data_8ZRO
# 
_entry.id   8ZRO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8ZRO         pdb_00008zro 10.2210/pdb8zro/pdb 
WWPDB D_1300048425 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZRO 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8ZR6 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              stefan.arold@kaust.edu.sa 
_pdbx_contact_author.name_first         Stefan 
_pdbx_contact_author.name_last          Arold 
_pdbx_contact_author.name_mi            T. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5278-0668 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Arold, S.T.'    1 ? 
'Hameed, U.F.S.' 2 ? 
# 
_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                     'Arabidopsis Carboxylesterase CXE15' 
_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 'Arold, S.T.'    1 ? 
primary 'Hameed, U.F.S.' 2 ? 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Strigolactones hydrolase CXE15' 
_entity.formula_weight             35835.363 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    3.1.1.- 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carboxylesterase 15,AtCXE15' 
# 
_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       
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSELLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSELLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   VAL n 
1 3   ALA n 
1 4   GLU n 
1 5   ASP n 
1 6   CYS n 
1 7   MET n 
1 8   GLY n 
1 9   LEU n 
1 10  LEU n 
1 11  GLN n 
1 12  LEU n 
1 13  LEU n 
1 14  SER n 
1 15  ASN n 
1 16  GLY n 
1 17  THR n 
1 18  VAL n 
1 19  LEU n 
1 20  ARG n 
1 21  SER n 
1 22  GLU n 
1 23  SER n 
1 24  ILE n 
1 25  ASP n 
1 26  LEU n 
1 27  ILE n 
1 28  THR n 
1 29  GLN n 
1 30  GLN n 
1 31  ILE n 
1 32  PRO n 
1 33  PHE n 
1 34  LYS n 
1 35  ASN n 
1 36  ASN n 
1 37  GLN n 
1 38  THR n 
1 39  VAL n 
1 40  LEU n 
1 41  PHE n 
1 42  LYS n 
1 43  ASP n 
1 44  SER n 
1 45  ILE n 
1 46  TYR n 
1 47  HIS n 
1 48  LYS n 
1 49  PRO n 
1 50  ASN n 
1 51  ASN n 
1 52  LEU n 
1 53  HIS n 
1 54  LEU n 
1 55  ARG n 
1 56  LEU n 
1 57  TYR n 
1 58  LYS n 
1 59  PRO n 
1 60  ILE n 
1 61  SER n 
1 62  ALA n 
1 63  SER n 
1 64  ASN n 
1 65  ARG n 
1 66  THR n 
1 67  ALA n 
1 68  LEU n 
1 69  PRO n 
1 70  VAL n 
1 71  VAL n 
1 72  VAL n 
1 73  PHE n 
1 74  PHE n 
1 75  HIS n 
1 76  GLY n 
1 77  GLY n 
1 78  GLY n 
1 79  PHE n 
1 80  CYS n 
1 81  PHE n 
1 82  GLY n 
1 83  SER n 
1 84  ARG n 
1 85  SER n 
1 86  TRP n 
1 87  PRO n 
1 88  HIS n 
1 89  PHE n 
1 90  HIS n 
1 91  ASN n 
1 92  PHE n 
1 93  CYS n 
1 94  LEU n 
1 95  THR n 
1 96  LEU n 
1 97  ALA n 
1 98  SER n 
1 99  SER n 
1 100 LEU n 
1 101 ASN n 
1 102 ALA n 
1 103 LEU n 
1 104 VAL n 
1 105 VAL n 
1 106 SER n 
1 107 PRO n 
1 108 ASP n 
1 109 TYR n 
1 110 ARG n 
1 111 LEU n 
1 112 ALA n 
1 113 PRO n 
1 114 GLU n 
1 115 HIS n 
1 116 ARG n 
1 117 LEU n 
1 118 PRO n 
1 119 ALA n 
1 120 ALA n 
1 121 PHE n 
1 122 GLU n 
1 123 ASP n 
1 124 ALA n 
1 125 GLU n 
1 126 ALA n 
1 127 VAL n 
1 128 LEU n 
1 129 THR n 
1 130 TRP n 
1 131 LEU n 
1 132 TRP n 
1 133 ASP n 
1 134 GLN n 
1 135 ALA n 
1 136 VAL n 
1 137 SER n 
1 138 ASP n 
1 139 GLY n 
1 140 VAL n 
1 141 ASN n 
1 142 HIS n 
1 143 TRP n 
1 144 PHE n 
1 145 GLU n 
1 146 ASP n 
1 147 GLY n 
1 148 THR n 
1 149 ASP n 
1 150 VAL n 
1 151 ASP n 
1 152 PHE n 
1 153 ASP n 
1 154 ARG n 
1 155 VAL n 
1 156 PHE n 
1 157 VAL n 
1 158 VAL n 
1 159 GLY n 
1 160 ASP n 
1 161 SER n 
1 162 SER n 
1 163 GLY n 
1 164 GLY n 
1 165 ASN n 
1 166 ILE n 
1 167 ALA n 
1 168 HIS n 
1 169 GLN n 
1 170 LEU n 
1 171 ALA n 
1 172 VAL n 
1 173 ARG n 
1 174 PHE n 
1 175 GLY n 
1 176 SER n 
1 177 GLY n 
1 178 SER n 
1 179 ILE n 
1 180 GLU n 
1 181 LEU n 
1 182 THR n 
1 183 PRO n 
1 184 VAL n 
1 185 ARG n 
1 186 VAL n 
1 187 ARG n 
1 188 GLY n 
1 189 TYR n 
1 190 VAL n 
1 191 LEU n 
1 192 MET n 
1 193 GLY n 
1 194 PRO n 
1 195 PHE n 
1 196 PHE n 
1 197 GLY n 
1 198 GLY n 
1 199 GLU n 
1 200 GLU n 
1 201 ARG n 
1 202 THR n 
1 203 ASN n 
1 204 SER n 
1 205 GLU n 
1 206 ASN n 
1 207 GLY n 
1 208 PRO n 
1 209 SER n 
1 210 GLU n 
1 211 ALA n 
1 212 LEU n 
1 213 LEU n 
1 214 SER n 
1 215 LEU n 
1 216 ASP n 
1 217 LEU n 
1 218 LEU n 
1 219 ASP n 
1 220 LYS n 
1 221 PHE n 
1 222 TRP n 
1 223 ARG n 
1 224 LEU n 
1 225 SER n 
1 226 LEU n 
1 227 PRO n 
1 228 ASN n 
1 229 GLY n 
1 230 ALA n 
1 231 THR n 
1 232 ARG n 
1 233 ASP n 
1 234 HIS n 
1 235 HIS n 
1 236 MET n 
1 237 ALA n 
1 238 ASN n 
1 239 PRO n 
1 240 PHE n 
1 241 GLY n 
1 242 PRO n 
1 243 THR n 
1 244 SER n 
1 245 PRO n 
1 246 THR n 
1 247 LEU n 
1 248 GLU n 
1 249 SER n 
1 250 ILE n 
1 251 SER n 
1 252 LEU n 
1 253 GLU n 
1 254 PRO n 
1 255 MET n 
1 256 LEU n 
1 257 VAL n 
1 258 ILE n 
1 259 VAL n 
1 260 GLY n 
1 261 GLY n 
1 262 SER n 
1 263 GLU n 
1 264 LEU n 
1 265 LEU n 
1 266 ARG n 
1 267 ASP n 
1 268 ARG n 
1 269 ALA n 
1 270 LYS n 
1 271 GLU n 
1 272 TYR n 
1 273 ALA n 
1 274 TYR n 
1 275 LYS n 
1 276 LEU n 
1 277 LYS n 
1 278 LYS n 
1 279 MET n 
1 280 GLY n 
1 281 GLY n 
1 282 LYS n 
1 283 ARG n 
1 284 VAL n 
1 285 ASP n 
1 286 TYR n 
1 287 ILE n 
1 288 GLU n 
1 289 PHE n 
1 290 GLU n 
1 291 ASN n 
1 292 LYS n 
1 293 GLU n 
1 294 HIS n 
1 295 GLY n 
1 296 PHE n 
1 297 TYR n 
1 298 SER n 
1 299 ASN n 
1 300 TYR n 
1 301 PRO n 
1 302 SER n 
1 303 SER n 
1 304 GLU n 
1 305 ALA n 
1 306 ALA n 
1 307 GLU n 
1 308 GLN n 
1 309 VAL n 
1 310 LEU n 
1 311 ARG n 
1 312 ILE n 
1 313 ILE n 
1 314 GLY n 
1 315 ASP n 
1 316 PHE n 
1 317 MET n 
1 318 ASN n 
1 319 ASN n 
1 320 LEU n 
1 321 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   321 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CXE15, At5g06570, F15M7.10' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   9   ?   ?   ?   A . n 
A 1 2   VAL 2   10  ?   ?   ?   A . n 
A 1 3   ALA 3   11  11  ALA ALA A . n 
A 1 4   GLU 4   12  12  GLU GLU A . n 
A 1 5   ASP 5   13  13  ASP ASP A . n 
A 1 6   CYS 6   14  14  CYS CYS A . n 
A 1 7   MET 7   15  15  MET MET A . n 
A 1 8   GLY 8   16  16  GLY GLY A . n 
A 1 9   LEU 9   17  17  LEU LEU A . n 
A 1 10  LEU 10  18  18  LEU LEU A . n 
A 1 11  GLN 11  19  19  GLN GLN A . n 
A 1 12  LEU 12  20  20  LEU LEU A . n 
A 1 13  LEU 13  21  21  LEU LEU A . n 
A 1 14  SER 14  22  22  SER SER A . n 
A 1 15  ASN 15  23  23  ASN ASN A . n 
A 1 16  GLY 16  24  24  GLY GLY A . n 
A 1 17  THR 17  25  25  THR THR A . n 
A 1 18  VAL 18  26  26  VAL VAL A . n 
A 1 19  LEU 19  27  27  LEU LEU A . n 
A 1 20  ARG 20  28  28  ARG ARG A . n 
A 1 21  SER 21  29  29  SER SER A . n 
A 1 22  GLU 22  30  ?   ?   ?   A . n 
A 1 23  SER 23  31  ?   ?   ?   A . n 
A 1 24  ILE 24  32  ?   ?   ?   A . n 
A 1 25  ASP 25  33  ?   ?   ?   A . n 
A 1 26  LEU 26  34  ?   ?   ?   A . n 
A 1 27  ILE 27  35  ?   ?   ?   A . n 
A 1 28  THR 28  36  ?   ?   ?   A . n 
A 1 29  GLN 29  37  ?   ?   ?   A . n 
A 1 30  GLN 30  38  ?   ?   ?   A . n 
A 1 31  ILE 31  39  ?   ?   ?   A . n 
A 1 32  PRO 32  40  ?   ?   ?   A . n 
A 1 33  PHE 33  41  ?   ?   ?   A . n 
A 1 34  LYS 34  42  ?   ?   ?   A . n 
A 1 35  ASN 35  43  43  ASN ASN A . n 
A 1 36  ASN 36  44  44  ASN ASN A . n 
A 1 37  GLN 37  45  45  GLN GLN A . n 
A 1 38  THR 38  46  46  THR THR A . n 
A 1 39  VAL 39  47  47  VAL VAL A . n 
A 1 40  LEU 40  48  48  LEU LEU A . n 
A 1 41  PHE 41  49  49  PHE PHE A . n 
A 1 42  LYS 42  50  50  LYS LYS A . n 
A 1 43  ASP 43  51  51  ASP ASP A . n 
A 1 44  SER 44  52  52  SER SER A . n 
A 1 45  ILE 45  53  53  ILE ILE A . n 
A 1 46  TYR 46  54  54  TYR TYR A . n 
A 1 47  HIS 47  55  55  HIS HIS A . n 
A 1 48  LYS 48  56  56  LYS LYS A . n 
A 1 49  PRO 49  57  57  PRO PRO A . n 
A 1 50  ASN 50  58  58  ASN ASN A . n 
A 1 51  ASN 51  59  59  ASN ASN A . n 
A 1 52  LEU 52  60  60  LEU LEU A . n 
A 1 53  HIS 53  61  61  HIS HIS A . n 
A 1 54  LEU 54  62  62  LEU LEU A . n 
A 1 55  ARG 55  63  63  ARG ARG A . n 
A 1 56  LEU 56  64  64  LEU LEU A . n 
A 1 57  TYR 57  65  65  TYR TYR A . n 
A 1 58  LYS 58  66  66  LYS LYS A . n 
A 1 59  PRO 59  67  67  PRO PRO A . n 
A 1 60  ILE 60  68  68  ILE ILE A . n 
A 1 61  SER 61  69  69  SER SER A . n 
A 1 62  ALA 62  70  70  ALA ALA A . n 
A 1 63  SER 63  71  71  SER SER A . n 
A 1 64  ASN 64  72  72  ASN ASN A . n 
A 1 65  ARG 65  73  73  ARG ARG A . n 
A 1 66  THR 66  74  74  THR THR A . n 
A 1 67  ALA 67  75  75  ALA ALA A . n 
A 1 68  LEU 68  76  76  LEU LEU A . n 
A 1 69  PRO 69  77  77  PRO PRO A . n 
A 1 70  VAL 70  78  78  VAL VAL A . n 
A 1 71  VAL 71  79  79  VAL VAL A . n 
A 1 72  VAL 72  80  80  VAL VAL A . n 
A 1 73  PHE 73  81  81  PHE PHE A . n 
A 1 74  PHE 74  82  82  PHE PHE A . n 
A 1 75  HIS 75  83  83  HIS HIS A . n 
A 1 76  GLY 76  84  84  GLY GLY A . n 
A 1 77  GLY 77  85  85  GLY GLY A . n 
A 1 78  GLY 78  86  86  GLY GLY A . n 
A 1 79  PHE 79  87  87  PHE PHE A . n 
A 1 80  CYS 80  88  88  CYS CYS A . n 
A 1 81  PHE 81  89  89  PHE PHE A . n 
A 1 82  GLY 82  90  90  GLY GLY A . n 
A 1 83  SER 83  91  91  SER SER A . n 
A 1 84  ARG 84  92  92  ARG ARG A . n 
A 1 85  SER 85  93  93  SER SER A . n 
A 1 86  TRP 86  94  94  TRP TRP A . n 
A 1 87  PRO 87  95  95  PRO PRO A . n 
A 1 88  HIS 88  96  96  HIS HIS A . n 
A 1 89  PHE 89  97  97  PHE PHE A . n 
A 1 90  HIS 90  98  98  HIS HIS A . n 
A 1 91  ASN 91  99  99  ASN ASN A . n 
A 1 92  PHE 92  100 100 PHE PHE A . n 
A 1 93  CYS 93  101 101 CYS CYS A . n 
A 1 94  LEU 94  102 102 LEU LEU A . n 
A 1 95  THR 95  103 103 THR THR A . n 
A 1 96  LEU 96  104 104 LEU LEU A . n 
A 1 97  ALA 97  105 105 ALA ALA A . n 
A 1 98  SER 98  106 106 SER SER A . n 
A 1 99  SER 99  107 107 SER SER A . n 
A 1 100 LEU 100 108 108 LEU LEU A . n 
A 1 101 ASN 101 109 109 ASN ASN A . n 
A 1 102 ALA 102 110 110 ALA ALA A . n 
A 1 103 LEU 103 111 111 LEU LEU A . n 
A 1 104 VAL 104 112 112 VAL VAL A . n 
A 1 105 VAL 105 113 113 VAL VAL A . n 
A 1 106 SER 106 114 114 SER SER A . n 
A 1 107 PRO 107 115 115 PRO PRO A . n 
A 1 108 ASP 108 116 116 ASP ASP A . n 
A 1 109 TYR 109 117 117 TYR TYR A . n 
A 1 110 ARG 110 118 118 ARG ARG A . n 
A 1 111 LEU 111 119 119 LEU LEU A . n 
A 1 112 ALA 112 120 120 ALA ALA A . n 
A 1 113 PRO 113 121 121 PRO PRO A . n 
A 1 114 GLU 114 122 122 GLU GLU A . n 
A 1 115 HIS 115 123 123 HIS HIS A . n 
A 1 116 ARG 116 124 124 ARG ARG A . n 
A 1 117 LEU 117 125 125 LEU LEU A . n 
A 1 118 PRO 118 126 126 PRO PRO A . n 
A 1 119 ALA 119 127 127 ALA ALA A . n 
A 1 120 ALA 120 128 128 ALA ALA A . n 
A 1 121 PHE 121 129 129 PHE PHE A . n 
A 1 122 GLU 122 130 130 GLU GLU A . n 
A 1 123 ASP 123 131 131 ASP ASP A . n 
A 1 124 ALA 124 132 132 ALA ALA A . n 
A 1 125 GLU 125 133 133 GLU GLU A . n 
A 1 126 ALA 126 134 134 ALA ALA A . n 
A 1 127 VAL 127 135 135 VAL VAL A . n 
A 1 128 LEU 128 136 136 LEU LEU A . n 
A 1 129 THR 129 137 137 THR THR A . n 
A 1 130 TRP 130 138 138 TRP TRP A . n 
A 1 131 LEU 131 139 139 LEU LEU A . n 
A 1 132 TRP 132 140 140 TRP TRP A . n 
A 1 133 ASP 133 141 141 ASP ASP A . n 
A 1 134 GLN 134 142 142 GLN GLN A . n 
A 1 135 ALA 135 143 143 ALA ALA A . n 
A 1 136 VAL 136 144 144 VAL VAL A . n 
A 1 137 SER 137 145 145 SER SER A . n 
A 1 138 ASP 138 146 146 ASP ASP A . n 
A 1 139 GLY 139 147 147 GLY GLY A . n 
A 1 140 VAL 140 148 148 VAL VAL A . n 
A 1 141 ASN 141 149 149 ASN ASN A . n 
A 1 142 HIS 142 150 150 HIS HIS A . n 
A 1 143 TRP 143 151 151 TRP TRP A . n 
A 1 144 PHE 144 152 152 PHE PHE A . n 
A 1 145 GLU 145 153 153 GLU GLU A . n 
A 1 146 ASP 146 154 154 ASP ASP A . n 
A 1 147 GLY 147 155 155 GLY GLY A . n 
A 1 148 THR 148 156 156 THR THR A . n 
A 1 149 ASP 149 157 157 ASP ASP A . n 
A 1 150 VAL 150 158 158 VAL VAL A . n 
A 1 151 ASP 151 159 159 ASP ASP A . n 
A 1 152 PHE 152 160 160 PHE PHE A . n 
A 1 153 ASP 153 161 161 ASP ASP A . n 
A 1 154 ARG 154 162 162 ARG ARG A . n 
A 1 155 VAL 155 163 163 VAL VAL A . n 
A 1 156 PHE 156 164 164 PHE PHE A . n 
A 1 157 VAL 157 165 165 VAL VAL A . n 
A 1 158 VAL 158 166 166 VAL VAL A . n 
A 1 159 GLY 159 167 167 GLY GLY A . n 
A 1 160 ASP 160 168 168 ASP ASP A . n 
A 1 161 SER 161 169 169 SER SER A . n 
A 1 162 SER 162 170 170 SER SER A . n 
A 1 163 GLY 163 171 171 GLY GLY A . n 
A 1 164 GLY 164 172 172 GLY GLY A . n 
A 1 165 ASN 165 173 173 ASN ASN A . n 
A 1 166 ILE 166 174 174 ILE ILE A . n 
A 1 167 ALA 167 175 175 ALA ALA A . n 
A 1 168 HIS 168 176 176 HIS HIS A . n 
A 1 169 GLN 169 177 177 GLN GLN A . n 
A 1 170 LEU 170 178 178 LEU LEU A . n 
A 1 171 ALA 171 179 179 ALA ALA A . n 
A 1 172 VAL 172 180 180 VAL VAL A . n 
A 1 173 ARG 173 181 181 ARG ARG A . n 
A 1 174 PHE 174 182 182 PHE PHE A . n 
A 1 175 GLY 175 183 183 GLY GLY A . n 
A 1 176 SER 176 184 184 SER SER A . n 
A 1 177 GLY 177 185 185 GLY GLY A . n 
A 1 178 SER 178 186 186 SER SER A . n 
A 1 179 ILE 179 187 187 ILE ILE A . n 
A 1 180 GLU 180 188 188 GLU GLU A . n 
A 1 181 LEU 181 189 189 LEU LEU A . n 
A 1 182 THR 182 190 190 THR THR A . n 
A 1 183 PRO 183 191 191 PRO PRO A . n 
A 1 184 VAL 184 192 192 VAL VAL A . n 
A 1 185 ARG 185 193 193 ARG ARG A . n 
A 1 186 VAL 186 194 194 VAL VAL A . n 
A 1 187 ARG 187 195 195 ARG ARG A . n 
A 1 188 GLY 188 196 196 GLY GLY A . n 
A 1 189 TYR 189 197 197 TYR TYR A . n 
A 1 190 VAL 190 198 198 VAL VAL A . n 
A 1 191 LEU 191 199 199 LEU LEU A . n 
A 1 192 MET 192 200 200 MET MET A . n 
A 1 193 GLY 193 201 201 GLY GLY A . n 
A 1 194 PRO 194 202 202 PRO PRO A . n 
A 1 195 PHE 195 203 203 PHE PHE A . n 
A 1 196 PHE 196 204 204 PHE PHE A . n 
A 1 197 GLY 197 205 205 GLY GLY A . n 
A 1 198 GLY 198 206 206 GLY GLY A . n 
A 1 199 GLU 199 207 207 GLU GLU A . n 
A 1 200 GLU 200 208 208 GLU GLU A . n 
A 1 201 ARG 201 209 209 ARG ARG A . n 
A 1 202 THR 202 210 210 THR THR A . n 
A 1 203 ASN 203 211 211 ASN ASN A . n 
A 1 204 SER 204 212 212 SER SER A . n 
A 1 205 GLU 205 213 213 GLU GLU A . n 
A 1 206 ASN 206 214 214 ASN ASN A . n 
A 1 207 GLY 207 215 215 GLY GLY A . n 
A 1 208 PRO 208 216 216 PRO PRO A . n 
A 1 209 SER 209 217 217 SER SER A . n 
A 1 210 GLU 210 218 218 GLU GLU A . n 
A 1 211 ALA 211 219 219 ALA ALA A . n 
A 1 212 LEU 212 220 220 LEU LEU A . n 
A 1 213 LEU 213 221 221 LEU LEU A . n 
A 1 214 SER 214 222 222 SER SER A . n 
A 1 215 LEU 215 223 223 LEU LEU A . n 
A 1 216 ASP 216 224 224 ASP ASP A . n 
A 1 217 LEU 217 225 225 LEU LEU A . n 
A 1 218 LEU 218 226 226 LEU LEU A . n 
A 1 219 ASP 219 227 227 ASP ASP A . n 
A 1 220 LYS 220 228 228 LYS LYS A . n 
A 1 221 PHE 221 229 229 PHE PHE A . n 
A 1 222 TRP 222 230 230 TRP TRP A . n 
A 1 223 ARG 223 231 231 ARG ARG A . n 
A 1 224 LEU 224 232 232 LEU LEU A . n 
A 1 225 SER 225 233 233 SER SER A . n 
A 1 226 LEU 226 234 234 LEU LEU A . n 
A 1 227 PRO 227 235 235 PRO PRO A . n 
A 1 228 ASN 228 236 236 ASN ASN A . n 
A 1 229 GLY 229 237 237 GLY GLY A . n 
A 1 230 ALA 230 238 238 ALA ALA A . n 
A 1 231 THR 231 239 239 THR THR A . n 
A 1 232 ARG 232 240 240 ARG ARG A . n 
A 1 233 ASP 233 241 241 ASP ASP A . n 
A 1 234 HIS 234 242 242 HIS HIS A . n 
A 1 235 HIS 235 243 243 HIS HIS A . n 
A 1 236 MET 236 244 244 MET MET A . n 
A 1 237 ALA 237 245 245 ALA ALA A . n 
A 1 238 ASN 238 246 246 ASN ASN A . n 
A 1 239 PRO 239 247 247 PRO PRO A . n 
A 1 240 PHE 240 248 248 PHE PHE A . n 
A 1 241 GLY 241 249 249 GLY GLY A . n 
A 1 242 PRO 242 250 250 PRO PRO A . n 
A 1 243 THR 243 251 251 THR THR A . n 
A 1 244 SER 244 252 252 SER SER A . n 
A 1 245 PRO 245 253 253 PRO PRO A . n 
A 1 246 THR 246 254 254 THR THR A . n 
A 1 247 LEU 247 255 255 LEU LEU A . n 
A 1 248 GLU 248 256 256 GLU GLU A . n 
A 1 249 SER 249 257 257 SER SER A . n 
A 1 250 ILE 250 258 258 ILE ILE A . n 
A 1 251 SER 251 259 259 SER SER A . n 
A 1 252 LEU 252 260 260 LEU LEU A . n 
A 1 253 GLU 253 261 261 GLU GLU A . n 
A 1 254 PRO 254 262 262 PRO PRO A . n 
A 1 255 MET 255 263 263 MET MET A . n 
A 1 256 LEU 256 264 264 LEU LEU A . n 
A 1 257 VAL 257 265 265 VAL VAL A . n 
A 1 258 ILE 258 266 266 ILE ILE A . n 
A 1 259 VAL 259 267 267 VAL VAL A . n 
A 1 260 GLY 260 268 268 GLY GLY A . n 
A 1 261 GLY 261 269 269 GLY GLY A . n 
A 1 262 SER 262 270 270 SER SER A . n 
A 1 263 GLU 263 271 271 GLU GLU A . n 
A 1 264 LEU 264 272 272 LEU LEU A . n 
A 1 265 LEU 265 273 273 LEU LEU A . n 
A 1 266 ARG 266 274 274 ARG ARG A . n 
A 1 267 ASP 267 275 275 ASP ASP A . n 
A 1 268 ARG 268 276 276 ARG ARG A . n 
A 1 269 ALA 269 277 277 ALA ALA A . n 
A 1 270 LYS 270 278 278 LYS LYS A . n 
A 1 271 GLU 271 279 279 GLU GLU A . n 
A 1 272 TYR 272 280 280 TYR TYR A . n 
A 1 273 ALA 273 281 281 ALA ALA A . n 
A 1 274 TYR 274 282 282 TYR TYR A . n 
A 1 275 LYS 275 283 283 LYS LYS A . n 
A 1 276 LEU 276 284 284 LEU LEU A . n 
A 1 277 LYS 277 285 285 LYS LYS A . n 
A 1 278 LYS 278 286 286 LYS LYS A . n 
A 1 279 MET 279 287 287 MET MET A . n 
A 1 280 GLY 280 288 288 GLY GLY A . n 
A 1 281 GLY 281 289 289 GLY GLY A . n 
A 1 282 LYS 282 290 290 LYS LYS A . n 
A 1 283 ARG 283 291 291 ARG ARG A . n 
A 1 284 VAL 284 292 292 VAL VAL A . n 
A 1 285 ASP 285 293 293 ASP ASP A . n 
A 1 286 TYR 286 294 294 TYR TYR A . n 
A 1 287 ILE 287 295 295 ILE ILE A . n 
A 1 288 GLU 288 296 296 GLU GLU A . n 
A 1 289 PHE 289 297 297 PHE PHE A . n 
A 1 290 GLU 290 298 298 GLU GLU A . n 
A 1 291 ASN 291 299 299 ASN ASN A . n 
A 1 292 LYS 292 300 300 LYS LYS A . n 
A 1 293 GLU 293 301 301 GLU GLU A . n 
A 1 294 HIS 294 302 302 HIS HIS A . n 
A 1 295 GLY 295 303 303 GLY GLY A . n 
A 1 296 PHE 296 304 304 PHE PHE A . n 
A 1 297 TYR 297 305 305 TYR TYR A . n 
A 1 298 SER 298 306 306 SER SER A . n 
A 1 299 ASN 299 307 307 ASN ASN A . n 
A 1 300 TYR 300 308 308 TYR TYR A . n 
A 1 301 PRO 301 309 309 PRO PRO A . n 
A 1 302 SER 302 310 310 SER SER A . n 
A 1 303 SER 303 311 311 SER SER A . n 
A 1 304 GLU 304 312 312 GLU GLU A . n 
A 1 305 ALA 305 313 313 ALA ALA A . n 
A 1 306 ALA 306 314 314 ALA ALA A . n 
A 1 307 GLU 307 315 315 GLU GLU A . n 
A 1 308 GLN 308 316 316 GLN GLN A . n 
A 1 309 VAL 309 317 317 VAL VAL A . n 
A 1 310 LEU 310 318 318 LEU LEU A . n 
A 1 311 ARG 311 319 319 ARG ARG A . n 
A 1 312 ILE 312 320 320 ILE ILE A . n 
A 1 313 ILE 313 321 321 ILE ILE A . n 
A 1 314 GLY 314 322 322 GLY GLY A . n 
A 1 315 ASP 315 323 323 ASP ASP A . n 
A 1 316 PHE 316 324 324 PHE PHE A . n 
A 1 317 MET 317 325 325 MET MET A . n 
A 1 318 ASN 318 326 326 ASN ASN A . n 
A 1 319 ASN 319 327 327 ASN ASN A . n 
A 1 320 LEU 320 328 328 LEU LEU A . n 
A 1 321 SER 321 329 329 SER SER A . n 
B 1 1   GLN 1   9   9   GLN GLN B . n 
B 1 2   VAL 2   10  10  VAL VAL B . n 
B 1 3   ALA 3   11  11  ALA ALA B . n 
B 1 4   GLU 4   12  12  GLU GLU B . n 
B 1 5   ASP 5   13  13  ASP ASP B . n 
B 1 6   CYS 6   14  14  CYS CYS B . n 
B 1 7   MET 7   15  15  MET MET B . n 
B 1 8   GLY 8   16  16  GLY GLY B . n 
B 1 9   LEU 9   17  17  LEU LEU B . n 
B 1 10  LEU 10  18  18  LEU LEU B . n 
B 1 11  GLN 11  19  19  GLN GLN B . n 
B 1 12  LEU 12  20  20  LEU LEU B . n 
B 1 13  LEU 13  21  21  LEU LEU B . n 
B 1 14  SER 14  22  22  SER SER B . n 
B 1 15  ASN 15  23  23  ASN ASN B . n 
B 1 16  GLY 16  24  24  GLY GLY B . n 
B 1 17  THR 17  25  25  THR THR B . n 
B 1 18  VAL 18  26  26  VAL VAL B . n 
B 1 19  LEU 19  27  27  LEU LEU B . n 
B 1 20  ARG 20  28  28  ARG ARG B . n 
B 1 21  SER 21  29  29  SER SER B . n 
B 1 22  GLU 22  30  ?   ?   ?   B . n 
B 1 23  SER 23  31  ?   ?   ?   B . n 
B 1 24  ILE 24  32  ?   ?   ?   B . n 
B 1 25  ASP 25  33  ?   ?   ?   B . n 
B 1 26  LEU 26  34  ?   ?   ?   B . n 
B 1 27  ILE 27  35  ?   ?   ?   B . n 
B 1 28  THR 28  36  ?   ?   ?   B . n 
B 1 29  GLN 29  37  ?   ?   ?   B . n 
B 1 30  GLN 30  38  ?   ?   ?   B . n 
B 1 31  ILE 31  39  ?   ?   ?   B . n 
B 1 32  PRO 32  40  ?   ?   ?   B . n 
B 1 33  PHE 33  41  ?   ?   ?   B . n 
B 1 34  LYS 34  42  ?   ?   ?   B . n 
B 1 35  ASN 35  43  43  ASN ASN B . n 
B 1 36  ASN 36  44  44  ASN ASN B . n 
B 1 37  GLN 37  45  45  GLN GLN B . n 
B 1 38  THR 38  46  46  THR THR B . n 
B 1 39  VAL 39  47  47  VAL VAL B . n 
B 1 40  LEU 40  48  48  LEU LEU B . n 
B 1 41  PHE 41  49  49  PHE PHE B . n 
B 1 42  LYS 42  50  50  LYS LYS B . n 
B 1 43  ASP 43  51  51  ASP ASP B . n 
B 1 44  SER 44  52  52  SER SER B . n 
B 1 45  ILE 45  53  53  ILE ILE B . n 
B 1 46  TYR 46  54  54  TYR TYR B . n 
B 1 47  HIS 47  55  55  HIS HIS B . n 
B 1 48  LYS 48  56  56  LYS LYS B . n 
B 1 49  PRO 49  57  57  PRO PRO B . n 
B 1 50  ASN 50  58  58  ASN ASN B . n 
B 1 51  ASN 51  59  59  ASN ASN B . n 
B 1 52  LEU 52  60  60  LEU LEU B . n 
B 1 53  HIS 53  61  61  HIS HIS B . n 
B 1 54  LEU 54  62  62  LEU LEU B . n 
B 1 55  ARG 55  63  63  ARG ARG B . n 
B 1 56  LEU 56  64  64  LEU LEU B . n 
B 1 57  TYR 57  65  65  TYR TYR B . n 
B 1 58  LYS 58  66  66  LYS LYS B . n 
B 1 59  PRO 59  67  67  PRO PRO B . n 
B 1 60  ILE 60  68  68  ILE ILE B . n 
B 1 61  SER 61  69  69  SER SER B . n 
B 1 62  ALA 62  70  70  ALA ALA B . n 
B 1 63  SER 63  71  71  SER SER B . n 
B 1 64  ASN 64  72  ?   ?   ?   B . n 
B 1 65  ARG 65  73  ?   ?   ?   B . n 
B 1 66  THR 66  74  ?   ?   ?   B . n 
B 1 67  ALA 67  75  ?   ?   ?   B . n 
B 1 68  LEU 68  76  ?   ?   ?   B . n 
B 1 69  PRO 69  77  ?   ?   ?   B . n 
B 1 70  VAL 70  78  78  VAL VAL B . n 
B 1 71  VAL 71  79  79  VAL VAL B . n 
B 1 72  VAL 72  80  80  VAL VAL B . n 
B 1 73  PHE 73  81  81  PHE PHE B . n 
B 1 74  PHE 74  82  82  PHE PHE B . n 
B 1 75  HIS 75  83  83  HIS HIS B . n 
B 1 76  GLY 76  84  84  GLY GLY B . n 
B 1 77  GLY 77  85  85  GLY GLY B . n 
B 1 78  GLY 78  86  86  GLY GLY B . n 
B 1 79  PHE 79  87  87  PHE PHE B . n 
B 1 80  CYS 80  88  88  CYS CYS B . n 
B 1 81  PHE 81  89  89  PHE PHE B . n 
B 1 82  GLY 82  90  90  GLY GLY B . n 
B 1 83  SER 83  91  91  SER SER B . n 
B 1 84  ARG 84  92  92  ARG ARG B . n 
B 1 85  SER 85  93  93  SER SER B . n 
B 1 86  TRP 86  94  94  TRP TRP B . n 
B 1 87  PRO 87  95  95  PRO PRO B . n 
B 1 88  HIS 88  96  96  HIS HIS B . n 
B 1 89  PHE 89  97  97  PHE PHE B . n 
B 1 90  HIS 90  98  98  HIS HIS B . n 
B 1 91  ASN 91  99  99  ASN ASN B . n 
B 1 92  PHE 92  100 100 PHE PHE B . n 
B 1 93  CYS 93  101 101 CYS CYS B . n 
B 1 94  LEU 94  102 102 LEU LEU B . n 
B 1 95  THR 95  103 103 THR THR B . n 
B 1 96  LEU 96  104 104 LEU LEU B . n 
B 1 97  ALA 97  105 105 ALA ALA B . n 
B 1 98  SER 98  106 106 SER SER B . n 
B 1 99  SER 99  107 107 SER SER B . n 
B 1 100 LEU 100 108 108 LEU LEU B . n 
B 1 101 ASN 101 109 109 ASN ASN B . n 
B 1 102 ALA 102 110 110 ALA ALA B . n 
B 1 103 LEU 103 111 111 LEU LEU B . n 
B 1 104 VAL 104 112 112 VAL VAL B . n 
B 1 105 VAL 105 113 113 VAL VAL B . n 
B 1 106 SER 106 114 114 SER SER B . n 
B 1 107 PRO 107 115 115 PRO PRO B . n 
B 1 108 ASP 108 116 116 ASP ASP B . n 
B 1 109 TYR 109 117 117 TYR TYR B . n 
B 1 110 ARG 110 118 118 ARG ARG B . n 
B 1 111 LEU 111 119 119 LEU LEU B . n 
B 1 112 ALA 112 120 120 ALA ALA B . n 
B 1 113 PRO 113 121 121 PRO PRO B . n 
B 1 114 GLU 114 122 122 GLU GLU B . n 
B 1 115 HIS 115 123 123 HIS HIS B . n 
B 1 116 ARG 116 124 124 ARG ARG B . n 
B 1 117 LEU 117 125 125 LEU LEU B . n 
B 1 118 PRO 118 126 126 PRO PRO B . n 
B 1 119 ALA 119 127 127 ALA ALA B . n 
B 1 120 ALA 120 128 128 ALA ALA B . n 
B 1 121 PHE 121 129 129 PHE PHE B . n 
B 1 122 GLU 122 130 130 GLU GLU B . n 
B 1 123 ASP 123 131 131 ASP ASP B . n 
B 1 124 ALA 124 132 132 ALA ALA B . n 
B 1 125 GLU 125 133 133 GLU GLU B . n 
B 1 126 ALA 126 134 134 ALA ALA B . n 
B 1 127 VAL 127 135 135 VAL VAL B . n 
B 1 128 LEU 128 136 136 LEU LEU B . n 
B 1 129 THR 129 137 137 THR THR B . n 
B 1 130 TRP 130 138 138 TRP TRP B . n 
B 1 131 LEU 131 139 139 LEU LEU B . n 
B 1 132 TRP 132 140 140 TRP TRP B . n 
B 1 133 ASP 133 141 141 ASP ASP B . n 
B 1 134 GLN 134 142 142 GLN GLN B . n 
B 1 135 ALA 135 143 143 ALA ALA B . n 
B 1 136 VAL 136 144 144 VAL VAL B . n 
B 1 137 SER 137 145 145 SER SER B . n 
B 1 138 ASP 138 146 146 ASP ASP B . n 
B 1 139 GLY 139 147 147 GLY GLY B . n 
B 1 140 VAL 140 148 148 VAL VAL B . n 
B 1 141 ASN 141 149 149 ASN ASN B . n 
B 1 142 HIS 142 150 150 HIS HIS B . n 
B 1 143 TRP 143 151 151 TRP TRP B . n 
B 1 144 PHE 144 152 152 PHE PHE B . n 
B 1 145 GLU 145 153 153 GLU GLU B . n 
B 1 146 ASP 146 154 154 ASP ASP B . n 
B 1 147 GLY 147 155 155 GLY GLY B . n 
B 1 148 THR 148 156 156 THR THR B . n 
B 1 149 ASP 149 157 157 ASP ASP B . n 
B 1 150 VAL 150 158 158 VAL VAL B . n 
B 1 151 ASP 151 159 159 ASP ASP B . n 
B 1 152 PHE 152 160 160 PHE PHE B . n 
B 1 153 ASP 153 161 161 ASP ASP B . n 
B 1 154 ARG 154 162 162 ARG ARG B . n 
B 1 155 VAL 155 163 163 VAL VAL B . n 
B 1 156 PHE 156 164 164 PHE PHE B . n 
B 1 157 VAL 157 165 165 VAL VAL B . n 
B 1 158 VAL 158 166 166 VAL VAL B . n 
B 1 159 GLY 159 167 167 GLY GLY B . n 
B 1 160 ASP 160 168 168 ASP ASP B . n 
B 1 161 SER 161 169 169 SER SER B . n 
B 1 162 SER 162 170 170 SER SER B . n 
B 1 163 GLY 163 171 171 GLY GLY B . n 
B 1 164 GLY 164 172 172 GLY GLY B . n 
B 1 165 ASN 165 173 173 ASN ASN B . n 
B 1 166 ILE 166 174 174 ILE ILE B . n 
B 1 167 ALA 167 175 175 ALA ALA B . n 
B 1 168 HIS 168 176 176 HIS HIS B . n 
B 1 169 GLN 169 177 177 GLN GLN B . n 
B 1 170 LEU 170 178 178 LEU LEU B . n 
B 1 171 ALA 171 179 179 ALA ALA B . n 
B 1 172 VAL 172 180 180 VAL VAL B . n 
B 1 173 ARG 173 181 181 ARG ARG B . n 
B 1 174 PHE 174 182 182 PHE PHE B . n 
B 1 175 GLY 175 183 183 GLY GLY B . n 
B 1 176 SER 176 184 ?   ?   ?   B . n 
B 1 177 GLY 177 185 ?   ?   ?   B . n 
B 1 178 SER 178 186 ?   ?   ?   B . n 
B 1 179 ILE 179 187 187 ILE ILE B . n 
B 1 180 GLU 180 188 188 GLU GLU B . n 
B 1 181 LEU 181 189 189 LEU LEU B . n 
B 1 182 THR 182 190 190 THR THR B . n 
B 1 183 PRO 183 191 191 PRO PRO B . n 
B 1 184 VAL 184 192 192 VAL VAL B . n 
B 1 185 ARG 185 193 193 ARG ARG B . n 
B 1 186 VAL 186 194 194 VAL VAL B . n 
B 1 187 ARG 187 195 195 ARG ARG B . n 
B 1 188 GLY 188 196 196 GLY GLY B . n 
B 1 189 TYR 189 197 197 TYR TYR B . n 
B 1 190 VAL 190 198 198 VAL VAL B . n 
B 1 191 LEU 191 199 199 LEU LEU B . n 
B 1 192 MET 192 200 200 MET MET B . n 
B 1 193 GLY 193 201 201 GLY GLY B . n 
B 1 194 PRO 194 202 202 PRO PRO B . n 
B 1 195 PHE 195 203 203 PHE PHE B . n 
B 1 196 PHE 196 204 204 PHE PHE B . n 
B 1 197 GLY 197 205 205 GLY GLY B . n 
B 1 198 GLY 198 206 206 GLY GLY B . n 
B 1 199 GLU 199 207 207 GLU GLU B . n 
B 1 200 GLU 200 208 208 GLU GLU B . n 
B 1 201 ARG 201 209 209 ARG ARG B . n 
B 1 202 THR 202 210 210 THR THR B . n 
B 1 203 ASN 203 211 211 ASN ASN B . n 
B 1 204 SER 204 212 212 SER SER B . n 
B 1 205 GLU 205 213 213 GLU GLU B . n 
B 1 206 ASN 206 214 214 ASN ASN B . n 
B 1 207 GLY 207 215 215 GLY GLY B . n 
B 1 208 PRO 208 216 216 PRO PRO B . n 
B 1 209 SER 209 217 217 SER SER B . n 
B 1 210 GLU 210 218 218 GLU GLU B . n 
B 1 211 ALA 211 219 219 ALA ALA B . n 
B 1 212 LEU 212 220 220 LEU LEU B . n 
B 1 213 LEU 213 221 221 LEU LEU B . n 
B 1 214 SER 214 222 222 SER SER B . n 
B 1 215 LEU 215 223 223 LEU LEU B . n 
B 1 216 ASP 216 224 224 ASP ASP B . n 
B 1 217 LEU 217 225 225 LEU LEU B . n 
B 1 218 LEU 218 226 226 LEU LEU B . n 
B 1 219 ASP 219 227 227 ASP ASP B . n 
B 1 220 LYS 220 228 228 LYS LYS B . n 
B 1 221 PHE 221 229 229 PHE PHE B . n 
B 1 222 TRP 222 230 230 TRP TRP B . n 
B 1 223 ARG 223 231 231 ARG ARG B . n 
B 1 224 LEU 224 232 232 LEU LEU B . n 
B 1 225 SER 225 233 233 SER SER B . n 
B 1 226 LEU 226 234 234 LEU LEU B . n 
B 1 227 PRO 227 235 235 PRO PRO B . n 
B 1 228 ASN 228 236 236 ASN ASN B . n 
B 1 229 GLY 229 237 237 GLY GLY B . n 
B 1 230 ALA 230 238 238 ALA ALA B . n 
B 1 231 THR 231 239 239 THR THR B . n 
B 1 232 ARG 232 240 240 ARG ARG B . n 
B 1 233 ASP 233 241 241 ASP ASP B . n 
B 1 234 HIS 234 242 242 HIS HIS B . n 
B 1 235 HIS 235 243 243 HIS HIS B . n 
B 1 236 MET 236 244 244 MET MET B . n 
B 1 237 ALA 237 245 245 ALA ALA B . n 
B 1 238 ASN 238 246 246 ASN ASN B . n 
B 1 239 PRO 239 247 247 PRO PRO B . n 
B 1 240 PHE 240 248 248 PHE PHE B . n 
B 1 241 GLY 241 249 249 GLY GLY B . n 
B 1 242 PRO 242 250 250 PRO PRO B . n 
B 1 243 THR 243 251 251 THR THR B . n 
B 1 244 SER 244 252 252 SER SER B . n 
B 1 245 PRO 245 253 253 PRO PRO B . n 
B 1 246 THR 246 254 254 THR THR B . n 
B 1 247 LEU 247 255 255 LEU LEU B . n 
B 1 248 GLU 248 256 256 GLU GLU B . n 
B 1 249 SER 249 257 257 SER SER B . n 
B 1 250 ILE 250 258 258 ILE ILE B . n 
B 1 251 SER 251 259 259 SER SER B . n 
B 1 252 LEU 252 260 260 LEU LEU B . n 
B 1 253 GLU 253 261 261 GLU GLU B . n 
B 1 254 PRO 254 262 262 PRO PRO B . n 
B 1 255 MET 255 263 263 MET MET B . n 
B 1 256 LEU 256 264 264 LEU LEU B . n 
B 1 257 VAL 257 265 265 VAL VAL B . n 
B 1 258 ILE 258 266 266 ILE ILE B . n 
B 1 259 VAL 259 267 267 VAL VAL B . n 
B 1 260 GLY 260 268 268 GLY GLY B . n 
B 1 261 GLY 261 269 269 GLY GLY B . n 
B 1 262 SER 262 270 270 SER SER B . n 
B 1 263 GLU 263 271 271 GLU GLU B . n 
B 1 264 LEU 264 272 272 LEU LEU B . n 
B 1 265 LEU 265 273 273 LEU LEU B . n 
B 1 266 ARG 266 274 274 ARG ARG B . n 
B 1 267 ASP 267 275 275 ASP ASP B . n 
B 1 268 ARG 268 276 276 ARG ARG B . n 
B 1 269 ALA 269 277 277 ALA ALA B . n 
B 1 270 LYS 270 278 278 LYS LYS B . n 
B 1 271 GLU 271 279 279 GLU GLU B . n 
B 1 272 TYR 272 280 280 TYR TYR B . n 
B 1 273 ALA 273 281 281 ALA ALA B . n 
B 1 274 TYR 274 282 282 TYR TYR B . n 
B 1 275 LYS 275 283 283 LYS LYS B . n 
B 1 276 LEU 276 284 284 LEU LEU B . n 
B 1 277 LYS 277 285 285 LYS LYS B . n 
B 1 278 LYS 278 286 286 LYS LYS B . n 
B 1 279 MET 279 287 287 MET MET B . n 
B 1 280 GLY 280 288 288 GLY GLY B . n 
B 1 281 GLY 281 289 289 GLY GLY B . n 
B 1 282 LYS 282 290 290 LYS LYS B . n 
B 1 283 ARG 283 291 291 ARG ARG B . n 
B 1 284 VAL 284 292 292 VAL VAL B . n 
B 1 285 ASP 285 293 293 ASP ASP B . n 
B 1 286 TYR 286 294 294 TYR TYR B . n 
B 1 287 ILE 287 295 295 ILE ILE B . n 
B 1 288 GLU 288 296 296 GLU GLU B . n 
B 1 289 PHE 289 297 297 PHE PHE B . n 
B 1 290 GLU 290 298 298 GLU GLU B . n 
B 1 291 ASN 291 299 299 ASN ASN B . n 
B 1 292 LYS 292 300 300 LYS LYS B . n 
B 1 293 GLU 293 301 301 GLU GLU B . n 
B 1 294 HIS 294 302 302 HIS HIS B . n 
B 1 295 GLY 295 303 303 GLY GLY B . n 
B 1 296 PHE 296 304 304 PHE PHE B . n 
B 1 297 TYR 297 305 305 TYR TYR B . n 
B 1 298 SER 298 306 306 SER SER B . n 
B 1 299 ASN 299 307 307 ASN ASN B . n 
B 1 300 TYR 300 308 308 TYR TYR B . n 
B 1 301 PRO 301 309 309 PRO PRO B . n 
B 1 302 SER 302 310 310 SER SER B . n 
B 1 303 SER 303 311 311 SER SER B . n 
B 1 304 GLU 304 312 312 GLU GLU B . n 
B 1 305 ALA 305 313 313 ALA ALA B . n 
B 1 306 ALA 306 314 314 ALA ALA B . n 
B 1 307 GLU 307 315 315 GLU GLU B . n 
B 1 308 GLN 308 316 316 GLN GLN B . n 
B 1 309 VAL 309 317 317 VAL VAL B . n 
B 1 310 LEU 310 318 318 LEU LEU B . n 
B 1 311 ARG 311 319 319 ARG ARG B . n 
B 1 312 ILE 312 320 320 ILE ILE B . n 
B 1 313 ILE 313 321 321 ILE ILE B . n 
B 1 314 GLY 314 322 322 GLY GLY B . n 
B 1 315 ASP 315 323 323 ASP ASP B . n 
B 1 316 PHE 316 324 324 PHE PHE B . n 
B 1 317 MET 317 325 325 MET MET B . n 
B 1 318 ASN 318 326 326 ASN ASN B . n 
B 1 319 ASN 319 327 327 ASN ASN B . n 
B 1 320 LEU 320 328 328 LEU LEU B . n 
B 1 321 SER 321 329 329 SER SER B . n 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZRO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     99.399 
_cell.length_a_esd                 ? 
_cell.length_b                     99.399 
_cell.length_b_esd                 ? 
_cell.length_c                     114.161 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZRO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZRO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.49 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 MSodium acetate trihydrate, 20% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-04 
_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   0.987 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZRO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.09 
_reflns.d_resolution_low                               49.75 
_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                                     8670 
_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                           98.20 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                19.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.09 
_reflns_shell.d_res_low                                     3.30 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             202 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.50 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.60 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZRO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.09 
_refine.ls_d_res_low                             49.70 
_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                     8666 
_refine.ls_number_reflns_R_free                  867 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    70.19 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2841 
_refine.ls_R_factor_R_free                       0.3387 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2782 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_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                      AF-Q9FG13-F1 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 40.56 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.45 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.09 
_refine_hist.d_res_low                        49.70 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4766 
_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        4766 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005 ? 4889 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.048 ? 6630 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 5.837 ? 652  ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.056 ? 709  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 871  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.09 3.28  . . 38  347  19.00  . . . . 0.3827 . . . . . . . . . . . . . . . 0.4212 
'X-RAY DIFFRACTION' 3.28 3.54  . . 67  618  34.00  . . . . 0.3642 . . . . . . . . . . . . . . . 0.3786 
'X-RAY DIFFRACTION' 3.54 3.89  . . 129 1197 65.00  . . . . 0.3463 . . . . . . . . . . . . . . . 0.3929 
'X-RAY DIFFRACTION' 3.89 4.45  . . 206 1828 100.00 . . . . 0.3049 . . . . . . . . . . . . . . . 0.3724 
'X-RAY DIFFRACTION' 4.46 5.61  . . 213 1866 100.00 . . . . 0.2786 . . . . . . . . . . . . . . . 0.3228 
'X-RAY DIFFRACTION' 5.61 49.70 . . 214 1943 100.00 . . . . 0.2407 . . . . . . . . . . . . . . . 0.3124 
# 
_struct.entry_id                     8ZRO 
_struct.title                        'Arabidopsis Carboxylesterase CXE15' 
_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        8ZRO 
_struct_keywords.text            'Catabolic enzyme, CXE15, strigolactoone, carboxylesterase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CXE15_ARATH 
_struct_ref.pdbx_db_accession          Q9FG13 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSELLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_struct_ref.pdbx_align_begin           9 
# 
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 8ZRO A 1 ? 321 ? Q9FG13 9 ? 329 ? 9 329 
2 1 8ZRO B 1 ? 321 ? Q9FG13 9 ? 329 ? 9 329 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2090  ? 
1 MORE         -4    ? 
1 'SSA (A^2)'  24510 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TRP A 86  ? ASN A 101 ? TRP A 94  ASN A 109 1 ? 16 
HELX_P HELX_P2  AA2 PRO A 118 ? GLN A 134 ? PRO A 126 GLN A 142 1 ? 17 
HELX_P HELX_P3  AA3 SER A 162 ? GLN A 169 ? SER A 170 GLN A 177 1 ? 8  
HELX_P HELX_P4  AA4 THR A 202 ? GLY A 207 ? THR A 210 GLY A 215 1 ? 6  
HELX_P HELX_P5  AA5 SER A 214 ? LEU A 226 ? SER A 222 LEU A 234 1 ? 13 
HELX_P HELX_P6  AA6 LEU A 265 ? MET A 279 ? LEU A 273 MET A 287 1 ? 15 
HELX_P HELX_P7  AA7 GLY A 295 ? TYR A 300 ? GLY A 303 TYR A 308 1 ? 6  
HELX_P HELX_P8  AA8 SER A 303 ? LEU A 320 ? SER A 311 LEU A 328 1 ? 18 
HELX_P HELX_P9  AA9 TRP B 86  ? LEU B 100 ? TRP B 94  LEU B 108 1 ? 15 
HELX_P HELX_P10 AB1 PRO B 118 ? VAL B 136 ? PRO B 126 VAL B 144 1 ? 19 
HELX_P HELX_P11 AB2 SER B 162 ? PHE B 174 ? SER B 170 PHE B 182 1 ? 13 
HELX_P HELX_P12 AB3 SER B 214 ? LEU B 226 ? SER B 222 LEU B 234 1 ? 13 
HELX_P HELX_P13 AB4 LEU B 265 ? GLY B 280 ? LEU B 273 GLY B 288 1 ? 16 
HELX_P HELX_P14 AB5 SER B 303 ? ASN B 319 ? SER B 311 ASN B 327 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 112 A . ? ALA 120 A PRO 113 A ? PRO 121 A 1 -2.27 
