61  MET E CE  1 
ATOM   9042  N N   . LEU E  1 62  ? 0.839   38.891 -1.434  1.00 44.53  ? 62  LEU E N   1 
ATOM   9043  C CA  . LEU E  1 62  ? 1.695   39.493 -0.377  1.00 44.95  ? 62  LEU E CA  1 
ATOM   9044  C C   . LEU E  1 62  ? 2.751   40.384 -1.039  1.00 43.94  ? 62  LEU E C   1 
ATOM   9045  O O   . LEU E  1 62  ? 2.987   41.497 -0.528  1.00 44.85  ? 62  LEU E O   1 
ATOM   9046  C CB  . LEU E  1 62  ? 2.335   38.381 0.460   1.00 42.82  ? 62  LEU E CB  1 
ATOM   9047  C CG  . LEU E  1 62  ? 1.375   37.633 1.385   1.00 42.91  ? 62  LEU E CG  1 
ATOM   9048  C CD1 . LEU E  1 62  ? 2.076   36.479 2.080   1.00 41.97  ? 62  LEU E CD1 1 
ATOM   9049  C CD2 . LEU E  1 62  ? 0.762   38.573 2.412   1.00 45.40  ? 62  LEU E CD2 1 
ATOM   9050  N N   . GLY E  1 63  ? 3.345   39.912 -2.139  1.00 41.13  ? 63  GLY E N   1 
ATOM   9051  C CA  . GLY E  1 63  ? 4.296   40.685 -2.959  1.00 42.65  ? 63  GLY E CA  1 
ATOM   9052  C C   . GLY E  1 63  ? 3.671   41.983 -3.440  1.00 44.77  ? 63  GLY E C   1 
ATOM   9053  O O   . GLY E  1 63  ? 4.294   43.046 -3.257  1.00 45.25  ? 63  GLY E O   1 
ATOM   9054  N N   . VAL E  1 64  ? 2.474   41.897 -4.024  1.00 47.34  ? 64  VAL E N   1 
ATOM   9055  C CA  . VAL E  1 64  ? 1.691   43.060 -4.537  1.00 50.56  ? 64  VAL E CA  1 
ATOM   9056  C C   . VAL E  1 64  ? 1.415   44.023 -3.375  1.00 51.75  ? 64  VAL E C   1 
ATOM   9057  O O   . VAL E  1 64  ? 1.794   45.206 -3.485  1.00 55.70  ? 64  VAL E O   1 
ATOM   9058  C CB  . VAL E  1 64  ? 0.385   42.598 -5.210  1.00 52.33  ? 64  VAL E CB  1 
ATOM   9059  C CG1 . VAL E  1 64  ? -0.561  43.760 -5.468  1.00 57.62  ? 64  VAL E CG1 1 
ATOM   9060  C CG2 . VAL E  1 64  ? 0.656   41.833 -6.496  1.00 53.23  ? 64  VAL E CG2 1 
ATOM   9061  N N   . ALA E  1 65  ? 0.778   43.530 -2.309  1.00 45.01  ? 65  ALA E N   1 
ATOM   9062  C CA  . ALA E  1 65  ? 0.414   44.304 -1.099  1.00 45.16  ? 65  ALA E CA  1 
ATOM   9063  C C   . ALA E  1 65  ? 1.637   45.090 -0.615  1.00 44.51  ? 65  ALA E C   1 
ATOM   9064  O O   . ALA E  1 65  ? 1.543   46.327 -0.467  1.00 45.36  ? 65  ALA E O   1 
ATOM   9065  C CB  . ALA E  1 65  ? -0.101  43.369 -0.033  1.00 44.37  ? 65  ALA E CB  1 
ATOM   9066  N N   . LEU E  1 66  ? 2.741   44.379 -0.384  1.00 47.35  ? 66  LEU E N   1 
ATOM   9067  C CA  . LEU E  1 66  ? 4.048   44.945 0.039   1.00 53.38  ? 66  LEU E CA  1 
ATOM   9068  C C   . LEU E  1 66  ? 4.378   46.175 -0.816  1.00 50.69  ? 66  LEU E C   1 
ATOM   9069  O O   . LEU E  1 66  ? 4.507   47.274 -0.243  1.00 56.44  ? 66  LEU E O   1 
ATOM   9070  C CB  . LEU E  1 66  ? 5.115   43.858 -0.121  1.00 58.05  ? 66  LEU E CB  1 
ATOM   9071  C CG  . LEU E  1 66  ? 6.392   44.071 0.686   1.00 62.43  ? 66  LEU E CG  1 
ATOM   9072  C CD1 . LEU E  1 66  ? 7.392   42.960 0.412   1.00 67.33  ? 66  LEU E CD1 1 
ATOM   9073  C CD2 . LEU E  1 66  ? 7.002   45.431 0.386   1.00 66.29  ? 66  LEU E CD2 1 
ATOM   9074  N N   . LEU E  1 67  ? 4.505   45.986 -2.134  1.00 45.25  ? 67  LEU E N   1 
ATOM   9075  C CA  . LEU E  1 67  ? 4.917   47.033 -3.108  1.00 46.78  ? 67  LEU E CA  1 
ATOM   9076  C C   . LEU E  1 67  ? 3.880   48.160 -3.124  1.00 43.50  ? 67  LEU E C   1 
ATOM   9077  O O   . LEU E  1 67  ? 4.283   49.335 -3.045  1.00 44.17  ? 67  LEU E O   1 
ATOM   9078  C CB  . LEU E  1 67  ? 5.065   46.405 -4.497  1.00 48.09  ? 67  LEU E CB  1 
ATOM   9079  C CG  . LEU E  1 67  ? 6.186   45.375 -4.632  1.00 45.66  ? 67  LEU E CG  1 
ATOM   9080  C CD1 . LEU E  1 67  ? 6.200   44.765 -6.025  1.00 46.30  ? 67  LEU E CD1 1 
ATOM   9081  C CD2 . LEU E  1 67  ? 7.534   45.998 -4.309  1.00 43.74  ? 67  LEU E CD2 1 
ATOM   9082  N N   . ALA E  1 68  ? 2.598   47.812 -3.235  1.00 44.42  ? 68  ALA E N   1 
ATOM   9083  C CA  . ALA E  1 68  ? 1.472   48.773 -3.237  1.00 44.90  ? 68  ALA E CA  1 
ATOM   9084  C C   . ALA E  1 68  ? 1.638   49.734 -2.056  1.00 41.39  ? 68  ALA E C   1 
ATOM   9085  O O   . ALA E  1 68  ? 1.548   50.958 -2.272  1.00 41.73  ? 68  ALA E O   1 
ATOM   9086  C CB  . ALA E  1 68  ? 0.156   48.037 -3.172  1.00 44.43  ? 68  ALA E CB  1 
ATOM   9087  N N   . TYR E  1 69  ? 1.892   49.192 -0.860  1.00 38.10  ? 69  TYR E N   1 
ATOM   9088  C CA  . TYR E  1 69  ? 1.961   49.959 0.410   1.00 38.68  ? 69  TYR E CA  1 
ATOM   9089  C C   . TYR E  1 69  ? 3.175   50.891 0.395   1.00 39.09  ? 69  TYR E C   1 
ATOM   9090  O O   . TYR E  1 69  ? 3.085   51.984 0.987   1.00 42.56  ? 69  TYR E O   1 
ATOM   9091  C CB  . TYR E  1 69  ? 1.936   49.019 1.616   1.00 40.10  ? 69  TYR E CB  1 
ATOM   9092  C CG  . TYR E  1 69  ? 0.565   48.911 2.230   1.00 41.73  ? 69  TYR E CG  1 
ATOM   9093  C CD1 . TYR E  1 69  ? 0.204   49.690 3.316   1.00 43.11  ? 69  TYR E CD1 1 
ATOM   9094  C CD2 . TYR E  1 69  ? -0.397  48.084 1.679   1.00 45.86  ? 69  TYR E CD2 1 
ATOM   9095  C CE1 . TYR E  1 69  ? -1.063  49.619 3.869   1.00 41.60  ? 69  TYR E CE1 1 
ATOM   9096  C CE2 . TYR E  1 69  ? -1.670  48.001 2.219   1.00 48.25  ? 69  TYR E CE2 1 
ATOM   9097  C CZ  . TYR E  1 69  ? -2.005  48.771 3.318   1.00 42.37  ? 69  TYR E CZ  1 
ATOM   9098  O OH  . TYR E  1 69  ? -3.257  48.693 3.854   1.00 47.56  ? 69  TYR E OH  1 
ATOM   9099  N N   . ILE E  1 70  ? 4.260   50.490 -0.275  1.00 40.07  ? 70  ILE E N   1 
ATOM   9100  C CA  . ILE E  1 70  ? 5.459   51.356 -0.480  1.00 38.79  ? 70  ILE E CA  1 
ATOM   9101  C C   . ILE E  1 70  ? 5.017   52.608 -1.245  1.00 38.93  ? 70  ILE E C   1 
ATOM   9102  O O   . ILE E  1 70  ? 5.399   53.717 -0.829  1.00 38.14  ? 70  ILE E O   1 
ATOM   9103  C CB  . ILE E  1 70  ? 6.590   50.601 -1.206  1.00 37.61  ? 70  ILE E CB  1 
ATOM   9104  C CG1 . ILE E  1 70  ? 7.172   49.490 -0.327  1.00 35.73  ? 70  ILE E CG1 1 
ATOM   9105  C CG2 . ILE E  1 70  ? 7.662   51.571 -1.680  1.00 38.41  ? 70  ILE E CG2 1 
ATOM   9106  C CD1 . ILE E  1 70  ? 8.292   48.709 -0.974  1.00 34.64  ? 70  ILE E CD1 1 
ATOM   9107  N N   . LEU E  1 71  ? 4.225   52.431 -2.306  1.00 41.86  ? 71  LEU E N   1 
ATOM   9108  C CA  . LEU E  1 71  ? 3.680   53.545 -3.127  1.00 49.26  ? 71  LEU E CA  1 
ATOM   9109  C C   . LEU E  1 71  ? 2.780   54.423 -2.249  1.00 50.84  ? 71  LEU E C   1 
ATOM   9110  O O   . LEU E  1 71  ? 2.971   55.651 -2.262  1.00 54.45  ? 71  LEU E O   1 
ATOM   9111  C CB  . LEU E  1 71  ? 2.917   52.973 -4.326  1.00 55.38  ? 71  LEU E CB  1 
ATOM   9112  C CG  . LEU E  1 71  ? 3.776   52.191 -5.320  1.00 68.04  ? 71  LEU E CG  1 
ATOM   9113  C CD1 . LEU E  1 71  ? 2.994   51.855 -6.579  1.00 69.67  ? 71  LEU E CD1 1 
ATOM   9114  C CD2 . LEU E  1 71  ? 5.043   52.959 -5.667  1.00 75.64  ? 71  LEU E CD2 1 
ATOM   9115  N N   . ILE E  1 72  ? 1.851   53.815 -1.506  1.00 48.44  ? 72  ILE E N   1 
ATOM   9116  C CA  . ILE E  1 72  ? 0.914   54.533 -0.590  1.00 48.04  ? 72  ILE E CA  1 
ATOM   9117  C C   . ILE E  1 72  ? 1.737   55.396 0.370   1.00 43.84  ? 72  ILE E C   1 
ATOM   9118  O O   . ILE E  1 72  ? 1.397   56.582 0.542   1.00 40.99  ? 72  ILE E O   1 
ATOM   9119  C CB  . ILE E  1 72  ? 0.003   53.549 0.171   1.00 50.64  ? 72  ILE E CB  1 
ATOM   9120  C CG1 . ILE E  1 72  ? -0.891  52.755 -0.784  1.00 53.52  ? 72  ILE E CG1 1 
ATOM   9121  C CG2 . ILE E  1 72  ? -0.811  54.278 1.230   1.00 50.56  ? 72  ILE E CG2 1 
ATOM   9122  C CD1 . ILE E  1 72  ? -1.722  51.694 -0.102  1.00 56.20  ? 72  ILE E CD1 1 
ATOM   9123  N N   . ILE E  1 73  ? 2.779   54.817 0.969   1.00 37.21  ? 73  ILE E N   1 
ATOM   9124  C CA  . ILE E  1 73  ? 3.683   55.519 1.926   1.00 38.20  ? 73  ILE E CA  1 
ATOM   9125  C C   . ILE E  1 73  ? 4.321   56.712 1.207   1.00 36.90  ? 73  ILE E C   1 
ATOM   9126  O O   . ILE E  1 73  ? 4.308   57.819 1.774   1.00 40.53  ? 73  ILE E O   1 
ATOM   9127  C CB  . ILE E  1 73  ? 4.740   54.555 2.498   1.00 36.60  ? 73  ILE E CB  1 
ATOM   9128  C CG1 . ILE E  1 73  ? 4.095   53.461 3.352   1.00 38.06  ? 73  ILE E CG1 1 
ATOM   9129  C CG2 . ILE E  1 73  ? 5.801   55.323 3.270   1.00 34.19  ? 73  ILE E CG2 1 
ATOM   9130  C CD1 . ILE E  1 73  ? 5.020   52.311 3.677   1.00 38.27  ? 73  ILE E CD1 1 
ATOM   9131  N N   . VAL E  1 74  ? 4.851   56.492 0.002   1.00 35.87  ? 74  VAL E N   1 
ATOM   9132  C CA  . VAL E  1 74  ? 5.508   57.547 -0.825  1.00 38.90  ? 74  VAL E CA  1 
ATOM   9133  C C   . VAL E  1 74  ? 4.488   58.659 -1.091  1.00 40.11  ? 74  VAL E C   1 
ATOM   9134  O O   . VAL E  1 74  ? 4.829   59.836 -0.868  1.00 43.96  ? 74  VAL E O   1 
ATOM   9135  C CB  . VAL E  1 74  ? 6.078   56.971 -2.135  1.00 37.81  ? 74  VAL E CB  1 
ATOM   9136  C CG1 . VAL E  1 74  ? 6.471   58.068 -3.112  1.00 39.03  ? 74  VAL E CG1 1 
ATOM   9137  C CG2 . VAL E  1 74  ? 7.252   56.041 -1.873  1.00 37.75  ? 74  VAL E CG2 1 
ATOM   9138  N N   . ALA E  1 75  ? 3.286   58.291 -1.544  1.00 39.81  ? 75  ALA E N   1 
ATOM   9139  C CA  . ALA E  1 75  ? 2.175   59.220 -1.857  1.00 40.31  ? 75  ALA E CA  1 
ATOM   9140  C C   . ALA E  1 75  ? 1.852   60.060 -0.618  1.00 42.35  ? 75  ALA E C   1 
ATOM   9141  O O   . ALA E  1 75  ? 1.632   61.277 -0.767  1.00 47.56  ? 75  ALA E O   1 
ATOM   9142  C CB  . ALA E  1 75  ? 0.965   58.449 -2.325  1.00 39.51  ? 75  ALA E CB  1 
ATOM   9143  N N   . PHE E  1 76  ? 1.826   59.424 0.556   1.00 41.35  ? 76  PHE E N   1 
ATOM   9144  C CA  . PHE E  1 76  ? 1.530   60.065 1.863   1.00 44.67  ? 76  PHE E CA  1 
ATOM   9145  C C   . PHE E  1 76  ? 2.592   61.129 2.158   1.00 43.34  ? 76  PHE E C   1 
ATOM   9146  O O   . PHE E  1 76  ? 2.229   62.247 2.562   1.00 44.86  ? 76  PHE E O   1 
ATOM   9147  C CB  . PHE E  1 76  ? 1.457   59.017 2.978   1.00 46.61  ? 76  PHE E CB  1 
ATOM   9148  C CG  . PHE E  1 76  ? 1.308   59.590 4.365   1.00 47.55  ? 76  PHE E CG  1 
ATOM   9149  C CD1 . PHE E  1 76  ? 2.402   59.699 5.210   1.00 49.74  ? 76  PHE E CD1 1 
ATOM   9150  C CD2 . PHE E  1 76  ? 0.076   60.029 4.825   1.00 45.16  ? 76  PHE E CD2 1 
ATOM   9151  C CE1 . PHE E  1 76  ? 2.265   60.229 6.485   1.00 51.93  ? 76  PHE E CE1 1 
ATOM   9152  C CE2 . PHE E  1 76  ? -0.058  60.564 6.098   1.00 47.76  ? 76  PHE E CE2 1 
ATOM   9153  C CZ  . PHE E  1 76  ? 1.037   60.665 6.926   1.00 48.87  ? 76  PHE E CZ  1 
ATOM   9154  N N   . LEU E  1 77  ? 3.867   60.788 1.954   1.00 47.81  ? 77  LEU E N   1 
ATOM   9155  C CA  . LEU E  1 77  ? 5.024   61.672 2.259   1.00 53.24  ? 77  LEU E CA  1 
ATOM   9156  C C   . LEU E  1 77  ? 5.034   62.869 1.298   1.00 53.42  ? 77  LEU E C   1 
ATOM   9157  O O   . LEU E  1 77  ? 5.538   63.938 1.697   1.00 48.15  ? 77  LEU E O   1 
ATOM   9158  C CB  . LEU E  1 77  ? 6.317   60.855 2.160   1.00 52.23  ? 77  LEU E CB  1 
ATOM   9159  C CG  . LEU E  1 77  ? 6.483   59.766 3.219   1.00 51.24  ? 77  LEU E CG  1 
ATOM   9160  C CD1 . LEU E  1 77  ? 7.799   59.026 3.038   1.00 51.92  ? 77  LEU E CD1 1 
ATOM   9161  C CD2 . LEU E  1 77  ? 6.389   60.347 4.622   1.00 50.40  ? 77  LEU E CD2 1 
ATOM   9162  N N   . LEU E  1 78  ? 4.481   62.704 0.092   1.00 50.35  ? 78  LEU E N   1 
ATOM   9163  C CA  . LEU E  1 78  ? 4.447   63.754 -0.963  1.00 54.75  ? 78  LEU E CA  1 
ATOM   9164  C C   . LEU E  1 78  ? 3.057   64.401 -1.033  1.00 54.60  ? 78  LEU E C   1 
ATOM   9165  O O   . LEU E  1 78  ? 2.864   65.281 -1.892  1.00 54.78  ? 78  LEU E O   1 
ATOM   9166  C CB  . LEU E  1 78  ? 4.809   63.117 -2.308  1.00 53.80  ? 78  LEU E CB  1 
ATOM   9167  C CG  . LEU E  1 78  ? 6.199   62.492 -2.394  1.00 50.30  ? 78  LEU E CG  1 
ATOM   9168  C CD1 . LEU E  1 78  ? 6.505   62.069 -3.823  1.00 47.53  ? 78  LEU E CD1 1 
ATOM   9169  C CD2 . LEU E  1 78  ? 7.264   63.452 -1.884  1.00 49.57  ? 78  LEU E CD2 1 
ATOM   9170  N N   . GLY E  1 79  ? 2.131   63.982 -0.167  1.00 57.30  ? 79  GLY E N   1 
ATOM   9171  C CA  . GLY E  1 79  ? 0.712   64.378 -0.234  1.00 55.79  ? 79  GLY E CA  1 
ATOM   9172  C C   . GLY E  1 79  ? 0.391   65.548 0.679   1.00 58.02  ? 79  GLY E C   1 
ATOM   9173  O O   . GLY E  1 79  ? -0.619  66.229 0.417   1.00 64.71  ? 79  GLY E O   1 
ATOM   9174  N N   . TYR E  1 80  ? 1.211   65.777 1.711   1.00 53.43  ? 80  TYR E N   1 
ATOM   9175  C CA  . TYR E  1 80  ? 0.969   66.801 2.762   1.00 52.83  ? 80  TYR E CA  1 
ATOM   9176  C C   . TYR E  1 80  ? 2.224   67.655 2.963   1.00 53.84  ? 80  TYR E C   1 
ATOM   9177  O O   . TYR E  1 80  ? 3.342   67.124 2.835   1.00 65.12  ? 80  TYR E O   1 
ATOM   9178  C CB  . TYR E  1 80  ? 0.534   66.135 4.071   1.00 54.44  ? 80  TYR E CB  1 
ATOM   9179  C CG  . TYR E  1 80  ? -0.840  65.516 4.026   1.00 51.59  ? 80  TYR E CG  1 
ATOM   9180  C CD1 . TYR E  1 80  ? -1.969  66.260 4.321   1.00 49.60  ? 80  TYR E CD1 1 
ATOM   9181  C CD2 . TYR E  1 80  ? -1.015  64.188 3.675   1.00 51.18  ? 80  TYR E CD2 1 
ATOM   9182  C CE1 . TYR E  1 80  ? -3.236  65.702 4.273   1.00 55.53  ? 80  TYR E CE1 1 
ATOM   9183  C CE2 . TYR E  1 80  ? -2.274  63.613 3.625   1.00 51.02  ? 80  TYR E CE2 1 
ATOM   9184  C CZ  . TYR E  1 80  ? -3.391  64.373 3.924   1.00 55.62  ? 80  TYR E CZ  1 
ATOM   9185  O OH  . TYR E  1 80  ? -4.640  63.821 3.878   1.00 57.99  ? 80  TYR E OH  1 
ATOM   9186  N N   . ASP E  1 81  ? 2.026   68.941 3.266   1.00 55.38  ? 81  ASP E N   1 
ATOM   9187  C CA  . ASP E  1 81  ? 3.097   69.913 3.610   1.00 55.43  ? 81  ASP E CA  1 
ATOM   9188  C C   . ASP E  1 81  ? 2.873   70.393 5.048   1.00 53.79  ? 81  ASP E C   1 
ATOM   9189  O O   . ASP E  1 81  ? 1.734   70.786 5.364   1.00 53.26  ? 81  ASP E O   1 
ATOM   9190  C CB  . ASP E  1 81  ? 3.108   71.092 2.633   1.00 54.71  ? 81  ASP E CB  1 
ATOM   9191  C CG  . ASP E  1 81  ? 2.894   70.694 1.184   1.00 57.95  ? 81  ASP E CG  1 
ATOM   9192  O OD1 . ASP E  1 81  ? 3.903   70.542 0.468   1.00 53.05  ? 81  ASP E OD1 1 
ATOM   9193  O OD2 . ASP E  1 81  ? 1.719   70.564 0.777   1.00 66.43  ? 81  ASP E OD2 1 
ATOM   9194  N N   . SER E  1 82  ? 3.914   70.357 5.885   1.00 51.04  ? 82  SER E N   1 
ATOM   9195  C CA  . SER E  1 82  ? 3.865   70.808 7.300   1.00 53.95  ? 82  SER E CA  1 
ATOM   9196  C C   . SER E  1 82  ? 3.801   72.338 7.340   1.00 55.10  ? 82  SER E C   1 
ATOM   9197  O O   . SER E  1 82  ? 4.600   72.980 6.634   1.00 52.01  ? 82  SER E O   1 
ATOM   9198  C CB  . SER E  1 82  ? 5.039   70.296 8.087   1.00 57.44  ? 82  SER E CB  1 
ATOM   9199  O OG  . SER E  1 82  ? 4.836   70.500 9.478   1.00 66.73  ? 82  SER E OG  1 
ATOM   9200  N N   . THR E  1 83  ? 2.879   72.889 8.135   1.00 64.15  ? 83  THR E N   1 
ATOM   9201  C CA  . THR E  1 83  ? 2.631   74.349 8.271   1.00 75.15  ? 83  THR E CA  1 
ATOM   9202  C C   . THR E  1 83  ? 2.364   74.678 9.744   1.00 77.24  ? 83  THR E C   1 
ATOM   9203  O O   . THR E  1 83  ? 2.489   73.766 10.585  1.00 65.51  ? 83  THR E O   1 
ATOM   9204  C CB  . THR E  1 83  ? 1.457   74.799 7.390   1.00 82.67  ? 83  THR E CB  1 
ATOM   9205  O OG1 . THR E  1 83  ? 0.274   74.176 7.890   1.00 97.52  ? 83  THR E OG1 1 
ATOM   9206  C CG2 . THR E  1 83  ? 1.633   74.449 5.928   1.00 82.59  ? 83  THR E CG2 1 
ATOM   9207  N N   . ALA E  1 84  ? 2.015   75.935 10.033  1.00 95.60  ? 84  ALA E N   1 
ATOM   9208  C CA  . ALA E  1 84  ? 1.586   76.416 11.366  1.00 99.72  ? 84  ALA E CA  1 
ATOM   9209  C C   . ALA E  1 84  ? 0.224   75.801 11.709  1.00 109.89 ? 84  ALA E C   1 
ATOM   9210  O O   . ALA E  1 84  ? -0.118  75.759 12.907  1.00 105.53 ? 84  ALA E O   1 
ATOM   9211  C CB  . ALA E  1 84  ? 1.528   77.924 11.376  1.00 90.97  ? 84  ALA E CB  1 
ATOM   9212  N N   . GLY E  1 85  ? -0.510  75.339 10.689  1.00 104.50 ? 85  GLY E N   1 
ATOM   9213  C CA  . GLY E  1 85  ? -1.886  74.817 10.806  1.00 89.65  ? 85  GLY E CA  1 
ATOM   9214  C C   . GLY E  1 85  ? -1.927  73.299 10.885  1.00 96.13  ? 85  GLY E C   1 
ATOM   9215  O O   . GLY E  1 85  ? -3.044  72.754 10.983  1.00 91.23  ? 85  GLY E O   1 
ATOM   9216  N N   . GLY E  1 86  ? -0.760  72.643 10.854  1.00 98.76  ? 86  GLY E N   1 
ATOM   9217  C CA  . GLY E  1 86  ? -0.618  71.174 10.943  1.00 83.04  ? 86  GLY E CA  1 
ATOM   9218  C C   . GLY E  1 86  ? 0.054   70.591 9.709   1.00 69.71  ? 86  GLY E C   1 
ATOM   9219  O O   . GLY E  1 86  ? 1.192   70.995 9.420   1.00 73.80  ? 86  GLY E O   1 
ATOM   9220  N N   . TRP E  1 87  ? -0.623  69.666 9.017   1.00 58.31  ? 87  TRP E N   1 
ATOM   9221  C CA  . TRP E  1 87  ? -0.205  69.087 7.710   1.00 51.47  ? 87  TRP E CA  1 
ATOM   9222  C C   . TRP E  1 87  ? -1.289  69.362 6.663   1.00 48.17  ? 87  TRP E C   1 
ATOM   9223  O O   . TRP E  1 87  ? -2.363  68.736 6.739   1.00 57.07  ? 87  TRP E O   1 
ATOM   9224  C CB  . TRP E  1 87  ? 0.076   67.585 7.839   1.00 47.86  ? 87  TRP E CB  1 
ATOM   9225  C CG  . TRP E  1 87  ? 1.327   67.268 8.598   1.00 45.61  ? 87  TRP E CG  1 
ATOM   9226  C CD1 . TRP E  1 87  ? 1.449   67.112 9.947   1.00 46.22  ? 87  TRP E CD1 1 
ATOM   9227  C CD2 . TRP E  1 87  ? 2.642   67.071 8.050   1.00 44.72  ? 87  TRP E CD2 1 
ATOM   9228  N NE1 . TRP E  1 87  ? 2.747   66.831 10.278  1.00 48.86  ? 87  TRP E NE1 1 
ATOM   9229  C CE2 . TRP E  1 87  ? 3.502   66.797 9.135   1.00 46.46  ? 87  TRP E CE2 1 
ATOM   9230  C CE3 . TRP E  1 87  ? 3.177   67.100 6.756   1.00 43.00  ? 87  TRP E CE3 1 
ATOM   9231  C CZ2 . TRP E  1 87  ? 4.865   66.556 8.961   1.00 45.30  ? 87  TRP E CZ2 1 
ATOM   9232  C CZ3 . TRP E  1 87  ? 4.523   66.861 6.587   1.00 42.91  ? 87  TRP E CZ3 1 
ATOM   9233  C CH2 . TRP E  1 87  ? 5.353   66.593 7.675   1.00 42.35  ? 87  TRP E CH2 1 
ATOM   9234  N N   . VAL E  1 88  ? -1.018  70.269 5.724   1.00 44.58  ? 88  VAL E N   1 
ATOM   9235  C CA  . VAL E  1 88  ? -2.019  70.765 4.733   1.00 48.60  ? 88  VAL E CA  1 
ATOM   9236  C C   . VAL E  1 88  ? -1.939  69.914 3.472   1.00 46.69  ? 88  VAL E C   1 
ATOM   9237  O O   . VAL E  1 88  ? -0.865  69.743 2.899   1.00 45.83  ? 88  VAL E O   1 
ATOM   9238  C CB  . VAL E  1 88  ? -1.808  72.256 4.411   1.00 49.32  ? 88  VAL E CB  1 
ATOM   9239  C CG1 . VAL E  1 88  ? -2.745  72.724 3.308   1.00 46.85  ? 88  VAL E CG1 1 
ATOM   9240  C CG2 . VAL E  1 88  ? -1.954  73.126 5.649   1.00 47.60  ? 88  VAL E CG2 1 
ATOM   9241  N N   . PRO E  1 89  ? -3.081  69.368 2.999   1.00 46.12  ? 89  PRO E N   1 
ATOM   9242  C CA  . PRO E  1 89  ? -3.116  68.603 1.755   1.00 47.05  ? 89  PRO E CA  1 
ATOM   9243  C C   . PRO E  1 89  ? -2.607  69.439 0.572   1.00 48.16  ? 89  PRO E C   1 
ATOM   9244  O O   . PRO E  1 89  ? -2.950  70.602 0.494   1.00 56.06  ? 89  PRO E O   1 
ATOM   9245  C CB  . PRO E  1 89  ? -4.602  68.255 1.560   1.00 43.47  ? 89  PRO E CB  1 
ATOM   9246  C CG  . PRO E  1 89  ? -5.215  68.386 2.943   1.00 47.16  ? 89  PRO E CG  1 
ATOM   9247  C CD  . PRO E  1 89  ? -4.401  69.459 3.639   1.00 48.50  ? 89  PRO E CD  1 
ATOM   9248  N N   . ASN E  1 90  ? -1.796  68.833 -0.300  1.00 49.53  ? 90  ASN E N   1 
ATOM   9249  C CA  . ASN E  1 90  ? -1.428  69.390 -1.628  1.00 51.26  ? 90  ASN E CA  1 
ATOM   9250  C C   . ASN E  1 90  ? -2.217  68.617 -2.693  1.00 53.13  ? 90  ASN E C   1 
ATOM   9251  O O   . ASN E  1 90  ? -3.099  67.821 -2.309  1.00 56.80  ? 90  ASN E O   1 
ATOM   9252  C CB  . ASN E  1 90  ? 0.087   69.373 -1.856  1.00 48.07  ? 90  ASN E CB  1 
ATOM   9253  C CG  . ASN E  1 90  ? 0.669   67.976 -1.906  1.00 50.43  ? 90  ASN E CG  1 
ATOM   9254  O OD1 . ASN E  1 90  ? 0.184   67.124 -2.649  1.00 62.12  ? 90  ASN E OD1 1 
ATOM   9255  N ND2 . ASN E  1 90  ? 1.709   67.735 -1.123  1.00 54.51  ? 90  ASN E ND2 1 
ATOM   9256  N N   . ASP E  1 91  ? -1.924  68.847 -3.976  1.00 57.08  ? 91  ASP E N   1 
ATOM   9257  C CA  . ASP E  1 91  ? -2.693  68.278 -5.115  1.00 63.47  ? 91  ASP E CA  1 
ATOM   9258  C C   . ASP E  1 91  ? -2.578  66.747 -5.104  1.00 62.45  ? 91  ASP E C   1 
ATOM   9259  O O   . ASP E  1 91  ? -3.540  66.082 -5.541  1.00 66.25  ? 91  ASP E O   1 
ATOM   9260  C CB  . ASP E  1 91  ? -2.229  68.873 -6.446  1.00 71.27  ? 91  ASP E CB  1 
ATOM   9261  C CG  . ASP E  1 91  ? -2.593  70.339 -6.615  1.00 77.89  ? 91  ASP E CG  1 
ATOM   9262  O OD1 . ASP E  1 91  ? -2.901  70.989 -5.596  1.00 74.04  ? 91  ASP E OD1 1 
ATOM   9263  O OD2 . ASP E  1 91  ? -2.570  70.819 -7.765  1.00 92.43  ? 91  ASP E OD2 1 
ATOM   9264  N N   . GLY E  1 92  ? -1.459  66.214 -4.605  1.00 63.77  ? 92  GLY E N   1 
ATOM   9265  C CA  . GLY E  1 92  ? -1.123  64.777 -4.672  1.00 63.77  ? 92  GLY E CA  1 
ATOM   9266  C C   . GLY E  1 92  ? -1.702  63.976 -3.516  1.00 59.29  ? 92  GLY E C   1 
ATOM   9267  O O   . GLY E  1 92  ? -1.477  62.747 -3.485  1.00 64.64  ? 92  GLY E O   1 
ATOM   9268  N N   . ALA E  1 93  ? -2.423  64.629 -2.599  1.00 52.54  ? 93  ALA E N   1 
ATOM   9269  C CA  . ALA E  1 93  ? -3.018  64.006 -1.393  1.00 51.96  ? 93  ALA E CA  1 
ATOM   9270  C C   . ALA E  1 93  ? -4.028  62.928 -1.807  1.00 50.77  ? 93  ALA E C   1 
ATOM   9271  O O   . ALA E  1 93  ? -4.156  61.917 -1.084  1.00 52.33  ? 93  ALA E O   1 
ATOM   9272  C CB  . ALA E  1 93  ? -3.661  65.063 -0.533  1.00 53.87  ? 93  ALA E CB  1 
ATOM   9273  N N   . ILE E  1 94  ? -4.716  63.148 -2.930  1.00 52.87  ? 94  ILE E N   1 
ATOM   9274  C CA  . ILE E  1 94  ? -5.738  62.219 -3.498  1.00 52.41  ? 94  ILE E CA  1 
ATOM   9275  C C   . ILE E  1 94  ? -5.078  60.867 -3.788  1.00 52.32  ? 94  ILE E C   1 
ATOM   9276  O O   . ILE E  1 94  ? -5.765  59.831 -3.661  1.00 57.90  ? 94  ILE E O   1 
ATOM   9277  C CB  . ILE E  1 94  ? -6.378  62.827 -4.764  1.00 49.24  ? 94  ILE E CB  1 
ATOM   9278  C CG1 . ILE E  1 94  ? -7.499  61.940 -5.313  1.00 51.01  ? 94  ILE E CG1 1 
ATOM   9279  C CG2 . ILE E  1 94  ? -5.321  63.120 -5.820  1.00 44.64  ? 94  ILE E CG2 1 
ATOM   9280  C CD1 . ILE E  1 94  ? -8.200  62.515 -6.523  1.00 53.07  ? 94  ILE E CD1 1 
ATOM   9281  N N   . ASN E  1 95  ? -3.794  60.885 -4.158  1.00 49.15  ? 95  ASN E N   1 
ATOM   9282  C CA  . ASN E  1 95  ? -3.036  59.695 -4.627  1.00 50.52  ? 95  ASN E CA  1 
ATOM   9283  C C   . ASN E  1 95  ? -2.952  58.664 -3.496  1.00 49.19  ? 95  ASN E C   1 
ATOM   9284  O O   . ASN E  1 95  ? -2.870  57.459 -3.804  1.00 50.96  ? 95  ASN E O   1 
ATOM   9285  C CB  . ASN E  1 95  ? -1.655  60.084 -5.157  1.00 54.24  ? 95  ASN E CB  1 
ATOM   9286  C CG  . ASN E  1 95  ? -1.735  60.926 -6.413  1.00 52.96  ? 95  ASN E CG  1 
ATOM   9287  O OD1 . ASN E  1 95  ? -2.754  60.923 -7.100  1.00 57.32  ? 95  ASN E OD1 1 
ATOM   9288  N ND2 . ASN E  1 95  ? -0.672  61.651 -6.720  1.00 52.56  ? 95  ASN E ND2 1 
ATOM   9289  N N   . ILE E  1 96  ? -2.976  59.120 -2.240  1.00 47.21  ? 96  ILE E N   1 
ATOM   9290  C CA  . ILE E  1 96  ? -2.949  58.238 -1.034  1.00 51.95  ? 96  ILE E CA  1 
ATOM   9291  C C   . ILE E  1 96  ? -4.126  57.260 -1.115  1.00 53.53  ? 96  ILE E C   1 
ATOM   9292  O O   . ILE E  1 96  ? -3.936  56.074 -0.775  1.00 64.68  ? 96  ILE E O   1 
ATOM   9293  C CB  . ILE E  1 96  ? -2.986  59.073 0.259   1.00 51.39  ? 96  ILE E CB  1 
ATOM   9294  C CG1 . ILE E  1 96  ? -1.750  59.968 0.374   1.00 60.17  ? 96  ILE E CG1 1 
ATOM   9295  C CG2 . ILE E  1 96  ? -3.151  58.178 1.478   1.00 46.60  ? 96  ILE E CG2 1 
ATOM   9296  C CD1 . ILE E  1 96  ? -1.800  60.932 1.533   1.00 69.27  ? 96  ILE E CD1 1 
ATOM   9297  N N   . PHE E  1 97  ? -5.290  57.746 -1.555  1.00 46.89  ? 97  PHE E N   1 
ATOM   9298  C CA  . PHE E  1 97  ? -6.542  56.960 -1.702  1.00 47.39  ? 97  PHE E CA  1 
ATOM   9299  C C   . PHE E  1 97  ? -6.525  56.243 -3.054  1.00 47.23  ? 97  PHE E C   1 
ATOM   9300  O O   . PHE E  1 97  ? -6.858  55.041 -3.107  1.00 43.58  ? 97  PHE E O   1 
ATOM   9301  C CB  . PHE E  1 97  ? -7.753  57.880 -1.546  1.00 53.95  ? 97  PHE E CB  1 
ATOM   9302  C CG  . PHE E  1 97  ? -7.853  58.511 -0.181  1.00 61.32  ? 97  PHE E CG  1 
ATOM   9303  C CD1 . PHE E  1 97  ? -8.658  57.952 0.799   1.00 59.50  ? 97  PHE E CD1 1 
ATOM   9304  C CD2 . PHE E  1 97  ? -7.119  59.644 0.132   1.00 64.62  ? 97  PHE E CD2 1 
ATOM   9305  C CE1 . PHE E  1 97  ? -8.740  58.524 2.058   1.00 61.79  ? 97  PHE E CE1 1 
ATOM   9306  C CE2 . PHE E  1 97  ? -7.205  60.217 1.391   1.00 62.83  ? 97  PHE E CE2 1 
ATOM   9307  C CZ  . PHE E  1 97  ? -8.012  59.653 2.352   1.00 65.64  ? 97  PHE E CZ  1 
ATOM   9308  N N   . SER E  1 98  ? -6.141  56.970 -4.106  1.00 47.80  ? 98  SER E N   1 
ATOM   9309  C CA  . SER E  1 98  ? -5.949  56.450 -5.484  1.00 50.86  ? 98  SER E CA  1 
ATOM   9310  C C   . SER E  1 98  ? -5.140  55.148 -5.443  1.00 54.32  ? 98  SER E C   1 
ATOM   9311  O O   . SER E  1 98  ? -5.609  54.140 -6.009  1.00 51.74  ? 98  SER E O   1 
ATOM   9312  C CB  . SER E  1 98  ? -5.277  57.482 -6.348  1.00 48.76  ? 98  SER E CB  1 
ATOM   9313  O OG  . SER E  1 98  ? -5.144  57.015 -7.681  1.00 58.85  ? 98  SER E OG  1 
ATOM   9314  N N   . THR E  1 99  ? -3.973  55.176 -4.791  1.00 56.87  ? 99  THR E N   1 
ATOM   9315  C CA  . THR E  1 99  ? -2.983  54.065 -4.757  1.00 54.93  ? 99  THR E CA  1 
ATOM   9316  C C   . THR E  1 99  ? -3.600  52.827 -4.095  1.00 49.74  ? 99  THR E C   1 
ATOM   9317  O O   . THR E  1 99  ? -3.261  51.708 -4.521  1.00 49.84  ? 99  THR E O   1 
ATOM   9318  C CB  . THR E  1 99  ? -1.694  54.486 -4.039  1.00 64.58  ? 99  THR E CB  1 
ATOM   9319  O OG1 . THR E  1 99  ? -1.293  55.755 -4.556  1.00 75.38  ? 99  THR E OG1 1 
ATOM   9320  C CG2 . THR E  1 99  ? -0.571  53.484 -4.208  1.00 71.91  ? 99  THR E CG2 1 
ATOM   9321  N N   . ARG E  1 100 ? -4.462  53.015 -3.093  1.00 47.03  ? 100 ARG E N   1 
ATOM   9322  C CA  . ARG E  1 100 ? -5.065  51.893 -2.325  1.00 46.71  ? 100 ARG E CA  1 
ATOM   9323  C C   . ARG E  1 100 ? -5.996  51.095 -3.243  1.00 46.92  ? 100 ARG E C   1 
ATOM   9324  O O   . ARG E  1 100 ? -6.006  49.855 -3.133  1.00 46.81  ? 100 ARG E O   1 
ATOM   9325  C CB  . ARG E  1 100 ? -5.810  52.398 -1.087  1.00 51.80  ? 100 ARG E CB  1 
ATOM   9326  C CG  . ARG E  1 100 ? -5.914  51.353 0.014   1.00 58.95  ? 100 ARG E CG  1 
ATOM   9327  C CD  . ARG E  1 100 ? -6.681  51.845 1.223   1.00 64.07  ? 100 ARG E CD  1 
ATOM   9328  N NE  . ARG E  1 100 ? -5.860  52.640 2.123   1.00 64.09  ? 100 ARG E NE  1 
ATOM   9329  C CZ  . ARG E  1 100 ? -5.063  52.134 3.055   1.00 66.92  ? 100 ARG E CZ  1 
ATOM   9330  N NH1 . ARG E  1 100 ? -4.963  50.824 3.207   1.00 68.05  ? 100 ARG E NH1 1 
ATOM   9331  N NH2 . ARG E  1 100 ? -4.365  52.942 3.832   1.00 75.21  ? 100 ARG E NH2 1 
ATOM   9332  N N   . TYR E  1 101 ? -6.744  51.778 -4.113  1.00 49.40  ? 101 TYR E N   1 
ATOM   9333  C CA  . TYR E  1 101 ? -7.624  51.150 -5.134  1.00 53.14  ? 101 TYR E CA  1 
ATOM   9334  C C   . TYR E  1 101 ? -6.764  50.267 -6.045  1.00 50.71  ? 101 TYR E C   1 
ATOM   9335  O O   . TYR E  1 101 ? -7.109  49.085 -6.244  1.00 52.42  ? 101 TYR E O   1 
ATOM   9336  C CB  . TYR E  1 101 ? -8.406  52.213 -5.912  1.00 57.11  ? 101 TYR E CB  1 
ATOM   9337  C CG  . TYR E  1 101 ? -9.596  52.769 -5.171  1.00 65.13  ? 101 TYR E CG  1 
ATOM   9338  C CD1 . TYR E  1 101 ? -10.819 52.118 -5.188  1.00 65.14  ? 101 TYR E CD1 1 
ATOM   9339  C CD2 . TYR E  1 101 ? -9.499  53.940 -4.436  1.00 73.93  ? 101 TYR E CD2 1 
ATOM   9340  C CE1 . TYR E  1 101 ? -11.914 52.614 -4.500  1.00 65.86  ? 101 TYR E CE1 1 
ATOM   9341  C CE2 . TYR E  1 101 ? -10.584 54.451 -3.744  1.00 77.44  ? 101 TYR E CE2 1 
ATOM   9342  C CZ  . TYR E  1 101 ? -11.797 53.787 -3.775  1.00 74.41  ? 101 TYR E CZ  1 
ATOM   9343  O OH  . TYR E  1 101 ? -12.870 54.288 -3.094  1.00 74.46  ? 101 TYR E OH  1 
ATOM   9344  N N   . ILE E  1 102 ? -5.667  50.825 -6.564  1.00 43.38  ? 102 ILE E N   1 
ATOM   9345  C CA  . ILE E  1 102 ? -4.669  50.098 -7.403  1.00 43.79  ? 102 ILE E CA  1 
ATOM   9346  C C   . ILE E  1 102 ? -4.311  48.781 -6.703  1.00 44.51  ? 102 ILE E C   1 
ATOM   9347  O O   . ILE E  1 102 ? -4.355  47.728 -7.365  1.00 42.11  ? 102 ILE E O   1 
ATOM   9348  C CB  . ILE E  1 102 ? -3.423  50.967 -7.660  1.00 46.51  ? 102 ILE E CB  1 
ATOM   9349  C CG1 . ILE E  1 102 ? -3.776  52.265 -8.392  1.00 51.52  ? 102 ILE E CG1 1 
ATOM   9350  C CG2 . ILE E  1 102 ? -2.366  50.171 -8.409  1.00 48.72  ? 102 ILE E CG2 1 
ATOM   9351  C CD1 . ILE E  1 102 ? -2.582  53.129 -8.733  1.00 52.06  ? 102 ILE E CD1 1 
ATOM   9352  N N   . GLU E  1 103 ? -3.973  48.843 -5.413  1.00 45.04  ? 103 GLU E N   1 
ATOM   9353  C CA  . GLU E  1 103 ? -3.634  47.654 -4.588  1.00 48.95  ? 103 GLU E CA  1 
ATOM   9354  C C   . GLU E  1 103 ? -4.761  46.624 -4.702  1.00 47.48  ? 103 GLU E C   1 
ATOM   9355  O O   . GLU E  1 103 ? -4.502  45.519 -5.213  1.00 58.29  ? 103 GLU E O   1 
ATOM   9356  C CB  . GLU E  1 103 ? -3.437  48.040 -3.122  1.00 56.25  ? 103 GLU E CB  1 
ATOM   9357  C CG  . GLU E  1 103 ? -3.306  46.840 -2.202  1.00 57.03  ? 103 GLU E CG  1 
ATOM   9358  C CD  . GLU E  1 103 ? -3.790  47.077 -0.783  1.00 60.68  ? 103 GLU E CD  1 
ATOM   9359  O OE1 . GLU E  1 103 ? -4.117  46.089 -0.103  1.00 56.82  ? 103 GLU E OE1 1 
ATOM   9360  O OE2 . GLU E  1 103 ? -3.845  48.250 -0.362  1.00 66.67  ? 103 GLU E OE2 1 
ATOM   9361  N N   . TRP E  1 104 ? -5.958  46.987 -4.234  1.00 47.62  ? 104 TRP E N   1 
ATOM   9362  C CA  . TRP E  1 104 ? -7.155  46.107 -4.176  1.00 49.59  ? 104 TRP E CA  1 
ATOM   9363  C C   . TRP E  1 104 ? -7.388  45.453 -5.541  1.00 50.27  ? 104 TRP E C   1 
ATOM   9364  O O   . TRP E  1 104 ? -7.645  44.234 -5.576  1.00 54.58  ? 104 TRP E O   1 
ATOM   9365  C CB  . TRP E  1 104 ? -8.387  46.900 -3.727  1.00 54.12  ? 104 TRP E CB  1 
ATOM   9366  C CG  . TRP E  1 104 ? -8.281  47.455 -2.342  1.00 55.32  ? 104 TRP E CG  1 
ATOM   9367  C CD1 . TRP E  1 104 ? -7.480  47.003 -1.335  1.00 62.10  ? 104 TRP E CD1 1 
ATOM   9368  C CD2 . TRP E  1 104 ? -9.031  48.553 -1.795  1.00 60.89  ? 104 TRP E CD2 1 
ATOM   9369  N NE1 . TRP E  1 104 ? -7.668  47.752 -0.205  1.00 64.16  ? 104 TRP E NE1 1 
ATOM   9370  C CE2 . TRP E  1 104 ? -8.616  48.709 -0.456  1.00 62.27  ? 104 TRP E CE2 1 
ATOM   9371  C CE3 . TRP E  1 104 ? -10.007 49.418 -2.303  1.00 62.60  ? 104 TRP E CE3 1 
ATOM   9372  C CZ2 . TRP E  1 104 ? -9.141  49.696 0.376   1.00 61.00  ? 104 TRP E CZ2 1 
ATOM   9373  C CZ3 . TRP E  1 104 ? -10.526 50.392 -1.480  1.00 61.31  ? 104 TRP E CZ3 1 
ATOM   9374  C CH2 . TRP E  1 104 ? -10.097 50.528 -0.160  1.00 63.09  ? 104 TRP E CH2 1 
ATOM   9375  N N   . THR E  1 105 ? -7.311  46.246 -6.614  1.00 47.39  ? 105 THR E N   1 
ATOM   9376  C CA  . THR E  1 105 ? -7.557  45.816 -8.016  1.00 45.78  ? 105 THR E CA  1 
ATOM   9377  C C   . THR E  1 105 ? -6.857  44.475 -8.267  1.00 49.72  ? 105 THR E C   1 
ATOM   9378  O O   . THR E  1 105 ? -7.463  43.614 -8.931  1.00 55.93  ? 105 THR E O   1 
ATOM   9379  C CB  . THR E  1 105 ? -7.091  46.890 -9.006  1.00 43.24  ? 105 THR E CB  1 
ATOM   9380  O OG1 . THR E  1 105 ? -7.828  48.082 -8.728  1.00 41.06  ? 105 THR E OG1 1 
ATOM   9381  C CG2 . THR E  1 105 ? -7.272  46.487 -10.454 1.00 40.81  ? 105 THR E CG2 1 
ATOM   9382  N N   . VAL E  1 106 ? -5.635  44.311 -7.749  1.00 48.85  ? 106 VAL E N   1 
ATOM   9383  C CA  . VAL E  1 106 ? -4.764  43.126 -8.012  1.00 48.09  ? 106 VAL E CA  1 
ATOM   9384  C C   . VAL E  1 106 ? -4.818  42.176 -6.811  1.00 48.26  ? 106 VAL E C   1 
ATOM   9385  O O   . VAL E  1 106 ? -4.984  40.963 -7.032  1.00 50.18  ? 106 VAL E O   1 
ATOM   9386  C CB  . VAL E  1 106 ? -3.316  43.547 -8.326  1.00 48.97  ? 106 VAL E CB  1 
ATOM   9387  C CG1 . VAL E  1 106 ? -2.471  42.359 -8.766  1.00 48.73  ? 106 VAL E CG1 1 
ATOM   9388  C CG2 . VAL E  1 106 ? -3.263  44.656 -9.367  1.00 49.46  ? 106 VAL E CG2 1 
ATOM   9389  N N   . SER E  1 107 ? -4.678  42.704 -5.592  1.00 50.17  ? 107 SER E N   1 
ATOM   9390  C CA  . SER E  1 107 ? -4.536  41.905 -4.345  1.00 54.80  ? 107 SER E CA  1 
ATOM   9391  C C   . SER E  1 107 ? -5.789  41.049 -4.114  1.00 56.73  ? 107 SER E C   1 
ATOM   9392  O O   . SER E  1 107 ? -5.634  39.884 -3.695  1.00 63.50  ? 107 SER E O   1 
ATOM   9393  C CB  . SER E  1 107 ? -4.237  42.786 -3.158  1.00 56.97  ? 107 SER E CB  1 
ATOM   9394  O OG  . SER E  1 107 ? -5.274  43.733 -2.951  1.00 65.06  ? 107 SER E OG  1 
ATOM   9395  N N   . VAL E  1 108 ? -6.978  41.598 -4.388  1.00 52.61  ? 108 VAL E N   1 
ATOM   9396  C CA  . VAL E  1 108 ? -8.291  40.948 -4.090  1.00 51.04  ? 108 VAL E CA  1 
ATOM   9397  C C   . VAL E  1 108 ? -8.488  39.749 -5.015  1.00 50.95  ? 108 VAL E C   1 
ATOM   9398  O O   . VAL E  1 108 ? -8.686  38.631 -4.544  1.00 48.51  ? 108 VAL E O   1 
ATOM   9399  C CB  . VAL E  1 108 ? -9.459  41.946 -4.204  1.00 53.52  ? 108 VAL E CB  1 
ATOM   9400  C CG1 . VAL E  1 108 ? -10.804 41.239 -4.198  1.00 56.77  ? 108 VAL E CG1 1 
ATOM   9401  C CG2 . VAL E  1 108 ? -9.407  42.997 -3.107  1.00 58.85  ? 108 VAL E CG2 1 
ATOM   9402  N N   . PRO E  1 109 ? -8.464  39.937 -6.355  1.00 50.40  ? 109 PRO E N   1 
ATOM   9403  C CA  . PRO E  1 109 ? -8.606  38.819 -7.287  1.00 50.05  ? 109 PRO E CA  1 
ATOM   9404  C C   . PRO E  1 109 ? -7.722  37.619 -6.909  1.00 53.52  ? 109 PRO E C   1 
ATOM   9405  O O   . PRO E  1 109 ? -8.176  36.496 -7.033  1.00 55.32  ? 109 PRO E O   1 
ATOM   9406  C CB  . PRO E  1 109 ? -8.175  39.428 -8.629  1.00 47.62  ? 109 PRO E CB  1 
ATOM   9407  C CG  . PRO E  1 109 ? -8.564  40.887 -8.502  1.00 46.84  ? 109 PRO E CG  1 
ATOM   9408  C CD  . PRO E  1 109 ? -8.321  41.229 -7.045  1.00 48.74  ? 109 PRO E CD  1 
ATOM   9409  N N   . LEU E  1 110 ? -6.492  37.883 -6.460  1.00 52.83  ? 110 LEU E N   1 
ATOM   9410  C CA  . LEU E  1 110 ? -5.526  36.840 -6.023  1.00 49.44  ? 110 LEU E CA  1 
ATOM   9411  C C   . LEU E  1 110 ? -6.092  36.116 -4.798  1.00 51.85  ? 110 LEU E C   1 
ATOM   9412  O O   . LEU E  1 110 ? -5.873  34.895 -4.682  1.00 54.53  ? 110 LEU E O   1 
ATOM   9413  C CB  . LEU E  1 110 ? -4.176  37.493 -5.717  1.00 46.58  ? 110 LEU E CB  1 
ATOM   9414  C CG  . LEU E  1 110 ? -3.383  37.957 -6.939  1.00 45.04  ? 110 LEU E CG  1 
ATOM   9415  C CD1 . LEU E  1 110 ? -2.113  38.684 -6.523  1.00 46.89  ? 110 LEU E CD1 1 
ATOM   9416  C CD2 . LEU E  1 110 ? -3.050  36.785 -7.850  1.00 41.23  ? 110 LEU E CD2 1 
ATOM   9417  N N   . LEU E  1 111 ? -6.798  36.846 -3.929  1.00 58.77  ? 111 LEU E N   1 
ATOM   9418  C CA  . LEU E  1 111 ? -7.452  36.298 -2.710  1.00 59.11  ? 111 LEU E CA  1 
ATOM   9419  C C   . LEU E  1 111 ? -8.525  35.284 -3.119  1.00 56.11  ? 111 LEU E C   1 
ATOM   9420  O O   . LEU E  1 111 ? -8.599  34.221 -2.474  1.00 59.18  ? 111 LEU E O   1 
ATOM   9421  C CB  . LEU E  1 111 ? -8.052  37.447 -1.896  1.00 55.51  ? 111 LEU E CB  1 
ATOM   9422  C CG  . LEU E  1 111 ? -7.040  38.273 -1.105  1.00 57.05  ? 111 LEU E CG  1 
ATOM   9423  C CD1 . LEU E  1 111 ? -7.706  39.478 -0.456  1.00 60.86  ? 111 LEU E CD1 1 
ATOM   9424  C CD2 . LEU E  1 111 ? -6.349  37.410 -0.060  1.00 58.47  ? 111 LEU E CD2 1 
ATOM   9425  N N   . THR E  1 112 ? -9.323  35.605 -4.142  1.00 50.84  ? 112 THR E N   1 
ATOM   9426  C CA  . THR E  1 112 ? -10.353 34.695 -4.711  1.00 56.20  ? 112 THR E CA  1 
ATOM   9427  C C   . THR E  1 112 ? -9.664  33.407 -5.176  1.00 58.12  ? 112 THR E C   1 
ATOM   9428  O O   . THR E  1 112 ? -10.030 32.325 -4.676  1.00 55.44  ? 112 THR E O   1 
ATOM   9429  C CB  . THR E  1 112 ? -11.133 35.351 -5.859  1.00 57.39  ? 112 THR E CB  1 
ATOM   9430  O OG1 . THR E  1 112 ? -10.266 35.457 -6.988  1.00 64.65  ? 112 THR E OG1 1 
ATOM   9431  C CG2 . THR E  1 112 ? -11.682 36.716 -5.507  1.00 60.51  ? 112 THR E CG2 1 
ATOM   9432  N N   . ILE E  1 113 ? -8.696  33.534 -6.089  1.00 58.80  ? 113 ILE E N   1 
ATOM   9433  C CA  . ILE E  1 113 ? -7.914  32.405 -6.677  1.00 55.75  ? 113 ILE E CA  1 
ATOM   9434  C C   . ILE E  1 113 ? -7.398  31.511 -5.545  1.00 55.61  ? 113 ILE E C   1 
ATOM   9435  O O   . ILE E  1 113 ? -7.511  30.274 -5.668  1.00 54.74  ? 113 ILE E O   1 
ATOM   9436  C CB  . ILE E  1 113 ? -6.760  32.941 -7.547  1.00 53.29  ? 113 ILE E CB  1 
ATOM   9437  C CG1 . ILE E  1 113 ? -7.279  33.701 -8.771  1.00 53.66  ? 113 ILE E CG1 1 
ATOM   9438  C CG2 . ILE E  1 113 ? -5.817  31.815 -7.941  1.00 52.74  ? 113 ILE E CG2 1 
ATOM   9439  C CD1 . ILE E  1 113 ? -6.264  34.630 -9.394  1.00 51.85  ? 113 ILE E CD1 1 
ATOM   9440  N N   . GLU E  1 114 ? -6.850  32.125 -4.491  1.00 59.35  ? 114 GLU E N   1 
ATOM   9441  C CA  . GLU E  1 114 ? -6.235  31.430 -3.329  1.00 66.92  ? 114 GLU E CA  1 
ATOM   9442  C C   . GLU E  1 114 ? -7.286  30.540 -2.656  1.00 64.04  ? 114 GLU E C   1 
ATOM   9443  O O   . GLU E  1 114 ? -6.951  29.391 -2.309  1.00 58.33  ? 114 GLU E O   1 
ATOM   9444  C CB  . GLU E  1 114 ? -5.658  32.446 -2.341  1.00 77.90  ? 114 GLU E CB  1 
ATOM   9445  C CG  . GLU E  1 114 ? -4.937  31.807 -1.165  1.00 88.35  ? 114 GLU E CG  1 
ATOM   9446  C CD  . GLU E  1 114 ? -4.265  32.791 -0.223  1.00 108.35 ? 114 GLU E CD  1 
ATOM   9447  O OE1 . GLU E  1 114 ? -3.904  32.375 0.897   1.00 112.20 ? 114 GLU E OE1 1 
ATOM   9448  O OE2 . GLU E  1 114 ? -4.108  33.969 -0.609  1.00 131.42 ? 114 GLU E OE2 1 
ATOM   9449  N N   . LEU E  1 115 ? -8.506  31.058 -2.479  1.00 60.57  ? 115 LEU E N   1 
ATOM   9450  C CA  . LEU E  1 115 ? -9.628  30.337 -1.822  1.00 58.07  ? 115 LEU E CA  1 
ATOM   9451  C C   . LEU E  1 115 ? -10.109 29.199 -2.729  1.00 58.63  ? 115 LEU E C   1 
ATOM   9452  O O   . LEU E  1 115 ? -10.313 28.086 -2.215  1.00 66.45  ? 115 LEU E O   1 
ATOM   9453  C CB  . LEU E  1 115 ? -10.764 31.320 -1.527  1.00 56.73  ? 115 LEU E CB  1 
ATOM   9454  C CG  . LEU E  1 115 ? -11.932 30.738 -0.733  1.00 55.84  ? 115 LEU E CG  1 
ATOM   9455  C CD1 . LEU E  1 115 ? -11.442 30.084 0.549   1.00 52.74  ? 115 LEU E CD1 1 
ATOM   9456  C CD2 . LEU E  1 115 ? -12.965 31.809 -0.418  1.00 57.51  ? 115 LEU E CD2 1 
ATOM   9457  N N   . LEU E  1 116 ? -10.281 29.476 -4.024  1.00 57.24  ? 116 LEU E N   1 
ATOM   9458  C CA  . LEU E  1 116 ? -10.768 28.497 -5.035  1.00 58.25  ? 116 LEU E CA  1 
ATOM   9459  C C   . LEU E  1 116 ? -9.747  27.365 -5.192  1.00 56.86  ? 116 LEU E C   1 
ATOM   9460  O O   . LEU E  1 116 ? -10.159 26.242 -5.537  1.00 56.27  ? 116 LEU E O   1 
ATOM   9461  C CB  . LEU E  1 116 ? -11.001 29.219 -6.366  1.00 62.28  ? 116 LEU E CB  1 
ATOM   9462  C CG  . LEU E  1 116 ? -12.148 30.228 -6.372  1.00 65.24  ? 116 LEU E CG  1 
ATOM   9463  C CD1 . LEU E  1 116 ? -12.335 30.827 -7.759  1.00 67.58  ? 116 LEU E CD1 1 
ATOM   9464  C CD2 . LEU E  1 116 ? -13.440 29.586 -5.889  1.00 65.03  ? 116 LEU E CD2 1 
ATOM   9465  N N   . ALA E  1 117 ? -8.467  27.653 -4.947  1.00 65.46  ? 117 ALA E N   1 
ATOM   9466  C CA  . ALA E  1 117 ? -7.343  26.696 -5.085  1.00 65.02  ? 117 ALA E CA  1 
ATOM   9467  C C   . ALA E  1 117 ? -7.454  25.602 -4.015  1.00 58.26  ? 117 ALA E C   1 
ATOM   9468  O O   . ALA E  1 117 ? -7.138  24.440 -4.331  1.00 50.33  ? 117 ALA E O   1 
ATOM   9469  C CB  . ALA E  1 117 ? -6.027  27.430 -4.995  1.00 65.80  ? 117 ALA E CB  1 
ATOM   9470  N N   . VAL E  1 118 ? -7.888  25.961 -2.801  1.00 58.62  ? 118 VAL E N   1 
ATOM   9471  C CA  . VAL E  1 118 ? -8.019  25.025 -1.643  1.00 66.02  ? 118 VAL E CA  1 
ATOM   9472  C C   . VAL E  1 118 ? -9.411  24.382 -1.678  1.00 75.64  ? 118 VAL E C   1 
ATOM   9473  O O   . VAL E  1 118 ? -9.648  23.444 -0.889  1.00 75.70  ? 118 VAL E O   1 
ATOM   9474  C CB  . VAL E  1 118 ? -7.763  25.731 -0.297  1.00 66.81  ? 118 VAL E CB  1 
ATOM   9475  C CG1 . VAL E  1 118 ? -6.291  26.060 -0.104  1.00 70.60  ? 118 VAL E CG1 1 
ATOM   9476  C CG2 . VAL E  1 118 ? -8.619  26.977 -0.136  1.00 72.22  ? 118 VAL E CG2 1 
ATOM   9477  N N   . CYS E  1 119 ? -10.294 24.878 -2.551  1.00 89.58  ? 119 CYS E N   1 
ATOM   9478  C CA  . CYS E  1 119 ? -11.629 24.287 -2.839  1.00 88.09  ? 119 CYS E CA  1 
ATOM   9479  C C   . CYS E  1 119 ? -11.450 23.051 -3.727  1.00 87.89  ? 119 CYS E C   1 
ATOM   9480  O O   . CYS E  1 119 ? -10.376 22.915 -4.351  1.00 67.50  ? 119 CYS E O   1 
ATOM   9481  C CB  . CYS E  1 119 ? -12.557 25.296 -3.506  1.00 88.92  ? 119 CYS E CB  1 
ATOM   9482  S SG  . CYS E  1 119 ? -13.264 26.502 -2.352  1.00 98.55  ? 119 CYS E SG  1 
ATOM   9483  N N   . ALA E  1 120 ? -12.471 22.192 -3.783  1.00 95.48  ? 120 ALA E N   1 
ATOM   9484  C CA  . ALA E  1 120 ? -12.437 20.869 -4.448  1.00 94.22  ? 120 ALA E CA  1 
ATOM   9485  C C   . ALA E  1 120 ? -12.943 20.977 -5.893  1.00 92.45  ? 120 ALA E C   1 
ATOM   9486  O O   . ALA E  1 120 ? -13.037 19.927 -6.554  1.00 98.07  ? 120 ALA E O   1 
ATOM   9487  C CB  . ALA E  1 120 ? -13.256 19.885 -3.651  1.00 93.17  ? 120 ALA E CB  1 
ATOM   9488  N N   . THR E  1 121 ? -13.257 22.192 -6.356  1.00 98.11  ? 121 THR E N   1 
ATOM   9489  C CA  . THR E  1 121 ? -13.720 22.487 -7.740  1.00 107.76 ? 121 THR E CA  1 
ATOM   9490  C C   . THR E  1 121 ? -12.825 21.740 -8.740  1.00 112.73 ? 121 THR E C   1 
ATOM   9491  O O   . THR E  1 121 ? -11.591 21.776 -8.555  1.00 110.90 ? 121 THR E O   1 
ATOM   9492  C CB  . THR E  1 121 ? -13.736 23.999 -8.003  1.00 115.95 ? 121 THR E CB  1 
ATOM   9493  O OG1 . THR E  1 121 ? -12.428 24.511 -7.753  1.00 126.63 ? 121 THR E OG1 1 
ATOM   9494  C CG2 . THR E  1 121 ? -14.732 24.748 -7.145  1.00 125.42 ? 121 THR E CG2 1 
ATOM   9495  N N   . LEU E  1 122 ? -13.419 21.093 -9.751  1.00 125.89 ? 122 LEU E N   1 
ATOM   9496  C CA  . LEU E  1 122 ? -12.700 20.248 -10.746 1.00 119.72 ? 122 LEU E CA  1 
ATOM   9497  C C   . LEU E  1 122 ? -13.093 20.650 -12.172 1.00 112.38 ? 122 LEU E C   1 
ATOM   9498  O O   . LEU E  1 122 ? -14.287 20.928 -12.398 1.00 112.21 ? 122 LEU E O   1 
ATOM   9499  C CB  . LEU E  1 122 ? -13.040 18.773 -10.500 1.00 116.04 ? 122 LEU E CB  1 
ATOM   9500  C CG  . LEU E  1 122 ? -12.876 18.281 -9.063  1.00 119.84 ? 122 LEU E CG  1 
ATOM   9501  C CD1 . LEU E  1 122 ? -13.349 16.842 -8.928  1.00 101.29 ? 122 LEU E CD1 1 
ATOM   9502  C CD2 . LEU E  1 122 ? -11.433 18.409 -8.597  1.00 129.57 ? 122 LEU E CD2 1 
ATOM   9503  N N   . GLY E  1 123 ? -12.116 20.661 -13.087 1.00 106.40 ? 123 GLY E N   1 
ATOM   9504  C CA  . GLY E  1 123 ? -12.318 20.801 -14.543 1.00 110.20 ? 123 GLY E CA  1 
ATOM   9505  C C   . GLY E  1 123 ? -12.792 22.189 -14.938 1.00 110.70 ? 123 GLY E C   1 
ATOM   9506  O O   . GLY E  1 123 ? -12.079 23.162 -14.631 1.00 113.92 ? 123 GLY E O   1 
ATOM   9507  N N   . VAL E  1 124 ? -13.952 22.268 -15.599 1.00 106.69 ? 124 VAL E N   1 
ATOM   9508  C CA  . VAL E  1 124 ? -14.553 23.521 -16.149 1.00 112.79 ? 124 VAL E CA  1 
ATOM   9509  C C   . VAL E  1 124 ? -15.174 24.331 -15.004 1.00 115.20 ? 124 VAL E C   1 
ATOM   9510  O O   . VAL E  1 124 ? -14.990 25.569 -14.989 1.00 135.71 ? 124 VAL E O   1 
ATOM   9511  C CB  . VAL E  1 124 ? -15.598 23.198 -17.234 1.00 116.68 ? 124 VAL E CB  1 
ATOM   9512  C CG1 . VAL E  1 124 ? -16.384 24.431 -17.657 1.00 120.03 ? 124 VAL E CG1 1 
ATOM   9513  C CG2 . VAL E  1 124 ? -14.961 22.522 -18.438 1.00 114.11 ? 124 VAL E CG2 1 
ATOM   9514  N N   . GLN E  1 125 ? -15.892 23.656 -14.099 1.00 101.40 ? 125 GLN E N   1 
ATOM   9515  C CA  . GLN E  1 125 ? -16.578 24.279 -12.935 1.00 89.58  ? 125 GLN E CA  1 
ATOM   9516  C C   . GLN E  1 125 ? -15.568 25.144 -12.173 1.00 99.50  ? 125 GLN E C   1 
ATOM   9517  O O   . GLN E  1 125 ? -15.964 26.225 -11.698 1.00 91.99  ? 125 GLN E O   1 
ATOM   9518  C CB  . GLN E  1 125 ? -17.184 23.206 -12.028 1.00 75.01  ? 125 GLN E CB  1 
ATOM   9519  N N   . ALA E  1 126 ? -14.317 24.680 -12.076 1.00 109.11 ? 126 ALA E N   1 
ATOM   9520  C CA  . ALA E  1 126 ? -13.194 25.356 -11.382 1.00 99.51  ? 126 ALA E CA  1 
ATOM   9521  C C   . ALA E  1 126 ? -12.743 26.580 -12.185 1.00 94.49  ? 126 ALA E C   1 
ATOM   9522  O O   . ALA E  1 126 ? -12.760 27.698 -11.627 1.00 107.21 ? 126 ALA E O   1 
ATOM   9523  C CB  . ALA E  1 126 ? -12.053 24.388 -11.188 1.00 91.81  ? 126 ALA E CB  1 
ATOM   9524  N N   . ARG E  1 127 ? -12.348 26.364 -13.445 1.00 84.32  ? 127 ARG E N   1 
ATOM   9525  C CA  . ARG E  1 127 ? -11.799 27.409 -14.350 1.00 80.73  ? 127 ARG E CA  1 
ATOM   9526  C C   . ARG E  1 127 ? -12.845 28.512 -14.555 1.00 85.67  ? 127 ARG E C   1 
ATOM   9527  O O   . ARG E  1 127 ? -12.447 29.697 -14.607 1.00 73.54  ? 127 ARG E O   1 
ATOM   9528  C CB  . ARG E  1 127 ? -11.377 26.792 -15.687 1.00 71.86  ? 127 ARG E CB  1 
ATOM   9529  N N   . ARG E  1 128 ? -14.126 28.138 -14.662 1.00 95.73  ? 128 ARG E N   1 
ATOM   9530  C CA  . ARG E  1 128 ? -15.259 29.084 -14.853 1.00 95.29  ? 128 ARG E CA  1 
ATOM   9531  C C   . ARG E  1 128 ? -15.381 29.981 -13.615 1.00 93.94  ? 128 ARG E C   1 
ATOM   9532  O O   . ARG E  1 128 ? -15.419 31.217 -13.784 1.00 98.49  ? 128 ARG E O   1 
ATOM   9533  C CB  . ARG E  1 128 ? -16.564 28.324 -15.112 1.00 89.03  ? 128 ARG E CB  1 
ATOM   9534  N N   . ASN E  1 129 ? -15.430 29.375 -12.424 1.00 85.95  ? 129 ASN E N   1 
ATOM   9535  C CA  . ASN E  1 129 ? -15.562 30.081 -11.121 1.00 85.77  ? 129 ASN E CA  1 
ATOM   9536  C C   . ASN E  1 129 ? -14.475 31.155 -11.016 1.00 77.18  ? 129 ASN E C   1 
ATOM   9537  O O   . ASN E  1 129 ? -14.829 32.330 -10.798 1.00 77.86  ? 129 ASN E O   1 
ATOM   9538  C CB  . ASN E  1 129 ? -15.485 29.113 -9.938  1.00 94.64  ? 129 ASN E CB  1 
ATOM   9539  C CG  . ASN E  1 129 ? -16.704 28.224 -9.828  1.00 102.30 ? 129 ASN E CG  1 
ATOM   9540  O OD1 . ASN E  1 129 ? -17.633 28.338 -10.624 1.00 111.97 ? 129 ASN E OD1 1 
ATOM   9541  N ND2 . ASN E  1 129 ? -16.708 27.336 -8.847  1.00 104.48 ? 129 ASN E ND2 1 
ATOM   9542  N N   . THR E  1 130 ? -13.208 30.757 -11.164 1.00 73.53  ? 130 THR E N   1 