2 LEU 117 A . ? LEU 125 A PRO 118 A ? PRO 126 A 1 8.25  
3 THR 182 A . ? THR 190 A PRO 183 A ? PRO 191 A 1 6.62  
4 GLY 241 A . ? GLY 249 A PRO 242 A ? PRO 250 A 1 -9.14 
5 ALA 112 B . ? ALA 120 B PRO 113 B ? PRO 121 B 1 -2.08 
6 LEU 117 B . ? LEU 125 B PRO 118 B ? PRO 126 B 1 7.10  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 11 ? 
AA2 ? 11 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? parallel      
AA2 5  6  ? parallel      
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? 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  GLU A 4   ? CYS A 6   ? GLU A 12  CYS A 14  
AA1 2  LEU A 10  ? LEU A 12  ? LEU A 18  LEU A 20  
AA1 3  VAL A 18  ? ARG A 20  ? VAL A 26  ARG A 28  
AA1 4  LEU B 40  ? HIS B 47  ? LEU B 48  HIS B 55  
AA1 5  LEU B 52  ? LYS B 58  ? LEU B 60  LYS B 66  
AA1 6  VAL B 104 ? PRO B 107 ? VAL B 112 PRO B 115 
AA1 7  VAL B 71  ? PHE B 74  ? VAL B 79  PHE B 82  
AA1 8  VAL B 155 ? ASP B 160 ? VAL B 163 ASP B 168 
AA1 9  VAL B 186 ? MET B 192 ? VAL B 194 MET B 200 
AA1 10 MET B 255 ? GLY B 260 ? MET B 263 GLY B 268 
AA1 11 VAL B 284 ? PHE B 289 ? VAL B 292 PHE B 297 
AA2 1  VAL A 284 ? PHE A 289 ? VAL A 292 PHE A 297 
AA2 2  MET A 255 ? GLY A 260 ? MET A 263 GLY A 268 
AA2 3  VAL A 186 ? MET A 192 ? VAL A 194 MET A 200 
AA2 4  ASP A 149 ? ASP A 160 ? ASP A 157 ASP A 168 
AA2 5  ALA A 67  ? PHE A 74  ? ALA A 75  PHE A 82  
AA2 6  LEU A 103 ? PRO A 107 ? LEU A 111 PRO A 115 
AA2 7  LEU A 52  ? PRO A 59  ? LEU A 60  PRO A 67  
AA2 8  VAL A 39  ? HIS A 47  ? VAL A 47  HIS A 55  
AA2 9  LEU B 19  ? ARG B 20  ? LEU B 27  ARG B 28  
AA2 10 LEU B 10  ? LEU B 13  ? LEU B 18  LEU B 21  
AA2 11 VAL B 2   ? CYS B 6   ? VAL B 10  CYS B 14  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N GLU A 4   ? N GLU A 12  O LEU A 12  ? O LEU A 20  
AA1 2  3  N GLN A 11  ? N GLN A 19  O LEU A 19  ? O LEU A 27  
AA1 3  4  N ARG A 20  ? N ARG A 28  O ASP B 43  ? O ASP B 51  
AA1 4  5  N LYS B 42  ? N LYS B 50  O LEU B 56  ? O LEU B 64  
AA1 5  6  N ARG B 55  ? N ARG B 63  O SER B 106 ? O SER B 114 
AA1 6  7  O VAL B 105 ? O VAL B 113 N VAL B 71  ? N VAL B 79  
AA1 7  8  N VAL B 72  ? N VAL B 80  O VAL B 158 ? O VAL B 166 
AA1 8  9  N VAL B 157 ? N VAL B 165 O VAL B 190 ? O VAL B 198 
AA1 9  10 N LEU B 191 ? N LEU B 199 O LEU B 256 ? O LEU B 264 
AA1 10 11 N VAL B 257 ? N VAL B 265 O ASP B 285 ? O ASP B 293 
AA2 1  2  O ASP A 285 ? O ASP A 293 N VAL A 257 ? N VAL A 265 
AA2 2  3  O LEU A 256 ? O LEU A 264 N LEU A 191 ? N LEU A 199 
AA2 3  4  O ARG A 187 ? O ARG A 195 N VAL A 155 ? N VAL A 163 
AA2 4  5  O ASP A 149 ? O ASP A 157 N LEU A 68  ? N LEU A 76  
AA2 5  6  N VAL A 71  ? N VAL A 79  O LEU A 103 ? O LEU A 111 
AA2 6  7  O SER A 106 ? O SER A 114 N ARG A 55  ? N ARG A 63  
AA2 7  8  O LYS A 58  ? O LYS A 66  N LEU A 40  ? N LEU A 48  
AA2 8  9  N ASP A 43  ? N ASP A 51  O ARG B 20  ? O ARG B 28  
AA2 9  10 O LEU B 19  ? O LEU B 27  N GLN B 11  ? N GLN B 19  
AA2 10 11 O LEU B 12  ? O LEU B 20  N ALA B 3   ? N ALA B 11  
# 
_pdbx_entry_details.entry_id                   8ZRO 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B ILE 320 ? ? OD1 B ASP 323 ? ? 1.29 
2 1 CE1 B PHE 182 ? ? OE1 B GLU 188 ? ? 1.78 
3 1 O   A LEU 189 ? ? O   A VAL 192 ? ? 1.80 
4 1 OG1 B THR 156 ? ? OD1 B ASP 159 ? ? 1.83 
5 1 CD1 B PHE 182 ? ? OE1 B GLU 188 ? ? 1.96 
6 1 NH2 B ARG 181 ? ? OE2 B GLU 188 ? ? 1.99 
7 1 CG1 B VAL 158 ? ? N   B ASP 161 ? ? 2.11 
8 1 O   B ALA 143 ? ? O   B SER 145 ? ? 2.15 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N  A GLY 24  ? ? CA A GLY 24  ? ? C  A GLY 24  ? ? 95.56  113.10 -17.54 2.50 N 
2  1 N  A THR 25  ? ? CA A THR 25  ? ? CB A THR 25  ? ? 125.87 110.30 15.57  1.90 N 
3  1 N  A ALA 179 ? ? CA A ALA 179 ? ? C  A ALA 179 ? ? 87.57  111.00 -23.43 2.70 N 
4  1 N  A LEU 189 ? ? CA A LEU 189 ? ? C  A LEU 189 ? ? 94.45  111.00 -16.55 2.70 N 
5  1 CB B SER 145 ? ? CA B SER 145 ? ? C  B SER 145 ? ? 127.99 110.10 17.89  1.90 N 
6  1 N  B SER 145 ? ? CA B SER 145 ? ? C  B SER 145 ? ? 73.15  111.00 -37.85 2.70 N 
7  1 N  B ASP 159 ? ? CA B ASP 159 ? ? C  B ASP 159 ? ? 86.29  111.00 -24.71 2.70 N 
8  1 CB B LEU 220 ? ? CA B LEU 220 ? ? C  B LEU 220 ? ? 96.26  110.20 -13.94 1.90 N 
9  1 N  B LEU 221 ? ? CA B LEU 221 ? ? CB B LEU 221 ? ? 122.45 110.40 12.05  2.00 N 
10 1 CB B SER 306 ? ? CA B SER 306 ? ? C  B SER 306 ? ? 87.30  110.10 -22.80 1.90 N 
11 1 N  B ASN 307 ? ? CA B ASN 307 ? ? CB B ASN 307 ? ? 127.05 110.60 16.45  1.80 N 
12 1 N  B ASN 307 ? ? CA B ASN 307 ? ? C  B ASN 307 ? ? 80.92  111.00 -30.08 2.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 25  ? ? -176.27 128.63  
2  1 GLN A 45  ? ? 54.69   -146.99 
3  1 THR A 46  ? ? 66.57   -2.93   
4  1 THR A 74  ? ? -163.27 -161.37 
5  1 TRP A 94  ? ? -49.76  151.05  
6  1 ALA A 143 ? ? -96.40  -60.38  
7  1 ASP A 146 ? ? 44.28   -125.37 
8  1 ASN A 149 ? ? 69.83   -15.89  
9  1 ASP A 154 ? ? -39.65  126.58  
10 1 SER A 169 ? ? 49.93   -118.44 
11 1 LEU A 178 ? ? 82.82   -9.55   
12 1 SER A 186 ? ? 74.82   -0.28   
13 1 ILE A 187 ? ? -0.83   101.81  
14 1 ASN A 211 ? ? -1.87   -59.26  
15 1 LEU A 220 ? ? -93.22  -61.08  
16 1 LEU A 255 ? ? 72.23   -42.07  
17 1 SER A 310 ? ? 55.46   5.61    
18 1 MET B 15  ? ? 57.66   14.71   
19 1 VAL B 26  ? ? 73.92   113.89  
20 1 THR B 46  ? ? -129.04 -163.96 
21 1 VAL B 47  ? ? 60.55   167.52  
22 1 ILE B 68  ? ? 72.46   -53.00  
23 1 TRP B 94  ? ? -49.44  150.96  
24 1 HIS B 150 ? ? 54.88   9.54    
25 1 TRP B 151 ? ? -127.33 -73.10  
26 1 SER B 169 ? ? 50.36   -118.69 
27 1 LEU B 189 ? ? 32.36   53.32   
28 1 THR B 210 ? ? -117.39 -90.52  
29 1 ASN B 211 ? ? -134.05 -37.74  
30 1 LEU B 220 ? ? 72.70   -15.93  
31 1 MET B 244 ? ? 81.85   0.97    
32 1 ALA B 245 ? ? -132.05 -58.04  
33 1 SER B 306 ? ? 38.62   36.20   
34 1 TYR B 308 ? ? 20.84   62.94   
35 1 SER B 310 ? ? 55.83   13.11   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 162 ? ? 0.084 'SIDE CHAIN' 
2 1 ARG B 193 ? ? 0.232 'SIDE CHAIN' 
3 1 ARG B 209 ? ? 0.290 'SIDE CHAIN' 
4 1 ARG B 319 ? ? 0.292 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLN 9   ? A GLN 1   
2  1 Y 1 A VAL 10  ? A VAL 2   
3  1 Y 1 A GLU 30  ? A GLU 22  
4  1 Y 1 A SER 31  ? A SER 23  
5  1 Y 1 A ILE 32  ? A ILE 24  
6  1 Y 1 A ASP 33  ? A ASP 25  
7  1 Y 1 A LEU 34  ? A LEU 26  
8  1 Y 1 A ILE 35  ? A ILE 27  
9  1 Y 1 A THR 36  ? A THR 28  
10 1 Y 1 A GLN 37  ? A GLN 29  
11 1 Y 1 A GLN 38  ? A GLN 30  
12 1 Y 1 A ILE 39  ? A ILE 31  
13 1 Y 1 A PRO 40  ? A PRO 32  
14 1 Y 1 A PHE 41  ? A PHE 33  
15 1 Y 1 A LYS 42  ? A LYS 34  
16 1 Y 1 B GLU 30  ? B GLU 22  
17 1 Y 1 B SER 31  ? B SER 23  
18 1 Y 1 B ILE 32  ? B ILE 24  
19 1 Y 1 B ASP 33  ? B ASP 25  
20 1 Y 1 B LEU 34  ? B LEU 26  
21 1 Y 1 B ILE 35  ? B ILE 27  
22 1 Y 1 B THR 36  ? B THR 28  
23 1 Y 1 B GLN 37  ? B GLN 29  
24 1 Y 1 B GLN 38  ? B GLN 30  
25 1 Y 1 B ILE 39  ? B ILE 31  
26 1 Y 1 B PRO 40  ? B PRO 32  
27 1 Y 1 B PHE 41  ? B PHE 33  
28 1 Y 1 B LYS 42  ? B LYS 34  
29 1 Y 1 B ASN 72  ? B ASN 64  
30 1 Y 1 B ARG 73  ? B ARG 65  
31 1 Y 1 B THR 74  ? B THR 66  
32 1 Y 1 B ALA 75  ? B ALA 67  
33 1 Y 1 B LEU 76  ? B LEU 68  
34 1 Y 1 B PRO 77  ? B PRO 69  
35 1 Y 1 B SER 184 ? B SER 176 
36 1 Y 1 B GLY 185 ? B GLY 177 
37 1 Y 1 B SER 186 ? B SER 178 
# 
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 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'Saudi Arabia' 
_pdbx_audit_support.grant_number           'King Abdullah University of Science and Technology' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-Q9FG13-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZRO 
_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]   0.010060 
_atom_sites.fract_transf_matrix[1][2]   0.005808 
_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]   0.011617 
_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]   0.008760 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . ALA A 1 3   ? -13.363 24.477  -37.073 1.00 104.48 ? 11  ALA A N   1 
ATOM 2    C CA  . ALA A 1 3   ? -13.729 25.756  -36.477 1.00 102.34 ? 11  ALA A CA  1 
ATOM 3    C C   . ALA A 1 3   ? -14.753 25.566  -35.362 1.00 95.84  ? 11  ALA A C   1 
ATOM 4    O O   . ALA A 1 3   ? -14.675 26.220  -34.322 1.00 100.64 ? 11  ALA A O   1 
ATOM 5    C CB  . ALA A 1 3   ? -14.265 26.705  -37.538 1.00 94.32  ? 11  ALA A CB  1 
ATOM 6    N N   . GLU A 1 4   ? -15.718 24.676  -35.582 1.00 92.39  ? 12  GLU A N   1 
ATOM 7    C CA  . GLU A 1 4   ? -16.717 24.363  -34.571 1.00 98.96  ? 12  GLU A CA  1 
ATOM 8    C C   . GLU A 1 4   ? -17.035 22.875  -34.623 1.00 98.29  ? 12  GLU A C   1 
ATOM 9    O O   . GLU A 1 4   ? -16.976 22.249  -35.684 1.00 92.26  ? 12  GLU A O   1 
ATOM 10   C CB  . GLU A 1 4   ? -18.001 25.187  -34.766 1.00 97.58  ? 12  GLU A CB  1 
ATOM 11   C CG  . GLU A 1 4   ? -17.952 26.663  -34.305 1.00 92.63  ? 12  GLU A CG  1 
ATOM 12   C CD  . GLU A 1 4   ? -17.557 26.900  -32.842 1.00 93.67  ? 12  GLU A CD  1 
ATOM 13   O OE1 . GLU A 1 4   ? -16.979 26.014  -32.179 1.00 92.19  ? 12  GLU A OE1 1 
ATOM 14   O OE2 . GLU A 1 4   ? -17.838 28.011  -32.346 1.00 90.79  ? 12  GLU A OE2 1 
ATOM 15   N N   . ASP A 1 5   ? -17.371 22.313  -33.461 1.00 95.96  ? 13  ASP A N   1 
ATOM 16   C CA  . ASP A 1 5   ? -17.584 20.871  -33.318 1.00 86.66  ? 13  ASP A CA  1 
ATOM 17   C C   . ASP A 1 5   ? -18.780 20.649  -32.394 1.00 82.96  ? 13  ASP A C   1 
ATOM 18   O O   . ASP A 1 5   ? -18.655 20.751  -31.170 1.00 83.08  ? 13  ASP A O   1 
ATOM 19   C CB  . ASP A 1 5   ? -16.327 20.189  -32.787 1.00 88.64  ? 13  ASP A CB  1 
ATOM 20   C CG  . ASP A 1 5   ? -16.460 18.677  -32.716 1.00 91.04  ? 13  ASP A CG  1 
ATOM 21   O OD1 . ASP A 1 5   ? -17.392 18.176  -32.054 1.00 86.84  ? 13  ASP A OD1 1 
ATOM 22   O OD2 . ASP A 1 5   ? -15.622 17.983  -33.331 1.00 88.11  ? 13  ASP A OD2 1 
ATOM 23   N N   . CYS A 1 6   ? -19.934 20.344  -32.987 1.00 81.84  ? 14  CYS A N   1 
ATOM 24   C CA  . CYS A 1 6   ? -21.160 20.062  -32.239 1.00 86.91  ? 14  CYS A CA  1 
ATOM 25   C C   . CYS A 1 6   ? -21.219 18.576  -31.903 1.00 85.02  ? 14  CYS A C   1 
ATOM 26   O O   . CYS A 1 6   ? -21.586 17.752  -32.744 1.00 88.17  ? 14  CYS A O   1 
ATOM 27   C CB  . CYS A 1 6   ? -22.387 20.495  -33.032 1.00 90.10  ? 14  CYS A CB  1 
ATOM 28   S SG  . CYS A 1 6   ? -22.829 22.228  -32.817 1.00 100.32 ? 14  CYS A SG  1 
ATOM 29   N N   . MET A 1 7   ? -20.860 18.233  -30.667 1.00 87.09  ? 15  MET A N   1 
ATOM 30   C CA  . MET A 1 7   ? -20.991 16.892  -30.102 1.00 87.51  ? 15  MET A CA  1 
ATOM 31   C C   . MET A 1 7   ? -20.206 15.835  -30.868 1.00 86.03  ? 15  MET A C   1 
ATOM 32   O O   . MET A 1 7   ? -20.416 14.635  -30.646 1.00 77.96  ? 15  MET A O   1 
ATOM 33   C CB  . MET A 1 7   ? -22.466 16.470  -30.031 1.00 80.85  ? 15  MET A CB  1 
ATOM 34   C CG  . MET A 1 7   ? -23.375 17.468  -29.342 1.00 81.50  ? 15  MET A CG  1 
ATOM 35   S SD  . MET A 1 7   ? -24.934 16.740  -28.804 1.00 96.34  ? 15  MET A SD  1 
ATOM 36   C CE  . MET A 1 7   ? -26.102 17.845  -29.599 1.00 77.67  ? 15  MET A CE  1 
ATOM 37   N N   . GLY A 1 8   ? -19.304 16.238  -31.762 1.00 90.09  ? 16  GLY A N   1 
ATOM 38   C CA  . GLY A 1 8   ? -18.609 15.307  -32.622 1.00 91.49  ? 16  GLY A CA  1 
ATOM 39   C C   . GLY A 1 8   ? -19.348 15.000  -33.909 1.00 95.44  ? 16  GLY A C   1 
ATOM 40   O O   . GLY A 1 8   ? -18.717 14.644  -34.911 1.00 97.87  ? 16  GLY A O   1 
ATOM 41   N N   . LEU A 1 9   ? -20.678 15.118  -33.896 1.00 89.70  ? 17  LEU A N   1 
ATOM 42   C CA  . LEU A 1 9   ? -21.498 14.750  -35.041 1.00 79.74  ? 17  LEU A CA  1 
ATOM 43   C C   . LEU A 1 9   ? -21.472 15.798  -36.145 1.00 79.71  ? 17  LEU A C   1 
ATOM 44   O O   . LEU A 1 9   ? -21.766 15.467  -37.298 1.00 84.56  ? 17  LEU A O   1 
ATOM 45   C CB  . LEU A 1 9   ? -22.943 14.510  -34.591 1.00 77.99  ? 17  LEU A CB  1 
ATOM 46   C CG  . LEU A 1 9   ? -23.166 13.419  -33.537 1.00 86.70  ? 17  LEU A CG  1 
ATOM 47   C CD1 . LEU A 1 9   ? -24.640 13.062  -33.443 1.00 81.43  ? 17  LEU A CD1 1 
ATOM 48   C CD2 . LEU A 1 9   ? -22.336 12.183  -33.851 1.00 81.12  ? 17  LEU A CD2 1 
ATOM 49   N N   . LEU A 1 10  ? -21.139 17.047  -35.823 1.00 79.45  ? 18  LEU A N   1 
ATOM 50   C CA  . LEU A 1 10  ? -21.048 18.118  -36.806 1.00 79.01  ? 18  LEU A CA  1 
ATOM 51   C C   . LEU A 1 10  ? -19.690 18.786  -36.665 1.00 80.55  ? 18  LEU A C   1 
ATOM 52   O O   . LEU A 1 10  ? -19.287 19.151  -35.556 1.00 85.73  ? 18  LEU A O   1 
ATOM 53   C CB  . LEU A 1 10  ? -22.183 19.138  -36.619 1.00 79.51  ? 18  LEU A CB  1 
ATOM 54   C CG  . LEU A 1 10  ? -22.527 20.232  -37.644 1.00 84.50  ? 18  LEU A CG  1 
ATOM 55   C CD1 . LEU A 1 10  ? -23.809 20.932  -37.215 1.00 85.16  ? 18  LEU A CD1 1 
ATOM 56   C CD2 . LEU A 1 10  ? -21.424 21.270  -37.857 1.00 78.28  ? 18  LEU A CD2 1 
ATOM 57   N N   . GLN A 1 11  ? -18.990 18.940  -37.786 1.00 76.33  ? 19  GLN A N   1 
ATOM 58   C CA  . GLN A 1 11  ? -17.684 19.595  -37.820 1.00 82.45  ? 19  GLN A CA  1 
ATOM 59   C C   . GLN A 1 11  ? -17.724 20.694  -38.877 1.00 88.90  ? 19  GLN A C   1 
ATOM 60   O O   . GLN A 1 11  ? -17.679 20.409  -40.077 1.00 91.96  ? 19  GLN A O   1 
ATOM 61   C CB  . GLN A 1 11  ? -16.570 18.595  -38.117 1.00 89.03  ? 19  GLN A CB  1 
ATOM 62   C CG  . GLN A 1 11  ? -16.508 17.413  -37.170 1.00 96.64  ? 19  GLN A CG  1 
ATOM 63   C CD  . GLN A 1 11  ? -15.615 16.306  -37.692 1.00 95.19  ? 19  GLN A CD  1 
ATOM 64   O OE1 . GLN A 1 11  ? -16.081 15.210  -38.005 1.00 88.26  ? 19  GLN A OE1 1 
ATOM 65   N NE2 . GLN A 1 11  ? -14.321 16.590  -37.796 1.00 91.92  ? 19  GLN A NE2 1 
ATOM 66   N N   . LEU A 1 12  ? -17.816 21.944  -38.432 1.00 92.51  ? 20  LEU A N   1 
ATOM 67   C CA  . LEU A 1 12  ? -17.678 23.095  -39.318 1.00 91.69  ? 20  LEU A CA  1 
ATOM 68   C C   . LEU A 1 12  ? -16.203 23.478  -39.320 1.00 91.28  ? 20  LEU A C   1 
ATOM 69   O O   . LEU A 1 12  ? -15.658 23.879  -38.287 1.00 95.17  ? 20  LEU A O   1 
ATOM 70   C CB  . LEU A 1 12  ? -18.581 24.241  -38.858 1.00 92.53  ? 20  LEU A CB  1 
ATOM 71   C CG  . LEU A 1 12  ? -18.664 25.610  -39.556 1.00 88.18  ? 20  LEU A CG  1 
ATOM 72   C CD1 . LEU A 1 12  ? -17.434 26.493  -39.362 1.00 93.26  ? 20  LEU A CD1 1 
ATOM 73   C CD2 . LEU A 1 12  ? -18.939 25.413  -41.040 1.00 87.34  ? 20  LEU A CD2 1 
ATOM 74   N N   . LEU A 1 13  ? -15.556 23.342  -40.472 1.00 88.75  ? 21  LEU A N   1 
ATOM 75   C CA  . LEU A 1 13  ? -14.128 23.590  -40.590 1.00 94.99  ? 21  LEU A CA  1 
ATOM 76   C C   . LEU A 1 13  ? -13.857 25.070  -40.845 1.00 96.68  ? 21  LEU A C   1 
ATOM 77   O O   . LEU A 1 13  ? -14.770 25.861  -41.096 1.00 93.62  ? 21  LEU A O   1 
ATOM 78   C CB  . LEU A 1 13  ? -13.526 22.721  -41.693 1.00 94.87  ? 21  LEU A CB  1 
ATOM 79   C CG  . LEU A 1 13  ? -13.782 21.220  -41.536 1.00 91.53  ? 21  LEU A CG  1 
ATOM 80   C CD1 . LEU A 1 13  ? -12.947 20.422  -42.521 1.00 103.70 ? 21  LEU A CD1 1 
ATOM 81   C CD2 . LEU A 1 13  ? -13.515 20.760  -40.107 1.00 89.31  ? 21  LEU A CD2 1 
ATOM 82   N N   . SER A 1 14  ? -12.576 25.444  -40.757 1.00 99.29  ? 22  SER A N   1 
ATOM 83   C CA  . SER A 1 14  ? -12.182 26.834  -40.974 1.00 96.69  ? 22  SER A CA  1 
ATOM 84   C C   . SER A 1 14  ? -12.683 27.348  -42.318 1.00 91.24  ? 22  SER A C   1 
ATOM 85   O O   . SER A 1 14  ? -13.347 28.388  -42.389 1.00 85.32  ? 22  SER A O   1 
ATOM 86   C CB  . SER A 1 14  ? -10.661 26.961  -40.879 1.00 96.35  ? 22  SER A CB  1 
ATOM 87   O OG  . SER A 1 14  ? -10.172 26.323  -39.712 1.00 89.37  ? 22  SER A OG  1 
ATOM 88   N N   . ASN A 1 15  ? -12.379 26.632  -43.396 1.00 95.48  ? 23  ASN A N   1 
ATOM 89   C CA  . ASN A 1 15  ? -12.957 26.961  -44.689 1.00 103.30 ? 23  ASN A CA  1 
ATOM 90   C C   . ASN A 1 15  ? -14.410 26.506  -44.683 1.00 104.62 ? 23  ASN A C   1 
ATOM 91   O O   . ASN A 1 15  ? -14.751 25.503  -44.050 1.00 99.79  ? 23  ASN A O   1 
ATOM 92   C CB  . ASN A 1 15  ? -12.177 26.294  -45.823 1.00 106.95 ? 23  ASN A CB  1 
ATOM 93   C CG  . ASN A 1 15  ? -12.701 26.674  -47.197 1.00 108.52 ? 23  ASN A CG  1 
ATOM 94   O OD1 . ASN A 1 15  ? -13.184 27.787  -47.403 1.00 102.55 ? 23  ASN A OD1 1 
ATOM 95   N ND2 . ASN A 1 15  ? -12.598 25.751  -48.147 1.00 108.97 ? 23  ASN A ND2 1 
ATOM 96   N N   . GLY A 1 16  ? -15.267 27.244  -45.385 1.00 111.45 ? 24  GLY A N   1 
ATOM 97   C CA  . GLY A 1 16  ? -16.681 26.915  -45.415 1.00 108.21 ? 24  GLY A CA  1 
ATOM 98   C C   . GLY A 1 16  ? -16.488 25.477  -45.864 1.00 103.32 ? 24  GLY A C   1 
ATOM 99   O O   . GLY A 1 16  ? -15.976 25.220  -46.959 1.00 99.61  ? 24  GLY A O   1 
ATOM 100  N N   . THR A 1 17  ? -16.899 24.531  -45.023 1.00 96.24  ? 25  THR A N   1 
ATOM 101  C CA  . THR A 1 17  ? -16.827 23.107  -45.317 1.00 93.53  ? 25  THR A CA  1 
ATOM 102  C C   . THR A 1 17  ? -17.505 22.535  -44.079 1.00 86.29  ? 25  THR A C   1 
ATOM 103  O O   . THR A 1 17  ? -17.135 22.873  -42.950 1.00 85.68  ? 25  THR A O   1 
ATOM 104  C CB  . THR A 1 17  ? -15.551 22.320  -45.646 1.00 98.50  ? 25  THR A CB  1 
ATOM 105  O OG1 . THR A 1 17  ? -14.567 22.549  -44.634 1.00 103.50 ? 25  THR A OG1 1 
ATOM 106  C CG2 . THR A 1 17  ? -14.987 22.758  -46.995 1.00 102.51 ? 25  THR A CG2 1 
ATOM 107  N N   . VAL A 1 18  ? -18.496 21.670  -44.283 1.00 88.26  ? 26  VAL A N   1 
ATOM 108  C CA  . VAL A 1 18  ? -19.266 21.094  -43.186 1.00 87.34  ? 26  VAL A CA  1 
ATOM 109  C C   . VAL A 1 18  ? -19.246 19.577  -43.315 1.00 87.46  ? 26  VAL A C   1 
ATOM 110  O O   . VAL A 1 18  ? -19.520 19.036  -44.393 1.00 85.49  ? 26  VAL A O   1 
ATOM 111  C CB  . VAL A 1 18  ? -20.718 21.607  -43.162 1.00 80.57  ? 26  VAL A CB  1 
ATOM 112  C CG1 . VAL A 1 18  ? -21.423 21.111  -41.910 1.00 76.87  ? 26  VAL A CG1 1 
ATOM 113  C CG2 . VAL A 1 18  ? -20.760 23.127  -43.243 1.00 78.85  ? 26  VAL A CG2 1 
ATOM 114  N N   . LEU A 1 19  ? -18.921 18.895  -42.219 1.00 85.89  ? 27  LEU A N   1 
ATOM 115  C CA  . LEU A 1 19  ? -18.867 17.442  -42.172 1.00 84.80  ? 27  LEU A CA  1 
ATOM 116  C C   . LEU A 1 19  ? -19.835 16.941  -41.108 1.00 84.51  ? 27  LEU A C   1 
ATOM 117  O O   . LEU A 1 19  ? -20.085 17.622  -40.108 1.00 87.88  ? 27  LEU A O   1 
ATOM 118  C CB  . LEU A 1 19  ? -17.450 16.927  -41.863 1.00 88.45  ? 27  LEU A CB  1 
ATOM 119  C CG  . LEU A 1 19  ? -16.279 17.081  -42.851 1.00 94.57  ? 27  LEU A CG  1 
ATOM 120  C CD1 . LEU A 1 19  ? -16.452 16.169  -44.061 1.00 95.29  ? 27  LEU A CD1 1 
ATOM 121  C CD2 . LEU A 1 19  ? -15.986 18.524  -43.271 1.00 94.19  ? 27  LEU A CD2 1 
ATOM 122  N N   . ARG A 1 20  ? -20.385 15.746  -41.326 1.00 77.18  ? 28  ARG A N   1 
ATOM 123  C CA  . ARG A 1 20  ? -21.376 15.184  -40.417 1.00 76.48  ? 28  ARG A CA  1 
ATOM 124  C C   . ARG A 1 20  ? -21.093 13.706  -40.185 1.00 73.17  ? 28  ARG A C   1 
ATOM 125  O O   . ARG A 1 20  ? -20.189 13.121  -40.783 1.00 74.36  ? 28  ARG A O   1 
ATOM 126  C CB  . ARG A 1 20  ? -22.800 15.384  -40.950 1.00 73.08  ? 28  ARG A CB  1 
ATOM 127  C CG  . ARG A 1 20  ? -23.207 16.841  -41.034 1.00 71.66  ? 28  ARG A CG  1 
ATOM 128  C CD  . ARG A 1 20  ? -24.705 17.008  -41.171 1.00 78.73  ? 28  ARG A CD  1 
ATOM 129  N NE  . ARG A 1 20  ? -25.064 18.415  -41.283 1.00 80.22  ? 28  ARG A NE  1 
ATOM 130  C CZ  . ARG A 1 20  ? -25.468 19.164  -40.265 1.00 73.48  ? 28  ARG A CZ  1 
ATOM 131  N NH1 . ARG A 1 20  ? -25.560 18.674  -39.039 1.00 74.71  ? 28  ARG A NH1 1 
ATOM 132  N NH2 . ARG A 1 20  ? -25.775 20.440  -40.480 1.00 68.88  ? 28  ARG A NH2 1 
ATOM 133  N N   . SER A 1 21  ? -21.881 13.107  -39.297 1.00 73.64  ? 29  SER A N   1 
ATOM 134  C CA  . SER A 1 21  ? -21.696 11.709  -38.916 1.00 72.52  ? 29  SER A CA  1 
ATOM 135  C C   . SER A 1 21  ? -23.036 10.993  -38.765 1.00 72.71  ? 29  SER A C   1 
ATOM 136  O O   . SER A 1 21  ? -23.477 10.706  -37.651 1.00 54.50  ? 29  SER A O   1 
ATOM 137  C CB  . SER A 1 21  ? -20.899 11.613  -37.613 1.00 73.27  ? 29  SER A CB  1 
ATOM 138  O OG  . SER A 1 21  ? -20.769 10.268  -37.187 1.00 77.86  ? 29  SER A OG  1 
ATOM 139  N N   . ASN A 1 35  ? -43.451 1.568   -34.095 1.00 108.72 ? 43  ASN A N   1 
ATOM 140  C CA  . ASN A 1 35  ? -44.602 0.710   -34.390 1.00 108.97 ? 43  ASN A CA  1 
ATOM 141  C C   . ASN A 1 35  ? -45.624 0.972   -33.253 1.00 114.27 ? 43  ASN A C   1 
ATOM 142  O O   . ASN A 1 35  ? -46.080 0.095   -32.503 1.00 112.78 ? 43  ASN A O   1 
ATOM 143  C CB  . ASN A 1 35  ? -44.168 -0.780  -34.629 1.00 108.88 ? 43  ASN A CB  1 
ATOM 144  C CG  . ASN A 1 35  ? -44.273 -1.693  -33.405 1.00 112.40 ? 43  ASN A CG  1 
ATOM 145  O OD1 . ASN A 1 35  ? -45.364 -2.113  -33.013 1.00 108.28 ? 43  ASN A OD1 1 
ATOM 146  N ND2 . ASN A 1 35  ? -43.117 -2.091  -32.865 1.00 117.67 ? 43  ASN A ND2 1 
ATOM 147  N N   . ASN A 1 36  ? -46.049 2.238   -33.174 1.00 109.86 ? 44  ASN A N   1 
ATOM 148  C CA  . ASN A 1 36  ? -47.154 2.575   -32.236 1.00 101.25 ? 44  ASN A CA  1 
ATOM 149  C C   . ASN A 1 36  ? -48.415 2.472   -33.094 1.00 101.31 ? 44  ASN A C   1 
ATOM 150  O O   . ASN A 1 36  ? -49.524 2.465   -32.521 1.00 105.71 ? 44  ASN A O   1 
ATOM 151  C CB  . ASN A 1 36  ? -46.951 3.934   -31.579 1.00 90.48  ? 44  ASN A CB  1 
ATOM 152  C CG  . ASN A 1 36  ? -45.826 3.928   -30.574 1.00 95.90  ? 44  ASN A CG  1 
ATOM 153  O OD1 . ASN A 1 36  ? -45.466 2.871   -30.045 1.00 100.04 ? 44  ASN A OD1 1 
ATOM 154  N ND2 . ASN A 1 36  ? -45.263 5.094   -30.293 1.00 91.02  ? 44  ASN A ND2 1 
ATOM 155  N N   . GLN A 1 37  ? -48.243 2.417   -34.421 1.00 103.36 ? 45  GLN A N   1 
ATOM 156  C CA  . GLN A 1 37  ? -49.370 2.218   -35.375 1.00 105.78 ? 45  GLN A CA  1 
ATOM 157  C C   . GLN A 1 37  ? -50.494 3.246   -35.203 1.00 101.54 ? 45  GLN A C   1 
ATOM 158  O O   . GLN A 1 37  ? -50.178 4.412   -34.890 1.00 98.48  ? 45  GLN A O   1 
ATOM 159  C CB  . GLN A 1 37  ? -49.915 0.797   -35.230 1.00 109.20 ? 45  GLN A CB  1 
ATOM 160  C CG  . GLN A 1 37  ? -48.837 -0.282  -35.262 1.00 106.72 ? 45  GLN A CG  1 
ATOM 161  C CD  . GLN A 1 37  ? -47.999 -0.250  -36.522 1.00 108.28 ? 45  GLN A CD  1 
ATOM 162  O OE1 . GLN A 1 37  ? -46.985 0.450   -36.608 1.00 105.86 ? 45  GLN A OE1 1 
ATOM 163  N NE2 . GLN A 1 37  ? -48.420 -1.013  -37.519 1.00 105.22 ? 45  GLN A NE2 1 
ATOM 164  N N   . THR A 1 38  ? -51.739 2.827   -35.452 1.00 106.28 ? 46  THR A N   1 
ATOM 165  C CA  . THR A 1 38  ? -52.929 3.717   -35.359 1.00 109.14 ? 46  THR A CA  1 
ATOM 166  C C   . THR A 1 38  ? -52.877 4.791   -36.436 1.00 103.69 ? 46  THR A C   1 
ATOM 167  O O   . THR A 1 38  ? -53.878 5.526   -36.576 1.00 95.73  ? 46  THR A O   1 
ATOM 168  C CB  . THR A 1 38  ? -53.090 4.288   -33.946 1.00 97.40  ? 46  THR A CB  1 
ATOM 169  O OG1 . THR A 1 38  ? -52.611 3.295   -33.044 1.00 95.71  ? 46  THR A OG1 1 
ATOM 170  C CG2 . THR A 1 38  ? -54.536 4.589   -33.597 1.00 88.28  ? 46  THR A CG2 1 
ATOM 171  N N   . VAL A 1 39  ? -51.810 4.839   -37.239 1.00 97.09  ? 47  VAL A N   1 
ATOM 172  C CA  . VAL A 1 39  ? -51.649 5.929   -38.198 1.00 88.33  ? 47  VAL A CA  1 
ATOM 173  C C   . VAL A 1 39  ? -50.900 5.418   -39.426 1.00 92.17  ? 47  VAL A C   1 
ATOM 174  O O   . VAL A 1 39  ? -49.962 4.622   -39.308 1.00 97.35  ? 47  VAL A O   1 
ATOM 175  C CB  . VAL A 1 39  ? -50.919 7.122   -37.541 1.00 92.04  ? 47  VAL A CB  1 
ATOM 176  C CG1 . VAL A 1 39  ? -50.177 7.963   -38.575 1.00 84.16  ? 47  VAL A CG1 1 
ATOM 177  C CG2 . VAL A 1 39  ? -51.891 7.960   -36.742 1.00 92.33  ? 47  VAL A CG2 1 
ATOM 178  N N   . LEU A 1 40  ? -51.312 5.890   -40.610 1.00 88.21  ? 48  LEU A N   1 
ATOM 179  C CA  . LEU A 1 40  ? -50.578 5.653   -41.849 1.00 83.94  ? 48  LEU A CA  1 
ATOM 180  C C   . LEU A 1 40  ? -49.792 6.902   -42.228 1.00 85.87  ? 48  LEU A C   1 
ATOM 181  O O   . LEU A 1 40  ? -50.200 8.026   -41.924 1.00 85.82  ? 48  LEU A O   1 
ATOM 182  C CB  . LEU A 1 40  ? -51.493 5.298   -43.027 1.00 69.57  ? 48  LEU A CB  1 
ATOM 183  C CG  . LEU A 1 40  ? -52.623 4.272   -43.013 1.00 69.92  ? 48  LEU A CG  1 
ATOM 184  C CD1 . LEU A 1 40  ? -53.950 4.951   -42.704 1.00 79.10  ? 48  LEU A CD1 1 
ATOM 185  C CD2 . LEU A 1 40  ? -52.673 3.533   -44.342 1.00 71.86  ? 48  LEU A CD2 1 
ATOM 186  N N   . PHE A 1 41  ? -48.666 6.701   -42.911 1.00 85.32  ? 49  PHE A N   1 
ATOM 187  C CA  . PHE A 1 41  ? -47.782 7.817   -43.214 1.00 74.08  ? 49  PHE A CA  1 
ATOM 188  C C   . PHE A 1 41  ? -47.090 7.620   -44.557 1.00 79.13  ? 49  PHE A C   1 
ATOM 189  O O   . PHE A 1 41  ? -46.838 6.491   -44.986 1.00 84.39  ? 49  PHE A O   1 
ATOM 190  C CB  . PHE A 1 41  ? -46.749 8.018   -42.096 1.00 70.22  ? 49  PHE A CB  1 
ATOM 191  C CG  . PHE A 1 41  ? -45.811 6.860   -41.914 1.00 70.67  ? 49  PHE A CG  1 
ATOM 192  C CD1 . PHE A 1 41  ? -46.144 5.815   -41.070 1.00 80.86  ? 49  PHE A CD1 1 
ATOM 193  C CD2 . PHE A 1 41  ? -44.588 6.828   -42.564 1.00 69.14  ? 49  PHE A CD2 1 
ATOM 194  C CE1 . PHE A 1 41  ? -45.287 4.751   -40.892 1.00 90.61  ? 49  PHE A CE1 1 
ATOM 195  C CE2 . PHE A 1 41  ? -43.727 5.767   -42.389 1.00 74.00  ? 49  PHE A CE2 1 
ATOM 196  C CZ  . PHE A 1 41  ? -44.076 4.729   -41.551 1.00 82.63  ? 49  PHE A CZ  1 
ATOM 197  N N   . LYS A 1 42  ? -46.796 8.742   -45.216 1.00 78.76  ? 50  LYS A N   1 
ATOM 198  C CA  . LYS A 1 42  ? -46.070 8.755   -46.481 1.00 69.84  ? 50  LYS A CA  1 
ATOM 199  C C   . LYS A 1 42  ? -45.482 10.143  -46.706 1.00 63.43  ? 50  LYS A C   1 
ATOM 200  O O   . LYS A 1 42  ? -45.894 11.120  -46.076 1.00 69.85  ? 50  LYS A O   1 
ATOM 201  C CB  . LYS A 1 42  ? -46.964 8.339   -47.652 1.00 74.90  ? 50  LYS A CB  1 
ATOM 202  C CG  . LYS A 1 42  ? -48.252 9.115   -47.791 1.00 75.57  ? 50  LYS A CG  1 
ATOM 203  C CD  . LYS A 1 42  ? -48.914 8.772   -49.111 1.00 73.32  ? 50  LYS A CD  1 
ATOM 204  C CE  . LYS A 1 42  ? -49.388 7.327   -49.125 1.00 74.53  ? 50  LYS A CE  1 
ATOM 205  N NZ  . LYS A 1 42  ? -49.770 6.882   -50.495 1.00 76.61  ? 50  LYS A NZ  1 
ATOM 206  N N   . ASP A 1 43  ? -44.514 10.216  -47.617 1.00 56.93  ? 51  ASP A N   1 
ATOM 207  C CA  . ASP A 1 43  ? -43.700 11.405  -47.828 1.00 57.29  ? 51  ASP A CA  1 
ATOM 208  C C   . ASP A 1 43  ? -44.030 12.072  -49.158 1.00 56.54  ? 51  ASP A C   1 
ATOM 209  O O   . ASP A 1 43  ? -44.647 11.475  -50.046 1.00 64.64  ? 51  ASP A O   1 
ATOM 210  C CB  . ASP A 1 43  ? -42.207 11.060  -47.806 1.00 57.77  ? 51  ASP A CB  1 
ATOM 211  C CG  . ASP A 1 43  ? -41.806 10.289  -46.572 1.00 62.18  ? 51  ASP A CG  1 
ATOM 212  O OD1 . ASP A 1 43  ? -42.363 10.569  -45.495 1.00 63.58  ? 51  ASP A OD1 1 
ATOM 213  O OD2 . ASP A 1 43  ? -40.936 9.401   -46.680 1.00 69.93  ? 51  ASP A OD2 1 
ATOM 214  N N   . SER A 1 44  ? -43.607 13.331  -49.282 1.00 48.70  ? 52  SER A N   1 
ATOM 215  C CA  . SER A 1 44  ? -43.809 14.093  -50.507 1.00 56.17  ? 52  SER A CA  1 
ATOM 216  C C   . SER A 1 44  ? -42.864 15.288  -50.529 1.00 57.77  ? 52  SER A C   1 
ATOM 217  O O   . SER A 1 44  ? -42.374 15.737  -49.491 1.00 57.85  ? 52  SER A O   1 
ATOM 218  C CB  . SER A 1 44  ? -45.261 14.566  -50.646 1.00 50.91  ? 52  SER A CB  1 
ATOM 219  O OG  . SER A 1 44  ? -45.437 15.325  -51.831 1.00 56.59  ? 52  SER A OG  1 
ATOM 220  N N   . ILE A 1 45  ? -42.621 15.794  -51.742 1.00 61.90  ? 53  ILE A N   1 
ATOM 221  C CA  . ILE A 1 45  ? -41.923 17.062  -51.922 1.00 57.43  ? 53  ILE A CA  1 
ATOM 222  C C   . ILE A 1 45  ? -42.857 18.207  -51.544 1.00 60.67  ? 53  ILE A C   1 
ATOM 223  O O   . ILE A 1 45  ? -44.084 18.117  -51.692 1.00 61.24  ? 53  ILE A O   1 
ATOM 224  C CB  . ILE A 1 45  ? -41.435 17.199  -53.380 1.00 62.48  ? 53  ILE A CB  1 
ATOM 225  C CG1 . ILE A 1 45  ? -40.217 18.127  -53.513 1.00 62.47  ? 53  ILE A CG1 1 
ATOM 226  C CG2 . ILE A 1 45  ? -42.559 17.667  -54.299 1.00 65.05  ? 53  ILE A CG2 1 
ATOM 227  C CD1 . ILE A 1 45  ? -39.026 17.765  -52.679 1.00 62.73  ? 53  ILE A CD1 1 
ATOM 228  N N   . TYR A 1 46  ? -42.281 19.289  -51.016 1.00 64.87  ? 54  TYR A N   1 
ATOM 229  C CA  . TYR A 1 46  ? -43.017 20.542  -50.901 1.00 64.89  ? 54  TYR A CA  1 
ATOM 230  C C   . TYR A 1 46  ? -42.270 21.746  -51.454 1.00 69.21  ? 54  TYR A C   1 
ATOM 231  O O   . TYR A 1 46  ? -42.898 22.790  -51.664 1.00 64.48  ? 54  TYR A O   1 
ATOM 232  C CB  . TYR A 1 46  ? -43.425 20.823  -49.444 1.00 57.86  ? 54  TYR A CB  1 
ATOM 233  C CG  . TYR A 1 46  ? -42.307 21.171  -48.486 1.00 58.93  ? 54  TYR A CG  1 
ATOM 234  C CD1 . TYR A 1 46  ? -41.528 20.182  -47.900 1.00 55.76  ? 54  TYR A CD1 1 
ATOM 235  C CD2 . TYR A 1 46  ? -42.046 22.494  -48.151 1.00 60.83  ? 54  TYR A CD2 1 
ATOM 236  C CE1 . TYR A 1 46  ? -40.517 20.503  -47.014 1.00 55.82  ? 54  TYR A CE1 1 
ATOM 237  C CE2 . TYR A 1 46  ? -41.035 22.825  -47.272 1.00 57.22  ? 54  TYR A CE2 1 
ATOM 238  C CZ  . TYR A 1 46  ? -40.274 21.827  -46.705 1.00 54.77  ? 54  TYR A CZ  1 
ATOM 239  O OH  . TYR A 1 46  ? -39.267 22.157  -45.827 1.00 51.37  ? 54  TYR A OH  1 
ATOM 240  N N   . HIS A 1 47  ? -40.964 21.644  -51.694 1.00 67.39  ? 55  HIS A N   1 
ATOM 241  C CA  . HIS A 1 47  ? -40.214 22.738  -52.305 1.00 65.56  ? 55  HIS A CA  1 
ATOM 242  C C   . HIS A 1 47  ? -39.148 22.128  -53.203 1.00 67.37  ? 55  HIS A C   1 
ATOM 243  O O   . HIS A 1 47  ? -38.151 21.591  -52.710 1.00 71.06  ? 55  HIS A O   1 
ATOM 244  C CB  . HIS A 1 47  ? -39.590 23.652  -51.255 1.00 68.80  ? 55  HIS A CB  1 
ATOM 245  C CG  . HIS A 1 47  ? -39.019 24.914  -51.823 1.00 72.91  ? 55  HIS A CG  1 
ATOM 246  N ND1 . HIS A 1 47  ? -37.665 25.110  -51.990 1.00 70.92  ? 55  HIS A ND1 1 
ATOM 247  C CD2 . HIS A 1 47  ? -39.620 26.042  -52.270 1.00 75.76  ? 55  HIS A CD2 1 
ATOM 248  C CE1 . HIS A 1 47  ? -37.457 26.306  -52.511 1.00 73.93  ? 55  HIS A CE1 1 
ATOM 249  N NE2 . HIS A 1 47  ? -38.627 26.892  -52.691 1.00 80.98  ? 55  HIS A NE2 1 
ATOM 250  N N   . LYS A 1 48  ? -39.361 22.210  -54.511 1.00 61.91  ? 56  LYS A N   1 
ATOM 251  C CA  . LYS A 1 48  ? -38.438 21.665  -55.499 1.00 64.56  ? 56  LYS A CA  1 
ATOM 252  C C   . LYS A 1 48  ? -37.125 22.447  -55.580 1.00 63.62  ? 56  LYS A C   1 
ATOM 253  O O   . LYS A 1 48  ? -36.060 21.819  -55.637 1.00 59.98  ? 56  LYS A O   1 
ATOM 254  C CB  . LYS A 1 48  ? -39.106 21.608  -56.876 1.00 70.04  ? 56  LYS A CB  1 
ATOM 255  C CG  . LYS A 1 48  ? -40.119 20.484  -57.020 1.00 66.33  ? 56  LYS A CG  1 
ATOM 256  C CD  . LYS A 1 48  ? -41.090 20.754  -58.157 1.00 79.52  ? 56  LYS A CD  1 
ATOM 257  C CE  . LYS A 1 48  ? -42.107 19.632  -58.290 1.00 77.67  ? 56  LYS A CE  1 
ATOM 258  N NZ  . LYS A 1 48  ? -41.520 18.427  -58.937 1.00 59.31  ? 56  LYS A NZ  1 
ATOM 259  N N   . PRO A 1 49  ? -37.134 23.791  -55.611 1.00 63.18  ? 57  PRO A N   1 
ATOM 260  C CA  . PRO A 1 49  ? -35.852 24.509  -55.745 1.00 66.89  ? 57  PRO A CA  1 
ATOM 261  C C   . PRO A 1 49  ? -34.841 24.170  -54.662 1.00 67.49  ? 57  PRO A C   1 
ATOM 262  O O   . PRO A 1 49  ? -33.634 24.215  -54.927 1.00 68.51  ? 57  PRO A O   1 
ATOM 263  C CB  . PRO A 1 49  ? -36.257 25.991  -55.705 1.00 72.92  ? 57  PRO A CB  1 
ATOM 264  C CG  . PRO A 1 49  ? -37.700 26.021  -55.997 1.00 71.86  ? 57  PRO A CG  1 
ATOM 265  C CD  . PRO A 1 49  ? -38.275 24.726  -55.544 1.00 65.88  ? 57  PRO A CD  1 
ATOM 266  N N   . ASN A 1 50  ? -35.286 23.840  -53.450 1.00 61.22  ? 58  ASN A N   1 
ATOM 267  C CA  . ASN A 1 50  ? -34.381 23.409  -52.392 1.00 59.56  ? 58  ASN A CA  1 
ATOM 268  C C   . ASN A 1 50  ? -34.472 21.917  -52.103 1.00 61.39  ? 58  ASN A C   1 
ATOM 269  O O   . ASN A 1 50  ? -33.751 21.431  -51.224 1.00 62.84  ? 58  ASN A O   1 
ATOM 270  C CB  . ASN A 1 50  ? -34.641 24.195  -51.100 1.00 58.56  ? 58  ASN A CB  1 
ATOM 271  C CG  . ASN A 1 50  ? -34.391 25.682  -51.258 1.00 60.26  ? 58  ASN A CG  1 
ATOM 272  O OD1 . ASN A 1 50  ? -35.110 26.507  -50.695 1.00 63.99  ? 58  ASN A OD1 1 
ATOM 273  N ND2 . ASN A 1 50  ? -33.365 26.031  -52.026 1.00 60.07  ? 58  ASN A ND2 1 
ATOM 274  N N   . ASN A 1 51  ? -35.336 21.183  -52.812 1.00 59.85  ? 59  ASN A N   1 
ATOM 275  C CA  . ASN A 1 51  ? -35.451 19.728  -52.687 1.00 56.97  ? 59  ASN A CA  1 
ATOM 276  C C   . ASN A 1 51  ? -35.759 19.331  -51.241 1.00 59.64  ? 59  ASN A C   1 
ATOM 277  O O   . ASN A 1 51  ? -35.028 18.573  -50.598 1.00 58.01  ? 59  ASN A O   1 
ATOM 278  C CB  . ASN A 1 51  ? -34.181 19.039  -53.201 1.00 56.86  ? 59  ASN A CB  1 
ATOM 279  C CG  . ASN A 1 51  ? -34.362 17.548  -53.394 1.00 63.63  ? 59  ASN A CG  1 
ATOM 280  O OD1 . ASN A 1 51  ? -35.244 17.109  -54.130 1.00 71.56  ? 59  ASN A OD1 1 
ATOM 281  N ND2 . ASN A 1 51  ? -33.520 16.760  -52.735 1.00 64.23  ? 59  ASN A ND2 1 
ATOM 282  N N   . LEU A 1 52  ? -36.866 19.867  -50.736 1.00 61.53  ? 60  LEU A N   1 
ATOM 283  C CA  . LEU A 1 52  ? -37.280 19.674  -49.353 1.00 61.92  ? 60  LEU A CA  1 
ATOM 284  C C   . LEU A 1 52  ? -38.510 18.778  -49.279 1.00 65.12  ? 60  LEU A C   1 
ATOM 285  O O   . LEU A 1 52  ? -39.501 19.021  -49.975 1.00 68.87  ? 60  LEU A O   1 
ATOM 286  C CB  . LEU A 1 52  ? -37.567 21.024  -48.700 1.00 61.52  ? 60  LEU A CB  1 
ATOM 287  C CG  . LEU A 1 52  ? -36.356 21.945  -48.561 1.00 61.87  ? 60  LEU A CG  1 
ATOM 288  C CD1 . LEU A 1 52  ? -36.704 23.126  -47.688 1.00 61.74  ? 60  LEU A CD1 1 
ATOM 289  C CD2 . LEU A 1 52  ? -35.155 21.199  -47.999 1.00 58.67  ? 60  LEU A CD2 1 
ATOM 290  N N   . HIS A 1 53  ? -38.466 17.783  -48.394 1.00 57.07  ? 61  HIS A N   1 
ATOM 291  C CA  . HIS A 1 53  ? -39.516 16.784  -48.267 1.00 54.73  ? 61  HIS A CA  1 
ATOM 292  C C   . HIS A 1 53  ? -40.173 16.862  -46.897 1.00 58.64  ? 61  HIS A C   1 
ATOM 293  O O   . HIS A 1 53  ? -39.530 17.182  -45.892 1.00 57.38  ? 61  HIS A O   1 
ATOM 294  C CB  . HIS A 1 53  ? -38.975 15.363  -48.479 1.00 54.88  ? 61  HIS A CB  1 
ATOM 295  C CG  . HIS A 1 53  ? -38.385 15.129  -49.834 1.00 60.09  ? 61  HIS A CG  1 
ATOM 296  N ND1 . HIS A 1 53  ? -37.027 15.083  -50.061 1.00 66.76  ? 61  HIS A ND1 1 
ATOM 297  C CD2 . HIS A 1 53  ? -38.975 14.872  -51.026 1.00 66.04  ? 61  HIS A CD2 1 
ATOM 298  C CE1 . HIS A 1 53  ? -36.805 14.843  -51.342 1.00 73.22  ? 61  HIS A CE1 1 
ATOM 299  N NE2 . HIS A 1 53  ? -37.970 14.709  -51.949 1.00 70.92  ? 61  HIS A NE2 1 
ATOM 300  N N   . LEU A 1 54  ? -41.472 16.570  -46.879 1.00 57.11  ? 62  LEU A N   1 
ATOM 301  C CA  . LEU A 1 54  ? -42.260 16.469  -45.662 1.00 50.63  ? 62  LEU A CA  1 
ATOM 302  C C   . LEU A 1 54  ? -42.970 15.122  -45.605 1.00 47.28  ? 62  LEU A C   1 
ATOM 303  O O   . LEU A 1 54  ? -43.093 14.418  -46.610 1.00 48.75  ? 62  LEU A O   1 
ATOM 304  C CB  . LEU A 1 54  ? -43.257 17.641  -45.563 1.00 44.70  ? 62  LEU A CB  1 
ATOM 305  C CG  . LEU A 1 54  ? -44.161 18.038  -46.737 1.00 52.66  ? 62  LEU A CG  1 
ATOM 306  C CD1 . LEU A 1 54  ? -45.116 16.956  -47.199 1.00 57.32  ? 62  LEU A CD1 1 
ATOM 307  C CD2 . LEU A 1 54  ? -44.939 19.294  -46.357 1.00 58.90  ? 62  LEU A CD2 1 
ATOM 308  N N   . ARG A 1 55  ? -43.422 14.766  -44.406 1.00 50.88  ? 63  ARG A N   1 
ATOM 309  C CA  . ARG A 1 55  ? -44.147 13.526  -44.168 1.00 51.24  ? 63  ARG A CA  1 
ATOM 310  C C   . ARG A 1 55  ? -45.542 13.830  -43.637 1.00 51.68  ? 63  ARG A C   1 
ATOM 311  O O   . ARG A 1 55  ? -45.720 14.735  -42.815 1.00 52.99  ? 63  ARG A O   1 
ATOM 312  C CB  . ARG A 1 55  ? -43.397 12.621  -43.177 1.00 52.17  ? 63  ARG A CB  1 
ATOM 313  C CG  . ARG A 1 55  ? -44.015 11.237  -43.016 1.00 56.65  ? 63  ARG A CG  1 
ATOM 314  C CD  . ARG A 1 55  ? -43.157 10.318  -42.150 1.00 67.76  ? 63  ARG A CD  1 
ATOM 315  N NE  . ARG A 1 55  ? -41.743 10.326  -42.508 1.00 64.70  ? 63  ARG A NE  1 
ATOM 316  C CZ  . ARG A 1 55  ? -41.105 9.306   -43.067 1.00 64.04  ? 63  ARG A CZ  1 
ATOM 317  N NH1 . ARG A 1 55  ? -41.728 8.175   -43.353 1.00 70.04  ? 63  ARG A NH1 1 
ATOM 318  N NH2 . ARG A 1 55  ? -39.809 9.423   -43.343 1.00 68.10  ? 63  ARG A NH2 1 
ATOM 319  N N   . LEU A 1 56  ? -46.527 13.072  -44.113 1.00 53.89  ? 64  LEU A N   1 
ATOM 320  C CA  . LEU A 1 56  ? -47.915 13.193  -43.686 1.00 60.42  ? 64  LEU A CA  1 
ATOM 321  C C   . LEU A 1 56  ? -48.300 11.977  -42.857 1.00 73.77  ? 64  LEU A C   1 
ATOM 322  O O   . LEU A 1 56  ? -47.983 10.843  -43.228 1.00 73.74  ? 64  LEU A O   1 
ATOM 323  C CB  . LEU A 1 56  ? -48.860 13.323  -44.884 1.00 61.86  ? 64  LEU A CB  1 
ATOM 324  C CG  . LEU A 1 56  ? -49.168 14.717  -45.434 1.00 65.49  ? 64  LEU A CG  1 
ATOM 325  C CD1 . LEU A 1 56  ? -47.910 15.481  -45.749 1.00 62.76  ? 64  LEU A CD1 1 
ATOM 326  C CD2 . LEU A 1 56  ? -50.052 14.618  -46.672 1.00 65.02  ? 64  LEU A CD2 1 
ATOM 327  N N   . TYR A 1 57  ? -48.969 12.220  -41.732 1.00 74.10  ? 65  TYR A N   1 
ATOM 328  C CA  . TYR A 1 57  ? -49.509 11.172  -40.877 1.00 63.47  ? 65  TYR A CA  1 
ATOM 329  C C   . TYR A 1 57  ? -51.024 11.299  -40.853 1.00 64.34  ? 65  TYR A C   1 
ATOM 330  O O   . TYR A 1 57  ? -51.552 12.380  -40.574 1.00 63.84  ? 65  TYR A O   1 
ATOM 331  C CB  . TYR A 1 57  ? -48.940 11.279  -39.460 1.00 57.22  ? 65  TYR A CB  1 
ATOM 332  C CG  . TYR A 1 57  ? -47.440 11.083  -39.370 1.00 57.95  ? 65  TYR A CG  1 
ATOM 333  C CD1 . TYR A 1 57  ? -46.558 12.104  -39.711 1.00 54.63  ? 65  TYR A CD1 1 
ATOM 334  C CD2 . TYR A 1 57  ? -46.907 9.888   -38.908 1.00 67.28  ? 65  TYR A CD2 1 
ATOM 335  C CE1 . TYR A 1 57  ? -45.188 11.925  -39.623 1.00 55.55  ? 65  TYR A CE1 1 
ATOM 336  C CE2 . TYR A 1 57  ? -45.545 9.705   -38.810 1.00 63.62  ? 65  TYR A CE2 1 
ATOM 337  C CZ  . TYR A 1 57  ? -44.689 10.723  -39.166 1.00 55.60  ? 65  TYR A CZ  1 
ATOM 338  O OH  . TYR A 1 57  ? -43.329 10.537  -39.065 1.00 50.08  ? 65  TYR A OH  1 
ATOM 339  N N   . LYS A 1 58  ? -51.724 10.193  -41.105 1.00 70.95  ? 66  LYS A N   1 
ATOM 340  C CA  . LYS A 1 58  ? -53.184 10.184  -41.077 1.00 75.01  ? 66  LYS A CA  1 
ATOM 341  C C   . LYS A 1 58  ? -53.704 9.021   -40.257 1.00 88.47  ? 66  LYS A C   1 
ATOM 342  O O   . LYS A 1 58  ? -53.295 7.865   -40.482 1.00 91.33  ? 66  LYS A O   1 
ATOM 343  C CB  . LYS A 1 58  ? -53.774 10.121  -42.489 1.00 73.27  ? 66  LYS A CB  1 
ATOM 344  C CG  . LYS A 1 58  ? -55.276 9.898   -42.472 1.00 77.13  ? 66  LYS A CG  1 
ATOM 345  C CD  . LYS A 1 58  ? -55.896 9.931   -43.851 1.00 86.39  ? 66  LYS A CD  1 
ATOM 346  C CE  . LYS A 1 58  ? -55.915 11.343  -44.408 1.00 90.66  ? 66  LYS A CE  1 
ATOM 347  N NZ  . LYS A 1 58  ? -56.377 11.372  -45.823 1.00 92.67  ? 66  LYS A NZ  1 
ATOM 348  N N   . PRO A 1 59  ? -54.586 9.262   -39.282 1.00 90.18  ? 67  PRO A N   1 
ATOM 349  C CA  . PRO A 1 59  ? -55.004 8.193   -38.380 1.00 92.10  ? 67  PRO A CA  1 
ATOM 350  C C   . PRO A 1 59  ? -55.748 7.086   -39.110 1.00 97.66  ? 67  PRO A C   1 
ATOM 351  O O   . PRO A 1 59  ? -56.466 7.324   -40.083 1.00 94.17  ? 67  PRO A O   1 
ATOM 352  C CB  . PRO A 1 59  ? -55.952 8.913   -37.412 1.00 89.85  ? 67  PRO A CB  1 
ATOM 353  C CG  . PRO A 1 59  ? -55.662 10.408  -37.601 1.00 77.63  ? 67  PRO A CG  1 
ATOM 354  C CD  . PRO A 1 59  ? -54.455 10.484  -38.483 1.00 81.37  ? 67  PRO A CD  1 
ATOM 355  N N   . ILE A 1 60  ? -55.573 5.866   -38.607 1.00 97.96  ? 68  ILE A N   1 
ATOM 356  C CA  . ILE A 1 60  ? -56.246 4.681   -39.128 1.00 103.35 ? 68  ILE A CA  1 
ATOM 357  C C   . ILE A 1 60  ? -57.473 4.436   -38.265 1.00 108.14 ? 68  ILE A C   1 
ATOM 358  O O   . ILE A 1 60  ? -58.469 3.864   -38.725 1.00 110.10 ? 68  ILE A O   1 
ATOM 359  C CB  . ILE A 1 60  ? -55.317 3.455   -39.135 1.00 92.13  ? 68  ILE A CB  1 
ATOM 360  C CG1 . ILE A 1 60  ? -55.333 2.773   -37.770 1.00 82.93  ? 68  ILE A CG1 1 
ATOM 361  C CG2 . ILE A 1 60  ? -53.930 3.806   -39.564 1.00 88.54  ? 68  ILE A CG2 1 
ATOM 362  C CD1 . ILE A 1 60  ? -54.501 1.579   -37.705 1.00 77.16  ? 68  ILE A CD1 1 
ATOM 363  N N   . SER A 1 61  ? -57.396 4.847   -36.992 1.00 100.98 ? 69  SER A N   1 
ATOM 364  C CA  . SER A 1 61  ? -58.577 4.884   -36.141 1.00 103.83 ? 69  SER A CA  1 
ATOM 365  C C   . SER A 1 61  ? -59.706 5.682   -36.774 1.00 110.63 ? 69  SER A C   1 
ATOM 366  O O   . SER A 1 61  ? -60.856 5.572   -36.332 1.00 111.74 ? 69  SER A O   1 
ATOM 367  C CB  . SER A 1 61  ? -58.221 5.472   -34.772 1.00 95.49  ? 69  SER A CB  1 
ATOM 368  O OG  . SER A 1 61  ? -57.282 6.525   -34.900 1.00 81.79  ? 69  SER A OG  1 
ATOM 369  N N   . ALA A 1 62  ? -59.397 6.503   -37.781 1.00 107.47 ? 70  ALA A N   1 
ATOM 370  C CA  . ALA A 1 62  ? -60.416 7.229   -38.520 1.00 103.57 ? 70  ALA A CA  1 
ATOM 371  C C   . ALA A 1 62  ? -61.450 6.253   -39.062 1.00 104.22 ? 70  ALA A C   1 
ATOM 372  O O   . ALA A 1 62  ? -61.151 5.440   -39.943 1.00 101.93 ? 70  ALA A O   1 
ATOM 373  C CB  . ALA A 1 62  ? -59.786 8.034   -39.659 1.00 93.83  ? 70  ALA A CB  1 