ATOM   9543  C CA  . THR E  1 130 ? -12.023 31.652 -11.091 1.00 78.22  ? 130 THR E CA  1 
ATOM   9544  C C   . THR E  1 130 ? -12.247 32.864 -12.004 1.00 83.12  ? 130 THR E C   1 
ATOM   9545  O O   . THR E  1 130 ? -12.147 34.006 -11.505 1.00 94.32  ? 130 THR E O   1 
ATOM   9546  C CB  . THR E  1 130 ? -10.738 30.899 -11.457 1.00 75.19  ? 130 THR E CB  1 
ATOM   9547  O OG1 . THR E  1 130 ? -10.730 29.665 -10.739 1.00 83.06  ? 130 THR E OG1 1 
ATOM   9548  C CG2 . THR E  1 130 ? -9.484  31.685 -11.139 1.00 76.69  ? 130 THR E CG2 1 
ATOM   9549  N N   . ALA E  1 131 ? -12.550 32.616 -13.283 1.00 79.56  ? 131 ALA E N   1 
ATOM   9550  C CA  . ALA E  1 131 ? -12.737 33.643 -14.336 1.00 69.04  ? 131 ALA E CA  1 
ATOM   9551  C C   . ALA E  1 131 ? -13.768 34.682 -13.877 1.00 65.26  ? 131 ALA E C   1 
ATOM   9552  O O   . ALA E  1 131 ? -13.514 35.891 -14.056 1.00 67.20  ? 131 ALA E O   1 
ATOM   9553  C CB  . ALA E  1 131 ? -13.158 32.985 -15.626 1.00 61.70  ? 131 ALA E CB  1 
ATOM   9554  N N   . ILE E  1 132 ? -14.886 34.219 -13.311 1.00 62.54  ? 132 ILE E N   1 
ATOM   9555  C CA  . ILE E  1 132 ? -16.013 35.076 -12.834 1.00 63.65  ? 132 ILE E CA  1 
ATOM   9556  C C   . ILE E  1 132 ? -15.553 35.849 -11.594 1.00 57.80  ? 132 ILE E C   1 
ATOM   9557  O O   . ILE E  1 132 ? -15.647 37.090 -11.605 1.00 59.14  ? 132 ILE E O   1 
ATOM   9558  C CB  . ILE E  1 132 ? -17.268 34.225 -12.554 1.00 70.82  ? 132 ILE E CB  1 
ATOM   9559  C CG1 . ILE E  1 132 ? -17.751 33.502 -13.814 1.00 70.52  ? 132 ILE E CG1 1 
ATOM   9560  C CG2 . ILE E  1 132 ? -18.369 35.073 -11.936 1.00 72.23  ? 132 ILE E CG2 1 
ATOM   9561  C CD1 . ILE E  1 132 ? -18.894 32.544 -13.575 1.00 71.52  ? 132 ILE E CD1 1 
ATOM   9562  N N   . ALA E  1 133 ? -15.070 35.135 -10.573 1.00 56.40  ? 133 ALA E N   1 
ATOM   9563  C CA  . ALA E  1 133 ? -14.596 35.699 -9.287  1.00 65.44  ? 133 ALA E CA  1 
ATOM   9564  C C   . ALA E  1 133 ? -13.570 36.808 -9.548  1.00 62.01  ? 133 ALA E C   1 
ATOM   9565  O O   . ALA E  1 133 ? -13.703 37.892 -8.947  1.00 64.94  ? 133 ALA E O   1 
ATOM   9566  C CB  . ALA E  1 133 ? -14.012 34.603 -8.430  1.00 71.23  ? 133 ALA E CB  1 
ATOM   9567  N N   . VAL E  1 134 ? -12.585 36.541 -10.411 1.00 58.11  ? 134 VAL E N   1 
ATOM   9568  C CA  . VAL E  1 134 ? -11.482 37.489 -10.749 1.00 58.56  ? 134 VAL E CA  1 
ATOM   9569  C C   . VAL E  1 134 ? -12.089 38.746 -11.384 1.00 54.94  ? 134 VAL E C   1 
ATOM   9570  O O   . VAL E  1 134 ? -11.917 39.837 -10.806 1.00 55.51  ? 134 VAL E O   1 
ATOM   9571  C CB  . VAL E  1 134 ? -10.431 36.837 -11.669 1.00 55.96  ? 134 VAL E CB  1 
ATOM   9572  C CG1 . VAL E  1 134 ? -9.502  37.871 -12.289 1.00 55.47  ? 134 VAL E CG1 1 
ATOM   9573  C CG2 . VAL E  1 134 ? -9.631  35.770 -10.937 1.00 55.21  ? 134 VAL E CG2 1 
ATOM   9574  N N   . THR E  1 135 ? -12.777 38.595 -12.520 1.00 58.95  ? 135 THR E N   1 
ATOM   9575  C CA  . THR E  1 135 ? -13.366 39.716 -13.302 1.00 59.55  ? 135 THR E CA  1 
ATOM   9576  C C   . THR E  1 135 ? -14.391 40.453 -12.432 1.00 54.63  ? 135 THR E C   1 
ATOM   9577  O O   . THR E  1 135 ? -14.450 41.694 -12.520 1.00 52.81  ? 135 THR E O   1 
ATOM   9578  C CB  . THR E  1 135 ? -13.982 39.224 -14.618 1.00 58.22  ? 135 THR E CB  1 
ATOM   9579  O OG1 . THR E  1 135 ? -14.958 38.231 -14.303 1.00 59.60  ? 135 THR E OG1 1 
ATOM   9580  C CG2 . THR E  1 135 ? -12.956 38.651 -15.570 1.00 60.95  ? 135 THR E CG2 1 
ATOM   9581  N N   . ALA E  1 136 ? -15.156 39.716 -11.621 1.00 51.68  ? 136 ALA E N   1 
ATOM   9582  C CA  . ALA E  1 136 ? -16.160 40.266 -10.681 1.00 56.74  ? 136 ALA E CA  1 
ATOM   9583  C C   . ALA E  1 136 ? -15.468 41.228 -9.711  1.00 58.68  ? 136 ALA E C   1 
ATOM   9584  O O   . ALA E  1 136 ? -15.832 42.423 -9.701  1.00 63.92  ? 136 ALA E O   1 
ATOM   9585  C CB  . ALA E  1 136 ? -16.859 39.148 -9.947  1.00 60.22  ? 136 ALA E CB  1 
ATOM   9586  N N   . THR E  1 137 ? -14.501 40.719 -8.938  1.00 58.00  ? 137 THR E N   1 
ATOM   9587  C CA  . THR E  1 137 ? -13.740 41.480 -7.910  1.00 54.60  ? 137 THR E CA  1 
ATOM   9588  C C   . THR E  1 137 ? -12.956 42.615 -8.581  1.00 53.82  ? 137 THR E C   1 
ATOM   9589  O O   . THR E  1 137 ? -12.922 43.719 -8.008  1.00 59.59  ? 137 THR E O   1 
ATOM   9590  C CB  . THR E  1 137 ? -12.827 40.555 -7.096  1.00 49.17  ? 137 THR E CB  1 
ATOM   9591  O OG1 . THR E  1 137 ? -12.073 39.745 -7.998  1.00 50.86  ? 137 THR E OG1 1 
ATOM   9592  C CG2 . THR E  1 137 ? -13.600 39.667 -6.146  1.00 48.53  ? 137 THR E CG2 1 
ATOM   9593  N N   . GLY E  1 138 ? -12.352 42.350 -9.743  1.00 52.65  ? 138 GLY E N   1 
ATOM   9594  C CA  . GLY E  1 138 ? -11.647 43.363 -10.552 1.00 53.91  ? 138 GLY E CA  1 
ATOM   9595  C C   . GLY E  1 138 ? -12.555 44.541 -10.859 1.00 63.22  ? 138 GLY E C   1 
ATOM   9596  O O   . GLY E  1 138 ? -12.179 45.685 -10.527 1.00 65.76  ? 138 GLY E O   1 
ATOM   9597  N N   . ALA E  1 139 ? -13.717 44.263 -11.459 1.00 66.42  ? 139 ALA E N   1 
ATOM   9598  C CA  . ALA E  1 139 ? -14.768 45.248 -11.806 1.00 63.14  ? 139 ALA E CA  1 
ATOM   9599  C C   . ALA E  1 139 ? -15.248 45.957 -10.535 1.00 61.33  ? 139 ALA E C   1 
ATOM   9600  O O   . ALA E  1 139 ? -15.338 47.201 -10.545 1.00 65.50  ? 139 ALA E O   1 
ATOM   9601  C CB  . ALA E  1 139 ? -15.906 44.549 -12.507 1.00 67.52  ? 139 ALA E CB  1 
ATOM   9602  N N   . MET E  1 140 ? -15.543 45.182 -9.486  1.00 56.56  ? 140 MET E N   1 
ATOM   9603  C CA  . MET E  1 140 ? -16.005 45.689 -8.167  1.00 60.99  ? 140 MET E CA  1 
ATOM   9604  C C   . MET E  1 140 ? -15.139 46.883 -7.749  1.00 61.93  ? 140 MET E C   1 
ATOM   9605  O O   . MET E  1 140 ? -15.709 47.950 -7.438  1.00 63.77  ? 140 MET E O   1 
ATOM   9606  C CB  . MET E  1 140 ? -15.907 44.598 -7.095  1.00 61.14  ? 140 MET E CB  1 
ATOM   9607  C CG  . MET E  1 140 ? -16.239 45.096 -5.702  1.00 62.30  ? 140 MET E CG  1 
ATOM   9608  S SD  . MET E  1 140 ? -16.204 43.779 -4.459  1.00 68.87  ? 140 MET E SD  1 
ATOM   9609  C CE  . MET E  1 140 ? -14.457 43.381 -4.446  1.00 72.85  ? 140 MET E CE  1 
ATOM   9610  N N   . ILE E  1 141 ? -13.816 46.697 -7.743  1.00 59.69  ? 141 ILE E N   1 
ATOM   9611  C CA  . ILE E  1 141 ? -12.816 47.721 -7.317  1.00 58.08  ? 141 ILE E CA  1 
ATOM   9612  C C   . ILE E  1 141 ? -12.835 48.877 -8.321  1.00 56.79  ? 141 ILE E C   1 
ATOM   9613  O O   . ILE E  1 141 ? -13.004 50.032 -7.884  1.00 57.45  ? 141 ILE E O   1 
ATOM   9614  C CB  . ILE E  1 141 ? -11.411 47.098 -7.184  1.00 56.29  ? 141 ILE E CB  1 
ATOM   9615  C CG1 . ILE E  1 141 ? -11.405 45.937 -6.187  1.00 55.83  ? 141 ILE E CG1 1 
ATOM   9616  C CG2 . ILE E  1 141 ? -10.380 48.155 -6.817  1.00 56.59  ? 141 ILE E CG2 1 
ATOM   9617  C CD1 . ILE E  1 141 ? -11.864 46.322 -4.799  1.00 50.93  ? 141 ILE E CD1 1 
ATOM   9618  N N   . PHE E  1 142 ? -12.672 48.572 -9.613  1.00 55.97  ? 142 PHE E N   1 
ATOM   9619  C CA  . PHE E  1 142 ? -12.561 49.575 -10.703 1.00 58.86  ? 142 PHE E CA  1 
ATOM   9620  C C   . PHE E  1 142 ? -13.759 50.529 -10.656 1.00 58.37  ? 142 PHE E C   1 
ATOM   9621  O O   . PHE E  1 142 ? -13.585 51.725 -10.958 1.00 54.70  ? 142 PHE E O   1 
ATOM   9622  C CB  . PHE E  1 142 ? -12.474 48.909 -12.077 1.00 59.53  ? 142 PHE E CB  1 
ATOM   9623  C CG  . PHE E  1 142 ? -12.289 49.895 -13.203 1.00 59.59  ? 142 PHE E CG  1 
ATOM   9624  C CD1 . PHE E  1 142 ? -13.300 50.133 -14.120 1.00 60.98  ? 142 PHE E CD1 1 
ATOM   9625  C CD2 . PHE E  1 142 ? -11.110 50.612 -13.321 1.00 59.80  ? 142 PHE E CD2 1 
ATOM   9626  C CE1 . PHE E  1 142 ? -13.125 51.051 -15.143 1.00 66.17  ? 142 PHE E CE1 1 
ATOM   9627  C CE2 . PHE E  1 142 ? -10.935 51.528 -14.346 1.00 61.52  ? 142 PHE E CE2 1 
ATOM   9628  C CZ  . PHE E  1 142 ? -11.942 51.746 -15.255 1.00 67.55  ? 142 PHE E CZ  1 
ATOM   9629  N N   . CYS E  1 143 ? -14.937 50.008 -10.300 1.00 62.76  ? 143 CYS E N   1 
ATOM   9630  C CA  . CYS E  1 143 ? -16.196 50.787 -10.152 1.00 72.53  ? 143 CYS E CA  1 
ATOM   9631  C C   . CYS E  1 143 ? -16.036 51.808 -9.020  1.00 67.11  ? 143 CYS E C   1 
ATOM   9632  O O   . CYS E  1 143 ? -16.183 53.020 -9.289  1.00 61.31  ? 143 CYS E O   1 
ATOM   9633  C CB  . CYS E  1 143 ? -17.386 49.874 -9.882  1.00 80.56  ? 143 CYS E CB  1 
ATOM   9634  S SG  . CYS E  1 143 ? -17.970 48.997 -11.356 1.00 84.94  ? 143 CYS E SG  1 
ATOM   9635  N N   . GLY E  1 144 ? -15.743 51.331 -7.807  1.00 61.55  ? 144 GLY E N   1 
ATOM   9636  C CA  . GLY E  1 144 ? -15.467 52.178 -6.631  1.00 67.15  ? 144 GLY E CA  1 
ATOM   9637  C C   . GLY E  1 144 ? -14.461 53.271 -6.956  1.00 67.87  ? 144 GLY E C   1 
ATOM   9638  O O   . GLY E  1 144 ? -14.625 54.394 -6.438  1.00 68.88  ? 144 GLY E O   1 
ATOM   9639  N N   . PHE E  1 145 ? -13.461 52.954 -7.786  1.00 61.92  ? 145 PHE E N   1 
ATOM   9640  C CA  . PHE E  1 145 ? -12.388 53.884 -8.230  1.00 56.59  ? 145 PHE E CA  1 
ATOM   9641  C C   . PHE E  1 145 ? -13.010 55.029 -9.039  1.00 58.80  ? 145 PHE E C   1 
ATOM   9642  O O   . PHE E  1 145 ? -12.692 56.201 -8.763  1.00 60.75  ? 145 PHE E O   1 
ATOM   9643  C CB  . PHE E  1 145 ? -11.325 53.139 -9.043  1.00 57.99  ? 145 PHE E CB  1 
ATOM   9644  C CG  . PHE E  1 145 ? -10.184 54.001 -9.526  1.00 62.30  ? 145 PHE E CG  1 
ATOM   9645  C CD1 . PHE E  1 145 ? -9.906  54.124 -10.878 1.00 61.56  ? 145 PHE E CD1 1 
ATOM   9646  C CD2 . PHE E  1 145 ? -9.388  54.695 -8.627  1.00 65.12  ? 145 PHE E CD2 1 
ATOM   9647  C CE1 . PHE E  1 145 ? -8.858  54.918 -11.319 1.00 60.44  ? 145 PHE E CE1 1 
ATOM   9648  C CE2 . PHE E  1 145 ? -8.340  55.489 -9.070  1.00 58.10  ? 145 PHE E CE2 1 
ATOM   9649  C CZ  . PHE E  1 145 ? -8.078  55.600 -10.414 1.00 58.69  ? 145 PHE E CZ  1 
ATOM   9650  N N   . LEU E  1 146 ? -13.869 54.693 -10.007 1.00 67.90  ? 146 LEU E N   1 
ATOM   9651  C CA  . LEU E  1 146 ? -14.578 55.672 -10.876 1.00 64.70  ? 146 LEU E CA  1 
ATOM   9652  C C   . LEU E  1 146 ? -15.386 56.638 -10.003 1.00 62.72  ? 146 LEU E C   1 
ATOM   9653  O O   . LEU E  1 146 ? -15.277 57.863 -10.215 1.00 60.66  ? 146 LEU E O   1 
ATOM   9654  C CB  . LEU E  1 146 ? -15.491 54.915 -11.846 1.00 60.75  ? 146 LEU E CB  1 
ATOM   9655  C CG  . LEU E  1 146 ? -14.778 54.211 -12.999 1.00 59.17  ? 146 LEU E CG  1 
ATOM   9656  C CD1 . LEU E  1 146 ? -15.773 53.483 -13.890 1.00 56.62  ? 146 LEU E CD1 1 
ATOM   9657  C CD2 . LEU E  1 146 ? -13.957 55.202 -13.810 1.00 54.84  ? 146 LEU E CD2 1 
ATOM   9658  N N   . GLY E  1 147 ? -16.162 56.096 -9.060  1.00 60.95  ? 147 GLY E N   1 
ATOM   9659  C CA  . GLY E  1 147 ? -17.058 56.868 -8.180  1.00 68.95  ? 147 GLY E CA  1 
ATOM   9660  C C   . GLY E  1 147 ? -16.296 57.831 -7.285  1.00 68.45  ? 147 GLY E C   1 
ATOM   9661  O O   . GLY E  1 147 ? -16.626 59.034 -7.299  1.00 77.14  ? 147 GLY E O   1 
ATOM   9662  N N   . ALA E  1 148 ? -15.306 57.325 -6.542  1.00 60.66  ? 148 ALA E N   1 
ATOM   9663  C CA  . ALA E  1 148 ? -14.649 58.018 -5.409  1.00 53.44  ? 148 ALA E CA  1 
ATOM   9664  C C   . ALA E  1 148 ? -13.511 58.924 -5.896  1.00 51.71  ? 148 ALA E C   1 
ATOM   9665  O O   . ALA E  1 148 ? -13.192 59.885 -5.174  1.00 55.49  ? 148 ALA E O   1 
ATOM   9666  C CB  . ALA E  1 148 ? -14.140 57.001 -4.417  1.00 50.69  ? 148 ALA E CB  1 
ATOM   9667  N N   . ILE E  1 149 ? -12.924 58.636 -7.062  1.00 53.80  ? 149 ILE E N   1 
ATOM   9668  C CA  . ILE E  1 149 ? -11.641 59.257 -7.516  1.00 62.81  ? 149 ILE E CA  1 
ATOM   9669  C C   . ILE E  1 149 ? -11.810 59.891 -8.903  1.00 69.89  ? 149 ILE E C   1 
ATOM   9670  O O   . ILE E  1 149 ? -11.672 61.125 -9.006  1.00 84.52  ? 149 ILE E O   1 
ATOM   9671  C CB  . ILE E  1 149 ? -10.503 58.216 -7.512  1.00 60.54  ? 149 ILE E CB  1 
ATOM   9672  C CG1 . ILE E  1 149 ? -10.257 57.633 -6.116  1.00 56.03  ? 149 ILE E CG1 1 
ATOM   9673  C CG2 . ILE E  1 149 ? -9.235  58.810 -8.106  1.00 61.14  ? 149 ILE E CG2 1 
ATOM   9674  C CD1 . ILE E  1 149 ? -9.529  58.565 -5.176  1.00 55.63  ? 149 ILE E CD1 1 
ATOM   9675  N N   . VAL E  1 150 ? -12.076 59.074 -9.926  1.00 74.78  ? 150 VAL E N   1 
ATOM   9676  C CA  . VAL E  1 150 ? -11.936 59.447 -11.367 1.00 80.43  ? 150 VAL E CA  1 
ATOM   9677  C C   . VAL E  1 150 ? -12.964 60.524 -11.739 1.00 80.48  ? 150 VAL E C   1 
ATOM   9678  O O   . VAL E  1 150 ? -12.541 61.592 -12.226 1.00 86.46  ? 150 VAL E O   1 
ATOM   9679  C CB  . VAL E  1 150 ? -12.068 58.215 -12.281 1.00 84.94  ? 150 VAL E CB  1 
ATOM   9680  C CG1 . VAL E  1 150 ? -11.939 58.593 -13.749 1.00 81.07  ? 150 VAL E CG1 1 
ATOM   9681  C CG2 . VAL E  1 150 ? -11.064 57.131 -11.918 1.00 85.48  ? 150 VAL E CG2 1 
ATOM   9682  N N   . ILE E  1 151 ? -14.255 60.247 -11.530 1.00 73.78  ? 151 ILE E N   1 
ATOM   9683  C CA  . ILE E  1 151 ? -15.393 61.091 -12.009 1.00 76.79  ? 151 ILE E CA  1 
ATOM   9684  C C   . ILE E  1 151 ? -15.459 62.389 -11.193 1.00 72.85  ? 151 ILE E C   1 
ATOM   9685  O O   . ILE E  1 151 ? -15.717 62.314 -9.977  1.00 67.13  ? 151 ILE E O   1 
ATOM   9686  C CB  . ILE E  1 151 ? -16.720 60.308 -11.941 1.00 80.59  ? 151 ILE E CB  1 
ATOM   9687  C CG1 . ILE E  1 151 ? -16.718 59.118 -12.903 1.00 82.41  ? 151 ILE E CG1 1 
ATOM   9688  C CG2 . ILE E  1 151 ? -17.905 61.230 -12.186 1.00 79.02  ? 151 ILE E CG2 1 
ATOM   9689  C CD1 . ILE E  1 151 ? -17.931 58.224 -12.779 1.00 84.48  ? 151 ILE E CD1 1 
ATOM   9690  N N   . ASP E  1 152 ? -15.246 63.531 -11.856 1.00 75.82  ? 152 ASP E N   1 
ATOM   9691  C CA  . ASP E  1 152 ? -15.354 64.894 -11.268 1.00 79.59  ? 152 ASP E CA  1 
ATOM   9692  C C   . ASP E  1 152 ? -14.551 64.949 -9.964  1.00 76.81  ? 152 ASP E C   1 
ATOM   9693  O O   . ASP E  1 152 ? -15.070 65.507 -8.979  1.00 82.82  ? 152 ASP E O   1 
ATOM   9694  C CB  . ASP E  1 152 ? -16.820 65.279 -11.050 1.00 84.34  ? 152 ASP E CB  1 
ATOM   9695  C CG  . ASP E  1 152 ? -17.632 65.318 -12.333 1.00 86.80  ? 152 ASP E CG  1 
ATOM   9696  O OD1 . ASP E  1 152 ? -17.086 65.781 -13.354 1.00 84.55  ? 152 ASP E OD1 1 
ATOM   9697  O OD2 . ASP E  1 152 ? -18.801 64.883 -12.304 1.00 76.56  ? 152 ASP E OD2 1 
ATOM   9698  N N   . ASN E  1 153 ? -13.338 64.386 -9.970  1.00 69.42  ? 153 ASN E N   1 
ATOM   9699  C CA  . ASN E  1 153 ? -12.378 64.412 -8.833  1.00 65.69  ? 153 ASN E CA  1 
ATOM   9700  C C   . ASN E  1 153 ? -13.063 63.887 -7.566  1.00 60.79  ? 153 ASN E C   1 
ATOM   9701  O O   . ASN E  1 153 ? -12.638 64.278 -6.463  1.00 48.59  ? 153 ASN E O   1 
ATOM   9702  C CB  . ASN E  1 153 ? -11.809 65.815 -8.620  1.00 69.10  ? 153 ASN E CB  1 
ATOM   9703  C CG  . ASN E  1 153 ? -11.283 66.425 -9.901  1.00 75.63  ? 153 ASN E CG  1 
ATOM   9704  O OD1 . ASN E  1 153 ? -10.920 65.708 -10.830 1.00 82.25  ? 153 ASN E OD1 1 
ATOM   9705  N ND2 . ASN E  1 153 ? -11.245 67.746 -9.962  1.00 81.62  ? 153 ASN E ND2 1 
ATOM   9706  N N   . GLY E  1 154 ? -14.080 63.035 -7.732  1.00 64.13  ? 154 GLY E N   1 
ATOM   9707  C CA  . GLY E  1 154 ? -14.778 62.334 -6.637  1.00 68.73  ? 154 GLY E CA  1 
ATOM   9708  C C   . GLY E  1 154 ? -15.611 63.275 -5.784  1.00 76.12  ? 154 GLY E C   1 
ATOM   9709  O O   . GLY E  1 154 ? -15.774 62.980 -4.586  1.00 81.39  ? 154 GLY E O   1 
ATOM   9710  N N   . THR E  1 155 ? -16.123 64.362 -6.372  1.00 81.06  ? 155 THR E N   1 
ATOM   9711  C CA  . THR E  1 155 ? -16.949 65.391 -5.681  1.00 77.97  ? 155 THR E CA  1 
ATOM   9712  C C   . THR E  1 155 ? -18.427 65.185 -6.036  1.00 76.96  ? 155 THR E C   1 
ATOM   9713  O O   . THR E  1 155 ? -19.287 65.539 -5.204  1.00 83.81  ? 155 THR E O   1 
ATOM   9714  C CB  . THR E  1 155 ? -16.475 66.809 -6.026  1.00 69.98  ? 155 THR E CB  1 
ATOM   9715  O OG1 . THR E  1 155 ? -16.496 66.951 -7.446  1.00 64.50  ? 155 THR E OG1 1 
ATOM   9716  C CG2 . THR E  1 155 ? -15.088 67.111 -5.500  1.00 69.09  ? 155 THR E CG2 1 
ATOM   9717  N N   . ASN E  1 156 ? -18.703 64.627 -7.219  1.00 70.03  ? 156 ASN E N   1 
ATOM   9718  C CA  . ASN E  1 156 ? -20.075 64.352 -7.727  1.00 71.27  ? 156 ASN E CA  1 
ATOM   9719  C C   . ASN E  1 156 ? -20.727 63.263 -6.866  1.00 64.15  ? 156 ASN E C   1 
ATOM   9720  O O   . ASN E  1 156 ? -20.328 62.089 -6.999  1.00 64.64  ? 156 ASN E O   1 
ATOM   9721  C CB  . ASN E  1 156 ? -20.055 63.952 -9.204  1.00 75.71  ? 156 ASN E CB  1 
ATOM   9722  C CG  . ASN E  1 156 ? -21.426 63.604 -9.744  1.00 80.29  ? 156 ASN E CG  1 
ATOM   9723  O OD1 . ASN E  1 156 ? -22.305 63.180 -8.999  1.00 78.87  ? 156 ASN E OD1 1 
ATOM   9724  N ND2 . ASN E  1 156 ? -21.618 63.783 -11.041 1.00 84.17  ? 156 ASN E ND2 1 
ATOM   9725  N N   . THR E  1 157 ? -21.700 63.644 -6.030  1.00 64.38  ? 157 THR E N   1 
ATOM   9726  C CA  . THR E  1 157 ? -22.406 62.747 -5.073  1.00 68.15  ? 157 THR E CA  1 
ATOM   9727  C C   . THR E  1 157 ? -23.250 61.720 -5.837  1.00 66.40  ? 157 THR E C   1 
ATOM   9728  O O   . THR E  1 157 ? -23.445 60.609 -5.306  1.00 67.13  ? 157 THR E O   1 
ATOM   9729  C CB  . THR E  1 157 ? -23.278 63.545 -4.095  1.00 68.39  ? 157 THR E CB  1 
ATOM   9730  O OG1 . THR E  1 157 ? -22.507 64.643 -3.606  1.00 70.38  ? 157 THR E OG1 1 
ATOM   9731  C CG2 . THR E  1 157 ? -23.768 62.712 -2.931  1.00 64.93  ? 157 THR E CG2 1 
ATOM   9732  N N   . GLY E  1 158 ? -23.742 62.084 -7.025  1.00 69.51  ? 158 GLY E N   1 
ATOM   9733  C CA  . GLY E  1 158 ? -24.511 61.184 -7.907  1.00 76.04  ? 158 GLY E CA  1 
ATOM   9734  C C   . GLY E  1 158 ? -23.700 59.956 -8.285  1.00 79.81  ? 158 GLY E C   1 
ATOM   9735  O O   . GLY E  1 158 ? -24.084 58.843 -7.872  1.00 73.88  ? 158 GLY E O   1 
ATOM   9736  N N   . ALA E  1 159 ? -22.610 60.158 -9.034  1.00 76.46  ? 159 ALA E N   1 
ATOM   9737  C CA  . ALA E  1 159 ? -21.679 59.106 -9.506  1.00 71.23  ? 159 ALA E CA  1 
ATOM   9738  C C   . ALA E  1 159 ? -21.129 58.323 -8.308  1.00 67.04  ? 159 ALA E C   1 
ATOM   9739  O O   . ALA E  1 159 ? -21.097 57.076 -8.376  1.00 71.23  ? 159 ALA E O   1 
ATOM   9740  C CB  . ALA E  1 159 ? -20.569 59.737 -10.311 1.00 69.95  ? 159 ALA E CB  1 
ATOM   9741  N N   . PHE E  1 160 ? -20.711 59.037 -7.258  1.00 63.03  ? 160 PHE E N   1 
ATOM   9742  C CA  . PHE E  1 160 ? -20.157 58.474 -5.998  1.00 64.07  ? 160 PHE E CA  1 
ATOM   9743  C C   . PHE E  1 160 ? -21.057 57.334 -5.509  1.00 64.58  ? 160 PHE E C   1 
ATOM   9744  O O   . PHE E  1 160 ? -20.534 56.244 -5.207  1.00 73.28  ? 160 PHE E O   1 
ATOM   9745  C CB  . PHE E  1 160 ? -20.029 59.569 -4.935  1.00 67.10  ? 160 PHE E CB  1 
ATOM   9746  C CG  . PHE E  1 160 ? -19.310 59.152 -3.676  1.00 70.89  ? 160 PHE E CG  1 
ATOM   9747  C CD1 . PHE E  1 160 ? -20.016 58.731 -2.560  1.00 75.45  ? 160 PHE E CD1 1 
ATOM   9748  C CD2 . PHE E  1 160 ? -17.926 59.187 -3.604  1.00 75.77  ? 160 PHE E CD2 1 
ATOM   9749  C CE1 . PHE E  1 160 ? -19.354 58.353 -1.403  1.00 77.80  ? 160 PHE E CE1 1 
ATOM   9750  C CE2 . PHE E  1 160 ? -17.264 58.805 -2.447  1.00 74.65  ? 160 PHE E CE2 1 
ATOM   9751  C CZ  . PHE E  1 160 ? -17.979 58.391 -1.348  1.00 75.35  ? 160 PHE E CZ  1 
ATOM   9752  N N   . ILE E  1 161 ? -22.368 57.584 -5.440  1.00 64.32  ? 161 ILE E N   1 
ATOM   9753  C CA  . ILE E  1 161 ? -23.389 56.618 -4.931  1.00 71.76  ? 161 ILE E CA  1 
ATOM   9754  C C   . ILE E  1 161 ? -23.746 55.626 -6.044  1.00 66.04  ? 161 ILE E C   1 
ATOM   9755  O O   . ILE E  1 161 ? -23.826 54.416 -5.751  1.00 60.15  ? 161 ILE E O   1 
ATOM   9756  C CB  . ILE E  1 161 ? -24.632 57.359 -4.397  1.00 76.55  ? 161 ILE E CB  1 
ATOM   9757  C CG1 . ILE E  1 161 ? -24.286 58.225 -3.182  1.00 80.74  ? 161 ILE E CG1 1 
ATOM   9758  C CG2 . ILE E  1 161 ? -25.756 56.378 -4.093  1.00 75.00  ? 161 ILE E CG2 1 
ATOM   9759  C CD1 . ILE E  1 161 ? -25.487 58.700 -2.397  1.00 80.83  ? 161 ILE E CD1 1 
ATOM   9760  N N   . LEU E  1 162 ? -23.952 56.120 -7.268  1.00 58.31  ? 162 LEU E N   1 
ATOM   9761  C CA  . LEU E  1 162 ? -24.314 55.289 -8.448  1.00 67.51  ? 162 LEU E CA  1 
ATOM   9762  C C   . LEU E  1 162 ? -23.353 54.098 -8.537  1.00 70.82  ? 162 LEU E C   1 
ATOM   9763  O O   . LEU E  1 162 ? -23.814 52.947 -8.373  1.00 67.24  ? 162 LEU E O   1 
ATOM   9764  C CB  . LEU E  1 162 ? -24.239 56.146 -9.717  1.00 71.88  ? 162 LEU E CB  1 
ATOM   9765  C CG  . LEU E  1 162 ? -24.951 55.579 -10.947 1.00 65.64  ? 162 LEU E CG  1 
ATOM   9766  C CD1 . LEU E  1 162 ? -24.380 56.172 -12.227 1.00 62.23  ? 162 LEU E CD1 1 
ATOM   9767  C CD2 . LEU E  1 162 ? -24.865 54.061 -10.987 1.00 60.53  ? 162 LEU E CD2 1 
ATOM   9768  N N   . TRP E  1 163 ? -22.068 54.380 -8.774  1.00 71.95  ? 163 TRP E N   1 
ATOM   9769  C CA  . TRP E  1 163 ? -21.018 53.379 -9.103  1.00 74.34  ? 163 TRP E CA  1 
ATOM   9770  C C   . TRP E  1 163 ? -20.734 52.480 -7.895  1.00 76.30  ? 163 TRP E C   1 
ATOM   9771  O O   . TRP E  1 163 ? -20.362 51.309 -8.111  1.00 85.03  ? 163 TRP E O   1 
ATOM   9772  C CB  . TRP E  1 163 ? -19.754 54.082 -9.609  1.00 71.53  ? 163 TRP E CB  1 
ATOM   9773  C CG  . TRP E  1 163 ? -19.910 54.616 -10.998 1.00 73.06  ? 163 TRP E CG  1 
ATOM   9774  C CD1 . TRP E  1 163 ? -20.206 55.898 -11.362 1.00 77.54  ? 163 TRP E CD1 1 
ATOM   9775  C CD2 . TRP E  1 163 ? -19.803 53.866 -12.221 1.00 77.09  ? 163 TRP E CD2 1 
ATOM   9776  N NE1 . TRP E  1 163 ? -20.275 56.000 -12.726 1.00 83.30  ? 163 TRP E NE1 1 
ATOM   9777  C CE2 . TRP E  1 163 ? -20.034 54.770 -13.280 1.00 81.70  ? 163 TRP E CE2 1 
ATOM   9778  C CE3 . TRP E  1 163 ? -19.529 52.528 -12.524 1.00 76.31  ? 163 TRP E CE3 1 
ATOM   9779  C CZ2 . TRP E  1 163 ? -19.998 54.374 -14.616 1.00 80.30  ? 163 TRP E CZ2 1 
ATOM   9780  C CZ3 . TRP E  1 163 ? -19.495 52.137 -13.844 1.00 79.47  ? 163 TRP E CZ3 1 
ATOM   9781  C CH2 . TRP E  1 163 ? -19.726 53.050 -14.875 1.00 79.69  ? 163 TRP E CH2 1 
ATOM   9782  N N   . ALA E  1 164 ? -20.901 53.005 -6.678  1.00 71.66  ? 164 ALA E N   1 
ATOM   9783  C CA  . ALA E  1 164 ? -20.813 52.232 -5.418  1.00 74.36  ? 164 ALA E CA  1 
ATOM   9784  C C   . ALA E  1 164 ? -21.842 51.096 -5.461  1.00 86.74  ? 164 ALA E C   1 
ATOM   9785  O O   . ALA E  1 164 ? -21.533 49.993 -4.971  1.00 93.17  ? 164 ALA E O   1 
ATOM   9786  C CB  . ALA E  1 164 ? -21.033 53.139 -4.235  1.00 70.33  ? 164 ALA E CB  1 
ATOM   9787  N N   . VAL E  1 165 ? -23.018 51.362 -6.039  1.00 86.09  ? 165 VAL E N   1 
ATOM   9788  C CA  . VAL E  1 165 ? -24.134 50.380 -6.174  1.00 76.05  ? 165 VAL E CA  1 
ATOM   9789  C C   . VAL E  1 165 ? -23.767 49.371 -7.269  1.00 66.11  ? 165 VAL E C   1 
ATOM   9790  O O   . VAL E  1 165 ? -23.831 48.157 -6.995  1.00 69.75  ? 165 VAL E O   1 
ATOM   9791  C CB  . VAL E  1 165 ? -25.473 51.081 -6.469  1.00 74.19  ? 165 VAL E CB  1 
ATOM   9792  C CG1 . VAL E  1 165 ? -26.545 50.085 -6.880  1.00 77.42  ? 165 VAL E CG1 1 