ATOM 374  N N   . SER A 1 63  ? -62.670 6.337   -38.543 1.00 106.21 ? 71  SER A N   1 
ATOM 375  C CA  . SER A 1 63  ? -63.806 5.574   -39.039 1.00 105.46 ? 71  SER A CA  1 
ATOM 376  C C   . SER A 1 63  ? -64.812 6.522   -39.678 1.00 117.61 ? 71  SER A C   1 
ATOM 377  O O   . SER A 1 63  ? -66.026 6.352   -39.550 1.00 119.29 ? 71  SER A O   1 
ATOM 378  C CB  . SER A 1 63  ? -64.447 4.755   -37.922 1.00 94.09  ? 71  SER A CB  1 
ATOM 379  O OG  . SER A 1 63  ? -63.468 4.027   -37.200 1.00 93.88  ? 71  SER A OG  1 
ATOM 380  N N   . ASN A 1 64  ? -64.291 7.538   -40.368 1.00 123.18 ? 72  ASN A N   1 
ATOM 381  C CA  . ASN A 1 64  ? -65.074 8.654   -40.891 1.00 125.81 ? 72  ASN A CA  1 
ATOM 382  C C   . ASN A 1 64  ? -65.812 9.361   -39.750 1.00 122.55 ? 72  ASN A C   1 
ATOM 383  O O   . ASN A 1 64  ? -67.038 9.481   -39.735 1.00 127.01 ? 72  ASN A O   1 
ATOM 384  C CB  . ASN A 1 64  ? -66.035 8.185   -41.990 1.00 126.25 ? 72  ASN A CB  1 
ATOM 385  C CG  . ASN A 1 64  ? -66.661 9.338   -42.752 1.00 125.70 ? 72  ASN A CG  1 
ATOM 386  O OD1 . ASN A 1 64  ? -66.457 10.507  -42.418 1.00 123.99 ? 72  ASN A OD1 1 
ATOM 387  N ND2 . ASN A 1 64  ? -67.424 9.014   -43.787 1.00 123.00 ? 72  ASN A ND2 1 
ATOM 388  N N   . ARG A 1 65  ? -65.025 9.825   -38.779 1.00 114.36 ? 73  ARG A N   1 
ATOM 389  C CA  . ARG A 1 65  ? -65.556 10.519  -37.613 1.00 109.65 ? 73  ARG A CA  1 
ATOM 390  C C   . ARG A 1 65  ? -66.014 11.957  -37.813 1.00 106.57 ? 73  ARG A C   1 
ATOM 391  O O   . ARG A 1 65  ? -67.160 12.304  -37.513 1.00 102.46 ? 73  ARG A O   1 
ATOM 392  C CB  . ARG A 1 65  ? -64.490 10.623  -36.520 1.00 107.66 ? 73  ARG A CB  1 
ATOM 393  C CG  . ARG A 1 65  ? -64.070 9.292   -35.925 1.00 112.99 ? 73  ARG A CG  1 
ATOM 394  C CD  . ARG A 1 65  ? -63.065 9.490   -34.803 1.00 119.06 ? 73  ARG A CD  1 
ATOM 395  N NE  . ARG A 1 65  ? -62.626 8.223   -34.232 1.00 125.68 ? 73  ARG A NE  1 
ATOM 396  C CZ  . ARG A 1 65  ? -63.288 7.549   -33.302 1.00 137.98 ? 73  ARG A CZ  1 
ATOM 397  N NH1 . ARG A 1 65  ? -64.434 7.992   -32.813 1.00 132.20 ? 73  ARG A NH1 1 
ATOM 398  N NH2 . ARG A 1 65  ? -62.789 6.400   -32.854 1.00 148.82 ? 73  ARG A NH2 1 
ATOM 399  N N   . THR A 1 66  ? -65.115 12.796  -38.323 1.00 107.33 ? 74  THR A N   1 
ATOM 400  C CA  . THR A 1 66  ? -65.416 14.195  -38.600 1.00 102.36 ? 74  THR A CA  1 
ATOM 401  C C   . THR A 1 66  ? -64.335 14.719  -39.537 1.00 101.30 ? 74  THR A C   1 
ATOM 402  O O   . THR A 1 66  ? -63.644 13.934  -40.195 1.00 97.47  ? 74  THR A O   1 
ATOM 403  C CB  . THR A 1 66  ? -65.565 15.099  -37.370 1.00 98.49  ? 74  THR A CB  1 
ATOM 404  O OG1 . THR A 1 66  ? -66.000 16.403  -37.778 1.00 99.66  ? 74  THR A OG1 1 
ATOM 405  C CG2 . THR A 1 66  ? -64.251 15.201  -36.593 1.00 94.60  ? 74  THR A CG2 1 
ATOM 406  N N   . ALA A 1 67  ? -64.188 16.037  -39.620 1.00 101.48 ? 75  ALA A N   1 
ATOM 407  C CA  . ALA A 1 67  ? -63.123 16.647  -40.403 1.00 93.45  ? 75  ALA A CA  1 
ATOM 408  C C   . ALA A 1 67  ? -61.881 16.784  -39.529 1.00 87.33  ? 75  ALA A C   1 
ATOM 409  O O   . ALA A 1 67  ? -61.935 17.394  -38.455 1.00 91.40  ? 75  ALA A O   1 
ATOM 410  C CB  . ALA A 1 67  ? -63.565 17.999  -40.955 1.00 90.22  ? 75  ALA A CB  1 
ATOM 411  N N   . LEU A 1 68  ? -60.772 16.213  -39.986 1.00 79.18  ? 76  LEU A N   1 
ATOM 412  C CA  . LEU A 1 68  ? -59.569 16.105  -39.170 1.00 76.19  ? 76  LEU A CA  1 
ATOM 413  C C   . LEU A 1 68  ? -58.806 17.429  -39.146 1.00 79.47  ? 76  LEU A C   1 
ATOM 414  O O   . LEU A 1 68  ? -58.737 18.126  -40.162 1.00 82.27  ? 76  LEU A O   1 
ATOM 415  C CB  . LEU A 1 68  ? -58.665 14.997  -39.704 1.00 75.45  ? 76  LEU A CB  1 
ATOM 416  C CG  . LEU A 1 68  ? -58.990 13.557  -39.309 1.00 81.52  ? 76  LEU A CG  1 
ATOM 417  C CD1 . LEU A 1 68  ? -60.124 13.004  -40.155 1.00 83.41  ? 76  LEU A CD1 1 
ATOM 418  C CD2 . LEU A 1 68  ? -57.747 12.706  -39.473 1.00 80.90  ? 76  LEU A CD2 1 
ATOM 419  N N   . PRO A 1 69  ? -58.230 17.797  -38.005 1.00 80.41  ? 77  PRO A N   1 
ATOM 420  C CA  . PRO A 1 69  ? -57.396 19.000  -37.945 1.00 78.37  ? 77  PRO A CA  1 
ATOM 421  C C   . PRO A 1 69  ? -55.979 18.706  -38.417 1.00 72.50  ? 77  PRO A C   1 
ATOM 422  O O   . PRO A 1 69  ? -55.553 17.554  -38.516 1.00 73.59  ? 77  PRO A O   1 
ATOM 423  C CB  . PRO A 1 69  ? -57.412 19.369  -36.459 1.00 74.31  ? 77  PRO A CB  1 
ATOM 424  C CG  . PRO A 1 69  ? -57.646 18.074  -35.753 1.00 72.10  ? 77  PRO A CG  1 
ATOM 425  C CD  . PRO A 1 69  ? -58.408 17.168  -36.684 1.00 78.33  ? 77  PRO A CD  1 
ATOM 426  N N   . VAL A 1 70  ? -55.242 19.777  -38.704 1.00 65.91  ? 78  VAL A N   1 
ATOM 427  C CA  . VAL A 1 70  ? -53.873 19.665  -39.193 1.00 53.84  ? 78  VAL A CA  1 
ATOM 428  C C   . VAL A 1 70  ? -52.913 20.108  -38.097 1.00 54.90  ? 78  VAL A C   1 
ATOM 429  O O   . VAL A 1 70  ? -53.151 21.110  -37.413 1.00 58.08  ? 78  VAL A O   1 
ATOM 430  C CB  . VAL A 1 70  ? -53.676 20.508  -40.469 1.00 60.51  ? 78  VAL A CB  1 
ATOM 431  C CG1 . VAL A 1 70  ? -52.217 20.507  -40.902 1.00 66.63  ? 78  VAL A CG1 1 
ATOM 432  C CG2 . VAL A 1 70  ? -54.576 19.999  -41.587 1.00 69.56  ? 78  VAL A CG2 1 
ATOM 433  N N   . VAL A 1 71  ? -51.826 19.356  -37.936 1.00 51.16  ? 79  VAL A N   1 
ATOM 434  C CA  . VAL A 1 71  ? -50.810 19.606  -36.914 1.00 50.96  ? 79  VAL A CA  1 
ATOM 435  C C   . VAL A 1 71  ? -49.451 19.621  -37.605 1.00 54.26  ? 79  VAL A C   1 
ATOM 436  O O   . VAL A 1 71  ? -48.864 18.562  -37.849 1.00 60.33  ? 79  VAL A O   1 
ATOM 437  C CB  . VAL A 1 71  ? -50.841 18.570  -35.785 1.00 53.25  ? 79  VAL A CB  1 
ATOM 438  C CG1 . VAL A 1 71  ? -49.853 18.947  -34.703 1.00 46.17  ? 79  VAL A CG1 1 
ATOM 439  C CG2 . VAL A 1 71  ? -52.233 18.477  -35.195 1.00 57.87  ? 79  VAL A CG2 1 
ATOM 440  N N   . VAL A 1 72  ? -48.936 20.808  -37.908 1.00 46.38  ? 80  VAL A N   1 
ATOM 441  C CA  . VAL A 1 72  ? -47.595 20.917  -38.475 1.00 45.74  ? 80  VAL A CA  1 
ATOM 442  C C   . VAL A 1 72  ? -46.578 20.805  -37.344 1.00 46.40  ? 80  VAL A C   1 
ATOM 443  O O   . VAL A 1 72  ? -46.536 21.654  -36.448 1.00 56.12  ? 80  VAL A O   1 
ATOM 444  C CB  . VAL A 1 72  ? -47.419 22.229  -39.251 1.00 50.68  ? 80  VAL A CB  1 
ATOM 445  C CG1 . VAL A 1 72  ? -46.007 22.313  -39.813 1.00 50.08  ? 80  VAL A CG1 1 
ATOM 446  C CG2 . VAL A 1 72  ? -48.451 22.331  -40.360 1.00 45.69  ? 80  VAL A CG2 1 
ATOM 447  N N   . PHE A 1 73  ? -45.750 19.761  -37.389 1.00 42.89  ? 81  PHE A N   1 
ATOM 448  C CA  . PHE A 1 73  ? -44.717 19.526  -36.384 1.00 48.12  ? 81  PHE A CA  1 
ATOM 449  C C   . PHE A 1 73  ? -43.353 19.900  -36.954 1.00 49.73  ? 81  PHE A C   1 
ATOM 450  O O   . PHE A 1 73  ? -42.873 19.266  -37.899 1.00 52.32  ? 81  PHE A O   1 
ATOM 451  C CB  . PHE A 1 73  ? -44.720 18.071  -35.920 1.00 48.64  ? 81  PHE A CB  1 
ATOM 452  C CG  . PHE A 1 73  ? -43.604 17.744  -34.969 1.00 51.78  ? 81  PHE A CG  1 
ATOM 453  C CD1 . PHE A 1 73  ? -43.628 18.213  -33.665 1.00 55.00  ? 81  PHE A CD1 1 
ATOM 454  C CD2 . PHE A 1 73  ? -42.523 16.982  -35.382 1.00 55.17  ? 81  PHE A CD2 1 
ATOM 455  C CE1 . PHE A 1 73  ? -42.600 17.919  -32.788 1.00 58.41  ? 81  PHE A CE1 1 
ATOM 456  C CE2 . PHE A 1 73  ? -41.491 16.685  -34.509 1.00 59.03  ? 81  PHE A CE2 1 
ATOM 457  C CZ  . PHE A 1 73  ? -41.530 17.154  -33.211 1.00 59.38  ? 81  PHE A CZ  1 
ATOM 458  N N   . PHE A 1 74  ? -42.732 20.924  -36.376 1.00 49.06  ? 82  PHE A N   1 
ATOM 459  C CA  . PHE A 1 74  ? -41.370 21.312  -36.714 1.00 49.55  ? 82  PHE A CA  1 
ATOM 460  C C   . PHE A 1 74  ? -40.416 20.688  -35.703 1.00 54.39  ? 82  PHE A C   1 
ATOM 461  O O   . PHE A 1 74  ? -40.494 20.983  -34.505 1.00 59.07  ? 82  PHE A O   1 
ATOM 462  C CB  . PHE A 1 74  ? -41.223 22.832  -36.735 1.00 51.49  ? 82  PHE A CB  1 
ATOM 463  C CG  . PHE A 1 74  ? -41.934 23.489  -37.881 1.00 57.67  ? 82  PHE A CG  1 
ATOM 464  C CD1 . PHE A 1 74  ? -41.414 23.427  -39.162 1.00 53.85  ? 82  PHE A CD1 1 
ATOM 465  C CD2 . PHE A 1 74  ? -43.123 24.169  -37.677 1.00 50.52  ? 82  PHE A CD2 1 
ATOM 466  C CE1 . PHE A 1 74  ? -42.067 24.029  -40.221 1.00 48.91  ? 82  PHE A CE1 1 
ATOM 467  C CE2 . PHE A 1 74  ? -43.779 24.776  -38.730 1.00 43.58  ? 82  PHE A CE2 1 
ATOM 468  C CZ  . PHE A 1 74  ? -43.251 24.704  -40.003 1.00 46.02  ? 82  PHE A CZ  1 
ATOM 469  N N   . HIS A 1 75  ? -39.518 19.834  -36.187 1.00 55.08  ? 83  HIS A N   1 
ATOM 470  C CA  . HIS A 1 75  ? -38.625 19.092  -35.311 1.00 56.78  ? 83  HIS A CA  1 
ATOM 471  C C   . HIS A 1 75  ? -37.531 20.001  -34.749 1.00 52.99  ? 83  HIS A C   1 
ATOM 472  O O   . HIS A 1 75  ? -37.314 21.127  -35.208 1.00 49.70  ? 83  HIS A O   1 
ATOM 473  C CB  . HIS A 1 75  ? -38.009 17.910  -36.058 1.00 63.12  ? 83  HIS A CB  1 
ATOM 474  C CG  . HIS A 1 75  ? -37.096 18.309  -37.175 1.00 61.10  ? 83  HIS A CG  1 
ATOM 475  N ND1 . HIS A 1 75  ? -35.790 18.700  -36.969 1.00 62.56  ? 83  HIS A ND1 1 
ATOM 476  C CD2 . HIS A 1 75  ? -37.303 18.380  -38.511 1.00 52.01  ? 83  HIS A CD2 1 
ATOM 477  C CE1 . HIS A 1 75  ? -35.232 18.992  -38.130 1.00 56.45  ? 83  HIS A CE1 1 
ATOM 478  N NE2 . HIS A 1 75  ? -36.129 18.806  -39.082 1.00 49.29  ? 83  HIS A NE2 1 
ATOM 479  N N   . GLY A 1 76  ? -36.839 19.490  -33.734 1.00 62.51  ? 84  GLY A N   1 
ATOM 480  C CA  . GLY A 1 76  ? -35.808 20.246  -33.054 1.00 63.07  ? 84  GLY A CA  1 
ATOM 481  C C   . GLY A 1 76  ? -34.425 20.095  -33.648 1.00 63.62  ? 84  GLY A C   1 
ATOM 482  O O   . GLY A 1 76  ? -34.262 20.017  -34.867 1.00 61.82  ? 84  GLY A O   1 
ATOM 483  N N   . GLY A 1 77  ? -33.421 20.051  -32.783 1.00 62.81  ? 85  GLY A N   1 
ATOM 484  C CA  . GLY A 1 77  ? -32.038 19.942  -33.195 1.00 65.45  ? 85  GLY A CA  1 
ATOM 485  C C   . GLY A 1 77  ? -31.279 21.247  -33.281 1.00 66.42  ? 85  GLY A C   1 
ATOM 486  O O   . GLY A 1 77  ? -30.253 21.293  -33.969 1.00 64.71  ? 85  GLY A O   1 
ATOM 487  N N   . GLY A 1 78  ? -31.727 22.285  -32.580 1.00 67.17  ? 86  GLY A N   1 
ATOM 488  C CA  . GLY A 1 78  ? -31.031 23.570  -32.578 1.00 70.27  ? 86  GLY A CA  1 
ATOM 489  C C   . GLY A 1 78  ? -30.655 24.085  -33.948 1.00 70.30  ? 86  GLY A C   1 
ATOM 490  O O   . GLY A 1 78  ? -29.574 24.663  -34.120 1.00 74.10  ? 86  GLY A O   1 
ATOM 491  N N   . PHE A 1 79  ? -31.524 23.875  -34.938 1.00 71.77  ? 87  PHE A N   1 
ATOM 492  C CA  . PHE A 1 79  ? -31.379 24.330  -36.319 1.00 72.34  ? 87  PHE A CA  1 
ATOM 493  C C   . PHE A 1 79  ? -30.209 23.674  -37.043 1.00 75.18  ? 87  PHE A C   1 
ATOM 494  O O   . PHE A 1 79  ? -29.954 24.013  -38.205 1.00 79.18  ? 87  PHE A O   1 
ATOM 495  C CB  . PHE A 1 79  ? -31.232 25.855  -36.423 1.00 68.71  ? 87  PHE A CB  1 
ATOM 496  C CG  . PHE A 1 79  ? -32.456 26.611  -35.993 1.00 67.67  ? 87  PHE A CG  1 
ATOM 497  C CD1 . PHE A 1 79  ? -33.563 26.700  -36.821 1.00 67.70  ? 87  PHE A CD1 1 
ATOM 498  C CD2 . PHE A 1 79  ? -32.499 27.235  -34.757 1.00 65.05  ? 87  PHE A CD2 1 
ATOM 499  C CE1 . PHE A 1 79  ? -34.690 27.395  -36.425 1.00 68.71  ? 87  PHE A CE1 1 
ATOM 500  C CE2 . PHE A 1 79  ? -33.622 27.932  -34.354 1.00 68.74  ? 87  PHE A CE2 1 
ATOM 501  C CZ  . PHE A 1 79  ? -34.719 28.012  -35.189 1.00 69.52  ? 87  PHE A CZ  1 
ATOM 502  N N   . CYS A 1 80  ? -29.488 22.749  -36.405 1.00 74.58  ? 88  CYS A N   1 
ATOM 503  C CA  . CYS A 1 80  ? -28.327 22.114  -37.009 1.00 72.95  ? 88  CYS A CA  1 
ATOM 504  C C   . CYS A 1 80  ? -28.439 20.601  -37.116 1.00 74.61  ? 88  CYS A C   1 
ATOM 505  O O   . CYS A 1 80  ? -27.620 19.989  -37.811 1.00 78.81  ? 88  CYS A O   1 
ATOM 506  C CB  . CYS A 1 80  ? -27.054 22.463  -36.221 1.00 70.79  ? 88  CYS A CB  1 
ATOM 507  S SG  . CYS A 1 80  ? -26.849 24.227  -35.869 1.00 89.89  ? 88  CYS A SG  1 
ATOM 508  N N   . PHE A 1 81  ? -29.423 19.984  -36.467 1.00 73.43  ? 89  PHE A N   1 
ATOM 509  C CA  . PHE A 1 81  ? -29.642 18.549  -36.558 1.00 71.53  ? 89  PHE A CA  1 
ATOM 510  C C   . PHE A 1 81  ? -31.129 18.287  -36.751 1.00 72.22  ? 89  PHE A C   1 
ATOM 511  O O   . PHE A 1 81  ? -31.965 19.185  -36.609 1.00 77.88  ? 89  PHE A O   1 
ATOM 512  C CB  . PHE A 1 81  ? -29.127 17.812  -35.315 1.00 69.45  ? 89  PHE A CB  1 
ATOM 513  C CG  . PHE A 1 81  ? -27.640 17.900  -35.128 1.00 73.50  ? 89  PHE A CG  1 
ATOM 514  C CD1 . PHE A 1 81  ? -26.781 17.445  -36.114 1.00 70.27  ? 89  PHE A CD1 1 
ATOM 515  C CD2 . PHE A 1 81  ? -27.101 18.431  -33.967 1.00 77.93  ? 89  PHE A CD2 1 
ATOM 516  C CE1 . PHE A 1 81  ? -25.410 17.524  -35.950 1.00 78.84  ? 89  PHE A CE1 1 
ATOM 517  C CE2 . PHE A 1 81  ? -25.732 18.511  -33.797 1.00 84.19  ? 89  PHE A CE2 1 
ATOM 518  C CZ  . PHE A 1 81  ? -24.887 18.057  -34.787 1.00 83.65  ? 89  PHE A CZ  1 
ATOM 519  N N   . GLY A 1 82  ? -31.450 17.037  -37.082 1.00 68.56  ? 90  GLY A N   1 
ATOM 520  C CA  . GLY A 1 82  ? -32.831 16.603  -37.144 1.00 61.86  ? 90  GLY A CA  1 
ATOM 521  C C   . GLY A 1 82  ? -33.310 16.218  -38.528 1.00 55.07  ? 90  GLY A C   1 
ATOM 522  O O   . GLY A 1 82  ? -32.826 16.743  -39.534 1.00 55.73  ? 90  GLY A O   1 
ATOM 523  N N   . SER A 1 83  ? -34.255 15.287  -38.587 1.00 55.15  ? 91  SER A N   1 
ATOM 524  C CA  . SER A 1 83  ? -34.878 14.896  -39.841 1.00 52.78  ? 91  SER A CA  1 
ATOM 525  C C   . SER A 1 83  ? -36.224 14.261  -39.534 1.00 56.70  ? 91  SER A C   1 
ATOM 526  O O   . SER A 1 83  ? -36.396 13.621  -38.495 1.00 62.07  ? 91  SER A O   1 
ATOM 527  C CB  . SER A 1 83  ? -33.991 13.930  -40.635 1.00 53.77  ? 91  SER A CB  1 
ATOM 528  O OG  . SER A 1 83  ? -34.674 13.418  -41.765 1.00 61.79  ? 91  SER A OG  1 
ATOM 529  N N   . ARG A 1 84  ? -37.189 14.477  -40.435 1.00 56.31  ? 92  ARG A N   1 
ATOM 530  C CA  . ARG A 1 84  ? -38.489 13.823  -40.299 1.00 58.41  ? 92  ARG A CA  1 
ATOM 531  C C   . ARG A 1 84  ? -38.347 12.311  -40.179 1.00 62.72  ? 92  ARG A C   1 
ATOM 532  O O   . ARG A 1 84  ? -39.173 11.657  -39.533 1.00 61.99  ? 92  ARG A O   1 
ATOM 533  C CB  . ARG A 1 84  ? -39.392 14.180  -41.483 1.00 55.96  ? 92  ARG A CB  1 
ATOM 534  C CG  . ARG A 1 84  ? -38.970 13.556  -42.801 1.00 65.22  ? 92  ARG A CG  1 
ATOM 535  C CD  . ARG A 1 84  ? -39.793 14.081  -43.970 1.00 55.27  ? 92  ARG A CD  1 
ATOM 536  N NE  . ARG A 1 84  ? -39.727 13.196  -45.129 1.00 49.14  ? 92  ARG A NE  1 
ATOM 537  C CZ  . ARG A 1 84  ? -38.626 12.922  -45.819 1.00 49.92  ? 92  ARG A CZ  1 
ATOM 538  N NH1 . ARG A 1 84  ? -37.463 13.482  -45.523 1.00 52.98  ? 92  ARG A NH1 1 
ATOM 539  N NH2 . ARG A 1 84  ? -38.694 12.069  -46.837 1.00 55.24  ? 92  ARG A NH2 1 
ATOM 540  N N   . SER A 1 85  ? -37.309 11.739  -40.797 1.00 64.91  ? 93  SER A N   1 
ATOM 541  C CA  . SER A 1 85  ? -37.097 10.297  -40.775 1.00 64.59  ? 93  SER A CA  1 
ATOM 542  C C   . SER A 1 85  ? -36.537 9.792   -39.450 1.00 62.17  ? 93  SER A C   1 
ATOM 543  O O   . SER A 1 85  ? -36.639 8.591   -39.175 1.00 59.62  ? 93  SER A O   1 
ATOM 544  C CB  . SER A 1 85  ? -36.163 9.885   -41.916 1.00 63.97  ? 93  SER A CB  1 
ATOM 545  O OG  . SER A 1 85  ? -34.963 10.640  -41.890 1.00 62.29  ? 93  SER A OG  1 
ATOM 546  N N   . TRP A 1 86  ? -35.929 10.669  -38.640 1.00 62.96  ? 94  TRP A N   1 
ATOM 547  C CA  . TRP A 1 86  ? -35.343 10.300  -37.352 1.00 66.82  ? 94  TRP A CA  1 
ATOM 548  C C   . TRP A 1 86  ? -36.316 9.492   -36.498 1.00 69.94  ? 94  TRP A C   1 
ATOM 549  O O   . TRP A 1 86  ? -37.535 9.666   -36.616 1.00 65.92  ? 94  TRP A O   1 
ATOM 550  C CB  . TRP A 1 86  ? -34.886 11.544  -36.586 1.00 62.67  ? 94  TRP A CB  1 
ATOM 551  C CG  . TRP A 1 86  ? -33.513 12.006  -36.957 1.00 62.53  ? 94  TRP A CG  1 
ATOM 552  C CD1 . TRP A 1 86  ? -32.828 11.708  -38.099 1.00 67.57  ? 94  TRP A CD1 1 
ATOM 553  C CD2 . TRP A 1 86  ? -32.634 12.806  -36.158 1.00 64.00  ? 94  TRP A CD2 1 
ATOM 554  N NE1 . TRP A 1 86  ? -31.588 12.300  -38.074 1.00 68.98  ? 94  TRP A NE1 1 
ATOM 555  C CE2 . TRP A 1 86  ? -31.443 12.976  -36.891 1.00 63.32  ? 94  TRP A CE2 1 
ATOM 556  C CE3 . TRP A 1 86  ? -32.743 13.404  -34.899 1.00 67.37  ? 94  TRP A CE3 1 
ATOM 557  C CZ2 . TRP A 1 86  ? -30.368 13.720  -36.407 1.00 60.72  ? 94  TRP A CZ2 1 
ATOM 558  C CZ3 . TRP A 1 86  ? -31.675 14.143  -34.420 1.00 67.78  ? 94  TRP A CZ3 1 
ATOM 559  C CH2 . TRP A 1 86  ? -30.504 14.293  -35.173 1.00 66.25  ? 94  TRP A CH2 1 
ATOM 560  N N   . PRO A 1 87  ? -35.817 8.606   -35.619 1.00 74.79  ? 95  PRO A N   1 
ATOM 561  C CA  . PRO A 1 87  ? -36.718 7.721   -34.864 1.00 70.69  ? 95  PRO A CA  1 
ATOM 562  C C   . PRO A 1 87  ? -37.693 8.457   -33.955 1.00 67.74  ? 95  PRO A C   1 
ATOM 563  O O   . PRO A 1 87  ? -38.902 8.436   -34.206 1.00 65.10  ? 95  PRO A O   1 
ATOM 564  C CB  . PRO A 1 87  ? -35.755 6.841   -34.054 1.00 65.16  ? 95  PRO A CB  1 
ATOM 565  C CG  . PRO A 1 87  ? -34.465 7.585   -34.020 1.00 65.65  ? 95  PRO A CG  1 
ATOM 566  C CD  . PRO A 1 87  ? -34.399 8.382   -35.283 1.00 69.86  ? 95  PRO A CD  1 
ATOM 567  N N   . HIS A 1 88  ? -37.195 9.108   -32.899 1.00 69.56  ? 96  HIS A N   1 
ATOM 568  C CA  . HIS A 1 88  ? -38.098 9.686   -31.909 1.00 77.68  ? 96  HIS A CA  1 
ATOM 569  C C   . HIS A 1 88  ? -38.879 10.874  -32.458 1.00 69.32  ? 96  HIS A C   1 
ATOM 570  O O   . HIS A 1 88  ? -39.947 11.193  -31.924 1.00 74.18  ? 96  HIS A O   1 
ATOM 571  C CB  . HIS A 1 88  ? -37.332 10.093  -30.646 1.00 83.03  ? 96  HIS A CB  1 
ATOM 572  C CG  . HIS A 1 88  ? -36.314 11.170  -30.864 1.00 83.73  ? 96  HIS A CG  1 
ATOM 573  N ND1 . HIS A 1 88  ? -35.405 11.142  -31.899 1.00 78.64  ? 96  HIS A ND1 1 
ATOM 574  C CD2 . HIS A 1 88  ? -36.055 12.301  -30.167 1.00 81.15  ? 96  HIS A CD2 1 
ATOM 575  C CE1 . HIS A 1 88  ? -34.635 12.214  -31.835 1.00 82.68  ? 96  HIS A CE1 1 
ATOM 576  N NE2 . HIS A 1 88  ? -35.009 12.933  -30.792 1.00 82.15  ? 96  HIS A NE2 1 
ATOM 577  N N   . PHE A 1 89  ? -38.380 11.534  -33.506 1.00 64.53  ? 97  PHE A N   1 
ATOM 578  C CA  . PHE A 1 89  ? -39.213 12.491  -34.229 1.00 65.79  ? 97  PHE A CA  1 
ATOM 579  C C   . PHE A 1 89  ? -40.390 11.783  -34.890 1.00 63.12  ? 97  PHE A C   1 
ATOM 580  O O   . PHE A 1 89  ? -41.549 12.171  -34.705 1.00 56.37  ? 97  PHE A O   1 
ATOM 581  C CB  . PHE A 1 89  ? -38.383 13.236  -35.275 1.00 67.12  ? 97  PHE A CB  1 
ATOM 582  C CG  . PHE A 1 89  ? -37.418 14.228  -34.696 1.00 70.76  ? 97  PHE A CG  1 
ATOM 583  C CD1 . PHE A 1 89  ? -37.636 14.780  -33.445 1.00 80.84  ? 97  PHE A CD1 1 
ATOM 584  C CD2 . PHE A 1 89  ? -36.300 14.622  -35.411 1.00 65.01  ? 97  PHE A CD2 1 
ATOM 585  C CE1 . PHE A 1 89  ? -36.749 15.699  -32.914 1.00 75.74  ? 97  PHE A CE1 1 
ATOM 586  C CE2 . PHE A 1 89  ? -35.412 15.540  -34.887 1.00 67.47  ? 97  PHE A CE2 1 
ATOM 587  C CZ  . PHE A 1 89  ? -35.636 16.079  -33.636 1.00 71.15  ? 97  PHE A CZ  1 
ATOM 588  N N   . HIS A 1 90  ? -40.099 10.736  -35.666 1.00 63.82  ? 98  HIS A N   1 
ATOM 589  C CA  . HIS A 1 90  ? -41.145 9.932   -36.294 1.00 65.45  ? 98  HIS A CA  1 
ATOM 590  C C   . HIS A 1 90  ? -42.119 9.393   -35.252 1.00 73.24  ? 98  HIS A C   1 
ATOM 591  O O   . HIS A 1 90  ? -43.340 9.507   -35.408 1.00 72.92  ? 98  HIS A O   1 
ATOM 592  C CB  . HIS A 1 90  ? -40.491 8.792   -37.082 1.00 64.33  ? 98  HIS A CB  1 
ATOM 593  C CG  . HIS A 1 90  ? -41.444 7.960   -37.884 1.00 65.18  ? 98  HIS A CG  1 
ATOM 594  N ND1 . HIS A 1 90  ? -42.801 8.193   -37.922 1.00 68.81  ? 98  HIS A ND1 1 
ATOM 595  C CD2 . HIS A 1 90  ? -41.224 6.889   -38.682 1.00 65.89  ? 98  HIS A CD2 1 
ATOM 596  C CE1 . HIS A 1 90  ? -43.377 7.301   -38.709 1.00 72.20  ? 98  HIS A CE1 1 
ATOM 597  N NE2 . HIS A 1 90  ? -42.442 6.498   -39.182 1.00 73.58  ? 98  HIS A NE2 1 
ATOM 598  N N   . ASN A 1 91  ? -41.589 8.791   -34.183 1.00 73.28  ? 99  ASN A N   1 
ATOM 599  C CA  . ASN A 1 91  ? -42.432 8.238   -33.126 1.00 69.46  ? 99  ASN A CA  1 
ATOM 600  C C   . ASN A 1 91  ? -43.381 9.288   -32.558 1.00 65.98  ? 99  ASN A C   1 
ATOM 601  O O   . ASN A 1 91  ? -44.583 9.040   -32.414 1.00 63.76  ? 99  ASN A O   1 
ATOM 602  C CB  . ASN A 1 91  ? -41.556 7.652   -32.017 1.00 72.62  ? 99  ASN A CB  1 
ATOM 603  C CG  . ASN A 1 91  ? -40.744 6.460   -32.486 1.00 73.98  ? 99  ASN A CG  1 
ATOM 604  O OD1 . ASN A 1 91  ? -40.958 5.940   -33.580 1.00 68.07  ? 99  ASN A OD1 1 
ATOM 605  N ND2 . ASN A 1 91  ? -39.804 6.021   -31.656 1.00 74.81  ? 99  ASN A ND2 1 
ATOM 606  N N   . PHE A 1 92  ? -42.852 10.470  -32.230 1.00 63.31  ? 100 PHE A N   1 
ATOM 607  C CA  . PHE A 1 92  ? -43.678 11.552  -31.699 1.00 64.48  ? 100 PHE A CA  1 
ATOM 608  C C   . PHE A 1 92  ? -44.811 11.903  -32.657 1.00 61.50  ? 100 PHE A C   1 
ATOM 609  O O   . PHE A 1 92  ? -45.965 12.058  -32.241 1.00 59.21  ? 100 PHE A O   1 
ATOM 610  C CB  . PHE A 1 92  ? -42.795 12.770  -31.407 1.00 62.93  ? 100 PHE A CB  1 
ATOM 611  C CG  . PHE A 1 92  ? -43.503 13.895  -30.697 1.00 65.19  ? 100 PHE A CG  1 
ATOM 612  C CD1 . PHE A 1 92  ? -44.293 14.796  -31.393 1.00 62.70  ? 100 PHE A CD1 1 
ATOM 613  C CD2 . PHE A 1 92  ? -43.380 14.044  -29.325 1.00 68.56  ? 100 PHE A CD2 1 
ATOM 614  C CE1 . PHE A 1 92  ? -44.935 15.828  -30.736 1.00 64.48  ? 100 PHE A CE1 1 
ATOM 615  C CE2 . PHE A 1 92  ? -44.026 15.070  -28.663 1.00 70.48  ? 100 PHE A CE2 1 
ATOM 616  C CZ  . PHE A 1 92  ? -44.805 15.963  -29.370 1.00 74.24  ? 100 PHE A CZ  1 
ATOM 617  N N   . CYS A 1 93  ? -44.492 12.062  -33.944 1.00 63.99  ? 101 CYS A N   1 
ATOM 618  C CA  . CYS A 1 93  ? -45.521 12.374  -34.932 1.00 63.39  ? 101 CYS A CA  1 
ATOM 619  C C   . CYS A 1 93  ? -46.624 11.321  -34.945 1.00 66.05  ? 101 CYS A C   1 
ATOM 620  O O   . CYS A 1 93  ? -47.806 11.656  -35.088 1.00 67.64  ? 101 CYS A O   1 
ATOM 621  C CB  . CYS A 1 93  ? -44.898 12.520  -36.318 1.00 58.37  ? 101 CYS A CB  1 
ATOM 622  S SG  . CYS A 1 93  ? -43.576 13.744  -36.434 1.00 66.49  ? 101 CYS A SG  1 
ATOM 623  N N   . LEU A 1 94  ? -46.260 10.041  -34.817 1.00 65.51  ? 102 LEU A N   1 
ATOM 624  C CA  . LEU A 1 94  ? -47.274 8.992   -34.752 1.00 68.48  ? 102 LEU A CA  1 
ATOM 625  C C   . LEU A 1 94  ? -48.165 9.162   -33.529 1.00 68.81  ? 102 LEU A C   1 
ATOM 626  O O   . LEU A 1 94  ? -49.388 9.004   -33.616 1.00 70.26  ? 102 LEU A O   1 
ATOM 627  C CB  . LEU A 1 94  ? -46.611 7.615   -34.738 1.00 69.86  ? 102 LEU A CB  1 
ATOM 628  C CG  . LEU A 1 94  ? -45.863 7.171   -35.995 1.00 66.10  ? 102 LEU A CG  1 
ATOM 629  C CD1 . LEU A 1 94  ? -44.643 6.347   -35.618 1.00 64.97  ? 102 LEU A CD1 1 
ATOM 630  C CD2 . LEU A 1 94  ? -46.780 6.386   -36.923 1.00 62.47  ? 102 LEU A CD2 1 
ATOM 631  N N   . THR A 1 95  ? -47.568 9.472   -32.376 1.00 64.47  ? 103 THR A N   1 
ATOM 632  C CA  . THR A 1 95  ? -48.352 9.662   -31.159 1.00 60.88  ? 103 THR A CA  1 
ATOM 633  C C   . THR A 1 95  ? -49.275 10.868  -31.283 1.00 60.90  ? 103 THR A C   1 
ATOM 634  O O   . THR A 1 95  ? -50.439 10.813  -30.866 1.00 62.45  ? 103 THR A O   1 
ATOM 635  C CB  . THR A 1 95  ? -47.432 9.812   -29.947 1.00 62.01  ? 103 THR A CB  1 
ATOM 636  O OG1 . THR A 1 95  ? -46.724 11.055  -30.029 1.00 68.39  ? 103 THR A OG1 1 
ATOM 637  C CG2 . THR A 1 95  ? -46.439 8.663   -29.884 1.00 66.08  ? 103 THR A CG2 1 
ATOM 638  N N   . LEU A 1 96  ? -48.762 11.976  -31.825 1.00 60.62  ? 104 LEU A N   1 
ATOM 639  C CA  . LEU A 1 96  ? -49.580 13.166  -32.041 1.00 64.40  ? 104 LEU A CA  1 
ATOM 640  C C   . LEU A 1 96  ? -50.821 12.847  -32.864 1.00 65.00  ? 104 LEU A C   1 
ATOM 641  O O   . LEU A 1 96  ? -51.950 13.107  -32.439 1.00 71.82  ? 104 LEU A O   1 
ATOM 642  C CB  . LEU A 1 96  ? -48.751 14.242  -32.746 1.00 65.33  ? 104 LEU A CB  1 
ATOM 643  C CG  . LEU A 1 96  ? -48.090 15.341  -31.919 1.00 60.83  ? 104 LEU A CG  1 
ATOM 644  C CD1 . LEU A 1 96  ? -47.763 16.535  -32.804 1.00 63.97  ? 104 LEU A CD1 1 
ATOM 645  C CD2 . LEU A 1 96  ? -48.976 15.760  -30.764 1.00 66.88  ? 104 LEU A CD2 1 
ATOM 646  N N   . ALA A 1 97  ? -50.620 12.271  -34.050 1.00 62.89  ? 105 ALA A N   1 
ATOM 647  C CA  . ALA A 1 97  ? -51.737 11.928  -34.926 1.00 68.98  ? 105 ALA A CA  1 
ATOM 648  C C   . ALA A 1 97  ? -52.758 11.051  -34.210 1.00 73.47  ? 105 ALA A C   1 
ATOM 649  O O   . ALA A 1 97  ? -53.955 11.354  -34.199 1.00 74.30  ? 105 ALA A O   1 
ATOM 650  C CB  . ALA A 1 97  ? -51.217 11.254  -36.194 1.00 69.54  ? 105 ALA A CB  1 
ATOM 651  N N   . SER A 1 98  ? -52.301 9.942   -33.624 1.00 74.82  ? 106 SER A N   1 
ATOM 652  C CA  . SER A 1 98  ? -53.199 9.028   -32.922 1.00 73.71  ? 106 SER A CA  1 
ATOM 653  C C   . SER A 1 98  ? -53.957 9.745   -31.811 1.00 73.60  ? 106 SER A C   1 
ATOM 654  O O   . SER A 1 98  ? -55.192 9.770   -31.799 1.00 72.54  ? 106 SER A O   1 
ATOM 655  C CB  . SER A 1 98  ? -52.412 7.841   -32.357 1.00 72.16  ? 106 SER A CB  1 
ATOM 656  O OG  . SER A 1 98  ? -51.425 8.268   -31.434 1.00 72.37  ? 106 SER A OG  1 
ATOM 657  N N   . SER A 1 99  ? -53.227 10.316  -30.850 1.00 73.18  ? 107 SER A N   1 
ATOM 658  C CA  . SER A 1 99  ? -53.870 10.887  -29.672 1.00 66.85  ? 107 SER A CA  1 
ATOM 659  C C   . SER A 1 99  ? -54.716 12.108  -30.019 1.00 68.24  ? 107 SER A C   1 
ATOM 660  O O   . SER A 1 99  ? -55.796 12.301  -29.449 1.00 72.84  ? 107 SER A O   1 
ATOM 661  C CB  . SER A 1 99  ? -52.812 11.257  -28.633 1.00 62.33  ? 107 SER A CB  1 
ATOM 662  O OG  . SER A 1 99  ? -51.979 10.152  -28.331 1.00 71.16  ? 107 SER A OG  1 
ATOM 663  N N   . LEU A 1 100 ? -54.246 12.943  -30.949 1.00 68.13  ? 108 LEU A N   1 
ATOM 664  C CA  . LEU A 1 100 ? -55.005 14.121  -31.355 1.00 70.73  ? 108 LEU A CA  1 
ATOM 665  C C   . LEU A 1 100 ? -56.070 13.838  -32.409 1.00 72.54  ? 108 LEU A C   1 
ATOM 666  O O   . LEU A 1 100 ? -56.892 14.723  -32.672 1.00 76.76  ? 108 LEU A O   1 
ATOM 667  C CB  . LEU A 1 100 ? -54.047 15.201  -31.875 1.00 68.43  ? 108 LEU A CB  1 
ATOM 668  C CG  . LEU A 1 100 ? -53.310 16.116  -30.887 1.00 68.25  ? 108 LEU A CG  1 
ATOM 669  C CD1 . LEU A 1 100 ? -52.627 15.346  -29.765 1.00 74.57  ? 108 LEU A CD1 1 
ATOM 670  C CD2 . LEU A 1 100 ? -52.278 16.939  -31.640 1.00 71.03  ? 108 LEU A CD2 1 
ATOM 671  N N   . ASN A 1 101 ? -56.102 12.639  -32.983 1.00 68.92  ? 109 ASN A N   1 
ATOM 672  C CA  . ASN A 1 101 ? -56.935 12.330  -34.147 1.00 75.51  ? 109 ASN A CA  1 
ATOM 673  C C   . ASN A 1 101 ? -56.814 13.432  -35.202 1.00 79.57  ? 109 ASN A C   1 
ATOM 674  O O   . ASN A 1 101 ? -57.779 14.109  -35.556 1.00 79.43  ? 109 ASN A O   1 
ATOM 675  C CB  . ASN A 1 101 ? -58.391 12.122  -33.730 1.00 78.52  ? 109 ASN A CB  1 
ATOM 676  C CG  . ASN A 1 101 ? -59.183 11.321  -34.742 1.00 88.85  ? 109 ASN A CG  1 
ATOM 677  O OD1 . ASN A 1 101 ? -60.228 11.766  -35.220 1.00 86.33  ? 109 ASN A OD1 1 
ATOM 678  N ND2 . ASN A 1 101 ? -58.693 10.133  -35.072 1.00 90.63  ? 109 ASN A ND2 1 
ATOM 679  N N   . ALA A 1 102 ? -55.591 13.598  -35.706 1.00 78.44  ? 110 ALA A N   1 
ATOM 680  C CA  . ALA A 1 102 ? -55.254 14.758  -36.517 1.00 75.91  ? 110 ALA A CA  1 
ATOM 681  C C   . ALA A 1 102 ? -54.259 14.381  -37.605 1.00 74.83  ? 110 ALA A C   1 
ATOM 682  O O   . ALA A 1 102 ? -53.430 13.483  -37.430 1.00 75.18  ? 110 ALA A O   1 
ATOM 683  C CB  . ALA A 1 102 ? -54.687 15.889  -35.655 1.00 71.61  ? 110 ALA A CB  1 
ATOM 684  N N   . LEU A 1 103 ? -54.357 15.081  -38.733 1.00 63.73  ? 111 LEU A N   1 
ATOM 685  C CA  . LEU A 1 103 ? -53.316 15.019  -39.751 1.00 55.52  ? 111 LEU A CA  1 
ATOM 686  C C   . LEU A 1 103 ? -52.066 15.741  -39.262 1.00 58.69  ? 111 LEU A C   1 
ATOM 687  O O   . LEU A 1 103 ? -52.122 16.916  -38.885 1.00 58.24  ? 111 LEU A O   1 
ATOM 688  C CB  . LEU A 1 103 ? -53.789 15.659  -41.054 1.00 58.62  ? 111 LEU A CB  1 
ATOM 689  C CG  . LEU A 1 103 ? -54.420 14.837  -42.176 1.00 63.09  ? 111 LEU A CG  1 
ATOM 690  C CD1 . LEU A 1 103 ? -54.542 15.721  -43.391 1.00 54.96  ? 111 LEU A CD1 1 
ATOM 691  C CD2 . LEU A 1 103 ? -53.585 13.637  -42.505 1.00 65.78  ? 111 LEU A CD2 1 
ATOM 692  N N   . VAL A 1 104 ? -50.939 15.037  -39.261 1.00 59.61  ? 112 VAL A N   1 
ATOM 693  C CA  . VAL A 1 104 ? -49.658 15.607  -38.867 1.00 55.93  ? 112 VAL A CA  1 
ATOM 694  C C   . VAL A 1 104 ? -48.826 15.853  -40.117 1.00 54.90  ? 112 VAL A C   1 
ATOM 695  O O   . VAL A 1 104 ? -48.784 15.013  -41.026 1.00 61.72  ? 112 VAL A O   1 
ATOM 696  C CB  . VAL A 1 104 ? -48.926 14.677  -37.880 1.00 61.19  ? 112 VAL A CB  1 
ATOM 697  C CG1 . VAL A 1 104 ? -47.517 15.178  -37.605 1.00 62.80  ? 112 VAL A CG1 1 
ATOM 698  C CG2 . VAL A 1 104 ? -49.715 14.564  -36.587 1.00 67.56  ? 112 VAL A CG2 1 
ATOM 699  N N   . VAL A 1 105 ? -48.164 17.007  -40.164 1.00 51.81  ? 113 VAL A N   1 
ATOM 700  C CA  . VAL A 1 105 ? -47.263 17.378  -41.250 1.00 47.96  ? 113 VAL A CA  1 
ATOM 701  C C   . VAL A 1 105 ? -45.888 17.608  -40.638 1.00 43.16  ? 113 VAL A C   1 
ATOM 702  O O   . VAL A 1 105 ? -45.669 18.617  -39.956 1.00 51.50  ? 113 VAL A O   1 
ATOM 703  C CB  . VAL A 1 105 ? -47.749 18.623  -42.005 1.00 54.50  ? 113 VAL A CB  1 
ATOM 704  C CG1 . VAL A 1 105 ? -46.733 19.034  -43.062 1.00 61.67  ? 113 VAL A CG1 1 
ATOM 705  C CG2 . VAL A 1 105 ? -49.109 18.364  -42.636 1.00 53.81  ? 113 VAL A CG2 1 
ATOM 706  N N   . SER A 1 106 ? -44.968 16.667  -40.861 1.00 41.49  ? 114 SER A N   1 
ATOM 707  C CA  . SER A 1 106 ? -43.613 16.735  -40.317 1.00 48.26  ? 114 SER A CA  1 
ATOM 708  C C   . SER A 1 106 ? -42.626 17.015  -41.444 1.00 52.29  ? 114 SER A C   1 
ATOM 709  O O   . SER A 1 106 ? -42.143 16.081  -42.103 1.00 53.17  ? 114 SER A O   1 
ATOM 710  C CB  . SER A 1 106 ? -43.258 15.433  -39.595 1.00 50.22  ? 114 SER A CB  1 
ATOM 711  O OG  . SER A 1 106 ? -41.967 15.508  -39.014 1.00 53.75  ? 114 SER A OG  1 
ATOM 712  N N   . PRO A 1 107 ? -42.289 18.276  -41.706 1.00 48.80  ? 115 PRO A N   1 
ATOM 713  C CA  . PRO A 1 107 ? -41.332 18.593  -42.769 1.00 46.70  ? 115 PRO A CA  1 
ATOM 714  C C   . PRO A 1 107 ? -39.885 18.619  -42.306 1.00 47.69  ? 115 PRO A C   1 
ATOM 715  O O   . PRO A 1 107 ? -39.572 18.850  -41.137 1.00 51.20  ? 115 PRO A O   1 
ATOM 716  C CB  . PRO A 1 107 ? -41.777 19.995  -43.208 1.00 47.88  ? 115 PRO A CB  1 
ATOM 717  C CG  . PRO A 1 107 ? -42.261 20.612  -41.941 1.00 44.91  ? 115 PRO A CG  1 
ATOM 718  C CD  . PRO A 1 107 ? -42.900 19.493  -41.143 1.00 44.78  ? 115 PRO A CD  1 
ATOM 719  N N   . ASP A 1 108 ? -38.992 18.376  -43.262 1.00 51.98  ? 116 ASP A N   1 
ATOM 720  C CA  . ASP A 1 108 ? -37.594 18.738  -43.090 1.00 50.52  ? 116 ASP A CA  1 
ATOM 721  C C   . ASP A 1 108 ? -37.397 20.203  -43.448 1.00 50.53  ? 116 ASP A C   1 
ATOM 722  O O   . ASP A 1 108 ? -37.974 20.703  -44.418 1.00 55.25  ? 116 ASP A O   1 
ATOM 723  C CB  . ASP A 1 108 ? -36.684 17.879  -43.970 1.00 55.99  ? 116 ASP A CB  1 
ATOM 724  C CG  . ASP A 1 108 ? -36.662 16.429  -43.551 1.00 56.97  ? 116 ASP A CG  1 
ATOM 725  O OD1 . ASP A 1 108 ? -36.210 16.141  -42.425 1.00 55.24  ? 116 ASP A OD1 1 
ATOM 726  O OD2 . ASP A 1 108 ? -37.061 15.573  -44.368 1.00 58.50  ? 116 ASP A OD2 1 
ATOM 727  N N   . TYR A 1 109 ? -36.575 20.892  -42.666 1.00 46.55  ? 117 TYR A N   1 
ATOM 728  C CA  . TYR A 1 109 ? -36.146 22.239  -43.000 1.00 54.98  ? 117 TYR A CA  1 
ATOM 729  C C   . TYR A 1 109 ? -34.631 22.255  -43.137 1.00 58.15  ? 117 TYR A C   1 
ATOM 730  O O   . TYR A 1 109 ? -33.933 21.423  -42.549 1.00 59.89  ? 117 TYR A O   1 
ATOM 731  C CB  . TYR A 1 109 ? -36.619 23.265  -41.953 1.00 60.59  ? 117 TYR A CB  1 
ATOM 732  C CG  . TYR A 1 109 ? -36.267 22.950  -40.513 1.00 62.25  ? 117 TYR A CG  1 
ATOM 733  C CD1 . TYR A 1 109 ? -34.975 23.131  -40.033 1.00 62.11  ? 117 TYR A CD1 1 
ATOM 734  C CD2 . TYR A 1 109 ? -37.231 22.477  -39.631 1.00 54.56  ? 117 TYR A CD2 1 
ATOM 735  C CE1 . TYR A 1 109 ? -34.655 22.850  -38.718 1.00 56.61  ? 117 TYR A CE1 1 
ATOM 736  C CE2 . TYR A 1 109 ? -36.919 22.190  -38.316 1.00 49.75  ? 117 TYR A CE2 1 
ATOM 737  C CZ  . TYR A 1 109 ? -35.630 22.379  -37.865 1.00 53.35  ? 117 TYR A CZ  1 
ATOM 738  O OH  . TYR A 1 109 ? -35.314 22.096  -36.556 1.00 52.17  ? 117 TYR A OH  1 
ATOM 739  N N   . ARG A 1 110 ? -34.131 23.187  -43.947 1.00 56.58  ? 118 ARG A N   1 
ATOM 740  C CA  . ARG A 1 110 ? -32.695 23.287  -44.168 1.00 57.10  ? 118 ARG A CA  1 
ATOM 741  C C   . ARG A 1 110 ? -31.962 23.514  -42.849 1.00 65.49  ? 118 ARG A C   1 
ATOM 742  O O   . ARG A 1 110 ? -32.473 24.152  -41.926 1.00 69.40  ? 118 ARG A O   1 
ATOM 743  C CB  . ARG A 1 110 ? -32.382 24.407  -45.160 1.00 58.28  ? 118 ARG A CB  1 
ATOM 744  C CG  . ARG A 1 110 ? -32.816 24.105  -46.585 1.00 61.23  ? 118 ARG A CG  1 
ATOM 745  C CD  . ARG A 1 110 ? -32.563 25.287  -47.509 1.00 63.79  ? 118 ARG A CD  1 
ATOM 746  N NE  . ARG A 1 110 ? -33.392 26.434  -47.158 1.00 65.02  ? 118 ARG A NE  1 
ATOM 747  C CZ  . ARG A 1 110 ? -33.373 27.598  -47.793 1.00 68.19  ? 118 ARG A CZ  1 
ATOM 748  N NH1 . ARG A 1 110 ? -32.508 27.842  -48.765 1.00 68.31  ? 118 ARG A NH1 1 
ATOM 749  N NH2 . ARG A 1 110 ? -34.218 28.555  -47.420 1.00 70.10  ? 118 ARG A NH2 1 
ATOM 750  N N   . LEU A 1 111 ? -30.749 22.978  -42.771 1.00 65.50  ? 119 LEU A N   1 
ATOM 751  C CA  . LEU A 1 111 ? -29.987 22.906  -41.535 1.00 63.40  ? 119 LEU A CA  1 
ATOM 752  C C   . LEU A 1 111 ? -28.739 23.773  -41.607 1.00 69.34  ? 119 LEU A C   1 
ATOM 753  O O   . LEU A 1 111 ? -28.087 23.858  -42.652 1.00 75.18  ? 119 LEU A O   1 
ATOM 754  C CB  . LEU A 1 111 ? -29.595 21.456  -41.239 1.00 68.57  ? 119 LEU A CB  1 
ATOM 755  C CG  . LEU A 1 111 ? -30.711 20.474  -40.886 1.00 71.25  ? 119 LEU A CG  1 
ATOM 756  C CD1 . LEU A 1 111 ? -30.179 19.426  -39.947 1.00 65.36  ? 119 LEU A CD1 1 
ATOM 757  C CD2 . LEU A 1 111 ? -31.863 21.203  -40.218 1.00 65.33  ? 119 LEU A CD2 1 
ATOM 758  N N   . ALA A 1 112 ? -28.424 24.419  -40.491 1.00 78.42  ? 120 ALA A N   1 
ATOM 759  C CA  . ALA A 1 112 ? -27.165 25.118  -40.313 1.00 80.92  ? 120 ALA A CA  1 
ATOM 760  C C   . ALA A 1 112 ? -26.051 24.117  -40.021 1.00 81.04  ? 120 ALA A C   1 
ATOM 761  O O   . ALA A 1 112 ? -26.318 22.982  -39.617 1.00 82.53  ? 120 ALA A O   1 
ATOM 762  C CB  . ALA A 1 112 ? -27.293 26.129  -39.176 1.00 80.32  ? 120 ALA A CB  1 
ATOM 763  N N   . PRO A 1 113 ? -24.778 24.506  -40.216 1.00 80.19  ? 121 PRO A N   1 
ATOM 764  C CA  . PRO A 1 113 ? -24.261 25.786  -40.730 1.00 78.49  ? 121 PRO A CA  1 
ATOM 765  C C   . PRO A 1 113 ? -24.346 25.901  -42.248 1.00 77.80  ? 121 PRO A C   1 
ATOM 766  O O   . PRO A 1 113 ? -24.130 26.984  -42.789 1.00 83.02  ? 121 PRO A O   1 
ATOM 767  C CB  . PRO A 1 113 ? -22.808 25.786  -40.243 1.00 86.74  ? 121 PRO A CB  1 
ATOM 768  C CG  . PRO A 1 113 ? -22.433 24.338  -40.220 1.00 90.43  ? 121 PRO A CG  1 
ATOM 769  C CD  . PRO A 1 113 ? -23.684 23.607  -39.803 1.00 85.29  ? 121 PRO A CD  1 
ATOM 770  N N   . GLU A 1 114 ? -24.631 24.804  -42.956 1.00 73.67  ? 122 GLU A N   1 
ATOM 771  C CA  . GLU A 1 114 ? -24.727 24.867  -44.411 1.00 75.79  ? 122 GLU A CA  1 
ATOM 772  C C   . GLU A 1 114 ? -25.778 25.881  -44.844 1.00 70.47  ? 122 GLU A C   1 
ATOM 773  O O   . GLU A 1 114 ? -25.535 26.708  -45.731 1.00 69.71  ? 122 GLU A O   1 
ATOM 774  C CB  . GLU A 1 114 ? -25.047 23.485  -44.986 1.00 75.07  ? 122 GLU A CB  1 
ATOM 775  C CG  . GLU A 1 114 ? -24.196 22.344  -44.445 1.00 74.31  ? 122 GLU A CG  1 
ATOM 776  C CD  . GLU A 1 114 ? -24.866 21.619  -43.296 1.00 73.11  ? 122 GLU A CD  1 
ATOM 777  O OE1 . GLU A 1 114 ? -25.919 22.096  -42.827 1.00 76.39  ? 122 GLU A OE1 1 
ATOM 778  O OE2 . GLU A 1 114 ? -24.355 20.561  -42.876 1.00 74.37  ? 122 GLU A OE2 1 
ATOM 779  N N   . HIS A 1 115 ? -26.955 25.830  -44.227 1.00 71.03  ? 123 HIS A N   1 
ATOM 780  C CA  . HIS A 1 115 ? -28.045 26.762  -44.503 1.00 66.48  ? 123 HIS A CA  1 
ATOM 781  C C   . HIS A 1 115 ? -28.359 27.522  -43.214 1.00 71.46  ? 123 HIS A C   1 
ATOM 782  O O   . HIS A 1 115 ? -29.081 27.016  -42.349 1.00 72.10  ? 123 HIS A O   1 
ATOM 783  C CB  . HIS A 1 115 ? -29.270 26.017  -45.030 1.00 65.03  ? 123 HIS A CB  1 
ATOM 784  C CG  . HIS A 1 115 ? -29.060 25.362  -46.363 1.00 62.78  ? 123 HIS A CG  1 
ATOM 785  N ND1 . HIS A 1 115 ? -28.843 24.007  -46.501 1.00 60.70  ? 123 HIS A ND1 1 
ATOM 786  C CD2 . HIS A 1 115 ? -29.044 25.874  -47.617 1.00 66.26  ? 123 HIS A CD2 1 
ATOM 787  C CE1 . HIS A 1 115 ? -28.696 23.714  -47.780 1.00 67.91  ? 123 HIS A CE1 1 
ATOM 788  N NE2 . HIS A 1 115 ? -28.814 24.829  -48.479 1.00 66.95  ? 123 HIS A NE2 1 
ATOM 789  N N   . ARG A 1 116 ? -27.814 28.728  -43.082 1.00 71.53  ? 124 ARG A N   1 
ATOM 790  C CA  . ARG A 1 116 ? -28.027 29.547  -41.901 1.00 67.98  ? 124 ARG A CA  1 
ATOM 791  C C   . ARG A 1 116 ? -29.400 30.213  -41.978 1.00 63.04  ? 124 ARG A C   1 
ATOM 792  O O   . ARG A 1 116 ? -29.992 30.343  -43.057 1.00 62.98  ? 124 ARG A O   1 
ATOM 793  C CB  . ARG A 1 116 ? -26.921 30.599  -41.802 1.00 70.45  ? 124 ARG A CB  1 
ATOM 794  C CG  . ARG A 1 116 ? -25.515 30.010  -41.658 1.00 73.68  ? 124 ARG A CG  1 
ATOM 795  C CD  . ARG A 1 116 ? -24.461 31.097  -41.536 1.00 84.91  ? 124 ARG A CD  1 
ATOM 796  N NE  . ARG A 1 116 ? -23.189 30.566  -41.063 1.00 86.15  ? 124 ARG A NE  1 
ATOM 797  C CZ  . ARG A 1 116 ? -22.854 30.470  -39.785 1.00 85.62  ? 124 ARG A CZ  1 
ATOM 798  N NH1 . ARG A 1 116 ? -23.682 30.849  -38.827 1.00 79.64  ? 124 ARG A NH1 1 
ATOM 799  N NH2 . ARG A 1 116 ? -21.662 29.978  -39.462 1.00 89.55  ? 124 ARG A NH2 1 
ATOM 800  N N   . LEU A 1 117 ? -29.904 30.648  -40.819 1.00 63.40  ? 125 LEU A N   1 
ATOM 801  C CA  . LEU A 1 117 ? -31.206 31.306  -40.796 1.00 63.37  ? 125 LEU A CA  1 
ATOM 802  C C   . LEU A 1 117 ? -31.143 32.572  -41.654 1.00 63.13  ? 125 LEU A C   1 
ATOM 803  O O   . LEU A 1 117 ? -30.080 33.192  -41.790 1.00 63.10  ? 125 LEU A O   1 
ATOM 804  C CB  . LEU A 1 117 ? -31.640 31.678  -39.375 1.00 56.62  ? 125 LEU A CB  1 
ATOM 805  C CG  . LEU A 1 117 ? -31.760 30.599  -38.308 1.00 51.98  ? 125 LEU A CG  1 
ATOM 806  C CD1 . LEU A 1 117 ? -30.545 30.824  -37.524 1.00 55.77  ? 125 LEU A CD1 1 
ATOM 807  C CD2 . LEU A 1 117 ? -32.977 30.711  -37.429 1.00 52.81  ? 125 LEU A CD2 1 
ATOM 808  N N   . PRO A 1 118 ? -32.272 32.990  -42.246 1.00 65.67  ? 126 PRO A N   1 
ATOM 809  C CA  . PRO A 1 118 ? -33.633 32.483  -42.055 1.00 64.64  ? 126 PRO A CA  1 
ATOM 810  C C   . PRO A 1 118 ? -34.002 31.317  -42.964 1.00 65.69  ? 126 PRO A C   1 
ATOM 811  O O   . PRO A 1 118 ? -35.179 31.170  -43.277 1.00 67.44  ? 126 PRO A O   1 
ATOM 812  C CB  . PRO A 1 118 ? -34.481 33.726  -42.344 1.00 68.45  ? 126 PRO A CB  1 
ATOM 813  C CG  . PRO A 1 118 ? -33.721 34.432  -43.437 1.00 74.31  ? 126 PRO A CG  1 
ATOM 814  C CD  . PRO A 1 118 ? -32.252 34.133  -43.182 1.00 68.84  ? 126 PRO A CD  1 
ATOM 815  N N   . ALA A 1 119 ? -33.035 30.516  -43.424 1.00 64.09  ? 127 ALA A N   1 
ATOM 816  C CA  . ALA A 1 119 ? -33.334 29.345  -44.247 1.00 66.52  ? 127 ALA A CA  1 
ATOM 817  C C   . ALA A 1 119 ? -34.491 28.525  -43.688 1.00 64.36  ? 127 ALA A C   1 
ATOM 818  O O   . ALA A 1 119 ? -35.463 28.238  -44.395 1.00 63.92  ? 127 ALA A O   1 
ATOM 819  C CB  . ALA A 1 119 ? -32.084 28.471  -44.387 1.00 61.93  ? 127 ALA A CB  1 
ATOM 820  N N   . ALA A 1 120 ? -34.399 28.138  -42.413 1.00 57.68  ? 128 ALA A N   1 
ATOM 821  C CA  . ALA A 1 120 ? -35.439 27.304  -41.816 1.00 59.14  ? 128 ALA A CA  1 
ATOM 822  C C   . ALA A 1 120 ? -36.794 28.006  -41.818 1.00 61.29  ? 128 ALA A C   1 
ATOM 823  O O   . ALA A 1 120 ? -37.827 27.372  -42.066 1.00 57.81  ? 128 ALA A O   1 
ATOM 824  C CB  . ALA A 1 120 ? -35.047 26.905  -40.393 1.00 65.70  ? 128 ALA A CB  1 
ATOM 825  N N   . PHE A 1 121 ? -36.815 29.314  -41.539 1.00 63.46  ? 129 PHE A N   1 
ATOM 826  C CA  . PHE A 1 121 ? -38.090 30.026  -41.515 1.00 63.48  ? 129 PHE A CA  1 
ATOM 827  C C   . PHE A 1 121 ? -38.700 30.118  -42.906 1.00 64.10  ? 129 PHE A C   1 
ATOM 828  O O   . PHE A 1 121 ? -39.910 29.922  -43.074 1.00 64.18  ? 129 PHE A O   1 
ATOM 829  C CB  . PHE A 1 121 ? -37.926 31.428  -40.936 1.00 63.89  ? 129 PHE A CB  1 
ATOM 830  C CG  . PHE A 1 121 ? -37.311 31.457  -39.578 1.00 59.00  ? 129 PHE A CG  1 
ATOM 831  C CD1 . PHE A 1 121 ? -37.825 30.684  -38.550 1.00 57.39  ? 129 PHE A CD1 1 
ATOM 832  C CD2 . PHE A 1 121 ? -36.269 32.319  -39.306 1.00 62.88  ? 129 PHE A CD2 1 
ATOM 833  C CE1 . PHE A 1 121 ? -37.266 30.722  -37.295 1.00 59.46  ? 129 PHE A CE1 1 
ATOM 834  C CE2 . PHE A 1 121 ? -35.722 32.376  -38.051 1.00 62.64  ? 129 PHE A CE2 1 
ATOM 835  C CZ  . PHE A 1 121 ? -36.216 31.570  -37.044 1.00 57.90  ? 129 PHE A CZ  1 
ATOM 836  N N   . GLU A 1 122 ? -37.883 30.448  -43.909 1.00 63.62  ? 130 GLU A N   1 
ATOM 837  C CA  . GLU A 1 122 ? -38.359 30.450  -45.287 1.00 61.31  ? 130 GLU A CA  1 