ATOM   9793  C CG2 . VAL E  1 165 ? -25.940 51.913 -5.285  1.00 67.75  ? 165 VAL E CG2 1 
ATOM   9794  N N   . ILE E  1 166 ? -23.395 49.857 -8.457  1.00 62.34  ? 166 ILE E N   1 
ATOM   9795  C CA  . ILE E  1 166 ? -22.882 49.015 -9.580  1.00 65.24  ? 166 ILE E CA  1 
ATOM   9796  C C   . ILE E  1 166 ? -21.797 48.088 -9.021  1.00 68.67  ? 166 ILE E C   1 
ATOM   9797  O O   . ILE E  1 166 ? -21.821 46.883 -9.339  1.00 66.21  ? 166 ILE E O   1 
ATOM   9798  C CB  . ILE E  1 166 ? -22.341 49.881 -10.735 1.00 66.37  ? 166 ILE E CB  1 
ATOM   9799  C CG1 . ILE E  1 166 ? -23.417 50.808 -11.306 1.00 69.33  ? 166 ILE E CG1 1 
ATOM   9800  C CG2 . ILE E  1 166 ? -21.719 49.005 -11.814 1.00 61.80  ? 166 ILE E CG2 1 
ATOM   9801  C CD1 . ILE E  1 166 ? -22.958 51.617 -12.497 1.00 73.22  ? 166 ILE E CD1 1 
ATOM   9802  N N   . SER E  1 167 ? -20.882 48.646 -8.224  1.00 67.91  ? 167 SER E N   1 
ATOM   9803  C CA  . SER E  1 167 ? -19.809 47.908 -7.508  1.00 65.54  ? 167 SER E CA  1 
ATOM   9804  C C   . SER E  1 167 ? -20.429 46.769 -6.689  1.00 60.69  ? 167 SER E C   1 
ATOM   9805  O O   . SER E  1 167 ? -20.024 45.609 -6.899  1.00 56.09  ? 167 SER E O   1 
ATOM   9806  C CB  . SER E  1 167 ? -18.999 48.839 -6.643  1.00 68.23  ? 167 SER E CB  1 
ATOM   9807  O OG  . SER E  1 167 ? -18.038 48.125 -5.881  1.00 70.73  ? 167 SER E OG  1 
ATOM   9808  N N   . CYS E  1 168 ? -21.382 47.094 -5.807  1.00 59.65  ? 168 CYS E N   1 
ATOM   9809  C CA  . CYS E  1 168 ? -22.061 46.141 -4.885  1.00 63.98  ? 168 CYS E CA  1 
ATOM   9810  C C   . CYS E  1 168 ? -22.678 44.983 -5.677  1.00 66.15  ? 168 CYS E C   1 
ATOM   9811  O O   . CYS E  1 168 ? -22.693 43.854 -5.149  1.00 67.78  ? 168 CYS E O   1 
ATOM   9812  C CB  . CYS E  1 168 ? -23.141 46.828 -4.058  1.00 66.21  ? 168 CYS E CB  1 
ATOM   9813  S SG  . CYS E  1 168 ? -22.482 47.970 -2.817  1.00 78.06  ? 168 CYS E SG  1 
ATOM   9814  N N   . VAL E  1 169 ? -23.180 45.255 -6.885  1.00 68.38  ? 169 VAL E N   1 
ATOM   9815  C CA  . VAL E  1 169 ? -23.697 44.214 -7.822  1.00 78.58  ? 169 VAL E CA  1 
ATOM   9816  C C   . VAL E  1 169 ? -22.603 43.154 -7.996  1.00 81.39  ? 169 VAL E C   1 
ATOM   9817  O O   . VAL E  1 169 ? -22.841 41.988 -7.624  1.00 78.37  ? 169 VAL E O   1 
ATOM   9818  C CB  . VAL E  1 169 ? -24.117 44.822 -9.174  1.00 77.93  ? 169 VAL E CB  1 
ATOM   9819  C CG1 . VAL E  1 169 ? -24.290 43.756 -10.246 1.00 76.33  ? 169 VAL E CG1 1 
ATOM   9820  C CG2 . VAL E  1 169 ? -25.376 45.665 -9.044  1.00 76.71  ? 169 VAL E CG2 1 
ATOM   9821  N N   . PHE E  1 170 ? -21.446 43.562 -8.524  1.00 77.17  ? 170 PHE E N   1 
ATOM   9822  C CA  . PHE E  1 170 ? -20.254 42.701 -8.741  1.00 75.27  ? 170 PHE E CA  1 
ATOM   9823  C C   . PHE E  1 170 ? -19.865 42.025 -7.421  1.00 70.85  ? 170 PHE E C   1 
ATOM   9824  O O   . PHE E  1 170 ? -19.542 40.821 -7.436  1.00 69.02  ? 170 PHE E O   1 
ATOM   9825  C CB  . PHE E  1 170 ? -19.097 43.520 -9.319  1.00 77.96  ? 170 PHE E CB  1 
ATOM   9826  C CG  . PHE E  1 170 ? -19.299 43.973 -10.744 1.00 81.33  ? 170 PHE E CG  1 
ATOM   9827  C CD1 . PHE E  1 170 ? -19.315 43.056 -11.784 1.00 75.34  ? 170 PHE E CD1 1 
ATOM   9828  C CD2 . PHE E  1 170 ? -19.464 45.315 -11.046 1.00 85.18  ? 170 PHE E CD2 1 
ATOM   9829  C CE1 . PHE E  1 170 ? -19.497 43.473 -13.094 1.00 72.32  ? 170 PHE E CE1 1 
ATOM   9830  C CE2 . PHE E  1 170 ? -19.644 45.731 -12.357 1.00 82.92  ? 170 PHE E CE2 1 
ATOM   9831  C CZ  . PHE E  1 170 ? -19.661 44.809 -13.378 1.00 74.77  ? 170 PHE E CZ  1 
ATOM   9832  N N   . TRP E  1 171 ? -19.903 42.776 -6.316  1.00 66.03  ? 171 TRP E N   1 
ATOM   9833  C CA  . TRP E  1 171 ? -19.574 42.280 -4.952  1.00 71.93  ? 171 TRP E CA  1 
ATOM   9834  C C   . TRP E  1 171 ? -20.375 41.006 -4.666  1.00 76.10  ? 171 TRP E C   1 
ATOM   9835  O O   . TRP E  1 171 ? -19.760 39.983 -4.294  1.00 72.37  ? 171 TRP E O   1 
ATOM   9836  C CB  . TRP E  1 171 ? -19.840 43.363 -3.896  1.00 72.43  ? 171 TRP E CB  1 
ATOM   9837  C CG  . TRP E  1 171 ? -19.495 42.942 -2.500  1.00 74.21  ? 171 TRP E CG  1 
ATOM   9838  C CD1 . TRP E  1 171 ? -18.442 42.162 -2.123  1.00 82.02  ? 171 TRP E CD1 1 
ATOM   9839  C CD2 . TRP E  1 171 ? -20.198 43.278 -1.289  1.00 78.36  ? 171 TRP E CD2 1 
ATOM   9840  N NE1 . TRP E  1 171 ? -18.439 41.987 -0.766  1.00 84.01  ? 171 TRP E NE1 1 
ATOM   9841  C CE2 . TRP E  1 171 ? -19.505 42.658 -0.227  1.00 80.82  ? 171 TRP E CE2 1 
ATOM   9842  C CE3 . TRP E  1 171 ? -21.345 44.025 -0.998  1.00 91.98  ? 171 TRP E CE3 1 
ATOM   9843  C CZ2 . TRP E  1 171 ? -19.918 42.771 1.099   1.00 90.07  ? 171 TRP E CZ2 1 
ATOM   9844  C CZ3 . TRP E  1 171 ? -21.752 44.137 0.314   1.00 96.53  ? 171 TRP E CZ3 1 
ATOM   9845  C CH2 . TRP E  1 171 ? -21.048 43.517 1.346   1.00 90.76  ? 171 TRP E CH2 1 
ATOM   9846  N N   . VAL E  1 172 ? -21.699 41.075 -4.835  1.00 83.53  ? 172 VAL E N   1 
ATOM   9847  C CA  . VAL E  1 172 ? -22.645 39.951 -4.568  1.00 83.80  ? 172 VAL E CA  1 
ATOM   9848  C C   . VAL E  1 172 ? -22.275 38.775 -5.479  1.00 84.60  ? 172 VAL E C   1 
ATOM   9849  O O   . VAL E  1 172 ? -22.094 37.658 -4.953  1.00 85.45  ? 172 VAL E O   1 
ATOM   9850  C CB  . VAL E  1 172 ? -24.108 40.388 -4.769  1.00 78.00  ? 172 VAL E CB  1 
ATOM   9851  C CG1 . VAL E  1 172 ? -25.061 39.206 -4.692  1.00 82.64  ? 172 VAL E CG1 1 
ATOM   9852  C CG2 . VAL E  1 172 ? -24.512 41.469 -3.778  1.00 72.03  ? 172 VAL E CG2 1 
ATOM   9853  N N   . ILE E  1 173 ? -22.162 39.026 -6.788  1.00 73.42  ? 173 ILE E N   1 
ATOM   9854  C CA  . ILE E  1 173 ? -21.772 38.009 -7.811  1.00 68.71  ? 173 ILE E CA  1 
ATOM   9855  C C   . ILE E  1 173 ? -20.597 37.195 -7.260  1.00 66.92  ? 173 ILE E C   1 
ATOM   9856  O O   . ILE E  1 173 ? -20.657 35.954 -7.321  1.00 67.70  ? 173 ILE E O   1 
ATOM   9857  C CB  . ILE E  1 173 ? -21.423 38.676 -9.157  1.00 67.32  ? 173 ILE E CB  1 
ATOM   9858  C CG1 . ILE E  1 173 ? -22.617 39.436 -9.740  1.00 66.58  ? 173 ILE E CG1 1 
ATOM   9859  C CG2 . ILE E  1 173 ? -20.869 37.654 -10.140 1.00 63.66  ? 173 ILE E CG2 1 
ATOM   9860  C CD1 . ILE E  1 173 ? -22.313 40.169 -11.027 1.00 65.07  ? 173 ILE E CD1 1 
ATOM   9861  N N   . ALA E  1 174 ? -19.573 37.879 -6.741  1.00 70.42  ? 174 ALA E N   1 
ATOM   9862  C CA  . ALA E  1 174 ? -18.345 37.276 -6.173  1.00 70.48  ? 174 ALA E CA  1 
ATOM   9863  C C   . ALA E  1 174 ? -18.713 36.396 -4.973  1.00 65.50  ? 174 ALA E C   1 
ATOM   9864  O O   . ALA E  1 174 ? -18.428 35.183 -5.017  1.00 62.89  ? 174 ALA E O   1 
ATOM   9865  C CB  . ALA E  1 174 ? -17.371 38.361 -5.790  1.00 74.52  ? 174 ALA E CB  1 
ATOM   9866  N N   . ASN E  1 175 ? -19.326 36.991 -3.945  1.00 66.61  ? 175 ASN E N   1 
ATOM   9867  C CA  . ASN E  1 175 ? -19.761 36.295 -2.704  1.00 72.41  ? 175 ASN E CA  1 
ATOM   9868  C C   . ASN E  1 175 ? -20.478 34.993 -3.080  1.00 76.27  ? 175 ASN E C   1 
ATOM   9869  O O   . ASN E  1 175 ? -20.121 33.936 -2.523  1.00 84.04  ? 175 ASN E O   1 
ATOM   9870  C CB  . ASN E  1 175 ? -20.659 37.189 -1.844  1.00 72.03  ? 175 ASN E CB  1 
ATOM   9871  C CG  . ASN E  1 175 ? -19.883 38.219 -1.052  1.00 67.34  ? 175 ASN E CG  1 
ATOM   9872  O OD1 . ASN E  1 175 ? -19.816 39.384 -1.436  1.00 68.23  ? 175 ASN E OD1 1 
ATOM   9873  N ND2 . ASN E  1 175 ? -19.298 37.798 0.058   1.00 64.50  ? 175 ASN E ND2 1 
ATOM   9874  N N   . VAL E  1 176 ? -21.452 35.078 -3.991  1.00 80.80  ? 176 VAL E N   1 
ATOM   9875  C CA  . VAL E  1 176 ? -22.249 33.919 -4.495  1.00 83.74  ? 176 VAL E CA  1 
ATOM   9876  C C   . VAL E  1 176 ? -21.284 32.843 -5.008  1.00 84.01  ? 176 VAL E C   1 
ATOM   9877  O O   . VAL E  1 176 ? -21.235 31.753 -4.402  1.00 94.42  ? 176 VAL E O   1 
ATOM   9878  C CB  . VAL E  1 176 ? -23.240 34.358 -5.590  1.00 81.43  ? 176 VAL E CB  1 
ATOM   9879  C CG1 . VAL E  1 176 ? -23.776 33.175 -6.381  1.00 81.26  ? 176 VAL E CG1 1 
ATOM   9880  C CG2 . VAL E  1 176 ? -24.381 35.184 -5.017  1.00 78.72  ? 176 VAL E CG2 1 
ATOM   9881  N N   . VAL E  1 177 ? -20.545 33.149 -6.079  1.00 73.13  ? 177 VAL E N   1 
ATOM   9882  C CA  . VAL E  1 177 ? -19.605 32.212 -6.765  1.00 70.73  ? 177 VAL E CA  1 
ATOM   9883  C C   . VAL E  1 177 ? -18.747 31.498 -5.713  1.00 71.79  ? 177 VAL E C   1 
ATOM   9884  O O   . VAL E  1 177 ? -18.643 30.255 -5.781  1.00 70.32  ? 177 VAL E O   1 
ATOM   9885  C CB  . VAL E  1 177 ? -18.724 32.950 -7.790  1.00 74.19  ? 177 VAL E CB  1 
ATOM   9886  C CG1 . VAL E  1 177 ? -17.656 32.039 -8.377  1.00 77.85  ? 177 VAL E CG1 1 
ATOM   9887  C CG2 . VAL E  1 177 ? -19.555 33.581 -8.896  1.00 77.45  ? 177 VAL E CG2 1 
ATOM   9888  N N   . LEU E  1 178 ? -18.152 32.259 -4.788  1.00 66.22  ? 178 LEU E N   1 
ATOM   9889  C CA  . LEU E  1 178 ? -17.230 31.741 -3.741  1.00 71.59  ? 178 LEU E CA  1 
ATOM   9890  C C   . LEU E  1 178 ? -18.006 30.840 -2.774  1.00 72.62  ? 178 LEU E C   1 
ATOM   9891  O O   . LEU E  1 178 ? -17.578 29.687 -2.572  1.00 74.93  ? 178 LEU E O   1 
ATOM   9892  C CB  . LEU E  1 178 ? -16.585 32.919 -3.004  1.00 74.25  ? 178 LEU E CB  1 
ATOM   9893  C CG  . LEU E  1 178 ? -15.533 33.691 -3.800  1.00 75.13  ? 178 LEU E CG  1 
ATOM   9894  C CD1 . LEU E  1 178 ? -15.052 34.908 -3.024  1.00 74.47  ? 178 LEU E CD1 1 
ATOM   9895  C CD2 . LEU E  1 178 ? -14.362 32.790 -4.167  1.00 72.49  ? 178 LEU E CD2 1 
ATOM   9896  N N   . ILE E  1 179 ? -19.100 31.354 -2.204  1.00 74.11  ? 179 ILE E N   1 
ATOM   9897  C CA  . ILE E  1 179 ? -19.952 30.635 -1.210  1.00 80.44  ? 179 ILE E CA  1 
ATOM   9898  C C   . ILE E  1 179 ? -20.412 29.303 -1.817  1.00 86.11  ? 179 ILE E C   1 
ATOM   9899  O O   . ILE E  1 179 ? -20.280 28.267 -1.134  1.00 79.33  ? 179 ILE E O   1 
ATOM   9900  C CB  . ILE E  1 179 ? -21.135 31.516 -0.767  1.00 80.41  ? 179 ILE E CB  1 
ATOM   9901  C CG1 . ILE E  1 179 ? -20.666 32.675 0.117   1.00 81.76  ? 179 ILE E CG1 1 
ATOM   9902  C CG2 . ILE E  1 179 ? -22.203 30.677 -0.080  1.00 82.32  ? 179 ILE E CG2 1 
ATOM   9903  C CD1 . ILE E  1 179 ? -21.710 33.743 0.343   1.00 86.00  ? 179 ILE E CD1 1 
ATOM   9904  N N   . ARG E  1 180 ? -20.929 29.333 -3.050  1.00 87.62  ? 180 ARG E N   1 
ATOM   9905  C CA  . ARG E  1 180 ? -21.373 28.123 -3.797  1.00 82.58  ? 180 ARG E CA  1 
ATOM   9906  C C   . ARG E  1 180 ? -20.219 27.113 -3.843  1.00 82.64  ? 180 ARG E C   1 
ATOM   9907  O O   . ARG E  1 180 ? -20.411 25.967 -3.376  1.00 79.59  ? 180 ARG E O   1 
ATOM   9908  C CB  . ARG E  1 180 ? -21.834 28.494 -5.211  1.00 72.27  ? 180 ARG E CB  1 
ATOM   9909  N N   . ALA E  1 181 ? -19.066 27.538 -4.373  1.00 80.10  ? 181 ALA E N   1 
ATOM   9910  C CA  . ALA E  1 181 ? -17.855 26.710 -4.587  1.00 71.61  ? 181 ALA E CA  1 
ATOM   9911  C C   . ALA E  1 181 ? -17.391 26.096 -3.261  1.00 67.54  ? 181 ALA E C   1 
ATOM   9912  O O   . ALA E  1 181 ? -16.898 24.951 -3.283  1.00 65.53  ? 181 ALA E O   1 
ATOM   9913  C CB  . ALA E  1 181 ? -16.768 27.549 -5.211  1.00 74.33  ? 181 ALA E CB  1 
ATOM   9914  N N   . VAL E  1 182 ? -17.531 26.835 -2.156  1.00 63.63  ? 182 VAL E N   1 
ATOM   9915  C CA  . VAL E  1 182 ? -17.122 26.392 -0.789  1.00 69.11  ? 182 VAL E CA  1 
ATOM   9916  C C   . VAL E  1 182 ? -18.133 25.356 -0.288  1.00 78.71  ? 182 VAL E C   1 
ATOM   9917  O O   . VAL E  1 182 ? -17.696 24.273 0.141   1.00 91.65  ? 182 VAL E O   1 
ATOM   9918  C CB  . VAL E  1 182 ? -17.007 27.579 0.187   1.00 68.84  ? 182 VAL E CB  1 
ATOM   9919  C CG1 . VAL E  1 182 ? -16.780 27.114 1.618   1.00 64.52  ? 182 VAL E CG1 1 
ATOM   9920  C CG2 . VAL E  1 182 ? -15.916 28.551 -0.237  1.00 70.84  ? 182 VAL E CG2 1 
ATOM   9921  N N   . ARG E  1 183 ? -19.428 25.685 -0.346  1.00 89.07  ? 183 ARG E N   1 
ATOM   9922  C CA  . ARG E  1 183 ? -20.543 24.831 0.150   1.00 88.49  ? 183 ARG E CA  1 
ATOM   9923  C C   . ARG E  1 183 ? -20.495 23.464 -0.543  1.00 92.47  ? 183 ARG E C   1 
ATOM   9924  O O   . ARG E  1 183 ? -20.910 22.471 0.087   1.00 104.76 ? 183 ARG E O   1 
ATOM   9925  C CB  . ARG E  1 183 ? -21.892 25.518 -0.086  1.00 90.94  ? 183 ARG E CB  1 
ATOM   9926  C CG  . ARG E  1 183 ? -23.049 24.899 0.686   1.00 85.03  ? 183 ARG E CG  1 
ATOM   9927  N N   . GLN E  1 184 ? -20.007 23.420 -1.788  1.00 87.82  ? 184 GLN E N   1 
ATOM   9928  C CA  . GLN E  1 184 ? -19.902 22.182 -2.609  1.00 83.87  ? 184 GLN E CA  1 
ATOM   9929  C C   . GLN E  1 184 ? -18.715 21.339 -2.131  1.00 80.62  ? 184 GLN E C   1 
ATOM   9930  O O   . GLN E  1 184 ? -18.816 20.098 -2.173  1.00 76.71  ? 184 GLN E O   1 
ATOM   9931  C CB  . GLN E  1 184 ? -19.728 22.531 -4.087  1.00 91.75  ? 184 GLN E CB  1 
ATOM   9932  C CG  . GLN E  1 184 ? -20.935 23.224 -4.698  1.00 101.69 ? 184 GLN E CG  1 
ATOM   9933  C CD  . GLN E  1 184 ? -20.697 23.595 -6.141  1.00 117.78 ? 184 GLN E CD  1 
ATOM   9934  O OE1 . GLN E  1 184 ? -19.656 23.289 -6.718  1.00 118.21 ? 184 GLN E OE1 1 
ATOM   9935  N NE2 . GLN E  1 184 ? -21.670 24.266 -6.735  1.00 136.28 ? 184 GLN E NE2 1 
ATOM   9936  N N   . SER E  1 185 ? -17.629 21.994 -1.710  1.00 90.52  ? 185 SER E N   1 
ATOM   9937  C CA  . SER E  1 185 ? -16.355 21.352 -1.291  1.00 96.59  ? 185 SER E CA  1 
ATOM   9938  C C   . SER E  1 185 ? -16.517 20.711 0.093   1.00 96.58  ? 185 SER E C   1 
ATOM   9939  O O   . SER E  1 185 ? -16.065 19.562 0.266   1.00 113.14 ? 185 SER E O   1 
ATOM   9940  C CB  . SER E  1 185 ? -15.220 22.345 -1.309  1.00 94.21  ? 185 SER E CB  1 
ATOM   9941  O OG  . SER E  1 185 ? -14.989 22.828 -2.625  1.00 87.98  ? 185 SER E OG  1 
ATOM   9942  N N   . LEU E  1 186 ? -17.148 21.425 1.031   1.00 91.68  ? 186 LEU E N   1 
ATOM   9943  C CA  . LEU E  1 186 ? -17.243 21.055 2.472   1.00 98.57  ? 186 LEU E CA  1 
ATOM   9944  C C   . LEU E  1 186 ? -17.709 19.607 2.627   1.00 100.84 ? 186 LEU E C   1 
ATOM   9945  O O   . LEU E  1 186 ? -17.197 18.881 3.476   1.00 93.29  ? 186 LEU E O   1 
ATOM   9946  C CB  . LEU E  1 186 ? -18.191 22.034 3.172   1.00 102.10 ? 186 LEU E CB  1 
ATOM   9947  C CG  . LEU E  1 186 ? -17.664 23.463 3.310   1.00 106.22 ? 186 LEU E CG  1 
ATOM   9948  C CD1 . LEU E  1 186 ? -18.710 24.373 3.937   1.00 107.77 ? 186 LEU E CD1 1 
ATOM   9949  C CD2 . LEU E  1 186 ? -16.374 23.491 4.119   1.00 110.51 ? 186 LEU E CD2 1 
ATOM   9950  N N   . PRO E  1 187 ? -18.701 19.139 1.835   1.00 107.66 ? 187 PRO E N   1 
ATOM   9951  C CA  . PRO E  1 187 ? -19.142 17.744 1.894   1.00 99.60  ? 187 PRO E CA  1 
ATOM   9952  C C   . PRO E  1 187 ? -18.031 16.719 1.614   1.00 95.33  ? 187 PRO E C   1 
ATOM   9953  O O   . PRO E  1 187 ? -17.970 15.736 2.327   1.00 88.50  ? 187 PRO E O   1 
ATOM   9954  C CB  . PRO E  1 187 ? -20.214 17.653 0.798   1.00 108.42 ? 187 PRO E CB  1 
ATOM   9955  C CG  . PRO E  1 187 ? -20.712 19.074 0.645   1.00 115.83 ? 187 PRO E CG  1 
ATOM   9956  C CD  . PRO E  1 187 ? -19.489 19.936 0.882   1.00 120.25 ? 187 PRO E CD  1 
ATOM   9957  N N   . THR E  1 188 ? -17.192 16.969 0.601   1.00 101.71 ? 188 THR E N   1 
ATOM   9958  C CA  . THR E  1 188 ? -16.157 16.020 0.096   1.00 100.77 ? 188 THR E CA  1 
ATOM   9959  C C   . THR E  1 188 ? -14.906 16.064 0.983   1.00 86.66  ? 188 THR E C   1 
ATOM   9960  O O   . THR E  1 188 ? -14.049 15.174 0.827   1.00 78.91  ? 188 THR E O   1 
ATOM   9961  C CB  . THR E  1 188 ? -15.774 16.310 -1.362  1.00 109.96 ? 188 THR E CB  1 
ATOM   9962  O OG1 . THR E  1 188 ? -15.033 17.529 -1.407  1.00 118.20 ? 188 THR E OG1 1 
ATOM   9963  C CG2 . THR E  1 188 ? -16.970 16.408 -2.282  1.00 110.30 ? 188 THR E CG2 1 
ATOM   9964  N N   . LEU E  1 189 ? -14.804 17.060 1.869   1.00 95.91  ? 189 LEU E N   1 
ATOM   9965  C CA  . LEU E  1 189 ? -13.641 17.255 2.777   1.00 95.15  ? 189 LEU E CA  1 
ATOM   9966  C C   . LEU E  1 189 ? -13.871 16.470 4.074   1.00 81.28  ? 189 LEU E C   1 
ATOM   9967  O O   . LEU E  1 189 ? -15.018 16.044 4.312   1.00 69.25  ? 189 LEU E O   1 
ATOM   9968  C CB  . LEU E  1 189 ? -13.469 18.749 3.069   1.00 99.28  ? 189 LEU E CB  1 
ATOM   9969  C CG  . LEU E  1 189 ? -13.164 19.637 1.863   1.00 108.78 ? 189 LEU E CG  1 
ATOM   9970  C CD1 . LEU E  1 189 ? -12.914 21.072 2.303   1.00 111.89 ? 189 LEU E CD1 1 
ATOM   9971  C CD2 . LEU E  1 189 ? -11.977 19.105 1.075   1.00 113.81 ? 189 LEU E CD2 1 
ATOM   9972  N N   . THR E  1 190 ? -12.813 16.290 4.872   1.00 77.91  ? 190 THR E N   1 
ATOM   9973  C CA  . THR E  1 190 ? -12.859 15.659 6.219   1.00 80.90  ? 190 THR E CA  1 
ATOM   9974  C C   . THR E  1 190 ? -13.444 16.662 7.208   1.00 84.11  ? 190 THR E C   1 
ATOM   9975  O O   . THR E  1 190 ? -13.684 17.812 6.851   1.00 73.37  ? 190 THR E O   1 
ATOM   9976  C CB  . THR E  1 190 ? -11.469 15.183 6.660   1.00 79.01  ? 190 THR E CB  1 
ATOM   9977  O OG1 . THR E  1 190 ? -10.698 16.322 7.043   1.00 78.31  ? 190 THR E OG1 1 
ATOM   9978  C CG2 . THR E  1 190 ? -10.749 14.408 5.579   1.00 79.04  ? 190 THR E CG2 1 
ATOM   9979  N N   . PRO E  1 191 ? -13.704 16.261 8.473   1.00 96.77  ? 191 PRO E N   1 
ATOM   9980  C CA  . PRO E  1 191 ? -14.193 17.192 9.491   1.00 96.54  ? 191 PRO E CA  1 
ATOM   9981  C C   . PRO E  1 191 ? -13.216 18.349 9.747   1.00 93.32  ? 191 PRO E C   1 
ATOM   9982  O O   . PRO E  1 191 ? -13.652 19.483 9.818   1.00 78.07  ? 191 PRO E O   1 
ATOM   9983  C CB  . PRO E  1 191 ? -14.324 16.327 10.755  1.00 93.60  ? 191 PRO E CB  1 
ATOM   9984  C CG  . PRO E  1 191 ? -14.425 14.906 10.234  1.00 98.08  ? 191 PRO E CG  1 
ATOM   9985  C CD  . PRO E  1 191 ? -13.573 14.888 8.982   1.00 96.02  ? 191 PRO E CD  1 
ATOM   9986  N N   . GLU E  1 192 ? -11.925 18.026 9.876   1.00 98.84  ? 192 GLU E N   1 
ATOM   9987  C CA  . GLU E  1 192 ? -10.837 18.981 10.215  1.00 100.58 ? 192 GLU E CA  1 
ATOM   9988  C C   . GLU E  1 192 ? -10.651 19.982 9.068   1.00 92.65  ? 192 GLU E C   1 
ATOM   9989  O O   . GLU E  1 192 ? -10.547 21.184 9.363   1.00 90.20  ? 192 GLU E O   1 
ATOM   9990  C CB  . GLU E  1 192 ? -9.546  18.225 10.538  1.00 107.71 ? 192 GLU E CB  1 
ATOM   9991  C CG  . GLU E  1 192 ? -9.507  16.810 9.990   1.00 113.12 ? 192 GLU E CG  1 
ATOM   9992  C CD  . GLU E  1 192 ? -8.300  16.003 10.436  1.00 115.26 ? 192 GLU E CD  1 
ATOM   9993  O OE1 . GLU E  1 192 ? -7.644  15.398 9.565   1.00 113.72 ? 192 GLU E OE1 1 
ATOM   9994  O OE2 . GLU E  1 192 ? -8.021  15.980 11.652  1.00 106.49 ? 192 GLU E OE2 1 
ATOM   9995  N N   . SER E  1 193 ? -10.612 19.505 7.818   1.00 88.88  ? 193 SER E N   1 
ATOM   9996  C CA  . SER E  1 193 ? -10.501 20.342 6.592   1.00 92.41  ? 193 SER E CA  1 
ATOM   9997  C C   . SER E  1 193 ? -11.754 21.218 6.454   1.00 97.19  ? 193 SER E C   1 
ATOM   9998  O O   . SER E  1 193 ? -11.612 22.450 6.311   1.00 103.31 ? 193 SER E O   1 
ATOM   9999  C CB  . SER E  1 193 ? -10.289 19.491 5.363   1.00 85.54  ? 193 SER E CB  1 
ATOM   10000 O OG  . SER E  1 193 ? -9.052  18.794 5.424   1.00 91.32  ? 193 SER E OG  1 
ATOM   10001 N N   . HIS E  1 194 ? -12.934 20.591 6.499   1.00 103.28 ? 194 HIS E N   1 
ATOM   10002 C CA  . HIS E  1 194 ? -14.271 21.244 6.459   1.00 104.22 ? 194 HIS E CA  1 
ATOM   10003 C C   . HIS E  1 194 ? -14.241 22.528 7.296   1.00 96.90  ? 194 HIS E C   1 
ATOM   10004 O O   . HIS E  1 194 ? -14.571 23.599 6.751   1.00 96.21  ? 194 HIS E O   1 
ATOM   10005 C CB  . HIS E  1 194 ? -15.343 20.253 6.940   1.00 112.11 ? 194 HIS E CB  1 
ATOM   10006 C CG  . HIS E  1 194 ? -16.681 20.864 7.199   1.00 114.46 ? 194 HIS E CG  1 
ATOM   10007 N ND1 . HIS E  1 194 ? -17.735 20.743 6.311   1.00 115.91 ? 194 HIS E ND1 1 
ATOM   10008 C CD2 . HIS E  1 194 ? -17.144 21.587 8.242   1.00 111.36 ? 194 HIS E CD2 1 
ATOM   10009 C CE1 . HIS E  1 194 ? -18.787 21.374 6.795   1.00 115.30 ? 194 HIS E CE1 1 
ATOM   10010 N NE2 . HIS E  1 194 ? -18.450 21.900 7.979   1.00 109.60 ? 194 HIS E NE2 1 
ATOM   10011 N N   . THR E  1 195 ? -13.852 22.412 8.570   1.00 84.36  ? 195 THR E N   1 
ATOM   10012 C CA  . THR E  1 195 ? -13.830 23.515 9.568   1.00 89.44  ? 195 THR E CA  1 
ATOM   10013 C C   . THR E  1 195 ? -12.940 24.661 9.074   1.00 89.64  ? 195 THR E C   1 
ATOM   10014 O O   . THR E  1 195 ? -13.406 25.815 9.107   1.00 84.27  ? 195 THR E O   1 
ATOM   10015 C CB  . THR E  1 195 ? -13.356 23.012 10.937  1.00 92.48  ? 195 THR E CB  1 
ATOM   10016 O OG1 . THR E  1 195 ? -14.180 21.904 11.300  1.00 99.41  ? 195 THR E OG1 1 
ATOM   10017 C CG2 . THR E  1 195 ? -13.411 24.077 12.012  1.00 88.30  ? 195 THR E CG2 1 
ATOM   10018 N N   . MET E  1 196 ? -11.710 24.352 8.649   1.00 88.96  ? 196 MET E N   1 
ATOM   10019 C CA  . MET E  1 196 ? -10.687 25.350 8.231   1.00 82.88  ? 196 MET E CA  1 
ATOM   10020 C C   . MET E  1 196 ? -11.213 26.158 7.039   1.00 75.62  ? 196 MET E C   1 
ATOM   10021 O O   . MET E  1 196 ? -11.200 27.404 7.121   1.00 88.26  ? 196 MET E O   1 
ATOM   10022 C CB  . MET E  1 196 ? -9.372  24.669 7.839   1.00 86.25  ? 196 MET E CB  1 
ATOM   10023 C CG  . MET E  1 196 ? -8.555  24.183 9.021   1.00 85.73  ? 196 MET E CG  1 
ATOM   10024 S SD  . MET E  1 196 ? -8.118  25.514 10.167  1.00 83.14  ? 196 MET E SD  1 
ATOM   10025 C CE  . MET E  1 196 ? -7.256  26.629 9.061   1.00 83.35  ? 196 MET E CE  1 
ATOM   10026 N N   . LEU E  1 197 ? -11.654 25.473 5.978   1.00 67.09  ? 197 LEU E N   1 
ATOM   10027 C CA  . LEU E  1 197 ? -12.167 26.105 4.733   1.00 70.20  ? 197 LEU E CA  1 
ATOM   10028 C C   . LEU E  1 197 ? -13.297 27.078 5.089   1.00 70.76  ? 197 LEU E C   1 
ATOM   10029 O O   . LEU E  1 197 ? -13.275 28.215 4.582   1.00 75.76  ? 197 LEU E O   1 
ATOM   10030 C CB  . LEU E  1 197 ? -12.654 25.024 3.763   1.00 69.84  ? 197 LEU E CB  1 
ATOM   10031 C CG  . LEU E  1 197 ? -12.975 25.522 2.353   1.00 73.68  ? 197 LEU E CG  1 
ATOM   10032 C CD1 . LEU E  1 197 ? -11.755 26.171 1.719   1.00 74.00  ? 197 LEU E CD1 1 
ATOM   10033 C CD2 . LEU E  1 197 ? -13.491 24.395 1.474   1.00 78.08  ? 197 LEU E CD2 1 
ATOM   10034 N N   . LYS E  1 198 ? -14.242 26.642 5.928   1.00 76.64  ? 198 LYS E N   1 
ATOM   10035 C CA  . LYS E  1 198 ? -15.361 27.479 6.442   1.00 78.52  ? 198 LYS E CA  1 
ATOM   10036 C C   . LYS E  1 198 ? -14.774 28.721 7.121   1.00 78.94  ? 198 LYS E C   1 
ATOM   10037 O O   . LYS E  1 198 ? -15.195 29.837 6.767   1.00 93.61  ? 198 LYS E O   1 
ATOM   10038 C CB  . LYS E  1 198 ? -16.237 26.680 7.413   1.00 74.32  ? 198 LYS E CB  1 
ATOM   10039 N N   . SER E  1 199 ? -13.830 28.525 8.048   1.00 73.17  ? 199 SER E N   1 
ATOM   10040 C CA  . SER E  1 199 ? -13.133 29.603 8.800   1.00 77.96  ? 199 SER E CA  1 
ATOM   10041 C C   . SER E  1 199 ? -12.532 30.617 7.821   1.00 82.90  ? 199 SER E C   1 
ATOM   10042 O O   . SER E  1 199 ? -12.894 31.811 7.905   1.00 93.82  ? 199 SER E O   1 
ATOM   10043 C CB  . SER E  1 199 ? -12.072 29.038 9.708   1.00 77.11  ? 199 SER E CB  1 
ATOM   10044 O OG  . SER E  1 199 ? -11.269 30.077 10.248  1.00 82.72  ? 199 SER E OG  1 
ATOM   10045 N N   . ALA E  1 200 ? -11.645 30.150 6.936   1.00 79.67  ? 200 ALA E N   1 
ATOM   10046 C CA  . ALA E  1 200 ? -10.943 30.966 5.919   1.00 75.63  ? 200 ALA E CA  1 
ATOM   10047 C C   . ALA E  1 200 ? -11.967 31.800 5.139   1.00 80.05  ? 200 ALA E C   1 
ATOM   10048 O O   . ALA E  1 200 ? -11.771 33.027 5.028   1.00 100.55 ? 200 ALA E O   1 
ATOM   10049 C CB  . ALA E  1 200 ? -10.146 30.070 5.003   1.00 71.29  ? 200 ALA E CB  1 
ATOM   10050 N N   . ALA E  1 201 ? -13.019 31.148 4.632   1.00 72.18  ? 201 ALA E N   1 
ATOM   10051 C CA  . ALA E  1 201 ? -14.089 31.754 3.804   1.00 74.75  ? 201 ALA E CA  1 
ATOM   10052 C C   . ALA E  1 201 ? -14.748 32.908 4.569   1.00 74.52  ? 201 ALA E C   1 
ATOM   10053 O O   . ALA E  1 201 ? -14.981 33.967 3.954   1.00 69.87  ? 201 ALA E O   1 
ATOM   10054 C CB  . ALA E  1 201 ? -15.097 30.700 3.420   1.00 75.87  ? 201 ALA E CB  1 
ATOM   10055 N N   . ILE E  1 202 ? -15.037 32.703 5.857   1.00 72.98  ? 202 ILE E N   1 
ATOM   10056 C CA  . ILE E  1 202 ? -15.675 33.718 6.748   1.00 75.56  ? 202 ILE E CA  1 
ATOM   10057 C C   . ILE E  1 202 ? -14.749 34.935 6.850   1.00 68.53  ? 202 ILE E C   1 
ATOM   10058 O O   . ILE E  1 202 ? -15.204 36.049 6.528   1.00 60.68  ? 202 ILE E O   1 
ATOM   10059 C CB  . ILE E  1 202 ? -15.991 33.117 8.132   1.00 73.76  ? 202 ILE E CB  1 
ATOM   10060 C CG1 . ILE E  1 202 ? -17.071 32.034 8.040   1.00 67.75  ? 202 ILE E CG1 1 
ATOM   10061 C CG2 . ILE E  1 202 ? -16.371 34.210 9.119   1.00 73.70  ? 202 ILE E CG2 1 
ATOM   10062 C CD1 . ILE E  1 202 ? -17.277 31.261 9.322   1.00 68.76  ? 202 ILE E CD1 1 
ATOM   10063 N N   . VAL E  1 203 ? -13.500 34.719 7.274   1.00 65.62  ? 203 VAL E N   1 
ATOM   10064 C CA  . VAL E  1 203 ? -12.480 35.790 7.491   1.00 63.07  ? 203 VAL E CA  1 
ATOM   10065 C C   . VAL E  1 203 ? -12.465 36.712 6.268   1.00 60.86  ? 203 VAL E C   1 
ATOM   10066 O O   . VAL E  1 203 ? -12.478 37.943 6.459   1.00 65.29  ? 203 VAL E O   1 
ATOM   10067 C CB  . VAL E  1 203 ? -11.081 35.203 7.756   1.00 67.48  ? 203 VAL E CB  1 
ATOM   10068 C CG1 . VAL E  1 203 ? -10.034 36.296 7.913   1.00 63.05  ? 203 VAL E CG1 1 
ATOM   10069 C CG2 . VAL E  1 203 ? -11.076 34.279 8.965   1.00 77.42  ? 203 VAL E CG2 1 
ATOM   10070 N N   . LEU E  1 204 ? -12.434 36.134 5.064   1.00 54.75  ? 204 LEU E N   1 
ATOM   10071 C CA  . LEU E  1 204 ? -12.366 36.886 3.783   1.00 59.00  ? 204 LEU E CA  1 
ATOM   10072 C C   . LEU E  1 204 ? -13.704 37.589 3.535   1.00 65.46  ? 204 LEU E C   1 
ATOM   10073 O O   . LEU E  1 204 ? -13.713 38.836 3.501   1.00 75.38  ? 204 LEU E O   1 
ATOM   10074 C CB  . LEU E  1 204 ? -12.023 35.921 2.644   1.00 58.75  ? 204 LEU E CB  1 
ATOM   10075 C CG  . LEU E  1 204 ? -11.925 36.551 1.255   1.00 66.25  ? 204 LEU E CG  1 
ATOM   10076 C CD1 . LEU E  1 204 ? -10.895 35.828 0.405   1.00 70.88  ? 204 LEU E CD1 1 
ATOM   10077 C CD2 . LEU E  1 204 ? -13.275 36.550 0.559   1.00 75.85  ? 204 LEU E CD2 1 
ATOM   10078 N N   . LEU E  1 205 ? -14.782 36.812 3.388   1.00 76.00  ? 205 LEU E N   1 
ATOM   10079 C CA  . LEU E  1 205 ? -16.132 37.290 2.981   1.00 75.13  ? 205 LEU E CA  1 
ATOM   10080 C C   . LEU E  1 205 ? -16.693 38.249 4.039   1.00 69.85  ? 205 LEU E C   1 
ATOM   10081 O O   . LEU E  1 205 ? -17.309 39.260 3.646   1.00 71.83  ? 205 LEU E O   1 
ATOM   10082 C CB  . LEU E  1 205 ? -17.047 36.077 2.785   1.00 77.77  ? 205 LEU E CB  1 
ATOM   10083 C CG  . LEU E  1 205 ? -16.598 35.093 1.706   1.00 81.07  ? 205 LEU E CG  1 
ATOM   10084 C CD1 . LEU E  1 205 ? -17.485 33.858 1.690   1.00 94.99  ? 205 LEU E CD1 1 
ATOM   10085 C CD2 . LEU E  1 205 ? -16.582 35.759 0.338   1.00 80.44  ? 205 LEU E CD2 1 
ATOM   10086 N N   . ALA E  1 206 ? -16.488 37.937 5.323   1.00 60.72  ? 206 ALA E N   1 
ATOM   10087 C CA  . ALA E  1 206 ? -16.911 38.764 6.477   1.00 60.45  ? 206 ALA E CA  1 
ATOM   10088 C C   . ALA E  1 206 ? -16.206 40.123 6.419   1.00 62.88  ? 206 ALA E C   1 
ATOM   10089 O O   . ALA E  1 206 ? -16.910 41.148 6.340   1.00 71.20  ? 206 ALA E O   1 
ATOM   10090 C CB  . ALA E  1 206 ? -16.609 38.046 7.770   1.00 64.99  ? 206 ALA E CB  1 
ATOM   10091 N N   . GLY E  1 207 ? -14.869 40.120 6.454   1.00 62.82  ? 207 GLY E N   1 
ATOM   10092 C CA  . GLY E  1 207 ? -14.027 41.333 6.446   1.00 61.69  ? 207 GLY E CA  1 
ATOM   10093 C C   . GLY E  1 207 ? -14.398 42.278 5.315   1.00 60.50  ? 207 GLY E C   1 
ATOM   10094 O O   . GLY E  1 207 ? -14.418 43.504 5.553   1.00 65.18  ? 207 GLY E O   1 
ATOM   10095 N N   . TRP E  1 208 ? -14.687 41.725 4.133   1.00 60.86  ? 208 TRP E N   1 
ATOM   10096 C CA  . TRP E  1 208 ? -15.031 42.467 2.889   1.00 64.13  ? 208 TRP E CA  1 
ATOM   10097 C C   . TRP E  1 208 ? -16.033 43.589 3.181   1.00 63.48  ? 208 TRP E C   1 
ATOM   10098 O O   . TRP E  1 208 ? -15.958 44.631 2.504   1.00 63.89  ? 208 TRP E O   1 
ATOM   10099 C CB  . TRP E  1 208 ? -15.578 41.501 1.832   1.00 69.94  ? 208 TRP E CB  1 
ATOM   10100 C CG  . TRP E  1 208 ? -14.514 40.856 1.002   1.00 78.02  ? 208 TRP E CG  1 
ATOM   10101 C CD1 . TRP E  1 208 ? -13.185 40.764 1.298   1.00 83.75  ? 208 TRP E CD1 1 
ATOM   10102 C CD2 . TRP E  1 208 ? -14.691 40.189 -0.260  1.00 83.90  ? 208 TRP E CD2 1 
ATOM   10103 N NE1 . TRP E  1 208 ? -12.522 40.097 0.304   1.00 90.99  ? 208 TRP E NE1 1 
ATOM   10104 C CE2 . TRP E  1 208 ? -13.419 39.731 -0.665  1.00 90.91  ? 208 TRP E CE2 1 
ATOM   10105 C CE3 . TRP E  1 208 ? -15.792 39.938 -1.085  1.00 83.55  ? 208 TRP E CE3 1 
ATOM   10106 C CZ2 . TRP E  1 208 ? -13.225 39.036 -1.858  1.00 90.28  ? 208 TRP E CZ2 1 
ATOM   10107 C CZ3 . TRP E  1 208 ? -15.599 39.253 -2.264  1.00 80.79  ? 208 TRP E CZ3 1 
ATOM   10108 C CH2 . TRP E  1 208 ? -14.332 38.809 -2.643  1.00 82.52  ? 208 TRP E CH2 1 
ATOM   10109 N N   . VAL E  1 209 ? -16.936 43.374 4.143   1.00 61.03  ? 209 VAL E N   1 
ATOM   10110 C CA  . VAL E  1 209 ? -18.066 44.292 4.477   1.00 60.64  ? 209 VAL E CA  1 
ATOM   10111 C C   . VAL E  1 209 ? -17.507 45.655 4.901   1.00 57.44  ? 209 VAL E C   1 
ATOM   10112 O O   . VAL E  1 209 ? -18.106 46.685 4.538   1.00 54.53  ? 209 VAL E O   1 
ATOM   10113 C CB  . VAL E  1 209 ? -18.954 43.692 5.584   1.00 67.19  ? 209 VAL E CB  1 
ATOM   10114 C CG1 . VAL E  1 209 ? -19.983 44.693 6.089   1.00 71.75  ? 209 VAL E CG1 1 
ATOM   10115 C CG2 . VAL E  1 209 ? -19.628 42.407 5.131   1.00 71.64  ? 209 VAL E CG2 1 
ATOM   10116 N N   . VAL E  1 210 ? -16.404 45.653 5.651   1.00 51.40  ? 210 VAL E N   1 
ATOM   10117 C CA  . VAL E  1 210 ? -15.801 46.872 6.263   1.00 51.55  ? 210 VAL E CA  1 
ATOM   10118 C C   . VAL E  1 210 ? -15.564 47.922 5.172   1.00 55.69  ? 210 VAL E C   1 
ATOM   10119 O O   . VAL E  1 210 ? -15.759 49.116 5.458   1.00 62.70  ? 210 VAL E O   1 
ATOM   10120 C CB  . VAL E  1 210 ? -14.496 46.536 7.007   1.00 50.18  ? 210 VAL E CB  1 
ATOM   10121 C CG1 . VAL E  1 210 ? -13.817 47.791 7.527   1.00 51.25  ? 210 VAL E CG1 1 
ATOM   10122 C CG2 . VAL E  1 210 ? -14.731 45.545 8.136   1.00 50.18  ? 210 VAL E CG2 1 
ATOM   10123 N N   . TYR E  1 211 ? -15.173 47.491 3.970   1.00 56.81  ? 211 TYR E N   1 
ATOM   10124 C CA  . TYR E  1 211 ? -14.689 48.372 2.874   1.00 64.62  ? 211 TYR E CA  1 
ATOM   10125 C C   . TYR E  1 211 ? -15.834 49.233 2.340   1.00 65.21  ? 211 TYR E C   1 
ATOM   10126 O O   . TYR E  1 211 ? -15.716 50.455 2.307   1.00 73.70  ? 211 TYR E O   1 
ATOM   10127 C CB  . TYR E  1 211 ? -13.984 47.538 1.802   1.00 68.03  ? 211 TYR E CB  1 
ATOM   10128 C CG  . TYR E  1 211 ? -12.694 46.924 2.285   1.00 70.43  ? 211 TYR E CG  1 
ATOM   10129 C CD1 . TYR E  1 211 ? -11.479 47.559 2.086   1.00 70.02  ? 211 TYR E CD1 1 
ATOM   10130 C CD2 . TYR E  1 211 ? -12.690 45.727 2.980   1.00 71.29  ? 211 TYR E CD2 1 
ATOM   10131 C CE1 . TYR E  1 211 ? -10.292 47.011 2.545   1.00 67.40  ? 211 TYR E CE1 1 
ATOM   10132 C CE2 . TYR E  1 211 ? -11.513 45.163 3.443   1.00 73.48  ? 211 TYR E CE2 1 
ATOM   10133 C CZ  . TYR E  1 211 ? -10.308 45.808 3.225   1.00 70.32  ? 211 TYR E CZ  1 
ATOM   10134 O OH  . TYR E  1 211 ? -9.147  45.257 3.683   1.00 69.56  ? 211 TYR E OH  1 
ATOM   10135 N N   . PRO E  1 212 ? -16.974 48.646 1.911   1.00 68.21  ? 212 PRO E N   1 
ATOM   10136 C CA  . PRO E  1 212 ? -18.114 49.439 1.450   1.00 65.65  ? 212 PRO E CA  1 
ATOM   10137 C C   . PRO E  1 212 ? -18.575 50.457 2.504   1.00 68.13  ? 212 PRO E C   1 
ATOM   10138 O O   . PRO E  1 212 ? -18.962 51.550 2.132   1.00 67.42  ? 212 PRO E O   1 
ATOM   10139 C CB  . PRO E  1 212 ? -19.217 48.401 1.193   1.00 63.51  ? 212 PRO E CB  1 
ATOM   10140 C CG  . PRO E  1 212 ? -18.467 47.103 0.966   1.00 66.75  ? 212 PRO E CG  1 
ATOM   10141 C CD  . PRO E  1 212 ? -17.225 47.200 1.829   1.00 70.49  ? 212 PRO E CD  1 
ATOM   10142 N N   . ILE E  1 213 ? -18.525 50.070 3.782   1.00 66.24  ? 213 ILE E N   1 
ATOM   10143 C CA  . ILE E  1 213 ? -18.929 50.916 4.945   1.00 65.83  ? 213 ILE E CA  1 
ATOM   10144 C C   . ILE E  1 213 ? -18.026 52.154 4.995   1.00 67.74  ? 213 ILE E C   1 
ATOM   10145 O O   . ILE E  1 213 ? -18.559 53.273 5.104   1.00 72.51  ? 213 ILE E O   1 
ATOM   10146 C CB  . ILE E  1 213 ? -18.866 50.108 6.256   1.00 59.67  ? 213 ILE E CB  1 
ATOM   10147 C CG1 . ILE E  1 213 ? -19.897 48.976 6.272   1.00 58.43  ? 213 ILE E CG1 1 
ATOM   10148 C CG2 . ILE E  1 213 ? -19.015 51.022 7.462   1.00 57.67  ? 213 ILE E CG2 1 
ATOM   10149 C CD1 . ILE E  1 213 ? -19.704 47.985 7.395   1.00 61.47  ? 213 ILE E CD1 1 
ATOM   10150 N N   . VAL E  1 214 ? -16.709 51.948 4.914   1.00 66.89  ? 214 VAL E N   1 
ATOM   10151 C CA  . VAL E  1 214 ? -15.675 53.022 5.002   1.00 66.26  ? 214 VAL E CA  1 
ATOM   10152 C C   . VAL E  1 214 ? -15.788 53.928 3.770   1.00 62.60  ? 214 VAL E C   1 
ATOM   10153 O O   . VAL E  1 214 ? -15.489 55.130 3.894   1.00 66.98  ? 214 VAL E O   1 
ATOM   10154 C CB  . VAL E  1 214 ? -14.263 52.422 5.135   1.00 69.64  ? 214 VAL E CB  1 
ATOM   10155 C CG1 . VAL E  1 214 ? -13.192 53.500 5.181   1.00 73.63  ? 214 VAL E CG1 1 
ATOM   10156 C CG2 . VAL E  1 214 ? -14.154 51.509 6.346   1.00 69.13  ? 214 VAL E CG2 1 
ATOM   10157 N N   . TYR E  1 215 ? -16.204 53.370 2.631   1.00 63.74  ? 215 TYR E N   1 
ATOM   10158 C CA  . TYR E  1 215 ? -16.324 54.081 1.330   1.00 66.70  ? 215 TYR E CA  1 
ATOM   10159 C C   . TYR E  1 215 ? -17.289 55.264 1.469   1.00 68.69  ? 215 TYR E C   1 
ATOM   10160 O O   . TYR E  1 215 ? -17.083 56.280 0.780   1.00 75.20  ? 215 TYR E O   1 
ATOM   10161 C CB  . TYR E  1 215 ? -16.806 53.126 0.236   1.00 65.61  ? 215 TYR E CB  1 
ATOM   10162 C CG  . TYR E  1 215 ? -17.088 53.778 -1.095  1.00 66.03  ? 215 TYR E CG  1 
ATOM   10163 C CD1 . TYR E  1 215 ? -18.245 54.512 -1.303  1.00 68.14  ? 215 TYR E CD1 1 
ATOM   10164 C CD2 . TYR E  1 215 ? -16.205 53.651 -2.153  1.00 72.59  ? 215 TYR E CD2 1 
ATOM   10165 C CE1 . TYR E  1 215 ? -18.512 55.109 -2.524  1.00 73.97  ? 215 TYR E CE1 1 
ATOM   10166 C CE2 . TYR E  1 215 ? -16.457 54.240 -3.381  1.00 74.56  ? 215 TYR E CE2 1 
ATOM   10167 C CZ  . TYR E  1 215 ? -17.615 54.972 -3.569  1.00 73.04  ? 215 TYR E CZ  1 
ATOM   10168 O OH  . TYR E  1 215 ? -17.871 55.555 -4.776  1.00 67.31  ? 215 TYR E OH  1 
ATOM   10169 N N   . PHE E  1 216 ? -18.299 55.128 2.337   1.00 68.48  ? 216 PHE E N   1 
ATOM   10170 C CA  . PHE E  1 216 ? -19.481 56.028 2.422   1.00 64.56  ? 216 PHE E CA  1 
ATOM   10171 C C   . PHE E  1 216 ? -19.308 57.074 3.530   1.00 61.44  ? 216 PHE E C   1 
ATOM   10172 O O   . PHE E  1 216 ? -20.106 58.027 3.568   1.00 76.24  ? 216 PHE E O   1 
ATOM   10173 C CB  . PHE E  1 216 ? -20.754 55.211 2.654   1.00 64.49  ? 216 PHE E CB  1 
ATOM   10174 C CG  . PHE E  1 216 ? -21.312 54.566 1.413   1.00 64.71  ? 216 PHE E CG  1 
ATOM   10175 C CD1 . PHE E  1 216 ? -21.760 55.340 0.355   1.00 67.27  ? 216 PHE E CD1 1 
ATOM   10176 C CD2 . PHE E  1 216 ? -21.393 53.187 1.301   1.00 59.35  ? 216 PHE E CD2 1 
ATOM   10177 C CE1 . PHE E  1 216 ? -22.275 54.750 -0.788  1.00 65.81  ? 216 PHE E CE1 1 
ATOM   10178 C CE2 . PHE E  1 216 ? -21.907 52.599 0.157   1.00 62.65  ? 216 PHE E CE2 1 
ATOM   10179 C CZ  . PHE E  1 216 ? -22.347 53.381 -0.885  1.00 64.77  ? 216 PHE E CZ  1 
ATOM   10180 N N   . LEU E  1 217 ? -18.311 56.908 4.402   1.00 55.92  ? 217 LEU E N   1 
ATOM   10181 C CA  . LEU E  1 217 ? -18.059 57.822 5.551   1.00 55.76  ? 217 LEU E CA  1 
ATOM   10182 C C   . LEU E  1 217 ? -17.876 59.254 5.049   1.00 57.43  ? 217 LEU E C   1 
ATOM   10183 O O   . LEU E  1 217 ? -18.304 60.200 5.705   1.00 50.43  ? 217 LEU E O   1 
ATOM   10184 C CB  . LEU E  1 217 ? -16.830 57.335 6.323   1.00 60.23  ? 217 LEU E CB  1 
ATOM   10185 C CG  . LEU E  1 217 ? -16.979 55.979 7.013   1.00 60.87  ? 217 LEU E CG  1 
ATOM   10186 C CD1 . LEU E  1 217 ? -15.786 55.698 7.913   1.00 60.37  ? 217 LEU E CD1 1 
ATOM   10187 C CD2 . LEU E  1 217 ? -18.273 55.910 7.809   1.00 63.04  ? 217 LEU E CD2 1 
ATOM   10188 N N   . PRO E  1 218 ? -17.226 59.470 3.881   1.00 73.58  ? 218 PRO E N   1 
ATOM   10189 C CA  . PRO E  1 218 ? -17.066 60.815 3.320   1.00 82.92  ? 218 PRO E CA  1 
ATOM   10190 C C   . PRO E  1 218 ? -18.382 61.588 3.131   1.00 79.95  ? 218 PRO E C   1 
ATOM   10191 O O   . PRO E  1 218 ? -18.323 62.785 2.890   1.00 75.45  ? 218 PRO E O   1 
ATOM   10192 C CB  . PRO E  1 218 ? -16.415 60.556 1.951   1.00 81.19  ? 218 PRO E CB  1 
ATOM   10193 C CG  . PRO E  1 218 ? -15.683 59.245 2.133   1.00 78.87  ? 218 PRO E CG  1 
ATOM   10194 C CD  . PRO E  1 218 ? -16.569 58.440 3.062   1.00 81.73  ? 218 PRO E CD  1 
ATOM   10195 N N   . LEU E  1 219 ? -19.526 60.902 3.240   1.00 72.61  ? 219 LEU E N   1 
ATOM   10196 C CA  . LEU E  1 219 ? -20.879 61.496 3.056   1.00 70.08  ? 219 LEU E CA  1 
ATOM   10197 C C   . LEU E  1 219 ? -21.311 62.206 4.343   1.00 68.44  ? 219 LEU E C   1 
ATOM   10198 O O   . LEU E  1 219 ? -22.070 63.188 4.242   1.00 70.43  ? 219 LEU E O   1 
ATOM   10199 C CB  . LEU E  1 219 ? -21.874 60.398 2.667   1.00 61.26  ? 219 LEU E CB  1 
ATOM   10200 C CG  . LEU E  1 219 ? -21.761 59.893 1.228   1.00 59.50  ? 219 LEU E CG  1 
ATOM   10201 C CD1 . LEU E  1 219 ? -22.782 58.801 0.951   1.00 59.53  ? 219 LEU E CD1 1 
ATOM   10202 C CD2 . LEU E  1 219 ? -21.919 61.034 0.234   1.00 55.25  ? 219 LEU E CD2 1 
ATOM   10203 N N   . PHE E  1 220 ? -20.843 61.730 5.502   1.00 70.29  ? 220 PHE E N   1 
ATOM   10204 C CA  . PHE E  1 220 ? -21.187 62.277 6.842   1.00 76.92  ? 220 PHE E CA  1 
ATOM   10205 C C   . PHE E  1 220 ? -20.259 63.454 7.171   1.00 76.42  ? 220 PHE E C   1 
ATOM   10206 O O   . PHE E  1 220 ? -20.178 63.837 8.355   1.00 79.42  ? 220 PHE E O   1 
ATOM   10207 C CB  . PHE E  1 220 ? -21.126 61.182 7.912   1.00 82.93  ? 220 PHE E CB  1 
ATOM   10208 C CG  . PHE E  1 220 ? -21.897 59.930 7.573   1.00 100.87 ? 220 PHE E CG  1 
ATOM   10209 C CD1 . PHE E  1 220 ? -21.449 58.686 7.988   1.00 101.22 ? 220 PHE E CD1 1 
ATOM   10210 C CD2 . PHE E  1 220 ? -23.053 59.993 6.809   1.00 108.38 ? 220 PHE E CD2 1 
ATOM   10211 C CE1 . PHE E  1 220 ? -22.151 57.536 7.665   1.00 107.87 ? 220 PHE E CE1 1 
ATOM   10212 C CE2 . PHE E  1 220 ? -23.753 58.841 6.484   1.00 102.65 ? 220 PHE E CE2 1 
ATOM   10213 C CZ  . PHE E  1 220 ? -23.301 57.615 6.913   1.00 109.11 ? 220 PHE E CZ  1 
ATOM   10214 N N   . GLY E  1 221 ? -19.593 64.010 6.153   1.00 72.06  ? 221 GLY E N   1 
ATOM   10215 C CA  . GLY E  1 221 ? -18.761 65.225 6.269   1.00 72.83  ? 221 GLY E CA  1 
ATOM   10216 C C   . GLY E  1 221 ? -17.288 64.944 6.020   1.00 73.03  ? 221 GLY E C   1 
ATOM   10217 O O   . GLY E  1 221 ? -16.976 63.861 5.485   1.00 80.23  ? 221 GLY E O   1 
ATOM   10218 N N   . ALA E  1 222 ? -16.418 65.892 6.390   1.00 68.71  ? 222 ALA E N   1 
ATOM   10219 C CA  . ALA E  1 222 ? -14.945 65.823 6.235   1.00 63.59  ? 222 ALA E CA  1 
ATOM   10220 C C   . ALA E  1 222 ? -14.268 66.416 7.476   1.00 58.49  ? 222 ALA E C   1 
ATOM   10221 O O   . ALA E  1 222 ? -14.804 67.386 8.040   1.00 61.78  ? 222 ALA E O   1 
ATOM   10222 C CB  . ALA E  1 222 ? -14.520 66.549 4.982   1.00 65.07  ? 222 ALA E CB  1 
ATOM   10223 N N   . SER E  1 223 ? -13.123 65.855 7.871   1.00 65.30  ? 223 SER E N   1 
ATOM   10224 C CA  . SER E  1 223 ? -12.383 66.212 9.109   1.00 70.02  ? 223 SER E CA  1 
ATOM   10225 C C   . SER E  1 223 ? -11.071 65.427 9.173   1.00 75.08  ? 223 SER E C   1 
ATOM   10226 O O   . SER E  1 223 ? -11.056 64.263 8.719   1.00 91.30  ? 223 SER E O   1 
ATOM   10227 C CB  . SER E  1 223 ? -13.230 65.950 10.328  1.00 72.92  ? 223 SER E CB  1 
ATOM   10228 O OG  . SER E  1 223 ? -12.438 65.941 11.507  1.00 81.04  ? 223 SER E OG  1 
ATOM   10229 N N   . GLY E  1 224 ? -10.017 66.045 9.715   1.00 69.65  ? 224 GLY E N   1 
ATOM   10230 C CA  . GLY E  1 224 ? -8.732  65.378 9.996   1.00 63.57  ? 224 GLY E CA  1 
ATOM   10231 C C   . GLY E  1 224 ? -8.959  64.045 10.688  1.00 60.16  ? 224 GLY E C   1 
ATOM   10232 O O   . GLY E  1 224 ? -8.361  63.039 10.252  1.00 67.39  ? 224 GLY E O   1 
ATOM   10233 N N   . GLY E  1 225 ? -9.813  64.040 11.716  1.00 58.44  ? 225 GLY E N   1 
ATOM   10234 C CA  . GLY E  1 225 ? -10.167 62.848 12.511  1.00 59.34  ? 225 GLY E CA  1 
ATOM   10235 C C   . GLY E  1 225 ? -10.806 61.767 11.656  1.00 56.11  ? 225 GLY E C   1 
ATOM   10236 O O   . GLY E  1 225 ? -10.404 60.592 11.790  1.00 51.61  ? 225 GLY E O   1 
ATOM   10237 N N   . LEU E  1 226 ? -11.775 62.140 10.813  1.00 49.60  ? 226 LEU E N   1 
ATOM   10238 C CA  . LEU E  1 226 ? -12.482 61.203 9.900   1.00 53.16  ? 226 LEU E CA  1 
ATOM   10239 C C   . LEU E  1 226 ? -11.465 60.612 8.919   1.00 56.51  ? 226 LEU E C   1 
ATOM   10240 O O   . LEU E  1 226 ? -11.349 59.371 8.865   1.00 65.99  ? 226 LEU E O   1 
ATOM   10241 C CB  . LEU E  1 226 ? -13.601 61.945 9.162   1.00 53.57  ? 226 LEU E CB  1 
ATOM   10242 C CG  . LEU E  1 226 ? -14.450 61.082 8.227   1.00 51.95  ? 226 LEU E CG  1 
ATOM   10243 C CD1 . LEU E  1 226 ? -15.086 59.925 8.981   1.00 48.49  ? 226 LEU E CD1 1 
ATOM   10244 C CD2 . LEU E  1 226 ? -15.516 61.913 7.529   1.00 52.22  ? 226 LEU E CD2 1 
ATOM   10245 N N   . THR E  1 227 ? -10.756 61.476 8.185   1.00 53.44  ? 227 THR E N   1 
ATOM   10246 C CA  . THR E  1 227 ? -9.720  61.097 7.187   1.00 51.80  ? 227 THR E CA  1 
ATOM   10247 C C   . THR E  1 227 ? -8.750  60.099 7.828   1.00 52.03  ? 227 THR E C   1 
ATOM   10248 O O   . THR E  1 227 ? -8.485  59.056 7.199   1.00 56.30  ? 227 THR E O   1 
ATOM   10249 C CB  . THR E  1 227 ? -8.999  62.336 6.643   1.00 51.25  ? 227 THR E CB  1 
ATOM   10250 O OG1 . THR E  1 227 ? -9.967  63.124 5.950   1.00 58.24  ? 227 THR E OG1 1 
ATOM   10251 C CG2 . THR E  1 227 ? -7.854  61.997 5.714   1.00 50.23  ? 227 THR E CG2 1 
ATOM   10252 N N   . THR E  1 228 ? -8.253  60.404 9.031   1.00 44.99  ? 228 THR E N   1 
ATOM   10253 C CA  . THR E  1 228 ? -7.346  59.524 9.816   1.00 41.95  ? 228 THR E CA  1 
ATOM   10254 C C   . THR E  1 228 ? -8.018  58.162 10.021  1.00 45.63  ? 228 THR E C   1 
ATOM   10255 O O   . THR E  1 228 ? -7.362  57.135 9.758   1.00 50.25  ? 228 THR E O   1 
ATOM   10256 C CB  . THR E  1 228 ? -6.966  60.157 11.159  1.00 40.51  ? 228 THR E CB  1 
ATOM   10257 O OG1 . THR E  1 228 ? -6.259  61.369 10.896  1.00 38.21  ? 228 THR E OG1 1 
ATOM   10258 C CG2 . THR E  1 228 ? -6.112  59.247 12.015  1.00 41.52  ? 228 THR E CG2 1 
ATOM   10259 N N   . THR E  1 229 ? -9.276  58.164 10.473  1.00 49.38  ? 229 THR E N   1 
ATOM   10260 C CA  . THR E  1 229 ? -10.096 56.946 10.718  1.00 50.46  ? 229 THR E CA  1 
ATOM   10261 C C   . THR E  1 229 ? -10.166 56.112 9.435   1.00 47.71  ? 229 THR E C   1 
ATOM   10262 O O   . THR E  1 229 ? -9.825  54.914 9.485   1.00 52.47  ? 229 THR E O   1 
ATOM   10263 C CB  . THR E  1 229 ? -11.504 57.311 11.205  1.00 48.93  ? 229 THR E CB  1 
ATOM   10264 O OG1 . THR E  1 229 ? -11.373 58.112 12.379  1.00 47.45  ? 229 THR E OG1 1 
ATOM   10265 C CG2 . THR E  1 229 ? -12.349 56.093 11.505  1.00 46.87  ? 229 THR E CG2 1 
ATOM   10266 N N   . ILE E  1 230 ? -10.597 56.732 8.335   1.00 46.29  ? 230 ILE E N   1 
ATOM   10267 C CA  . ILE E  1 230 ? -10.727 56.089 6.994   1.00 54.47  ? 230 ILE E CA  1 
ATOM   10268 C C   . ILE E  1 230 ? -9.408  55.386 6.652   1.00 56.32  ? 230 ILE E C   1 
ATOM   10269 O O   . ILE E  1 230 ? -9.445  54.179 6.344   1.00 66.46  ? 230 ILE E O   1 
ATOM   10270 C CB  . ILE E  1 230 ? -11.120 57.131 5.928   1.00 62.79  ? 230 ILE E CB  1 
ATOM   10271 C CG1 . ILE E  1 230 ? -12.565 57.605 6.112   1.00 66.21  ? 230 ILE E CG1 1 
ATOM   10272 C CG2 . ILE E  1 230 ? -10.877 56.591 4.527   1.00 64.41  ? 230 ILE E CG2 1 
ATOM   10273 C CD1 . ILE E  1 230 ? -12.910 58.851 5.325   1.00 67.92  ? 230 ILE E CD1 1 
ATOM   10274 N N   . LEU E  1 231 ? -8.290  56.115 6.718   1.00 50.03  ? 231 LEU E N   1 
ATOM   10275 C CA  . LEU E  1 231 ? -6.942  55.620 6.329   1.00 48.19  ? 231 LEU E CA  1 
ATOM   10276 C C   . LEU E  1 231 ? -6.542  54.440 7.222   1.00 48.89  ? 231 LEU E C   1 
ATOM   10277 O O   . LEU E  1 231 ? -6.174  53.386 6.667   1.00 50.85  ? 231 LEU E O   1 
ATOM   10278 C CB  . LEU E  1 231 ? -5.929  56.765 6.438   1.00 44.58  ? 231 LEU E CB  1 
ATOM   10279 C CG  . LEU E  1 231 ? -6.058  57.857 5.378   1.00 43.29  ? 231 LEU E CG  1 
ATOM   10280 C CD1 . LEU E  1 231 ? -4.937  58.873 5.505   1.00 41.11  ? 231 LEU E CD1 1 
ATOM   10281 C CD2 . LEU E  1 231 ? -6.073  57.260 3.980   1.00 44.52  ? 231 LEU E CD2 1 
ATOM   10282 N N   . ILE E  1 232 ? -6.611  54.614 8.547   1.00 47.82  ? 232 ILE E N   1 
ATOM   10283 C CA  . ILE E  1 232 ? -6.124  53.621 9.552   1.00 48.44  ? 232 ILE E CA  1 
ATOM   10284 C C   . ILE E  1 232 ? -6.985  52.357 9.474   1.00 48.49  ? 232 ILE E C   1 
ATOM   10285 O O   . ILE E  1 232 ? -6.407  51.255 9.456   1.00 50.09  ? 232 ILE E O   1 
ATOM   10286 C CB  . ILE E  1 232 ? -6.120  54.217 10.973  1.00 48.59  ? 232 ILE E CB  1 
ATOM   10287 C CG1 . ILE E  1 232 ? -5.117  55.367 11.094  1.00 49.37  ? 232 ILE E CG1 1 
ATOM   10288 C CG2 . ILE E  1 232 ? -5.865  53.130 12.007  1.00 47.46  ? 232 ILE E CG2 1 
ATOM   10289 C CD1 . ILE E  1 232 ? -4.939  55.887 12.502  1.00 53.53  ? 232 ILE E CD1 1 
ATOM   10290 N N   . THR E  1 233 ? -8.310  52.512 9.440   1.00 51.90  ? 233 THR E N   1 
ATOM   10291 C CA  . THR E  1 233 ? -9.283  51.388 9.394   1.00 55.15  ? 233 THR E CA  1 
ATOM   10292 C C   . THR E  1 233 ? -8.954  50.486 8.199   1.00 52.70  ? 233 THR E C   1 
ATOM   10293 O O   . THR E  1 233 ? -8.796  49.268 8.407   1.00 52.95  ? 233 THR E O   1 