ATOM 838  C C   . GLU A 1 122 ? -38.953 29.099  -45.659 1.00 60.24  ? 130 GLU A C   1 
ATOM 839  O O   . GLU A 1 122 ? -40.014 29.029  -46.289 1.00 63.34  ? 130 GLU A O   1 
ATOM 840  C CB  . GLU A 1 122 ? -37.218 30.820  -46.233 1.00 62.77  ? 130 GLU A CB  1 
ATOM 841  C CG  . GLU A 1 122 ? -36.683 32.225  -46.033 1.00 68.77  ? 130 GLU A CG  1 
ATOM 842  C CD  . GLU A 1 122 ? -35.561 32.562  -46.994 1.00 75.96  ? 130 GLU A CD  1 
ATOM 843  O OE1 . GLU A 1 122 ? -35.219 31.701  -47.831 1.00 68.75  ? 130 GLU A OE1 1 
ATOM 844  O OE2 . GLU A 1 122 ? -35.019 33.684  -46.908 1.00 81.07  ? 130 GLU A OE2 1 
ATOM 845  N N   . ASP A 1 123 ? -38.275 28.014  -45.279 1.00 57.01  ? 131 ASP A N   1 
ATOM 846  C CA  . ASP A 1 123 ? -38.786 26.679  -45.561 1.00 57.65  ? 131 ASP A CA  1 
ATOM 847  C C   . ASP A 1 123 ? -40.097 26.426  -44.831 1.00 60.17  ? 131 ASP A C   1 
ATOM 848  O O   . ASP A 1 123 ? -41.007 25.795  -45.379 1.00 64.94  ? 131 ASP A O   1 
ATOM 849  C CB  . ASP A 1 123 ? -37.745 25.636  -45.165 1.00 53.54  ? 131 ASP A CB  1 
ATOM 850  C CG  . ASP A 1 123 ? -36.418 25.855  -45.850 1.00 54.28  ? 131 ASP A CG  1 
ATOM 851  O OD1 . ASP A 1 123 ? -36.401 26.474  -46.933 1.00 60.92  ? 131 ASP A OD1 1 
ATOM 852  O OD2 . ASP A 1 123 ? -35.391 25.415  -45.297 1.00 61.59  ? 131 ASP A OD2 1 
ATOM 853  N N   . ALA A 1 124 ? -40.208 26.904  -43.589 1.00 57.15  ? 132 ALA A N   1 
ATOM 854  C CA  . ALA A 1 124 ? -41.457 26.775  -42.843 1.00 55.12  ? 132 ALA A CA  1 
ATOM 855  C C   . ALA A 1 124 ? -42.615 27.411  -43.601 1.00 55.59  ? 132 ALA A C   1 
ATOM 856  O O   . ALA A 1 124 ? -43.682 26.805  -43.753 1.00 58.69  ? 132 ALA A O   1 
ATOM 857  C CB  . ALA A 1 124 ? -41.308 27.406  -41.460 1.00 53.24  ? 132 ALA A CB  1 
ATOM 858  N N   . GLU A 1 125 ? -42.426 28.649  -44.062 1.00 53.39  ? 133 GLU A N   1 
ATOM 859  C CA  . GLU A 1 125 ? -43.430 29.297  -44.900 1.00 56.39  ? 133 GLU A CA  1 
ATOM 860  C C   . GLU A 1 125 ? -43.747 28.458  -46.132 1.00 59.82  ? 133 GLU A C   1 
ATOM 861  O O   . GLU A 1 125 ? -44.898 28.412  -46.581 1.00 61.27  ? 133 GLU A O   1 
ATOM 862  C CB  . GLU A 1 125 ? -42.949 30.687  -45.307 1.00 65.30  ? 133 GLU A CB  1 
ATOM 863  C CG  . GLU A 1 125 ? -43.039 31.720  -44.200 1.00 71.54  ? 133 GLU A CG  1 
ATOM 864  C CD  . GLU A 1 125 ? -42.447 33.049  -44.609 1.00 79.27  ? 133 GLU A CD  1 
ATOM 865  O OE1 . GLU A 1 125 ? -42.769 33.526  -45.716 1.00 80.25  ? 133 GLU A OE1 1 
ATOM 866  O OE2 . GLU A 1 125 ? -41.659 33.616  -43.823 1.00 75.98  ? 133 GLU A OE2 1 
ATOM 867  N N   . ALA A 1 126 ? -42.773 27.705  -46.631 1.00 58.81  ? 134 ALA A N   1 
ATOM 868  C CA  . ALA A 1 126 ? -43.052 26.939  -47.866 1.00 54.32  ? 134 ALA A CA  1 
ATOM 869  C C   . ALA A 1 126 ? -43.996 25.789  -47.531 1.00 61.21  ? 134 ALA A C   1 
ATOM 870  O O   . ALA A 1 126 ? -44.825 25.427  -48.384 1.00 59.82  ? 134 ALA A O   1 
ATOM 871  C CB  . ALA A 1 126 ? -41.779 26.436  -48.477 1.00 50.31  ? 134 ALA A CB  1 
ATOM 872  N N   . VAL A 1 127 ? -43.869 25.232  -46.325 1.00 64.59  ? 135 VAL A N   1 
ATOM 873  C CA  . VAL A 1 127 ? -44.785 24.142  -45.879 1.00 59.56  ? 135 VAL A CA  1 
ATOM 874  C C   . VAL A 1 127 ? -46.214 24.684  -45.930 1.00 60.16  ? 135 VAL A C   1 
ATOM 875  O O   . VAL A 1 127 ? -47.060 24.074  -46.601 1.00 63.26  ? 135 VAL A O   1 
ATOM 876  C CB  . VAL A 1 127 ? -44.437 23.677  -44.457 1.00 49.38  ? 135 VAL A CB  1 
ATOM 877  C CG1 . VAL A 1 127 ? -45.227 22.439  -44.057 1.00 50.47  ? 135 VAL A CG1 1 
ATOM 878  C CG2 . VAL A 1 127 ? -42.945 23.442  -44.285 1.00 51.07  ? 135 VAL A CG2 1 
ATOM 879  N N   . LEU A 1 128 ? -46.458 25.797  -45.247 1.00 57.57  ? 136 LEU A N   1 
ATOM 880  C CA  . LEU A 1 128 ? -47.822 26.373  -45.200 1.00 57.63  ? 136 LEU A CA  1 
ATOM 881  C C   . LEU A 1 128 ? -48.331 26.590  -46.629 1.00 63.90  ? 136 LEU A C   1 
ATOM 882  O O   . LEU A 1 128 ? -49.446 26.131  -46.931 1.00 73.00  ? 136 LEU A O   1 
ATOM 883  C CB  . LEU A 1 128 ? -47.778 27.668  -44.400 1.00 58.67  ? 136 LEU A CB  1 
ATOM 884  C CG  . LEU A 1 128 ? -48.167 27.551  -42.924 1.00 57.96  ? 136 LEU A CG  1 
ATOM 885  C CD1 . LEU A 1 128 ? -47.106 26.810  -42.132 1.00 52.13  ? 136 LEU A CD1 1 
ATOM 886  C CD2 . LEU A 1 128 ? -48.420 28.925  -42.335 1.00 60.12  ? 136 LEU A CD2 1 
ATOM 887  N N   . THR A 1 129 ? -47.542 27.253  -47.475 1.00 64.35  ? 137 THR A N   1 
ATOM 888  C CA  . THR A 1 129 ? -47.998 27.545  -48.848 1.00 64.76  ? 137 THR A CA  1 
ATOM 889  C C   . THR A 1 129 ? -48.329 26.245  -49.539 1.00 61.84  ? 137 THR A C   1 
ATOM 890  O O   . THR A 1 129 ? -49.315 26.211  -50.294 1.00 63.47  ? 137 THR A O   1 
ATOM 891  C CB  . THR A 1 129 ? -46.917 28.319  -49.595 1.00 65.82  ? 137 THR A CB  1 
ATOM 892  O OG1 . THR A 1 129 ? -45.765 27.486  -49.547 1.00 68.24  ? 137 THR A OG1 1 
ATOM 893  C CG2 . THR A 1 129 ? -46.632 29.669  -48.963 1.00 61.93  ? 137 THR A CG2 1 
ATOM 894  N N   . TRP A 1 130 ? -47.533 25.206  -49.294 1.00 58.01  ? 138 TRP A N   1 
ATOM 895  C CA  . TRP A 1 130 ? -47.765 23.886  -49.926 1.00 61.36  ? 138 TRP A CA  1 
ATOM 896  C C   . TRP A 1 130 ? -49.112 23.339  -49.485 1.00 66.61  ? 138 TRP A C   1 
ATOM 897  O O   . TRP A 1 130 ? -49.886 22.885  -50.340 1.00 70.67  ? 138 TRP A O   1 
ATOM 898  C CB  . TRP A 1 130 ? -46.644 22.917  -49.541 1.00 64.00  ? 138 TRP A CB  1 
ATOM 899  C CG  . TRP A 1 130 ? -46.778 21.542  -50.139 1.00 71.52  ? 138 TRP A CG  1 
ATOM 900  C CD1 . TRP A 1 130 ? -46.374 21.146  -51.378 1.00 77.30  ? 138 TRP A CD1 1 
ATOM 901  C CD2 . TRP A 1 130 ? -47.353 20.375  -49.514 1.00 69.01  ? 138 TRP A CD2 1 
ATOM 902  N NE1 . TRP A 1 130 ? -46.650 19.819  -51.568 1.00 74.88  ? 138 TRP A NE1 1 
ATOM 903  C CE2 . TRP A 1 130 ? -47.253 19.320  -50.445 1.00 67.24  ? 138 TRP A CE2 1 
ATOM 904  C CE3 . TRP A 1 130 ? -47.941 20.121  -48.272 1.00 63.53  ? 138 TRP A CE3 1 
ATOM 905  C CZ2 . TRP A 1 130 ? -47.717 18.038  -50.169 1.00 65.56  ? 138 TRP A CZ2 1 
ATOM 906  C CZ3 . TRP A 1 130 ? -48.405 18.854  -48.002 1.00 61.39  ? 138 TRP A CZ3 1 
ATOM 907  C CH2 . TRP A 1 130 ? -48.292 17.830  -48.938 1.00 64.93  ? 138 TRP A CH2 1 
ATOM 908  N N   . LEU A 1 131 ? -49.378 23.380  -48.183 1.00 67.70  ? 139 LEU A N   1 
ATOM 909  C CA  . LEU A 1 131 ? -50.650 22.837  -47.646 1.00 67.04  ? 139 LEU A CA  1 
ATOM 910  C C   . LEU A 1 131 ? -51.831 23.608  -48.248 1.00 71.54  ? 139 LEU A C   1 
ATOM 911  O O   . LEU A 1 131 ? -52.899 23.005  -48.422 1.00 73.33  ? 139 LEU A O   1 
ATOM 912  C CB  . LEU A 1 131 ? -50.604 22.933  -46.124 1.00 56.89  ? 139 LEU A CB  1 
ATOM 913  C CG  . LEU A 1 131 ? -49.813 21.830  -45.421 1.00 61.75  ? 139 LEU A CG  1 
ATOM 914  C CD1 . LEU A 1 131 ? -49.410 22.283  -44.035 1.00 67.16  ? 139 LEU A CD1 1 
ATOM 915  C CD2 . LEU A 1 131 ? -50.660 20.576  -45.351 1.00 64.17  ? 139 LEU A CD2 1 
ATOM 916  N N   . TRP A 1 132 ? -51.641 24.891  -48.548 1.00 68.89  ? 140 TRP A N   1 
ATOM 917  C CA  . TRP A 1 132 ? -52.711 25.689  -49.189 1.00 68.42  ? 140 TRP A CA  1 
ATOM 918  C C   . TRP A 1 132 ? -52.888 25.194  -50.612 1.00 73.64  ? 140 TRP A C   1 
ATOM 919  O O   . TRP A 1 132 ? -54.026 25.169  -51.103 1.00 77.34  ? 140 TRP A O   1 
ATOM 920  C CB  . TRP A 1 132 ? -52.351 27.175  -49.170 1.00 68.42  ? 140 TRP A CB  1 
ATOM 921  C CG  . TRP A 1 132 ? -53.429 28.067  -49.719 1.00 77.63  ? 140 TRP A CG  1 
ATOM 922  C CD1 . TRP A 1 132 ? -54.423 28.686  -49.021 1.00 80.55  ? 140 TRP A CD1 1 
ATOM 923  C CD2 . TRP A 1 132 ? -53.618 28.436  -51.101 1.00 79.96  ? 140 TRP A CD2 1 
ATOM 924  N NE1 . TRP A 1 132 ? -55.211 29.418  -49.867 1.00 85.39  ? 140 TRP A NE1 1 
ATOM 925  C CE2 . TRP A 1 132 ? -54.745 29.282  -51.148 1.00 87.23  ? 140 TRP A CE2 1 
ATOM 926  C CE3 . TRP A 1 132 ? -52.948 28.135  -52.291 1.00 81.91  ? 140 TRP A CE3 1 
ATOM 927  C CZ2 . TRP A 1 132 ? -55.213 29.827  -52.340 1.00 86.08  ? 140 TRP A CZ2 1 
ATOM 928  C CZ3 . TRP A 1 132 ? -53.413 28.674  -53.468 1.00 87.18  ? 140 TRP A CZ3 1 
ATOM 929  C CH2 . TRP A 1 132 ? -54.530 29.507  -53.490 1.00 85.69  ? 140 TRP A CH2 1 
ATOM 930  N N   . ASP A 1 133 ? -51.789 24.810  -51.252 1.00 72.14  ? 141 ASP A N   1 
ATOM 931  C CA  . ASP A 1 133 ? -51.879 24.250  -52.623 1.00 76.11  ? 141 ASP A CA  1 
ATOM 932  C C   . ASP A 1 133 ? -52.434 22.835  -52.526 1.00 78.18  ? 141 ASP A C   1 
ATOM 933  O O   . ASP A 1 133 ? -52.819 22.281  -53.565 1.00 83.62  ? 141 ASP A O   1 
ATOM 934  C CB  . ASP A 1 133 ? -50.537 24.247  -53.329 1.00 80.43  ? 141 ASP A CB  1 
ATOM 935  C CG  . ASP A 1 133 ? -50.597 24.086  -54.840 1.00 88.10  ? 141 ASP A CG  1 
ATOM 936  O OD1 . ASP A 1 133 ? -51.679 24.328  -55.413 1.00 89.14  ? 141 ASP A OD1 1 
ATOM 937  O OD2 . ASP A 1 133 ? -49.561 23.718  -55.428 1.00 86.44  ? 141 ASP A OD2 1 
ATOM 938  N N   . GLN A 1 134 ? -52.447 22.267  -51.324 1.00 76.27  ? 142 GLN A N   1 
ATOM 939  C CA  . GLN A 1 134 ? -53.044 20.921  -51.142 1.00 81.99  ? 142 GLN A CA  1 
ATOM 940  C C   . GLN A 1 134 ? -54.421 21.083  -50.479 1.00 89.29  ? 142 GLN A C   1 
ATOM 941  O O   . GLN A 1 134 ? -55.041 20.050  -50.157 1.00 89.98  ? 142 GLN A O   1 
ATOM 942  C CB  . GLN A 1 134 ? -52.075 20.036  -50.363 1.00 80.48  ? 142 GLN A CB  1 
ATOM 943  C CG  . GLN A 1 134 ? -50.722 19.870  -51.042 1.00 77.47  ? 142 GLN A CG  1 
ATOM 944  C CD  . GLN A 1 134 ? -50.710 18.787  -52.096 1.00 83.16  ? 142 GLN A CD  1 
ATOM 945  O OE1 . GLN A 1 134 ? -51.585 17.916  -52.140 1.00 87.25  ? 142 GLN A OE1 1 
ATOM 946  N NE2 . GLN A 1 134 ? -49.705 18.830  -52.958 1.00 84.96  ? 142 GLN A NE2 1 
ATOM 947  N N   . ALA A 1 135 ? -54.848 22.319  -50.210 1.00 89.44  ? 143 ALA A N   1 
ATOM 948  C CA  . ALA A 1 135 ? -56.223 22.552  -49.709 1.00 89.15  ? 143 ALA A CA  1 
ATOM 949  C C   . ALA A 1 135 ? -57.007 22.904  -50.956 1.00 85.95  ? 143 ALA A C   1 
ATOM 950  O O   . ALA A 1 135 ? -57.960 22.189  -51.318 1.00 84.68  ? 143 ALA A O   1 
ATOM 951  C CB  . ALA A 1 135 ? -56.243 23.686  -48.731 1.00 89.02  ? 143 ALA A CB  1 
ATOM 952  N N   . VAL A 1 136 ? -56.585 23.985  -51.607 1.00 87.28  ? 144 VAL A N   1 
ATOM 953  C CA  . VAL A 1 136 ? -57.176 24.288  -52.933 1.00 91.10  ? 144 VAL A CA  1 
ATOM 954  C C   . VAL A 1 136 ? -56.532 23.255  -53.863 1.00 90.35  ? 144 VAL A C   1 
ATOM 955  O O   . VAL A 1 136 ? -55.608 22.556  -53.398 1.00 94.95  ? 144 VAL A O   1 
ATOM 956  C CB  . VAL A 1 136 ? -56.838 25.731  -53.328 1.00 91.79  ? 144 VAL A CB  1 
ATOM 957  C CG1 . VAL A 1 136 ? -56.950 26.669  -52.135 1.00 84.45  ? 144 VAL A CG1 1 
ATOM 958  C CG2 . VAL A 1 136 ? -55.455 25.834  -53.959 1.00 88.24  ? 144 VAL A CG2 1 
ATOM 959  N N   . SER A 1 137 ? -57.001 23.168  -55.113 1.00 92.37  ? 145 SER A N   1 
ATOM 960  C CA  . SER A 1 137 ? -56.482 22.158  -56.076 1.00 99.95  ? 145 SER A CA  1 
ATOM 961  C C   . SER A 1 137 ? -56.628 20.756  -55.468 1.00 101.56 ? 145 SER A C   1 
ATOM 962  O O   . SER A 1 137 ? -55.692 19.939  -55.622 1.00 104.29 ? 145 SER A O   1 
ATOM 963  C CB  . SER A 1 137 ? -55.061 22.459  -56.503 1.00 93.18  ? 145 SER A CB  1 
ATOM 964  O OG  . SER A 1 137 ? -54.115 21.877  -55.618 1.00 88.89  ? 145 SER A OG  1 
ATOM 965  N N   . ASP A 1 138 ? -57.764 20.492  -54.813 1.00 98.74  ? 146 ASP A N   1 
ATOM 966  C CA  . ASP A 1 138 ? -58.027 19.156  -54.205 1.00 101.25 ? 146 ASP A CA  1 
ATOM 967  C C   . ASP A 1 138 ? -56.778 18.665  -53.468 1.00 101.26 ? 146 ASP A C   1 
ATOM 968  O O   . ASP A 1 138 ? -56.280 19.407  -52.598 1.00 105.87 ? 146 ASP A O   1 
ATOM 969  C CB  . ASP A 1 138 ? -58.511 18.151  -55.239 1.00 109.34 ? 146 ASP A CB  1 
ATOM 970  C CG  . ASP A 1 138 ? -59.919 18.381  -55.767 1.00 107.86 ? 146 ASP A CG  1 
ATOM 971  O OD1 . ASP A 1 138 ? -60.660 19.161  -55.135 1.00 103.50 ? 146 ASP A OD1 1 
ATOM 972  O OD2 . ASP A 1 138 ? -60.257 17.787  -56.812 1.00 108.31 ? 146 ASP A OD2 1 
ATOM 973  N N   . GLY A 1 139 ? -56.298 17.464  -53.803 1.00 92.75  ? 147 GLY A N   1 
ATOM 974  C CA  . GLY A 1 139 ? -55.138 16.887  -53.097 1.00 88.94  ? 147 GLY A CA  1 
ATOM 975  C C   . GLY A 1 139 ? -55.569 16.282  -51.776 1.00 99.99  ? 147 GLY A C   1 
ATOM 976  O O   . GLY A 1 139 ? -55.062 15.195  -51.433 1.00 89.54  ? 147 GLY A O   1 
ATOM 977  N N   . VAL A 1 140 ? -56.457 16.988  -51.080 1.00 109.25 ? 148 VAL A N   1 
ATOM 978  C CA  . VAL A 1 140 ? -57.000 16.469  -49.799 1.00 110.06 ? 148 VAL A CA  1 
ATOM 979  C C   . VAL A 1 140 ? -57.506 15.044  -50.043 1.00 104.95 ? 148 VAL A C   1 
ATOM 980  O O   . VAL A 1 140 ? -58.200 14.837  -51.067 1.00 98.66  ? 148 VAL A O   1 
ATOM 981  C CB  . VAL A 1 140 ? -58.125 17.392  -49.301 1.00 106.34 ? 148 VAL A CB  1 
ATOM 982  C CG1 . VAL A 1 140 ? -58.803 16.843  -48.053 1.00 104.82 ? 148 VAL A CG1 1 
ATOM 983  C CG2 . VAL A 1 140 ? -57.641 18.818  -49.066 1.00 100.28 ? 148 VAL A CG2 1 
ATOM 984  N N   . ASN A 1 141 ? -57.107 14.099  -49.188 1.00 100.86 ? 149 ASN A N   1 
ATOM 985  C CA  . ASN A 1 141 ? -57.616 12.703  -49.281 1.00 100.51 ? 149 ASN A CA  1 
ATOM 986  C C   . ASN A 1 141 ? -57.065 12.001  -50.525 1.00 96.34  ? 149 ASN A C   1 
ATOM 987  O O   . ASN A 1 141 ? -57.166 10.764  -50.577 1.00 92.12  ? 149 ASN A O   1 
ATOM 988  C CB  . ASN A 1 141 ? -59.139 12.652  -49.223 1.00 104.20 ? 149 ASN A CB  1 
ATOM 989  C CG  . ASN A 1 141 ? -59.638 11.245  -49.025 1.00 105.56 ? 149 ASN A CG  1 
ATOM 990  O OD1 . ASN A 1 141 ? -58.967 10.426  -48.389 1.00 102.75 ? 149 ASN A OD1 1 
ATOM 991  N ND2 . ASN A 1 141 ? -60.810 10.949  -49.564 1.00 105.50 ? 149 ASN A ND2 1 
ATOM 992  N N   . HIS A 1 142 ? -56.518 12.736  -51.493 1.00 98.94  ? 150 HIS A N   1 
ATOM 993  C CA  . HIS A 1 142 ? -55.881 12.032  -52.635 1.00 97.91  ? 150 HIS A CA  1 
ATOM 994  C C   . HIS A 1 142 ? -54.570 11.465  -52.101 1.00 96.30  ? 150 HIS A C   1 
ATOM 995  O O   . HIS A 1 142 ? -53.997 10.546  -52.709 1.00 97.32  ? 150 HIS A O   1 
ATOM 996  C CB  . HIS A 1 142 ? -55.683 12.961  -53.832 1.00 96.57  ? 150 HIS A CB  1 
ATOM 997  C CG  . HIS A 1 142 ? -56.945 13.331  -54.530 1.00 102.13 ? 150 HIS A CG  1 
ATOM 998  N ND1 . HIS A 1 142 ? -57.341 12.740  -55.710 1.00 105.24 ? 150 HIS A ND1 1 
ATOM 999  C CD2 . HIS A 1 142 ? -57.891 14.228  -54.228 1.00 100.37 ? 150 HIS A CD2 1 
ATOM 1000 C CE1 . HIS A 1 142 ? -58.492 13.269  -56.098 1.00 104.16 ? 150 HIS A CE1 1 
ATOM 1001 N NE2 . HIS A 1 142 ? -58.844 14.175  -55.212 1.00 101.20 ? 150 HIS A NE2 1 
ATOM 1002 N N   . TRP A 1 143 ? -54.107 12.020  -50.983 1.00 91.56  ? 151 TRP A N   1 
ATOM 1003 C CA  . TRP A 1 143 ? -52.881 11.490  -50.351 1.00 88.41  ? 151 TRP A CA  1 
ATOM 1004 C C   . TRP A 1 143 ? -53.180 10.096  -49.836 1.00 91.11  ? 151 TRP A C   1 
ATOM 1005 O O   . TRP A 1 143 ? -52.657 9.117   -50.397 1.00 89.58  ? 151 TRP A O   1 
ATOM 1006 C CB  . TRP A 1 143 ? -52.460 12.391  -49.188 1.00 88.59  ? 151 TRP A CB  1 
ATOM 1007 C CG  . TRP A 1 143 ? -52.542 13.865  -49.469 1.00 84.56  ? 151 TRP A CG  1 
ATOM 1008 C CD1 . TRP A 1 143 ? -51.935 14.552  -50.478 1.00 85.97  ? 151 TRP A CD1 1 
ATOM 1009 C CD2 . TRP A 1 143 ? -53.263 14.845  -48.695 1.00 80.75  ? 151 TRP A CD2 1 
ATOM 1010 N NE1 . TRP A 1 143 ? -52.236 15.884  -50.394 1.00 86.00  ? 151 TRP A NE1 1 
ATOM 1011 C CE2 . TRP A 1 143 ? -53.044 16.095  -49.309 1.00 78.65  ? 151 TRP A CE2 1 
ATOM 1012 C CE3 . TRP A 1 143 ? -54.066 14.785  -47.553 1.00 85.13  ? 151 TRP A CE3 1 
ATOM 1013 C CZ2 . TRP A 1 143 ? -53.603 17.270  -48.818 1.00 81.00  ? 151 TRP A CZ2 1 
ATOM 1014 C CZ3 . TRP A 1 143 ? -54.616 15.950  -47.068 1.00 87.39  ? 151 TRP A CZ3 1 
ATOM 1015 C CH2 . TRP A 1 143 ? -54.382 17.174  -47.690 1.00 84.71  ? 151 TRP A CH2 1 
ATOM 1016 N N   . PHE A 1 144 ? -54.002 10.020  -48.791 1.00 96.37  ? 152 PHE A N   1 
ATOM 1017 C CA  . PHE A 1 144 ? -54.342 8.713   -48.180 1.00 97.69  ? 152 PHE A CA  1 
ATOM 1018 C C   . PHE A 1 144 ? -55.780 8.558   -48.634 1.00 100.83 ? 152 PHE A C   1 
ATOM 1019 O O   . PHE A 1 144 ? -56.633 9.310   -48.129 1.00 106.32 ? 152 PHE A O   1 
ATOM 1020 C CB  . PHE A 1 144 ? -54.223 8.755   -46.658 1.00 88.59  ? 152 PHE A CB  1 
ATOM 1021 C CG  . PHE A 1 144 ? -52.870 9.129   -46.074 1.00 80.74  ? 152 PHE A CG  1 
ATOM 1022 C CD1 . PHE A 1 144 ? -51.940 8.148   -45.757 1.00 83.04  ? 152 PHE A CD1 1 
ATOM 1023 C CD2 . PHE A 1 144 ? -52.546 10.453  -45.811 1.00 75.36  ? 152 PHE A CD2 1 
ATOM 1024 C CE1 . PHE A 1 144 ? -50.715 8.486   -45.212 1.00 79.55  ? 152 PHE A CE1 1 
ATOM 1025 C CE2 . PHE A 1 144 ? -51.319 10.783  -45.263 1.00 78.20  ? 152 PHE A CE2 1 
ATOM 1026 C CZ  . PHE A 1 144 ? -50.409 9.800   -44.964 1.00 74.35  ? 152 PHE A CZ  1 
ATOM 1027 N N   . GLU A 1 145 ? -56.059 7.620   -49.538 1.00 102.45 ? 153 GLU A N   1 
ATOM 1028 C CA  . GLU A 1 145 ? -57.425 7.512   -50.123 1.00 109.09 ? 153 GLU A CA  1 
ATOM 1029 C C   . GLU A 1 145 ? -58.495 7.196   -49.059 1.00 106.13 ? 153 GLU A C   1 
ATOM 1030 O O   . GLU A 1 145 ? -59.682 7.467   -49.336 1.00 101.32 ? 153 GLU A O   1 
ATOM 1031 C CB  . GLU A 1 145 ? -57.427 6.476   -51.246 1.00 119.48 ? 153 GLU A CB  1 
ATOM 1032 C CG  . GLU A 1 145 ? -56.079 6.350   -51.951 1.00 134.55 ? 153 GLU A CG  1 
ATOM 1033 C CD  . GLU A 1 145 ? -55.647 7.535   -52.796 1.00 150.57 ? 153 GLU A CD  1 
ATOM 1034 O OE1 . GLU A 1 145 ? -56.516 8.323   -53.225 1.00 148.95 ? 153 GLU A OE1 1 
ATOM 1035 O OE2 . GLU A 1 145 ? -54.427 7.663   -53.029 1.00 152.51 ? 153 GLU A OE2 1 
ATOM 1036 N N   . ASP A 1 146 ? -58.114 6.649   -47.902 1.00 107.83 ? 154 ASP A N   1 
ATOM 1037 C CA  . ASP A 1 146 ? -59.108 6.420   -46.816 1.00 103.76 ? 154 ASP A CA  1 
ATOM 1038 C C   . ASP A 1 146 ? -60.012 7.653   -46.836 1.00 106.06 ? 154 ASP A C   1 
ATOM 1039 O O   . ASP A 1 146 ? -59.479 8.776   -46.776 1.00 104.91 ? 154 ASP A O   1 
ATOM 1040 C CB  . ASP A 1 146 ? -58.445 6.114   -45.484 1.00 94.96  ? 154 ASP A CB  1 
ATOM 1041 C CG  . ASP A 1 146 ? -57.774 4.752   -45.384 1.00 93.25  ? 154 ASP A CG  1 
ATOM 1042 O OD1 . ASP A 1 146 ? -58.049 3.896   -46.251 1.00 87.13  ? 154 ASP A OD1 1 
ATOM 1043 O OD2 . ASP A 1 146 ? -56.970 4.560   -44.448 1.00 98.63  ? 154 ASP A OD2 1 
ATOM 1044 N N   . GLY A 1 147 ? -61.327 7.451   -46.928 1.00 104.91 ? 155 GLY A N   1 
ATOM 1045 C CA  . GLY A 1 147 ? -62.273 8.578   -46.874 1.00 98.13  ? 155 GLY A CA  1 
ATOM 1046 C C   . GLY A 1 147 ? -61.982 9.357   -45.617 1.00 92.12  ? 155 GLY A C   1 
ATOM 1047 O O   . GLY A 1 147 ? -62.150 8.791   -44.520 1.00 84.05  ? 155 GLY A O   1 
ATOM 1048 N N   . THR A 1 148 ? -61.549 10.605  -45.772 1.00 97.57  ? 156 THR A N   1 
ATOM 1049 C CA  . THR A 1 148 ? -61.192 11.442  -44.612 1.00 100.02 ? 156 THR A CA  1 
ATOM 1050 C C   . THR A 1 148 ? -61.429 12.880  -44.980 1.00 99.09  ? 156 THR A C   1 
ATOM 1051 O O   . THR A 1 148 ? -60.921 13.307  -46.038 1.00 101.88 ? 156 THR A O   1 
ATOM 1052 C CB  . THR A 1 148 ? -59.725 11.211  -44.256 1.00 98.84  ? 156 THR A CB  1 
ATOM 1053 O OG1 . THR A 1 148 ? -59.700 10.032  -43.458 1.00 98.73  ? 156 THR A OG1 1 
ATOM 1054 C CG2 . THR A 1 148 ? -59.124 12.370  -43.482 1.00 90.54  ? 156 THR A CG2 1 
ATOM 1055 N N   . ASP A 1 149 ? -62.180 13.612  -44.162 1.00 93.59  ? 157 ASP A N   1 
ATOM 1056 C CA  . ASP A 1 149 ? -62.324 15.065  -44.439 1.00 99.02  ? 157 ASP A CA  1 
ATOM 1057 C C   . ASP A 1 149 ? -61.197 15.792  -43.699 1.00 100.60 ? 157 ASP A C   1 
ATOM 1058 O O   . ASP A 1 149 ? -60.886 15.383  -42.563 1.00 101.44 ? 157 ASP A O   1 
ATOM 1059 C CB  . ASP A 1 149 ? -63.723 15.553  -44.105 1.00 98.36  ? 157 ASP A CB  1 
ATOM 1060 C CG  . ASP A 1 149 ? -64.811 15.073  -45.054 1.00 101.18 ? 157 ASP A CG  1 
ATOM 1061 O OD1 . ASP A 1 149 ? -64.463 14.585  -46.148 1.00 91.74  ? 157 ASP A OD1 1 
ATOM 1062 O OD2 . ASP A 1 149 ? -66.000 15.185  -44.685 1.00 111.54 ? 157 ASP A OD2 1 
ATOM 1063 N N   . VAL A 1 150 ? -60.589 16.804  -44.329 1.00 96.11  ? 158 VAL A N   1 
ATOM 1064 C CA  . VAL A 1 150 ? -59.484 17.577  -43.682 1.00 88.03  ? 158 VAL A CA  1 
ATOM 1065 C C   . VAL A 1 150 ? -59.963 19.011  -43.418 1.00 88.95  ? 158 VAL A C   1 
ATOM 1066 O O   . VAL A 1 150 ? -60.215 19.742  -44.393 1.00 93.90  ? 158 VAL A O   1 
ATOM 1067 C CB  . VAL A 1 150 ? -58.193 17.578  -44.515 1.00 82.50  ? 158 VAL A CB  1 
ATOM 1068 C CG1 . VAL A 1 150 ? -57.058 18.259  -43.764 1.00 78.87  ? 158 VAL A CG1 1 
ATOM 1069 C CG2 . VAL A 1 150 ? -57.795 16.169  -44.934 1.00 85.24  ? 158 VAL A CG2 1 
ATOM 1070 N N   . ASP A 1 151 ? -60.077 19.387  -42.144 1.00 85.87  ? 159 ASP A N   1 
ATOM 1071 C CA  . ASP A 1 151 ? -60.540 20.751  -41.783 1.00 86.83  ? 159 ASP A CA  1 
ATOM 1072 C C   . ASP A 1 151 ? -59.347 21.697  -41.811 1.00 83.69  ? 159 ASP A C   1 
ATOM 1073 O O   . ASP A 1 151 ? -58.738 21.920  -40.748 1.00 78.00  ? 159 ASP A O   1 
ATOM 1074 C CB  . ASP A 1 151 ? -61.214 20.784  -40.426 1.00 92.18  ? 159 ASP A CB  1 
ATOM 1075 C CG  . ASP A 1 151 ? -62.387 21.748  -40.322 1.00 95.40  ? 159 ASP A CG  1 
ATOM 1076 O OD1 . ASP A 1 151 ? -62.379 22.760  -41.055 1.00 91.27  ? 159 ASP A OD1 1 
ATOM 1077 O OD2 . ASP A 1 151 ? -63.294 21.479  -39.510 1.00 103.04 ? 159 ASP A OD2 1 
ATOM 1078 N N   . PHE A 1 152 ? -59.041 22.226  -42.991 1.00 86.74  ? 160 PHE A N   1 
ATOM 1079 C CA  . PHE A 1 152 ? -57.902 23.166  -43.132 1.00 81.03  ? 160 PHE A CA  1 
ATOM 1080 C C   . PHE A 1 152 ? -58.196 24.434  -42.327 1.00 84.92  ? 160 PHE A C   1 
ATOM 1081 O O   . PHE A 1 152 ? -57.257 25.214  -42.087 1.00 76.67  ? 160 PHE A O   1 
ATOM 1082 C CB  . PHE A 1 152 ? -57.709 23.326  -44.640 1.00 73.05  ? 160 PHE A CB  1 
ATOM 1083 C CG  . PHE A 1 152 ? -56.878 22.213  -45.265 1.00 78.84  ? 160 PHE A CG  1 
ATOM 1084 C CD1 . PHE A 1 152 ? -55.571 21.983  -44.854 1.00 79.82  ? 160 PHE A CD1 1 
ATOM 1085 C CD2 . PHE A 1 152 ? -57.407 21.395  -46.255 1.00 85.96  ? 160 PHE A CD2 1 
ATOM 1086 C CE1 . PHE A 1 152 ? -54.813 20.976  -45.427 1.00 75.89  ? 160 PHE A CE1 1 
ATOM 1087 C CE2 . PHE A 1 152 ? -56.644 20.386  -46.822 1.00 86.87  ? 160 PHE A CE2 1 
ATOM 1088 C CZ  . PHE A 1 152 ? -55.351 20.180  -46.408 1.00 78.78  ? 160 PHE A CZ  1 
ATOM 1089 N N   . ASP A 1 153 ? -59.452 24.646  -41.909 1.00 91.55  ? 161 ASP A N   1 
ATOM 1090 C CA  . ASP A 1 153 ? -59.694 25.798  -41.050 1.00 80.73  ? 161 ASP A CA  1 
ATOM 1091 C C   . ASP A 1 153 ? -59.065 25.642  -39.669 1.00 79.46  ? 161 ASP A C   1 
ATOM 1092 O O   . ASP A 1 153 ? -58.785 26.651  -39.012 1.00 82.78  ? 161 ASP A O   1 
ATOM 1093 C CB  . ASP A 1 153 ? -61.200 26.034  -40.919 1.00 83.73  ? 161 ASP A CB  1 
ATOM 1094 C CG  . ASP A 1 153 ? -61.533 27.402  -40.366 1.00 85.55  ? 161 ASP A CG  1 
ATOM 1095 O OD1 . ASP A 1 153 ? -60.689 28.314  -40.480 1.00 79.45  ? 161 ASP A OD1 1 
ATOM 1096 O OD2 . ASP A 1 153 ? -62.643 27.566  -39.817 1.00 92.23  ? 161 ASP A OD2 1 
ATOM 1097 N N   . ARG A 1 154 ? -58.846 24.409  -39.209 1.00 76.06  ? 162 ARG A N   1 
ATOM 1098 C CA  . ARG A 1 154 ? -58.241 24.148  -37.902 1.00 73.11  ? 162 ARG A CA  1 
ATOM 1099 C C   . ARG A 1 154 ? -56.814 23.615  -38.059 1.00 67.27  ? 162 ARG A C   1 
ATOM 1100 O O   . ARG A 1 154 ? -56.587 22.405  -38.065 1.00 64.44  ? 162 ARG A O   1 
ATOM 1101 C CB  . ARG A 1 154 ? -59.134 23.131  -37.109 1.00 74.96  ? 162 ARG A CB  1 
ATOM 1102 C CG  . ARG A 1 154 ? -60.528 23.621  -36.675 1.00 82.73  ? 162 ARG A CG  1 
ATOM 1103 C CD  . ARG A 1 154 ? -61.336 22.536  -35.951 1.00 83.86  ? 162 ARG A CD  1 
ATOM 1104 N NE  . ARG A 1 154 ? -62.655 22.977  -35.506 1.00 86.14  ? 162 ARG A NE  1 
ATOM 1105 C CZ  . ARG A 1 154 ? -63.744 23.014  -36.263 1.00 83.79  ? 162 ARG A CZ  1 
ATOM 1106 N NH1 . ARG A 1 154 ? -63.723 22.624  -37.527 1.00 76.49  ? 162 ARG A NH1 1 
ATOM 1107 N NH2 . ARG A 1 154 ? -64.887 23.441  -35.734 1.00 86.24  ? 162 ARG A NH2 1 
ATOM 1108 N N   . VAL A 1 155 ? -55.841 24.523  -38.167 1.00 63.93  ? 163 VAL A N   1 
ATOM 1109 C CA  . VAL A 1 155 ? -54.427 24.156  -38.250 1.00 57.79  ? 163 VAL A CA  1 
ATOM 1110 C C   . VAL A 1 155 ? -53.746 24.544  -36.943 1.00 58.12  ? 163 VAL A C   1 
ATOM 1111 O O   . VAL A 1 155 ? -54.088 25.562  -36.331 1.00 69.82  ? 163 VAL A O   1 
ATOM 1112 C CB  . VAL A 1 155 ? -53.710 24.795  -39.456 1.00 62.30  ? 163 VAL A CB  1 
ATOM 1113 C CG1 . VAL A 1 155 ? -52.329 24.184  -39.631 1.00 67.15  ? 163 VAL A CG1 1 
ATOM 1114 C CG2 . VAL A 1 155 ? -54.502 24.557  -40.710 1.00 59.99  ? 163 VAL A CG2 1 
ATOM 1115 N N   . PHE A 1 156 ? -52.779 23.731  -36.518 1.00 53.72  ? 164 PHE A N   1 
ATOM 1116 C CA  . PHE A 1 156 ? -52.043 23.953  -35.276 1.00 58.88  ? 164 PHE A CA  1 
ATOM 1117 C C   . PHE A 1 156 ? -50.570 23.637  -35.484 1.00 55.80  ? 164 PHE A C   1 
ATOM 1118 O O   . PHE A 1 156 ? -50.224 22.518  -35.874 1.00 56.12  ? 164 PHE A O   1 
ATOM 1119 C CB  . PHE A 1 156 ? -52.622 23.114  -34.133 1.00 68.58  ? 164 PHE A CB  1 
ATOM 1120 C CG  . PHE A 1 156 ? -54.021 23.507  -33.742 1.00 74.99  ? 164 PHE A CG  1 
ATOM 1121 C CD1 . PHE A 1 156 ? -54.233 24.611  -32.932 1.00 77.19  ? 164 PHE A CD1 1 
ATOM 1122 C CD2 . PHE A 1 156 ? -55.120 22.801  -34.202 1.00 78.13  ? 164 PHE A CD2 1 
ATOM 1123 C CE1 . PHE A 1 156 ? -55.511 24.984  -32.562 1.00 76.31  ? 164 PHE A CE1 1 
ATOM 1124 C CE2 . PHE A 1 156 ? -56.403 23.175  -33.842 1.00 78.20  ? 164 PHE A CE2 1 
ATOM 1125 C CZ  . PHE A 1 156 ? -56.597 24.270  -33.023 1.00 79.79  ? 164 PHE A CZ  1 
ATOM 1126 N N   . VAL A 1 157 ? -49.709 24.615  -35.227 1.00 50.91  ? 165 VAL A N   1 
ATOM 1127 C CA  . VAL A 1 157 ? -48.265 24.435  -35.321 1.00 46.78  ? 165 VAL A CA  1 
ATOM 1128 C C   . VAL A 1 157 ? -47.745 23.908  -33.990 1.00 52.77  ? 165 VAL A C   1 
ATOM 1129 O O   . VAL A 1 157 ? -48.208 24.320  -32.922 1.00 62.44  ? 165 VAL A O   1 
ATOM 1130 C CB  . VAL A 1 157 ? -47.581 25.760  -35.715 1.00 52.68  ? 165 VAL A CB  1 
ATOM 1131 C CG1 . VAL A 1 157 ? -46.065 25.641  -35.637 1.00 55.18  ? 165 VAL A CG1 1 
ATOM 1132 C CG2 . VAL A 1 157 ? -48.018 26.184  -37.109 1.00 49.24  ? 165 VAL A CG2 1 
ATOM 1133 N N   . VAL A 1 158 ? -46.776 22.994  -34.051 1.00 46.37  ? 166 VAL A N   1 
ATOM 1134 C CA  . VAL A 1 158 ? -46.148 22.421  -32.862 1.00 47.71  ? 166 VAL A CA  1 
ATOM 1135 C C   . VAL A 1 158 ? -44.641 22.407  -33.085 1.00 49.80  ? 166 VAL A C   1 
ATOM 1136 O O   . VAL A 1 158 ? -44.163 21.831  -34.069 1.00 60.65  ? 166 VAL A O   1 
ATOM 1137 C CB  . VAL A 1 158 ? -46.652 20.999  -32.552 1.00 52.79  ? 166 VAL A CB  1 
ATOM 1138 C CG1 . VAL A 1 158 ? -45.867 20.400  -31.395 1.00 58.61  ? 166 VAL A CG1 1 
ATOM 1139 C CG2 . VAL A 1 158 ? -48.138 21.017  -32.224 1.00 52.84  ? 166 VAL A CG2 1 
ATOM 1140 N N   . GLY A 1 159 ? -43.895 23.037  -32.180 1.00 51.30  ? 167 GLY A N   1 
ATOM 1141 C CA  . GLY A 1 159 ? -42.462 23.186  -32.356 1.00 55.70  ? 167 GLY A CA  1 
ATOM 1142 C C   . GLY A 1 159 ? -41.605 22.690  -31.207 1.00 65.53  ? 167 GLY A C   1 
ATOM 1143 O O   . GLY A 1 159 ? -41.734 23.163  -30.074 1.00 67.98  ? 167 GLY A O   1 
ATOM 1144 N N   . ASP A 1 160 ? -40.722 21.737  -31.490 1.00 66.23  ? 168 ASP A N   1 
ATOM 1145 C CA  . ASP A 1 160 ? -39.791 21.202  -30.507 1.00 59.07  ? 168 ASP A CA  1 
ATOM 1146 C C   . ASP A 1 160 ? -38.455 21.920  -30.666 1.00 59.99  ? 168 ASP A C   1 
ATOM 1147 O O   . ASP A 1 160 ? -37.963 22.090  -31.785 1.00 64.07  ? 168 ASP A O   1 
ATOM 1148 C CB  . ASP A 1 160 ? -39.623 19.688  -30.700 1.00 64.91  ? 168 ASP A CB  1 
ATOM 1149 C CG  . ASP A 1 160 ? -38.527 19.072  -29.822 1.00 72.21  ? 168 ASP A CG  1 
ATOM 1150 O OD1 . ASP A 1 160 ? -37.774 19.789  -29.133 1.00 70.63  ? 168 ASP A OD1 1 
ATOM 1151 O OD2 . ASP A 1 160 ? -38.415 17.828  -29.835 1.00 73.46  ? 168 ASP A OD2 1 
ATOM 1152 N N   . SER A 1 161 ? -37.866 22.321  -29.537 1.00 58.77  ? 169 SER A N   1 
ATOM 1153 C CA  . SER A 1 161 ? -36.559 22.975  -29.520 1.00 65.42  ? 169 SER A CA  1 
ATOM 1154 C C   . SER A 1 161 ? -36.493 24.130  -30.514 1.00 67.49  ? 169 SER A C   1 
ATOM 1155 O O   . SER A 1 161 ? -37.228 25.114  -30.380 1.00 61.50  ? 169 SER A O   1 
ATOM 1156 C CB  . SER A 1 161 ? -35.446 21.964  -29.808 1.00 63.36  ? 169 SER A CB  1 
ATOM 1157 O OG  . SER A 1 161 ? -34.177 22.480  -29.437 1.00 51.17  ? 169 SER A OG  1 
ATOM 1158 N N   . SER A 1 162 ? -35.589 24.025  -31.493 1.00 62.95  ? 170 SER A N   1 
ATOM 1159 C CA  . SER A 1 162 ? -35.551 24.983  -32.594 1.00 61.66  ? 170 SER A CA  1 
ATOM 1160 C C   . SER A 1 162 ? -36.916 25.134  -33.254 1.00 59.65  ? 170 SER A C   1 
ATOM 1161 O O   . SER A 1 162 ? -37.307 26.241  -33.639 1.00 63.68  ? 170 SER A O   1 
ATOM 1162 C CB  . SER A 1 162 ? -34.503 24.552  -33.620 1.00 67.37  ? 170 SER A CB  1 
ATOM 1163 O OG  . SER A 1 162 ? -34.715 23.214  -34.038 1.00 71.80  ? 170 SER A OG  1 
ATOM 1164 N N   . GLY A 1 163 ? -37.638 24.021  -33.421 1.00 59.61  ? 171 GLY A N   1 
ATOM 1165 C CA  . GLY A 1 163 ? -38.984 24.084  -33.974 1.00 59.58  ? 171 GLY A CA  1 
ATOM 1166 C C   . GLY A 1 163 ? -39.868 25.102  -33.280 1.00 65.10  ? 171 GLY A C   1 
ATOM 1167 O O   . GLY A 1 163 ? -40.710 25.742  -33.915 1.00 64.02  ? 171 GLY A O   1 
ATOM 1168 N N   . GLY A 1 164 ? -39.711 25.241  -31.961 1.00 64.08  ? 172 GLY A N   1 
ATOM 1169 C CA  . GLY A 1 164 ? -40.463 26.256  -31.242 1.00 58.13  ? 172 GLY A CA  1 
ATOM 1170 C C   . GLY A 1 164 ? -40.173 27.654  -31.753 1.00 56.13  ? 172 GLY A C   1 
ATOM 1171 O O   . GLY A 1 164 ? -41.088 28.453  -31.967 1.00 55.85  ? 172 GLY A O   1 
ATOM 1172 N N   . ASN A 1 165 ? -38.888 27.974  -31.932 1.00 56.88  ? 173 ASN A N   1 
ATOM 1173 C CA  . ASN A 1 165 ? -38.505 29.247  -32.539 1.00 58.23  ? 173 ASN A CA  1 
ATOM 1174 C C   . ASN A 1 165 ? -39.211 29.444  -33.876 1.00 55.27  ? 173 ASN A C   1 
ATOM 1175 O O   . ASN A 1 165 ? -39.727 30.529  -34.170 1.00 61.09  ? 173 ASN A O   1 
ATOM 1176 C CB  . ASN A 1 165 ? -36.984 29.305  -32.711 1.00 61.43  ? 173 ASN A CB  1 
ATOM 1177 C CG  . ASN A 1 165 ? -36.485 30.693  -33.072 1.00 62.60  ? 173 ASN A CG  1 
ATOM 1178 O OD1 . ASN A 1 165 ? -36.994 31.336  -33.989 1.00 61.01  ? 173 ASN A OD1 1 
ATOM 1179 N ND2 . ASN A 1 165 ? -35.475 31.160  -32.347 1.00 66.82  ? 173 ASN A ND2 1 
ATOM 1180 N N   . ILE A 1 166 ? -39.211 28.402  -34.712 1.00 51.56  ? 174 ILE A N   1 
ATOM 1181 C CA  . ILE A 1 166 ? -39.940 28.434  -35.978 1.00 52.68  ? 174 ILE A CA  1 
ATOM 1182 C C   . ILE A 1 166 ? -41.397 28.813  -35.741 1.00 56.40  ? 174 ILE A C   1 
ATOM 1183 O O   . ILE A 1 166 ? -41.986 29.599  -36.492 1.00 55.22  ? 174 ILE A O   1 
ATOM 1184 C CB  . ILE A 1 166 ? -39.814 27.079  -36.697 1.00 47.27  ? 174 ILE A CB  1 
ATOM 1185 C CG1 . ILE A 1 166 ? -38.345 26.743  -36.950 1.00 52.34  ? 174 ILE A CG1 1 
ATOM 1186 C CG2 . ILE A 1 166 ? -40.597 27.084  -37.996 1.00 41.49  ? 174 ILE A CG2 1 
ATOM 1187 C CD1 . ILE A 1 166 ? -38.124 25.365  -37.526 1.00 54.00  ? 174 ILE A CD1 1 
ATOM 1188 N N   . ALA A 1 167 ? -42.014 28.201  -34.726 1.00 63.87  ? 175 ALA A N   1 
ATOM 1189 C CA  . ALA A 1 167 ? -43.407 28.486  -34.386 1.00 59.90  ? 175 ALA A CA  1 
ATOM 1190 C C   . ALA A 1 167 ? -43.628 29.952  -34.017 1.00 64.19  ? 175 ALA A C   1 
ATOM 1191 O O   . ALA A 1 167 ? -44.681 30.519  -34.335 1.00 63.30  ? 175 ALA A O   1 
ATOM 1192 C CB  . ALA A 1 167 ? -43.869 27.570  -33.253 1.00 64.46  ? 175 ALA A CB  1 
ATOM 1193 N N   . HIS A 1 168 ? -42.694 30.558  -33.275 1.00 68.26  ? 176 HIS A N   1 
ATOM 1194 C CA  . HIS A 1 168 ? -42.814 31.970  -32.906 1.00 66.79  ? 176 HIS A CA  1 
ATOM 1195 C C   . HIS A 1 168 ? -42.916 32.853  -34.144 1.00 64.55  ? 176 HIS A C   1 
ATOM 1196 O O   . HIS A 1 168 ? -43.938 33.517  -34.346 1.00 66.83  ? 176 HIS A O   1 
ATOM 1197 C CB  . HIS A 1 168 ? -41.644 32.407  -32.026 1.00 69.08  ? 176 HIS A CB  1 
ATOM 1198 C CG  . HIS A 1 168 ? -41.544 33.891  -31.852 1.00 72.77  ? 176 HIS A CG  1 
ATOM 1199 N ND1 . HIS A 1 168 ? -40.685 34.671  -32.594 1.00 75.63  ? 176 HIS A ND1 1 
ATOM 1200 C CD2 . HIS A 1 168 ? -42.215 34.741  -31.036 1.00 71.73  ? 176 HIS A CD2 1 
ATOM 1201 C CE1 . HIS A 1 168 ? -40.813 35.933  -32.228 1.00 77.15  ? 176 HIS A CE1 1 
ATOM 1202 N NE2 . HIS A 1 168 ? -41.739 36.005  -31.289 1.00 75.08  ? 176 HIS A NE2 1 
ATOM 1203 N N   . GLN A 1 169 ? -41.870 32.892  -34.970 1.00 60.17  ? 177 GLN A N   1 
ATOM 1204 C CA  . GLN A 1 169 ? -42.039 33.397  -36.324 1.00 61.22  ? 177 GLN A CA  1 
ATOM 1205 C C   . GLN A 1 169 ? -43.010 32.497  -37.084 1.00 59.81  ? 177 GLN A C   1 
ATOM 1206 O O   . GLN A 1 169 ? -43.308 31.384  -36.659 1.00 59.79  ? 177 GLN A O   1 
ATOM 1207 C CB  . GLN A 1 169 ? -40.713 33.361  -37.083 1.00 56.91  ? 177 GLN A CB  1 
ATOM 1208 C CG  . GLN A 1 169 ? -39.759 34.495  -36.720 1.00 60.49  ? 177 GLN A CG  1 
ATOM 1209 C CD  . GLN A 1 169 ? -38.935 34.226  -35.476 1.00 64.11  ? 177 GLN A CD  1 
ATOM 1210 O OE1 . GLN A 1 169 ? -38.866 35.063  -34.578 1.00 74.43  ? 177 GLN A OE1 1 
ATOM 1211 N NE2 . GLN A 1 169 ? -38.309 33.060  -35.415 1.00 63.40  ? 177 GLN A NE2 1 
ATOM 1212 N N   . LEU A 1 170 ? -43.554 32.991  -38.197 1.00 61.42  ? 178 LEU A N   1 
ATOM 1213 C CA  . LEU A 1 170 ? -44.490 32.142  -38.931 1.00 66.04  ? 178 LEU A CA  1 
ATOM 1214 C C   . LEU A 1 170 ? -45.853 32.296  -38.247 1.00 66.83  ? 178 LEU A C   1 
ATOM 1215 O O   . LEU A 1 170 ? -46.859 31.796  -38.761 1.00 70.07  ? 178 LEU A O   1 
ATOM 1216 C CB  . LEU A 1 170 ? -44.084 30.661  -39.017 1.00 53.14  ? 178 LEU A CB  1 
ATOM 1217 C CG  . LEU A 1 170 ? -44.970 29.652  -39.745 1.00 48.37  ? 178 LEU A CG  1 
ATOM 1218 C CD1 . LEU A 1 170 ? -44.952 29.930  -41.236 1.00 61.57  ? 178 LEU A CD1 1 
ATOM 1219 C CD2 . LEU A 1 170 ? -44.530 28.228  -39.429 1.00 51.46  ? 178 LEU A CD2 1 
ATOM 1220 N N   . ALA A 1 171 ? -45.912 32.950  -37.079 1.00 64.01  ? 179 ALA A N   1 
ATOM 1221 C CA  . ALA A 1 171 ? -47.202 33.296  -36.489 1.00 67.85  ? 179 ALA A CA  1 
ATOM 1222 C C   . ALA A 1 171 ? -47.453 34.168  -37.709 1.00 80.52  ? 179 ALA A C   1 
ATOM 1223 O O   . ALA A 1 171 ? -46.767 35.172  -37.917 1.00 82.12  ? 179 ALA A O   1 
ATOM 1224 C CB  . ALA A 1 171 ? -47.030 33.972  -35.125 1.00 53.38  ? 179 ALA A CB  1 
ATOM 1225 N N   . VAL A 1 172 ? -48.489 33.790  -38.469 1.00 81.33  ? 180 VAL A N   1 
ATOM 1226 C CA  . VAL A 1 172 ? -48.845 34.212  -39.826 1.00 77.21  ? 180 VAL A CA  1 
ATOM 1227 C C   . VAL A 1 172 ? -48.752 35.733  -39.863 1.00 73.46  ? 180 VAL A C   1 
ATOM 1228 O O   . VAL A 1 172 ? -48.166 36.298  -40.792 1.00 78.19  ? 180 VAL A O   1 
ATOM 1229 C CB  . VAL A 1 172 ? -50.285 33.751  -40.118 1.00 78.00  ? 180 VAL A CB  1 
ATOM 1230 C CG1 . VAL A 1 172 ? -51.258 34.439  -39.158 1.00 60.84  ? 180 VAL A CG1 1 
ATOM 1231 C CG2 . VAL A 1 172 ? -50.660 34.040  -41.564 1.00 82.06  ? 180 VAL A CG2 1 
ATOM 1232 N N   . ARG A 1 173 ? -49.311 36.415  -38.863 1.00 73.89  ? 181 ARG A N   1 
ATOM 1233 C CA  . ARG A 1 173 ? -49.102 37.856  -38.785 1.00 75.74  ? 181 ARG A CA  1 
ATOM 1234 C C   . ARG A 1 173 ? -47.622 38.126  -38.543 1.00 80.75  ? 181 ARG A C   1 
ATOM 1235 O O   . ARG A 1 173 ? -46.984 38.892  -39.274 1.00 80.47  ? 181 ARG A O   1 
ATOM 1236 C CB  . ARG A 1 173 ? -49.993 38.466  -37.699 1.00 73.71  ? 181 ARG A CB  1 
ATOM 1237 C CG  . ARG A 1 173 ? -49.782 39.958  -37.379 1.00 77.77  ? 181 ARG A CG  1 
ATOM 1238 C CD  . ARG A 1 173 ? -49.321 40.827  -38.573 1.00 68.87  ? 181 ARG A CD  1 
ATOM 1239 N NE  . ARG A 1 173 ? -50.092 40.638  -39.800 1.00 72.47  ? 181 ARG A NE  1 
ATOM 1240 C CZ  . ARG A 1 173 ? -49.679 41.013  -41.004 1.00 75.91  ? 181 ARG A CZ  1 
ATOM 1241 N NH1 . ARG A 1 173 ? -48.510 41.608  -41.180 1.00 72.73  ? 181 ARG A NH1 1 
ATOM 1242 N NH2 . ARG A 1 173 ? -50.452 40.774  -42.061 1.00 73.72  ? 181 ARG A NH2 1 
ATOM 1243 N N   . PHE A 1 174 ? -47.069 37.593  -37.453 1.00 81.99  ? 182 PHE A N   1 
ATOM 1244 C CA  . PHE A 1 174 ? -45.637 37.865  -37.149 1.00 78.08  ? 182 PHE A CA  1 
ATOM 1245 C C   . PHE A 1 174 ? -44.814 37.394  -38.354 1.00 74.66  ? 182 PHE A C   1 
ATOM 1246 O O   . PHE A 1 174 ? -43.622 37.754  -38.459 1.00 74.50  ? 182 PHE A O   1 
ATOM 1247 C CB  . PHE A 1 174 ? -45.220 37.165  -35.850 1.00 68.58  ? 182 PHE A CB  1 
ATOM 1248 C CG  . PHE A 1 174 ? -43.837 37.541  -35.334 1.00 86.93  ? 182 PHE A CG  1 
ATOM 1249 C CD1 . PHE A 1 174 ? -42.710 36.822  -35.712 1.00 92.64  ? 182 PHE A CD1 1 
ATOM 1250 C CD2 . PHE A 1 174 ? -43.667 38.615  -34.470 1.00 95.66  ? 182 PHE A CD2 1 
ATOM 1251 C CE1 . PHE A 1 174 ? -41.454 37.181  -35.254 1.00 93.96  ? 182 PHE A CE1 1 
ATOM 1252 C CE2 . PHE A 1 174 ? -42.410 38.965  -34.008 1.00 99.99  ? 182 PHE A CE2 1 
ATOM 1253 C CZ  . PHE A 1 174 ? -41.307 38.250  -34.403 1.00 103.63 ? 182 PHE A CZ  1 
ATOM 1254 N N   . GLY A 1 175 ? -45.441 36.649  -39.273 1.00 66.36  ? 183 GLY A N   1 
ATOM 1255 C CA  . GLY A 1 175 ? -44.712 36.063  -40.418 1.00 76.08  ? 183 GLY A CA  1 
ATOM 1256 C C   . GLY A 1 175 ? -44.508 37.028  -41.569 1.00 88.59  ? 183 GLY A C   1 
ATOM 1257 O O   . GLY A 1 175 ? -44.572 38.253  -41.336 1.00 93.35  ? 183 GLY A O   1 
ATOM 1258 N N   . SER A 1 176 ? -44.287 36.501  -42.778 1.00 89.39  ? 184 SER A N   1 
ATOM 1259 C CA  . SER A 1 176 ? -43.964 37.376  -43.936 1.00 93.67  ? 184 SER A CA  1 
ATOM 1260 C C   . SER A 1 176 ? -45.227 37.837  -44.676 1.00 98.61  ? 184 SER A C   1 
ATOM 1261 O O   . SER A 1 176 ? -45.433 37.386  -45.823 1.00 98.12  ? 184 SER A O   1 
ATOM 1262 C CB  . SER A 1 176 ? -43.004 36.694  -44.879 1.00 87.33  ? 184 SER A CB  1 
ATOM 1263 O OG  . SER A 1 176 ? -41.814 36.318  -44.200 1.00 88.07  ? 184 SER A OG  1 
ATOM 1264 N N   . GLY A 1 177 ? -46.039 38.691  -44.050 1.00 95.69  ? 185 GLY A N   1 
ATOM 1265 C CA  . GLY A 1 177 ? -47.194 39.279  -44.755 1.00 90.55  ? 185 GLY A CA  1 
ATOM 1266 C C   . GLY A 1 177 ? -48.496 38.663  -44.295 1.00 92.05  ? 185 GLY A C   1 
ATOM 1267 O O   . GLY A 1 177 ? -49.542 39.302  -44.533 1.00 92.34  ? 185 GLY A O   1 
ATOM 1268 N N   . SER A 1 178 ? -48.442 37.465  -43.702 1.00 90.65  ? 186 SER A N   1 
ATOM 1269 C CA  . SER A 1 178 ? -49.649 36.775  -43.165 1.00 92.26  ? 186 SER A CA  1 
ATOM 1270 C C   . SER A 1 178 ? -50.497 36.197  -44.289 1.00 96.51  ? 186 SER A C   1 
ATOM 1271 O O   . SER A 1 178 ? -51.559 35.585  -43.845 1.00 91.80  ? 186 SER A O   1 
ATOM 1272 C CB  . SER A 1 178 ? -50.499 37.657  -42.278 1.00 90.68  ? 186 SER A CB  1 
ATOM 1273 O OG  . SER A 1 178 ? -51.041 38.749  -43.008 1.00 91.16  ? 186 SER A OG  1 
ATOM 1274 N N   . ILE A 1 179 ? -50.058 36.388  -45.559 1.00 101.91 ? 187 ILE A N   1 
ATOM 1275 C CA  . ILE A 1 179 ? -50.765 35.911  -46.791 1.00 101.31 ? 187 ILE A CA  1 
ATOM 1276 C C   . ILE A 1 179 ? -51.990 35.197  -46.277 1.00 91.77  ? 187 ILE A C   1 
ATOM 1277 O O   . ILE A 1 179 ? -51.891 34.013  -45.958 1.00 80.19  ? 187 ILE A O   1 
ATOM 1278 C CB  . ILE A 1 179 ? -49.865 34.974  -47.611 1.00 102.03 ? 187 ILE A CB  1 
ATOM 1279 C CG1 . ILE A 1 179 ? -48.416 35.464  -47.628 1.00 92.25  ? 187 ILE A CG1 1 
ATOM 1280 C CG2 . ILE A 1 179 ? -50.417 34.789  -49.025 1.00 91.83  ? 187 ILE A CG2 1 
ATOM 1281 C CD1 . ILE A 1 179 ? -47.442 34.547  -46.913 1.00 84.76  ? 187 ILE A CD1 1 
ATOM 1282 N N   . GLU A 1 180 ? -53.130 35.870  -46.350 1.00 96.69  ? 188 GLU A N   1 
ATOM 1283 C CA  . GLU A 1 180 ? -54.165 35.206  -45.570 1.00 97.27  ? 188 GLU A CA  1 
ATOM 1284 C C   . GLU A 1 180 ? -54.483 33.995  -46.433 1.00 87.50  ? 188 GLU A C   1 
ATOM 1285 O O   . GLU A 1 180 ? -55.092 34.110  -47.502 1.00 81.85  ? 188 GLU A O   1 
ATOM 1286 C CB  . GLU A 1 180 ? -55.344 36.148  -45.323 1.00 101.46 ? 188 GLU A CB  1 
ATOM 1287 C CG  . GLU A 1 180 ? -55.006 37.325  -44.424 1.00 107.14 ? 188 GLU A CG  1 
ATOM 1288 C CD  . GLU A 1 180 ? -56.167 38.281  -44.250 1.00 125.65 ? 188 GLU A CD  1 
ATOM 1289 O OE1 . GLU A 1 180 ? -57.173 38.134  -44.976 1.00 135.78 ? 188 GLU A OE1 1 
ATOM 1290 O OE2 . GLU A 1 180 ? -56.073 39.180  -43.388 1.00 127.21 ? 188 GLU A OE2 1 
ATOM 1291 N N   . LEU A 1 181 ? -54.059 32.825  -45.949 1.00 82.83  ? 189 LEU A N   1 
ATOM 1292 C CA  . LEU A 1 181 ? -54.055 31.590  -46.723 1.00 79.46  ? 189 LEU A CA  1 
ATOM 1293 C C   . LEU A 1 181 ? -55.457 31.175  -46.291 1.00 81.15  ? 189 LEU A C   1 
ATOM 1294 O O   . LEU A 1 181 ? -55.598 30.375  -45.362 1.00 80.90  ? 189 LEU A O   1 
ATOM 1295 C CB  . LEU A 1 181 ? -53.021 30.571  -46.227 1.00 73.63  ? 189 LEU A CB  1 
ATOM 1296 C CG  . LEU A 1 181 ? -51.499 30.663  -46.428 1.00 71.27  ? 189 LEU A CG  1 
ATOM 1297 C CD1 . LEU A 1 181 ? -51.119 31.154  -47.827 1.00 79.93  ? 189 LEU A CD1 1 
ATOM 1298 C CD2 . LEU A 1 181 ? -50.772 31.415  -45.307 1.00 78.49  ? 189 LEU A CD2 1 
ATOM 1299 N N   . THR A 1 182 ? -56.490 31.709  -46.934 1.00 82.97  ? 190 THR A N   1 
ATOM 1300 C CA  . THR A 1 182 ? -57.838 31.210  -46.714 1.00 86.74  ? 190 THR A CA  1 