ATOM   10294 C CB  . THR E  1 233 ? -10.727 51.901 9.338   1.00 56.81  ? 233 THR E CB  1 
ATOM   10295 O OG1 . THR E  1 233 ? -10.985 52.627 10.540  1.00 59.08  ? 233 THR E OG1 1 
ATOM   10296 C CG2 . THR E  1 233 ? -11.735 50.784 9.193   1.00 59.65  ? 233 THR E CG2 1 
ATOM   10297 N N   . LEU E  1 234 ? -8.844  51.073 7.004   1.00 50.71  ? 234 LEU E N   1 
ATOM   10298 C CA  . LEU E  1 234 ? -8.550  50.355 5.733   1.00 54.95  ? 234 LEU E CA  1 
ATOM   10299 C C   . LEU E  1 234 ? -7.223  49.596 5.862   1.00 53.34  ? 234 LEU E C   1 
ATOM   10300 O O   . LEU E  1 234 ? -7.135  48.466 5.340   1.00 53.99  ? 234 LEU E O   1 
ATOM   10301 C CB  . LEU E  1 234 ? -8.497  51.365 4.583   1.00 57.73  ? 234 LEU E CB  1 
ATOM   10302 C CG  . LEU E  1 234 ? -9.842  51.962 4.168   1.00 55.26  ? 234 LEU E CG  1 
ATOM   10303 C CD1 . LEU E  1 234 ? -9.660  52.995 3.066   1.00 52.21  ? 234 LEU E CD1 1 
ATOM   10304 C CD2 . LEU E  1 234 ? -10.809 50.874 3.724   1.00 52.27  ? 234 LEU E CD2 1 
ATOM   10305 N N   . THR E  1 235 ? -6.229  50.196 6.522   1.00 47.44  ? 235 THR E N   1 
ATOM   10306 C CA  . THR E  1 235 ? -4.893  49.587 6.759   1.00 46.71  ? 235 THR E CA  1 
ATOM   10307 C C   . THR E  1 235 ? -5.054  48.357 7.660   1.00 41.59  ? 235 THR E C   1 
ATOM   10308 O O   . THR E  1 235 ? -4.596  47.271 7.260   1.00 42.98  ? 235 THR E O   1 
ATOM   10309 C CB  . THR E  1 235 ? -3.912  50.605 7.352   1.00 49.02  ? 235 THR E CB  1 
ATOM   10310 O OG1 . THR E  1 235 ? -3.856  51.719 6.461   1.00 48.51  ? 235 THR E OG1 1 
ATOM   10311 C CG2 . THR E  1 235 ? -2.524  50.037 7.552   1.00 50.43  ? 235 THR E CG2 1 
ATOM   10312 N N   . VAL E  1 236 ? -5.686  48.528 8.823   1.00 39.19  ? 236 VAL E N   1 
ATOM   10313 C CA  . VAL E  1 236 ? -5.962  47.434 9.801   1.00 42.63  ? 236 VAL E CA  1 
ATOM   10314 C C   . VAL E  1 236 ? -6.751  46.334 9.083   1.00 41.35  ? 236 VAL E C   1 
ATOM   10315 O O   . VAL E  1 236 ? -6.413  45.148 9.262   1.00 44.89  ? 236 VAL E O   1 
ATOM   10316 C CB  . VAL E  1 236 ? -6.716  47.962 11.037  1.00 45.99  ? 236 VAL E CB  1 
ATOM   10317 C CG1 . VAL E  1 236 ? -7.229  46.830 11.915  1.00 48.28  ? 236 VAL E CG1 1 
ATOM   10318 C CG2 . VAL E  1 236 ? -5.859  48.927 11.844  1.00 44.74  ? 236 VAL E CG2 1 
ATOM   10319 N N   . ALA E  1 237 ? -7.756  46.724 8.294   1.00 41.62  ? 237 ALA E N   1 
ATOM   10320 C CA  . ALA E  1 237 ? -8.601  45.820 7.481   1.00 41.17  ? 237 ALA E CA  1 
ATOM   10321 C C   . ALA E  1 237 ? -7.709  45.000 6.542   1.00 46.09  ? 237 ALA E C   1 
ATOM   10322 O O   . ALA E  1 237 ? -7.728  43.757 6.642   1.00 57.82  ? 237 ALA E O   1 
ATOM   10323 C CB  . ALA E  1 237 ? -9.621  46.623 6.713   1.00 40.09  ? 237 ALA E CB  1 
ATOM   10324 N N   . ASP E  1 238 ? -6.953  45.681 5.674   1.00 49.30  ? 238 ASP E N   1 
ATOM   10325 C CA  . ASP E  1 238 ? -6.019  45.060 4.696   1.00 47.16  ? 238 ASP E CA  1 
ATOM   10326 C C   . ASP E  1 238 ? -5.165  44.007 5.409   1.00 44.32  ? 238 ASP E C   1 
ATOM   10327 O O   . ASP E  1 238 ? -5.176  42.842 4.968   1.00 45.23  ? 238 ASP E O   1 
ATOM   10328 C CB  . ASP E  1 238 ? -5.137  46.113 4.020   1.00 48.27  ? 238 ASP E CB  1 
ATOM   10329 C CG  . ASP E  1 238 ? -5.800  46.796 2.837   1.00 52.00  ? 238 ASP E CG  1 
ATOM   10330 O OD1 . ASP E  1 238 ? -5.177  47.711 2.262   1.00 50.07  ? 238 ASP E OD1 1 
ATOM   10331 O OD2 . ASP E  1 238 ? -6.932  46.402 2.495   1.00 61.84  ? 238 ASP E OD2 1 
ATOM   10332 N N   . VAL E  1 239 ? -4.460  44.411 6.470   1.00 42.64  ? 239 VAL E N   1 
ATOM   10333 C CA  . VAL E  1 239 ? -3.476  43.562 7.204   1.00 43.80  ? 239 VAL E CA  1 
ATOM   10334 C C   . VAL E  1 239 ? -4.190  42.322 7.752   1.00 43.82  ? 239 VAL E C   1 
ATOM   10335 O O   . VAL E  1 239 ? -3.750  41.199 7.426   1.00 45.34  ? 239 VAL E O   1 
ATOM   10336 C CB  . VAL E  1 239 ? -2.775  44.349 8.329   1.00 42.14  ? 239 VAL E CB  1 
ATOM   10337 C CG1 . VAL E  1 239 ? -2.016  43.431 9.274   1.00 41.51  ? 239 VAL E CG1 1 
ATOM   10338 C CG2 . VAL E  1 239 ? -1.853  45.419 7.768   1.00 42.84  ? 239 VAL E CG2 1 
ATOM   10339 N N   . ILE E  1 240 ? -5.247  42.522 8.545   1.00 44.01  ? 240 ILE E N   1 
ATOM   10340 C CA  . ILE E  1 240 ? -5.981  41.433 9.257   1.00 49.10  ? 240 ILE E CA  1 
ATOM   10341 C C   . ILE E  1 240 ? -6.513  40.425 8.232   1.00 54.47  ? 240 ILE E C   1 
ATOM   10342 O O   . ILE E  1 240 ? -6.233  39.218 8.386   1.00 59.45  ? 240 ILE E O   1 
ATOM   10343 C CB  . ILE E  1 240 ? -7.111  42.007 10.132  1.00 47.34  ? 240 ILE E CB  1 
ATOM   10344 C CG1 . ILE E  1 240 ? -6.557  42.740 11.356  1.00 50.59  ? 240 ILE E CG1 1 
ATOM   10345 C CG2 . ILE E  1 240 ? -8.085  40.910 10.528  1.00 48.66  ? 240 ILE E CG2 1 
ATOM   10346 C CD1 . ILE E  1 240 ? -7.616  43.379 12.222  1.00 54.64  ? 240 ILE E CD1 1 
ATOM   10347 N N   . VAL E  1 241 ? -7.248  40.906 7.226   1.00 54.11  ? 241 VAL E N   1 
ATOM   10348 C CA  . VAL E  1 241 ? -7.900  40.058 6.184   1.00 54.06  ? 241 VAL E CA  1 
ATOM   10349 C C   . VAL E  1 241 ? -6.829  39.246 5.465   1.00 53.26  ? 241 VAL E C   1 
ATOM   10350 O O   . VAL E  1 241 ? -6.925  38.024 5.382   1.00 54.02  ? 241 VAL E O   1 
ATOM   10351 C CB  . VAL E  1 241 ? -8.713  40.909 5.189   1.00 57.31  ? 241 VAL E CB  1 
ATOM   10352 C CG1 . VAL E  1 241 ? -9.163  40.090 3.988   1.00 57.29  ? 241 VAL E CG1 1 
ATOM   10353 C CG2 . VAL E  1 241 ? -9.902  41.578 5.861   1.00 57.06  ? 241 VAL E CG2 1 
ATOM   10354 N N   . LYS E  1 242 ? -5.810  39.944 4.956   1.00 55.96  ? 242 LYS E N   1 
ATOM   10355 C CA  . LYS E  1 242 ? -4.860  39.354 4.028   1.00 57.67  ? 242 LYS E CA  1 
ATOM   10356 C C   . LYS E  1 242 ? -4.036  38.275 4.724   1.00 54.18  ? 242 LYS E C   1 
ATOM   10357 O O   . LYS E  1 242 ? -3.880  37.179 4.187   1.00 54.39  ? 242 LYS E O   1 
ATOM   10358 C CB  . LYS E  1 242 ? -3.949  40.429 3.431   1.00 58.84  ? 242 LYS E CB  1 
ATOM   10359 C CG  . LYS E  1 242 ? -4.609  41.322 2.391   1.00 59.04  ? 242 LYS E CG  1 
ATOM   10360 C CD  . LYS E  1 242 ? -3.674  42.356 1.804   1.00 65.61  ? 242 LYS E CD  1 
ATOM   10361 C CE  . LYS E  1 242 ? -4.399  43.469 1.062   1.00 68.69  ? 242 LYS E CE  1 
ATOM   10362 N NZ  . LYS E  1 242 ? -5.531  42.962 0.279   1.00 70.60  ? 242 LYS E NZ  1 
ATOM   10363 N N   . LEU E  1 243 ? -3.484  38.580 5.901   1.00 54.07  ? 243 LEU E N   1 
ATOM   10364 C CA  . LEU E  1 243 ? -2.623  37.590 6.527   1.00 57.25  ? 243 LEU E CA  1 
ATOM   10365 C C   . LEU E  1 243 ? -3.448  36.711 7.474   1.00 55.59  ? 243 LEU E C   1 
ATOM   10366 O O   . LEU E  1 243 ? -3.070  35.542 7.618   1.00 62.51  ? 243 LEU E O   1 
ATOM   10367 C CB  . LEU E  1 243 ? -1.392  38.221 7.192   1.00 54.48  ? 243 LEU E CB  1 
ATOM   10368 C CG  . LEU E  1 243 ? -1.600  39.493 8.004   1.00 61.53  ? 243 LEU E CG  1 
ATOM   10369 C CD1 . LEU E  1 243 ? -2.297  39.188 9.320   1.00 67.15  ? 243 LEU E CD1 1 
ATOM   10370 C CD2 . LEU E  1 243 ? -0.261  40.179 8.243   1.00 61.28  ? 243 LEU E CD2 1 
ATOM   10371 N N   . GLY E  1 244 ? -4.562  37.201 8.027   1.00 53.94  ? 244 GLY E N   1 
ATOM   10372 C CA  . GLY E  1 244 ? -5.531  36.350 8.749   1.00 53.23  ? 244 GLY E CA  1 
ATOM   10373 C C   . GLY E  1 244 ? -6.029  35.220 7.859   1.00 52.32  ? 244 GLY E C   1 
ATOM   10374 O O   . GLY E  1 244 ? -5.809  34.040 8.203   1.00 59.33  ? 244 GLY E O   1 
ATOM   10375 N N   . PHE E  1 245 ? -6.659  35.574 6.737   1.00 47.85  ? 245 PHE E N   1 
ATOM   10376 C CA  . PHE E  1 245 ? -7.184  34.639 5.709   1.00 50.58  ? 245 PHE E CA  1 
ATOM   10377 C C   . PHE E  1 245 ? -6.054  33.731 5.205   1.00 57.73  ? 245 PHE E C   1 
ATOM   10378 O O   . PHE E  1 245 ? -6.213  32.499 5.235   1.00 68.78  ? 245 PHE E O   1 
ATOM   10379 C CB  . PHE E  1 245 ? -7.823  35.426 4.562   1.00 51.65  ? 245 PHE E CB  1 
ATOM   10380 C CG  . PHE E  1 245 ? -8.030  34.648 3.288   1.00 55.53  ? 245 PHE E CG  1 
ATOM   10381 C CD1 . PHE E  1 245 ? -7.152  34.788 2.224   1.00 55.91  ? 245 PHE E CD1 1 
ATOM   10382 C CD2 . PHE E  1 245 ? -9.104  33.784 3.147   1.00 56.90  ? 245 PHE E CD2 1 
ATOM   10383 C CE1 . PHE E  1 245 ? -7.342  34.078 1.048   1.00 59.64  ? 245 PHE E CE1 1 
ATOM   10384 C CE2 . PHE E  1 245 ? -9.294  33.076 1.970   1.00 62.62  ? 245 PHE E CE2 1 
ATOM   10385 C CZ  . PHE E  1 245 ? -8.413  33.224 0.922   1.00 63.51  ? 245 PHE E CZ  1 
ATOM   10386 N N   . SER E  1 246 ? -4.951  34.326 4.746   1.00 62.50  ? 246 SER E N   1 
ATOM   10387 C CA  . SER E  1 246 ? -3.799  33.619 4.125   1.00 62.68  ? 246 SER E CA  1 
ATOM   10388 C C   . SER E  1 246 ? -3.322  32.481 5.037   1.00 60.56  ? 246 SER E C   1 
ATOM   10389 O O   . SER E  1 246 ? -3.166  31.354 4.532   1.00 66.38  ? 246 SER E O   1 
ATOM   10390 C CB  . SER E  1 246 ? -2.681  34.575 3.796   1.00 65.29  ? 246 SER E CB  1 
ATOM   10391 O OG  . SER E  1 246 ? -2.010  34.997 4.973   1.00 75.69  ? 246 SER E OG  1 
ATOM   10392 N N   . THR E  1 247 ? -3.099  32.760 6.326   1.00 58.09  ? 247 THR E N   1 
ATOM   10393 C CA  . THR E  1 247 ? -2.652  31.762 7.337   1.00 61.31  ? 247 THR E CA  1 
ATOM   10394 C C   . THR E  1 247 ? -3.602  30.561 7.318   1.00 62.56  ? 247 THR E C   1 
ATOM   10395 O O   . THR E  1 247 ? -3.116  29.421 7.453   1.00 70.44  ? 247 THR E O   1 
ATOM   10396 C CB  . THR E  1 247 ? -2.581  32.360 8.748   1.00 54.13  ? 247 THR E CB  1 
ATOM   10397 O OG1 . THR E  1 247 ? -1.742  33.513 8.695   1.00 62.25  ? 247 THR E OG1 1 
ATOM   10398 C CG2 . THR E  1 247 ? -2.043  31.389 9.776   1.00 55.14  ? 247 THR E CG2 1 
ATOM   10399 N N   . GLN E  1 248 ? -4.903  30.818 7.153   1.00 64.25  ? 248 GLN E N   1 
ATOM   10400 C CA  . GLN E  1 248 ? -5.978  29.791 7.197   1.00 65.05  ? 248 GLN E CA  1 
ATOM   10401 C C   . GLN E  1 248 ? -5.866  28.873 5.974   1.00 62.10  ? 248 GLN E C   1 
ATOM   10402 O O   . GLN E  1 248 ? -5.769  27.648 6.175   1.00 66.23  ? 248 GLN E O   1 
ATOM   10403 C CB  . GLN E  1 248 ? -7.350  30.464 7.279   1.00 66.31  ? 248 GLN E CB  1 
ATOM   10404 C CG  . GLN E  1 248 ? -7.590  31.174 8.604   1.00 64.47  ? 248 GLN E CG  1 
ATOM   10405 C CD  . GLN E  1 248 ? -7.708  30.204 9.753   1.00 64.59  ? 248 GLN E CD  1 
ATOM   10406 O OE1 . GLN E  1 248 ? -8.553  29.311 9.750   1.00 75.28  ? 248 GLN E OE1 1 
ATOM   10407 N NE2 . GLN E  1 248 ? -6.859  30.376 10.753  1.00 68.96  ? 248 GLN E NE2 1 
ATOM   10408 N N   . THR E  1 249 ? -5.875  29.441 4.764   1.00 60.37  ? 249 THR E N   1 
ATOM   10409 C CA  . THR E  1 249 ? -5.808  28.689 3.481   1.00 62.50  ? 249 THR E CA  1 
ATOM   10410 C C   . THR E  1 249 ? -4.540  27.827 3.461   1.00 62.65  ? 249 THR E C   1 
ATOM   10411 O O   . THR E  1 249 ? -4.583  26.736 2.864   1.00 67.72  ? 249 THR E O   1 
ATOM   10412 C CB  . THR E  1 249 ? -5.866  29.624 2.267   1.00 65.96  ? 249 THR E CB  1 
ATOM   10413 O OG1 . THR E  1 249 ? -4.782  30.547 2.360   1.00 75.19  ? 249 THR E OG1 1 
ATOM   10414 C CG2 . THR E  1 249 ? -7.176  30.374 2.169   1.00 64.41  ? 249 THR E CG2 1 
ATOM   10415 N N   . HIS E  1 250 ? -3.457  28.299 4.085   1.00 64.22  ? 250 HIS E N   1 
ATOM   10416 C CA  . HIS E  1 250 ? -2.189  27.537 4.248   1.00 72.12  ? 250 HIS E CA  1 
ATOM   10417 C C   . HIS E  1 250 ? -2.469  26.281 5.081   1.00 68.71  ? 250 HIS E C   1 
ATOM   10418 O O   . HIS E  1 250 ? -2.227  25.167 4.576   1.00 68.22  ? 250 HIS E O   1 
ATOM   10419 C CB  . HIS E  1 250 ? -1.093  28.411 4.876   1.00 77.71  ? 250 HIS E CB  1 
ATOM   10420 C CG  . HIS E  1 250 ? 0.251   27.759 4.885   1.00 77.52  ? 250 HIS E CG  1 
ATOM   10421 N ND1 . HIS E  1 250 ? 0.911   27.419 3.717   1.00 75.66  ? 250 HIS E ND1 1 
ATOM   10422 C CD2 . HIS E  1 250 ? 1.060   27.386 5.902   1.00 71.19  ? 250 HIS E CD2 1 
ATOM   10423 C CE1 . HIS E  1 250 ? 2.067   26.859 4.016   1.00 74.06  ? 250 HIS E CE1 1 
ATOM   10424 N NE2 . HIS E  1 250 ? 2.185   26.831 5.350   1.00 72.79  ? 250 HIS E NE2 1 
ATOM   10425 N N   . ARG E  1 251 ? -2.973  26.462 6.305   1.00 66.64  ? 251 ARG E N   1 
ATOM   10426 C CA  . ARG E  1 251 ? -3.300  25.355 7.242   1.00 67.50  ? 251 ARG E CA  1 
ATOM   10427 C C   . ARG E  1 251 ? -4.171  24.327 6.510   1.00 63.77  ? 251 ARG E C   1 
ATOM   10428 O O   . ARG E  1 251 ? -3.963  23.123 6.736   1.00 70.87  ? 251 ARG E O   1 
ATOM   10429 C CB  . ARG E  1 251 ? -3.958  25.913 8.507   1.00 77.68  ? 251 ARG E CB  1 
ATOM   10430 C CG  . ARG E  1 251 ? -3.055  26.865 9.280   1.00 102.31 ? 251 ARG E CG  1 
ATOM   10431 C CD  . ARG E  1 251 ? -3.736  27.582 10.432  1.00 109.97 ? 251 ARG E CD  1 
ATOM   10432 N NE  . ARG E  1 251 ? -3.270  27.103 11.725  1.00 117.53 ? 251 ARG E NE  1 
ATOM   10433 C CZ  . ARG E  1 251 ? -3.709  26.003 12.325  1.00 129.25 ? 251 ARG E CZ  1 
ATOM   10434 N NH1 . ARG E  1 251 ? -4.632  25.255 11.746  1.00 129.98 ? 251 ARG E NH1 1 
ATOM   10435 N NH2 . ARG E  1 251 ? -3.220  25.653 13.501  1.00 132.39 ? 251 ARG E NH2 1 
ATOM   10436 N N   . VAL E  1 252 ? -5.082  24.785 5.644   1.00 58.21  ? 252 VAL E N   1 
ATOM   10437 C CA  . VAL E  1 252 ? -5.967  23.918 4.807   1.00 57.85  ? 252 VAL E CA  1 
ATOM   10438 C C   . VAL E  1 252 ? -5.091  23.064 3.883   1.00 61.35  ? 252 VAL E C   1 
ATOM   10439 O O   . VAL E  1 252 ? -5.123  21.827 4.017   1.00 77.37  ? 252 VAL E O   1 
ATOM   10440 C CB  . VAL E  1 252 ? -6.977  24.749 3.990   1.00 57.89  ? 252 VAL E CB  1 
ATOM   10441 C CG1 . VAL E  1 252 ? -7.746  23.892 2.994   1.00 58.05  ? 252 VAL E CG1 1 
ATOM   10442 C CG2 . VAL E  1 252 ? -7.937  25.515 4.883   1.00 59.68  ? 252 VAL E CG2 1 
ATOM   10443 N N   . ALA E  1 253 ? -4.350  23.709 2.976   1.00 62.64  ? 253 ALA E N   1 
ATOM   10444 C CA  . ALA E  1 253 ? -3.494  23.068 1.951   1.00 59.82  ? 253 ALA E CA  1 
ATOM   10445 C C   . ALA E  1 253 ? -2.648  21.962 2.592   1.00 56.33  ? 253 ALA E C   1 
ATOM   10446 O O   . ALA E  1 253 ? -2.521  20.887 1.978   1.00 61.43  ? 253 ALA E O   1 
ATOM   10447 C CB  . ALA E  1 253 ? -2.626  24.106 1.284   1.00 60.46  ? 253 ALA E CB  1 
ATOM   10448 N N   . LYS E  1 254 ? -2.094  22.222 3.780   1.00 53.64  ? 254 LYS E N   1 
ATOM   10449 C CA  . LYS E  1 254 ? -1.227  21.271 4.527   1.00 58.44  ? 254 LYS E CA  1 
ATOM   10450 C C   . LYS E  1 254 ? -2.060  20.058 4.956   1.00 62.76  ? 254 LYS E C   1 
ATOM   10451 O O   . LYS E  1 254 ? -1.613  18.921 4.713   1.00 59.33  ? 254 LYS E O   1 
ATOM   10452 C CB  . LYS E  1 254 ? -0.586  21.964 5.734   1.00 62.48  ? 254 LYS E CB  1 
ATOM   10453 C CG  . LYS E  1 254 ? 0.476   22.999 5.390   1.00 65.58  ? 254 LYS E CG  1 
ATOM   10454 C CD  . LYS E  1 254 ? 1.049   23.710 6.595   1.00 69.00  ? 254 LYS E CD  1 
ATOM   10455 C CE  . LYS E  1 254 ? 1.956   22.833 7.432   1.00 66.54  ? 254 LYS E CE  1 
ATOM   10456 N NZ  . LYS E  1 254 ? 2.406   23.531 8.659   1.00 69.32  ? 254 LYS E NZ  1 
ATOM   10457 N N   . LEU E  1 255 ? -3.221  20.303 5.570   1.00 74.40  ? 255 LEU E N   1 
ATOM   10458 C CA  . LEU E  1 255 ? -4.178  19.257 6.024   1.00 79.73  ? 255 LEU E CA  1 
ATOM   10459 C C   . LEU E  1 255 ? -4.545  18.369 4.829   1.00 69.49  ? 255 LEU E C   1 
ATOM   10460 O O   . LEU E  1 255 ? -4.411  17.136 4.944   1.00 71.86  ? 255 LEU E O   1 
ATOM   10461 C CB  . LEU E  1 255 ? -5.416  19.946 6.610   1.00 83.06  ? 255 LEU E CB  1 
ATOM   10462 C CG  . LEU E  1 255 ? -6.145  19.202 7.728   1.00 93.06  ? 255 LEU E CG  1 
ATOM   10463 C CD1 . LEU E  1 255 ? -5.186  18.355 8.554   1.00 101.88 ? 255 LEU E CD1 1 
ATOM   10464 C CD2 . LEU E  1 255 ? -6.896  20.183 8.618   1.00 88.78  ? 255 LEU E CD2 1 
ATOM   10465 N N   . ARG E  1 256 ? -4.978  18.986 3.727   1.00 59.49  ? 256 ARG E N   1 
ATOM   10466 C CA  . ARG E  1 256 ? -5.397  18.295 2.479   1.00 61.45  ? 256 ARG E CA  1 
ATOM   10467 C C   . ARG E  1 256 ? -4.207  17.516 1.904   1.00 61.56  ? 256 ARG E C   1 
ATOM   10468 O O   . ARG E  1 256 ? -4.427  16.402 1.393   1.00 67.98  ? 256 ARG E O   1 
ATOM   10469 C CB  . ARG E  1 256 ? -5.950  19.316 1.480   1.00 63.01  ? 256 ARG E CB  1 
ATOM   10470 C CG  . ARG E  1 256 ? -7.339  19.828 1.832   1.00 68.04  ? 256 ARG E CG  1 
ATOM   10471 C CD  . ARG E  1 256 ? -8.420  19.236 0.946   1.00 72.42  ? 256 ARG E CD  1 
ATOM   10472 N NE  . ARG E  1 256 ? -8.729  20.100 -0.187  1.00 76.11  ? 256 ARG E NE  1 
ATOM   10473 C CZ  . ARG E  1 256 ? -9.355  19.705 -1.291  1.00 76.96  ? 256 ARG E CZ  1 
ATOM   10474 N NH1 . ARG E  1 256 ? -9.741  18.447 -1.421  1.00 77.74  ? 256 ARG E NH1 1 
ATOM   10475 N NH2 . ARG E  1 256 ? -9.595  20.567 -2.264  1.00 82.15  ? 256 ARG E NH2 1 
ATOM   10476 N N   . THR E  1 257 ? -2.998  18.081 1.984   1.00 61.17  ? 257 THR E N   1 
ATOM   10477 C CA  . THR E  1 257 ? -1.737  17.444 1.518   1.00 57.57  ? 257 THR E CA  1 
ATOM   10478 C C   . THR E  1 257 ? -1.442  16.214 2.381   1.00 58.40  ? 257 THR E C   1 
ATOM   10479 O O   . THR E  1 257 ? -1.176  15.142 1.806   1.00 55.92  ? 257 THR E O   1 
ATOM   10480 C CB  . THR E  1 257 ? -0.554  18.419 1.560   1.00 55.98  ? 257 THR E CB  1 
ATOM   10481 O OG1 . THR E  1 257 ? -0.841  19.510 0.685   1.00 53.39  ? 257 THR E OG1 1 
ATOM   10482 C CG2 . THR E  1 257 ? 0.751   17.768 1.155   1.00 60.13  ? 257 THR E CG2 1 
ATOM   10483 N N   . ALA E  1 258 ? -1.479  16.378 3.707   1.00 59.52  ? 258 ALA E N   1 
ATOM   10484 C CA  . ALA E  1 258 ? -1.236  15.310 4.704   1.00 67.57  ? 258 ALA E CA  1 
ATOM   10485 C C   . ALA E  1 258 ? -2.237  14.171 4.480   1.00 75.43  ? 258 ALA E C   1 
ATOM   10486 O O   . ALA E  1 258 ? -1.810  12.996 4.483   1.00 72.40  ? 258 ALA E O   1 
ATOM   10487 C CB  . ALA E  1 258 ? -1.338  15.877 6.099   1.00 64.98  ? 258 ALA E CB  1 
ATOM   10488 N N   . GLU E  1 259 ? -3.516  14.515 4.288   1.00 81.75  ? 259 GLU E N   1 
ATOM   10489 C CA  . GLU E  1 259 ? -4.624  13.553 4.036   1.00 78.60  ? 259 GLU E CA  1 
ATOM   10490 C C   . GLU E  1 259 ? -4.261  12.685 2.824   1.00 76.01  ? 259 GLU E C   1 
ATOM   10491 O O   . GLU E  1 259 ? -4.271  11.445 2.961   1.00 86.27  ? 259 GLU E O   1 
ATOM   10492 C CB  . GLU E  1 259 ? -5.947  14.300 3.837   1.00 76.61  ? 259 GLU E CB  1 
ATOM   10493 C CG  . GLU E  1 259 ? -6.522  14.872 5.126   1.00 82.83  ? 259 GLU E CG  1 
ATOM   10494 C CD  . GLU E  1 259 ? -7.753  15.752 4.965   1.00 89.78  ? 259 GLU E CD  1 
ATOM   10495 O OE1 . GLU E  1 259 ? -8.215  15.919 3.819   1.00 90.48  ? 259 GLU E OE1 1 
ATOM   10496 O OE2 . GLU E  1 259 ? -8.247  16.275 5.987   1.00 100.95 ? 259 GLU E OE2 1 
ATOM   10497 N N   . ASP E  1 260 ? -3.939  13.318 1.691   1.00 64.83  ? 260 ASP E N   1 
ATOM   10498 C CA  . ASP E  1 260 ? -3.554  12.639 0.423   1.00 63.20  ? 260 ASP E CA  1 
ATOM   10499 C C   . ASP E  1 260 ? -2.417  11.648 0.703   1.00 57.59  ? 260 ASP E C   1 
ATOM   10500 O O   . ASP E  1 260 ? -2.452  10.536 0.147   1.00 50.15  ? 260 ASP E O   1 
ATOM   10501 C CB  . ASP E  1 260 ? -3.154  13.652 -0.653  1.00 70.07  ? 260 ASP E CB  1 
ATOM   10502 C CG  . ASP E  1 260 ? -4.322  14.447 -1.214  1.00 74.32  ? 260 ASP E CG  1 
ATOM   10503 O OD1 . ASP E  1 260 ? -4.079  15.322 -2.067  1.00 75.33  ? 260 ASP E OD1 1 
ATOM   10504 O OD2 . ASP E  1 260 ? -5.465  14.182 -0.795  1.00 75.59  ? 260 ASP E OD2 1 
ATOM   10505 N N   . VAL E  1 261 ? -1.446  12.040 1.531   1.00 60.27  ? 261 VAL E N   1 
ATOM   10506 C CA  . VAL E  1 261 ? -0.268  11.197 1.896   1.00 68.18  ? 261 VAL E CA  1 
ATOM   10507 C C   . VAL E  1 261 ? -0.764  9.978  2.682   1.00 65.08  ? 261 VAL E C   1 
ATOM   10508 O O   . VAL E  1 261 ? -0.372  8.850  2.325   1.00 63.25  ? 261 VAL E O   1 
ATOM   10509 C CB  . VAL E  1 261 ? 0.785   11.996 2.692   1.00 70.82  ? 261 VAL E CB  1 
ATOM   10510 C CG1 . VAL E  1 261 ? 1.829   11.086 3.323   1.00 65.88  ? 261 VAL E CG1 1 
ATOM   10511 C CG2 . VAL E  1 261 ? 1.455   13.056 1.831   1.00 75.28  ? 261 VAL E CG2 1 
ATOM   10512 N N   . ARG E  1 262 ? -1.596  10.204 3.704   1.00 66.77  ? 262 ARG E N   1 
ATOM   10513 C CA  . ARG E  1 262 ? -2.146  9.141  4.589   1.00 69.41  ? 262 ARG E CA  1 
ATOM   10514 C C   . ARG E  1 262 ? -3.026  8.190  3.768   1.00 72.60  ? 262 ARG E C   1 
ATOM   10515 O O   . ARG E  1 262 ? -2.922  6.968  3.975   1.00 69.20  ? 262 ARG E O   1 
ATOM   10516 C CB  . ARG E  1 262 ? -2.938  9.755  5.747   1.00 70.80  ? 262 ARG E CB  1 
ATOM   10517 C CG  . ARG E  1 262 ? -2.075  10.443 6.795   1.00 73.12  ? 262 ARG E CG  1 
ATOM   10518 C CD  . ARG E  1 262 ? -2.831  10.703 8.084   1.00 79.67  ? 262 ARG E CD  1 
ATOM   10519 N NE  . ARG E  1 262 ? -4.048  11.479 7.883   1.00 81.25  ? 262 ARG E NE  1 
ATOM   10520 C CZ  . ARG E  1 262 ? -4.145  12.794 8.050   1.00 86.74  ? 262 ARG E CZ  1 
ATOM   10521 N NH1 . ARG E  1 262 ? -3.091  13.498 8.425   1.00 85.91  ? 262 ARG E NH1 1 
ATOM   10522 N NH2 . ARG E  1 262 ? -5.300  13.401 7.842   1.00 90.49  ? 262 ARG E NH2 1 
ATOM   10523 N N   . ALA E  1 263 ? -3.859  8.735  2.876   1.00 81.04  ? 263 ALA E N   1 
ATOM   10524 C CA  . ALA E  1 263 ? -4.774  7.976  1.990   1.00 77.76  ? 263 ALA E CA  1 
ATOM   10525 C C   . ALA E  1 263 ? -3.963  7.222  0.930   1.00 74.08  ? 263 ALA E C   1 
ATOM   10526 O O   . ALA E  1 263 ? -4.565  6.434  0.174   1.00 83.03  ? 263 ALA E O   1 
ATOM   10527 C CB  . ALA E  1 263 ? -5.772  8.915  1.356   1.00 81.11  ? 263 ALA E CB  1 
ATOM   10528 N N   . GLY E  1 264 ? -2.649  7.463  0.879   1.00 67.54  ? 264 GLY E N   1 
ATOM   10529 C CA  . GLY E  1 264 ? -1.716  6.830  -0.073  1.00 60.52  ? 264 GLY E CA  1 
ATOM   10530 C C   . GLY E  1 264 ? -1.975  7.276  -1.503  1.00 60.29  ? 264 GLY E C   1 
ATOM   10531 O O   . GLY E  1 264 ? -1.617  6.519  -2.424  1.00 59.65  ? 264 GLY E O   1 
ATOM   10532 N N   . ASP E  1 265 ? -2.571  8.459  -1.682  1.00 70.35  ? 265 ASP E N   1 
ATOM   10533 C CA  . ASP E  1 265 ? -2.880  9.061  -3.008  1.00 71.32  ? 265 ASP E CA  1 
ATOM   10534 C C   . ASP E  1 265 ? -1.613  9.710  -3.573  1.00 66.27  ? 265 ASP E C   1 
ATOM   10535 O O   . ASP E  1 265 ? -1.477  9.771  -4.809  1.00 71.38  ? 265 ASP E O   1 
ATOM   10536 C CB  . ASP E  1 265 ? -3.997  10.105 -2.914  1.00 78.32  ? 265 ASP E CB  1 
ATOM   10537 C CG  . ASP E  1 265 ? -5.369  9.524  -2.627  1.00 84.03  ? 265 ASP E CG  1 
ATOM   10538 O OD1 . ASP E  1 265 ? -5.611  8.369  -3.026  1.00 91.97  ? 265 ASP E OD1 1 
ATOM   10539 O OD2 . ASP E  1 265 ? -6.184  10.234 -2.004  1.00 99.20  ? 265 ASP E OD2 1 
ATOM   10540 N N   . ASP E  1 266 ? -0.731  10.186 -2.691  1.00 63.05  ? 266 ASP E N   1 
ATOM   10541 C CA  . ASP E  1 266 ? 0.504   10.927 -3.058  1.00 61.99  ? 266 ASP E CA  1 
ATOM   10542 C C   . ASP E  1 266 ? 1.545   10.723 -1.955  1.00 56.84  ? 266 ASP E C   1 
ATOM   10543 O O   . ASP E  1 266 ? 1.223   10.053 -0.953  1.00 45.97  ? 266 ASP E O   1 
ATOM   10544 C CB  . ASP E  1 266 ? 0.204   12.411 -3.286  1.00 61.18  ? 266 ASP E CB  1 
ATOM   10545 C CG  . ASP E  1 266 ? 1.064   13.062 -4.357  1.00 57.00  ? 266 ASP E CG  1 
ATOM   10546 O OD1 . ASP E  1 266 ? 0.557   13.988 -5.024  1.00 51.78  ? 266 ASP E OD1 1 
ATOM   10547 O OD2 . ASP E  1 266 ? 2.235   12.642 -4.514  1.00 47.03  ? 266 ASP E OD2 1 
ATOM   10548 N N   . VAL E  1 267 ? 2.741   11.284 -2.147  1.00 63.30  ? 267 VAL E N   1 
ATOM   10549 C CA  . VAL E  1 267 ? 3.885   11.203 -1.193  1.00 64.03  ? 267 VAL E CA  1 
ATOM   10550 C C   . VAL E  1 267 ? 4.495   12.603 -1.053  1.00 62.00  ? 267 VAL E C   1 
ATOM   10551 O O   . VAL E  1 267 ? 4.445   13.373 -2.033  1.00 65.68  ? 267 VAL E O   1 
ATOM   10552 C CB  . VAL E  1 267 ? 4.925   10.164 -1.656  1.00 59.82  ? 267 VAL E CB  1 
ATOM   10553 C CG1 . VAL E  1 267 ? 5.419   10.447 -3.068  1.00 51.45  ? 267 VAL E CG1 1 
ATOM   10554 C CG2 . VAL E  1 267 ? 6.091   10.059 -0.683  1.00 66.06  ? 267 VAL E CG2 1 
ATOM   10555 N N   . HIS E  1 268 ? 5.035   12.918 0.128   1.00 60.00  ? 268 HIS E N   1 
ATOM   10556 C CA  . HIS E  1 268 ? 5.666   14.226 0.449   1.00 58.73  ? 268 HIS E CA  1 
ATOM   10557 C C   . HIS E  1 268 ? 7.028   13.982 1.093   1.00 59.78  ? 268 HIS E C   1 
ATOM   10558 O O   . HIS E  1 268 ? 7.144   13.195 2.029   1.00 62.27  ? 268 HIS E O   1 
ATOM   10559 C CB  . HIS E  1 268 ? 4.729   15.065 1.326   1.00 56.55  ? 268 HIS E CB  1 
ATOM   10560 C CG  . HIS E  1 268 ? 4.995   16.529 1.242   1.00 55.74  ? 268 HIS E CG  1 
ATOM   10561 N ND1 . HIS E  1 268 ? 5.580   17.233 2.275   1.00 56.63  ? 268 HIS E ND1 1 
ATOM   10562 C CD2 . HIS E  1 268 ? 4.770   17.419 0.253   1.00 56.98  ? 268 HIS E CD2 1 
ATOM   10563 C CE1 . HIS E  1 268 ? 5.701   18.497 1.927   1.00 56.05  ? 268 HIS E CE1 1 
ATOM   10564 N NE2 . HIS E  1 268 ? 5.212   18.638 0.690   1.00 56.94  ? 268 HIS E NE2 1 
ATOM   10565 N N   . PRO E  1 269 ? 8.096   14.662 0.616   1.00 59.39  ? 269 PRO E N   1 
ATOM   10566 C CA  . PRO E  1 269 ? 9.467   14.313 0.991   1.00 58.84  ? 269 PRO E CA  1 
ATOM   10567 C C   . PRO E  1 269 ? 9.862   14.723 2.419   1.00 56.61  ? 269 PRO E C   1 
ATOM   10568 O O   . PRO E  1 269 ? 10.946  14.367 2.842   1.00 62.03  ? 269 PRO E O   1 
ATOM   10569 C CB  . PRO E  1 269 ? 10.308  15.082 -0.039  1.00 57.72  ? 269 PRO E CB  1 
ATOM   10570 C CG  . PRO E  1 269 ? 9.466   16.296 -0.368  1.00 59.87  ? 269 PRO E CG  1 
ATOM   10571 C CD  . PRO E  1 269 ? 8.034   15.807 -0.306  1.00 58.94  ? 269 PRO E CD  1 
ATOM   10572 N N   . GLU E  1 270 ? 8.986   15.451 3.118   1.00 58.09  ? 270 GLU E N   1 
ATOM   10573 C CA  . GLU E  1 270 ? 9.198   15.894 4.522   1.00 59.40  ? 270 GLU E CA  1 
ATOM   10574 C C   . GLU E  1 270 ? 7.928   15.622 5.335   1.00 55.21  ? 270 GLU E C   1 
ATOM   10575 O O   . GLU E  1 270 ? 6.839   15.552 4.732   1.00 59.32  ? 270 GLU E O   1 
ATOM   10576 C CB  . GLU E  1 270 ? 9.561   17.380 4.571   1.00 61.25  ? 270 GLU E CB  1 
ATOM   10577 C CG  . GLU E  1 270 ? 8.369   18.303 4.384   1.00 68.96  ? 270 GLU E CG  1 
ATOM   10578 C CD  . GLU E  1 270 ? 8.697   19.785 4.458   1.00 73.13  ? 270 GLU E CD  1 
ATOM   10579 O OE1 . GLU E  1 270 ? 9.893   20.126 4.383   1.00 80.55  ? 270 GLU E OE1 1 
ATOM   10580 O OE2 . GLU E  1 270 ? 7.756   20.593 4.592   1.00 68.56  ? 270 GLU E OE2 1 
ATOM   10581 N N   . SER E  1 271 ? 8.068   15.474 6.654   1.00 52.21  ? 271 SER E N   1 
ATOM   10582 C CA  . SER E  1 271 ? 6.942   15.332 7.613   1.00 55.77  ? 271 SER E CA  1 
ATOM   10583 C C   . SER E  1 271 ? 6.186   16.662 7.707   1.00 56.73  ? 271 SER E C   1 
ATOM   10584 O O   . SER E  1 271 ? 6.849   17.717 7.762   1.00 58.50  ? 271 SER E O   1 
ATOM   10585 C CB  . SER E  1 271 ? 7.432   14.876 8.963   1.00 58.30  ? 271 SER E CB  1 
ATOM   10586 O OG  . SER E  1 271 ? 8.604   15.582 9.345   1.00 56.78  ? 271 SER E OG  1 
ATOM   10587 N N   . ILE E  1 272 ? 4.851   16.606 7.714   1.00 52.17  ? 272 ILE E N   1 
ATOM   10588 C CA  . ILE E  1 272 ? 3.952   17.794 7.804   1.00 47.92  ? 272 ILE E CA  1 
ATOM   10589 C C   . ILE E  1 272 ? 3.422   17.898 9.237   1.00 49.72  ? 272 ILE E C   1 
ATOM   10590 O O   . ILE E  1 272 ? 2.949   16.875 9.768   1.00 49.96  ? 272 ILE E O   1 
ATOM   10591 C CB  . ILE E  1 272 ? 2.810   17.695 6.774   1.00 48.61  ? 272 ILE E CB  1 
ATOM   10592 C CG1 . ILE E  1 272 ? 3.345   17.658 5.339   1.00 47.27  ? 272 ILE E CG1 1 
ATOM   10593 C CG2 . ILE E  1 272 ? 1.803   18.819 6.974   1.00 51.50  ? 272 ILE E CG2 1 
ATOM   10594 C CD1 . ILE E  1 272 ? 2.276   17.445 4.287   1.00 46.31  ? 272 ILE E CD1 1 
ATOM   10595 N N   . TRP E  1 273 ? 3.509   19.092 9.831   1.00 56.17  ? 273 TRP E N   1 
ATOM   10596 C CA  . TRP E  1 273 ? 3.097   19.379 11.231  1.00 61.12  ? 273 TRP E CA  1 
ATOM   10597 C C   . TRP E  1 273 ? 2.072   20.516 11.245  1.00 62.95  ? 273 TRP E C   1 
ATOM   10598 O O   . TRP E  1 273 ? 2.133   21.375 10.344  1.00 62.06  ? 273 TRP E O   1 
ATOM   10599 C CB  . TRP E  1 273 ? 4.317   19.723 12.095  1.00 61.59  ? 273 TRP E CB  1 
ATOM   10600 C CG  . TRP E  1 273 ? 5.337   18.630 12.168  1.00 61.27  ? 273 TRP E CG  1 
ATOM   10601 C CD1 . TRP E  1 273 ? 6.231   18.274 11.200  1.00 60.90  ? 273 TRP E CD1 1 
ATOM   10602 C CD2 . TRP E  1 273 ? 5.569   17.742 13.276  1.00 66.72  ? 273 TRP E CD2 1 
ATOM   10603 N NE1 . TRP E  1 273 ? 7.000   17.226 11.626  1.00 67.17  ? 273 TRP E NE1 1 
ATOM   10604 C CE2 . TRP E  1 273 ? 6.619   16.879 12.897  1.00 71.12  ? 273 TRP E CE2 1 
ATOM   10605 C CE3 . TRP E  1 273 ? 4.994   17.592 14.544  1.00 69.22  ? 273 TRP E CE3 1 
ATOM   10606 C CZ2 . TRP E  1 273 ? 7.107   15.886 13.744  1.00 78.24  ? 273 TRP E CZ2 1 
ATOM   10607 C CZ3 . TRP E  1 273 ? 5.477   16.610 15.379  1.00 72.34  ? 273 TRP E CZ3 1 
ATOM   10608 C CH2 . TRP E  1 273 ? 6.518   15.769 14.983  1.00 78.06  ? 273 TRP E CH2 1 
ATOM   10609 N N   . ILE E  1 274 ? 1.173   20.506 12.234  1.00 70.65  ? 274 ILE E N   1 
ATOM   10610 C CA  . ILE E  1 274 ? 0.185   21.593 12.504  1.00 75.40  ? 274 ILE E CA  1 
ATOM   10611 C C   . ILE E  1 274 ? 0.022   21.722 14.021  1.00 85.58  ? 274 ILE E C   1 
ATOM   10612 O O   . ILE E  1 274 ? -0.463  20.758 14.650  1.00 85.18  ? 274 ILE E O   1 
ATOM   10613 C CB  . ILE E  1 274 ? -1.160  21.322 11.800  1.00 67.87  ? 274 ILE E CB  1 
ATOM   10614 C CG1 . ILE E  1 274 ? -0.991  21.178 10.286  1.00 70.53  ? 274 ILE E CG1 1 
ATOM   10615 C CG2 . ILE E  1 274 ? -2.175  22.400 12.146  1.00 67.65  ? 274 ILE E CG2 1 
ATOM   10616 C CD1 . ILE E  1 274 ? -2.276  20.875 9.554   1.00 76.07  ? 274 ILE E CD1 1 
ATOM   10617 N N   . SER E  1 275 ? 0.425   22.867 14.579  1.00 93.19  ? 275 SER E N   1 
ATOM   10618 C CA  . SER E  1 275 ? 0.365   23.174 16.032  1.00 97.53  ? 275 SER E CA  1 
ATOM   10619 C C   . SER E  1 275 ? 1.148   22.115 16.817  1.00 100.37 ? 275 SER E C   1 
ATOM   10620 O O   . SER E  1 275 ? 0.715   21.762 17.932  1.00 101.54 ? 275 SER E O   1 
ATOM   10621 C CB  . SER E  1 275 ? -1.063  23.264 16.497  1.00 97.92  ? 275 SER E CB  1 
ATOM   10622 O OG  . SER E  1 275 ? -1.760  24.272 15.781  1.00 100.90 ? 275 SER E OG  1 
ATOM   10623 N N   . SER E  1 276 ? 2.249   21.625 16.239  1.00 100.46 ? 276 SER E N   1 
ATOM   10624 C CA  . SER E  1 276 ? 3.227   20.706 16.880  1.00 101.29 ? 276 SER E CA  1 
ATOM   10625 C C   . SER E  1 276 ? 2.716   19.261 16.843  1.00 89.62  ? 276 SER E C   1 
ATOM   10626 O O   . SER E  1 276 ? 3.359   18.397 17.473  1.00 85.25  ? 276 SER E O   1 
ATOM   10627 C CB  . SER E  1 276 ? 3.528   21.138 18.293  1.00 108.25 ? 276 SER E CB  1 
ATOM   10628 O OG  . SER E  1 276 ? 4.046   22.459 18.318  1.00 112.40 ? 276 SER E OG  1 
ATOM   10629 N N   . VAL E  1 277 ? 1.608   19.011 16.137  1.00 77.29  ? 277 VAL E N   1 
ATOM   10630 C CA  . VAL E  1 277 ? 1.005   17.655 15.969  1.00 73.19  ? 277 VAL E CA  1 
ATOM   10631 C C   . VAL E  1 277 ? 1.321   17.152 14.555  1.00 70.53  ? 277 VAL E C   1 
ATOM   10632 O O   . VAL E  1 277 ? 0.887   17.807 13.588  1.00 70.15  ? 277 VAL E O   1 
ATOM   10633 C CB  . VAL E  1 277 ? -0.514  17.670 16.230  1.00 67.53  ? 277 VAL E CB  1 
ATOM   10634 C CG1 . VAL E  1 277 ? -1.128  16.293 16.038  1.00 64.18  ? 277 VAL E CG1 1 
ATOM   10635 C CG2 . VAL E  1 277 ? -0.847  18.213 17.611  1.00 70.03  ? 277 VAL E CG2 1 
ATOM   10636 N N   . LYS E  1 278 ? 2.049   16.036 14.448  1.00 60.55  ? 278 LYS E N   1 
ATOM   10637 C CA  . LYS E  1 278 ? 2.437   15.413 13.154  1.00 61.81  ? 278 LYS E CA  1 
ATOM   10638 C C   . LYS E  1 278 ? 1.169   14.999 12.401  1.00 65.17  ? 278 LYS E C   1 
ATOM   10639 O O   . LYS E  1 278 ? 0.254   14.458 13.045  1.00 72.30  ? 278 LYS E O   1 
ATOM   10640 C CB  . LYS E  1 278 ? 3.353   14.207 13.385  1.00 60.04  ? 278 LYS E CB  1 
ATOM   10641 C CG  . LYS E  1 278 ? 3.956   13.615 12.119  1.00 63.86  ? 278 LYS E CG  1 
ATOM   10642 C CD  . LYS E  1 278 ? 4.805   12.388 12.370  1.00 72.11  ? 278 LYS E CD  1 
ATOM   10643 C CE  . LYS E  1 278 ? 5.907   12.207 11.347  1.00 85.16  ? 278 LYS E CE  1 
ATOM   10644 N NZ  . LYS E  1 278 ? 6.607   10.912 11.517  1.00 83.84  ? 278 LYS E NZ  1 
ATOM   10645 N N   . GLN E  1 279 ? 1.128   15.248 11.089  1.00 67.03  ? 279 GLN E N   1 
ATOM   10646 C CA  . GLN E  1 279 ? -0.048  14.988 10.215  1.00 68.53  ? 279 GLN E CA  1 
ATOM   10647 C C   . GLN E  1 279 ? 0.296   13.881 9.214   1.00 68.60  ? 279 GLN E C   1 
ATOM   10648 O O   . GLN E  1 279 ? -0.522  12.956 9.047   1.00 73.74  ? 279 GLN E O   1 
ATOM   10649 C CB  . GLN E  1 279 ? -0.456  16.269 9.486   1.00 71.02  ? 279 GLN E CB  1 
ATOM   10650 C CG  . GLN E  1 279 ? -0.889  17.382 10.427  1.00 65.42  ? 279 GLN E CG  1 
ATOM   10651 C CD  . GLN E  1 279 ? -2.170  17.036 11.143  1.00 64.12  ? 279 GLN E CD  1 
ATOM   10652 O OE1 . GLN E  1 279 ? -3.145  16.601 10.533  1.00 73.51  ? 279 GLN E OE1 1 
ATOM   10653 N NE2 . GLN E  1 279 ? -2.178  17.230 12.452  1.00 58.19  ? 279 GLN E NE2 1 
ATOM   10654 N N   . SER E  1 280 ? 1.457   13.994 8.567   1.00 67.99  ? 280 SER E N   1 
ATOM   10655 C CA  . SER E  1 280 ? 1.998   13.001 7.604   1.00 61.93  ? 280 SER E CA  1 
ATOM   10656 C C   . SER E  1 280 ? 3.464   12.715 7.940   1.00 56.78  ? 280 SER E C   1 
ATOM   10657 O O   . SER E  1 280 ? 4.066   13.501 8.701   1.00 52.63  ? 280 SER E O   1 
ATOM   10658 C CB  . SER E  1 280 ? 1.841   13.485 6.186   1.00 60.96  ? 280 SER E CB  1 
ATOM   10659 O OG  . SER E  1 280 ? 2.962   14.262 5.790   1.00 58.93  ? 280 SER E OG  1 
ATOM   10660 N N   . ASP E  1 281 ? 4.006   11.622 7.399   1.00 63.04  ? 281 ASP E N   1 
ATOM   10661 C CA  . ASP E  1 281 ? 5.435   11.237 7.537   1.00 65.42  ? 281 ASP E CA  1 
ATOM   10662 C C   . ASP E  1 281 ? 6.136   11.498 6.201   1.00 55.66  ? 281 ASP E C   1 
ATOM   10663 O O   . ASP E  1 281 ? 5.459   11.428 5.157   1.00 57.30  ? 281 ASP E O   1 
ATOM   10664 C CB  . ASP E  1 281 ? 5.575   9.774  7.967   1.00 75.78  ? 281 ASP E CB  1 
ATOM   10665 C CG  . ASP E  1 281 ? 4.798   9.435  9.228   1.00 91.96  ? 281 ASP E CG  1 
ATOM   10666 O OD1 . ASP E  1 281 ? 4.375   8.268  9.360   1.00 101.88 ? 281 ASP E OD1 1 
ATOM   10667 O OD2 . ASP E  1 281 ? 4.617   10.343 10.068  1.00 119.37 ? 281 ASP E OD2 1 
ATOM   10668 N N   . ALA E  1 282 ? 7.435   11.802 6.241   1.00 52.39  ? 282 ALA E N   1 
ATOM   10669 C CA  . ALA E  1 282 ? 8.291   11.974 5.045   1.00 48.52  ? 282 ALA E CA  1 
ATOM   10670 C C   . ALA E  1 282 ? 8.318   10.657 4.262   1.00 47.09  ? 282 ALA E C   1 
ATOM   10671 O O   . ALA E  1 282 ? 8.394   9.589  4.902   1.00 40.52  ? 282 ALA E O   1 
ATOM   10672 C CB  . ALA E  1 282 ? 9.678   12.404 5.454   1.00 48.88  ? 282 ALA E CB  1 
ATOM   10673 N N   . GLY E  1 283 ? 8.237   10.740 2.932   1.00 48.10  ? 283 GLY E N   1 
ATOM   10674 C CA  . GLY E  1 283 ? 8.316   9.586  2.015   1.00 49.49  ? 283 GLY E CA  1 
ATOM   10675 C C   . GLY E  1 283 ? 8.885   9.989  0.667   1.00 50.48  ? 283 GLY E C   1 
ATOM   10676 O O   . GLY E  1 283 ? 8.693   11.159 0.274   1.00 59.61  ? 283 GLY E O   1 
ATOM   10677 N N   . LEU E  1 284 ? 9.564   9.063  -0.013  1.00 47.71  ? 284 LEU E N   1 
ATOM   10678 C CA  . LEU E  1 284 ? 10.094  9.263  -1.388  1.00 53.27  ? 284 LEU E CA  1 
ATOM   10679 C C   . LEU E  1 284 ? 9.243   8.476  -2.378  1.00 54.34  ? 284 LEU E C   1 
ATOM   10680 O O   . LEU E  1 284 ? 8.638   7.469  -2.019  1.00 50.88  ? 284 LEU E O   1 
ATOM   10681 C CB  . LEU E  1 284 ? 11.552  8.801  -1.448  1.00 56.29  ? 284 LEU E CB  1 
ATOM   10682 C CG  . LEU E  1 284 ? 12.553  9.666  -0.686  1.00 58.74  ? 284 LEU E CG  1 
ATOM   10683 C CD1 . LEU E  1 284 ? 13.976  9.216  -0.982  1.00 60.32  ? 284 LEU E CD1 1 
ATOM   10684 C CD2 . LEU E  1 284 ? 12.381  11.138 -1.029  1.00 60.11  ? 284 LEU E CD2 1 
ATOM   10685 N N   . PRO E  1 285 ? 9.162   8.924  -3.649  1.00 53.36  ? 285 PRO E N   1 
ATOM   10686 C CA  . PRO E  1 285 ? 8.569   8.117  -4.712  1.00 59.00  ? 285 PRO E CA  1 
ATOM   10687 C C   . PRO E  1 285 ? 9.418   6.865  -4.981  1.00 64.71  ? 285 PRO E C   1 
ATOM   10688 O O   . PRO E  1 285 ? 10.614  6.906  -4.752  1.00 75.08  ? 285 PRO E O   1 
ATOM   10689 C CB  . PRO E  1 285 ? 8.567   9.039  -5.942  1.00 57.54  ? 285 PRO E CB  1 
ATOM   10690 C CG  . PRO E  1 285 ? 8.794   10.434 -5.383  1.00 57.96  ? 285 PRO E CG  1 
ATOM   10691 C CD  . PRO E  1 285 ? 9.618   10.236 -4.129  1.00 54.62  ? 285 PRO E CD  1 
ATOM   10692 N N   . ARG E  1 286 ? 8.784   5.789  -5.448  1.00 61.06  ? 286 ARG E N   1 
ATOM   10693 C CA  . ARG E  1 286 ? 9.476   4.542  -5.865  1.00 62.15  ? 286 ARG E CA  1 
ATOM   10694 C C   . ARG E  1 286 ? 10.400  4.866  -7.045  1.00 57.68  ? 286 ARG E C   1 
ATOM   10695 O O   . ARG E  1 286 ? 9.976   5.631  -7.936  1.00 56.49  ? 286 ARG E O   1 
ATOM   10696 C CB  . ARG E  1 286 ? 8.444   3.473  -6.233  1.00 67.97  ? 286 ARG E CB  1 
ATOM   10697 C CG  . ARG E  1 286 ? 7.349   3.975  -7.163  1.00 78.35  ? 286 ARG E CG  1 
ATOM   10698 C CD  . ARG E  1 286 ? 6.340   2.904  -7.525  1.00 84.74  ? 286 ARG E CD  1 
ATOM   10699 N NE  . ARG E  1 286 ? 6.026   2.954  -8.944  1.00 82.89  ? 286 ARG E NE  1 
ATOM   10700 C CZ  . ARG E  1 286 ? 6.855   2.561  -9.904  1.00 87.37  ? 286 ARG E CZ  1 
ATOM   10701 N NH1 . ARG E  1 286 ? 8.049   2.086  -9.590  1.00 90.55  ? 286 ARG E NH1 1 
ATOM   10702 N NH2 . ARG E  1 286 ? 6.492   2.645  -11.171 1.00 90.44  ? 286 ARG E NH2 1 
ATOM   10703 N N   . GLU E  1 287 ? 11.618  4.316  -7.038  1.00 51.05  ? 287 GLU E N   1 
ATOM   10704 C CA  . GLU E  1 287 ? 12.565  4.371  -8.184  1.00 49.36  ? 287 GLU E CA  1 
ATOM   10705 C C   . GLU E  1 287 ? 11.913  3.685  -9.387  1.00 48.13  ? 287 GLU E C   1 
ATOM   10706 O O   . GLU E  1 287 ? 11.215  2.676  -9.181  1.00 55.64  ? 287 GLU E O   1 
ATOM   10707 C CB  . GLU E  1 287 ? 13.888  3.680  -7.848  1.00 52.57  ? 287 GLU E CB  1 
ATOM   10708 C CG  . GLU E  1 287 ? 14.693  4.373  -6.765  1.00 54.84  ? 287 GLU E CG  1 
ATOM   10709 C CD  . GLU E  1 287 ? 15.970  3.637  -6.399  1.00 61.94  ? 287 GLU E CD  1 
ATOM   10710 O OE1 . GLU E  1 287 ? 16.614  3.094  -7.319  1.00 67.67  ? 287 GLU E OE1 1 
ATOM   10711 O OE2 . GLU E  1 287 ? 16.310  3.595  -5.197  1.00 64.39  ? 287 GLU E OE2 1 
ATOM   10712 N N   . VAL E  1 288 ? 12.147  4.207  -10.592 1.00 53.46  ? 288 VAL E N   1 
ATOM   10713 C CA  . VAL E  1 288 ? 11.524  3.717  -11.858 1.00 57.22  ? 288 VAL E CA  1 
ATOM   10714 C C   . VAL E  1 288 ? 12.629  3.357  -12.858 1.00 66.19  ? 288 VAL E C   1 
ATOM   10715 O O   . VAL E  1 288 ? 13.594  4.138  -12.981 1.00 78.23  ? 288 VAL E O   1 
ATOM   10716 C CB  . VAL E  1 288 ? 10.563  4.771  -12.439 1.00 59.90  ? 288 VAL E CB  1 
ATOM   10717 C CG1 . VAL E  1 288 ? 9.979   4.323  -13.770 1.00 60.88  ? 288 VAL E CG1 1 
ATOM   10718 C CG2 . VAL E  1 288 ? 9.458   5.132  -11.455 1.00 59.18  ? 288 VAL E CG2 1 
ATOM   10719 N N   . TYR E  1 289 ? 12.486  2.214  -13.539 1.00 77.01  ? 289 TYR E N   1 
ATOM   10720 C CA  . TYR E  1 289 ? 13.430  1.704  -14.571 1.00 84.61  ? 289 TYR E CA  1 
ATOM   10721 C C   . TYR E  1 289 ? 12.857  1.964  -15.969 1.00 77.92  ? 289 TYR E C   1 
ATOM   10722 O O   . TYR E  1 289 ? 11.631  2.138  -16.097 1.00 87.02  ? 289 TYR E O   1 
ATOM   10723 C CB  . TYR E  1 289 ? 13.707  0.212  -14.366 1.00 91.36  ? 289 TYR E CB  1 
ATOM   10724 C CG  . TYR E  1 289 ? 14.429  -0.126 -13.085 1.00 105.37 ? 289 TYR E CG  1 
ATOM   10725 C CD1 . TYR E  1 289 ? 15.813  -0.082 -13.006 1.00 110.34 ? 289 TYR E CD1 1 
ATOM   10726 C CD2 . TYR E  1 289 ? 13.728  -0.495 -11.950 1.00 107.53 ? 289 TYR E CD2 1 
ATOM   10727 C CE1 . TYR E  1 289 ? 16.480  -0.394 -11.832 1.00 112.06 ? 289 TYR E CE1 1 
ATOM   10728 C CE2 . TYR E  1 289 ? 14.380  -0.810 -10.769 1.00 109.89 ? 289 TYR E CE2 1 
ATOM   10729 C CZ  . TYR E  1 289 ? 15.760  -0.760 -10.709 1.00 109.50 ? 289 TYR E CZ  1 
ATOM   10730 O OH  . TYR E  1 289 ? 16.401  -1.072 -9.545  1.00 107.70 ? 289 TYR E OH  1 
ATOM   10731 N N   . LEU E  1 290 ? 13.726  1.977  -16.986 1.00 74.68  ? 290 LEU E N   1 
ATOM   10732 C CA  . LEU E  1 290 ? 13.359  2.198  -18.412 1.00 70.04  ? 290 LEU E CA  1 
ATOM   10733 C C   . LEU E  1 290 ? 14.316  1.404  -19.311 1.00 66.84  ? 290 LEU E C   1 
ATOM   10734 O O   . LEU E  1 290 ? 14.205  1.414  -20.538 1.00 58.97  ? 290 LEU E O   1 
ATOM   10735 C CB  . LEU E  1 290 ? 13.425  3.698  -18.720 1.00 70.02  ? 290 LEU E CB  1 
ATOM   10736 C CG  . LEU E  1 290 ? 12.753  4.615  -17.697 1.00 72.85  ? 290 LEU E CG  1 
ATOM   10737 C CD1 . LEU E  1 290 ? 12.927  6.077  -18.081 1.00 66.60  ? 290 LEU E CD1 1 
ATOM   10738 C CD2 . LEU E  1 290 ? 11.277  4.277  -17.542 1.00 75.02  ? 290 LEU E CD2 1 
HETATM 10739 C C1  . LFA F  2 .   ? 30.457  61.702 22.640  1.00 70.02  ? 401 LFA A C1  1 
HETATM 10740 C C2  . LFA F  2 .   ? 29.106  61.877 23.296  1.00 70.76  ? 401 LFA A C2  1 
HETATM 10741 C C3  . LFA F  2 .   ? 28.170  60.704 23.111  1.00 72.22  ? 401 LFA A C3  1 
HETATM 10742 C C4  . LFA F  2 .   ? 28.653  59.390 23.687  1.00 71.83  ? 401 LFA A C4  1 
HETATM 10743 C C5  . LFA F  2 .   ? 27.547  58.471 24.161  1.00 70.61  ? 401 LFA A C5  1 
HETATM 10744 C C6  . LFA F  2 .   ? 27.622  57.061 23.618  1.00 72.34  ? 401 LFA A C6  1 
HETATM 10745 C C7  . LFA F  2 .   ? 26.975  56.012 24.500  1.00 73.60  ? 401 LFA A C7  1 
HETATM 10746 C C8  . LFA F  2 .   ? 27.075  54.596 23.968  1.00 70.00  ? 401 LFA A C8  1 
HETATM 10747 C C9  . LFA F  2 .   ? 26.325  53.561 24.782  1.00 59.86  ? 401 LFA A C9  1 
HETATM 10748 C C10 . LFA F  2 .   ? 26.343  52.165 24.187  1.00 61.46  ? 401 LFA A C10 1 
HETATM 10749 C C11 . LFA F  2 .   ? 25.665  51.108 25.036  1.00 44.60  ? 401 LFA A C11 1 
HETATM 10750 C C1  . LFA G  2 .   ? 32.899  58.211 21.859  1.00 61.13  ? 402 LFA A C1  1 
HETATM 10751 C C2  . LFA G  2 .   ? 31.703  57.286 21.939  1.00 68.09  ? 402 LFA A C2  1 
HETATM 10752 C C3  . LFA G  2 .   ? 32.057  55.835 22.166  1.00 65.57  ? 402 LFA A C3  1 
HETATM 10753 C C4  . LFA G  2 .   ? 30.885  54.876 22.148  1.00 60.99  ? 402 LFA A C4  1 
HETATM 10754 C C5  . LFA G  2 .   ? 31.278  53.413 22.191  1.00 58.07  ? 402 LFA A C5  1 
HETATM 10755 C C6  . LFA G  2 .   ? 30.112  52.447 22.226  1.00 51.30  ? 402 LFA A C6  1 
HETATM 10756 C C7  . LFA G  2 .   ? 30.501  50.986 22.119  1.00 40.56  ? 402 LFA A C7  1 
HETATM 10757 P P   . PO4 H  3 .   ? 26.678  27.229 15.527  1.00 107.47 ? 403 PO4 A P   1 
HETATM 10758 O O1  . PO4 H  3 .   ? 26.071  27.637 14.189  1.00 114.85 ? 403 PO4 A O1  1 
HETATM 10759 O O2  . PO4 H  3 .   ? 28.046  27.882 15.684  1.00 100.33 ? 403 PO4 A O2  1 
HETATM 10760 O O3  . PO4 H  3 .   ? 26.831  25.711 15.577  1.00 88.81  ? 403 PO4 A O3  1 
HETATM 10761 O O4  . PO4 H  3 .   ? 25.763  27.688 16.658  1.00 108.97 ? 403 PO4 A O4  1 
HETATM 10762 C C1  . LFA I  2 .   ? 32.422  60.564 26.609  1.00 49.86  ? 404 LFA A C1  1 
HETATM 10763 C C2  . LFA I  2 .   ? 32.592  59.155 26.086  1.00 50.20  ? 404 LFA A C2  1 
HETATM 10764 C C3  . LFA I  2 .   ? 31.711  58.125 26.759  1.00 52.03  ? 404 LFA A C3  1 
HETATM 10765 C C4  . LFA I  2 .   ? 31.665  56.780 26.062  1.00 48.15  ? 404 LFA A C4  1 
HETATM 10766 C C5  . LFA I  2 .   ? 31.182  55.635 26.927  1.00 41.04  ? 404 LFA A C5  1 
HETATM 10767 C C6  . LFA I  2 .   ? 31.524  54.261 26.387  1.00 39.61  ? 404 LFA A C6  1 
HETATM 10768 C C7  . LFA I  2 .   ? 31.157  53.115 27.306  1.00 34.52  ? 404 LFA A C7  1 
HETATM 10769 C C1  . LFA J  2 .   ? 21.888  48.758 3.700   1.00 67.25  ? 405 LFA A C1  1 
HETATM 10770 C C2  . LFA J  2 .   ? 21.528  50.105 4.288   1.00 68.76  ? 405 LFA A C2  1 
HETATM 10771 C C3  . LFA J  2 .   ? 21.807  51.272 3.373   1.00 69.11  ? 405 LFA A C3  1 
HETATM 10772 C C4  . LFA J  2 .   ? 20.913  52.475 3.583   1.00 69.09  ? 405 LFA A C4  1 
HETATM 10773 C C5  . LFA J  2 .   ? 21.017  53.519 2.494   1.00 71.86  ? 405 LFA A C5  1 
HETATM 10774 C C6  . LFA J  2 .   ? 20.326  54.829 2.805   1.00 67.66  ? 405 LFA A C6  1 
HETATM 10775 C C7  . LFA J  2 .   ? 20.554  55.917 1.775   1.00 62.96  ? 405 LFA A C7  1 
HETATM 10776 C C8  . LFA J  2 .   ? 21.991  56.386 1.665   1.00 56.24  ? 405 LFA A C8  1 
HETATM 10777 C C9  . LFA J  2 .   ? 22.290  57.220 0.435   1.00 48.28  ? 405 LFA A C9  1 
HETATM 10778 C C10 . LFA J  2 .   ? 22.139  56.478 -0.877  1.00 40.97  ? 405 LFA A C10 1 
HETATM 10779 C C14 . LFA K  2 .   ? 16.118  57.109 -1.011  1.00 61.23  ? 406 LFA A C14 1 
HETATM 10780 C C15 . LFA K  2 .   ? 16.644  55.792 -0.487  1.00 66.16  ? 406 LFA A C15 1 
HETATM 10781 C C16 . LFA K  2 .   ? 16.246  54.590 -1.312  1.00 65.78  ? 406 LFA A C16 1 
HETATM 10782 C C17 . LFA K  2 .   ? 16.385  53.267 -0.595  1.00 68.20  ? 406 LFA A C17 1 
HETATM 10783 C C18 . LFA K  2 .   ? 17.630  52.489 -0.953  1.00 73.29  ? 406 LFA A C18 1 
HETATM 10784 C C19 . LFA K  2 .   ? 17.815  51.206 -0.177  1.00 78.32  ? 406 LFA A C19 1 
HETATM 10785 C C20 . LFA K  2 .   ? 17.033  50.031 -0.721  1.00 71.45  ? 406 LFA A C20 1 
HETATM 10786 C C1  . RET L  4 .   ? 8.804   50.786 25.644  1.00 80.80  ? 407 RET A C1  1 
HETATM 10787 C C2  . RET L  4 .   ? 8.124   51.979 26.322  1.00 82.06  ? 407 RET A C2  1 
HETATM 10788 C C3  . RET L  4 .   ? 8.434   52.087 27.771  1.00 86.06  ? 407 RET A C3  1 
HETATM 10789 C C4  . RET L  4 .   ? 8.007   50.827 28.514  1.00 87.60  ? 407 RET A C4  1 
HETATM 10790 C C5  . RET L  4 .   ? 8.260   49.555 27.755  1.00 85.41  ? 407 RET A C5  1 
HETATM 10791 C C6  . RET L  4 .   ? 8.802   49.544 26.520  1.00 81.74  ? 407 RET A C6  1 
HETATM 10792 C C7  . RET L  4 .   ? 9.368   48.330 25.984  1.00 75.61  ? 407 RET A C7  1 
HETATM 10793 C C8  . RET L  4 .   ? 10.057  48.200 24.815  1.00 72.16  ? 407 RET A C8  1 
HETATM 10794 C C9  . RET L  4 .   ? 10.768  47.081 24.378  1.00 69.98  ? 407 RET A C9  1 