ATOM 1301 C C   . THR A 1 182 ? -57.907 30.344  -47.970 1.00 87.31  ? 190 THR A C   1 
ATOM 1302 O O   . THR A 1 182 ? -57.497 30.798  -49.048 1.00 85.62  ? 190 THR A O   1 
ATOM 1303 C CB  . THR A 1 182 ? -58.854 32.351  -46.798 1.00 86.15  ? 190 THR A CB  1 
ATOM 1304 O OG1 . THR A 1 182 ? -58.634 33.270  -45.719 1.00 85.18  ? 190 THR A OG1 1 
ATOM 1305 C CG2 . THR A 1 182 ? -60.274 31.814  -46.711 1.00 83.01  ? 190 THR A CG2 1 
ATOM 1306 N N   . PRO A 1 183 ? -58.400 29.098  -47.884 1.00 84.20  ? 191 PRO A N   1 
ATOM 1307 C CA  . PRO A 1 183 ? -59.043 28.394  -46.759 1.00 83.63  ? 191 PRO A CA  1 
ATOM 1308 C C   . PRO A 1 183 ? -58.189 27.947  -45.566 1.00 86.68  ? 191 PRO A C   1 
ATOM 1309 O O   . PRO A 1 183 ? -58.750 27.845  -44.475 1.00 95.77  ? 191 PRO A O   1 
ATOM 1310 C CB  . PRO A 1 183 ? -59.662 27.174  -47.450 1.00 88.99  ? 191 PRO A CB  1 
ATOM 1311 C CG  . PRO A 1 183 ? -58.716 26.855  -48.556 1.00 93.29  ? 191 PRO A CG  1 
ATOM 1312 C CD  . PRO A 1 183 ? -58.121 28.173  -49.000 1.00 88.68  ? 191 PRO A CD  1 
ATOM 1313 N N   . VAL A 1 184 ? -56.882 27.677  -45.653 1.00 84.59  ? 192 VAL A N   1 
ATOM 1314 C CA  . VAL A 1 184 ? -56.188 27.139  -44.486 1.00 85.61  ? 192 VAL A CA  1 
ATOM 1315 C C   . VAL A 1 184 ? -55.902 28.261  -43.498 1.00 77.77  ? 192 VAL A C   1 
ATOM 1316 O O   . VAL A 1 184 ? -55.508 29.370  -43.873 1.00 73.29  ? 192 VAL A O   1 
ATOM 1317 C CB  . VAL A 1 184 ? -54.888 26.416  -44.900 1.00 81.07  ? 192 VAL A CB  1 
ATOM 1318 C CG1 . VAL A 1 184 ? -55.187 25.249  -45.810 1.00 79.76  ? 192 VAL A CG1 1 
ATOM 1319 C CG2 . VAL A 1 184 ? -53.899 27.346  -45.555 1.00 80.20  ? 192 VAL A CG2 1 
ATOM 1320 N N   . ARG A 1 185 ? -56.128 27.970  -42.219 1.00 72.85  ? 193 ARG A N   1 
ATOM 1321 C CA  . ARG A 1 185 ? -56.127 28.980  -41.165 1.00 78.38  ? 193 ARG A CA  1 
ATOM 1322 C C   . ARG A 1 185 ? -55.489 28.382  -39.920 1.00 74.45  ? 193 ARG A C   1 
ATOM 1323 O O   . ARG A 1 185 ? -56.025 27.428  -39.348 1.00 73.75  ? 193 ARG A O   1 
ATOM 1324 C CB  . ARG A 1 185 ? -57.551 29.450  -40.866 1.00 86.72  ? 193 ARG A CB  1 
ATOM 1325 C CG  . ARG A 1 185 ? -57.656 30.510  -39.782 1.00 84.63  ? 193 ARG A CG  1 
ATOM 1326 C CD  . ARG A 1 185 ? -59.115 30.855  -39.546 1.00 79.85  ? 193 ARG A CD  1 
ATOM 1327 N NE  . ARG A 1 185 ? -59.300 31.798  -38.451 1.00 85.85  ? 193 ARG A NE  1 
ATOM 1328 C CZ  . ARG A 1 185 ? -60.475 32.096  -37.914 1.00 93.68  ? 193 ARG A CZ  1 
ATOM 1329 N NH1 . ARG A 1 185 ? -61.609 31.697  -38.468 1.00 94.48  ? 193 ARG A NH1 1 
ATOM 1330 N NH2 . ARG A 1 185 ? -60.517 32.871  -36.835 1.00 96.58  ? 193 ARG A NH2 1 
ATOM 1331 N N   . VAL A 1 186 ? -54.343 28.926  -39.509 1.00 69.89  ? 194 VAL A N   1 
ATOM 1332 C CA  . VAL A 1 186 ? -53.722 28.501  -38.262 1.00 67.22  ? 194 VAL A CA  1 
ATOM 1333 C C   . VAL A 1 186 ? -54.534 29.028  -37.086 1.00 76.21  ? 194 VAL A C   1 
ATOM 1334 O O   . VAL A 1 186 ? -54.984 30.183  -37.082 1.00 83.70  ? 194 VAL A O   1 
ATOM 1335 C CB  . VAL A 1 186 ? -52.257 28.963  -38.203 1.00 59.40  ? 194 VAL A CB  1 
ATOM 1336 C CG1 . VAL A 1 186 ? -52.172 30.464  -38.046 1.00 62.02  ? 194 VAL A CG1 1 
ATOM 1337 C CG2 . VAL A 1 186 ? -51.525 28.247  -37.075 1.00 59.08  ? 194 VAL A CG2 1 
ATOM 1338 N N   . ARG A 1 187 ? -54.760 28.175  -36.090 1.00 75.18  ? 195 ARG A N   1 
ATOM 1339 C CA  . ARG A 1 187 ? -55.505 28.570  -34.900 1.00 73.65  ? 195 ARG A CA  1 
ATOM 1340 C C   . ARG A 1 187 ? -54.610 28.785  -33.688 1.00 71.52  ? 195 ARG A C   1 
ATOM 1341 O O   . ARG A 1 187 ? -54.707 29.822  -33.022 1.00 72.18  ? 195 ARG A O   1 
ATOM 1342 C CB  . ARG A 1 187 ? -56.575 27.518  -34.574 1.00 72.97  ? 195 ARG A CB  1 
ATOM 1343 C CG  . ARG A 1 187 ? -57.649 27.358  -35.636 1.00 75.75  ? 195 ARG A CG  1 
ATOM 1344 C CD  . ARG A 1 187 ? -58.721 28.422  -35.522 1.00 80.24  ? 195 ARG A CD  1 
ATOM 1345 N NE  . ARG A 1 187 ? -59.733 28.274  -36.559 1.00 87.98  ? 195 ARG A NE  1 
ATOM 1346 C CZ  . ARG A 1 187 ? -61.021 28.066  -36.321 1.00 84.51  ? 195 ARG A CZ  1 
ATOM 1347 N NH1 . ARG A 1 187 ? -61.533 28.221  -35.112 1.00 82.35  ? 195 ARG A NH1 1 
ATOM 1348 N NH2 . ARG A 1 187 ? -61.828 27.773  -37.337 1.00 87.79  ? 195 ARG A NH2 1 
ATOM 1349 N N   . GLY A 1 188 ? -53.734 27.825  -33.381 1.00 69.07  ? 196 GLY A N   1 
ATOM 1350 C CA  . GLY A 1 188 ? -52.900 27.902  -32.205 1.00 66.29  ? 196 GLY A CA  1 
ATOM 1351 C C   . GLY A 1 188 ? -51.461 27.529  -32.528 1.00 63.60  ? 196 GLY A C   1 
ATOM 1352 O O   . GLY A 1 188 ? -51.161 26.985  -33.593 1.00 66.37  ? 196 GLY A O   1 
ATOM 1353 N N   . TYR A 1 189 ? -50.577 27.837  -31.582 1.00 62.35  ? 197 TYR A N   1 
ATOM 1354 C CA  . TYR A 1 189 ? -49.150 27.557  -31.714 1.00 60.53  ? 197 TYR A CA  1 
ATOM 1355 C C   . TYR A 1 189 ? -48.649 26.951  -30.414 1.00 64.20  ? 197 TYR A C   1 
ATOM 1356 O O   . TYR A 1 189 ? -48.711 27.594  -29.361 1.00 69.64  ? 197 TYR A O   1 
ATOM 1357 C CB  . TYR A 1 189 ? -48.337 28.816  -32.045 1.00 55.22  ? 197 TYR A CB  1 
ATOM 1358 C CG  . TYR A 1 189 ? -48.591 29.417  -33.409 1.00 65.14  ? 197 TYR A CG  1 
ATOM 1359 C CD1 . TYR A 1 189 ? -49.805 30.019  -33.720 1.00 69.50  ? 197 TYR A CD1 1 
ATOM 1360 C CD2 . TYR A 1 189 ? -47.616 29.363  -34.396 1.00 66.78  ? 197 TYR A CD2 1 
ATOM 1361 C CE1 . TYR A 1 189 ? -50.029 30.565  -34.969 1.00 69.93  ? 197 TYR A CE1 1 
ATOM 1362 C CE2 . TYR A 1 189 ? -47.833 29.900  -35.645 1.00 62.98  ? 197 TYR A CE2 1 
ATOM 1363 C CZ  . TYR A 1 189 ? -49.040 30.498  -35.928 1.00 64.94  ? 197 TYR A CZ  1 
ATOM 1364 O OH  . TYR A 1 189 ? -49.251 31.034  -37.177 1.00 64.63  ? 197 TYR A OH  1 
ATOM 1365 N N   . VAL A 1 190 ? -48.151 25.719  -30.488 1.00 54.57  ? 198 VAL A N   1 
ATOM 1366 C CA  . VAL A 1 190 ? -47.577 25.031  -29.340 1.00 52.46  ? 198 VAL A CA  1 
ATOM 1367 C C   . VAL A 1 190 ? -46.061 25.111  -29.444 1.00 53.50  ? 198 VAL A C   1 
ATOM 1368 O O   . VAL A 1 190 ? -45.481 24.767  -30.481 1.00 61.93  ? 198 VAL A O   1 
ATOM 1369 C CB  . VAL A 1 190 ? -48.052 23.569  -29.269 1.00 57.72  ? 198 VAL A CB  1 
ATOM 1370 C CG1 . VAL A 1 190 ? -47.338 22.832  -28.146 1.00 55.06  ? 198 VAL A CG1 1 
ATOM 1371 C CG2 . VAL A 1 190 ? -49.560 23.509  -29.081 1.00 59.98  ? 198 VAL A CG2 1 
ATOM 1372 N N   . LEU A 1 191 ? -45.420 25.562  -28.368 1.00 54.83  ? 199 LEU A N   1 
ATOM 1373 C CA  . LEU A 1 191 ? -43.994 25.888  -28.358 1.00 57.61  ? 199 LEU A CA  1 
ATOM 1374 C C   . LEU A 1 191 ? -43.336 25.097  -27.233 1.00 58.90  ? 199 LEU A C   1 
ATOM 1375 O O   . LEU A 1 191 ? -43.469 25.442  -26.055 1.00 60.68  ? 199 LEU A O   1 
ATOM 1376 C CB  . LEU A 1 191 ? -43.765 27.387  -28.201 1.00 56.31  ? 199 LEU A CB  1 
ATOM 1377 C CG  . LEU A 1 191 ? -43.832 28.205  -29.492 1.00 57.21  ? 199 LEU A CG  1 
ATOM 1378 C CD1 . LEU A 1 191 ? -45.254 28.326  -30.001 1.00 57.23  ? 199 LEU A CD1 1 
ATOM 1379 C CD2 . LEU A 1 191 ? -43.221 29.579  -29.268 1.00 57.99  ? 199 LEU A CD2 1 
ATOM 1380 N N   . MET A 1 192 ? -42.625 24.040  -27.609 1.00 58.47  ? 200 MET A N   1 
ATOM 1381 C CA  . MET A 1 192 ? -42.161 23.015  -26.682 1.00 59.24  ? 200 MET A CA  1 
ATOM 1382 C C   . MET A 1 192 ? -40.658 23.166  -26.491 1.00 60.85  ? 200 MET A C   1 
ATOM 1383 O O   . MET A 1 192 ? -39.877 22.811  -27.381 1.00 68.62  ? 200 MET A O   1 
ATOM 1384 C CB  . MET A 1 192 ? -42.517 21.634  -27.219 1.00 67.73  ? 200 MET A CB  1 
ATOM 1385 C CG  . MET A 1 192 ? -44.002 21.464  -27.462 1.00 66.29  ? 200 MET A CG  1 
ATOM 1386 S SD  . MET A 1 192 ? -44.434 19.750  -27.739 1.00 71.64  ? 200 MET A SD  1 
ATOM 1387 C CE  . MET A 1 192 ? -44.391 19.205  -26.044 1.00 66.78  ? 200 MET A CE  1 
ATOM 1388 N N   . GLY A 1 193 ? -40.260 23.666  -25.322 1.00 65.54  ? 201 GLY A N   1 
ATOM 1389 C CA  . GLY A 1 193 ? -38.886 24.029  -25.061 1.00 66.88  ? 201 GLY A CA  1 
ATOM 1390 C C   . GLY A 1 193 ? -38.279 24.855  -26.179 1.00 63.58  ? 201 GLY A C   1 
ATOM 1391 O O   . GLY A 1 193 ? -37.277 24.469  -26.788 1.00 63.86  ? 201 GLY A O   1 
ATOM 1392 N N   . PRO A 1 194 ? -38.881 26.009  -26.473 1.00 62.45  ? 202 PRO A N   1 
ATOM 1393 C CA  . PRO A 1 194 ? -38.460 26.780  -27.649 1.00 63.56  ? 202 PRO A CA  1 
ATOM 1394 C C   . PRO A 1 194 ? -37.029 27.279  -27.516 1.00 61.25  ? 202 PRO A C   1 
ATOM 1395 O O   . PRO A 1 194 ? -36.614 27.762  -26.461 1.00 66.27  ? 202 PRO A O   1 
ATOM 1396 C CB  . PRO A 1 194 ? -39.454 27.947  -27.683 1.00 63.66  ? 202 PRO A CB  1 
ATOM 1397 C CG  . PRO A 1 194 ? -40.589 27.523  -26.811 1.00 64.74  ? 202 PRO A CG  1 
ATOM 1398 C CD  . PRO A 1 194 ? -39.975 26.677  -25.750 1.00 61.58  ? 202 PRO A CD  1 
ATOM 1399 N N   . PHE A 1 195 ? -36.282 27.171  -28.611 1.00 61.01  ? 203 PHE A N   1 
ATOM 1400 C CA  . PHE A 1 195 ? -34.869 27.542  -28.649 1.00 56.93  ? 203 PHE A CA  1 
ATOM 1401 C C   . PHE A 1 195 ? -34.770 29.043  -28.897 1.00 63.38  ? 203 PHE A C   1 
ATOM 1402 O O   . PHE A 1 195 ? -34.723 29.506  -30.038 1.00 64.38  ? 203 PHE A O   1 
ATOM 1403 C CB  . PHE A 1 195 ? -34.149 26.737  -29.723 1.00 58.43  ? 203 PHE A CB  1 
ATOM 1404 C CG  . PHE A 1 195 ? -32.675 26.994  -29.798 1.00 68.23  ? 203 PHE A CG  1 
ATOM 1405 C CD1 . PHE A 1 195 ? -31.898 26.986  -28.653 1.00 67.85  ? 203 PHE A CD1 1 
ATOM 1406 C CD2 . PHE A 1 195 ? -32.061 27.213  -31.020 1.00 80.01  ? 203 PHE A CD2 1 
ATOM 1407 C CE1 . PHE A 1 195 ? -30.539 27.211  -28.724 1.00 74.41  ? 203 PHE A CE1 1 
ATOM 1408 C CE2 . PHE A 1 195 ? -30.703 27.436  -31.096 1.00 77.37  ? 203 PHE A CE2 1 
ATOM 1409 C CZ  . PHE A 1 195 ? -29.942 27.433  -29.946 1.00 80.19  ? 203 PHE A CZ  1 
ATOM 1410 N N   . PHE A 1 196 ? -34.739 29.817  -27.816 1.00 65.51  ? 204 PHE A N   1 
ATOM 1411 C CA  . PHE A 1 196 ? -34.629 31.265  -27.895 1.00 63.12  ? 204 PHE A CA  1 
ATOM 1412 C C   . PHE A 1 196 ? -33.255 31.712  -27.411 1.00 71.12  ? 204 PHE A C   1 
ATOM 1413 O O   . PHE A 1 196 ? -32.548 30.977  -26.716 1.00 75.65  ? 204 PHE A O   1 
ATOM 1414 C CB  . PHE A 1 196 ? -35.723 31.951  -27.070 1.00 62.09  ? 204 PHE A CB  1 
ATOM 1415 C CG  . PHE A 1 196 ? -37.083 31.891  -27.702 1.00 59.14  ? 204 PHE A CG  1 
ATOM 1416 C CD1 . PHE A 1 196 ? -37.292 32.386  -28.977 1.00 69.04  ? 204 PHE A CD1 1 
ATOM 1417 C CD2 . PHE A 1 196 ? -38.161 31.372  -27.005 1.00 61.74  ? 204 PHE A CD2 1 
ATOM 1418 C CE1 . PHE A 1 196 ? -38.543 32.329  -29.560 1.00 68.61  ? 204 PHE A CE1 1 
ATOM 1419 C CE2 . PHE A 1 196 ? -39.417 31.327  -27.578 1.00 63.27  ? 204 PHE A CE2 1 
ATOM 1420 C CZ  . PHE A 1 196 ? -39.608 31.804  -28.858 1.00 66.09  ? 204 PHE A CZ  1 
ATOM 1421 N N   . GLY A 1 197 ? -32.881 32.940  -27.786 1.00 74.56  ? 205 GLY A N   1 
ATOM 1422 C CA  . GLY A 1 197 ? -31.529 33.414  -27.593 1.00 86.55  ? 205 GLY A CA  1 
ATOM 1423 C C   . GLY A 1 197 ? -31.493 34.796  -26.965 1.00 94.85  ? 205 GLY A C   1 
ATOM 1424 O O   . GLY A 1 197 ? -32.522 35.444  -26.758 1.00 92.27  ? 205 GLY A O   1 
ATOM 1425 N N   . GLY A 1 198 ? -30.273 35.229  -26.656 1.00 90.60  ? 206 GLY A N   1 
ATOM 1426 C CA  . GLY A 1 198 ? -30.025 36.529  -26.067 1.00 90.57  ? 206 GLY A CA  1 
ATOM 1427 C C   . GLY A 1 198 ? -28.668 36.578  -25.395 1.00 92.25  ? 206 GLY A C   1 
ATOM 1428 O O   . GLY A 1 198 ? -28.199 35.566  -24.864 1.00 87.01  ? 206 GLY A O   1 
ATOM 1429 N N   . GLU A 1 199 ? -28.021 37.747  -25.413 1.00 93.59  ? 207 GLU A N   1 
ATOM 1430 C CA  . GLU A 1 199 ? -26.676 37.848  -24.854 1.00 92.39  ? 207 GLU A CA  1 
ATOM 1431 C C   . GLU A 1 199 ? -26.697 37.724  -23.335 1.00 94.47  ? 207 GLU A C   1 
ATOM 1432 O O   . GLU A 1 199 ? -25.877 37.003  -22.756 1.00 94.23  ? 207 GLU A O   1 
ATOM 1433 C CB  . GLU A 1 199 ? -26.021 39.163  -25.285 1.00 95.57  ? 207 GLU A CB  1 
ATOM 1434 C CG  . GLU A 1 199 ? -25.446 39.173  -26.707 1.00 90.14  ? 207 GLU A CG  1 
ATOM 1435 C CD  . GLU A 1 199 ? -24.297 38.190  -26.936 1.00 98.54  ? 207 GLU A CD  1 
ATOM 1436 O OE1 . GLU A 1 199 ? -23.942 37.422  -26.018 1.00 96.93  ? 207 GLU A OE1 1 
ATOM 1437 O OE2 . GLU A 1 199 ? -23.747 38.181  -28.060 1.00 100.98 ? 207 GLU A OE2 1 
ATOM 1438 N N   . GLU A 1 200 ? -27.627 38.406  -22.673 1.00 92.30  ? 208 GLU A N   1 
ATOM 1439 C CA  . GLU A 1 200 ? -27.745 38.295  -21.224 1.00 96.52  ? 208 GLU A CA  1 
ATOM 1440 C C   . GLU A 1 200 ? -28.374 36.958  -20.850 1.00 94.69  ? 208 GLU A C   1 
ATOM 1441 O O   . GLU A 1 200 ? -29.505 36.659  -21.251 1.00 94.87  ? 208 GLU A O   1 
ATOM 1442 C CB  . GLU A 1 200 ? -28.573 39.444  -20.660 1.00 103.87 ? 208 GLU A CB  1 
ATOM 1443 C CG  . GLU A 1 200 ? -28.461 39.566  -19.148 1.00 108.60 ? 208 GLU A CG  1 
ATOM 1444 C CD  . GLU A 1 200 ? -29.434 40.569  -18.566 1.00 115.29 ? 208 GLU A CD  1 
ATOM 1445 O OE1 . GLU A 1 200 ? -29.342 41.764  -18.919 1.00 118.08 ? 208 GLU A OE1 1 
ATOM 1446 O OE2 . GLU A 1 200 ? -30.293 40.159  -17.758 1.00 120.20 ? 208 GLU A OE2 1 
ATOM 1447 N N   . ARG A 1 201 ? -27.640 36.156  -20.087 1.00 89.75  ? 209 ARG A N   1 
ATOM 1448 C CA  . ARG A 1 201 ? -28.159 34.894  -19.586 1.00 90.06  ? 209 ARG A CA  1 
ATOM 1449 C C   . ARG A 1 201 ? -29.120 35.146  -18.426 1.00 94.65  ? 209 ARG A C   1 
ATOM 1450 O O   . ARG A 1 201 ? -29.048 36.166  -17.734 1.00 96.24  ? 209 ARG A O   1 
ATOM 1451 C CB  . ARG A 1 201 ? -27.026 33.969  -19.125 1.00 91.04  ? 209 ARG A CB  1 
ATOM 1452 C CG  . ARG A 1 201 ? -26.263 33.215  -20.225 1.00 93.92  ? 209 ARG A CG  1 
ATOM 1453 C CD  . ARG A 1 201 ? -25.775 34.118  -21.349 1.00 90.45  ? 209 ARG A CD  1 
ATOM 1454 N NE  . ARG A 1 201 ? -24.575 33.602  -21.998 1.00 94.45  ? 209 ARG A NE  1 
ATOM 1455 C CZ  . ARG A 1 201 ? -24.551 32.575  -22.836 1.00 92.97  ? 209 ARG A CZ  1 
ATOM 1456 N NH1 . ARG A 1 201 ? -25.653 31.919  -23.159 1.00 89.21  ? 209 ARG A NH1 1 
ATOM 1457 N NH2 . ARG A 1 201 ? -23.390 32.197  -23.365 1.00 91.97  ? 209 ARG A NH2 1 
ATOM 1458 N N   . THR A 1 202 ? -30.033 34.201  -18.221 1.00 99.22  ? 210 THR A N   1 
ATOM 1459 C CA  . THR A 1 202 ? -30.952 34.236  -17.093 1.00 103.40 ? 210 THR A CA  1 
ATOM 1460 C C   . THR A 1 202 ? -30.797 32.949  -16.293 1.00 100.61 ? 210 THR A C   1 
ATOM 1461 O O   . THR A 1 202 ? -30.649 31.870  -16.873 1.00 97.61  ? 210 THR A O   1 
ATOM 1462 C CB  . THR A 1 202 ? -32.404 34.403  -17.561 1.00 105.32 ? 210 THR A CB  1 
ATOM 1463 O OG1 . THR A 1 202 ? -32.513 35.583  -18.363 1.00 103.82 ? 210 THR A OG1 1 
ATOM 1464 C CG2 . THR A 1 202 ? -33.323 34.564  -16.364 1.00 101.56 ? 210 THR A CG2 1 
ATOM 1465 N N   . ASN A 1 203 ? -30.829 33.080  -14.960 1.00 102.67 ? 211 ASN A N   1 
ATOM 1466 C CA  . ASN A 1 203 ? -30.631 32.015  -13.972 1.00 105.19 ? 211 ASN A CA  1 
ATOM 1467 C C   . ASN A 1 203 ? -30.408 30.621  -14.555 1.00 102.68 ? 211 ASN A C   1 
ATOM 1468 O O   . ASN A 1 203 ? -29.373 29.996  -14.303 1.00 102.88 ? 211 ASN A O   1 
ATOM 1469 C CB  . ASN A 1 203 ? -31.830 31.954  -13.021 1.00 105.82 ? 211 ASN A CB  1 
ATOM 1470 C CG  . ASN A 1 203 ? -32.407 33.322  -12.716 1.00 111.10 ? 211 ASN A CG  1 
ATOM 1471 O OD1 . ASN A 1 203 ? -31.740 34.176  -12.133 1.00 116.20 ? 211 ASN A OD1 1 
ATOM 1472 N ND2 . ASN A 1 203 ? -33.659 33.532  -13.105 1.00 104.85 ? 211 ASN A ND2 1 
ATOM 1473 N N   . SER A 1 204 ? -31.383 30.132  -15.329 1.00 101.25 ? 212 SER A N   1 
ATOM 1474 C CA  . SER A 1 204 ? -31.349 28.753  -15.812 1.00 99.15  ? 212 SER A CA  1 
ATOM 1475 C C   . SER A 1 204 ? -30.131 28.492  -16.693 1.00 95.31  ? 212 SER A C   1 
ATOM 1476 O O   . SER A 1 204 ? -29.432 27.488  -16.513 1.00 96.52  ? 212 SER A O   1 
ATOM 1477 C CB  . SER A 1 204 ? -32.641 28.429  -16.563 1.00 94.73  ? 212 SER A CB  1 
ATOM 1478 O OG  . SER A 1 204 ? -33.008 29.487  -17.431 1.00 92.71  ? 212 SER A OG  1 
ATOM 1479 N N   . GLU A 1 205 ? -29.881 29.365  -17.677 1.00 93.96  ? 213 GLU A N   1 
ATOM 1480 C CA  . GLU A 1 205 ? -28.666 29.238  -18.481 1.00 97.27  ? 213 GLU A CA  1 
ATOM 1481 C C   . GLU A 1 205 ? -27.415 29.120  -17.618 1.00 97.53  ? 213 GLU A C   1 
ATOM 1482 O O   . GLU A 1 205 ? -26.484 28.381  -17.960 1.00 94.72  ? 213 GLU A O   1 
ATOM 1483 C CB  . GLU A 1 205 ? -28.503 30.419  -19.445 1.00 97.28  ? 213 GLU A CB  1 
ATOM 1484 C CG  . GLU A 1 205 ? -29.394 30.434  -20.681 1.00 91.18  ? 213 GLU A CG  1 
ATOM 1485 C CD  . GLU A 1 205 ? -30.617 31.306  -20.547 1.00 94.37  ? 213 GLU A CD  1 
ATOM 1486 O OE1 . GLU A 1 205 ? -31.095 31.520  -19.419 1.00 98.68  ? 213 GLU A OE1 1 
ATOM 1487 O OE2 . GLU A 1 205 ? -31.069 31.825  -21.585 1.00 86.33  ? 213 GLU A OE2 1 
ATOM 1488 N N   . ASN A 1 206 ? -27.373 29.838  -16.497 1.00 94.96  ? 214 ASN A N   1 
ATOM 1489 C CA  . ASN A 1 206 ? -26.193 29.855  -15.643 1.00 90.54  ? 214 ASN A CA  1 
ATOM 1490 C C   . ASN A 1 206 ? -26.139 28.727  -14.621 1.00 92.21  ? 214 ASN A C   1 
ATOM 1491 O O   . ASN A 1 206 ? -25.127 28.607  -13.923 1.00 96.62  ? 214 ASN A O   1 
ATOM 1492 C CB  . ASN A 1 206 ? -26.098 31.196  -14.910 1.00 90.38  ? 214 ASN A CB  1 
ATOM 1493 C CG  . ASN A 1 206 ? -26.035 32.375  -15.861 1.00 90.54  ? 214 ASN A CG  1 
ATOM 1494 O OD1 . ASN A 1 206 ? -26.986 33.146  -15.975 1.00 89.46  ? 214 ASN A OD1 1 
ATOM 1495 N ND2 . ASN A 1 206 ? -24.908 32.519  -16.550 1.00 81.78  ? 214 ASN A ND2 1 
ATOM 1496 N N   . GLY A 1 207 ? -27.173 27.899  -14.502 1.00 92.13  ? 215 GLY A N   1 
ATOM 1497 C CA  . GLY A 1 207 ? -27.127 26.832  -13.531 1.00 90.73  ? 215 GLY A CA  1 
ATOM 1498 C C   . GLY A 1 207 ? -26.592 25.532  -14.097 1.00 94.21  ? 215 GLY A C   1 
ATOM 1499 O O   . GLY A 1 207 ? -25.671 25.514  -14.919 1.00 91.03  ? 215 GLY A O   1 
ATOM 1500 N N   . PRO A 1 208 ? -27.172 24.408  -13.665 1.00 96.35  ? 216 PRO A N   1 
ATOM 1501 C CA  . PRO A 1 208 ? -26.602 23.091  -13.990 1.00 96.23  ? 216 PRO A CA  1 
ATOM 1502 C C   . PRO A 1 208 ? -26.956 22.678  -15.413 1.00 89.68  ? 216 PRO A C   1 
ATOM 1503 O O   . PRO A 1 208 ? -28.132 22.526  -15.751 1.00 89.60  ? 216 PRO A O   1 
ATOM 1504 C CB  . PRO A 1 208 ? -27.242 22.164  -12.950 1.00 95.10  ? 216 PRO A CB  1 
ATOM 1505 C CG  . PRO A 1 208 ? -28.546 22.808  -12.639 1.00 92.96  ? 216 PRO A CG  1 
ATOM 1506 C CD  . PRO A 1 208 ? -28.332 24.301  -12.761 1.00 90.65  ? 216 PRO A CD  1 
ATOM 1507 N N   . SER A 1 209 ? -25.933 22.511  -16.252 1.00 86.96  ? 217 SER A N   1 
ATOM 1508 C CA  . SER A 1 209 ? -26.155 21.993  -17.596 1.00 98.31  ? 217 SER A CA  1 
ATOM 1509 C C   . SER A 1 209 ? -26.753 20.593  -17.531 1.00 97.94  ? 217 SER A C   1 
ATOM 1510 O O   . SER A 1 209 ? -26.416 19.787  -16.658 1.00 99.33  ? 217 SER A O   1 
ATOM 1511 C CB  . SER A 1 209 ? -24.850 21.987  -18.389 1.00 98.95  ? 217 SER A CB  1 
ATOM 1512 O OG  . SER A 1 209 ? -24.591 23.269  -18.934 1.00 97.20  ? 217 SER A OG  1 
ATOM 1513 N N   . GLU A 1 210 ? -27.650 20.314  -18.470 1.00 94.07  ? 218 GLU A N   1 
ATOM 1514 C CA  . GLU A 1 210 ? -28.436 19.094  -18.476 1.00 90.45  ? 218 GLU A CA  1 
ATOM 1515 C C   . GLU A 1 210 ? -27.595 17.916  -18.961 1.00 99.33  ? 218 GLU A C   1 
ATOM 1516 O O   . GLU A 1 210 ? -26.444 18.068  -19.380 1.00 101.79 ? 218 GLU A O   1 
ATOM 1517 C CB  . GLU A 1 210 ? -29.668 19.294  -19.350 1.00 87.34  ? 218 GLU A CB  1 
ATOM 1518 C CG  . GLU A 1 210 ? -30.676 20.216  -18.677 1.00 88.80  ? 218 GLU A CG  1 
ATOM 1519 C CD  . GLU A 1 210 ? -32.109 19.957  -19.046 1.00 89.15  ? 218 GLU A CD  1 
ATOM 1520 O OE1 . GLU A 1 210 ? -32.449 20.030  -20.245 1.00 81.79  ? 218 GLU A OE1 1 
ATOM 1521 O OE2 . GLU A 1 210 ? -32.916 19.792  -18.112 1.00 96.67  ? 218 GLU A OE2 1 
ATOM 1522 N N   . ALA A 1 211 ? -28.185 16.720  -18.892 1.00 97.35  ? 219 ALA A N   1 
ATOM 1523 C CA  . ALA A 1 211 ? -27.604 15.565  -19.572 1.00 95.18  ? 219 ALA A CA  1 
ATOM 1524 C C   . ALA A 1 211 ? -27.396 15.842  -21.057 1.00 98.12  ? 219 ALA A C   1 
ATOM 1525 O O   . ALA A 1 211 ? -26.344 15.519  -21.621 1.00 104.35 ? 219 ALA A O   1 
ATOM 1526 C CB  . ALA A 1 211 ? -28.494 14.337  -19.372 1.00 94.70  ? 219 ALA A CB  1 
ATOM 1527 N N   . LEU A 1 212 ? -28.393 16.438  -21.708 1.00 91.77  ? 220 LEU A N   1 
ATOM 1528 C CA  . LEU A 1 212 ? -28.308 16.746  -23.133 1.00 83.82  ? 220 LEU A CA  1 
ATOM 1529 C C   . LEU A 1 212 ? -27.791 18.164  -23.353 1.00 81.44  ? 220 LEU A C   1 
ATOM 1530 O O   . LEU A 1 212 ? -26.740 18.364  -23.969 1.00 82.86  ? 220 LEU A O   1 
ATOM 1531 C CB  . LEU A 1 212 ? -29.676 16.564  -23.801 1.00 81.08  ? 220 LEU A CB  1 
ATOM 1532 C CG  . LEU A 1 212 ? -29.706 16.395  -25.324 1.00 84.62  ? 220 LEU A CG  1 
ATOM 1533 C CD1 . LEU A 1 212 ? -28.464 15.677  -25.833 1.00 89.16  ? 220 LEU A CD1 1 
ATOM 1534 C CD2 . LEU A 1 212 ? -30.970 15.667  -25.760 1.00 74.21  ? 220 LEU A CD2 1 
ATOM 1535 N N   . LEU A 1 213 ? -28.525 19.151  -22.852 1.00 78.53  ? 221 LEU A N   1 
ATOM 1536 C CA  . LEU A 1 213 ? -28.292 20.552  -23.171 1.00 81.12  ? 221 LEU A CA  1 
ATOM 1537 C C   . LEU A 1 213 ? -27.251 21.147  -22.232 1.00 92.37  ? 221 LEU A C   1 
ATOM 1538 O O   . LEU A 1 213 ? -27.346 20.993  -21.011 1.00 97.95  ? 221 LEU A O   1 
ATOM 1539 C CB  . LEU A 1 213 ? -29.595 21.351  -23.090 1.00 74.06  ? 221 LEU A CB  1 
ATOM 1540 C CG  . LEU A 1 213 ? -30.593 21.266  -24.251 1.00 78.24  ? 221 LEU A CG  1 
ATOM 1541 C CD1 . LEU A 1 213 ? -29.968 21.835  -25.514 1.00 70.75  ? 221 LEU A CD1 1 
ATOM 1542 C CD2 . LEU A 1 213 ? -31.104 19.853  -24.499 1.00 86.48  ? 221 LEU A CD2 1 
ATOM 1543 N N   . SER A 1 214 ? -26.255 21.815  -22.808 1.00 89.15  ? 222 SER A N   1 
ATOM 1544 C CA  . SER A 1 214 ? -25.264 22.553  -22.042 1.00 85.82  ? 222 SER A CA  1 
ATOM 1545 C C   . SER A 1 214 ? -25.189 23.970  -22.587 1.00 83.34  ? 222 SER A C   1 
ATOM 1546 O O   . SER A 1 214 ? -25.399 24.202  -23.780 1.00 83.87  ? 222 SER A O   1 
ATOM 1547 C CB  . SER A 1 214 ? -23.881 21.890  -22.107 1.00 91.36  ? 222 SER A CB  1 
ATOM 1548 O OG  . SER A 1 214 ? -23.161 22.319  -23.251 1.00 91.90  ? 222 SER A OG  1 
ATOM 1549 N N   . LEU A 1 215 ? -24.881 24.915  -21.694 1.00 87.20  ? 223 LEU A N   1 
ATOM 1550 C CA  . LEU A 1 215 ? -24.850 26.328  -22.065 1.00 91.75  ? 223 LEU A CA  1 
ATOM 1551 C C   . LEU A 1 215 ? -23.954 26.560  -23.276 1.00 88.02  ? 223 LEU A C   1 
ATOM 1552 O O   . LEU A 1 215 ? -24.359 27.211  -24.247 1.00 87.10  ? 223 LEU A O   1 
ATOM 1553 C CB  . LEU A 1 215 ? -24.409 27.166  -20.858 1.00 96.62  ? 223 LEU A CB  1 
ATOM 1554 C CG  . LEU A 1 215 ? -24.442 28.702  -20.871 1.00 91.62  ? 223 LEU A CG  1 
ATOM 1555 C CD1 . LEU A 1 215 ? -23.364 29.343  -21.727 1.00 84.05  ? 223 LEU A CD1 1 
ATOM 1556 C CD2 . LEU A 1 215 ? -25.810 29.145  -21.357 1.00 81.57  ? 223 LEU A CD2 1 
ATOM 1557 N N   . ASP A 1 216 ? -22.728 26.033  -23.235 1.00 86.26  ? 224 ASP A N   1 
ATOM 1558 C CA  . ASP A 1 216 ? -21.825 26.186  -24.370 1.00 88.82  ? 224 ASP A CA  1 
ATOM 1559 C C   . ASP A 1 216 ? -22.400 25.561  -25.634 1.00 92.86  ? 224 ASP A C   1 
ATOM 1560 O O   . ASP A 1 216 ? -22.177 26.076  -26.735 1.00 93.60  ? 224 ASP A O   1 
ATOM 1561 C CB  . ASP A 1 216 ? -20.461 25.576  -24.049 1.00 91.96  ? 224 ASP A CB  1 
ATOM 1562 C CG  . ASP A 1 216 ? -19.411 25.929  -25.084 1.00 105.88 ? 224 ASP A CG  1 
ATOM 1563 O OD1 . ASP A 1 216 ? -19.444 27.066  -25.598 1.00 99.51  ? 224 ASP A OD1 1 
ATOM 1564 O OD2 . ASP A 1 216 ? -18.555 25.070  -25.384 1.00 121.15 ? 224 ASP A OD2 1 
ATOM 1565 N N   . LEU A 1 217 ? -23.152 24.466  -25.497 1.00 95.00  ? 225 LEU A N   1 
ATOM 1566 C CA  . LEU A 1 217 ? -23.775 23.836  -26.659 1.00 92.14  ? 225 LEU A CA  1 
ATOM 1567 C C   . LEU A 1 217 ? -24.822 24.747  -27.290 1.00 90.31  ? 225 LEU A C   1 
ATOM 1568 O O   . LEU A 1 217 ? -24.878 24.886  -28.518 1.00 92.57  ? 225 LEU A O   1 
ATOM 1569 C CB  . LEU A 1 217 ? -24.393 22.495  -26.263 1.00 85.45  ? 225 LEU A CB  1 
ATOM 1570 C CG  . LEU A 1 217 ? -25.246 21.799  -27.325 1.00 81.86  ? 225 LEU A CG  1 
ATOM 1571 C CD1 . LEU A 1 217 ? -24.367 21.222  -28.423 1.00 90.00  ? 225 LEU A CD1 1 
ATOM 1572 C CD2 . LEU A 1 217 ? -26.104 20.715  -26.696 1.00 86.43  ? 225 LEU A CD2 1 
ATOM 1573 N N   . LEU A 1 218 ? -25.683 25.357  -26.468 1.00 89.06  ? 226 LEU A N   1 
ATOM 1574 C CA  . LEU A 1 218 ? -26.652 26.307  -27.010 1.00 82.99  ? 226 LEU A CA  1 
ATOM 1575 C C   . LEU A 1 218 ? -25.961 27.469  -27.715 1.00 83.24  ? 226 LEU A C   1 
ATOM 1576 O O   . LEU A 1 218 ? -26.433 27.936  -28.759 1.00 80.19  ? 226 LEU A O   1 
ATOM 1577 C CB  . LEU A 1 218 ? -27.593 26.818  -25.921 1.00 85.88  ? 226 LEU A CB  1 
ATOM 1578 C CG  . LEU A 1 218 ? -28.402 25.732  -25.206 1.00 82.49  ? 226 LEU A CG  1 
ATOM 1579 C CD1 . LEU A 1 218 ? -28.099 25.668  -23.713 1.00 76.88  ? 226 LEU A CD1 1 
ATOM 1580 C CD2 . LEU A 1 218 ? -29.886 25.874  -25.487 1.00 83.99  ? 226 LEU A CD2 1 
ATOM 1581 N N   . ASP A 1 219 ? -24.853 27.965  -27.154 1.00 88.04  ? 227 ASP A N   1 
ATOM 1582 C CA  . ASP A 1 219 ? -24.065 28.972  -27.860 1.00 90.61  ? 227 ASP A CA  1 
ATOM 1583 C C   . ASP A 1 219 ? -23.603 28.443  -29.211 1.00 87.32  ? 227 ASP A C   1 
ATOM 1584 O O   . ASP A 1 219 ? -23.687 29.144  -30.226 1.00 87.55  ? 227 ASP A O   1 
ATOM 1585 C CB  . ASP A 1 219 ? -22.865 29.413  -27.021 1.00 95.67  ? 227 ASP A CB  1 
ATOM 1586 C CG  . ASP A 1 219 ? -23.213 29.641  -25.570 1.00 89.86  ? 227 ASP A CG  1 
ATOM 1587 O OD1 . ASP A 1 219 ? -24.290 30.204  -25.294 1.00 87.95  ? 227 ASP A OD1 1 
ATOM 1588 O OD2 . ASP A 1 219 ? -22.389 29.280  -24.705 1.00 87.75  ? 227 ASP A OD2 1 
ATOM 1589 N N   . LYS A 1 220 ? -23.075 27.215  -29.231 1.00 88.32  ? 228 LYS A N   1 
ATOM 1590 C CA  . LYS A 1 220 ? -22.692 26.572  -30.485 1.00 86.64  ? 228 LYS A CA  1 
ATOM 1591 C C   . LYS A 1 220 ? -23.833 26.623  -31.492 1.00 85.08  ? 228 LYS A C   1 
ATOM 1592 O O   . LYS A 1 220 ? -23.710 27.239  -32.557 1.00 83.88  ? 228 LYS A O   1 
ATOM 1593 C CB  . LYS A 1 220 ? -22.275 25.122  -30.226 1.00 86.89  ? 228 LYS A CB  1 
ATOM 1594 C CG  . LYS A 1 220 ? -21.015 24.953  -29.404 1.00 88.99  ? 228 LYS A CG  1 
ATOM 1595 C CD  . LYS A 1 220 ? -19.802 25.408  -30.183 1.00 89.93  ? 228 LYS A CD  1 
ATOM 1596 C CE  . LYS A 1 220 ? -19.282 24.272  -31.046 1.00 92.49  ? 228 LYS A CE  1 
ATOM 1597 N NZ  . LYS A 1 220 ? -18.426 23.342  -30.261 1.00 93.32  ? 228 LYS A NZ  1 
ATOM 1598 N N   . PHE A 1 221 ? -24.962 25.989  -31.151 1.00 85.87  ? 229 PHE A N   1 
ATOM 1599 C CA  . PHE A 1 221 ? -26.167 26.042  -31.976 1.00 84.03  ? 229 PHE A CA  1 
ATOM 1600 C C   . PHE A 1 221 ? -26.390 27.424  -32.566 1.00 83.09  ? 229 PHE A C   1 
ATOM 1601 O O   . PHE A 1 221 ? -26.588 27.571  -33.775 1.00 84.66  ? 229 PHE A O   1 
ATOM 1602 C CB  . PHE A 1 221 ? -27.387 25.623  -31.155 1.00 83.09  ? 229 PHE A CB  1 
ATOM 1603 C CG  . PHE A 1 221 ? -27.511 24.143  -30.952 1.00 85.44  ? 229 PHE A CG  1 
ATOM 1604 C CD1 . PHE A 1 221 ? -26.637 23.266  -31.570 1.00 80.54  ? 229 PHE A CD1 1 
ATOM 1605 C CD2 . PHE A 1 221 ? -28.509 23.629  -30.140 1.00 85.28  ? 229 PHE A CD2 1 
ATOM 1606 C CE1 . PHE A 1 221 ? -26.758 21.903  -31.385 1.00 79.92  ? 229 PHE A CE1 1 
ATOM 1607 C CE2 . PHE A 1 221 ? -28.634 22.270  -29.949 1.00 84.03  ? 229 PHE A CE2 1 
ATOM 1608 C CZ  . PHE A 1 221 ? -27.757 21.404  -30.571 1.00 81.88  ? 229 PHE A CZ  1 
ATOM 1609 N N   . TRP A 1 222 ? -26.352 28.455  -31.720 1.00 79.48  ? 230 TRP A N   1 
ATOM 1610 C CA  . TRP A 1 222 ? -26.536 29.814  -32.214 1.00 76.44  ? 230 TRP A CA  1 
ATOM 1611 C C   . TRP A 1 222 ? -25.423 30.213  -33.180 1.00 74.10  ? 230 TRP A C   1 
ATOM 1612 O O   . TRP A 1 222 ? -25.695 30.713  -34.278 1.00 73.96  ? 230 TRP A O   1 
ATOM 1613 C CB  . TRP A 1 222 ? -26.642 30.799  -31.048 1.00 76.29  ? 230 TRP A CB  1 
ATOM 1614 C CG  . TRP A 1 222 ? -27.930 30.680  -30.265 1.00 76.37  ? 230 TRP A CG  1 
ATOM 1615 C CD1 . TRP A 1 222 ? -28.057 30.466  -28.922 1.00 78.80  ? 230 TRP A CD1 1 
ATOM 1616 C CD2 . TRP A 1 222 ? -29.267 30.732  -30.788 1.00 69.08  ? 230 TRP A CD2 1 
ATOM 1617 N NE1 . TRP A 1 222 ? -29.386 30.405  -28.574 1.00 75.75  ? 230 TRP A NE1 1 
ATOM 1618 C CE2 . TRP A 1 222 ? -30.148 30.567  -29.701 1.00 71.17  ? 230 TRP A CE2 1 
ATOM 1619 C CE3 . TRP A 1 222 ? -29.804 30.912  -32.067 1.00 71.46  ? 230 TRP A CE3 1 
ATOM 1620 C CZ2 . TRP A 1 222 ? -31.532 30.566  -29.857 1.00 72.53  ? 230 TRP A CZ2 1 
ATOM 1621 C CZ3 . TRP A 1 222 ? -31.179 30.915  -32.218 1.00 72.00  ? 230 TRP A CZ3 1 
ATOM 1622 C CH2 . TRP A 1 222 ? -32.027 30.746  -31.119 1.00 73.27  ? 230 TRP A CH2 1 
ATOM 1623 N N   . ARG A 1 223 ? -24.161 29.984  -32.800 1.00 78.03  ? 231 ARG A N   1 
ATOM 1624 C CA  . ARG A 1 223 ? -23.040 30.366  -33.660 1.00 80.78  ? 231 ARG A CA  1 
ATOM 1625 C C   . ARG A 1 223 ? -23.167 29.785  -35.066 1.00 78.33  ? 231 ARG A C   1 
ATOM 1626 O O   . ARG A 1 223 ? -23.014 30.503  -36.061 1.00 70.83  ? 231 ARG A O   1 
ATOM 1627 C CB  . ARG A 1 223 ? -21.712 29.948  -33.030 1.00 83.00  ? 231 ARG A CB  1 
ATOM 1628 C CG  . ARG A 1 223 ? -21.207 30.883  -31.930 1.00 82.40  ? 231 ARG A CG  1 
ATOM 1629 C CD  . ARG A 1 223 ? -19.782 30.521  -31.552 1.00 86.28  ? 231 ARG A CD  1 
ATOM 1630 N NE  . ARG A 1 223 ? -19.703 29.350  -30.687 1.00 90.61  ? 231 ARG A NE  1 
ATOM 1631 C CZ  . ARG A 1 223 ? -19.920 29.377  -29.379 1.00 95.51  ? 231 ARG A CZ  1 
ATOM 1632 N NH1 . ARG A 1 223 ? -20.360 30.468  -28.776 1.00 92.81  ? 231 ARG A NH1 1 
ATOM 1633 N NH2 . ARG A 1 223 ? -19.733 28.270  -28.665 1.00 93.01  ? 231 ARG A NH2 1 
ATOM 1634 N N   . LEU A 1 224 ? -23.458 28.486  -35.170 1.00 75.13  ? 232 LEU A N   1 
ATOM 1635 C CA  . LEU A 1 224 ? -23.631 27.889  -36.491 1.00 73.95  ? 232 LEU A CA  1 
ATOM 1636 C C   . LEU A 1 224 ? -24.892 28.394  -37.174 1.00 80.42  ? 232 LEU A C   1 
ATOM 1637 O O   . LEU A 1 224 ? -24.940 28.465  -38.408 1.00 87.13  ? 232 LEU A O   1 
ATOM 1638 C CB  . LEU A 1 224 ? -23.681 26.360  -36.413 1.00 74.93  ? 232 LEU A CB  1 
ATOM 1639 C CG  . LEU A 1 224 ? -22.398 25.540  -36.261 1.00 79.69  ? 232 LEU A CG  1 
ATOM 1640 C CD1 . LEU A 1 224 ? -21.556 25.670  -37.525 1.00 89.19  ? 232 LEU A CD1 1 
ATOM 1641 C CD2 . LEU A 1 224 ? -21.614 25.915  -35.022 1.00 83.66  ? 232 LEU A CD2 1 
ATOM 1642 N N   . SER A 1 225 ? -25.918 28.744  -36.396 1.00 77.71  ? 233 SER A N   1 
ATOM 1643 C CA  . SER A 1 225 ? -27.213 29.046  -36.988 1.00 76.70  ? 233 SER A CA  1 
ATOM 1644 C C   . SER A 1 225 ? -27.294 30.471  -37.523 1.00 80.52  ? 233 SER A C   1 
ATOM 1645 O O   . SER A 1 225 ? -27.540 30.670  -38.717 1.00 80.72  ? 233 SER A O   1 
ATOM 1646 C CB  . SER A 1 225 ? -28.325 28.775  -35.975 1.00 74.31  ? 233 SER A CB  1 
ATOM 1647 O OG  . SER A 1 225 ? -28.133 29.505  -34.788 1.00 79.10  ? 233 SER A OG  1 
ATOM 1648 N N   . LEU A 1 226 ? -27.072 31.479  -36.674 1.00 85.10  ? 234 LEU A N   1 
ATOM 1649 C CA  . LEU A 1 226 ? -27.365 32.847  -37.095 1.00 80.81  ? 234 LEU A CA  1 
ATOM 1650 C C   . LEU A 1 226 ? -26.343 33.341  -38.121 1.00 79.89  ? 234 LEU A C   1 
ATOM 1651 O O   . LEU A 1 226 ? -25.234 32.805  -38.217 1.00 78.91  ? 234 LEU A O   1 
ATOM 1652 C CB  . LEU A 1 226 ? -27.397 33.808  -35.904 1.00 73.93  ? 234 LEU A CB  1 
ATOM 1653 C CG  . LEU A 1 226 ? -28.300 33.580  -34.692 1.00 74.39  ? 234 LEU A CG  1 
ATOM 1654 C CD1 . LEU A 1 226 ? -27.509 33.053  -33.537 1.00 76.83  ? 234 LEU A CD1 1 
ATOM 1655 C CD2 . LEU A 1 226 ? -29.024 34.852  -34.312 1.00 81.12  ? 234 LEU A CD2 1 
ATOM 1656 N N   . PRO A 1 227 ? -26.713 34.345  -38.926 1.00 72.82  ? 235 PRO A N   1 
ATOM 1657 C CA  . PRO A 1 227 ? -25.770 34.895  -39.911 1.00 73.45  ? 235 PRO A CA  1 
ATOM 1658 C C   . PRO A 1 227 ? -24.466 35.340  -39.266 1.00 83.25  ? 235 PRO A C   1 
ATOM 1659 O O   . PRO A 1 227 ? -24.441 35.798  -38.122 1.00 82.70  ? 235 PRO A O   1 
ATOM 1660 C CB  . PRO A 1 227 ? -26.533 36.082  -40.513 1.00 78.16  ? 235 PRO A CB  1 
ATOM 1661 C CG  . PRO A 1 227 ? -27.962 35.775  -40.276 1.00 74.99  ? 235 PRO A CG  1 
ATOM 1662 C CD  . PRO A 1 227 ? -28.018 35.028  -38.982 1.00 71.83  ? 235 PRO A CD  1 
ATOM 1663 N N   . ASN A 1 228 ? -23.373 35.175  -40.009 1.00 86.33  ? 236 ASN A N   1 
ATOM 1664 C CA  . ASN A 1 228 ? -22.046 35.524  -39.518 1.00 85.14  ? 236 ASN A CA  1 
ATOM 1665 C C   . ASN A 1 228 ? -21.999 36.967  -39.033 1.00 86.47  ? 236 ASN A C   1 
ATOM 1666 O O   . ASN A 1 228 ? -22.480 37.881  -39.708 1.00 84.66  ? 236 ASN A O   1 
ATOM 1667 C CB  . ASN A 1 228 ? -21.016 35.301  -40.626 1.00 87.51  ? 236 ASN A CB  1 
ATOM 1668 C CG  . ASN A 1 228 ? -20.886 33.841  -41.007 1.00 92.05  ? 236 ASN A CG  1 
ATOM 1669 O OD1 . ASN A 1 228 ? -20.362 33.033  -40.241 1.00 89.30  ? 236 ASN A OD1 1 
ATOM 1670 N ND2 . ASN A 1 228 ? -21.368 33.494  -42.196 1.00 88.37  ? 236 ASN A ND2 1 
ATOM 1671 N N   . GLY A 1 229 ? -21.416 37.164  -37.850 1.00 89.99  ? 237 GLY A N   1 
ATOM 1672 C CA  . GLY A 1 229 ? -21.315 38.468  -37.240 1.00 89.97  ? 237 GLY A CA  1 
ATOM 1673 C C   . GLY A 1 229 ? -22.492 38.867  -36.375 1.00 91.04  ? 237 GLY A C   1 
ATOM 1674 O O   . GLY A 1 229 ? -22.373 39.816  -35.591 1.00 93.19  ? 237 GLY A O   1 
ATOM 1675 N N   . ALA A 1 230 ? -23.624 38.178  -36.495 1.00 90.59  ? 238 ALA A N   1 
ATOM 1676 C CA  . ALA A 1 230 ? -24.801 38.528  -35.718 1.00 90.51  ? 238 ALA A CA  1 
ATOM 1677 C C   . ALA A 1 230 ? -24.588 38.200  -34.241 1.00 83.61  ? 238 ALA A C   1 
ATOM 1678 O O   . ALA A 1 230 ? -23.603 37.572  -33.843 1.00 77.44  ? 238 ALA A O   1 
ATOM 1679 C CB  . ALA A 1 230 ? -26.036 37.803  -36.252 1.00 87.32  ? 238 ALA A CB  1 
ATOM 1680 N N   . THR A 1 231 ? -25.539 38.637  -33.424 1.00 85.80  ? 239 THR A N   1 
ATOM 1681 C CA  . THR A 1 231 ? -25.492 38.471  -31.981 1.00 86.64  ? 239 THR A CA  1 
ATOM 1682 C C   . THR A 1 231 ? -26.682 37.635  -31.527 1.00 91.96  ? 239 THR A C   1 
ATOM 1683 O O   . THR A 1 231 ? -27.641 37.417  -32.270 1.00 92.55  ? 239 THR A O   1 
ATOM 1684 C CB  . THR A 1 231 ? -25.489 39.829  -31.268 1.00 87.42  ? 239 THR A CB  1 
ATOM 1685 O OG1 . THR A 1 231 ? -25.362 39.629  -29.855 1.00 88.86  ? 239 THR A OG1 1 
ATOM 1686 C CG2 . THR A 1 231 ? -26.778 40.584  -31.559 1.00 83.69  ? 239 THR A CG2 1 
ATOM 1687 N N   . ARG A 1 232 ? -26.600 37.149  -30.287 1.00 85.59  ? 240 ARG A N   1 
ATOM 1688 C CA  . ARG A 1 232 ? -27.677 36.343  -29.724 1.00 85.02  ? 240 ARG A CA  1 
ATOM 1689 C C   . ARG A 1 232 ? -28.988 37.112  -29.611 1.00 87.46  ? 240 ARG A C   1 
ATOM 1690 O O   . ARG A 1 232 ? -30.054 36.489  -29.556 1.00 90.68  ? 240 ARG A O   1 
ATOM 1691 C CB  . ARG A 1 232 ? -27.259 35.811  -28.354 1.00 86.91  ? 240 ARG A CB  1 
ATOM 1692 C CG  . ARG A 1 232 ? -26.202 34.717  -28.406 1.00 85.52  ? 240 ARG A CG  1 
ATOM 1693 C CD  . ARG A 1 232 ? -26.228 33.876  -27.144 1.00 89.77  ? 240 ARG A CD  1 
ATOM 1694 N NE  . ARG A 1 232 ? -25.767 34.644  -25.993 1.00 87.06  ? 240 ARG A NE  1 
ATOM 1695 C CZ  . ARG A 1 232 ? -24.557 34.543  -25.462 1.00 87.13  ? 240 ARG A CZ  1 
ATOM 1696 N NH1 . ARG A 1 232 ? -23.639 33.742  -25.980 1.00 82.60  ? 240 ARG A NH1 1 
ATOM 1697 N NH2 . ARG A 1 232 ? -24.250 35.285  -24.402 1.00 89.96  ? 240 ARG A NH2 1 
ATOM 1698 N N   . ASP A 1 233 ? -28.939 38.442  -29.573 1.00 86.31  ? 241 ASP A N   1 
ATOM 1699 C CA  . ASP A 1 233 ? -30.134 39.273  -29.522 1.00 86.01  ? 241 ASP A CA  1 
ATOM 1700 C C   . ASP A 1 233 ? -30.700 39.598  -30.902 1.00 86.22  ? 241 ASP A C   1 
ATOM 1701 O O   . ASP A 1 233 ? -31.615 40.421  -31.004 1.00 85.55  ? 241 ASP A O   1 
ATOM 1702 C CB  . ASP A 1 233 ? -29.845 40.564  -28.754 1.00 90.05  ? 241 ASP A CB  1 
ATOM 1703 C CG  . ASP A 1 233 ? -29.705 40.332  -27.265 1.00 94.94  ? 241 ASP A CG  1 
ATOM 1704 O OD1 . ASP A 1 233 ? -30.737 40.097  -26.602 1.00 93.79  ? 241 ASP A OD1 1 
ATOM 1705 O OD2 . ASP A 1 233 ? -28.567 40.390  -26.755 1.00 99.51  ? 241 ASP A OD2 1 
ATOM 1706 N N   . HIS A 1 234 ? -30.161 38.992  -31.958 1.00 88.44  ? 242 HIS A N   1 
ATOM 1707 C CA  . HIS A 1 234 ? -30.754 39.081  -33.287 1.00 88.05  ? 242 HIS A CA  1 
ATOM 1708 C C   . HIS A 1 234 ? -32.210 38.629  -33.203 1.00 84.80  ? 242 HIS A C   1 
ATOM 1709 O O   . HIS A 1 234 ? -32.538 37.704  -32.455 1.00 84.62  ? 242 HIS A O   1 
ATOM 1710 C CB  . HIS A 1 234 ? -29.927 38.205  -34.237 1.00 82.30  ? 242 HIS A CB  1 
ATOM 1711 C CG  . HIS A 1 234 ? -30.241 38.365  -35.694 1.00 78.02  ? 242 HIS A CG  1 
ATOM 1712 N ND1 . HIS A 1 234 ? -31.474 38.745  -36.174 1.00 78.93  ? 242 HIS A ND1 1 
ATOM 1713 C CD2 . HIS A 1 234 ? -29.454 38.188  -36.783 1.00 75.46  ? 242 HIS A CD2 1 
ATOM 1714 C CE1 . HIS A 1 234 ? -31.433 38.799  -37.494 1.00 79.77  ? 242 HIS A CE1 1 
ATOM 1715 N NE2 . HIS A 1 234 ? -30.219 38.465  -37.888 1.00 73.28  ? 242 HIS A NE2 1 
ATOM 1716 N N   . HIS A 1 235 ? -33.093 39.288  -33.967 1.00 80.86  ? 243 HIS A N   1 
ATOM 1717 C CA  . HIS A 1 235 ? -34.520 38.972  -33.888 1.00 82.84  ? 243 HIS A CA  1 
ATOM 1718 C C   . HIS A 1 235 ? -34.830 37.513  -34.194 1.00 82.32  ? 243 HIS A C   1 
ATOM 1719 O O   . HIS A 1 235 ? -35.883 37.016  -33.778 1.00 85.64  ? 243 HIS A O   1 
ATOM 1720 C CB  . HIS A 1 235 ? -35.336 39.871  -34.823 1.00 84.69  ? 243 HIS A CB  1 
ATOM 1721 C CG  . HIS A 1 235 ? -34.983 39.738  -36.272 1.00 77.73  ? 243 HIS A CG  1 
ATOM 1722 N ND1 . HIS A 1 235 ? -34.126 40.606  -36.914 1.00 80.54  ? 243 HIS A ND1 1 
ATOM 1723 C CD2 . HIS A 1 235 ? -35.388 38.847  -37.208 1.00 75.96  ? 243 HIS A CD2 1 
ATOM 1724 C CE1 . HIS A 1 235 ? -34.019 40.255  -38.184 1.00 81.62  ? 243 HIS A CE1 1 
ATOM 1725 N NE2 . HIS A 1 235 ? -34.768 39.186  -38.385 1.00 78.63  ? 243 HIS A NE2 1 
ATOM 1726 N N   . MET A 1 236 ? -33.951 36.819  -34.911 1.00 76.61  ? 244 MET A N   1 
ATOM 1727 C CA  . MET A 1 236 ? -34.176 35.421  -35.252 1.00 73.65  ? 244 MET A CA  1 
ATOM 1728 C C   . MET A 1 236 ? -33.856 34.486  -34.092 1.00 76.17  ? 244 MET A C   1 
ATOM 1729 O O   . MET A 1 236 ? -34.172 33.293  -34.169 1.00 79.97  ? 244 MET A O   1 
ATOM 1730 C CB  . MET A 1 236 ? -33.368 35.065  -36.500 1.00 69.92  ? 244 MET A CB  1 
ATOM 1731 C CG  . MET A 1 236 ? -33.857 35.838  -37.719 1.00 71.13  ? 244 MET A CG  1 
ATOM 1732 S SD  . MET A 1 236 ? -33.277 35.216  -39.303 1.00 79.39  ? 244 MET A SD  1 
ATOM 1733 C CE  . MET A 1 236 ? -31.524 35.141  -38.978 1.00 64.36  ? 244 MET A CE  1 
ATOM 1734 N N   . ALA A 1 237 ? -33.248 35.006  -33.027 1.00 80.44  ? 245 ALA A N   1 
ATOM 1735 C CA  . ALA A 1 237 ? -32.993 34.276  -31.792 1.00 80.16  ? 245 ALA A CA  1 
ATOM 1736 C C   . ALA A 1 237 ? -33.750 34.860  -30.609 1.00 80.32  ? 245 ALA A C   1 
ATOM 1737 O O   . ALA A 1 237 ? -34.435 34.120  -29.892 1.00 74.34  ? 245 ALA A O   1 
ATOM 1738 C CB  . ALA A 1 237 ? -31.486 34.257  -31.489 1.00 79.98  ? 245 ALA A CB  1 
ATOM 1739 N N   . ASN A 1 238 ? -33.637 36.170  -30.374 1.00 83.46  ? 246 ASN A N   1 
ATOM 1740 C CA  . ASN A 1 238 ? -34.357 36.833  -29.294 1.00 85.88  ? 246 ASN A CA  1 
ATOM 1741 C C   . ASN A 1 238 ? -35.598 37.515  -29.847 1.00 90.17  ? 246 ASN A C   1 
ATOM 1742 O O   . ASN A 1 238 ? -35.475 38.381  -30.729 1.00 93.68  ? 246 ASN A O   1 
ATOM 1743 C CB  . ASN A 1 238 ? -33.457 37.858  -28.611 1.00 90.63  ? 246 ASN A CB  1 
ATOM 1744 C CG  . ASN A 1 238 ? -34.118 38.518  -27.415 1.00 85.82  ? 246 ASN A CG  1 
ATOM 1745 O OD1 . ASN A 1 238 ? -35.218 38.146  -27.011 1.00 85.41  ? 246 ASN A OD1 1 
ATOM 1746 N ND2 . ASN A 1 238 ? -33.448 39.516  -26.849 1.00 86.44  ? 246 ASN A ND2 1 
ATOM 1747 N N   . PRO A 1 239 ? -36.801 37.168  -29.377 1.00 84.70  ? 247 PRO A N   1 
ATOM 1748 C CA  . PRO A 1 239 ? -38.003 37.910  -29.793 1.00 85.35  ? 247 PRO A CA  1 
ATOM 1749 C C   . PRO A 1 239 ? -38.143 39.282  -29.155 1.00 86.05  ? 247 PRO A C   1 
ATOM 1750 O O   . PRO A 1 239 ? -39.013 40.051  -29.585 1.00 90.08  ? 247 PRO A O   1 
ATOM 1751 C CB  . PRO A 1 239 ? -39.157 36.993  -29.352 1.00 80.19  ? 247 PRO A CB  1 
ATOM 1752 C CG  . PRO A 1 239 ? -38.524 35.683  -29.005 1.00 76.55  ? 247 PRO A CG  1 
ATOM 1753 C CD  . PRO A 1 239 ? -37.142 36.006  -28.544 1.00 79.44  ? 247 PRO A CD  1 
ATOM 1754 N N   . PHE A 1 240 ? -37.334 39.618  -28.153 1.00 85.05  ? 248 PHE A N   1 
ATOM 1755 C CA  . PHE A 1 240 ? -37.459 40.884  -27.432 1.00 91.84  ? 248 PHE A CA  1 
ATOM 1756 C C   . PHE A 1 240 ? -36.176 41.698  -27.565 1.00 95.73  ? 248 PHE A C   1 
ATOM 1757 O O   . PHE A 1 240 ? -35.294 41.650  -26.706 1.00 97.05  ? 248 PHE A O   1 
ATOM 1758 C CB  . PHE A 1 240 ? -37.829 40.630  -25.955 1.00 92.09  ? 248 PHE A CB  1 
ATOM 1759 C CG  . PHE A 1 240 ? -39.133 39.905  -25.777 1.00 93.66  ? 248 PHE A CG  1 
ATOM 1760 C CD1 . PHE A 1 240 ? -40.250 40.291  -26.499 1.00 94.27  ? 248 PHE A CD1 1 
ATOM 1761 C CD2 . PHE A 1 240 ? -39.245 38.840  -24.898 1.00 88.46  ? 248 PHE A CD2 1 
ATOM 1762 C CE1 . PHE A 1 240 ? -41.456 39.636  -26.345 1.00 89.66  ? 248 PHE A CE1 1 
ATOM 1763 C CE2 . PHE A 1 240 ? -40.451 38.178  -24.742 1.00 86.67  ? 248 PHE A CE2 1 
ATOM 1764 C CZ  . PHE A 1 240 ? -41.557 38.578  -25.469 1.00 89.96  ? 248 PHE A CZ  1 