HETATM 10795 C C10 . RET L  4 .   ? 11.431  47.068 23.138  1.00 70.36  ? 407 RET A C10 1 
HETATM 10796 C C11 . RET L  4 .   ? 12.171  46.054 22.559  1.00 67.36  ? 407 RET A C11 1 
HETATM 10797 C C12 . RET L  4 .   ? 12.737  46.033 21.295  1.00 68.01  ? 407 RET A C12 1 
HETATM 10798 C C13 . RET L  4 .   ? 13.433  44.971 20.665  1.00 59.50  ? 407 RET A C13 1 
HETATM 10799 C C14 . RET L  4 .   ? 13.872  45.084 19.382  1.00 58.08  ? 407 RET A C14 1 
HETATM 10800 C C15 . RET L  4 .   ? 14.687  44.025 18.674  1.00 62.35  ? 407 RET A C15 1 
HETATM 10801 C C16 . RET L  4 .   ? 8.064   50.504 24.327  1.00 77.19  ? 407 RET A C16 1 
HETATM 10802 C C17 . RET L  4 .   ? 10.247  51.198 25.311  1.00 78.93  ? 407 RET A C17 1 
HETATM 10803 C C18 . RET L  4 .   ? 7.873   48.319 28.522  1.00 86.75  ? 407 RET A C18 1 
HETATM 10804 C C19 . RET L  4 .   ? 10.849  45.855 25.210  1.00 66.17  ? 407 RET A C19 1 
HETATM 10805 C C20 . RET L  4 .   ? 13.648  43.768 21.472  1.00 60.95  ? 407 RET A C20 1 
HETATM 10806 C C1  . LFA M  2 .   ? 48.031  50.982 -5.680  1.00 55.95  ? 401 LFA B C1  1 
HETATM 10807 C C2  . LFA M  2 .   ? 47.866  51.973 -6.815  1.00 56.98  ? 401 LFA B C2  1 
HETATM 10808 C C3  . LFA M  2 .   ? 48.118  53.415 -6.434  1.00 51.95  ? 401 LFA B C3  1 
HETATM 10809 C C4  . LFA M  2 .   ? 47.960  54.402 -7.572  1.00 51.12  ? 401 LFA B C4  1 
HETATM 10810 C C5  . LFA M  2 .   ? 48.148  55.854 -7.180  1.00 50.78  ? 401 LFA B C5  1 
HETATM 10811 C C6  . LFA M  2 .   ? 47.998  56.842 -8.322  1.00 46.86  ? 401 LFA B C6  1 
HETATM 10812 C C7  . LFA M  2 .   ? 48.328  58.273 -7.954  1.00 47.64  ? 401 LFA B C7  1 
HETATM 10813 C C8  . LFA M  2 .   ? 47.670  59.320 -8.826  1.00 43.60  ? 401 LFA B C8  1 
HETATM 10814 C C9  . LFA M  2 .   ? 48.504  59.767 -10.005 1.00 38.76  ? 401 LFA B C9  1 
HETATM 10815 C C10 . LFA M  2 .   ? 48.448  61.255 -10.282 1.00 38.72  ? 401 LFA B C10 1 
HETATM 10816 C C11 . LFA M  2 .   ? 49.408  62.084 -9.454  1.00 34.02  ? 401 LFA B C11 1 
HETATM 10817 C C1  . LFA N  2 .   ? 40.326  42.438 -12.982 1.00 66.70  ? 402 LFA B C1  1 
HETATM 10818 C C2  . LFA N  2 .   ? 39.102  42.687 -12.130 1.00 69.72  ? 402 LFA B C2  1 
HETATM 10819 C C3  . LFA N  2 .   ? 37.972  41.716 -12.377 1.00 76.98  ? 402 LFA B C3  1 
HETATM 10820 C C4  . LFA N  2 .   ? 37.638  40.818 -11.207 1.00 80.60  ? 402 LFA B C4  1 
HETATM 10821 C C5  . LFA N  2 .   ? 36.695  39.681 -11.538 1.00 81.09  ? 402 LFA B C5  1 
HETATM 10822 C C6  . LFA N  2 .   ? 36.967  38.402 -10.777 1.00 79.50  ? 402 LFA B C6  1 
HETATM 10823 C C7  . LFA N  2 .   ? 35.759  37.506 -10.601 1.00 78.73  ? 402 LFA B C7  1 
HETATM 10824 C C8  . LFA N  2 .   ? 35.336  37.296 -9.163  1.00 68.25  ? 402 LFA B C8  1 
HETATM 10825 C C9  . LFA N  2 .   ? 35.059  35.854 -8.795  1.00 61.12  ? 402 LFA B C9  1 
HETATM 10826 C C10 . LFA N  2 .   ? 35.861  35.347 -7.614  1.00 56.50  ? 402 LFA B C10 1 
HETATM 10827 C C11 . LFA N  2 .   ? 35.115  34.378 -6.716  1.00 53.73  ? 402 LFA B C11 1 
HETATM 10828 C C12 . LFA N  2 .   ? 35.360  34.574 -5.231  1.00 44.10  ? 402 LFA B C12 1 
HETATM 10829 P P   . PO4 O  3 .   ? 38.510  25.481 -8.435  1.00 102.81 ? 403 PO4 B P   1 
HETATM 10830 O O1  . PO4 O  3 .   ? 37.889  25.521 -9.829  1.00 92.00  ? 403 PO4 B O1  1 
HETATM 10831 O O2  . PO4 O  3 .   ? 40.029  25.410 -8.555  1.00 90.10  ? 403 PO4 B O2  1 
HETATM 10832 O O3  . PO4 O  3 .   ? 38.002  24.253 -7.689  1.00 92.60  ? 403 PO4 B O3  1 
HETATM 10833 O O4  . PO4 O  3 .   ? 38.119  26.738 -7.667  1.00 103.92 ? 403 PO4 B O4  1 
HETATM 10834 C C1  . RET P  4 .   ? 43.246  50.617 11.009  1.00 55.43  ? 404 RET B C1  1 
HETATM 10835 C C2  . RET P  4 .   ? 43.707  51.830 11.819  1.00 53.88  ? 404 RET B C2  1 
HETATM 10836 C C3  . RET P  4 .   ? 45.179  51.890 12.004  1.00 56.12  ? 404 RET B C3  1 
HETATM 10837 C C4  . RET P  4 .   ? 45.686  50.646 12.719  1.00 58.08  ? 404 RET B C4  1 
HETATM 10838 C C5  . RET P  4 .   ? 45.004  49.378 12.293  1.00 59.88  ? 404 RET B C5  1 
HETATM 10839 C C6  . RET P  4 .   ? 44.023  49.360 11.369  1.00 59.78  ? 404 RET B C6  1 
HETATM 10840 C C7  . RET P  4 .   ? 43.661  48.128 10.714  1.00 57.51  ? 404 RET B C7  1 
HETATM 10841 C C8  . RET P  4 .   ? 42.770  47.981 9.693   1.00 58.64  ? 404 RET B C8  1 
HETATM 10842 C C9  . RET P  4 .   ? 42.538  46.829 8.944   1.00 62.57  ? 404 RET B C9  1 
HETATM 10843 C C10 . RET P  4 .   ? 41.573  46.797 7.921   1.00 59.21  ? 404 RET B C10 1 
HETATM 10844 C C11 . RET P  4 .   ? 41.214  45.742 7.104   1.00 56.22  ? 404 RET B C11 1 
HETATM 10845 C C12 . RET P  4 .   ? 40.205  45.700 6.161   1.00 53.11  ? 404 RET B C12 1 
HETATM 10846 C C13 . RET P  4 .   ? 39.791  44.600 5.367   1.00 56.90  ? 404 RET B C13 1 
HETATM 10847 C C14 . RET P  4 .   ? 38.718  44.709 4.533   1.00 60.03  ? 404 RET B C14 1 
HETATM 10848 C C15 . RET P  4 .   ? 38.273  43.619 3.585   1.00 65.97  ? 404 RET B C15 1 
HETATM 10849 C C16 . RET P  4 .   ? 41.747  50.409 11.284  1.00 57.65  ? 404 RET B C16 1 
HETATM 10850 C C17 . RET P  4 .   ? 43.432  50.943 9.517   1.00 50.92  ? 404 RET B C17 1 
HETATM 10851 C C18 . RET P  4 .   ? 45.546  48.155 12.980  1.00 61.94  ? 404 RET B C18 1 
HETATM 10852 C C19 . RET P  4 .   ? 43.305  45.582 9.203   1.00 60.33  ? 404 RET B C19 1 
HETATM 10853 C C20 . RET P  4 .   ? 40.576  43.365 5.493   1.00 58.65  ? 404 RET B C20 1 
HETATM 10854 C C1  . LFA Q  2 .   ? 28.426  58.964 -13.346 1.00 55.28  ? 401 LFA C C1  1 
HETATM 10855 C C2  . LFA Q  2 .   ? 27.233  58.033 -13.296 1.00 57.07  ? 401 LFA C C2  1 
HETATM 10856 C C3  . LFA Q  2 .   ? 26.277  58.298 -12.154 1.00 50.01  ? 401 LFA C C3  1 
HETATM 10857 C C4  . LFA Q  2 .   ? 25.650  57.053 -11.557 1.00 40.74  ? 401 LFA C C4  1 
HETATM 10858 C C5  . LFA Q  2 .   ? 24.727  57.313 -10.384 1.00 34.13  ? 401 LFA C C5  1 
HETATM 10859 C C6  . LFA Q  2 .   ? 24.249  56.062 -9.678  1.00 30.43  ? 401 LFA C C6  1 
HETATM 10860 P P   . PO4 R  3 .   ? 19.018  24.082 -25.770 1.00 117.90 ? 402 PO4 C P   1 
HETATM 10861 O O1  . PO4 R  3 .   ? 17.899  24.717 -26.588 1.00 102.84 ? 402 PO4 C O1  1 
HETATM 10862 O O2  . PO4 R  3 .   ? 20.339  24.216 -26.521 1.00 106.33 ? 402 PO4 C O2  1 
HETATM 10863 O O3  . PO4 R  3 .   ? 18.703  22.609 -25.547 1.00 113.97 ? 402 PO4 C O3  1 
HETATM 10864 O O4  . PO4 R  3 .   ? 19.128  24.787 -24.422 1.00 124.74 ? 402 PO4 C O4  1 
HETATM 10865 C C1  . LFA S  2 .   ? 18.413  52.773 -9.890  1.00 59.54  ? 403 LFA C C1  1 
HETATM 10866 C C2  . LFA S  2 .   ? 19.341  53.960 -10.041 1.00 62.02  ? 403 LFA C C2  1 
HETATM 10867 C C3  . LFA S  2 .   ? 18.696  55.292 -9.729  1.00 60.45  ? 403 LFA C C3  1 
HETATM 10868 C C4  . LFA S  2 .   ? 19.617  56.490 -9.853  1.00 54.28  ? 403 LFA C C4  1 
HETATM 10869 C C5  . LFA S  2 .   ? 18.955  57.818 -9.547  1.00 47.86  ? 403 LFA C C5  1 
HETATM 10870 C C6  . LFA S  2 .   ? 19.848  59.027 -9.741  1.00 37.40  ? 403 LFA C C6  1 
HETATM 10871 C C1  . RET T  4 .   ? 40.334  48.337 -26.196 1.00 65.19  ? 404 RET C C1  1 
HETATM 10872 C C2  . RET T  4 .   ? 41.307  49.491 -26.455 1.00 62.88  ? 404 RET C C2  1 
HETATM 10873 C C3  . RET T  4 .   ? 41.929  49.448 -27.803 1.00 63.56  ? 404 RET C C3  1 
HETATM 10874 C C4  . RET T  4 .   ? 42.696  48.148 -28.007 1.00 61.14  ? 404 RET C C4  1 
HETATM 10875 C C5  . RET T  4 .   ? 42.021  46.945 -27.413 1.00 62.93  ? 404 RET C C5  1 
HETATM 10876 C C6  . RET T  4 .   ? 40.846  47.021 -26.758 1.00 64.84  ? 404 RET C C6  1 
HETATM 10877 C C7  . RET T  4 .   ? 40.050  45.836 -26.549 1.00 63.12  ? 404 RET C C7  1 
HETATM 10878 C C8  . RET T  4 .   ? 38.796  45.784 -26.020 1.00 63.90  ? 404 RET C C8  1 
HETATM 10879 C C9  . RET T  4 .   ? 37.949  44.680 -25.965 1.00 63.40  ? 404 RET C C9  1 
HETATM 10880 C C10 . RET T  4 .   ? 36.677  44.752 -25.363 1.00 64.81  ? 404 RET C C10 1 
HETATM 10881 C C11 . RET T  4 .   ? 35.723  43.763 -25.220 1.00 61.38  ? 404 RET C C11 1 
HETATM 10882 C C12 . RET T  4 .   ? 34.518  43.838 -24.544 1.00 58.69  ? 404 RET C C12 1 
HETATM 10883 C C13 . RET T  4 .   ? 33.567  42.810 -24.333 1.00 55.98  ? 404 RET C C13 1 
HETATM 10884 C C14 . RET T  4 .   ? 32.451  43.019 -23.578 1.00 57.31  ? 404 RET C C14 1 
HETATM 10885 C C15 . RET T  4 .   ? 31.334  42.010 -23.467 1.00 63.89  ? 404 RET C C15 1 
HETATM 10886 C C16 . RET T  4 .   ? 40.134  48.217 -24.676 1.00 68.31  ? 404 RET C C16 1 
HETATM 10887 C C17 . RET T  4 .   ? 38.986  48.701 -26.839 1.00 63.60  ? 404 RET C C17 1 
HETATM 10888 C C18 . RET T  4 .   ? 42.776  45.667 -27.650 1.00 67.17  ? 404 RET C C18 1 
HETATM 10889 C C19 . RET T  4 .   ? 38.368  43.380 -26.539 1.00 57.74  ? 404 RET C C19 1 
HETATM 10890 C C20 . RET T  4 .   ? 33.850  41.526 -24.977 1.00 54.95  ? 404 RET C C20 1 
HETATM 10891 C C1  . OLA U  5 .   ? -0.925  60.350 -10.676 1.00 92.28  ? 401 OLA D C1  1 
HETATM 10892 O O1  . OLA U  5 .   ? -2.045  60.377 -10.131 1.00 98.62  ? 401 OLA D O1  1 
HETATM 10893 O O2  . OLA U  5 .   ? -0.762  60.185 -11.901 1.00 92.46  ? 401 OLA D O2  1 
HETATM 10894 C C2  . OLA U  5 .   ? 0.307   60.517 -9.801  1.00 84.52  ? 401 OLA D C2  1 
HETATM 10895 C C3  . OLA U  5 .   ? 0.656   59.305 -8.992  1.00 76.02  ? 401 OLA D C3  1 
HETATM 10896 C C4  . OLA U  5 .   ? 1.551   59.617 -7.803  1.00 74.21  ? 401 OLA D C4  1 
HETATM 10897 C C5  . OLA U  5 .   ? 1.618   58.506 -6.778  1.00 73.51  ? 401 OLA D C5  1 
HETATM 10898 C C6  . OLA U  5 .   ? 2.726   58.648 -5.757  1.00 72.56  ? 401 OLA D C6  1 
HETATM 10899 C C7  . OLA U  5 .   ? 4.128   58.760 -6.344  1.00 71.67  ? 401 OLA D C7  1 
HETATM 10900 C C8  . OLA U  5 .   ? 4.533   57.605 -7.206  1.00 73.30  ? 401 OLA D C8  1 
HETATM 10901 C C9  . OLA U  5 .   ? 5.803   56.949 -6.765  1.00 78.59  ? 401 OLA D C9  1 
HETATM 10902 C C10 . OLA U  5 .   ? 6.959   57.035 -7.372  1.00 87.36  ? 401 OLA D C10 1 
HETATM 10903 C C11 . OLA U  5 .   ? 8.179   56.232 -7.040  1.00 95.57  ? 401 OLA D C11 1 
HETATM 10904 C C12 . OLA U  5 .   ? 8.750   55.501 -8.217  1.00 95.53  ? 401 OLA D C12 1 
HETATM 10905 C C13 . OLA U  5 .   ? 7.711   54.988 -9.201  1.00 89.67  ? 401 OLA D C13 1 
HETATM 10906 C C14 . OLA U  5 .   ? 8.088   53.695 -9.884  1.00 88.44  ? 401 OLA D C14 1 
HETATM 10907 C C15 . OLA U  5 .   ? 6.915   52.799 -10.215 1.00 86.56  ? 401 OLA D C15 1 
HETATM 10908 C C16 . OLA U  5 .   ? 6.769   51.596 -9.310  1.00 77.31  ? 401 OLA D C16 1 
HETATM 10909 C C17 . OLA U  5 .   ? 5.887   50.502 -9.859  1.00 73.26  ? 401 OLA D C17 1 
HETATM 10910 C C18 . OLA U  5 .   ? 5.963   49.204 -9.087  1.00 72.57  ? 401 OLA D C18 1 
HETATM 10911 P P   . PO4 V  3 .   ? -3.912  24.870 -12.610 1.00 99.86  ? 402 PO4 D P   1 
HETATM 10912 O O1  . PO4 V  3 .   ? -4.335  25.762 -13.775 1.00 92.89  ? 402 PO4 D O1  1 
HETATM 10913 O O2  . PO4 V  3 .   ? -2.616  24.152 -12.966 1.00 92.74  ? 402 PO4 D O2  1 
HETATM 10914 O O3  . PO4 V  3 .   ? -5.002  23.842 -12.332 1.00 96.19  ? 402 PO4 D O3  1 
HETATM 10915 O O4  . PO4 V  3 .   ? -3.694  25.725 -11.367 1.00 99.86  ? 402 PO4 D O4  1 
HETATM 10916 C C1  . LFA W  2 .   ? 15.743  60.779 -6.497  1.00 85.60  ? 403 LFA D C1  1 
HETATM 10917 C C2  . LFA W  2 .   ? 15.060  59.481 -6.128  1.00 89.61  ? 403 LFA D C2  1 
HETATM 10918 C C3  . LFA W  2 .   ? 15.955  58.266 -6.199  1.00 87.28  ? 403 LFA D C3  1 
HETATM 10919 C C4  . LFA W  2 .   ? 15.323  56.993 -5.679  1.00 89.37  ? 403 LFA D C4  1 
HETATM 10920 C C5  . LFA W  2 .   ? 16.168  55.749 -5.858  1.00 88.98  ? 403 LFA D C5  1 
HETATM 10921 C C6  . LFA W  2 .   ? 15.427  54.452 -5.608  1.00 86.01  ? 403 LFA D C6  1 
HETATM 10922 C C7  . LFA W  2 .   ? 16.233  53.200 -5.883  1.00 80.10  ? 403 LFA D C7  1 
HETATM 10923 C C8  . LFA W  2 .   ? 15.480  51.907 -5.643  1.00 70.72  ? 403 LFA D C8  1 
HETATM 10924 C C9  . LFA W  2 .   ? 16.357  50.673 -5.564  1.00 62.38  ? 403 LFA D C9  1 
HETATM 10925 C C10 . LFA W  2 .   ? 15.596  49.369 -5.432  1.00 44.29  ? 403 LFA D C10 1 
HETATM 10926 C C1  . LFA X  2 .   ? 14.554  56.452 -12.016 1.00 70.24  ? 404 LFA D C1  1 
HETATM 10927 C C2  . LFA X  2 .   ? 14.792  56.761 -10.555 1.00 75.48  ? 404 LFA D C2  1 
HETATM 10928 C C3  . LFA X  2 .   ? 13.739  56.206 -9.625  1.00 78.39  ? 404 LFA D C3  1 
HETATM 10929 C C4  . LFA X  2 .   ? 13.643  54.698 -9.613  1.00 82.55  ? 404 LFA D C4  1 
HETATM 10930 C C5  . LFA X  2 .   ? 12.573  54.148 -8.698  1.00 86.00  ? 404 LFA D C5  1 
HETATM 10931 C C6  . LFA X  2 .   ? 12.356  52.657 -8.822  1.00 86.08  ? 404 LFA D C6  1 
HETATM 10932 C C7  . LFA X  2 .   ? 11.529  52.049 -7.712  1.00 81.47  ? 404 LFA D C7  1 
HETATM 10933 C C8  . LFA X  2 .   ? 11.094  50.624 -7.971  1.00 76.89  ? 404 LFA D C8  1 
HETATM 10934 C C9  . LFA X  2 .   ? 10.361  49.970 -6.817  1.00 68.82  ? 404 LFA D C9  1 
HETATM 10935 C C10 . LFA X  2 .   ? 9.113   50.701 -6.366  1.00 56.81  ? 404 LFA D C10 1 
HETATM 10936 C C11 . LFA X  2 .   ? 7.959   49.794 -5.995  1.00 45.62  ? 404 LFA D C11 1 
HETATM 10937 C C1  . LFA Y  2 .   ? 16.067  33.182 -3.976  1.00 50.98  ? 405 LFA D C1  1 
HETATM 10938 C C2  . LFA Y  2 .   ? 16.241  31.873 -4.712  1.00 54.52  ? 405 LFA D C2  1 
HETATM 10939 C C3  . LFA Y  2 .   ? 16.218  30.653 -3.822  1.00 59.69  ? 405 LFA D C3  1 
HETATM 10940 C C4  . LFA Y  2 .   ? 16.204  29.330 -4.556  1.00 65.09  ? 405 LFA D C4  1 
HETATM 10941 C C5  . LFA Y  2 .   ? 16.217  28.112 -3.656  1.00 66.38  ? 405 LFA D C5  1 
HETATM 10942 C C6  . LFA Y  2 .   ? 16.504  26.807 -4.371  1.00 62.02  ? 405 LFA D C6  1 
HETATM 10943 C C7  . LFA Y  2 .   ? 16.336  25.567 -3.514  1.00 56.21  ? 405 LFA D C7  1 
HETATM 10944 C C8  . LFA Y  2 .   ? 17.635  24.912 -3.089  1.00 44.19  ? 405 LFA D C8  1 
HETATM 10945 C C1  . RET Z  4 .   ? 3.796   47.716 -34.437 1.00 72.48  ? 406 RET D C1  1 
HETATM 10946 C C2  . RET Z  4 .   ? 3.896   48.815 -35.497 1.00 73.48  ? 406 RET D C2  1 
HETATM 10947 C C3  . RET Z  4 .   ? 2.785   48.786 -36.484 1.00 72.47  ? 406 RET D C3  1 
HETATM 10948 C C4  . RET Z  4 .   ? 2.752   47.455 -37.219 1.00 68.96  ? 406 RET D C4  1 
HETATM 10949 C C5  . RET Z  4 .   ? 3.058   46.273 -36.345 1.00 69.70  ? 406 RET D C5  1 
HETATM 10950 C C6  . RET Z  4 .   ? 3.343   46.393 -35.033 1.00 68.45  ? 406 RET D C6  1 
HETATM 10951 C C7  . RET Z  4 .   ? 3.255   45.250 -34.160 1.00 59.78  ? 406 RET D C7  1 
HETATM 10952 C C8  . RET Z  4 .   ? 3.400   45.247 -32.807 1.00 59.05  ? 406 RET D C8  1 
HETATM 10953 C C9  . RET Z  4 .   ? 3.139   44.187 -31.941 1.00 64.43  ? 406 RET D C9  1 
HETATM 10954 C C10 . RET Z  4 .   ? 3.349   44.301 -30.554 1.00 63.53  ? 406 RET D C10 1 
HETATM 10955 C C11 . RET Z  4 .   ? 3.154   43.353 -29.569 1.00 60.41  ? 406 RET D C11 1 
HETATM 10956 C C12 . RET Z  4 .   ? 3.440   43.453 -28.220 1.00 58.63  ? 406 RET D C12 1 
HETATM 10957 C C13 . RET Z  4 .   ? 3.300   42.459 -27.218 1.00 61.39  ? 406 RET D C13 1 
HETATM 10958 C C14 . RET Z  4 .   ? 3.692   42.698 -25.934 1.00 61.14  ? 406 RET D C14 1 
HETATM 10959 C C15 . RET Z  4 .   ? 3.484   41.721 -24.798 1.00 63.19  ? 406 RET D C15 1 
HETATM 10960 C C16 . RET Z  4 .   ? 5.182   47.558 -33.789 1.00 73.19  ? 406 RET D C16 1 
HETATM 10961 C C17 . RET Z  4 .   ? 2.801   48.180 -33.361 1.00 69.22  ? 406 RET D C17 1 
HETATM 10962 C C18 . RET Z  4 .   ? 2.992   44.964 -37.081 1.00 75.67  ? 406 RET D C18 1 
HETATM 10963 C C19 . RET Z  4 .   ? 2.630   42.886 -32.455 1.00 63.98  ? 406 RET D C19 1 
HETATM 10964 C C20 . RET Z  4 .   ? 2.710   41.184 -27.641 1.00 61.54  ? 406 RET D C20 1 
HETATM 10965 C C1  . LFA AA 2 .   ? -6.924  60.518 16.347  1.00 49.43  ? 401 LFA E C1  1 
HETATM 10966 C C2  . LFA AA 2 .   ? -8.346  60.268 15.900  1.00 51.89  ? 401 LFA E C2  1 
HETATM 10967 C C3  . LFA AA 2 .   ? -8.495  59.189 14.850  1.00 53.22  ? 401 LFA E C3  1 
HETATM 10968 C C4  . LFA AA 2 .   ? -8.405  57.761 15.351  1.00 52.44  ? 401 LFA E C4  1 
HETATM 10969 C C5  . LFA AA 2 .   ? -9.155  56.755 14.499  1.00 51.43  ? 401 LFA E C5  1 
HETATM 10970 C C6  . LFA AA 2 .   ? -8.773  55.311 14.743  1.00 49.99  ? 401 LFA E C6  1 
HETATM 10971 C C7  . LFA AA 2 .   ? -9.492  54.316 13.856  1.00 47.61  ? 401 LFA E C7  1 
HETATM 10972 C C8  . LFA AA 2 .   ? -9.122  52.869 14.109  1.00 44.97  ? 401 LFA E C8  1 
HETATM 10973 C C9  . LFA AA 2 .   ? -10.124 51.863 13.577  1.00 42.19  ? 401 LFA E C9  1 
HETATM 10974 C C10 . LFA AA 2 .   ? -9.781  50.416 13.875  1.00 38.68  ? 401 LFA E C10 1 
HETATM 10975 C C11 . LFA AA 2 .   ? -10.765 49.408 13.313  1.00 33.28  ? 401 LFA E C11 1 
HETATM 10976 P P   . PO4 BA 3 .   ? 1.068   26.009 12.189  1.00 105.37 ? 402 PO4 E P   1 
HETATM 10977 O O1  . PO4 BA 3 .   ? 0.345   25.988 10.845  1.00 92.12  ? 402 PO4 E O1  1 
HETATM 10978 O O2  . PO4 BA 3 .   ? 1.585   27.416 12.470  1.00 88.65  ? 402 PO4 E O2  1 
HETATM 10979 O O3  . PO4 BA 3 .   ? 2.241   25.036 12.152  1.00 91.03  ? 402 PO4 E O3  1 
HETATM 10980 O O4  . PO4 BA 3 .   ? 0.102   25.596 13.292  1.00 104.46 ? 402 PO4 E O4  1 
HETATM 10981 C C8  . LFA CA 2 .   ? 12.532  51.275 2.417   1.00 77.81  ? 403 LFA E C8  1 
HETATM 10982 C C9  . LFA CA 2 .   ? 12.524  50.121 1.444   1.00 82.65  ? 403 LFA E C9  1 
HETATM 10983 C C10 . LFA CA 2 .   ? 12.912  50.492 0.032   1.00 89.62  ? 403 LFA E C10 1 
HETATM 10984 C C11 . LFA CA 2 .   ? 12.394  51.837 -0.423  1.00 96.18  ? 403 LFA E C11 1 
HETATM 10985 C C12 . LFA CA 2 .   ? 12.377  52.027 -1.924  1.00 98.39  ? 403 LFA E C12 1 
HETATM 10986 C C13 . LFA CA 2 .   ? 11.448  53.123 -2.397  1.00 96.40  ? 403 LFA E C13 1 
HETATM 10987 C C14 . LFA CA 2 .   ? 11.725  53.617 -3.796  1.00 88.75  ? 403 LFA E C14 1 
HETATM 10988 C C15 . LFA CA 2 .   ? 10.879  54.796 -4.215  1.00 80.96  ? 403 LFA E C15 1 
HETATM 10989 C C16 . LFA CA 2 .   ? 11.532  56.143 -4.003  1.00 79.22  ? 403 LFA E C16 1 
HETATM 10990 C C17 . LFA CA 2 .   ? 10.856  57.278 -4.737  1.00 79.14  ? 403 LFA E C17 1 
HETATM 10991 C C18 . LFA CA 2 .   ? 11.187  58.656 -4.210  1.00 78.84  ? 403 LFA E C18 1 
HETATM 10992 C C19 . LFA CA 2 .   ? 10.343  59.762 -4.802  1.00 77.22  ? 403 LFA E C19 1 
HETATM 10993 C C20 . LFA CA 2 .   ? 10.902  61.153 -4.600  1.00 70.50  ? 403 LFA E C20 1 
HETATM 10994 C C1  . RET DA 4 .   ? -15.529 49.286 -2.734  1.00 65.88  ? 404 RET E C1  1 
HETATM 10995 C C2  . RET DA 4 .   ? -16.446 50.412 -3.218  1.00 72.10  ? 404 RET E C2  1 
HETATM 10996 C C3  . RET DA 4 .   ? -17.748 50.460 -2.507  1.00 77.24  ? 404 RET E C3  1 
HETATM 10997 C C4  . RET DA 4 .   ? -18.507 49.151 -2.683  1.00 78.37  ? 404 RET E C4  1 
HETATM 10998 C C5  . RET DA 4 .   ? -17.634 47.930 -2.640  1.00 75.80  ? 404 RET E C5  1 
HETATM 10999 C C6  . RET DA 4 .   ? -16.298 48.001 -2.473  1.00 73.09  ? 404 RET E C6  1 
HETATM 11000 C C7  . RET DA 4 .   ? -15.553 46.838 -2.059  1.00 76.64  ? 404 RET E C7  1 
HETATM 11001 C C8  . RET DA 4 .   ? -14.236 46.793 -1.710  1.00 72.79  ? 404 RET E C8  1 
HETATM 11002 C C9  . RET DA 4 .   ? -13.560 45.712 -1.145  1.00 71.27  ? 404 RET E C9  1 
HETATM 11003 C C10 . RET DA 4 .   ? -12.182 45.761 -0.876  1.00 70.25  ? 404 RET E C10 1 
HETATM 11004 C C11 . RET DA 4 .   ? -11.366 44.780 -0.343  1.00 71.87  ? 404 RET E C11 1 
HETATM 11005 C C12 . RET DA 4 .   ? -9.995  44.823 -0.168  1.00 74.46  ? 404 RET E C12 1 
HETATM 11006 C C13 . RET DA 4 .   ? -9.138  43.808 0.331   1.00 72.19  ? 404 RET E C13 1 
HETATM 11007 C C14 . RET DA 4 .   ? -7.788  43.993 0.373   1.00 71.70  ? 404 RET E C14 1 
HETATM 11008 C C15 . RET DA 4 .   ? -6.821  42.993 0.962   1.00 78.47  ? 404 RET E C15 1 
HETATM 11009 C C16 . RET DA 4 .   ? -14.460 49.054 -3.814  1.00 61.38  ? 404 RET E C16 1 
HETATM 11010 C C17 . RET DA 4 .   ? -14.835 49.758 -1.446  1.00 62.77  ? 404 RET E C17 1 
HETATM 11011 C C18 . RET DA 4 .   ? -18.408 46.646 -2.766  1.00 78.68  ? 404 RET E C18 1 
HETATM 11012 C C19 . RET DA 4 .   ? -14.277 44.456 -0.808  1.00 75.03  ? 404 RET E C19 1 
HETATM 11013 C C20 . RET DA 4 .   ? -9.783  42.576 0.792   1.00 74.23  ? 404 RET E C20 1 
HETATM 11014 O O   . HOH EA 6 .   ? 3.206   63.217 25.064  1.00 56.69  ? 501 HOH A O   1 
HETATM 11015 O O   . HOH EA 6 .   ? 24.194  27.642 12.225  1.00 52.54  ? 502 HOH A O   1 
HETATM 11016 O O   . HOH EA 6 .   ? 21.666  64.609 8.167   1.00 26.20  ? 503 HOH A O   1 
HETATM 11017 O O   . HOH EA 6 .   ? 17.068  64.588 25.187  1.00 66.79  ? 504 HOH A O   1 
HETATM 11018 O O   . HOH FA 6 .   ? 36.015  69.000 -13.421 1.00 26.84  ? 501 HOH B O   1 
HETATM 11019 O O   . HOH FA 6 .   ? 40.304  65.228 -0.861  1.00 56.76  ? 502 HOH B O   1 
HETATM 11020 O O   . HOH FA 6 .   ? 35.768  56.830 -13.878 1.00 42.34  ? 503 HOH B O   1 
HETATM 11021 O O   . HOH FA 6 .   ? 41.610  16.070 -0.406  1.00 46.45  ? 504 HOH B O   1 
HETATM 11022 O O   . HOH FA 6 .   ? 41.717  63.438 15.051  1.00 66.38  ? 505 HOH B O   1 
HETATM 11023 O O   . HOH FA 6 .   ? 29.572  58.266 9.619   1.00 42.81  ? 506 HOH B O   1 
HETATM 11024 O O   . HOH FA 6 .   ? 32.002  63.951 -7.389  1.00 32.77  ? 507 HOH B O   1 
HETATM 11025 O O   . HOH FA 6 .   ? 46.413  63.574 2.814   1.00 27.19  ? 508 HOH B O   1 
HETATM 11026 O O   . HOH FA 6 .   ? 36.072  70.024 -16.840 1.00 37.07  ? 509 HOH B O   1 
HETATM 11027 O O   . HOH GA 6 .   ? 44.725  60.955 -24.066 1.00 40.96  ? 501 HOH C O   1 
HETATM 11028 O O   . HOH GA 6 .   ? 22.295  9.941  -14.546 1.00 21.59  ? 502 HOH C O   1 
HETATM 11029 O O   . HOH GA 6 .   ? 20.084  63.200 -21.707 1.00 35.39  ? 503 HOH C O   1 
HETATM 11030 O O   . HOH GA 6 .   ? 33.642  61.479 -32.573 1.00 44.58  ? 504 HOH C O   1 
HETATM 11031 O O   . HOH GA 6 .   ? 29.811  1.734  1.873   1.00 30.04  ? 505 HOH C O   1 
HETATM 11032 O O   . HOH GA 6 .   ? 27.688  28.806 -19.265 1.00 36.96  ? 506 HOH C O   1 
HETATM 11033 O O   . HOH HA 6 .   ? -0.468  63.433 -24.504 1.00 55.58  ? 501 HOH D O   1 
HETATM 11034 O O   . HOH HA 6 .   ? 8.047   59.987 -38.523 1.00 54.51  ? 502 HOH D O   1 
HETATM 11035 O O   . HOH HA 6 .   ? 6.712   28.088 -14.321 1.00 56.84  ? 503 HOH D O   1 
HETATM 11036 O O   . HOH HA 6 .   ? 5.791   28.235 -18.480 1.00 51.61  ? 504 HOH D O   1 
HETATM 11037 O O   . HOH HA 6 .   ? 14.285  56.235 -26.538 1.00 56.08  ? 505 HOH D O   1 
HETATM 11038 O O   . HOH HA 6 .   ? 0.418   26.386 -13.190 1.00 46.77  ? 506 HOH D O   1 
HETATM 11039 O O   . HOH HA 6 .   ? -3.454  61.764 -30.274 1.00 67.37  ? 507 HOH D O   1 
HETATM 11040 O O   . HOH IA 6 .   ? -17.396 61.796 -8.048  1.00 102.68 ? 501 HOH E O   1 
HETATM 11041 O O   . HOH IA 6 .   ? 3.471   64.257 4.119   1.00 42.33  ? 502 HOH E O   1 
HETATM 11042 O O   . HOH IA 6 .   ? -3.961  57.374 -10.255 1.00 51.28  ? 503 HOH E O   1 
HETATM 11043 O O   . HOH IA 6 .   ? -1.775  29.154 0.906   1.00 55.14  ? 504 HOH E O   1 
HETATM 11044 O O   . HOH IA 6 .   ? -13.320 63.366 5.122   1.00 40.43  ? 505 HOH E O   1 
# 