ATOM 1765 N N   . GLY A 1 241 ? -36.084 42.451  -28.659 1.00 100.34 ? 249 GLY A N   1 
ATOM 1766 C CA  . GLY A 1 241 ? -35.087 43.483  -28.809 1.00 97.15  ? 249 GLY A CA  1 
ATOM 1767 C C   . GLY A 1 241 ? -33.681 42.999  -29.091 1.00 95.93  ? 249 GLY A C   1 
ATOM 1768 O O   . GLY A 1 241 ? -33.349 41.820  -28.929 1.00 96.29  ? 249 GLY A O   1 
ATOM 1769 N N   . PRO A 1 242 ? -32.816 43.927  -29.526 1.00 90.16  ? 250 PRO A N   1 
ATOM 1770 C CA  . PRO A 1 242 ? -33.126 45.310  -29.934 1.00 80.90  ? 250 PRO A CA  1 
ATOM 1771 C C   . PRO A 1 242 ? -33.890 45.407  -31.258 1.00 83.85  ? 250 PRO A C   1 
ATOM 1772 O O   . PRO A 1 242 ? -34.827 46.188  -31.396 1.00 81.79  ? 250 PRO A O   1 
ATOM 1773 C CB  . PRO A 1 242 ? -31.739 45.959  -30.032 1.00 87.05  ? 250 PRO A CB  1 
ATOM 1774 C CG  . PRO A 1 242 ? -30.800 44.829  -30.322 1.00 85.44  ? 250 PRO A CG  1 
ATOM 1775 C CD  . PRO A 1 242 ? -31.374 43.635  -29.605 1.00 92.24  ? 250 PRO A CD  1 
ATOM 1776 N N   . THR A 1 243 ? -33.499 44.600  -32.246 1.00 84.35  ? 251 THR A N   1 
ATOM 1777 C CA  . THR A 1 243 ? -34.044 44.695  -33.597 1.00 83.60  ? 251 THR A CA  1 
ATOM 1778 C C   . THR A 1 243 ? -35.411 44.038  -33.758 1.00 84.30  ? 251 THR A C   1 
ATOM 1779 O O   . THR A 1 243 ? -36.094 44.308  -34.752 1.00 84.99  ? 251 THR A O   1 
ATOM 1780 C CB  . THR A 1 243 ? -33.056 44.089  -34.598 1.00 89.74  ? 251 THR A CB  1 
ATOM 1781 O OG1 . THR A 1 243 ? -33.474 44.392  -35.934 1.00 98.51  ? 251 THR A OG1 1 
ATOM 1782 C CG2 . THR A 1 243 ? -32.959 42.582  -34.419 1.00 87.10  ? 251 THR A CG2 1 
ATOM 1783 N N   . SER A 1 244 ? -35.821 43.184  -32.823 1.00 84.12  ? 252 SER A N   1 
ATOM 1784 C CA  . SER A 1 244 ? -37.068 42.448  -32.964 1.00 85.84  ? 252 SER A CA  1 
ATOM 1785 C C   . SER A 1 244 ? -38.275 43.388  -32.893 1.00 84.26  ? 252 SER A C   1 
ATOM 1786 O O   . SER A 1 244 ? -38.183 44.496  -32.360 1.00 80.50  ? 252 SER A O   1 
ATOM 1787 C CB  . SER A 1 244 ? -37.160 41.370  -31.885 1.00 89.25  ? 252 SER A CB  1 
ATOM 1788 O OG  . SER A 1 244 ? -37.318 41.941  -30.600 1.00 97.05  ? 252 SER A OG  1 
ATOM 1789 N N   . PRO A 1 245 ? -39.434 42.959  -33.436 1.00 85.50  ? 253 PRO A N   1 
ATOM 1790 C CA  . PRO A 1 245 ? -40.606 43.850  -33.503 1.00 86.94  ? 253 PRO A CA  1 
ATOM 1791 C C   . PRO A 1 245 ? -41.215 44.180  -32.145 1.00 93.74  ? 253 PRO A C   1 
ATOM 1792 O O   . PRO A 1 245 ? -40.743 43.704  -31.107 1.00 92.78  ? 253 PRO A O   1 
ATOM 1793 C CB  . PRO A 1 245 ? -41.594 43.070  -34.383 1.00 85.95  ? 253 PRO A CB  1 
ATOM 1794 C CG  . PRO A 1 245 ? -40.770 42.050  -35.100 1.00 86.93  ? 253 PRO A CG  1 
ATOM 1795 C CD  . PRO A 1 245 ? -39.664 41.699  -34.163 1.00 89.56  ? 253 PRO A CD  1 
ATOM 1796 N N   . THR A 1 246 ? -42.263 45.010  -32.149 1.00 96.31  ? 254 THR A N   1 
ATOM 1797 C CA  . THR A 1 246 ? -42.891 45.441  -30.902 1.00 101.61 ? 254 THR A CA  1 
ATOM 1798 C C   . THR A 1 246 ? -43.736 44.334  -30.280 1.00 104.89 ? 254 THR A C   1 
ATOM 1799 O O   . THR A 1 246 ? -43.808 44.225  -29.051 1.00 107.79 ? 254 THR A O   1 
ATOM 1800 C CB  . THR A 1 246 ? -43.754 46.677  -31.162 1.00 95.54  ? 254 THR A CB  1 
ATOM 1801 O OG1 . THR A 1 246 ? -44.687 46.394  -32.213 1.00 94.99  ? 254 THR A OG1 1 
ATOM 1802 C CG2 . THR A 1 246 ? -42.886 47.847  -31.588 1.00 90.10  ? 254 THR A CG2 1 
ATOM 1803 N N   . LEU A 1 247 ? -44.390 43.520  -31.112 1.00 98.79  ? 255 LEU A N   1 
ATOM 1804 C CA  . LEU A 1 247 ? -45.290 42.436  -30.721 1.00 96.57  ? 255 LEU A CA  1 
ATOM 1805 C C   . LEU A 1 247 ? -46.616 42.956  -30.171 1.00 96.76  ? 255 LEU A C   1 
ATOM 1806 O O   . LEU A 1 247 ? -47.670 42.424  -30.530 1.00 92.91  ? 255 LEU A O   1 
ATOM 1807 C CB  . LEU A 1 247 ? -44.590 41.507  -29.724 1.00 99.08  ? 255 LEU A CB  1 
ATOM 1808 C CG  . LEU A 1 247 ? -43.296 40.881  -30.252 1.00 94.62  ? 255 LEU A CG  1 
ATOM 1809 C CD1 . LEU A 1 247 ? -42.124 41.264  -29.357 1.00 93.77  ? 255 LEU A CD1 1 
ATOM 1810 C CD2 . LEU A 1 247 ? -43.403 39.365  -30.364 1.00 90.88  ? 255 LEU A CD2 1 
ATOM 1811 N N   . GLU A 1 248 ? -46.595 44.002  -29.339 1.00 97.76  ? 256 GLU A N   1 
ATOM 1812 C CA  . GLU A 1 248 ? -47.851 44.603  -28.901 1.00 95.42  ? 256 GLU A CA  1 
ATOM 1813 C C   . GLU A 1 248 ? -48.741 44.955  -30.086 1.00 99.17  ? 256 GLU A C   1 
ATOM 1814 O O   . GLU A 1 248 ? -49.911 44.557  -30.126 1.00 100.29 ? 256 GLU A O   1 
ATOM 1815 C CB  . GLU A 1 248 ? -47.590 45.844  -28.049 1.00 93.85  ? 256 GLU A CB  1 
ATOM 1816 C CG  . GLU A 1 248 ? -46.936 45.568  -26.719 1.00 98.30  ? 256 GLU A CG  1 
ATOM 1817 C CD  . GLU A 1 248 ? -46.616 46.799  -25.913 1.00 107.51 ? 256 GLU A CD  1 
ATOM 1818 O OE1 . GLU A 1 248 ? -46.725 47.920  -26.451 1.00 106.68 ? 256 GLU A OE1 1 
ATOM 1819 O OE2 . GLU A 1 248 ? -46.276 46.639  -24.721 1.00 111.85 ? 256 GLU A OE2 1 
ATOM 1820 N N   . SER A 1 249 ? -48.190 45.664  -31.077 1.00 95.22  ? 257 SER A N   1 
ATOM 1821 C CA  . SER A 1 249 ? -48.978 46.100  -32.230 1.00 92.89  ? 257 SER A CA  1 
ATOM 1822 C C   . SER A 1 249 ? -49.622 44.922  -32.958 1.00 95.10  ? 257 SER A C   1 
ATOM 1823 O O   . SER A 1 249 ? -50.850 44.840  -33.075 1.00 92.77  ? 257 SER A O   1 
ATOM 1824 C CB  . SER A 1 249 ? -48.097 46.905  -33.190 1.00 92.57  ? 257 SER A CB  1 
ATOM 1825 O OG  . SER A 1 249 ? -47.147 46.071  -33.826 1.00 93.90  ? 257 SER A OG  1 
ATOM 1826 N N   . ILE A 1 250 ? -48.799 44.019  -33.496 1.00 101.01 ? 258 ILE A N   1 
ATOM 1827 C CA  . ILE A 1 250 ? -49.324 42.868  -34.222 1.00 94.98  ? 258 ILE A CA  1 
ATOM 1828 C C   . ILE A 1 250 ? -50.184 42.010  -33.304 1.00 89.18  ? 258 ILE A C   1 
ATOM 1829 O O   . ILE A 1 250 ? -49.825 41.740  -32.150 1.00 79.62  ? 258 ILE A O   1 
ATOM 1830 C CB  . ILE A 1 250 ? -48.177 42.055  -34.846 1.00 85.85  ? 258 ILE A CB  1 
ATOM 1831 C CG1 . ILE A 1 250 ? -47.080 41.799  -33.813 1.00 80.86  ? 258 ILE A CG1 1 
ATOM 1832 C CG2 . ILE A 1 250 ? -47.607 42.780  -36.053 1.00 94.53  ? 258 ILE A CG2 1 
ATOM 1833 C CD1 . ILE A 1 250 ? -45.867 41.090  -34.369 1.00 90.72  ? 258 ILE A CD1 1 
ATOM 1834 N N   . SER A 1 251 ? -51.341 41.592  -33.810 1.00 87.84  ? 259 SER A N   1 
ATOM 1835 C CA  . SER A 1 251 ? -52.194 40.666  -33.078 1.00 88.30  ? 259 SER A CA  1 
ATOM 1836 C C   . SER A 1 251 ? -51.706 39.240  -33.302 1.00 80.41  ? 259 SER A C   1 
ATOM 1837 O O   . SER A 1 251 ? -51.508 38.815  -34.444 1.00 88.82  ? 259 SER A O   1 
ATOM 1838 C CB  . SER A 1 251 ? -53.652 40.807  -33.516 1.00 90.71  ? 259 SER A CB  1 
ATOM 1839 O OG  . SER A 1 251 ? -54.074 42.157  -33.449 1.00 92.35  ? 259 SER A OG  1 
ATOM 1840 N N   . LEU A 1 252 ? -51.506 38.506  -32.210 1.00 69.08  ? 260 LEU A N   1 
ATOM 1841 C CA  . LEU A 1 252 ? -51.010 37.138  -32.254 1.00 67.03  ? 260 LEU A CA  1 
ATOM 1842 C C   . LEU A 1 252 ? -52.125 36.152  -31.932 1.00 74.99  ? 260 LEU A C   1 
ATOM 1843 O O   . LEU A 1 252 ? -53.119 36.486  -31.280 1.00 77.52  ? 260 LEU A O   1 
ATOM 1844 C CB  . LEU A 1 252 ? -49.839 36.945  -31.284 1.00 61.15  ? 260 LEU A CB  1 
ATOM 1845 C CG  . LEU A 1 252 ? -48.483 37.450  -31.783 1.00 59.09  ? 260 LEU A CG  1 
ATOM 1846 C CD1 . LEU A 1 252 ? -47.350 36.852  -30.964 1.00 72.83  ? 260 LEU A CD1 1 
ATOM 1847 C CD2 . LEU A 1 252 ? -48.303 37.137  -33.262 1.00 69.02  ? 260 LEU A CD2 1 
ATOM 1848 N N   . GLU A 1 253 ? -51.941 34.923  -32.404 1.00 74.57  ? 261 GLU A N   1 
ATOM 1849 C CA  . GLU A 1 253 ? -52.857 33.831  -32.127 1.00 71.04  ? 261 GLU A CA  1 
ATOM 1850 C C   . GLU A 1 253 ? -52.584 33.225  -30.752 1.00 72.22  ? 261 GLU A C   1 
ATOM 1851 O O   . GLU A 1 253 ? -51.487 33.368  -30.206 1.00 65.45  ? 261 GLU A O   1 
ATOM 1852 C CB  . GLU A 1 253 ? -52.725 32.764  -33.212 1.00 71.43  ? 261 GLU A CB  1 
ATOM 1853 C CG  . GLU A 1 253 ? -52.946 33.259  -34.645 1.00 75.02  ? 261 GLU A CG  1 
ATOM 1854 C CD  . GLU A 1 253 ? -54.363 33.746  -34.911 1.00 84.69  ? 261 GLU A CD  1 
ATOM 1855 O OE1 . GLU A 1 253 ? -54.775 34.775  -34.333 1.00 87.18  ? 261 GLU A OE1 1 
ATOM 1856 O OE2 . GLU A 1 253 ? -55.071 33.091  -35.705 1.00 81.71  ? 261 GLU A OE2 1 
ATOM 1857 N N   . PRO A 1 254 ? -53.580 32.562  -30.158 1.00 69.73  ? 262 PRO A N   1 
ATOM 1858 C CA  . PRO A 1 254 ? -53.367 31.927  -28.849 1.00 67.21  ? 262 PRO A CA  1 
ATOM 1859 C C   . PRO A 1 254 ? -52.269 30.873  -28.906 1.00 65.44  ? 262 PRO A C   1 
ATOM 1860 O O   . PRO A 1 254 ? -52.174 30.093  -29.856 1.00 69.01  ? 262 PRO A O   1 
ATOM 1861 C CB  . PRO A 1 254 ? -54.733 31.311  -28.525 1.00 75.40  ? 262 PRO A CB  1 
ATOM 1862 C CG  . PRO A 1 254 ? -55.702 32.089  -29.359 1.00 70.03  ? 262 PRO A CG  1 
ATOM 1863 C CD  . PRO A 1 254 ? -54.969 32.409  -30.619 1.00 64.53  ? 262 PRO A CD  1 
ATOM 1864 N N   . MET A 1 255 ? -51.434 30.857  -27.868 1.00 64.64  ? 263 MET A N   1 
ATOM 1865 C CA  . MET A 1 255 ? -50.234 30.033  -27.845 1.00 59.55  ? 263 MET A CA  1 
ATOM 1866 C C   . MET A 1 255 ? -50.207 29.165  -26.592 1.00 62.97  ? 263 MET A C   1 
ATOM 1867 O O   . MET A 1 255 ? -50.961 29.391  -25.642 1.00 68.78  ? 263 MET A O   1 
ATOM 1868 C CB  . MET A 1 255 ? -48.988 30.919  -27.905 1.00 59.02  ? 263 MET A CB  1 
ATOM 1869 C CG  . MET A 1 255 ? -48.930 31.758  -29.166 1.00 62.92  ? 263 MET A CG  1 
ATOM 1870 S SD  . MET A 1 255 ? -47.489 32.827  -29.258 1.00 67.29  ? 263 MET A SD  1 
ATOM 1871 C CE  . MET A 1 255 ? -46.259 31.624  -29.717 1.00 61.12  ? 263 MET A CE  1 
ATOM 1872 N N   . LEU A 1 256 ? -49.332 28.156  -26.603 1.00 63.95  ? 264 LEU A N   1 
ATOM 1873 C CA  . LEU A 1 256 ? -49.136 27.287  -25.447 1.00 63.96  ? 264 LEU A CA  1 
ATOM 1874 C C   . LEU A 1 256 ? -47.654 26.943  -25.363 1.00 56.23  ? 264 LEU A C   1 
ATOM 1875 O O   . LEU A 1 256 ? -47.092 26.389  -26.313 1.00 65.07  ? 264 LEU A O   1 
ATOM 1876 C CB  . LEU A 1 256 ? -49.989 26.016  -25.551 1.00 62.17  ? 264 LEU A CB  1 
ATOM 1877 C CG  . LEU A 1 256 ? -50.196 25.114  -24.323 1.00 61.47  ? 264 LEU A CG  1 
ATOM 1878 C CD1 . LEU A 1 256 ? -51.172 23.998  -24.649 1.00 64.83  ? 264 LEU A CD1 1 
ATOM 1879 C CD2 . LEU A 1 256 ? -48.928 24.534  -23.721 1.00 55.00  ? 264 LEU A CD2 1 
ATOM 1880 N N   . VAL A 1 257 ? -47.023 27.281  -24.240 1.00 50.19  ? 265 VAL A N   1 
ATOM 1881 C CA  . VAL A 1 257 ? -45.607 27.008  -24.003 1.00 55.81  ? 265 VAL A CA  1 
ATOM 1882 C C   . VAL A 1 257 ? -45.471 25.868  -22.999 1.00 57.64  ? 265 VAL A C   1 
ATOM 1883 O O   . VAL A 1 257 ? -46.072 25.911  -21.918 1.00 60.11  ? 265 VAL A O   1 
ATOM 1884 C CB  . VAL A 1 257 ? -44.871 28.265  -23.505 1.00 59.83  ? 265 VAL A CB  1 
ATOM 1885 C CG1 . VAL A 1 257 ? -43.379 27.987  -23.350 1.00 55.37  ? 265 VAL A CG1 1 
ATOM 1886 C CG2 . VAL A 1 257 ? -45.107 29.430  -24.454 1.00 60.44  ? 265 VAL A CG2 1 
ATOM 1887 N N   . ILE A 1 258 ? -44.681 24.852  -23.354 1.00 63.49  ? 266 ILE A N   1 
ATOM 1888 C CA  . ILE A 1 258 ? -44.378 23.722  -22.478 1.00 59.90  ? 266 ILE A CA  1 
ATOM 1889 C C   . ILE A 1 258 ? -42.870 23.664  -22.276 1.00 64.84  ? 266 ILE A C   1 
ATOM 1890 O O   . ILE A 1 258 ? -42.112 23.631  -23.253 1.00 70.33  ? 266 ILE A O   1 
ATOM 1891 C CB  . ILE A 1 258 ? -44.884 22.383  -23.053 1.00 57.37  ? 266 ILE A CB  1 
ATOM 1892 C CG1 . ILE A 1 258 ? -46.405 22.283  -22.985 1.00 58.86  ? 266 ILE A CG1 1 
ATOM 1893 C CG2 . ILE A 1 258 ? -44.243 21.205  -22.323 1.00 63.01  ? 266 ILE A CG2 1 
ATOM 1894 C CD1 . ILE A 1 258 ? -47.012 21.555  -24.170 1.00 59.37  ? 266 ILE A CD1 1 
ATOM 1895 N N   . VAL A 1 259 ? -42.436 23.643  -21.012 1.00 68.25  ? 267 VAL A N   1 
ATOM 1896 C CA  . VAL A 1 259 ? -41.018 23.624  -20.662 1.00 73.47  ? 267 VAL A CA  1 
ATOM 1897 C C   . VAL A 1 259 ? -40.816 22.696  -19.470 1.00 72.45  ? 267 VAL A C   1 
ATOM 1898 O O   . VAL A 1 259 ? -41.697 22.547  -18.617 1.00 71.23  ? 267 VAL A O   1 
ATOM 1899 C CB  . VAL A 1 259 ? -40.475 25.038  -20.336 1.00 77.91  ? 267 VAL A CB  1 
ATOM 1900 C CG1 . VAL A 1 259 ? -38.960 25.018  -20.144 1.00 79.19  ? 267 VAL A CG1 1 
ATOM 1901 C CG2 . VAL A 1 259 ? -40.846 26.021  -21.419 1.00 80.52  ? 267 VAL A CG2 1 
ATOM 1902 N N   . GLY A 1 260 ? -39.637 22.079  -19.411 1.00 78.13  ? 268 GLY A N   1 
ATOM 1903 C CA  . GLY A 1 260 ? -39.253 21.267  -18.268 1.00 81.69  ? 268 GLY A CA  1 
ATOM 1904 C C   . GLY A 1 260 ? -38.629 22.116  -17.171 1.00 80.87  ? 268 GLY A C   1 
ATOM 1905 O O   . GLY A 1 260 ? -37.922 23.084  -17.443 1.00 79.13  ? 268 GLY A O   1 
ATOM 1906 N N   . GLY A 1 261 ? -38.927 21.748  -15.922 1.00 78.94  ? 269 GLY A N   1 
ATOM 1907 C CA  . GLY A 1 261 ? -38.419 22.501  -14.782 1.00 79.88  ? 269 GLY A CA  1 
ATOM 1908 C C   . GLY A 1 261 ? -36.914 22.694  -14.793 1.00 84.52  ? 269 GLY A C   1 
ATOM 1909 O O   . GLY A 1 261 ? -36.417 23.783  -14.493 1.00 85.43  ? 269 GLY A O   1 
ATOM 1910 N N   . SER A 1 262 ? -36.167 21.643  -15.134 1.00 83.18  ? 270 SER A N   1 
ATOM 1911 C CA  . SER A 1 262 ? -34.709 21.691  -15.099 1.00 79.25  ? 270 SER A CA  1 
ATOM 1912 C C   . SER A 1 262 ? -34.088 22.270  -16.364 1.00 81.21  ? 270 SER A C   1 
ATOM 1913 O O   . SER A 1 262 ? -32.856 22.348  -16.442 1.00 85.90  ? 270 SER A O   1 
ATOM 1914 C CB  . SER A 1 262 ? -34.138 20.292  -14.852 1.00 77.42  ? 270 SER A CB  1 
ATOM 1915 O OG  . SER A 1 262 ? -34.669 19.724  -13.668 1.00 70.30  ? 270 SER A OG  1 
ATOM 1916 N N   . GLU A 1 263 ? -34.892 22.662  -17.349 1.00 80.37  ? 271 GLU A N   1 
ATOM 1917 C CA  . GLU A 1 263 ? -34.356 23.163  -18.608 1.00 79.65  ? 271 GLU A CA  1 
ATOM 1918 C C   . GLU A 1 263 ? -33.536 24.431  -18.392 1.00 79.70  ? 271 GLU A C   1 
ATOM 1919 O O   . GLU A 1 263 ? -33.817 25.237  -17.501 1.00 87.18  ? 271 GLU A O   1 
ATOM 1920 C CB  . GLU A 1 263 ? -35.490 23.443  -19.592 1.00 78.32  ? 271 GLU A CB  1 
ATOM 1921 C CG  . GLU A 1 263 ? -36.064 22.204  -20.248 1.00 80.15  ? 271 GLU A CG  1 
ATOM 1922 C CD  . GLU A 1 263 ? -36.733 22.509  -21.572 1.00 82.80  ? 271 GLU A CD  1 
ATOM 1923 O OE1 . GLU A 1 263 ? -36.029 22.938  -22.510 1.00 81.05  ? 271 GLU A OE1 1 
ATOM 1924 O OE2 . GLU A 1 263 ? -37.962 22.316  -21.677 1.00 87.06  ? 271 GLU A OE2 1 
ATOM 1925 N N   . LEU A 1 264 ? -32.510 24.607  -19.231 1.00 75.57  ? 272 LEU A N   1 
ATOM 1926 C CA  . LEU A 1 264 ? -31.749 25.852  -19.225 1.00 82.86  ? 272 LEU A CA  1 
ATOM 1927 C C   . LEU A 1 264 ? -32.519 26.990  -19.875 1.00 78.06  ? 272 LEU A C   1 
ATOM 1928 O O   . LEU A 1 264 ? -32.197 28.160  -19.636 1.00 82.43  ? 272 LEU A O   1 
ATOM 1929 C CB  . LEU A 1 264 ? -30.409 25.696  -19.951 1.00 86.38  ? 272 LEU A CB  1 
ATOM 1930 C CG  . LEU A 1 264 ? -29.330 24.723  -19.469 1.00 90.05  ? 272 LEU A CG  1 
ATOM 1931 C CD1 . LEU A 1 264 ? -29.692 23.297  -19.812 1.00 93.09  ? 272 LEU A CD1 1 
ATOM 1932 C CD2 . LEU A 1 264 ? -27.975 25.092  -20.055 1.00 89.36  ? 272 LEU A CD2 1 
ATOM 1933 N N   . LEU A 1 265 ? -33.513 26.672  -20.703 1.00 69.80  ? 273 LEU A N   1 
ATOM 1934 C CA  . LEU A 1 265 ? -34.395 27.662  -21.303 1.00 68.99  ? 273 LEU A CA  1 
ATOM 1935 C C   . LEU A 1 265 ? -35.724 27.752  -20.569 1.00 73.07  ? 273 LEU A C   1 
ATOM 1936 O O   . LEU A 1 265 ? -36.728 28.175  -21.151 1.00 71.99  ? 273 LEU A O   1 
ATOM 1937 C CB  . LEU A 1 265 ? -34.603 27.364  -22.788 1.00 73.39  ? 273 LEU A CB  1 
ATOM 1938 C CG  . LEU A 1 265 ? -33.487 27.796  -23.748 1.00 74.46  ? 273 LEU A CG  1 
ATOM 1939 C CD1 . LEU A 1 265 ? -32.116 27.294  -23.350 1.00 75.47  ? 273 LEU A CD1 1 
ATOM 1940 C CD2 . LEU A 1 265 ? -33.805 27.329  -25.159 1.00 76.66  ? 273 LEU A CD2 1 
ATOM 1941 N N   . ARG A 1 266 ? -35.736 27.363  -19.293 1.00 75.24  ? 274 ARG A N   1 
ATOM 1942 C CA  . ARG A 1 266 ? -36.920 27.521  -18.458 1.00 81.60  ? 274 ARG A CA  1 
ATOM 1943 C C   . ARG A 1 266 ? -37.298 28.990  -18.333 1.00 85.68  ? 274 ARG A C   1 
ATOM 1944 O O   . ARG A 1 266 ? -38.424 29.390  -18.650 1.00 79.54  ? 274 ARG A O   1 
ATOM 1945 C CB  . ARG A 1 266 ? -36.663 26.918  -17.077 1.00 86.33  ? 274 ARG A CB  1 
ATOM 1946 C CG  . ARG A 1 266 ? -37.771 27.184  -16.094 1.00 89.36  ? 274 ARG A CG  1 
ATOM 1947 C CD  . ARG A 1 266 ? -37.282 27.294  -14.662 1.00 89.96  ? 274 ARG A CD  1 
ATOM 1948 N NE  . ARG A 1 266 ? -38.380 27.626  -13.760 1.00 87.99  ? 274 ARG A NE  1 
ATOM 1949 C CZ  . ARG A 1 266 ? -38.645 28.847  -13.311 1.00 84.35  ? 274 ARG A CZ  1 
ATOM 1950 N NH1 . ARG A 1 266 ? -37.940 29.897  -13.702 1.00 78.97  ? 274 ARG A NH1 1 
ATOM 1951 N NH2 . ARG A 1 266 ? -39.663 29.023  -12.474 1.00 81.16  ? 274 ARG A NH2 1 
ATOM 1952 N N   . ASP A 1 267 ? -36.366 29.803  -17.837 1.00 88.53  ? 275 ASP A N   1 
ATOM 1953 C CA  . ASP A 1 267 ? -36.645 31.217  -17.626 1.00 86.43  ? 275 ASP A CA  1 
ATOM 1954 C C   . ASP A 1 267 ? -36.864 31.942  -18.946 1.00 77.00  ? 275 ASP A C   1 
ATOM 1955 O O   . ASP A 1 267 ? -37.698 32.851  -19.028 1.00 72.55  ? 275 ASP A O   1 
ATOM 1956 C CB  . ASP A 1 267 ? -35.495 31.855  -16.853 1.00 89.48  ? 275 ASP A CB  1 
ATOM 1957 C CG  . ASP A 1 267 ? -35.113 31.060  -15.624 1.00 91.80  ? 275 ASP A CG  1 
ATOM 1958 O OD1 . ASP A 1 267 ? -35.942 30.255  -15.154 1.00 90.49  ? 275 ASP A OD1 1 
ATOM 1959 O OD2 . ASP A 1 267 ? -33.977 31.231  -15.138 1.00 90.32  ? 275 ASP A OD2 1 
ATOM 1960 N N   . ARG A 1 268 ? -36.120 31.558  -19.987 1.00 74.25  ? 276 ARG A N   1 
ATOM 1961 C CA  . ARG A 1 268 ? -36.306 32.157  -21.307 1.00 72.68  ? 276 ARG A CA  1 
ATOM 1962 C C   . ARG A 1 268 ? -37.751 32.047  -21.769 1.00 71.80  ? 276 ARG A C   1 
ATOM 1963 O O   . ARG A 1 268 ? -38.377 33.046  -22.141 1.00 69.95  ? 276 ARG A O   1 
ATOM 1964 C CB  . ARG A 1 268 ? -35.381 31.487  -22.321 1.00 80.03  ? 276 ARG A CB  1 
ATOM 1965 C CG  . ARG A 1 268 ? -33.967 32.007  -22.305 1.00 80.45  ? 276 ARG A CG  1 
ATOM 1966 C CD  . ARG A 1 268 ? -33.840 33.373  -22.957 1.00 73.72  ? 276 ARG A CD  1 
ATOM 1967 N NE  . ARG A 1 268 ? -32.456 33.650  -23.319 1.00 81.74  ? 276 ARG A NE  1 
ATOM 1968 C CZ  . ARG A 1 268 ? -31.771 34.712  -22.919 1.00 90.88  ? 276 ARG A CZ  1 
ATOM 1969 N NH1 . ARG A 1 268 ? -32.297 35.605  -22.096 1.00 95.25  ? 276 ARG A NH1 1 
ATOM 1970 N NH2 . ARG A 1 268 ? -30.516 34.868  -23.330 1.00 92.33  ? 276 ARG A NH2 1 
ATOM 1971 N N   . ALA A 1 269 ? -38.301 30.832  -21.745 1.00 74.78  ? 277 ALA A N   1 
ATOM 1972 C CA  . ALA A 1 269 ? -39.682 30.646  -22.168 1.00 75.32  ? 277 ALA A CA  1 
ATOM 1973 C C   . ALA A 1 269 ? -40.665 31.198  -21.145 1.00 81.00  ? 277 ALA A C   1 
ATOM 1974 O O   . ALA A 1 269 ? -41.764 31.626  -21.516 1.00 79.98  ? 277 ALA A O   1 
ATOM 1975 C CB  . ALA A 1 269 ? -39.956 29.170  -22.439 1.00 71.63  ? 277 ALA A CB  1 
ATOM 1976 N N   . LYS A 1 270 ? -40.304 31.188  -19.859 1.00 84.26  ? 278 LYS A N   1 
ATOM 1977 C CA  . LYS A 1 270 ? -41.152 31.840  -18.867 1.00 83.51  ? 278 LYS A CA  1 
ATOM 1978 C C   . LYS A 1 270 ? -41.138 33.350  -19.059 1.00 85.36  ? 278 LYS A C   1 
ATOM 1979 O O   . LYS A 1 270 ? -42.197 33.983  -19.135 1.00 87.03  ? 278 LYS A O   1 
ATOM 1980 C CB  . LYS A 1 270 ? -40.713 31.466  -17.451 1.00 79.21  ? 278 LYS A CB  1 
ATOM 1981 C CG  . LYS A 1 270 ? -41.813 31.657  -16.417 1.00 81.10  ? 278 LYS A CG  1 
ATOM 1982 C CD  . LYS A 1 270 ? -41.360 31.265  -15.023 1.00 83.11  ? 278 LYS A CD  1 
ATOM 1983 C CE  . LYS A 1 270 ? -42.333 31.778  -13.973 1.00 75.36  ? 278 LYS A CE  1 
ATOM 1984 N NZ  . LYS A 1 270 ? -43.519 30.890  -13.817 1.00 69.72  ? 278 LYS A NZ  1 
ATOM 1985 N N   . GLU A 1 271 ? -39.943 33.948  -19.129 1.00 77.16  ? 279 GLU A N   1 
ATOM 1986 C CA  . GLU A 1 271 ? -39.839 35.370  -19.450 1.00 70.21  ? 279 GLU A CA  1 
ATOM 1987 C C   . GLU A 1 271 ? -40.599 35.693  -20.725 1.00 74.15  ? 279 GLU A C   1 
ATOM 1988 O O   . GLU A 1 271 ? -41.287 36.717  -20.810 1.00 80.32  ? 279 GLU A O   1 
ATOM 1989 C CB  . GLU A 1 271 ? -38.375 35.782  -19.602 1.00 74.63  ? 279 GLU A CB  1 
ATOM 1990 C CG  . GLU A 1 271 ? -38.170 37.265  -19.859 1.00 89.91  ? 279 GLU A CG  1 
ATOM 1991 C CD  . GLU A 1 271 ? -36.706 37.653  -19.873 1.00 100.51 ? 279 GLU A CD  1 
ATOM 1992 O OE1 . GLU A 1 271 ? -35.855 36.741  -19.898 1.00 94.24  ? 279 GLU A OE1 1 
ATOM 1993 O OE2 . GLU A 1 271 ? -36.404 38.866  -19.871 1.00 114.31 ? 279 GLU A OE2 1 
ATOM 1994 N N   . TYR A 1 272 ? -40.470 34.833  -21.734 1.00 75.21  ? 280 TYR A N   1 
ATOM 1995 C CA  . TYR A 1 272 ? -41.232 34.957  -22.967 1.00 75.97  ? 280 TYR A CA  1 
ATOM 1996 C C   . TYR A 1 272 ? -42.721 34.972  -22.640 1.00 77.36  ? 280 TYR A C   1 
ATOM 1997 O O   . TYR A 1 272 ? -43.373 36.011  -22.783 1.00 83.94  ? 280 TYR A O   1 
ATOM 1998 C CB  . TYR A 1 272 ? -40.855 33.817  -23.920 1.00 72.35  ? 280 TYR A CB  1 
ATOM 1999 C CG  . TYR A 1 272 ? -41.703 33.666  -25.166 1.00 71.29  ? 280 TYR A CG  1 
ATOM 2000 C CD1 . TYR A 1 272 ? -42.863 32.898  -25.170 1.00 70.43  ? 280 TYR A CD1 1 
ATOM 2001 C CD2 . TYR A 1 272 ? -41.332 34.296  -26.345 1.00 75.76  ? 280 TYR A CD2 1 
ATOM 2002 C CE1 . TYR A 1 272 ? -43.622 32.763  -26.324 1.00 66.12  ? 280 TYR A CE1 1 
ATOM 2003 C CE2 . TYR A 1 272 ? -42.080 34.172  -27.490 1.00 75.18  ? 280 TYR A CE2 1 
ATOM 2004 C CZ  . TYR A 1 272 ? -43.222 33.409  -27.479 1.00 68.46  ? 280 TYR A CZ  1 
ATOM 2005 O OH  . TYR A 1 272 ? -43.955 33.301  -28.634 1.00 65.73  ? 280 TYR A OH  1 
ATOM 2006 N N   . ALA A 1 273 ? -43.239 33.853  -22.125 1.00 75.87  ? 281 ALA A N   1 
ATOM 2007 C CA  . ALA A 1 273 ? -44.663 33.742  -21.812 1.00 79.19  ? 281 ALA A CA  1 
ATOM 2008 C C   . ALA A 1 273 ? -45.142 34.917  -20.967 1.00 82.52  ? 281 ALA A C   1 
ATOM 2009 O O   . ALA A 1 273 ? -46.165 35.541  -21.271 1.00 86.55  ? 281 ALA A O   1 
ATOM 2010 C CB  . ALA A 1 273 ? -44.942 32.417  -21.100 1.00 79.44  ? 281 ALA A CB  1 
ATOM 2011 N N   . TYR A 1 274 ? -44.427 35.204  -19.877 1.00 81.24  ? 282 TYR A N   1 
ATOM 2012 C CA  . TYR A 1 274 ? -44.685 36.387  -19.059 1.00 82.62  ? 282 TYR A CA  1 
ATOM 2013 C C   . TYR A 1 274 ? -44.931 37.633  -19.910 1.00 85.30  ? 282 TYR A C   1 
ATOM 2014 O O   . TYR A 1 274 ? -45.930 38.335  -19.724 1.00 86.12  ? 282 TYR A O   1 
ATOM 2015 C CB  . TYR A 1 274 ? -43.502 36.601  -18.106 1.00 86.52  ? 282 TYR A CB  1 
ATOM 2016 C CG  . TYR A 1 274 ? -43.763 37.453  -16.874 1.00 96.81  ? 282 TYR A CG  1 
ATOM 2017 C CD1 . TYR A 1 274 ? -44.862 38.300  -16.790 1.00 96.32  ? 282 TYR A CD1 1 
ATOM 2018 C CD2 . TYR A 1 274 ? -42.900 37.396  -15.786 1.00 93.40  ? 282 TYR A CD2 1 
ATOM 2019 C CE1 . TYR A 1 274 ? -45.085 39.072  -15.658 1.00 93.79  ? 282 TYR A CE1 1 
ATOM 2020 C CE2 . TYR A 1 274 ? -43.115 38.157  -14.657 1.00 92.31  ? 282 TYR A CE2 1 
ATOM 2021 C CZ  . TYR A 1 274 ? -44.208 38.993  -14.595 1.00 95.35  ? 282 TYR A CZ  1 
ATOM 2022 O OH  . TYR A 1 274 ? -44.416 39.750  -13.463 1.00 95.31  ? 282 TYR A OH  1 
ATOM 2023 N N   . LYS A 1 275 ? -44.031 37.918  -20.859 1.00 84.96  ? 283 LYS A N   1 
ATOM 2024 C CA  . LYS A 1 275 ? -44.112 39.174  -21.604 1.00 82.97  ? 283 LYS A CA  1 
ATOM 2025 C C   . LYS A 1 275 ? -45.307 39.212  -22.556 1.00 83.84  ? 283 LYS A C   1 
ATOM 2026 O O   . LYS A 1 275 ? -46.060 40.192  -22.568 1.00 84.31  ? 283 LYS A O   1 
ATOM 2027 C CB  . LYS A 1 275 ? -42.806 39.424  -22.357 1.00 84.87  ? 283 LYS A CB  1 
ATOM 2028 C CG  . LYS A 1 275 ? -42.788 40.751  -23.099 1.00 91.00  ? 283 LYS A CG  1 
ATOM 2029 C CD  . LYS A 1 275 ? -41.455 40.977  -23.790 1.00 88.89  ? 283 LYS A CD  1 
ATOM 2030 C CE  . LYS A 1 275 ? -41.449 42.291  -24.550 1.00 85.34  ? 283 LYS A CE  1 
ATOM 2031 N NZ  . LYS A 1 275 ? -40.149 42.533  -25.237 1.00 82.98  ? 283 LYS A NZ  1 
ATOM 2032 N N   . LEU A 1 276 ? -45.491 38.172  -23.379 1.00 84.21  ? 284 LEU A N   1 
ATOM 2033 C CA  . LEU A 1 276 ? -46.672 38.129  -24.245 1.00 89.99  ? 284 LEU A CA  1 
ATOM 2034 C C   . LEU A 1 276 ? -47.948 38.223  -23.424 1.00 91.39  ? 284 LEU A C   1 
ATOM 2035 O O   . LEU A 1 276 ? -48.860 38.994  -23.748 1.00 97.61  ? 284 LEU A O   1 
ATOM 2036 C CB  . LEU A 1 276 ? -46.700 36.862  -25.108 1.00 90.95  ? 284 LEU A CB  1 
ATOM 2037 C CG  . LEU A 1 276 ? -45.670 36.502  -26.183 1.00 88.76  ? 284 LEU A CG  1 
ATOM 2038 C CD1 . LEU A 1 276 ? -45.460 37.678  -27.130 1.00 93.33  ? 284 LEU A CD1 1 
ATOM 2039 C CD2 . LEU A 1 276 ? -44.361 36.064  -25.599 1.00 85.17  ? 284 LEU A CD2 1 
ATOM 2040 N N   . LYS A 1 277 ? -48.035 37.421  -22.365 1.00 89.94  ? 285 LYS A N   1 
ATOM 2041 C CA  . LYS A 1 277 ? -49.226 37.405  -21.530 1.00 87.77  ? 285 LYS A CA  1 
ATOM 2042 C C   . LYS A 1 277 ? -49.467 38.772  -20.891 1.00 91.98  ? 285 LYS A C   1 
ATOM 2043 O O   . LYS A 1 277 ? -50.622 39.184  -20.724 1.00 91.17  ? 285 LYS A O   1 
ATOM 2044 C CB  . LYS A 1 277 ? -49.083 36.296  -20.489 1.00 82.97  ? 285 LYS A CB  1 
ATOM 2045 C CG  . LYS A 1 277 ? -50.377 35.836  -19.880 1.00 90.55  ? 285 LYS A CG  1 
ATOM 2046 C CD  . LYS A 1 277 ? -50.138 35.037  -18.613 1.00 89.84  ? 285 LYS A CD  1 
ATOM 2047 C CE  . LYS A 1 277 ? -49.683 33.621  -18.905 1.00 85.37  ? 285 LYS A CE  1 
ATOM 2048 N NZ  . LYS A 1 277 ? -50.860 32.711  -18.997 1.00 89.98  ? 285 LYS A NZ  1 
ATOM 2049 N N   . LYS A 1 278 ? -48.393 39.493  -20.547 1.00 98.56  ? 286 LYS A N   1 
ATOM 2050 C CA  . LYS A 1 278 ? -48.483 40.833  -19.971 1.00 102.70 ? 286 LYS A CA  1 
ATOM 2051 C C   . LYS A 1 278 ? -48.856 41.891  -21.013 1.00 103.60 ? 286 LYS A C   1 
ATOM 2052 O O   . LYS A 1 278 ? -49.153 43.036  -20.648 1.00 103.64 ? 286 LYS A O   1 
ATOM 2053 C CB  . LYS A 1 278 ? -47.145 41.173  -19.290 1.00 102.85 ? 286 LYS A CB  1 
ATOM 2054 C CG  . LYS A 1 278 ? -46.923 42.622  -18.854 1.00 102.40 ? 286 LYS A CG  1 
ATOM 2055 C CD  . LYS A 1 278 ? -45.847 42.718  -17.779 1.00 102.11 ? 286 LYS A CD  1 
ATOM 2056 C CE  . LYS A 1 278 ? -45.843 44.094  -17.128 1.00 101.05 ? 286 LYS A CE  1 
ATOM 2057 N NZ  . LYS A 1 278 ? -44.825 44.195  -16.044 1.00 84.23  ? 286 LYS A NZ  1 
ATOM 2058 N N   . MET A 1 279 ? -48.933 41.523  -22.288 1.00 101.08 ? 287 MET A N   1 
ATOM 2059 C CA  . MET A 1 279 ? -49.283 42.470  -23.333 1.00 96.04  ? 287 MET A CA  1 
ATOM 2060 C C   . MET A 1 279 ? -50.796 42.467  -23.530 1.00 91.20  ? 287 MET A C   1 
ATOM 2061 O O   . MET A 1 279 ? -51.522 41.648  -22.962 1.00 94.12  ? 287 MET A O   1 
ATOM 2062 C CB  . MET A 1 279 ? -48.550 42.134  -24.635 1.00 92.31  ? 287 MET A CB  1 
ATOM 2063 C CG  . MET A 1 279 ? -47.057 42.427  -24.591 1.00 96.72  ? 287 MET A CG  1 
ATOM 2064 S SD  . MET A 1 279 ? -46.197 42.140  -26.151 1.00 116.93 ? 287 MET A SD  1 
ATOM 2065 C CE  . MET A 1 279 ? -44.504 42.459  -25.653 1.00 102.06 ? 287 MET A CE  1 
ATOM 2066 N N   . GLY A 1 280 ? -51.276 43.403  -24.343 1.00 86.57  ? 288 GLY A N   1 
ATOM 2067 C CA  . GLY A 1 280 ? -52.703 43.498  -24.573 1.00 92.73  ? 288 GLY A CA  1 
ATOM 2068 C C   . GLY A 1 280 ? -53.296 42.464  -25.504 1.00 89.85  ? 288 GLY A C   1 
ATOM 2069 O O   . GLY A 1 280 ? -52.878 42.343  -26.661 1.00 90.75  ? 288 GLY A O   1 
ATOM 2070 N N   . GLY A 1 281 ? -54.279 41.717  -25.011 1.00 88.46  ? 289 GLY A N   1 
ATOM 2071 C CA  . GLY A 1 281 ? -55.063 40.814  -25.838 1.00 88.51  ? 289 GLY A CA  1 
ATOM 2072 C C   . GLY A 1 281 ? -54.565 39.396  -26.033 1.00 87.58  ? 289 GLY A C   1 
ATOM 2073 O O   . GLY A 1 281 ? -55.363 38.457  -26.057 1.00 87.88  ? 289 GLY A O   1 
ATOM 2074 N N   . LYS A 1 282 ? -53.252 39.226  -26.175 1.00 90.17  ? 290 LYS A N   1 
ATOM 2075 C CA  . LYS A 1 282 ? -52.690 37.932  -26.547 1.00 91.07  ? 290 LYS A CA  1 
ATOM 2076 C C   . LYS A 1 282 ? -52.994 36.866  -25.502 1.00 90.60  ? 290 LYS A C   1 
ATOM 2077 O O   . LYS A 1 282 ? -52.843 37.088  -24.297 1.00 91.83  ? 290 LYS A O   1 
ATOM 2078 C CB  . LYS A 1 282 ? -51.179 38.059  -26.751 1.00 85.13  ? 290 LYS A CB  1 
ATOM 2079 C CG  . LYS A 1 282 ? -50.790 38.612  -28.117 1.00 82.92  ? 290 LYS A CG  1 
ATOM 2080 C CD  . LYS A 1 282 ? -51.112 40.097  -28.215 1.00 86.71  ? 290 LYS A CD  1 
ATOM 2081 C CE  . LYS A 1 282 ? -51.251 40.551  -29.648 1.00 76.40  ? 290 LYS A CE  1 
ATOM 2082 N NZ  . LYS A 1 282 ? -51.658 41.981  -29.750 1.00 78.95  ? 290 LYS A NZ  1 
ATOM 2083 N N   . ARG A 1 283 ? -53.416 35.698  -25.984 1.00 88.52  ? 291 ARG A N   1 
ATOM 2084 C CA  . ARG A 1 283 ? -53.722 34.541  -25.151 1.00 76.78  ? 291 ARG A CA  1 
ATOM 2085 C C   . ARG A 1 283 ? -52.506 33.623  -25.130 1.00 75.35  ? 291 ARG A C   1 
ATOM 2086 O O   . ARG A 1 283 ? -52.170 33.006  -26.145 1.00 74.33  ? 291 ARG A O   1 
ATOM 2087 C CB  . ARG A 1 283 ? -54.953 33.817  -25.692 1.00 75.41  ? 291 ARG A CB  1 
ATOM 2088 C CG  . ARG A 1 283 ? -56.240 34.606  -25.533 1.00 81.84  ? 291 ARG A CG  1 
ATOM 2089 C CD  . ARG A 1 283 ? -57.413 33.913  -26.202 1.00 79.58  ? 291 ARG A CD  1 
ATOM 2090 N NE  . ARG A 1 283 ? -57.718 32.621  -25.602 1.00 84.46  ? 291 ARG A NE  1 
ATOM 2091 C CZ  . ARG A 1 283 ? -58.652 31.794  -26.051 1.00 85.95  ? 291 ARG A CZ  1 
ATOM 2092 N NH1 . ARG A 1 283 ? -59.379 32.086  -27.117 1.00 83.27  ? 291 ARG A NH1 1 
ATOM 2093 N NH2 . ARG A 1 283 ? -58.857 30.642  -25.419 1.00 83.21  ? 291 ARG A NH2 1 
ATOM 2094 N N   . VAL A 1 284 ? -51.844 33.536  -23.980 1.00 77.86  ? 292 VAL A N   1 
ATOM 2095 C CA  . VAL A 1 284 ? -50.650 32.713  -23.827 1.00 78.58  ? 292 VAL A CA  1 
ATOM 2096 C C   . VAL A 1 284 ? -50.803 31.873  -22.567 1.00 83.47  ? 292 VAL A C   1 
ATOM 2097 O O   . VAL A 1 284 ? -50.968 32.417  -21.470 1.00 85.02  ? 292 VAL A O   1 
ATOM 2098 C CB  . VAL A 1 284 ? -49.367 33.560  -23.757 1.00 72.49  ? 292 VAL A CB  1 
ATOM 2099 C CG1 . VAL A 1 284 ? -48.226 32.749  -23.158 1.00 70.09  ? 292 VAL A CG1 1 
ATOM 2100 C CG2 . VAL A 1 284 ? -48.996 34.066  -25.141 1.00 73.14  ? 292 VAL A CG2 1 
ATOM 2101 N N   . ASP A 1 285 ? -50.770 30.554  -22.727 1.00 78.54  ? 293 ASP A N   1 
ATOM 2102 C CA  . ASP A 1 285 ? -50.725 29.631  -21.604 1.00 72.17  ? 293 ASP A CA  1 
ATOM 2103 C C   . ASP A 1 285 ? -49.308 29.101  -21.427 1.00 69.51  ? 293 ASP A C   1 
ATOM 2104 O O   . ASP A 1 285 ? -48.560 28.937  -22.394 1.00 74.36  ? 293 ASP A O   1 
ATOM 2105 C CB  . ASP A 1 285 ? -51.694 28.465  -21.807 1.00 75.14  ? 293 ASP A CB  1 
ATOM 2106 C CG  . ASP A 1 285 ? -53.133 28.844  -21.515 1.00 87.18  ? 293 ASP A CG  1 
ATOM 2107 O OD1 . ASP A 1 285 ? -53.410 29.291  -20.382 1.00 87.17  ? 293 ASP A OD1 1 
ATOM 2108 O OD2 . ASP A 1 285 ? -53.986 28.693  -22.415 1.00 79.76  ? 293 ASP A OD2 1 
ATOM 2109 N N   . TYR A 1 286 ? -48.944 28.832  -20.176 1.00 70.74  ? 294 TYR A N   1 
ATOM 2110 C CA  . TYR A 1 286 ? -47.612 28.350  -19.842 1.00 65.56  ? 294 TYR A CA  1 
ATOM 2111 C C   . TYR A 1 286 ? -47.760 27.189  -18.873 1.00 73.74  ? 294 TYR A C   1 
ATOM 2112 O O   . TYR A 1 286 ? -48.485 27.295  -17.878 1.00 83.03  ? 294 TYR A O   1 
ATOM 2113 C CB  . TYR A 1 286 ? -46.755 29.483  -19.248 1.00 66.33  ? 294 TYR A CB  1 
ATOM 2114 C CG  . TYR A 1 286 ? -45.464 29.063  -18.569 1.00 65.25  ? 294 TYR A CG  1 
ATOM 2115 C CD1 . TYR A 1 286 ? -45.455 28.536  -17.280 1.00 67.63  ? 294 TYR A CD1 1 
ATOM 2116 C CD2 . TYR A 1 286 ? -44.247 29.202  -19.224 1.00 64.60  ? 294 TYR A CD2 1 
ATOM 2117 C CE1 . TYR A 1 286 ? -44.271 28.160  -16.671 1.00 74.93  ? 294 TYR A CE1 1 
ATOM 2118 C CE2 . TYR A 1 286 ? -43.063 28.830  -18.624 1.00 73.58  ? 294 TYR A CE2 1 
ATOM 2119 C CZ  . TYR A 1 286 ? -43.079 28.310  -17.350 1.00 79.51  ? 294 TYR A CZ  1 
ATOM 2120 O OH  . TYR A 1 286 ? -41.895 27.942  -16.758 1.00 83.11  ? 294 TYR A OH  1 
ATOM 2121 N N   . ILE A 1 287 ? -47.064 26.091  -19.158 1.00 71.60  ? 295 ILE A N   1 
ATOM 2122 C CA  . ILE A 1 287 ? -47.077 24.902  -18.314 1.00 66.53  ? 295 ILE A CA  1 
ATOM 2123 C C   . ILE A 1 287 ? -45.638 24.473  -18.081 1.00 62.50  ? 295 ILE A C   1 
ATOM 2124 O O   . ILE A 1 287 ? -44.860 24.349  -19.033 1.00 67.05  ? 295 ILE A O   1 
ATOM 2125 C CB  . ILE A 1 287 ? -47.877 23.746  -18.947 1.00 69.15  ? 295 ILE A CB  1 
ATOM 2126 C CG1 . ILE A 1 287 ? -49.165 24.252  -19.596 1.00 67.77  ? 295 ILE A CG1 1 
ATOM 2127 C CG2 . ILE A 1 287 ? -48.186 22.682  -17.903 1.00 79.98  ? 295 ILE A CG2 1 
ATOM 2128 C CD1 . ILE A 1 287 ? -50.219 24.693  -18.602 1.00 65.57  ? 295 ILE A CD1 1 
ATOM 2129 N N   . GLU A 1 288 ? -45.286 24.245  -16.821 1.00 65.85  ? 296 GLU A N   1 
ATOM 2130 C CA  . GLU A 1 288 ? -43.971 23.744  -16.457 1.00 68.13  ? 296 GLU A CA  1 
ATOM 2131 C C   . GLU A 1 288 ? -44.109 22.336  -15.900 1.00 67.59  ? 296 GLU A C   1 
ATOM 2132 O O   . GLU A 1 288 ? -45.067 22.034  -15.182 1.00 69.67  ? 296 GLU A O   1 
ATOM 2133 C CB  . GLU A 1 288 ? -43.303 24.647  -15.423 1.00 66.81  ? 296 GLU A CB  1 
ATOM 2134 C CG  . GLU A 1 288 ? -41.795 24.673  -15.522 1.00 71.95  ? 296 GLU A CG  1 
ATOM 2135 C CD  . GLU A 1 288 ? -41.201 25.828  -14.756 1.00 78.87  ? 296 GLU A CD  1 
ATOM 2136 O OE1 . GLU A 1 288 ? -41.382 25.887  -13.527 1.00 83.81  ? 296 GLU A OE1 1 
ATOM 2137 O OE2 . GLU A 1 288 ? -40.614 26.718  -15.397 1.00 77.94  ? 296 GLU A OE2 1 
ATOM 2138 N N   . PHE A 1 289 ? -43.155 21.477  -16.235 1.00 68.41  ? 297 PHE A N   1 
ATOM 2139 C CA  . PHE A 1 289 ? -43.108 20.121  -15.707 1.00 74.68  ? 297 PHE A CA  1 
ATOM 2140 C C   . PHE A 1 289 ? -41.877 20.000  -14.821 1.00 74.95  ? 297 PHE A C   1 
ATOM 2141 O O   . PHE A 1 289 ? -40.746 20.146  -15.298 1.00 73.09  ? 297 PHE A O   1 
ATOM 2142 C CB  . PHE A 1 289 ? -43.090 19.092  -16.838 1.00 76.65  ? 297 PHE A CB  1 
ATOM 2143 C CG  . PHE A 1 289 ? -44.428 18.899  -17.501 1.00 76.35  ? 297 PHE A CG  1 
ATOM 2144 C CD1 . PHE A 1 289 ? -45.037 19.943  -18.179 1.00 71.94  ? 297 PHE A CD1 1 
ATOM 2145 C CD2 . PHE A 1 289 ? -45.082 17.679  -17.437 1.00 85.30  ? 297 PHE A CD2 1 
ATOM 2146 C CE1 . PHE A 1 289 ? -46.264 19.773  -18.789 1.00 78.08  ? 297 PHE A CE1 1 
ATOM 2147 C CE2 . PHE A 1 289 ? -46.312 17.503  -18.046 1.00 84.67  ? 297 PHE A CE2 1 
ATOM 2148 C CZ  . PHE A 1 289 ? -46.903 18.553  -18.722 1.00 85.26  ? 297 PHE A CZ  1 
ATOM 2149 N N   . GLU A 1 290 ? -42.104 19.738  -13.536 1.00 77.29  ? 298 GLU A N   1 
ATOM 2150 C CA  . GLU A 1 290 ? -41.052 19.856  -12.536 1.00 84.37  ? 298 GLU A CA  1 
ATOM 2151 C C   . GLU A 1 290 ? -39.944 18.834  -12.765 1.00 79.54  ? 298 GLU A C   1 
ATOM 2152 O O   . GLU A 1 290 ? -40.204 17.679  -13.111 1.00 74.99  ? 298 GLU A O   1 
ATOM 2153 C CB  . GLU A 1 290 ? -41.636 19.689  -11.133 1.00 90.93  ? 298 GLU A CB  1 
ATOM 2154 C CG  . GLU A 1 290 ? -42.568 18.499  -10.990 1.00 91.42  ? 298 GLU A CG  1 
ATOM 2155 C CD  . GLU A 1 290 ? -43.144 18.376  -9.596  1.00 89.30  ? 298 GLU A CD  1 
ATOM 2156 O OE1 . GLU A 1 290 ? -42.359 18.416  -8.626  1.00 90.76  ? 298 GLU A OE1 1 
ATOM 2157 O OE2 . GLU A 1 290 ? -44.380 18.245  -9.469  1.00 85.54  ? 298 GLU A OE2 1 
ATOM 2158 N N   . ASN A 1 291 ? -38.700 19.299  -12.629 1.00 78.20  ? 299 ASN A N   1 
ATOM 2159 C CA  . ASN A 1 291 ? -37.458 18.526  -12.680 1.00 78.81  ? 299 ASN A CA  1 
ATOM 2160 C C   . ASN A 1 291 ? -37.195 17.891  -14.041 1.00 83.78  ? 299 ASN A C   1 
ATOM 2161 O O   . ASN A 1 291 ? -36.237 17.122  -14.184 1.00 84.92  ? 299 ASN A O   1 
ATOM 2162 C CB  . ASN A 1 291 ? -37.382 17.468  -11.551 1.00 88.53  ? 299 ASN A CB  1 
ATOM 2163 C CG  . ASN A 1 291 ? -38.210 16.204  -11.817 1.00 92.48  ? 299 ASN A CG  1 
ATOM 2164 O OD1 . ASN A 1 291 ? -38.183 15.620  -12.903 1.00 93.28  ? 299 ASN A OD1 1 
ATOM 2165 N ND2 . ASN A 1 291 ? -38.955 15.780  -10.804 1.00 90.39  ? 299 ASN A ND2 1 
ATOM 2166 N N   . LYS A 1 292 ? -37.995 18.213  -15.053 1.00 86.78  ? 300 LYS A N   1 
ATOM 2167 C CA  . LYS A 1 292 ? -37.881 17.566  -16.351 1.00 82.26  ? 300 LYS A CA  1 
ATOM 2168 C C   . LYS A 1 292 ? -36.834 18.252  -17.219 1.00 82.62  ? 300 LYS A C   1 
ATOM 2169 O O   . LYS A 1 292 ? -36.604 19.461  -17.119 1.00 84.87  ? 300 LYS A O   1 
ATOM 2170 C CB  . LYS A 1 292 ? -39.233 17.561  -17.065 1.00 75.62  ? 300 LYS A CB  1 
ATOM 2171 C CG  . LYS A 1 292 ? -40.346 16.972  -16.229 1.00 82.78  ? 300 LYS A CG  1 
ATOM 2172 C CD  . LYS A 1 292 ? -40.089 15.506  -15.946 1.00 89.05  ? 300 LYS A CD  1 
ATOM 2173 C CE  . LYS A 1 292 ? -41.195 14.907  -15.099 1.00 88.27  ? 300 LYS A CE  1 
ATOM 2174 N NZ  . LYS A 1 292 ? -40.963 13.464  -14.819 1.00 81.85  ? 300 LYS A NZ  1 
ATOM 2175 N N   . GLU A 1 293 ? -36.193 17.459  -18.072 1.00 83.47  ? 301 GLU A N   1 
ATOM 2176 C CA  . GLU A 1 293 ? -35.177 17.958  -18.983 1.00 87.43  ? 301 GLU A CA  1 
ATOM 2177 C C   . GLU A 1 293 ? -35.780 18.270  -20.350 1.00 89.75  ? 301 GLU A C   1 
ATOM 2178 O O   . GLU A 1 293 ? -36.933 17.945  -20.642 1.00 84.05  ? 301 GLU A O   1 
ATOM 2179 C CB  . GLU A 1 293 ? -34.039 16.946  -19.115 1.00 91.12  ? 301 GLU A CB  1 
ATOM 2180 C CG  . GLU A 1 293 ? -33.291 16.687  -17.813 1.00 85.48  ? 301 GLU A CG  1 
ATOM 2181 C CD  . GLU A 1 293 ? -31.789 16.608  -18.003 1.00 95.76  ? 301 GLU A CD  1 
ATOM 2182 O OE1 . GLU A 1 293 ? -31.346 15.960  -18.973 1.00 94.04  ? 301 GLU A OE1 1 
ATOM 2183 O OE2 . GLU A 1 293 ? -31.051 17.191  -17.180 1.00 98.92  ? 301 GLU A OE2 1 
ATOM 2184 N N   . HIS A 1 294 ? -34.981 18.923  -21.193 1.00 86.23  ? 302 HIS A N   1 
ATOM 2185 C CA  . HIS A 1 294 ? -35.458 19.340  -22.504 1.00 88.78  ? 302 HIS A CA  1 
ATOM 2186 C C   . HIS A 1 294 ? -35.826 18.118  -23.340 1.00 86.89  ? 302 HIS A C   1 
ATOM 2187 O O   . HIS A 1 294 ? -35.104 17.116  -23.356 1.00 83.92  ? 302 HIS A O   1 
ATOM 2188 C CB  . HIS A 1 294 ? -34.387 20.174  -23.211 1.00 87.12  ? 302 HIS A CB  1 
ATOM 2189 C CG  . HIS A 1 294 ? -34.830 20.760  -24.517 1.00 80.24  ? 302 HIS A CG  1 
ATOM 2190 N ND1 . HIS A 1 294 ? -36.155 20.843  -24.886 1.00 80.30  ? 302 HIS A ND1 1 
ATOM 2191 C CD2 . HIS A 1 294 ? -34.121 21.293  -25.540 1.00 74.80  ? 302 HIS A CD2 1 
ATOM 2192 C CE1 . HIS A 1 294 ? -36.243 21.403  -26.080 1.00 83.07  ? 302 HIS A CE1 1 
ATOM 2193 N NE2 . HIS A 1 294 ? -35.023 21.684  -26.499 1.00 84.45  ? 302 HIS A NE2 1 
ATOM 2194 N N   . GLY A 1 295 ? -36.954 18.207  -24.041 1.00 80.70  ? 303 GLY A N   1 
ATOM 2195 C CA  . GLY A 1 295 ? -37.422 17.106  -24.862 1.00 76.11  ? 303 GLY A CA  1 
ATOM 2196 C C   . GLY A 1 295 ? -37.812 15.871  -24.080 1.00 70.67  ? 303 GLY A C   1 
ATOM 2197 O O   . GLY A 1 295 ? -37.637 14.752  -24.571 1.00 69.30  ? 303 GLY A O   1 
ATOM 2198 N N   . PHE A 1 296 ? -38.337 16.048  -22.865 1.00 80.46  ? 304 PHE A N   1 
ATOM 2199 C CA  . PHE A 1 296 ? -38.848 14.919  -22.091 1.00 81.57  ? 304 PHE A CA  1 
ATOM 2200 C C   . PHE A 1 296 ? -40.061 14.285  -22.764 1.00 80.87  ? 304 PHE A C   1 
ATOM 2201 O O   . PHE A 1 296 ? -40.267 13.069  -22.675 1.00 84.54  ? 304 PHE A O   1 
ATOM 2202 C CB  . PHE A 1 296 ? -39.188 15.371  -20.666 1.00 79.71  ? 304 PHE A CB  1 
ATOM 2203 C CG  . PHE A 1 296 ? -40.266 16.425  -20.590 1.00 81.61  ? 304 PHE A CG  1 
ATOM 2204 C CD1 . PHE A 1 296 ? -41.607 16.078  -20.661 1.00 78.96  ? 304 PHE A CD1 1 
ATOM 2205 C CD2 . PHE A 1 296 ? -39.937 17.765  -20.481 1.00 79.68  ? 304 PHE A CD2 1 
ATOM 2206 C CE1 . PHE A 1 296 ? -42.595 17.042  -20.602 1.00 72.99  ? 304 PHE A CE1 1 
ATOM 2207 C CE2 . PHE A 1 296 ? -40.919 18.734  -20.423 1.00 79.79  ? 304 PHE A CE2 1 
ATOM 2208 C CZ  . PHE A 1 296 ? -42.252 18.372  -20.484 1.00 72.72  ? 304 PHE A CZ  1 
ATOM 2209 N N   . TYR A 1 297 ? -40.879 15.100  -23.433 1.00 75.48  ? 305 TYR A N   1 
ATOM 2210 C CA  . TYR A 1 297 ? -42.005 14.588  -24.207 1.00 74.14  ? 305 TYR A CA  1 
ATOM 2211 C C   . TYR A 1 297 ? -41.561 13.654  -25.326 1.00 75.59  ? 305 TYR A C   1 
ATOM 2212 O O   . TYR A 1 297 ? -42.221 12.644  -25.597 1.00 68.25  ? 305 TYR A O   1 
ATOM 2213 C CB  . TYR A 1 297 ? -42.816 15.757  -24.779 1.00 72.21  ? 305 TYR A CB  1 
ATOM 2214 C CG  . TYR A 1 297 ? -41.995 16.858  -25.434 1.00 74.50  ? 305 TYR A CG  1 
ATOM 2215 C CD1 . TYR A 1 297 ? -41.292 17.782  -24.666 1.00 74.33  ? 305 TYR A CD1 1 
ATOM 2216 C CD2 . TYR A 1 297 ? -41.903 16.959  -26.817 1.00 76.67  ? 305 TYR A CD2 1 
ATOM 2217 C CE1 . TYR A 1 297 ? -40.544 18.783  -25.252 1.00 72.15  ? 305 TYR A CE1 1 
ATOM 2218 C CE2 . TYR A 1 297 ? -41.153 17.959  -27.414 1.00 72.81  ? 305 TYR A CE2 1 
ATOM 2219 C CZ  . TYR A 1 297 ? -40.475 18.866  -26.625 1.00 72.04  ? 305 TYR A CZ  1 
ATOM 2220 O OH  . TYR A 1 297 ? -39.725 19.862  -27.206 1.00 72.03  ? 305 TYR A OH  1 
ATOM 2221 N N   . SER A 1 298 ? -40.446 13.968  -25.981 1.00 76.55  ? 306 SER A N   1 
ATOM 2222 C CA  . SER A 1 298 ? -39.978 13.152  -27.098 1.00 72.81  ? 306 SER A CA  1 
ATOM 2223 C C   . SER A 1 298 ? -39.134 11.969  -26.632 1.00 76.94  ? 306 SER A C   1 
ATOM 2224 O O   . SER A 1 298 ? -39.435 10.811  -26.943 1.00 87.33  ? 306 SER A O   1 
ATOM 2225 C CB  . SER A 1 298 ? -39.192 14.018  -28.087 1.00 74.00  ? 306 SER A CB  1 
ATOM 2226 O OG  . SER A 1 298 ? -40.074 14.809  -28.863 1.00 81.53  ? 306 SER A OG  1 
ATOM 2227 N N   . ASN A 1 299 ? -38.065 12.254  -25.886 1.00 74.59  ? 307 ASN A N   1 
ATOM 2228 C CA  . ASN A 1 299 ? -37.123 11.222  -25.457 1.00 73.18  ? 307 ASN A CA  1 
ATOM 2229 C C   . ASN A 1 299 ? -37.758 10.146  -24.581 1.00 73.23  ? 307 ASN A C   1 
ATOM 2230 O O   . ASN A 1 299 ? -37.346 8.981   -24.647 1.00 74.01  ? 307 ASN A O   1 
ATOM 2231 C CB  . ASN A 1 299 ? -35.966 11.884  -24.709 1.00 78.30  ? 307 ASN A CB  1 
ATOM 2232 C CG  . ASN A 1 299 ? -35.246 12.917  -25.552 1.00 79.14  ? 307 ASN A CG  1 
ATOM 2233 O OD1 . ASN A 1 299 ? -35.673 13.236  -26.662 1.00 83.67  ? 307 ASN A OD1 1 
ATOM 2234 N ND2 . ASN A 1 299 ? -34.148 13.448  -25.027 1.00 72.92  ? 307 ASN A ND2 1 
ATOM 2235 N N   . TYR A 1 300 ? -38.744 10.495  -23.759 1.00 78.92  ? 308 TYR A N   1 
ATOM 2236 C CA  . TYR A 1 300 ? -39.336 9.559   -22.800 1.00 80.01  ? 308 TYR A CA  1 
ATOM 2237 C C   . TYR A 1 300 ? -40.849 9.487   -22.977 1.00 76.91  ? 308 TYR A C   1 
ATOM 2238 O O   . TYR A 1 300 ? -41.609 9.910   -22.097 1.00 72.79  ? 308 TYR A O   1 
ATOM 2239 C CB  . TYR A 1 300 ? -38.976 9.950   -21.366 1.00 77.99  ? 308 TYR A CB  1 
ATOM 2240 C CG  . TYR A 1 300 ? -37.495 9.878   -21.071 1.00 78.80  ? 308 TYR A CG  1 
ATOM 2241 C CD1 . TYR A 1 300 ? -36.847 8.654   -20.960 1.00 79.40  ? 308 TYR A CD1 1 
ATOM 2242 C CD2 . TYR A 1 300 ? -36.746 11.034  -20.900 1.00 84.91  ? 308 TYR A CD2 1 
ATOM 2243 C CE1 . TYR A 1 300 ? -35.491 8.587   -20.692 1.00 83.98  ? 308 TYR A CE1 1 
ATOM 2244 C CE2 . TYR A 1 300 ? -35.393 10.977  -20.631 1.00 90.07  ? 308 TYR A CE2 1 
ATOM 2245 C CZ  . TYR A 1 300 ? -34.770 9.751   -20.527 1.00 85.63  ? 308 TYR A CZ  1 
ATOM 2246 O OH  . TYR A 1 300 ? -33.421 9.693   -20.259 1.00 87.37  ? 308 TYR A OH  1 
ATOM 2247 N N   . PRO A 1 301 ? -41.322 8.952   -24.102 1.00 74.02  ? 309 PRO A N   1 
ATOM 2248 C CA  . PRO A 1 301 ? -42.770 8.897   -24.336 1.00 79.45  ? 309 PRO A CA  1 
ATOM 2249 C C   . PRO A 1 301 ? -43.445 7.899   -23.406 1.00 80.93  ? 309 PRO A C   1 
ATOM 2250 O O   . PRO A 1 301 ? -42.803 7.170   -22.647 1.00 81.81  ? 309 PRO A O   1 
ATOM 2251 C CB  . PRO A 1 301 ? -42.880 8.452   -25.796 1.00 74.79  ? 309 PRO A CB  1 
ATOM 2252 C CG  . PRO A 1 301 ? -41.629 7.685   -26.047 1.00 73.25  ? 309 PRO A CG  1 
ATOM 2253 C CD  . PRO A 1 301 ? -40.561 8.276   -25.168 1.00 68.83  ? 309 PRO A CD  1 
ATOM 2254 N N   . SER A 1 302 ? -44.780 7.889   -23.474 1.00 75.53  ? 310 SER A N   1 
ATOM 2255 C CA  . SER A 1 302 ? -45.639 7.026   -22.664 1.00 83.81  ? 310 SER A CA  1 
ATOM 2256 C C   . SER A 1 302 ? -45.380 7.190   -21.165 1.00 86.51  ? 310 SER A C   1 
ATOM 2257 O O   . SER A 1 302 ? -45.953 6.460   -20.351 1.00 86.42  ? 310 SER A O   1 
ATOM 2258 C CB  . SER A 1 302 ? -45.367 5.551   -22.979 1.00 93.61  ? 310 SER A CB  1 
ATOM 2259 O OG  . SER A 1 302 ? -46.349 4.716   -22.389 1.00 100.95 ? 310 SER A OG  1 
ATOM 2260 N N   . SER A 1 303 ? -44.527 8.142   -20.796 1.00 89.92  ? 311 SER A N   1 
ATOM 2261 C CA  . SER A 1 303 ? -44.343 8.512   -19.398 1.00 87.58  ? 311 SER A CA  1 
ATOM 2262 C C   . SER A 1 303 ? -45.500 9.428   -19.011 1.00 85.43  ? 311 SER A C   1 
ATOM 2263 O O   . SER A 1 303 ? -46.110 10.086  -19.859 1.00 87.79  ? 311 SER A O   1 
ATOM 2264 C CB  . SER A 1 303 ? -43.009 9.238   -19.208 1.00 84.76  ? 311 SER A CB  1 
ATOM 2265 O OG  . SER A 1 303 ? -43.117 10.609  -19.551 1.00 84.04  ? 311 SER A OG  1 
ATOM 2266 N N   . GLU A 1 304 ? -45.825 9.421   -17.714 1.00 85.56  ? 312 GLU A N   1 
ATOM 2267 C CA  . GLU A 1 304 ? -46.855 10.299  -17.164 1.00 89.01  ? 312 GLU A CA  1 
ATOM 2268 C C   . GLU A 1 304 ? -46.744 11.721  -17.707 1.00 91.06  ? 312 GLU A C   1 
ATOM 2269 O O   . GLU A 1 304 ? -47.733 12.301  -18.169 1.00 91.19  ? 312 GLU A O   1 
ATOM 2270 C CB  . GLU A 1 304 ? -46.774 10.295  -15.633 1.00 93.47  ? 312 GLU A CB  1 
ATOM 2271 C CG  . GLU A 1 304 ? -45.404 10.649  -15.067 1.00 96.68  ? 312 GLU A CG  1 
ATOM 2272 C CD  . GLU A 1 304 ? -45.159 10.058  -13.698 1.00 92.77  ? 312 GLU A CD  1 
ATOM 2273 O OE1 . GLU A 1 304 ? -46.102 9.478   -13.123 1.00 95.85  ? 312 GLU A OE1 1 
ATOM 2274 O OE2 . GLU A 1 304 ? -44.023 10.184  -13.194 1.00 86.74  ? 312 GLU A OE2 1 
ATOM 2275 N N   . ALA A 1 305 ? -45.544 12.306  -17.629 1.00 87.71  ? 313 ALA A N   1 
ATOM 2276 C CA  . ALA A 1 305 ? -45.312 13.636  -18.182 1.00 90.43  ? 313 ALA A CA  1 
ATOM 2277 C C   . ALA A 1 305 ? -45.705 13.697  -19.652 1.00 89.99  ? 313 ALA A C   1 
ATOM 2278 O O   . ALA A 1 305 ? -46.425 14.606  -20.078 1.00 83.58  ? 313 ALA A O   1 
ATOM 2279 C CB  . ALA A 1 305 ? -43.847 14.032  -17.996 1.00 83.60  ? 313 ALA A CB  1 
ATOM 2280 N N   . ALA A 1 306 ? -45.236 12.728  -20.443 1.00 89.48  ? 314 ALA A N   1 
ATOM 2281 C CA  . ALA A 1 306 ? -45.534 12.722  -21.871 1.00 82.25  ? 314 ALA A CA  1 
ATOM 2282 C C   . ALA A 1 306 ? -47.036 12.651  -22.118 1.00 80.82  ? 314 ALA A C   1 
ATOM 2283 O O   . ALA A 1 306 ? -47.618 13.548  -22.735 1.00 83.89  ? 314 ALA A O   1 
ATOM 2284 C CB  . ALA A 1 306 ? -44.818 11.555  -22.553 1.00 77.98  ? 314 ALA A CB  1 
ATOM 2285 N N   . GLU A 1 307 ? -47.688 11.606  -21.597 1.00 83.67  ? 315 GLU A N   1 
ATOM 2286 C CA  . GLU A 1 307 ? -49.125 11.449  -21.801 1.00 87.22  ? 315 GLU A CA  1 
ATOM 2287 C C   . GLU A 1 307 ? -49.902 12.674  -21.344 1.00 87.23  ? 315 GLU A C   1 
ATOM 2288 O O   . GLU A 1 307 ? -50.932 13.012  -21.939 1.00 79.23  ? 315 GLU A O   1 
ATOM 2289 C CB  . GLU A 1 307 ? -49.631 10.200  -21.082 1.00 90.93  ? 315 GLU A CB  1 
ATOM 2290 C CG  . GLU A 1 307 ? -49.330 8.908   -21.820 1.00 91.72  ? 315 GLU A CG  1 
ATOM 2291 C CD  . GLU A 1 307 ? -50.226 8.713   -23.027 1.00 101.39 ? 315 GLU A CD  1 
ATOM 2292 O OE1 . GLU A 1 307 ? -51.324 9.308   -23.057 1.00 108.78 ? 315 GLU A OE1 1 
ATOM 2293 O OE2 . GLU A 1 307 ? -49.834 7.965   -23.948 1.00 100.46 ? 315 GLU A OE2 1 
ATOM 2294 N N   . GLN A 1 308 ? -49.434 13.349  -20.293 1.00 89.56  ? 316 GLN A N   1 
ATOM 2295 C CA  . GLN A 1 308 ? -50.039 14.621  -19.919 1.00 89.01  ? 316 GLN A CA  1 
ATOM 2296 C C   . GLN A 1 308 ? -49.897 15.633  -21.048 1.00 87.78  ? 316 GLN A C   1 
ATOM 2297 O O   . GLN A 1 308 ? -50.881 16.256  -21.461 1.00 80.64  ? 316 GLN A O   1 
ATOM 2298 C CB  . GLN A 1 308 ? -49.404 15.152  -18.633 1.00 89.99  ? 316 GLN A CB  1 
ATOM 2299 C CG  . GLN A 1 308 ? -50.254 16.178  -17.895 1.00 94.06  ? 316 GLN A CG  1 
ATOM 2300 C CD  . GLN A 1 308 ? -49.668 16.560  -16.550 1.00 98.34  ? 316 GLN A CD  1 
ATOM 2301 O OE1 . GLN A 1 308 ? -48.554 16.162  -16.210 1.00 95.57  ? 316 GLN A OE1 1 
ATOM 2302 N NE2 . GLN A 1 308 ? -50.419 17.336  -15.775 1.00 102.29 ? 316 GLN A NE2 1 
ATOM 2303 N N   . VAL A 1 309 ? -48.683 15.762  -21.599 1.00 88.99  ? 317 VAL A N   1 
ATOM 2304 C CA  . VAL A 1 309 ? -48.426 16.702  -22.693 1.00 79.33  ? 317 VAL A CA  1 
ATOM 2305 C C   . VAL A 1 309 ? -49.431 16.523  -23.825 1.00 73.00  ? 317 VAL A C   1 
ATOM 2306 O O   . VAL A 1 309 ? -49.915 17.505  -24.401 1.00 73.39  ? 317 VAL A O   1 
ATOM 2307 C CB  . VAL A 1 309 ? -46.978 16.559  -23.194 1.00 69.87  ? 317 VAL A CB  1 
ATOM 2308 C CG1 . VAL A 1 309 ? -46.774 17.410  -24.414 1.00 60.28  ? 317 VAL A CG1 1 
ATOM 2309 C CG2 . VAL A 1 309 ? -46.002 16.978  -22.106 1.00 66.77  ? 317 VAL A CG2 1 
ATOM 2310 N N   . LEU A 1 310 ? -49.783 15.279  -24.148 1.00 74.68  ? 318 LEU A N   1 
ATOM 2311 C CA  . LEU A 1 310 ? -50.739 15.076  -25.228 1.00 80.66  ? 318 LEU A CA  1 
ATOM 2312 C C   . LEU A 1 310 ? -52.171 15.338  -24.783 1.00 80.08  ? 318 LEU A C   1 
ATOM 2313 O O   . LEU A 1 310 ? -53.061 15.427  -25.635 1.00 70.69  ? 318 LEU A O   1 
ATOM 2314 C CB  . LEU A 1 310 ? -50.648 13.656  -25.809 1.00 81.63  ? 318 LEU A CB  1 
ATOM 2315 C CG  . LEU A 1 310 ? -49.408 13.096  -26.528 1.00 79.01  ? 318 LEU A CG  1 
ATOM 2316 C CD1 . LEU A 1 310 ? -48.939 14.048  -27.627 1.00 72.54  ? 318 LEU A CD1 1 
ATOM 2317 C CD2 . LEU A 1 310 ? -48.264 12.720  -25.603 1.00 79.78  ? 318 LEU A CD2 1 
ATOM 2318 N N   . ARG A 1 311 ? -52.414 15.465  -23.475 1.00 85.35  ? 319 ARG A N   1 
ATOM 2319 C CA  . ARG A 1 311 ? -53.742 15.841  -23.004 1.00 91.24  ? 319 ARG A CA  1 
ATOM 2320 C C   . ARG A 1 311 ? -53.960 17.354  -22.982 1.00 91.17  ? 319 ARG A C   1 
ATOM 2321 O O   . ARG A 1 311 ? -55.093 17.802  -23.193 1.00 93.08  ? 319 ARG A O   1 
ATOM 2322 C CB  . ARG A 1 311 ? -54.008 15.226  -21.628 1.00 95.68  ? 319 ARG A CB  1 
ATOM 2323 C CG  . ARG A 1 311 ? -54.286 13.720  -21.698 1.00 89.92  ? 319 ARG A CG  1 
ATOM 2324 C CD  . ARG A 1 311 ? -54.520 13.094  -20.328 1.00 86.02  ? 319 ARG A CD  1 
ATOM 2325 N NE  . ARG A 1 311 ? -53.314 13.039  -19.510 1.00 92.96  ? 319 ARG A NE  1 
ATOM 2326 C CZ  . ARG A 1 311 ? -52.917 11.965  -18.838 1.00 87.71  ? 319 ARG A CZ  1 
ATOM 2327 N NH1 . ARG A 1 311 ? -53.591 10.828  -18.891 1.00 86.67  ? 319 ARG A NH1 1 
ATOM 2328 N NH2 . ARG A 1 311 ? -51.809 12.031  -18.104 1.00 78.99  ? 319 ARG A NH2 1 
ATOM 2329 N N   . ILE A 1 312 ? -52.916 18.160  -22.754 1.00 84.58  ? 320 ILE A N   1 
ATOM 2330 C CA  . ILE A 1 312 ? -53.109 19.610  -22.792 1.00 86.39  ? 320 ILE A CA  1 
ATOM 2331 C C   . ILE A 1 312 ? -53.258 20.084  -24.233 1.00 87.95  ? 320 ILE A C   1 
ATOM 2332 O O   . ILE A 1 312 ? -54.160 20.867  -24.552 1.00 86.61  ? 320 ILE A O   1 
ATOM 2333 C CB  . ILE A 1 312 ? -51.978 20.371  -22.069 1.00 81.39  ? 320 ILE A CB  1 
ATOM 2334 C CG1 . ILE A 1 312 ? -51.741 19.870  -20.646 1.00 93.92  ? 320 ILE A CG1 1 
ATOM 2335 C CG2 . ILE A 1 312 ? -52.287 21.864  -22.033 1.00 81.10  ? 320 ILE A CG2 1 
ATOM 2336 C CD1 . ILE A 1 312 ? -50.504 19.038  -20.476 1.00 96.98  ? 320 ILE A CD1 1 
ATOM 2337 N N   . ILE A 1 313 ? -52.350 19.649  -25.115 1.00 85.03  ? 321 ILE A N   1 
ATOM 2338 C CA  . ILE A 1 313 ? -52.430 20.023  -26.526 1.00 81.28  ? 321 ILE A CA  1 
ATOM 2339 C C   . ILE A 1 313 ? -53.805 19.692  -27.090 1.00 83.67  ? 321 ILE A C   1 
ATOM 2340 O O   . ILE A 1 313 ? -54.378 20.468  -27.862 1.00 78.42  ? 321 ILE A O   1 
ATOM 2341 C CB  . ILE A 1 313 ? -51.309 19.332  -27.326 1.00 76.68  ? 321 ILE A CB  1 
ATOM 2342 C CG1 . ILE A 1 313 ? -49.941 19.842  -26.875 1.00 73.25  ? 321 ILE A CG1 1 
ATOM 2343 C CG2 . ILE A 1 313 ? -51.494 19.552  -28.820 1.00 72.88  ? 321 ILE A CG2 1 
ATOM 2344 C CD1 . ILE A 1 313 ? -48.798 18.912  -27.216 1.00 66.72  ? 321 ILE A CD1 1 
ATOM 2345 N N   . GLY A 1 314 ? -54.354 18.538  -26.715 1.00 86.77  ? 322 GLY A N   1 
ATOM 2346 C CA  . GLY A 1 314 ? -55.714 18.187  -27.073 1.00 89.04  ? 322 GLY A CA  1 
ATOM 2347 C C   . GLY A 1 314 ? -56.719 19.233  -26.638 1.00 90.10  ? 322 GLY A C   1 
ATOM 2348 O O   . GLY A 1 314 ? -57.470 19.763  -27.461 1.00 81.68  ? 322 GLY A O   1 
ATOM 2349 N N   . ASP A 1 315 ? -56.736 19.537  -25.337 1.00 96.76  ? 323 ASP A N   1 
ATOM 2350 C CA  . ASP A 1 315 ? -57.598 20.601  -24.828 1.00 97.97  ? 323 ASP A CA  1 
ATOM 2351 C C   . ASP A 1 315 ? -57.305 21.926  -25.523 1.00 96.25  ? 323 ASP A C   1 
ATOM 2352 O O   . ASP A 1 315 ? -58.226 22.647  -25.924 1.00 95.35  ? 323 ASP A O   1 
ATOM 2353 C CB  . ASP A 1 315 ? -57.435 20.736  -23.313 1.00 99.72  ? 323 ASP A CB  1 
ATOM 2354 C CG  . ASP A 1 315 ? -57.761 19.454  -22.573 1.00 94.59  ? 323 ASP A CG  1 
ATOM 2355 O OD1 . ASP A 1 315 ? -58.795 18.831  -22.890 1.00 93.59  ? 323 ASP A OD1 1 
ATOM 2356 O OD2 . ASP A 1 315 ? -56.994 19.079  -21.663 1.00 90.06  ? 323 ASP A OD2 1 
ATOM 2357 N N   . PHE A 1 316 ? -56.020 22.273  -25.647 1.00 95.43  ? 324 PHE A N   1 
ATOM 2358 C CA  . PHE A 1 316 ? -55.625 23.487  -26.358 1.00 88.89  ? 324 PHE A CA  1 
ATOM 2359 C C   . PHE A 1 316 ? -56.234 23.550  -27.753 1.00 88.92  ? 324 PHE A C   1 
ATOM 2360 O O   . PHE A 1 316 ? -56.576 24.632  -28.242 1.00 85.76  ? 324 PHE A O   1 
ATOM 2361 C CB  . PHE A 1 316 ? -54.103 23.564  -26.441 1.00 82.75  ? 324 PHE A CB  1 
ATOM 2362 C CG  . PHE A 1 316 ? -53.589 24.853  -27.018 1.00 75.91  ? 324 PHE A CG  1 
ATOM 2363 C CD1 . PHE A 1 316 ? -53.598 26.018  -26.269 1.00 80.58  ? 324 PHE A CD1 1 
ATOM 2364 C CD2 . PHE A 1 316 ? -53.079 24.895  -28.305 1.00 74.46  ? 324 PHE A CD2 1 
ATOM 2365 C CE1 . PHE A 1 316 ? -53.123 27.203  -26.797 1.00 74.51  ? 324 PHE A CE1 1 
ATOM 2366 C CE2 . PHE A 1 316 ? -52.600 26.076  -28.839 1.00 74.87  ? 324 PHE A CE2 1 
ATOM 2367 C CZ  . PHE A 1 316 ? -52.622 27.232  -28.084 1.00 70.03  ? 324 PHE A CZ  1 
ATOM 2368 N N   . MET A 1 317 ? -56.364 22.401  -28.415 1.00 91.50  ? 325 MET A N   1 
ATOM 2369 C CA  . MET A 1 317 ? -56.990 22.374  -29.732 1.00 89.36  ? 325 MET A CA  1 
ATOM 2370 C C   . MET A 1 317 ? -58.509 22.436  -29.637 1.00 88.32  ? 325 MET A C   1 
ATOM 2371 O O   . MET A 1 317 ? -59.152 23.139  -30.425 1.00 88.68  ? 325 MET A O   1 
ATOM 2372 C CB  . MET A 1 317 ? -56.547 21.129  -30.497 1.00 85.49  ? 325 MET A CB  1 
ATOM 2373 C CG  . MET A 1 317 ? -55.080 21.149  -30.887 1.00 82.88  ? 325 MET A CG  1 
ATOM 2374 S SD  . MET A 1 317 ? -54.509 19.545  -31.459 1.00 70.64  ? 325 MET A SD  1 
ATOM 2375 C CE  . MET A 1 317 ? -55.132 19.520  -33.136 1.00 74.86  ? 325 MET A CE  1 
ATOM 2376 N N   . ASN A 1 318 ? -59.100 21.711  -28.685 1.00 86.60  ? 326 ASN A N   1 
ATOM 2377 C CA  . ASN A 1 318 ? -60.556 21.640  -28.621 1.00 86.60  ? 326 ASN A CA  1 
ATOM 2378 C C   . ASN A 1 318 ? -61.167 22.931  -28.089 1.00 88.17  ? 326 ASN A C   1 
ATOM 2379 O O   . ASN A 1 318 ? -62.299 23.268  -28.452 1.00 90.74  ? 326 ASN A O   1 
ATOM 2380 C CB  . ASN A 1 318 ? -60.992 20.449  -27.768 1.00 83.34  ? 326 ASN A CB  1 
ATOM 2381 C CG  . ASN A 1 318 ? -60.588 19.118  -28.376 1.00 88.01  ? 326 ASN A CG  1 
ATOM 2382 O OD1 . ASN A 1 318 ? -59.774 18.386  -27.814 1.00 93.43  ? 326 ASN A OD1 1 
ATOM 2383 N ND2 . ASN A 1 318 ? -61.151 18.803  -29.536 1.00 78.03  ? 326 ASN A ND2 1 
ATOM 2384 N N   . ASN A 1 319 ? -60.448 23.665  -27.234 1.00 90.48  ? 327 ASN A N   1 
ATOM 2385 C CA  . ASN A 1 319 ? -60.928 24.989  -26.849 1.00 96.01  ? 327 ASN A CA  1 
ATOM 2386 C C   . ASN A 1 319 ? -60.792 25.982  -27.995 1.00 91.16  ? 327 ASN A C   1 
ATOM 2387 O O   . ASN A 1 319 ? -61.611 26.900  -28.120 1.00 88.50  ? 327 ASN A O   1 
ATOM 2388 C CB  . ASN A 1 319 ? -60.172 25.501  -25.623 1.00 96.33  ? 327 ASN A CB  1 
ATOM 2389 C CG  . ASN A 1 319 ? -60.277 24.565  -24.438 1.00 98.62  ? 327 ASN A CG  1 
ATOM 2390 O OD1 . ASN A 1 319 ? -61.374 24.228  -23.994 1.00 96.89  ? 327 ASN A OD1 1 
ATOM 2391 N ND2 . ASN A 1 319 ? -59.132 24.149  -23.911 1.00 94.61  ? 327 ASN A ND2 1 
ATOM 2392 N N   . LEU A 1 320 ? -59.774 25.815  -28.834 1.00 93.60  ? 328 LEU A N   1 
ATOM 2393 C CA  . LEU A 1 320 ? -59.541 26.684  -29.979 1.00 90.68  ? 328 LEU A CA  1 
ATOM 2394 C C   . LEU A 1 320 ? -60.297 26.244  -31.225 1.00 84.77  ? 328 LEU A C   1 
ATOM 2395 O O   . LEU A 1 320 ? -60.182 26.901  -32.265 1.00 85.88  ? 328 LEU A O   1 
ATOM 2396 C CB  . LEU A 1 320 ? -58.040 26.776  -30.283 1.00 82.24  ? 328 LEU A CB  1 
ATOM 2397 C CG  . LEU A 1 320 ? -57.216 27.812  -29.510 1.00 75.86  ? 328 LEU A CG  1 
ATOM 2398 C CD1 . LEU A 1 320 ? -57.679 29.197  -29.914 1.00 83.52  ? 328 LEU A CD1 1 
ATOM 2399 C CD2 . LEU A 1 320 ? -57.308 27.654  -27.999 1.00 81.38  ? 328 LEU A CD2 1 
ATOM 2400 N N   . SER A 1 321 ? -61.062 25.161  -31.151 1.00 84.34  ? 329 SER A N   1 
ATOM 2401 C CA  . SER A 1 321 ? -61.829 24.700  -32.300 1.00 85.88  ? 329 SER A CA  1 
ATOM 2402 C C   . SER A 1 321 ? -63.108 25.517  -32.431 1.00 87.42  ? 329 SER A C   1 
ATOM 2403 O O   . SER A 1 321 ? -63.749 25.841  -31.432 1.00 82.46  ? 329 SER A O   1 
ATOM 2404 C CB  . SER A 1 321 ? -62.160 23.211  -32.174 1.00 81.74  ? 329 SER A CB  1 
ATOM 2405 O OG  . SER A 1 321 ? -60.996 22.417  -32.323 1.00 75.73  ? 329 SER A OG  1 
ATOM 2406 O OXT . SER A 1 321 ? -63.520 25.875  -33.534 1.00 88.47  ? 329 SER A OXT 1 
ATOM 2407 N N   . GLN B 1 1   ? -56.193 10.898  -59.110 1.00 83.27  ? 9   GLN B N   1 
ATOM 2408 C CA  . GLN B 1 1   ? -56.058 9.603   -59.765 1.00 87.37  ? 9   GLN B CA  1 
ATOM 2409 C C   . GLN B 1 1   ? -54.589 9.279   -60.006 1.00 85.08  ? 9   GLN B C   1 
ATOM 2410 O O   . GLN B 1 1   ? -53.840 10.103  -60.532 1.00 79.18  ? 9   GLN B O   1 
ATOM 2411 C CB  . GLN B 1 1   ? -56.827 9.585   -61.086 1.00 83.33  ? 9   GLN B CB  1 
ATOM 2412 C CG  . GLN B 1 1   ? -58.278 10.009  -60.961 1.00 80.40  ? 9   GLN B CG  1 
ATOM 2413 C CD  . GLN B 1 1   ? -58.857 10.482  -62.278 1.00 80.55  ? 9   GLN B CD  1 
ATOM 2414 O OE1 . GLN B 1 1   ? -58.921 9.726   -63.248 1.00 87.87  ? 9   GLN B OE1 1 
ATOM 2415 N NE2 . GLN B 1 1   ? -59.277 11.740  -62.322 1.00 84.70  ? 9   GLN B NE2 1 
ATOM 2416 N N   . VAL B 1 2   ? -54.184 8.069   -59.604 1.00 85.31  ? 10  VAL B N   1 
ATOM 2417 C CA  . VAL B 1 2   ? -52.750 7.654   -59.705 1.00 83.76  ? 10  VAL B CA  1 
ATOM 2418 C C   . VAL B 1 2   ? -52.513 7.646   -61.217 1.00 88.53  ? 10  VAL B C   1 
ATOM 2419 O O   . VAL B 1 2   ? -53.149 6.829   -61.912 1.00 94.93  ? 10  VAL B O   1 
ATOM 2420 C CB  . VAL B 1 2   ? -52.481 6.330   -58.965 1.00 81.21  ? 10  VAL B CB  1 
ATOM 2421 C CG1 . VAL B 1 2   ? -51.019 6.195   -58.564 1.00 75.99  ? 10  VAL B CG1 1 
ATOM 2422 C CG2 . VAL B 1 2   ? -53.383 6.171   -57.749 1.00 84.98  ? 10  VAL B CG2 1 
ATOM 2423 N N   . ALA B 1 3   ? -51.601 8.493   -61.687 1.00 86.14  ? 11  ALA B N   1 
ATOM 2424 C CA  . ALA B 1 3   ? -51.277 8.542   -63.109 1.00 80.96  ? 11  ALA B CA  1 
ATOM 2425 C C   . ALA B 1 3   ? -50.222 7.463   -63.310 1.00 77.86  ? 11  ALA B C   1 
ATOM 2426 O O   . ALA B 1 3   ? -50.228 6.760   -64.327 1.00 84.42  ? 11  ALA B O   1 
ATOM 2427 C CB  . ALA B 1 3   ? -50.737 9.912   -63.520 1.00 75.16  ? 11  ALA B CB  1 
ATOM 2428 N N   . GLU B 1 4   ? -49.308 7.317   -62.353 1.00 75.65  ? 12  GLU B N   1 
ATOM 2429 C CA  . GLU B 1 4   ? -48.303 6.268   -62.396 1.00 80.45  ? 12  GLU B CA  1 
ATOM 2430 C C   . GLU B 1 4   ? -48.066 5.748   -60.986 1.00 83.02  ? 12  GLU B C   1 
ATOM 2431 O O   . GLU B 1 4   ? -48.136 6.500   -60.011 1.00 82.19  ? 12  GLU B O   1 
ATOM 2432 C CB  . GLU B 1 4   ? -46.987 6.770   -63.008 1.00 81.09  ? 12  GLU B CB  1 
ATOM 2433 C CG  . GLU B 1 4   ? -46.914 6.607   -64.517 1.00 86.32  ? 12  GLU B CG  1 
ATOM 2434 C CD  . GLU B 1 4   ? -46.705 5.169   -64.943 1.00 90.85  ? 12  GLU B CD  1 
ATOM 2435 O OE1 . GLU B 1 4   ? -46.394 4.324   -64.078 1.00 80.83  ? 12  GLU B OE1 1 
ATOM 2436 O OE2 . GLU B 1 4   ? -46.862 4.883   -66.148 1.00 102.19 ? 12  GLU B OE2 1 
ATOM 2437 N N   . ASP B 1 5   ? -47.769 4.453   -60.890 1.00 80.68  ? 13  ASP B N   1 
ATOM 2438 C CA  . ASP B 1 5   ? -47.622 3.772   -59.603 1.00 73.79  ? 13  ASP B CA  1 
ATOM 2439 C C   . ASP B 1 5   ? -46.452 2.804   -59.738 1.00 76.15  ? 13  ASP B C   1 
ATOM 2440 O O   . ASP B 1 5   ? -46.600 1.719   -60.311 1.00 79.22  ? 13  ASP B O   1 
ATOM 2441 C CB  . ASP B 1 5   ? -48.908 3.054   -59.215 1.00 81.07  ? 13  ASP B CB  1 
ATOM 2442 C CG  . ASP B 1 5   ? -48.856 2.472   -57.815 1.00 89.46  ? 13  ASP B CG  1 
ATOM 2443 O OD1 . ASP B 1 5   ? -47.959 1.649   -57.536 1.00 93.20  ? 13  ASP B OD1 1 
ATOM 2444 O OD2 . ASP B 1 5   ? -49.713 2.848   -56.985 1.00 90.98  ? 13  ASP B OD2 1 
ATOM 2445 N N   . CYS B 1 6   ? -45.290 3.203   -59.225 1.00 75.28  ? 14  CYS B N   1 
ATOM 2446 C CA  . CYS B 1 6   ? -44.091 2.370   -59.285 1.00 79.28  ? 14  CYS B CA  1 
ATOM 2447 C C   . CYS B 1 6   ? -44.077 1.472   -58.050 1.00 79.83  ? 14  CYS B C   1 
ATOM 2448 O O   . CYS B 1 6   ? -43.624 1.877   -56.977 1.00 87.55  ? 14  CYS B O   1 
ATOM 2449 C CB  . CYS B 1 6   ? -42.852 3.255   -59.380 1.00 78.13  ? 14  CYS B CB  1 
ATOM 2450 S SG  . CYS B 1 6   ? -41.429 2.488   -60.163 1.00 86.32  ? 14  CYS B SG  1 
ATOM 2451 N N   . MET B 1 7   ? -44.572 0.241   -58.211 1.00 78.22  ? 15  MET B N   1 
ATOM 2452 C CA  . MET B 1 7   ? -44.571 -0.817  -57.195 1.00 90.04  ? 15  MET B CA  1 
ATOM 2453 C C   . MET B 1 7   ? -45.286 -0.410  -55.907 1.00 98.64  ? 15  MET B C   1 
ATOM 2454 O O   . MET B 1 7   ? -45.138 -1.078  -54.877 1.00 103.92 ? 15  MET B O   1 
ATOM 2455 C CB  . MET B 1 7   ? -43.160 -1.317  -56.852 1.00 92.15  ? 15  MET B CB  1 
ATOM 2456 C CG  . MET B 1 7   ? -42.451 -2.091  -57.950 1.00 85.52  ? 15  MET B CG  1 
ATOM 2457 S SD  . MET B 1 7   ? -40.671 -1.789  -57.956 1.00 86.77  ? 15  MET B SD  1 
ATOM 2458 C CE  . MET B 1 7   ? -40.599 -0.011  -58.080 1.00 73.77  ? 15  MET B CE  1 
ATOM 2459 N N   . GLY B 1 8   ? -46.065 0.670   -55.928 1.00 92.25  ? 16  GLY B N   1 
ATOM 2460 C CA  . GLY B 1 8   ? -46.688 1.191   -54.732 1.00 85.34  ? 16  GLY B CA  1 
ATOM 2461 C C   . GLY B 1 8   ? -45.858 2.211   -53.977 1.00 86.18  ? 16  GLY B C   1 
ATOM 2462 O O   . GLY B 1 8   ? -46.424 3.048   -53.265 1.00 84.71  ? 16  GLY B O   1 
ATOM 2463 N N   . LEU B 1 9   ? -44.529 2.154   -54.098 1.00 86.90  ? 17  LEU B N   1 
ATOM 2464 C CA  . LEU B 1 9   ? -43.668 3.048   -53.333 1.00 80.57  ? 17  LEU B CA  1 
ATOM 2465 C C   . LEU B 1 9   ? -43.639 4.459   -53.907 1.00 77.21  ? 17  LEU B C   1 
ATOM 2466 O O   . LEU B 1 9   ? -43.302 5.399   -53.180 1.00 77.21  ? 17  LEU B O   1 
ATOM 2467 C CB  . LEU B 1 9   ? -42.240 2.492   -53.257 1.00 72.80  ? 17  LEU B CB  1 
ATOM 2468 C CG  . LEU B 1 9   ? -42.003 1.104   -52.646 1.00 74.49  ? 17  LEU B CG  1 
ATOM 2469 C CD1 . LEU B 1 9   ? -42.211 -0.007  -53.659 1.00 68.80  ? 17  LEU B CD1 1 
ATOM 2470 C CD2 . LEU B 1 9   ? -40.606 1.023   -52.044 1.00 80.90  ? 17  LEU B CD2 1 
ATOM 2471 N N   . LEU B 1 10  ? -43.972 4.629   -55.186 1.00 70.92  ? 18  LEU B N   1 
ATOM 2472 C CA  . LEU B 1 10  ? -44.031 5.940   -55.818 1.00 69.35  ? 18  LEU B CA  1 
ATOM 2473 C C   . LEU B 1 10  ? -45.386 6.081   -56.494 1.00 72.45  ? 18  LEU B C   1 
ATOM 2474 O O   . LEU B 1 10  ? -45.792 5.202   -57.261 1.00 83.35  ? 18  LEU B O   1 
ATOM 2475 C CB  . LEU B 1 10  ? -42.889 6.113   -56.829 1.00 70.35  ? 18  LEU B CB  1 
ATOM 2476 C CG  . LEU B 1 10  ? -42.479 7.496   -57.354 1.00 66.94  ? 18  LEU B CG  1 
ATOM 2477 C CD1 . LEU B 1 10  ? -41.187 7.368   -58.148 1.00 64.11  ? 18  LEU B CD1 1 
ATOM 2478 C CD2 . LEU B 1 10  ? -43.551 8.173   -58.203 1.00 73.31  ? 18  LEU B CD2 1 
ATOM 2479 N N   . GLN B 1 11  ? -46.080 7.182   -56.213 1.00 69.27  ? 19  GLN B N   1 
ATOM 2480 C CA  . GLN B 1 11  ? -47.388 7.460   -56.800 1.00 72.25  ? 19  GLN B CA  1 
ATOM 2481 C C   . GLN B 1 11  ? -47.384 8.860   -57.401 1.00 70.49  ? 19  GLN B C   1 
ATOM 2482 O O   . GLN B 1 11  ? -47.428 9.854   -56.670 1.00 74.40  ? 19  GLN B O   1 
ATOM 2483 C CB  . GLN B 1 11  ? -48.497 7.315   -55.757 1.00 81.39  ? 19  GLN B CB  1 
ATOM 2484 C CG  . GLN B 1 11  ? -48.671 5.891   -55.247 1.00 88.79  ? 19  GLN B CG  1 
ATOM 2485 C CD  . GLN B 1 11  ? -49.400 5.829   -53.920 1.00 89.77  ? 19  GLN B CD  1 
ATOM 2486 O OE1 . GLN B 1 11  ? -48.820 5.465   -52.896 1.00 80.21  ? 19  GLN B OE1 1 
ATOM 2487 N NE2 . GLN B 1 11  ? -50.679 6.185   -53.930 1.00 95.35  ? 19  GLN B NE2 1 
ATOM 2488 N N   . LEU B 1 12  ? -47.327 8.937   -58.728 1.00 72.71  ? 20  LEU B N   1 
ATOM 2489 C CA  . LEU B 1 12  ? -47.467 10.198  -59.448 1.00 71.69  ? 20  LEU B CA  1 
ATOM 2490 C C   . LEU B 1 12  ? -48.943 10.407  -59.772 1.00 74.49  ? 20  LEU B C   1 
ATOM 2491 O O   . LEU B 1 12  ? -49.543 9.603   -60.493 1.00 79.28  ? 20  LEU B O   1 
ATOM 2492 C CB  . LEU B 1 12  ? -46.622 10.185  -60.723 1.00 68.31  ? 20  LEU B CB  1 
ATOM 2493 C CG  . LEU B 1 12  ? -46.888 11.187  -61.852 1.00 68.21  ? 20  LEU B CG  1 
ATOM 2494 C CD1 . LEU B 1 12  ? -47.067 12.613  -61.323 1.00 69.58  ? 20  LEU B CD1 1 
ATOM 2495 C CD2 . LEU B 1 12  ? -45.781 11.126  -62.894 1.00 66.06  ? 20  LEU B CD2 1 
ATOM 2496 N N   . LEU B 1 13  ? -49.527 11.479  -59.240 1.00 76.18  ? 21  LEU B N   1 
ATOM 2497 C CA  . LEU B 1 13  ? -50.951 11.717  -59.414 1.00 77.78  ? 21  LEU B CA  1 
ATOM 2498 C C   . LEU B 1 13  ? -51.236 12.419  -60.740 1.00 69.12  ? 21  LEU B C   1 
ATOM 2499 O O   . LEU B 1 13  ? -50.336 12.901  -61.433 1.00 70.74  ? 21  LEU B O   1 
ATOM 2500 C CB  . LEU B 1 13  ? -51.505 12.558  -58.265 1.00 82.65  ? 21  LEU B CB  1 
ATOM 2501 C CG  . LEU B 1 13  ? -51.303 12.113  -56.819 1.00 74.01  ? 21  LEU B CG  1 
ATOM 2502 C CD1 . LEU B 1 13  ? -52.200 12.932  -55.905 1.00 69.05  ? 21  LEU B CD1 1 
ATOM 2503 C CD2 . LEU B 1 13  ? -51.585 10.628  -56.656 1.00 75.29  ? 21  LEU B CD2 1 
ATOM 2504 N N   . SER B 1 14  ? -52.522 12.444  -61.098 1.00 75.73  ? 22  SER B N   1 
ATOM 2505 C CA  . SER B 1 14  ? -52.960 13.127  -62.312 1.00 91.50  ? 22  SER B CA  1 
ATOM 2506 C C   . SER B 1 14  ? -52.545 14.593  -62.302 1.00 85.03  ? 22  SER B C   1 
ATOM 2507 O O   . SER B 1 14  ? -51.971 15.098  -63.275 1.00 81.76  ? 22  SER B O   1 
ATOM 2508 C CB  . SER B 1 14  ? -54.474 12.991  -62.472 1.00 92.79  ? 22  SER B CB  1 
ATOM 2509 O OG  . SER B 1 14  ? -54.864 11.630  -62.429 1.00 88.93  ? 22  SER B OG  1 
ATOM 2510 N N   . ASN B 1 15  ? -52.825 15.295  -61.201 1.00 77.68  ? 23  ASN B N   1 
ATOM 2511 C CA  . ASN B 1 15  ? -52.404 16.687  -61.095 1.00 77.58  ? 23  ASN B CA  1 
ATOM 2512 C C   . ASN B 1 15  ? -50.895 16.815  -60.921 1.00 75.80  ? 23  ASN B C   1 
ATOM 2513 O O   . ASN B 1 15  ? -50.317 17.836  -61.313 1.00 75.17  ? 23  ASN B O   1 
ATOM 2514 C CB  . ASN B 1 15  ? -53.152 17.370  -59.949 1.00 87.35  ? 23  ASN B CB  1 
ATOM 2515 C CG  . ASN B 1 15  ? -52.830 16.768  -58.598 1.00 89.77  ? 23  ASN B CG  1 
ATOM 2516 O OD1 . ASN B 1 15  ? -52.547 15.576  -58.488 1.00 84.82  ? 23  ASN B OD1 1 
ATOM 2517 N ND2 . ASN B 1 15  ? -52.906 17.585  -57.554 1.00 91.65  ? 23  ASN B ND2 1 
ATOM 2518 N N   . GLY B 1 16  ? -50.238 15.808  -60.349 1.00 81.49  ? 24  GLY B N   1 
ATOM 2519 C CA  . GLY B 1 16  ? -48.792 15.872  -60.258 1.00 84.00  ? 24  GLY B CA  1 
ATOM 2520 C C   . GLY B 1 16  ? -48.214 16.338  -58.937 1.00 77.41  ? 24  GLY B C   1 
ATOM 2521 O O   . GLY B 1 16  ? -47.592 17.401  -58.882 1.00 80.07  ? 24  GLY B O   1 
ATOM 2522 N N   . THR B 1 17  ? -48.436 15.557  -57.873 1.00 71.72  ? 25  THR B N   1 
ATOM 2523 C CA  . THR B 1 17  ? -47.879 15.896  -56.542 1.00 80.60  ? 25  THR B CA  1 
ATOM 2524 C C   . THR B 1 17  ? -46.767 14.925  -56.220 1.00 75.66  ? 25  THR B C   1 
ATOM 2525 O O   . THR B 1 17  ? -45.780 15.375  -55.596 1.00 72.68  ? 25  THR B O   1 
ATOM 2526 C CB  . THR B 1 17  ? -48.972 15.844  -55.475 1.00 79.48  ? 25  THR B CB  1 
ATOM 2527 O OG1 . THR B 1 17  ? -49.188 14.458  -55.232 1.00 78.72  ? 25  THR B OG1 1 
ATOM 2528 C CG2 . THR B 1 17  ? -50.262 16.504  -55.924 1.00 74.68  ? 25  THR B CG2 1 
ATOM 2529 N N   . VAL B 1 18  ? -46.924 13.651  -56.606 1.00 68.46  ? 26  VAL B N   1 
ATOM 2530 C CA  . VAL B 1 18  ? -45.892 12.587  -56.371 1.00 65.04  ? 26  VAL B CA  1 
ATOM 2531 C C   . VAL B 1 18  ? -45.878 12.182  -54.884 1.00 66.48  ? 26  VAL B C   1 
ATOM 2532 O O   . VAL B 1 18  ? -45.485 13.015  -54.038 1.00 61.67  ? 26  VAL B O   1 
ATOM 2533 C CB  . VAL B 1 18  ? -44.469 12.922  -56.864 1.00 63.86  ? 26  VAL B CB  1 
ATOM 2534 C CG1 . VAL B 1 18  ? -43.565 11.699  -56.787 1.00 56.28  ? 26  VAL B CG1 1 
ATOM 2535 C CG2 . VAL B 1 18  ? -44.477 13.500  -58.274 1.00 68.32  ? 26  VAL B CG2 1 
ATOM 2536 N N   . LEU B 1 19  ? -46.266 10.938  -54.589 1.00 68.06  ? 27  LEU B N   1 
ATOM 2537 C CA  . LEU B 1 19  ? -46.238 10.435  -53.190 1.00 59.45  ? 27  LEU B CA  1 
ATOM 2538 C C   . LEU B 1 19  ? -45.128 9.379   -53.071 1.00 58.36  ? 27  LEU B C   1 
ATOM 2539 O O   . LEU B 1 19  ? -44.777 8.774   -54.108 1.00 70.29  ? 27  LEU B O   1 
ATOM 2540 C CB  . LEU B 1 19  ? -47.602 9.855   -52.824 1.00 64.79  ? 27  LEU B CB  1 
ATOM 2541 C CG  . LEU B 1 19  ? -48.611 10.843  -52.230 1.00 68.89  ? 27  LEU B CG  1 
ATOM 2542 C CD1 . LEU B 1 19  ? -47.909 11.905  -51.404 1.00 70.94  ? 27  LEU B CD1 1 
ATOM 2543 C CD2 . LEU B 1 19  ? -49.461 11.481  -53.315 1.00 66.52  ? 27  LEU B CD2 1 
ATOM 2544 N N   . ARG B 1 20  ? -44.602 9.168   -51.860 1.00 58.37  ? 28  ARG B N   1 
ATOM 2545 C CA  . ARG B 1 20  ? -43.557 8.172   -51.667 1.00 68.06  ? 28  ARG B CA  1 
ATOM 2546 C C   . ARG B 1 20  ? -43.837 7.385   -50.393 1.00 74.72  ? 28  ARG B C   1 
ATOM 2547 O O   . ARG B 1 20  ? -44.789 7.664   -49.661 1.00 73.11  ? 28  ARG B O   1 
ATOM 2548 C CB  . ARG B 1 20  ? -42.172 8.828   -51.626 1.00 69.53  ? 28  ARG B CB  1 
ATOM 2549 C CG  . ARG B 1 20  ? -41.052 7.924   -52.113 1.00 68.12  ? 28  ARG B CG  1 
ATOM 2550 C CD  . ARG B 1 20  ? -40.722 8.179   -53.571 1.00 65.91  ? 28  ARG B CD  1 
ATOM 2551 N NE  . ARG B 1 20  ? -39.980 9.421   -53.747 1.00 68.32  ? 28  ARG B NE  1 
ATOM 2552 C CZ  . ARG B 1 20  ? -39.348 9.759   -54.862 1.00 57.74  ? 28  ARG B CZ  1 
ATOM 2553 N NH1 . ARG B 1 20  ? -39.363 8.977   -55.928 1.00 51.35  ? 28  ARG B NH1 1 
ATOM 2554 N NH2 . ARG B 1 20  ? -38.687 10.912  -54.908 1.00 57.99  ? 28  ARG B NH2 1 
ATOM 2555 N N   . SER B 1 21  ? -43.000 6.386   -50.134 1.00 79.00  ? 29  SER B N   1 
ATOM 2556 C CA  . SER B 1 21  ? -43.178 5.509   -48.983 1.00 80.52  ? 29  SER B CA  1 
ATOM 2557 C C   . SER B 1 21  ? -41.836 5.210   -48.321 1.00 78.84  ? 29  SER B C   1 
ATOM 2558 O O   . SER B 1 21  ? -41.212 4.184   -48.591 1.00 69.04  ? 29  SER B O   1 
ATOM 2559 C CB  . SER B 1 21  ? -43.864 4.206   -49.398 1.00 77.31  ? 29  SER B CB  1 
ATOM 2560 O OG  . SER B 1 21  ? -45.176 4.447   -49.881 1.00 67.44  ? 29  SER B OG  1 
ATOM 2561 N N   . ASN B 1 35  ? -22.097 -8.758  -44.241 1.00 71.10  ? 43  ASN B N   1 
ATOM 2562 C CA  . ASN B 1 35  ? -22.652 -7.978  -43.145 1.00 72.61  ? 43  ASN B CA  1 
ATOM 2563 C C   . ASN B 1 35  ? -21.611 -7.844  -42.039 1.00 80.02  ? 43  ASN B C   1 
ATOM 2564 O O   . ASN B 1 35  ? -21.878 -8.169  -40.882 1.00 79.68  ? 43  ASN B O   1 
ATOM 2565 C CB  . ASN B 1 35  ? -23.908 -8.662  -42.602 1.00 71.71  ? 43  ASN B CB  1 
ATOM 2566 C CG  . ASN B 1 35  ? -24.933 -8.945  -43.685 1.00 70.19  ? 43  ASN B CG  1 
ATOM 2567 O OD1 . ASN B 1 35  ? -24.715 -8.633  -44.856 1.00 75.25  ? 43  ASN B OD1 1 
ATOM 2568 N ND2 . ASN B 1 35  ? -26.038 -9.578  -43.306 1.00 61.28  ? 43  ASN B ND2 1 
ATOM 2569 N N   . ASN B 1 36  ? -20.415 -7.375  -42.398 1.00 83.11  ? 44  ASN B N   1 
ATOM 2570 C CA  . ASN B 1 36  ? -19.374 -7.133  -41.406 1.00 82.04  ? 44  ASN B CA  1 
ATOM 2571 C C   . ASN B 1 36  ? -19.082 -5.633  -41.417 1.00 85.46  ? 44  ASN B C   1 
ATOM 2572 O O   . ASN B 1 36  ? -19.846 -4.842  -41.981 1.00 81.59  ? 44  ASN B O   1 
ATOM 2573 C CB  . ASN B 1 36  ? -18.059 -7.757  -41.876 1.00 90.48  ? 44  ASN B CB  1 
ATOM 2574 C CG  . ASN B 1 36  ? -17.165 -8.155  -40.723 1.00 96.27  ? 44  ASN B CG  1 
ATOM 2575 O OD1 . ASN B 1 36  ? -16.165 -7.499  -40.440 1.00 98.86  ? 44  ASN B OD1 1 
ATOM 2576 N ND2 . ASN B 1 36  ? -17.540 -9.225  -40.029 1.00 92.59  ? 44  ASN B ND2 1 
ATOM 2577 N N   . GLN B 1 37  ? -18.077 -5.213  -40.653 1.00 94.29  ? 45  GLN B N   1 
ATOM 2578 C CA  . GLN B 1 37  ? -17.907 -3.745  -40.525 1.00 97.45  ? 45  GLN B CA  1 
ATOM 2579 C C   . GLN B 1 37  ? -16.446 -3.311  -40.490 1.00 102.89 ? 45  GLN B C   1 
ATOM 2580 O O   . GLN B 1 37  ? -15.788 -3.537  -39.455 1.00 104.95 ? 45  GLN B O   1 
ATOM 2581 C CB  . GLN B 1 37  ? -18.554 -3.244  -39.232 1.00 95.36  ? 45  GLN B CB  1 
ATOM 2582 C CG  . GLN B 1 37  ? -20.074 -3.362  -39.199 1.00 96.30  ? 45  GLN B CG  1 
ATOM 2583 C CD  . GLN B 1 37  ? -20.676 -2.926  -37.881 1.00 93.60  ? 45  GLN B CD  1 
ATOM 2584 O OE1 . GLN B 1 37  ? -20.023 -2.959  -36.833 1.00 94.83  ? 45  GLN B OE1 1 
ATOM 2585 N NE2 . GLN B 1 37  ? -21.931 -2.504  -37.925 1.00 85.92  ? 45  GLN B NE2 1 
ATOM 2586 N N   . THR B 1 38  ? -15.972 -2.707  -41.574 1.00 109.98 ? 46  THR B N   1 
ATOM 2587 C CA  . THR B 1 38  ? -14.626 -2.106  -41.568 1.00 106.35 ? 46  THR B CA  1 
ATOM 2588 C C   . THR B 1 38  ? -14.827 -0.706  -42.083 1.00 107.45 ? 46  THR B C   1 
ATOM 2589 O O   . THR B 1 38  ? -16.003 -0.294  -42.150 1.00 114.59 ? 46  THR B O   1 
ATOM 2590 C CB  . THR B 1 38  ? -13.664 -2.896  -42.448 1.00 107.35 ? 46  THR B CB  1 
ATOM 2591 O OG1 . THR B 1 38  ? -14.386 -3.140  -43.651 1.00 103.90 ? 46  THR B OG1 1 
ATOM 2592 C CG2 . THR B 1 38  ? -13.236 -4.208  -41.816 1.00 104.34 ? 46  THR B CG2 1 
ATOM 2593 N N   . VAL B 1 39  ? -13.762 -0.012  -42.500 1.00 104.46 ? 47  VAL B N   1 
ATOM 2594 C CA  . VAL B 1 39  ? -13.848 1.344   -43.148 1.00 112.82 ? 47  VAL B CA  1 
ATOM 2595 C C   . VAL B 1 39  ? -14.491 2.418   -42.245 1.00 109.54 ? 47  VAL B C   1 
ATOM 2596 O O   . VAL B 1 39  ? -15.043 2.075   -41.179 1.00 108.41 ? 47  VAL B O   1 
ATOM 2597 C CB  . VAL B 1 39  ? -14.494 1.337   -44.557 1.00 107.32 ? 47  VAL B CB  1 
ATOM 2598 C CG1 . VAL B 1 39  ? -14.259 0.034   -45.309 1.00 101.87 ? 47  VAL B CG1 1 
ATOM 2599 C CG2 . VAL B 1 39  ? -15.969 1.722   -44.565 1.00 102.80 ? 47  VAL B CG2 1 
ATOM 2600 N N   . LEU B 1 40  ? -14.369 3.690   -42.645 1.00 106.55 ? 48  LEU B N   1 
ATOM 2601 C CA  . LEU B 1 40  ? -14.990 4.807   -41.887 1.00 103.91 ? 48  LEU B CA  1 
ATOM 2602 C C   . LEU B 1 40  ? -15.722 5.711   -42.889 1.00 103.09 ? 48  LEU B C   1 
ATOM 2603 O O   . LEU B 1 40  ? -15.292 5.750   -44.061 1.00 101.43 ? 48  LEU B O   1 
ATOM 2604 C CB  . LEU B 1 40  ? -13.915 5.569   -41.116 1.00 105.67 ? 48  LEU B CB  1 
ATOM 2605 C CG  . LEU B 1 40  ? -12.709 6.050   -41.928 1.00 108.53 ? 48  LEU B CG  1 
ATOM 2606 C CD1 . LEU B 1 40  ? -12.751 7.549   -42.157 1.00 104.63 ? 48  LEU B CD1 1 
ATOM 2607 C CD2 . LEU B 1 40  ? -11.408 5.651   -41.260 1.00 109.08 ? 48  LEU B CD2 1 
ATOM 2608 N N   . PHE B 1 41  ? -16.777 6.410   -42.458 1.00 99.54  ? 49  PHE B N   1 
ATOM 2609 C CA  . PHE B 1 41  ? -17.571 7.206   -43.431 1.00 91.54  ? 49  PHE B CA  1 
ATOM 2610 C C   . PHE B 1 41  ? -18.178 8.448   -42.809 1.00 89.10  ? 49  PHE B C   1 
ATOM 2611 O O   . PHE B 1 41  ? -18.550 8.411   -41.621 1.00 93.75  ? 49  PHE B O   1 
ATOM 2612 C CB  . PHE B 1 41  ? -18.724 6.376   -43.999 1.00 91.92  ? 49  PHE B CB  1 
ATOM 2613 C CG  . PHE B 1 41  ? -19.217 5.203   -43.165 1.00 89.66  ? 49  PHE B CG  1 
ATOM 2614 C CD1 . PHE B 1 41  ? -18.665 3.938   -43.316 1.00 97.39  ? 49  PHE B CD1 1 
ATOM 2615 C CD2 . PHE B 1 41  ? -20.253 5.364   -42.256 1.00 93.31  ? 49  PHE B CD2 1 
ATOM 2616 C CE1 . PHE B 1 41  ? -19.119 2.872   -42.560 1.00 100.99 ? 49  PHE B CE1 1 
ATOM 2617 C CE2 . PHE B 1 41  ? -20.707 4.293   -41.505 1.00 101.43 ? 49  PHE B CE2 1 
ATOM 2618 C CZ  . PHE B 1 41  ? -20.140 3.050   -41.659 1.00 104.28 ? 49  PHE B CZ  1 
ATOM 2619 N N   . LYS B 1 42  ? -18.275 9.529   -43.588 1.00 91.15  ? 50  LYS B N   1 
ATOM 2620 C CA  . LYS B 1 42  ? -18.969 10.728  -43.126 1.00 90.77  ? 50  LYS B CA  1 
ATOM 2621 C C   . LYS B 1 42  ? -19.524 11.464  -44.340 1.00 91.91  ? 50  LYS B C   1 
ATOM 2622 O O   . LYS B 1 42  ? -19.084 11.245  -45.471 1.00 97.68  ? 50  LYS B O   1 
ATOM 2623 C CB  . LYS B 1 42  ? -18.046 11.645  -42.318 1.00 93.92  ? 50  LYS B CB  1 
ATOM 2624 C CG  . LYS B 1 42  ? -16.765 11.993  -43.025 1.00 92.64  ? 50  LYS B CG  1 
ATOM 2625 C CD  . LYS B 1 42  ? -16.007 13.103  -42.318 1.00 97.27  ? 50  LYS B CD  1 
ATOM 2626 C CE  . LYS B 1 42  ? -15.653 12.695  -40.896 1.00 91.34  ? 50  LYS B CE  1 
ATOM 2627 N NZ  . LYS B 1 42  ? -15.167 13.833  -40.068 1.00 86.08  ? 50  LYS B NZ  1 
ATOM 2628 N N   . ASP B 1 43  ? -20.493 12.345  -44.091 1.00 83.40  ? 51  ASP B N   1 
ATOM 2629 C CA  . ASP B 1 43  ? -21.264 12.996  -45.144 1.00 81.20  ? 51  ASP B CA  1 
ATOM 2630 C C   . ASP B 1 43  ? -20.947 14.485  -45.221 1.00 80.57  ? 51  ASP B C   1 
ATOM 2631 O O   . ASP B 1 43  ? -20.391 15.074  -44.289 1.00 86.58  ? 51  ASP B O   1 
ATOM 2632 C CB  . ASP B 1 43  ? -22.769 12.809  -44.917 1.00 81.09  ? 51  ASP B CB  1 
ATOM 2633 C CG  . ASP B 1 43  ? -23.187 11.356  -44.959 1.00 84.28  ? 51  ASP B CG  1 
ATOM 2634 O OD1 . ASP B 1 43  ? -22.297 10.482  -44.991 1.00 85.17  ? 51  ASP B OD1 1 
ATOM 2635 O OD2 . ASP B 1 43  ? -24.406 11.089  -44.965 1.00 84.52  ? 51  ASP B OD2 1 
ATOM 2636 N N   . SER B 1 44  ? -21.316 15.092  -46.352 1.00 69.78  ? 52  SER B N   1 
ATOM 2637 C CA  . SER B 1 44  ? -21.107 16.519  -46.564 1.00 73.54  ? 52  SER B CA  1 
ATOM 2638 C C   . SER B 1 44  ? -22.002 17.009  -47.695 1.00 72.98  ? 52  SER B C   1 
ATOM 2639 O O   . SER B 1 44  ? -22.464 16.230  -48.532 1.00 72.50  ? 52  SER B O   1 
ATOM 2640 C CB  . SER B 1 44  ? -19.642 16.838  -46.874 1.00 78.50  ? 52  SER B CB  1 
ATOM 2641 O OG  . SER B 1 44  ? -19.474 18.223  -47.130 1.00 81.50  ? 52  SER B OG  1 
ATOM 2642 N N   . ILE B 1 45  ? -22.231 18.326  -47.706 1.00 73.22  ? 53  ILE B N   1 
ATOM 2643 C CA  . ILE B 1 45  ? -22.919 18.976  -48.820 1.00 73.19  ? 53  ILE B CA  1 
ATOM 2644 C C   . ILE B 1 45  ? -21.996 19.064  -50.033 1.00 78.01  ? 53  ILE B C   1 
ATOM 2645 O O   . ILE B 1 45  ? -20.764 19.105  -49.907 1.00 82.78  ? 53  ILE B O   1 
ATOM 2646 C CB  . ILE B 1 45  ? -23.426 20.372  -48.408 1.00 68.90  ? 53  ILE B CB  1 
ATOM 2647 C CG1 . ILE B 1 45  ? -24.714 20.719  -49.161 1.00 67.59  ? 53  ILE B CG1 1 
ATOM 2648 C CG2 . ILE B 1 45  ? -22.359 21.440  -48.634 1.00 72.73  ? 53  ILE B CG2 1 
ATOM 2649 C CD1 . ILE B 1 45  ? -25.523 21.818  -48.506 1.00 64.47  ? 53  ILE B CD1 1 
ATOM 2650 N N   . TYR B 1 46  ? -22.592 19.038  -51.230 1.00 76.27  ? 54  TYR B N   1 
ATOM 2651 C CA  . TYR B 1 46  ? -21.865 19.393  -52.445 1.00 71.63  ? 54  TYR B CA  1 
ATOM 2652 C C   . TYR B 1 46  ? -22.574 20.419  -53.317 1.00 71.92  ? 54  TYR B C   1 
ATOM 2653 O O   . TYR B 1 46  ? -21.930 20.982  -54.212 1.00 82.81  ? 54  TYR B O   1 
ATOM 2654 C CB  . TYR B 1 46  ? -21.554 18.136  -53.283 1.00 71.40  ? 54  TYR B CB  1 
ATOM 2655 C CG  . TYR B 1 46  ? -22.709 17.440  -54.002 1.00 73.82  ? 54  TYR B CG  1 
ATOM 2656 C CD1 . TYR B 1 46  ? -23.398 18.057  -55.043 1.00 76.78  ? 54  TYR B CD1 1 
ATOM 2657 C CD2 . TYR B 1 46  ? -23.111 16.163  -53.632 1.00 75.78  ? 54  TYR B CD2 1 
ATOM 2658 C CE1 . TYR B 1 46  ? -24.431 17.418  -55.700 1.00 75.87  ? 54  TYR B CE1 1 
ATOM 2659 C CE2 . TYR B 1 46  ? -24.143 15.519  -54.280 1.00 76.00  ? 54  TYR B CE2 1 
ATOM 2660 C CZ  . TYR B 1 46  ? -24.801 16.149  -55.311 1.00 74.96  ? 54  TYR B CZ  1 
ATOM 2661 O OH  . TYR B 1 46  ? -25.832 15.500  -55.950 1.00 74.32  ? 54  TYR B OH  1 
ATOM 2662 N N   . HIS B 1 47  ? -23.864 20.678  -53.100 1.00 67.82  ? 55  HIS B N   1 
ATOM 2663 C CA  . HIS B 1 47  ? -24.607 21.678  -53.864 1.00 67.32  ? 55  HIS B CA  1 
ATOM 2664 C C   . HIS B 1 47  ? -25.598 22.336  -52.914 1.00 69.06  ? 55  HIS B C   1 
ATOM 2665 O O   . HIS B 1 47  ? -26.601 21.724  -52.537 1.00 72.61  ? 55  HIS B O   1 
ATOM 2666 C CB  . HIS B 1 47  ? -25.323 21.045  -55.058 1.00 62.33  ? 55  HIS B CB  1 
ATOM 2667 C CG  . HIS B 1 47  ? -25.853 22.039  -56.045 1.00 71.87  ? 55  HIS B CG  1 
ATOM 2668 N ND1 . HIS B 1 47  ? -25.224 23.237  -56.306 1.00 81.54  ? 55  HIS B ND1 1 
ATOM 2669 C CD2 . HIS B 1 47  ? -26.956 22.015  -56.830 1.00 75.83  ? 55  HIS B CD2 1 
ATOM 2670 C CE1 . HIS B 1 47  ? -25.911 23.903  -57.217 1.00 78.33  ? 55  HIS B CE1 1 
ATOM 2671 N NE2 . HIS B 1 47  ? -26.968 23.185  -57.549 1.00 77.05  ? 55  HIS B NE2 1 
ATOM 2672 N N   . LYS B 1 48  ? -25.310 23.583  -52.527 1.00 71.93  ? 56  LYS B N   1 
ATOM 2673 C CA  . LYS B 1 48  ? -26.171 24.290  -51.576 1.00 70.67  ? 56  LYS B CA  1 
ATOM 2674 C C   . LYS B 1 48  ? -27.521 24.697  -52.159 1.00 70.37  ? 56  LYS B C   1 
ATOM 2675 O O   . LYS B 1 48  ? -28.541 24.514  -51.471 1.00 69.73  ? 56  LYS B O   1 
ATOM 2676 C CB  . LYS B 1 48  ? -25.430 25.510  -51.017 1.00 75.49  ? 56  LYS B CB  1 
ATOM 2677 C CG  . LYS B 1 48  ? -24.229 25.182  -50.148 1.00 84.50  ? 56  LYS B CG  1 
ATOM 2678 C CD  . LYS B 1 48  ? -23.541 26.455  -49.668 1.00 100.60 ? 56  LYS B CD  1 
ATOM 2679 C CE  . LYS B 1 48  ? -22.347 26.144  -48.778 1.00 95.30  ? 56  LYS B CE  1 
ATOM 2680 N NZ  . LYS B 1 48  ? -21.643 27.375  -48.317 1.00 108.44 ? 56  LYS B NZ  1 
ATOM 2681 N N   . PRO B 1 49  ? -27.614 25.269  -53.369 1.00 71.06  ? 57  PRO B N   1 
ATOM 2682 C CA  . PRO B 1 49  ? -28.929 25.743  -53.844 1.00 72.72  ? 57  PRO B CA  1 
ATOM 2683 C C   . PRO B 1 49  ? -30.014 24.679  -53.871 1.00 71.91  ? 57  PRO B C   1 
ATOM 2684 O O   . PRO B 1 49  ? -31.187 25.009  -53.650 1.00 72.18  ? 57  PRO B O   1 
ATOM 2685 C CB  . PRO B 1 49  ? -28.625 26.268  -55.254 1.00 75.10  ? 57  PRO B CB  1 
ATOM 2686 C CG  . PRO B 1 49  ? -27.186 26.611  -55.228 1.00 71.94  ? 57  PRO B CG  1 
ATOM 2687 C CD  . PRO B 1 49  ? -26.542 25.614  -54.323 1.00 72.27  ? 57  PRO B CD  1 
ATOM 2688 N N   . ASN B 1 50  ? -29.675 23.417  -54.126 1.00 74.54  ? 58  ASN B N   1 
ATOM 2689 C CA  . ASN B 1 50  ? -30.661 22.347  -54.099 1.00 73.18  ? 58  ASN B CA  1 
ATOM 2690 C C   . ASN B 1 50  ? -30.515 21.418  -52.899 1.00 70.28  ? 58  ASN B C   1 
ATOM 2691 O O   . ASN B 1 50  ? -31.321 20.493  -52.753 1.00 67.23  ? 58  ASN B O   1 
ATOM 2692 C CB  . ASN B 1 50  ? -30.599 21.539  -55.401 1.00 66.36  ? 58  ASN B CB  1 
ATOM 2693 C CG  . ASN B 1 50  ? -30.853 22.390  -56.627 1.00 72.55  ? 58  ASN B CG  1 
ATOM 2694 O OD1 . ASN B 1 50  ? -31.387 23.495  -56.529 1.00 78.90  ? 58  ASN B OD1 1 
ATOM 2695 N ND2 . ASN B 1 50  ? -30.478 21.876  -57.793 1.00 72.02  ? 58  ASN B ND2 1 
ATOM 2696 N N   . ASN B 1 51  ? -29.535 21.658  -52.024 1.00 67.05  ? 59  ASN B N   1 
ATOM 2697 C CA  . ASN B 1 51  ? -29.343 20.892  -50.789 1.00 71.26  ? 59  ASN B CA  1 
ATOM 2698 C C   . ASN B 1 51  ? -29.105 19.404  -51.071 1.00 72.05  ? 59  ASN B C   1 
ATOM 2699 O O   . ASN B 1 51  ? -29.863 18.527  -50.647 1.00 75.70  ? 59  ASN B O   1 
ATOM 2700 C CB  . ASN B 1 51  ? -30.527 21.102  -49.837 1.00 68.56  ? 59  ASN B CB  1 
ATOM 2701 C CG  . ASN B 1 51  ? -30.306 20.472  -48.477 1.00 73.85  ? 59  ASN B CG  1 
ATOM 2702 O OD1 . ASN B 1 51  ? -29.312 20.748  -47.806 1.00 73.30  ? 59  ASN B OD1 1 
ATOM 2703 N ND2 . ASN B 1 51  ? -31.235 19.618  -48.063 1.00 79.24  ? 59  ASN B ND2 1 
ATOM 2704 N N   . LEU B 1 52  ? -28.035 19.136  -51.818 1.00 68.61  ? 60  LEU B N   1 
ATOM 2705 C CA  . LEU B 1 52  ? -27.623 17.784  -52.183 1.00 68.71  ? 60  LEU B CA  1 
ATOM 2706 C C   . LEU B 1 52  ? -26.361 17.400  -51.420 1.00 72.69  ? 60  LEU B C   1 
ATOM 2707 O O   . LEU B 1 52  ? -25.407 18.183  -51.351 1.00 73.41  ? 60  LEU B O   1 
ATOM 2708 C CB  . LEU B 1 52  ? -27.396 17.656  -53.690 1.00 67.38  ? 60  LEU B CB  1 
ATOM 2709 C CG  . LEU B 1 52  ? -28.599 17.431  -54.613 1.00 74.55  ? 60  LEU B CG  1 
ATOM 2710 C CD1 . LEU B 1 52  ? -29.726 18.383  -54.383 1.00 71.50  ? 60  LEU B CD1 1 
ATOM 2711 C CD2 . LEU B 1 52  ? -28.131 17.573  -56.050 1.00 72.92  ? 60  LEU B CD2 1 
ATOM 2712 N N   . HIS B 1 53  ? -26.367 16.199  -50.842 1.00 70.69  ? 61  HIS B N   1 
ATOM 2713 C CA  . HIS B 1 53  ? -25.293 15.719  -49.986 1.00 71.45  ? 61  HIS B CA  1 
ATOM 2714 C C   . HIS B 1 53  ? -24.681 14.446  -50.560 1.00 74.20  ? 61  HIS B C   1 
ATOM 2715 O O   . HIS B 1 53  ? -25.364 13.646  -51.206 1.00 74.80  ? 61  HIS B O   1 
ATOM 2716 C CB  . HIS B 1 53  ? -25.808 15.458  -48.568 1.00 74.80  ? 61  HIS B CB  1 
ATOM 2717 C CG  . HIS B 1 53  ? -26.504 16.636  -47.960 1.00 74.60  ? 61  HIS B CG  1 
ATOM 2718 N ND1 . HIS B 1 53  ? -25.863 17.829  -47.703 1.00 73.12  ? 61  HIS B ND1 1 
ATOM 2719 C CD2 . HIS B 1 53  ? -27.787 16.804  -47.561 1.00 71.69  ? 61  HIS B CD2 1 
ATOM 2720 C CE1 . HIS B 1 53  ? -26.722 18.681  -47.171 1.00 75.45  ? 61  HIS B CE1 1 
ATOM 2721 N NE2 . HIS B 1 53  ? -27.896 18.083  -47.074 1.00 73.81  ? 61  HIS B NE2 1 
ATOM 2722 N N   . LEU B 1 54  ? -23.381 14.269  -50.324 1.00 74.87  ? 62  LEU B N   1 
ATOM 2723 C CA  . LEU B 1 54  ? -22.669 13.050  -50.683 1.00 74.33  ? 62  LEU B CA  1 
ATOM 2724 C C   . LEU B 1 54  ? -21.970 12.471  -49.456 1.00 75.85  ? 62  LEU B C   1 
ATOM 2725 O O   . LEU B 1 54  ? -21.807 13.141  -48.433 1.00 76.53  ? 62  LEU B O   1 
ATOM 2726 C CB  . LEU B 1 54  ? -21.660 13.297  -51.819 1.00 69.75  ? 62  LEU B CB  1 
ATOM 2727 C CG  . LEU B 1 54  ? -20.562 14.355  -51.729 1.00 68.60  ? 62  LEU B CG  1 
ATOM 2728 C CD1 . LEU B 1 54  ? -19.371 13.758  -51.068 1.00 73.76  ? 62  LEU B CD1 1 
ATOM 2729 C CD2 . LEU B 1 54  ? -20.154 14.819  -53.113 1.00 71.53  ? 62  LEU B CD2 1 
ATOM 2730 N N   . ARG B 1 55  ? -21.569 11.204  -49.568 1.00 72.50  ? 63  ARG B N   1 
ATOM 2731 C CA  . ARG B 1 55  ? -20.899 10.475  -48.496 1.00 82.00  ? 63  ARG B CA  1 
ATOM 2732 C C   . ARG B 1 55  ? -19.504 10.032  -48.925 1.00 86.54  ? 63  ARG B C   1 
ATOM 2733 O O   . ARG B 1 55  ? -19.301 9.617   -50.070 1.00 85.61  ? 63  ARG B O   1 
ATOM 2734 C CB  . ARG B 1 55  ? -21.746 9.263   -48.073 1.00 82.57  ? 63  ARG B CB  1 
ATOM 2735 C CG  . ARG B 1 55  ? -21.150 8.405   -46.967 1.00 85.73  ? 63  ARG B CG  1 
ATOM 2736 C CD  . ARG B 1 55  ? -22.217 7.523   -46.320 1.00 82.88  ? 63  ARG B CD  1 
ATOM 2737 N NE  . ARG B 1 55  ? -23.269 8.328   -45.708 1.00 74.43  ? 63  ARG B NE  1 
ATOM 2738 C CZ  . ARG B 1 55  ? -24.350 7.838   -45.114 1.00 74.77  ? 63  ARG B CZ  1 
ATOM 2739 N NH1 . ARG B 1 55  ? -24.561 6.537   -45.025 1.00 80.12  ? 63  ARG B NH1 1 
ATOM 2740 N NH2 . ARG B 1 55  ? -25.238 8.678   -44.588 1.00 75.01  ? 63  ARG B NH2 1 
ATOM 2741 N N   . LEU B 1 56  ? -18.544 10.124  -48.003 1.00 90.94  ? 64  LEU B N   1 
ATOM 2742 C CA  . LEU B 1 56  ? -17.162 9.715   -48.238 1.00 92.75  ? 64  LEU B CA  1 
ATOM 2743 C C   . LEU B 1 56  ? -16.872 8.446   -47.448 1.00 97.82  ? 64  LEU B C   1 
ATOM 2744 O O   . LEU B 1 56  ? -17.245 8.348   -46.277 1.00 96.69  ? 64  LEU B O   1 
ATOM 2745 C CB  . LEU B 1 56  ? -16.158 10.792  -47.809 1.00 88.64  ? 64  LEU B CB  1 
ATOM 2746 C CG  . LEU B 1 56  ? -15.834 12.055  -48.617 1.00 85.61  ? 64  LEU B CG  1 
ATOM 2747 C CD1 . LEU B 1 56  ? -15.142 11.766  -49.954 1.00 91.18  ? 64  LEU B CD1 1 
ATOM 2748 C CD2 . LEU B 1 56  ? -17.028 12.974  -48.756 1.00 82.55  ? 64  LEU B CD2 1 
ATOM 2749 N N   . TYR B 1 57  ? -16.222 7.476   -48.088 1.00 97.11  ? 65  TYR B N   1 
ATOM 2750 C CA  . TYR B 1 57  ? -15.759 6.256   -47.435 1.00 97.72  ? 65  TYR B CA  1 
ATOM 2751 C C   . TYR B 1 57  ? -14.241 6.195   -47.523 1.00 105.25 ? 65  TYR B C   1 
ATOM 2752 O O   . TYR B 1 57  ? -13.685 6.434   -48.595 1.00 100.50 ? 65  TYR B O   1 
ATOM 2753 C CB  . TYR B 1 57  ? -16.363 5.013   -48.097 1.00 95.08  ? 65  TYR B CB  1 
ATOM 2754 C CG  . TYR B 1 57  ? -17.858 4.885   -47.944 1.00 92.48  ? 65  TYR B CG  1 
ATOM 2755 C CD1 . TYR B 1 57  ? -18.721 5.628   -48.738 1.00 90.57  ? 65  TYR B CD1 1 
ATOM 2756 C CD2 . TYR B 1 57  ? -18.407 4.002   -47.024 1.00 96.22  ? 65  TYR B CD2 1 
ATOM 2757 C CE1 . TYR B 1 57  ? -20.090 5.511   -48.603 1.00 95.18  ? 65  TYR B CE1 1 
ATOM 2758 C CE2 . TYR B 1 57  ? -19.776 3.875   -46.885 1.00 91.51  ? 65  TYR B CE2 1 
ATOM 2759 C CZ  . TYR B 1 57  ? -20.612 4.633   -47.677 1.00 94.17  ? 65  TYR B CZ  1 
ATOM 2760 O OH  . TYR B 1 57  ? -21.976 4.514   -47.551 1.00 93.60  ? 65  TYR B OH  1 
ATOM 2761 N N   . LYS B 1 58  ? -13.563 5.901   -46.412 1.00 109.13 ? 66  LYS B N   1 
ATOM 2762 C CA  . LYS B 1 58  ? -12.113 5.706   -46.448 1.00 110.83 ? 66  LYS B CA  1 
ATOM 2763 C C   . LYS B 1 58  ? -11.817 4.406   -45.704 1.00 110.51 ? 66  LYS B C   1 
ATOM 2764 O O   . LYS B 1 58  ? -12.186 4.275   -44.521 1.00 110.68 ? 66  LYS B O   1 
ATOM 2765 C CB  . LYS B 1 58  ? -11.356 6.892   -45.846 1.00 109.73 ? 66  LYS B CB  1 
ATOM 2766 C CG  . LYS B 1 58  ? -9.875  6.635   -45.637 1.00 111.75 ? 66  LYS B CG  1 
ATOM 2767 C CD  . LYS B 1 58  ? -9.233  7.703   -44.775 1.00 115.09 ? 66  LYS B CD  1 
ATOM 2768 C CE  . LYS B 1 58  ? -7.801  7.334   -44.425 1.00 116.31 ? 66  LYS B CE  1 
ATOM 2769 N NZ  . LYS B 1 58  ? -7.207  8.268   -43.433 1.00 115.92 ? 66  LYS B NZ  1 
ATOM 2770 N N   . PRO B 1 59  ? -11.150 3.438   -46.344 1.00 112.93 ? 67  PRO B N   1 
ATOM 2771 C CA  . PRO B 1 59  ? -11.083 2.072   -45.796 1.00 113.52 ? 67  PRO B CA  1 
ATOM 2772 C C   . PRO B 1 59  ? -10.476 1.839   -44.421 1.00 117.54 ? 67  PRO B C   1 
ATOM 2773 O O   . PRO B 1 59  ? -10.654 0.735   -43.906 1.00 122.23 ? 67  PRO B O   1 
ATOM 2774 C CB  . PRO B 1 59  ? -10.534 1.272   -46.983 1.00 117.33 ? 67  PRO B CB  1 
ATOM 2775 C CG  . PRO B 1 59  ? -9.647  2.237   -47.677 1.00 118.39 ? 67  PRO B CG  1 
ATOM 2776 C CD  . PRO B 1 59  ? -10.316 3.586   -47.549 1.00 116.44 ? 67  PRO B CD  1 
ATOM 2777 N N   . ILE B 1 60  ? -9.812  2.821   -43.804 1.00 117.92 ? 68  ILE B N   1 
ATOM 2778 C CA  . ILE B 1 60  ? -9.143  2.716   -42.496 1.00 119.62 ? 68  ILE B CA  1 
ATOM 2779 C C   . ILE B 1 60  ? -7.880  1.865   -42.680 1.00 122.74 ? 68  ILE B C   1 
ATOM 2780 O O   . ILE B 1 60  ? -6.783  2.282   -42.291 1.00 124.19 ? 68  ILE B O   1 
ATOM 2781 C CB  . ILE B 1 60  ? -9.947  2.209   -41.275 1.00 110.21 ? 68  ILE B CB  1 
ATOM 2782 C CG1 . ILE B 1 60  ? -9.031  2.073   -40.057 1.00 112.51 ? 68  ILE B CG1 1 
ATOM 2783 C CG2 . ILE B 1 60  ? -10.661 0.882   -41.527 1.00 109.35 ? 68  ILE B CG2 1 
ATOM 2784 C CD1 . ILE B 1 60  ? -9.758  1.712   -38.787 1.00 108.69 ? 68  ILE B CD1 1 
ATOM 2785 N N   . SER B 1 61  ? -8.022  0.667   -43.255 1.00 120.73 ? 69  SER B N   1 
ATOM 2786 C CA  . SER B 1 61  ? -6.920  -0.168  -43.732 1.00 121.96 ? 69  SER B CA  1 
ATOM 2787 C C   . SER B 1 61  ? -6.040  0.574   -44.732 1.00 129.36 ? 69  SER B C   1 
ATOM 2788 O O   . SER B 1 61  ? -4.950  0.106   -45.081 1.00 132.23 ? 69  SER B O   1 
ATOM 2789 C CB  . SER B 1 61  ? -7.465  -1.460  -44.348 1.00 120.66 ? 69  SER B CB  1 
ATOM 2790 O OG  . SER B 1 61  ? -8.555  -1.194  -45.215 1.00 119.60 ? 69  SER B OG  1 
ATOM 2791 N N   . ALA B 1 62  ? -6.527  1.722   -45.204 1.00 130.69 ? 70  ALA B N   1 
ATOM 2792 C CA  . ALA B 1 62  ? -5.808  2.569   -46.145 1.00 128.36 ? 70  ALA B CA  1 
ATOM 2793 C C   . ALA B 1 62  ? -4.374  2.818   -45.694 1.00 128.94 ? 70  ALA B C   1 
ATOM 2794 O O   . ALA B 1 62  ? -4.066  2.847   -44.498 1.00 131.40 ? 70  ALA B O   1 
ATOM 2795 C CB  . ALA B 1 62  ? -6.538  3.904   -46.314 1.00 120.89 ? 70  ALA B CB  1 
ATOM 2796 N N   . SER B 1 63  ? -3.491  2.970   -46.677 1.00 123.45 ? 71  SER B N   1 
ATOM 2797 C CA  . SER B 1 63  ? -2.091  3.280   -46.426 1.00 115.33 ? 71  SER B CA  1 
ATOM 2798 C C   . SER B 1 63  ? -1.782  4.724   -46.803 1.00 104.77 ? 71  SER B C   1 
ATOM 2799 O O   . SER B 1 63  ? -0.711  5.024   -47.329 1.00 91.00  ? 71  SER B O   1 
ATOM 2800 C CB  . SER B 1 63  ? -1.188  2.335   -47.225 1.00 103.46 ? 71  SER B CB  1 
ATOM 2801 O OG  . SER B 1 63  ? -1.541  0.979   -47.021 1.00 92.20  ? 71  SER B OG  1 
ATOM 2802 N N   . VAL B 1 70  ? -10.100 8.403   -57.243 1.00 96.79  ? 78  VAL B N   1 
ATOM 2803 C CA  . VAL B 1 70  ? -11.236 8.292   -56.332 1.00 85.78  ? 78  VAL B CA  1 
ATOM 2804 C C   . VAL B 1 70  ? -12.330 7.557   -57.048 1.00 89.17  ? 78  VAL B C   1 
ATOM 2805 O O   . VAL B 1 70  ? -12.451 7.641   -58.269 1.00 94.65  ? 78  VAL B O   1 
ATOM 2806 C CB  . VAL B 1 70  ? -11.728 9.626   -55.844 1.00 87.85  ? 78  VAL B CB  1 
ATOM 2807 C CG1 . VAL B 1 70  ? -10.566 10.496  -55.486 1.00 88.15  ? 78  VAL B CG1 1 
ATOM 2808 C CG2 . VAL B 1 70  ? -12.724 10.272  -56.808 1.00 98.41  ? 78  VAL B CG2 1 
ATOM 2809 N N   . VAL B 1 71  ? -13.170 6.867   -56.306 1.00 82.25  ? 79  VAL B N   1 
ATOM 2810 C CA  . VAL B 1 71  ? -14.186 6.023   -56.909 1.00 80.41  ? 79  VAL B CA  1 
ATOM 2811 C C   . VAL B 1 71  ? -15.537 6.676   -56.633 1.00 80.97  ? 79  VAL B C   1 
ATOM 2812 O O   . VAL B 1 71  ? -16.085 6.575   -55.527 1.00 87.50  ? 79  VAL B O   1 
ATOM 2813 C CB  . VAL B 1 71  ? -14.120 4.592   -56.369 1.00 78.02  ? 79  VAL B CB  1 
ATOM 2814 C CG1 . VAL B 1 71  ? -15.063 3.684   -57.146 1.00 74.19  ? 79  VAL B CG1 1 
ATOM 2815 C CG2 . VAL B 1 71  ? -12.686 4.079   -56.444 1.00 79.88  ? 79  VAL B CG2 1 
ATOM 2816 N N   . VAL B 1 72  ? -16.061 7.381   -57.635 1.00 75.59  ? 80  VAL B N   1 
ATOM 2817 C CA  . VAL B 1 72  ? -17.399 7.959   -57.550 1.00 78.68  ? 80  VAL B CA  1 
ATOM 2818 C C   . VAL B 1 72  ? -18.421 6.870   -57.849 1.00 81.90  ? 80  VAL B C   1 
ATOM 2819 O O   . VAL B 1 72  ? -18.469 6.341   -58.964 1.00 86.74  ? 80  VAL B O   1 
ATOM 2820 C CB  . VAL B 1 72  ? -17.563 9.143   -58.515 1.00 81.13  ? 80  VAL B CB  1 
ATOM 2821 C CG1 . VAL B 1 72  ? -18.790 9.972   -58.137 1.00 75.96  ? 80  VAL B CG1 1 
ATOM 2822 C CG2 . VAL B 1 72  ? -16.310 10.005  -58.545 1.00 86.54  ? 80  VAL B CG2 1 
ATOM 2823 N N   . PHE B 1 73  ? -19.257 6.549   -56.863 1.00 75.94  ? 81  PHE B N   1 
ATOM 2824 C CA  . PHE B 1 73  ? -20.305 5.547   -57.025 1.00 70.49  ? 81  PHE B CA  1 
ATOM 2825 C C   . PHE B 1 73  ? -21.648 6.251   -57.173 1.00 71.64  ? 81  PHE B C   1 
ATOM 2826 O O   . PHE B 1 73  ? -22.135 6.881   -56.228 1.00 67.79  ? 81  PHE B O   1 
ATOM 2827 C CB  . PHE B 1 73  ? -20.339 4.575   -55.848 1.00 63.96  ? 81  PHE B CB  1 
ATOM 2828 C CG  . PHE B 1 73  ? -21.472 3.588   -55.916 1.00 67.36  ? 81  PHE B CG  1 
ATOM 2829 C CD1 . PHE B 1 73  ? -21.446 2.557   -56.842 1.00 70.23  ? 81  PHE B CD1 1 
ATOM 2830 C CD2 . PHE B 1 73  ? -22.568 3.700   -55.076 1.00 74.65  ? 81  PHE B CD2 1 
ATOM 2831 C CE1 . PHE B 1 73  ? -22.484 1.647   -56.919 1.00 73.91  ? 81  PHE B CE1 1 
ATOM 2832 C CE2 . PHE B 1 73  ? -23.612 2.791   -55.150 1.00 76.27  ? 81  PHE B CE2 1 
ATOM 2833 C CZ  . PHE B 1 73  ? -23.568 1.764   -56.074 1.00 73.87  ? 81  PHE B CZ  1 
ATOM 2834 N N   . PHE B 1 74  ? -22.249 6.134   -58.351 1.00 74.39  ? 82  PHE B N   1 
ATOM 2835 C CA  . PHE B 1 74  ? -23.594 6.632   -58.593 1.00 73.47  ? 82  PHE B CA  1 
ATOM 2836 C C   . PHE B 1 74  ? -24.571 5.475   -58.430 1.00 76.51  ? 82  PHE B C   1 
ATOM 2837 O O   . PHE B 1 74  ? -24.506 4.491   -59.175 1.00 71.99  ? 82  PHE B O   1 
ATOM 2838 C CB  . PHE B 1 74  ? -23.704 7.261   -59.981 1.00 68.41  ? 82  PHE B CB  1 
ATOM 2839 C CG  . PHE B 1 74  ? -23.127 8.645   -60.060 1.00 72.68  ? 82  PHE B CG  1 
ATOM 2840 C CD1 . PHE B 1 74  ? -23.832 9.732   -59.570 1.00 71.36  ? 82  PHE B CD1 1 
ATOM 2841 C CD2 . PHE B 1 74  ? -21.875 8.857   -60.612 1.00 81.32  ? 82  PHE B CD2 1 
ATOM 2842 C CE1 . PHE B 1 74  ? -23.301 11.008  -59.637 1.00 72.41  ? 82  PHE B CE1 1 
ATOM 2843 C CE2 . PHE B 1 74  ? -21.340 10.129  -60.682 1.00 81.74  ? 82  PHE B CE2 1 
ATOM 2844 C CZ  . PHE B 1 74  ? -22.053 11.206  -60.193 1.00 75.28  ? 82  PHE B CZ  1 
ATOM 2845 N N   . HIS B 1 75  ? -25.471 5.599   -57.460 1.00 78.13  ? 83  HIS B N   1 
ATOM 2846 C CA  . HIS B 1 75  ? -26.385 4.519   -57.126 1.00 75.34  ? 83  HIS B CA  1 
ATOM 2847 C C   . HIS B 1 75  ? -27.468 4.375   -58.193 1.00 69.09  ? 83  HIS B C   1 
ATOM 2848 O O   . HIS B 1 75  ? -27.660 5.238   -59.055 1.00 68.16  ? 83  HIS B O   1 
ATOM 2849 C CB  . HIS B 1 75  ? -27.009 4.762   -55.752 1.00 76.99  ? 83  HIS B CB  1 
ATOM 2850 C CG  . HIS B 1 75  ? -27.884 5.974   -55.694 1.00 74.90  ? 83  HIS B CG  1 
ATOM 2851 N ND1 . HIS B 1 75  ? -29.187 5.978   -56.143 1.00 77.57  ? 83  HIS B ND1 1 
ATOM 2852 C CD2 . HIS B 1 75  ? -27.638 7.227   -55.243 1.00 70.58  ? 83  HIS B CD2 1 
ATOM 2853 C CE1 . HIS B 1 75  ? -29.707 7.180   -55.968 1.00 72.88  ? 83  HIS B CE1 1 
ATOM 2854 N NE2 . HIS B 1 75  ? -28.788 7.956   -55.424 1.00 70.22  ? 83  HIS B NE2 1 
ATOM 2855 N N   . GLY B 1 76  ? -28.182 3.254   -58.124 1.00 66.82  ? 84  GLY B N   1 
ATOM 2856 C CA  . GLY B 1 76  ? -29.204 2.943   -59.100 1.00 70.25  ? 84  GLY B CA  1 
ATOM 2857 C C   . GLY B 1 76  ? -30.579 3.466   -58.749 1.00 64.60  ? 84  GLY B C   1 
ATOM 2858 O O   . GLY B 1 76  ? -30.723 4.565   -58.210 1.00 63.50  ? 84  GLY B O   1 
ATOM 2859 N N   . GLY B 1 77  ? -31.599 2.677   -59.057 1.00 63.54  ? 85  GLY B N   1 
ATOM 2860 C CA  . GLY B 1 77  ? -32.975 3.049   -58.814 1.00 63.24  ? 85  GLY B CA  1 
ATOM 2861 C C   . GLY B 1 77  ? -33.701 3.658   -59.992 1.00 70.01  ? 85  GLY B C   1 
ATOM 2862 O O   . GLY B 1 77  ? -34.714 4.335   -59.781 1.00 72.42  ? 85  GLY B O   1 
ATOM 2863 N N   . GLY B 1 78  ? -33.237 3.412   -61.214 1.00 72.50  ? 86  GLY B N   1 
ATOM 2864 C CA  . GLY B 1 78  ? -33.906 3.924   -62.407 1.00 63.75  ? 86  GLY B CA  1 
ATOM 2865 C C   . GLY B 1 78  ? -34.266 5.390   -62.351 1.00 59.03  ? 86  GLY B C   1 
ATOM 2866 O O   . GLY B 1 78  ? -35.338 5.785   -62.828 1.00 59.29  ? 86  GLY B O   1 
ATOM 2867 N N   . PHE B 1 79  ? -33.396 6.212   -61.761 1.00 59.70  ? 87  PHE B N   1 
ATOM 2868 C CA  . PHE B 1 79  ? -33.533 7.662   -61.647 1.00 70.52  ? 87  PHE B CA  1 
ATOM 2869 C C   . PHE B 1 79  ? -34.709 8.086   -60.775 1.00 68.91  ? 87  PHE B C   1 
ATOM 2870 O O   . PHE B 1 79  ? -34.951 9.292   -60.635 1.00 64.37  ? 87  PHE B O   1 
ATOM 2871 C CB  . PHE B 1 79  ? -33.669 8.346   -63.014 1.00 71.25  ? 87  PHE B CB  1 
ATOM 2872 C CG  . PHE B 1 79  ? -32.448 8.223   -63.875 1.00 70.58  ? 87  PHE B CG  1 
ATOM 2873 C CD1 . PHE B 1 79  ? -31.334 9.006   -63.636 1.00 70.38  ? 87  PHE B CD1 1 
ATOM 2874 C CD2 . PHE B 1 79  ? -32.410 7.311   -64.916 1.00 67.80  ? 87  PHE B CD2 1 
ATOM 2875 C CE1 . PHE B 1 79  ? -30.214 8.895   -64.428 1.00 63.90  ? 87  PHE B CE1 1 
ATOM 2876 C CE2 . PHE B 1 79  ? -31.287 7.190   -65.708 1.00 65.77  ? 87  PHE B CE2 1 
ATOM 2877 C CZ  . PHE B 1 79  ? -30.186 7.983   -65.462 1.00 64.75  ? 87  PHE B CZ  1 
ATOM 2878 N N   . CYS B 1 80  ? -35.447 7.147   -60.181 1.00 66.56  ? 88  CYS B N   1 
ATOM 2879 C CA  . CYS B 1 80  ? -36.613 7.471   -59.376 1.00 63.39  ? 88  CYS B CA  1 
ATOM 2880 C C   . CYS B 1 80  ? -36.522 6.980   -57.939 1.00 64.24  ? 88  CYS B C   1 
ATOM 2881 O O   . CYS B 1 80  ? -37.339 7.399   -57.112 1.00 61.02  ? 88  CYS B O   1 
ATOM 2882 C CB  . CYS B 1 80  ? -37.885 6.895   -60.019 1.00 60.52  ? 88  CYS B CB  1 
ATOM 2883 S SG  . CYS B 1 80  ? -38.069 7.262   -61.782 1.00 64.52  ? 88  CYS B SG  1 
ATOM 2884 N N   . PHE B 1 81  ? -35.553 6.128   -57.614 1.00 60.94  ? 89  PHE B N   1 
ATOM 2885 C CA  . PHE B 1 81  ? -35.360 5.646   -56.256 1.00 58.26  ? 89  PHE B CA  1 
ATOM 2886 C C   . PHE B 1 81  ? -33.877 5.702   -55.922 1.00 66.36  ? 89  PHE B C   1 
ATOM 2887 O O   . PHE B 1 81  ? -33.027 5.912   -56.794 1.00 72.07  ? 89  PHE B O   1 
ATOM 2888 C CB  . PHE B 1 81  ? -35.896 4.219   -56.080 1.00 62.19  ? 89  PHE B CB  1 
ATOM 2889 C CG  . PHE B 1 81  ? -37.367 4.091   -56.339 1.00 67.21  ? 89  PHE B CG  1 
ATOM 2890 C CD1 . PHE B 1 81  ? -38.278 4.800   -55.576 1.00 67.63  ? 89  PHE B CD1 1 
ATOM 2891 C CD2 . PHE B 1 81  ? -37.839 3.270   -57.349 1.00 69.34  ? 89  PHE B CD2 1 
ATOM 2892 C CE1 . PHE B 1 81  ? -39.636 4.692   -55.813 1.00 71.75  ? 89  PHE B CE1 1 
ATOM 2893 C CE2 . PHE B 1 81  ? -39.193 3.158   -57.590 1.00 65.24  ? 89  PHE B CE2 1 
ATOM 2894 C CZ  . PHE B 1 81  ? -40.094 3.868   -56.823 1.00 68.34  ? 89  PHE B CZ  1 
ATOM 2895 N N   . GLY B 1 82  ? -33.573 5.515   -54.639 1.00 67.04  ? 90  GLY B N   1 
ATOM 2896 C CA  . GLY B 1 82  ? -32.197 5.383   -54.204 1.00 65.01  ? 90  GLY B CA  1 
ATOM 2897 C C   . GLY B 1 82  ? -31.705 6.499   -53.309 1.00 61.53  ? 90  GLY B C   1 
ATOM 2898 O O   . GLY B 1 82  ? -32.164 7.639   -53.406 1.00 60.43  ? 90  GLY B O   1 
ATOM 2899 N N   . SER B 1 83  ? -30.773 6.171   -52.420 1.00 63.49  ? 91  SER B N   1 
ATOM 2900 C CA  . SER B 1 83  ? -30.130 7.155   -51.564 1.00 65.16  ? 91  SER B CA  1 
ATOM 2901 C C   . SER B 1 83  ? -28.805 6.583   -51.089 1.00 69.05  ? 91  SER B C   1 
ATOM 2902 O O   . SER B 1 83  ? -28.672 5.370   -50.908 1.00 72.68  ? 91  SER B O   1 
ATOM 2903 C CB  . SER B 1 83  ? -31.018 7.536   -50.374 1.00 69.91  ? 91  SER B CB  1 
ATOM 2904 O OG  . SER B 1 83  ? -30.318 8.348   -49.446 1.00 73.14  ? 91  SER B OG  1 
ATOM 2905 N N   . ARG B 1 84  ? -27.817 7.465   -50.920 1.00 65.48  ? 92  ARG B N   1 
ATOM 2906 C CA  . ARG B 1 84  ? -26.534 7.045   -50.363 1.00 68.85  ? 92  ARG B CA  1 
ATOM 2907 C C   . ARG B 1 84  ? -26.706 6.330   -49.028 1.00 75.64  ? 92  ARG B C   1 
ATOM 2908 O O   . ARG B 1 84  ? -25.914 5.443   -48.691 1.00 81.51  ? 92  ARG B O   1 
ATOM 2909 C CB  . ARG B 1 84  ? -25.608 8.254   -50.211 1.00 76.71  ? 92  ARG B CB  1 
ATOM 2910 C CG  . ARG B 1 84  ? -26.054 9.245   -49.152 1.00 77.22  ? 92  ARG B CG  1 
ATOM 2911 C CD  . ARG B 1 84  ? -25.222 10.515  -49.174 1.00 78.90  ? 92  ARG B CD  1 
ATOM 2912 N NE  . ARG B 1 84  ? -25.369 11.280  -47.940 1.00 81.28  ? 92  ARG B NE  1 
ATOM 2913 C CZ  . ARG B 1 84  ? -26.472 11.922  -47.578 1.00 81.21  ? 92  ARG B CZ  1 
ATOM 2914 N NH1 . ARG B 1 84  ? -27.548 11.937  -48.347 1.00 84.15  ? 92  ARG B NH1 1 
ATOM 2915 N NH2 . ARG B 1 84  ? -26.492 12.573  -46.418 1.00 77.74  ? 92  ARG B NH2 1 
ATOM 2916 N N   . SER B 1 85  ? -27.737 6.695   -48.261 1.00 78.24  ? 93  SER B N   1 
ATOM 2917 C CA  . SER B 1 85  ? -27.976 6.105   -46.949 1.00 81.11  ? 93  SER B CA  1 
ATOM 2918 C C   . SER B 1 85  ? -28.581 4.707   -47.014 1.00 83.49  ? 93  SER B C   1 
ATOM 2919 O O   . SER B 1 85  ? -28.511 3.978   -46.018 1.00 79.69  ? 93  SER B O   1 
ATOM 2920 C CB  . SER B 1 85  ? -28.889 7.016   -46.124 1.00 83.18  ? 93  SER B CB  1 
ATOM 2921 O OG  . SER B 1 85  ? -30.075 7.324   -46.837 1.00 91.67  ? 93  SER B OG  1 
ATOM 2922 N N   . TRP B 1 86  ? -29.193 4.327   -48.145 1.00 86.07  ? 94  TRP B N   1 
ATOM 2923 C CA  . TRP B 1 86  ? -29.819 3.017   -48.316 1.00 80.33  ? 94  TRP B CA  1 
ATOM 2924 C C   . TRP B 1 86  ? -28.893 1.881   -47.896 1.00 80.87  ? 94  TRP B C   1 
ATOM 2925 O O   . TRP B 1 86  ? -27.667 2.013   -47.999 1.00 80.97  ? 94  TRP B O   1 
ATOM 2926 C CB  . TRP B 1 86  ? -30.258 2.806   -49.766 1.00 69.27  ? 94  TRP B CB  1 
ATOM 2927 C CG  . TRP B 1 86  ? -31.614 3.347   -50.068 1.00 63.05  ? 94  TRP B CG  1 
ATOM 2928 C CD1 . TRP B 1 86  ? -32.301 4.287   -49.357 1.00 65.51  ? 94  TRP B CD1 1 
ATOM 2929 C CD2 . TRP B 1 86  ? -32.479 2.936   -51.131 1.00 59.35  ? 94  TRP B CD2 1 
ATOM 2930 N NE1 . TRP B 1 86  ? -33.529 4.510   -49.932 1.00 65.90  ? 94  TRP B NE1 1 
ATOM 2931 C CE2 . TRP B 1 86  ? -33.664 3.690   -51.021 1.00 63.15  ? 94  TRP B CE2 1 
ATOM 2932 C CE3 . TRP B 1 86  ? -32.362 2.011   -52.174 1.00 61.85  ? 94  TRP B CE3 1 
ATOM 2933 C CZ2 . TRP B 1 86  ? -34.724 3.549   -51.915 1.00 66.95  ? 94  TRP B CZ2 1 
ATOM 2934 C CZ3 . TRP B 1 86  ? -33.414 1.873   -53.060 1.00 59.29  ? 94  TRP B CZ3 1 
ATOM 2935 C CH2 . TRP B 1 86  ? -34.580 2.638   -52.925 1.00 67.14  ? 94  TRP B CH2 1 
ATOM 2936 N N   . PRO B 1 87  ? -29.439 0.746   -47.431 1.00 80.18  ? 95  PRO B N   1 
ATOM 2937 C CA  . PRO B 1 87  ? -28.579 -0.329  -46.915 1.00 83.54  ? 95  PRO B CA  1 
ATOM 2938 C C   . PRO B 1 87  ? -27.617 -0.975  -47.900 1.00 91.38  ? 95  PRO B C   1 
ATOM 2939 O O   . PRO B 1 87  ? -26.403 -0.939  -47.682 1.00 89.43  ? 95  PRO B O   1 
ATOM 2940 C CB  . PRO B 1 87  ? -29.581 -1.387  -46.430 1.00 80.97  ? 95  PRO B CB  1 
ATOM 2941 C CG  . PRO B 1 87  ? -30.863 -1.074  -47.117 1.00 76.78  ? 95  PRO B CG  1 
ATOM 2942 C CD  . PRO B 1 87  ? -30.871 0.398   -47.378 1.00 75.61  ? 95  PRO B CD  1 
ATOM 2943 N N   . HIS B 1 88  ? -28.129 -1.553  -48.992 1.00 91.84  ? 96  HIS B N   1 
ATOM 2944 C CA  . HIS B 1 88  ? -27.268 -2.335  -49.872 1.00 90.95  ? 96  HIS B CA  1 
ATOM 2945 C C   . HIS B 1 88  ? -26.474 -1.388  -50.763 1.00 88.78  ? 96  HIS B C   1 
ATOM 2946 O O   . HIS B 1 88  ? -25.417 -1.781  -51.270 1.00 92.94  ? 96  HIS B O   1 
ATOM 2947 C CB  . HIS B 1 88  ? -28.054 -3.329  -50.732 1.00 89.55  ? 96  HIS B CB  1 
ATOM 2948 C CG  . HIS B 1 88  ? -29.230 -2.732  -51.438 1.00 89.52  ? 96  HIS B CG  1 
ATOM 2949 N ND1 . HIS B 1 88  ? -30.295 -2.165  -50.772 1.00 82.03  ? 96  HIS B ND1 1 
ATOM 2950 C CD2 . HIS B 1 88  ? -29.508 -2.617  -52.758 1.00 95.24  ? 96  HIS B CD2 1 
ATOM 2951 C CE1 . HIS B 1 88  ? -31.179 -1.727  -51.651 1.00 86.87  ? 96  HIS B CE1 1 
ATOM 2952 N NE2 . HIS B 1 88  ? -30.725 -1.989  -52.863 1.00 89.34  ? 96  HIS B NE2 1 
ATOM 2953 N N   . PHE B 1 89  ? -26.948 -0.156  -50.968 1.00 83.10  ? 97  PHE B N   1 
ATOM 2954 C CA  . PHE B 1 89  ? -26.082 0.859   -51.558 1.00 85.52  ? 97  PHE B CA  1 
ATOM 2955 C C   . PHE B 1 89  ? -24.904 1.147   -50.638 1.00 83.02  ? 97  PHE B C   1 
ATOM 2956 O O   . PHE B 1 89  ? -23.742 1.074   -51.054 1.00 78.96  ? 97  PHE B O   1 
ATOM 2957 C CB  . PHE B 1 89  ? -26.866 2.142   -51.843 1.00 83.09  ? 97  PHE B CB  1 
ATOM 2958 C CG  . PHE B 1 89  ? -27.807 2.039   -53.008 1.00 77.30  ? 97  PHE B CG  1 
ATOM 2959 C CD1 . PHE B 1 89  ? -27.584 1.115   -54.014 1.00 72.01  ? 97  PHE B CD1 1 
ATOM 2960 C CD2 . PHE B 1 89  ? -28.900 2.884   -53.111 1.00 72.34  ? 97  PHE B CD2 1 
ATOM 2961 C CE1 . PHE B 1 89  ? -28.441 1.025   -55.095 1.00 75.00  ? 97  PHE B CE1 1 
ATOM 2962 C CE2 . PHE B 1 89  ? -29.760 2.799   -54.190 1.00 70.54  ? 97  PHE B CE2 1 
ATOM 2963 C CZ  . PHE B 1 89  ? -29.531 1.868   -55.182 1.00 76.46  ? 97  PHE B CZ  1 
ATOM 2964 N N   . HIS B 1 90  ? -25.196 1.463   -49.373 1.00 86.28  ? 98  HIS B N   1 
ATOM 2965 C CA  . HIS B 1 90  ? -24.143 1.671   -48.385 1.00 93.99  ? 98  HIS B CA  1 
ATOM 2966 C C   . HIS B 1 90  ? -23.240 0.447   -48.285 1.00 97.66  ? 98  HIS B C   1 
ATOM 2967 O O   . HIS B 1 90  ? -22.011 0.570   -48.341 1.00 100.28 ? 98  HIS B O   1 
ATOM 2968 C CB  . HIS B 1 90  ? -24.769 2.011   -47.029 1.00 87.80  ? 98  HIS B CB  1 
ATOM 2969 C CG  . HIS B 1 90  ? -23.795 2.515   -46.012 1.00 94.30  ? 98  HIS B CG  1 
ATOM 2970 N ND1 . HIS B 1 90  ? -23.725 3.842   -45.648 1.00 96.11  ? 98  HIS B ND1 1 
ATOM 2971 C CD2 . HIS B 1 90  ? -22.869 1.872   -45.263 1.00 97.41  ? 98  HIS B CD2 1 
ATOM 2972 C CE1 . HIS B 1 90  ? -22.789 3.996   -44.729 1.00 102.97 ? 98  HIS B CE1 1 
ATOM 2973 N NE2 . HIS B 1 90  ? -22.252 2.816   -44.479 1.00 102.57 ? 98  HIS B NE2 1 
ATOM 2974 N N   . ASN B 1 91  ? -23.837 -0.746  -48.159 1.00 92.23  ? 99  ASN B N   1 
ATOM 2975 C CA  . ASN B 1 91  ? -23.054 -1.976  -48.030 1.00 96.45  ? 99  ASN B CA  1 
ATOM 2976 C C   . ASN B 1 91  ? -22.045 -2.126  -49.161 1.00 99.93  ? 99  ASN B C   1 
ATOM 2977 O O   . ASN B 1 91  ? -20.873 -2.442  -48.922 1.00 103.35 ? 99  ASN B O   1 
ATOM 2978 C CB  . ASN B 1 91  ? -23.972 -3.196  -47.951 1.00 105.00 ? 99  ASN B CB  1 
ATOM 2979 C CG  . ASN B 1 91  ? -24.992 -3.081  -46.840 1.00 112.37 ? 99  ASN B CG  1 
ATOM 2980 O OD1 . ASN B 1 91  ? -26.168 -3.390  -47.023 1.00 120.20 ? 99  ASN B OD1 1 
ATOM 2981 N ND2 . ASN B 1 91  ? -24.547 -2.614  -45.679 1.00 106.09 ? 99  ASN B ND2 1 
ATOM 2982 N N   . PHE B 1 92  ? -22.484 -1.920  -50.403 1.00 96.60  ? 100 PHE B N   1 
ATOM 2983 C CA  . PHE B 1 92  ? -21.545 -1.957  -51.518 1.00 94.71  ? 100 PHE B CA  1 
ATOM 2984 C C   . PHE B 1 92  ? -20.427 -0.940  -51.332 1.00 93.12  ? 100 PHE B C   1 
ATOM 2985 O O   . PHE B 1 92  ? -19.244 -1.286  -51.425 1.00 94.35  ? 100 PHE B O   1 
ATOM 2986 C CB  . PHE B 1 92  ? -22.289 -1.732  -52.834 1.00 98.22  ? 100 PHE B CB  1 
ATOM 2987 C CG  . PHE B 1 92  ? -21.647 -2.399  -54.017 1.00 99.99  ? 100 PHE B CG  1 
ATOM 2988 C CD1 . PHE B 1 92  ? -21.365 -3.753  -54.004 1.00 101.16 ? 100 PHE B CD1 1 
ATOM 2989 C CD2 . PHE B 1 92  ? -21.393 -1.680  -55.173 1.00 91.26  ? 100 PHE B CD2 1 
ATOM 2990 C CE1 . PHE B 1 92  ? -20.788 -4.367  -55.098 1.00 91.02  ? 100 PHE B CE1 1 
ATOM 2991 C CE2 . PHE B 1 92  ? -20.824 -2.289  -56.274 1.00 92.02  ? 100 PHE B CE2 1 
ATOM 2992 C CZ  . PHE B 1 92  ? -20.522 -3.634  -56.236 1.00 91.47  ? 100 PHE B CZ  1 
ATOM 2993 N N   . CYS B 1 93  ? -20.782 0.305   -50.995 1.00 93.04  ? 101 CYS B N   1 
ATOM 2994 C CA  . CYS B 1 93  ? -19.779 1.361   -50.855 1.00 92.52  ? 101 CYS B CA  1 
ATOM 2995 C C   . CYS B 1 93  ? -18.665 0.987   -49.882 1.00 94.66  ? 101 CYS B C   1 
ATOM 2996 O O   . CYS B 1 93  ? -17.491 1.283   -50.139 1.00 94.49  ? 101 CYS B O   1 
ATOM 2997 C CB  . CYS B 1 93  ? -20.440 2.671   -50.433 1.00 90.96  ? 101 CYS B CB  1 
ATOM 2998 S SG  . CYS B 1 93  ? -21.727 3.265   -51.553 1.00 97.68  ? 101 CYS B SG  1 
ATOM 2999 N N   . LEU B 1 94  ? -19.000 0.348   -48.754 1.00 93.71  ? 102 LEU B N   1 
ATOM 3000 C CA  . LEU B 1 94  ? -17.933 -0.126  -47.874 1.00 103.15 ? 102 LEU B CA  1 
ATOM 3001 C C   . LEU B 1 94  ? -17.068 -1.163  -48.581 1.00 101.22 ? 102 LEU B C   1 
ATOM 3002 O O   . LEU B 1 94  ? -15.840 -1.160  -48.437 1.00 102.21 ? 102 LEU B O   1 
ATOM 3003 C CB  . LEU B 1 94  ? -18.469 -0.713  -46.560 1.00 108.12 ? 102 LEU B CB  1 
ATOM 3004 C CG  . LEU B 1 94  ? -19.496 -0.088  -45.608 1.00 100.08 ? 102 LEU B CG  1 
ATOM 3005 C CD1 . LEU B 1 94  ? -20.850 -0.575  -45.922 1.00 96.43  ? 102 LEU B CD1 1 
ATOM 3006 C CD2 . LEU B 1 94  ? -19.184 -0.432  -44.160 1.00 97.41  ? 102 LEU B CD2 1 
ATOM 3007 N N   . THR B 1 95  ? -17.693 -2.059  -49.352 1.00 100.74 ? 103 THR B N   1 
ATOM 3008 C CA  . THR B 1 95  ? -16.949 -3.134  -50.003 1.00 104.56 ? 103 THR B CA  1 
ATOM 3009 C C   . THR B 1 95  ? -15.956 -2.598  -51.032 1.00 102.78 ? 103 THR B C   1 
ATOM 3010 O O   . THR B 1 95  ? -14.789 -3.006  -51.040 1.00 104.48 ? 103 THR B O   1 
ATOM 3011 C CB  . THR B 1 95  ? -17.919 -4.126  -50.643 1.00 102.54 ? 103 THR B CB  1 
ATOM 3012 O OG1 . THR B 1 95  ? -18.933 -4.480  -49.693 1.00 107.33 ? 103 THR B OG1 1 
ATOM 3013 C CG2 . THR B 1 95  ? -17.182 -5.385  -51.059 1.00 102.54 ? 103 THR B CG2 1 
ATOM 3014 N N   . LEU B 1 96  ? -16.393 -1.694  -51.921 1.00 99.32  ? 104 LEU B N   1 
ATOM 3015 C CA  . LEU B 1 96  ? -15.429 -1.062  -52.821 1.00 98.03  ? 104 LEU B CA  1 
ATOM 3016 C C   . LEU B 1 96  ? -14.326 -0.388  -52.020 1.00 98.85  ? 104 LEU B C   1 
ATOM 3017 O O   . LEU B 1 96  ? -13.137 -0.563  -52.303 1.00 104.02 ? 104 LEU B O   1 
ATOM 3018 C CB  . LEU B 1 96  ? -16.074 -0.054  -53.785 1.00 94.82  ? 104 LEU B CB  1 
ATOM 3019 C CG  . LEU B 1 96  ? -17.291 -0.247  -54.698 1.00 90.04  ? 104 LEU B CG  1 
ATOM 3020 C CD1 . LEU B 1 96  ? -18.590 0.077   -54.021 1.00 87.56  ? 104 LEU B CD1 1 
ATOM 3021 C CD2 . LEU B 1 96  ? -17.125 0.591   -55.968 1.00 85.24  ? 104 LEU B CD2 1 
ATOM 3022 N N   . ALA B 1 97  ? -14.711 0.410   -51.023 1.00 102.57 ? 105 ALA B N   1 
ATOM 3023 C CA  . ALA B 1 97  ? -13.742 1.118   -50.196 1.00 109.50 ? 105 ALA B CA  1 
ATOM 3024 C C   . ALA B 1 97  ? -12.692 0.181   -49.604 1.00 112.66 ? 105 ALA B C   1 
ATOM 3025 O O   . ALA B 1 97  ? -11.490 0.360   -49.826 1.00 110.38 ? 105 ALA B O   1 
ATOM 3026 C CB  . ALA B 1 97  ? -14.481 1.876   -49.092 1.00 105.32 ? 105 ALA B CB  1 
ATOM 3027 N N   . SER B 1 98  ? -13.134 -0.825  -48.846 1.00 114.25 ? 106 SER B N   1 
ATOM 3028 C CA  . SER B 1 98  ? -12.204 -1.741  -48.191 1.00 115.00 ? 106 SER B CA  1 
ATOM 3029 C C   . SER B 1 98  ? -11.336 -2.492  -49.194 1.00 113.29 ? 106 SER B C   1 
ATOM 3030 O O   . SER B 1 98  ? -10.118 -2.297  -49.239 1.00 113.71 ? 106 SER B O   1 
ATOM 3031 C CB  . SER B 1 98  ? -12.972 -2.715  -47.291 1.00 114.16 ? 106 SER B CB  1 
ATOM 3032 O OG  . SER B 1 98  ? -13.748 -3.614  -48.057 1.00 110.19 ? 106 SER B OG  1 
ATOM 3033 N N   . SER B 1 99  ? -11.955 -3.331  -50.029 1.00 113.11 ? 107 SER B N   1 
ATOM 3034 C CA  . SER B 1 99  ? -11.186 -4.247  -50.871 1.00 117.48 ? 107 SER B CA  1 
ATOM 3035 C C   . SER B 1 99  ? -10.361 -3.516  -51.923 1.00 115.67 ? 107 SER B C   1 
ATOM 3036 O O   . SER B 1 99  ? -9.249  -3.949  -52.249 1.00 119.17 ? 107 SER B O   1 
ATOM 3037 C CB  . SER B 1 99  ? -12.117 -5.257  -51.526 1.00 110.69 ? 107 SER B CB  1 
ATOM 3038 O OG  . SER B 1 99  ? -12.845 -5.991  -50.558 1.00 105.47 ? 107 SER B OG  1 
ATOM 3039 N N   . LEU B 1 100 ? -10.882 -2.426  -52.483 1.00 108.51 ? 108 LEU B N   1 
ATOM 3040 C CA  . LEU B 1 100 ? -10.071 -1.625  -53.391 1.00 105.40 ? 108 LEU B CA  1 
ATOM 3041 C C   . LEU B 1 100 ? -9.094  -0.740  -52.639 1.00 107.63 ? 108 LEU B C   1 
ATOM 3042 O O   . LEU B 1 100 ? -8.281  -0.067  -53.277 1.00 98.61  ? 108 LEU B O   1 
ATOM 3043 C CB  . LEU B 1 100 ? -10.936 -0.752  -54.312 1.00 100.23 ? 108 LEU B CB  1 
ATOM 3044 C CG  . LEU B 1 100 ? -11.408 -1.292  -55.663 1.00 97.45  ? 108 LEU B CG  1 
ATOM 3045 C CD1 . LEU B 1 100 ? -10.244 -1.242  -56.635 1.00 101.16 ? 108 LEU B CD1 1 
ATOM 3046 C CD2 . LEU B 1 100 ? -11.969 -2.692  -55.565 1.00 95.16  ? 108 LEU B CD2 1 
ATOM 3047 N N   . ASN B 1 101 ? -9.135  -0.750  -51.306 1.00 115.22 ? 109 ASN B N   1 
ATOM 3048 C CA  . ASN B 1 101 ? -8.430  0.230   -50.483 1.00 112.01 ? 109 ASN B CA  1 
ATOM 3049 C C   . ASN B 1 101 ? -8.718  1.634   -51.009 1.00 113.37 ? 109 ASN B C   1 
ATOM 3050 O O   . ASN B 1 101 ? -7.833  2.359   -51.460 1.00 113.62 ? 109 ASN B O   1 
ATOM 3051 C CB  . ASN B 1 101 ? -6.925  -0.065  -50.452 1.00 110.45 ? 109 ASN B CB  1 
ATOM 3052 C CG  . ASN B 1 101 ? -6.247  0.500   -49.231 1.00 106.12 ? 109 ASN B CG  1 
ATOM 3053 O OD1 . ASN B 1 101 ? -5.752  1.625   -49.256 1.00 114.19 ? 109 ASN B OD1 1 
ATOM 3054 N ND2 . ASN B 1 101 ? -6.257  -0.255  -48.144 1.00 99.89  ? 109 ASN B ND2 1 
ATOM 3055 N N   . ALA B 1 102 ? -9.990  2.015   -50.902 1.00 111.80 ? 110 ALA B N   1 
ATOM 3056 C CA  . ALA B 1 102 ? -10.457 3.135   -51.694 1.00 110.39 ? 110 ALA B CA  1 
ATOM 3057 C C   . ALA B 1 102 ? -11.371 4.108   -50.965 1.00 110.98 ? 110 ALA B C   1 
ATOM 3058 O O   . ALA B 1 102 ? -12.205 3.732   -50.137 1.00 114.11 ? 110 ALA B O   1 
ATOM 3059 C CB  . ALA B 1 102 ? -11.206 2.614   -52.929 1.00 100.68 ? 110 ALA B CB  1 
ATOM 3060 N N   . LEU B 1 103 ? -11.169 5.375   -51.301 1.00 106.38 ? 111 LEU B N   1 
ATOM 3061 C CA  . LEU B 1 103 ? -12.097 6.451   -51.011 1.00 102.59 ? 111 LEU B CA  1 
ATOM 3062 C C   . LEU B 1 103 ? -13.266 6.379   -51.988 1.00 98.06  ? 111 LEU B C   1 
ATOM 3063 O O   . LEU B 1 103 ? -13.072 6.485   -53.204 1.00 95.00  ? 111 LEU B O   1 
ATOM 3064 C CB  . LEU B 1 103 ? -11.371 7.788   -51.129 1.00 100.34 ? 111 LEU B CB  1 
ATOM 3065 C CG  . LEU B 1 103 ? -12.123 9.103   -50.940 1.00 95.37  ? 111 LEU B CG  1 
ATOM 3066 C CD1 . LEU B 1 103 ? -12.662 9.239   -49.533 1.00 94.69  ? 111 LEU B CD1 1 
ATOM 3067 C CD2 . LEU B 1 103 ? -11.186 10.241  -51.280 1.00 96.85  ? 111 LEU B CD2 1 
ATOM 3068 N N   . VAL B 1 104 ? -14.479 6.225   -51.468 1.00 96.03  ? 112 VAL B N   1 
ATOM 3069 C CA  . VAL B 1 104 ? -15.680 6.185   -52.292 1.00 87.26  ? 112 VAL B CA  1 
ATOM 3070 C C   . VAL B 1 104 ? -16.432 7.492   -52.103 1.00 85.94  ? 112 VAL B C   1 
ATOM 3071 O O   . VAL B 1 104 ? -16.522 8.010   -50.984 1.00 90.15  ? 112 VAL B O   1 
ATOM 3072 C CB  . VAL B 1 104 ? -16.566 4.969   -51.949 1.00 86.99  ? 112 VAL B CB  1 
ATOM 3073 C CG1 . VAL B 1 104 ? -17.906 5.043   -52.674 1.00 77.12  ? 112 VAL B CG1 1 
ATOM 3074 C CG2 . VAL B 1 104 ? -15.841 3.676   -52.294 1.00 87.67  ? 112 VAL B CG2 1 
ATOM 3075 N N   . VAL B 1 105 ? -16.967 8.026   -53.195 1.00 75.21  ? 113 VAL B N   1 
ATOM 3076 C CA  . VAL B 1 105 ? -17.795 9.225   -53.161 1.00 77.59  ? 113 VAL B CA  1 
ATOM 3077 C C   . VAL B 1 105 ? -19.164 8.785   -53.655 1.00 75.29  ? 113 VAL B C   1 
ATOM 3078 O O   . VAL B 1 105 ? -19.364 8.567   -54.856 1.00 78.33  ? 113 VAL B O   1 
ATOM 3079 C CB  . VAL B 1 105 ? -17.223 10.364  -54.014 1.00 77.80  ? 113 VAL B CB  1 
ATOM 3080 C CG1 . VAL B 1 105 ? -18.207 11.530  -54.085 1.00 73.69  ? 113 VAL B CG1 1 
ATOM 3081 C CG2 . VAL B 1 105 ? -15.881 10.823  -53.460 1.00 78.22  ? 113 VAL B CG2 1 
ATOM 3082 N N   . SER B 1 106 ? -20.107 8.632   -52.724 1.00 73.37  ? 114 SER B N   1 
ATOM 3083 C CA  . SER B 1 106 ? -21.462 8.173   -53.015 1.00 69.92  ? 114 SER B CA  1 
ATOM 3084 C C   . SER B 1 106 ? -22.421 9.341   -52.842 1.00 70.83  ? 114 SER B C   1 
ATOM 3085 O O   . SER B 1 106 ? -22.910 9.592   -51.730 1.00 75.12  ? 114 SER B O   1 
ATOM 3086 C CB  . SER B 1 106 ? -21.848 7.009   -52.099 1.00 71.09  ? 114 SER B CB  1 
ATOM 3087 O OG  . SER B 1 106 ? -23.134 6.510   -52.419 1.00 65.87  ? 114 SER B OG  1 
ATOM 3088 N N   . PRO B 1 107 ? -22.721 10.085  -53.901 1.00 65.56  ? 115 PRO B N   1 
ATOM 3089 C CA  . PRO B 1 107 ? -23.651 11.208  -53.786 1.00 65.69  ? 115 PRO B CA  1 
ATOM 3090 C C   . PRO B 1 107 ? -25.099 10.808  -54.007 1.00 63.63  ? 115 PRO B C   1 
ATOM 3091 O O   . PRO B 1 107 ? -25.417 9.834   -54.693 1.00 71.70  ? 115 PRO B O   1 
ATOM 3092 C CB  . PRO B 1 107 ? -23.177 12.149  -54.902 1.00 67.52  ? 115 PRO B CB  1 
ATOM 3093 C CG  . PRO B 1 107 ? -22.681 11.216  -55.957 1.00 71.94  ? 115 PRO B CG  1 
ATOM 3094 C CD  . PRO B 1 107 ? -22.097 10.021  -55.235 1.00 67.34  ? 115 PRO B CD  1 
ATOM 3095 N N   . ASP B 1 108 ? -25.986 11.588  -53.398 1.00 63.25  ? 116 ASP B N   1 
ATOM 3096 C CA  . ASP B 1 108 ? -27.381 11.591  -53.803 1.00 65.42  ? 116 ASP B CA  1 
ATOM 3097 C C   . ASP B 1 108 ? -27.565 12.533  -54.984 1.00 60.56  ? 116 ASP B C   1 
ATOM 3098 O O   . ASP B 1 108 ? -26.986 13.622  -55.025 1.00 60.98  ? 116 ASP B O   1 
ATOM 3099 C CB  . ASP B 1 108 ? -28.281 12.018  -52.644 1.00 73.11  ? 116 ASP B CB  1 
ATOM 3100 C CG  . ASP B 1 108 ? -28.365 10.967  -51.554 1.00 73.25  ? 116 ASP B CG  1 
ATOM 3101 O OD1 . ASP B 1 108 ? -28.004 9.801   -51.819 1.00 72.40  ? 116 ASP B OD1 1 
ATOM 3102 O OD2 . ASP B 1 108 ? -28.795 11.308  -50.431 1.00 69.74  ? 116 ASP B OD2 1 
ATOM 3103 N N   . TYR B 1 109 ? -28.377 12.110  -55.947 1.00 59.54  ? 117 TYR B N   1 
ATOM 3104 C CA  . TYR B 1 109 ? -28.789 12.967  -57.045 1.00 51.18  ? 117 TYR B CA  1 
ATOM 3105 C C   . TYR B 1 109 ? -30.303 13.109  -57.022 1.00 47.28  ? 117 TYR B C   1 
ATOM 3106 O O   . TYR B 1 109 ? -31.012 12.242  -56.502 1.00 53.59  ? 117 TYR B O   1 
ATOM 3107 C CB  . TYR B 1 109 ? -28.304 12.422  -58.405 1.00 46.59  ? 117 TYR B CB  1 
ATOM 3108 C CG  . TYR B 1 109 ? -28.654 10.976  -58.695 1.00 48.69  ? 117 TYR B CG  1 
ATOM 3109 C CD1 . TYR B 1 109 ? -29.943 10.607  -59.061 1.00 55.40  ? 117 TYR B CD1 1 
ATOM 3110 C CD2 . TYR B 1 109 ? -27.688 9.980   -58.613 1.00 50.57  ? 117 TYR B CD2 1 
ATOM 3111 C CE1 . TYR B 1 109 ? -30.261 9.288   -59.331 1.00 60.18  ? 117 TYR B CE1 1 
ATOM 3112 C CE2 . TYR B 1 109 ? -27.997 8.658   -58.880 1.00 58.73  ? 117 TYR B CE2 1 
ATOM 3113 C CZ  . TYR B 1 109 ? -29.284 8.318   -59.239 1.00 63.63  ? 117 TYR B CZ  1 
ATOM 3114 O OH  . TYR B 1 109 ? -29.598 7.005   -59.506 1.00 66.50  ? 117 TYR B OH  1 
ATOM 3115 N N   . ARG B 1 110 ? -30.790 14.227  -57.555 1.00 41.50  ? 118 ARG B N   1 
ATOM 3116 C CA  . ARG B 1 110 ? -32.224 14.479  -57.572 1.00 41.49  ? 118 ARG B CA  1 
ATOM 3117 C C   . ARG B 1 110 ? -32.958 13.364  -58.309 1.00 44.81  ? 118 ARG B C   1 
ATOM 3118 O O   . ARG B 1 110 ? -32.441 12.762  -59.253 1.00 53.82  ? 118 ARG B O   1 
ATOM 3119 C CB  . ARG B 1 110 ? -32.522 15.833  -58.214 1.00 48.51  ? 118 ARG B CB  1 
ATOM 3120 C CG  . ARG B 1 110 ? -32.082 17.025  -57.380 1.00 49.29  ? 118 ARG B CG  1 
ATOM 3121 C CD  . ARG B 1 110 ? -32.301 18.331  -58.127 1.00 59.81  ? 118 ARG B CD  1 
ATOM 3122 N NE  . ARG B 1 110 ? -31.515 18.397  -59.353 1.00 61.72  ? 118 ARG B NE  1 
ATOM 3123 C CZ  . ARG B 1 110 ? -31.616 19.362  -60.258 1.00 65.54  ? 118 ARG B CZ  1 
ATOM 3124 N NH1 . ARG B 1 110 ? -32.534 20.310  -60.159 1.00 70.99  ? 118 ARG B NH1 1 
ATOM 3125 N NH2 . ARG B 1 110 ? -30.795 19.358  -61.304 1.00 66.64  ? 118 ARG B NH2 1 
ATOM 3126 N N   . LEU B 1 111 ? -34.178 13.090  -57.861 1.00 50.21  ? 119 LEU B N   1 
ATOM 3127 C CA  . LEU B 1 111 ? -34.946 11.932  -58.291 1.00 53.89  ? 119 LEU B CA  1 
ATOM 3128 C C   . LEU B 1 111 ? -36.185 12.352  -59.070 1.00 53.14  ? 119 LEU B C   1 
ATOM 3129 O O   . LEU B 1 111 ? -36.838 13.344  -58.734 1.00 56.09  ? 119 LEU B O   1 
ATOM 3130 C CB  . LEU B 1 111 ? -35.355 11.089  -57.080 1.00 58.17  ? 119 LEU B CB  1 
ATOM 3131 C CG  . LEU B 1 111 ? -34.250 10.370  -56.307 1.00 58.38  ? 119 LEU B CG  1 
ATOM 3132 C CD1 . LEU B 1 111 ? -34.793 9.097   -55.717 1.00 55.07  ? 119 LEU B CD1 1 
ATOM 3133 C CD2 . LEU B 1 111 ? -33.091 10.036  -57.229 1.00 53.77  ? 119 LEU B CD2 1 
ATOM 3134 N N   . ALA B 1 112 ? -36.495 11.588  -60.112 1.00 52.21  ? 120 ALA B N   1 
ATOM 3135 C CA  . ALA B 1 112 ? -37.744 11.715  -60.840 1.00 54.10  ? 120 ALA B CA  1 
ATOM 3136 C C   . ALA B 1 112 ? -38.876 11.064  -60.050 1.00 53.70  ? 120 ALA B C   1 
ATOM 3137 O O   . ALA B 1 112 ? -38.629 10.243  -59.164 1.00 57.21  ? 120 ALA B O   1 
ATOM 3138 C CB  . ALA B 1 112 ? -37.606 11.070  -62.217 1.00 61.54  ? 120 ALA B CB  1 
ATOM 3139 N N   . PRO B 1 113 ? -40.141 11.410  -60.347 1.00 48.04  ? 121 PRO B N   1 
ATOM 3140 C CA  . PRO B 1 113 ? -40.634 12.390  -61.330 1.00 51.59  ? 121 PRO B CA  1 
ATOM 3141 C C   . PRO B 1 113 ? -40.535 13.831  -60.844 1.00 53.09  ? 121 PRO B C   1 
ATOM 3142 O O   . PRO B 1 113 ? -40.734 14.751  -61.634 1.00 60.85  ? 121 PRO B O   1 
ATOM 3143 C CB  . PRO B 1 113 ? -42.092 11.965  -61.533 1.00 50.90  ? 121 PRO B CB  1 
ATOM 3144 C CG  . PRO B 1 113 ? -42.489 11.378  -60.218 1.00 54.68  ? 121 PRO B CG  1 
ATOM 3145 C CD  . PRO B 1 113 ? -41.251 10.701  -59.686 1.00 55.24  ? 121 PRO B CD  1 
ATOM 3146 N N   . GLU B 1 114 ? -40.259 14.058  -59.557 1.00 47.87  ? 122 GLU B N   1 
ATOM 3147 C CA  . GLU B 1 114 ? -40.150 15.425  -59.057 1.00 55.08  ? 122 GLU B CA  1 
ATOM 3148 C C   . GLU B 1 114 ? -39.079 16.196  -59.816 1.00 52.60  ? 122 GLU B C   1 
ATOM 3149 O O   . GLU B 1 114 ? -39.304 17.329  -60.257 1.00 51.57  ? 122 GLU B O   1 
ATOM 3150 C CB  . GLU B 1 114 ? -39.841 15.428  -57.559 1.00 59.57  ? 122 GLU B CB  1 
ATOM 3151 C CG  . GLU B 1 114 ? -40.756 14.570  -56.700 1.00 58.72  ? 122 GLU B CG  1 
ATOM 3152 C CD  . GLU B 1 114 ? -40.167 13.202  -56.430 1.00 60.02  ? 122 GLU B CD  1 
ATOM 3153 O OE1 . GLU B 1 114 ? -39.155 12.856  -57.076 1.00 62.57  ? 122 GLU B OE1 1 
ATOM 3154 O OE2 . GLU B 1 114 ? -40.692 12.487  -55.553 1.00 55.65  ? 122 GLU B OE2 1 
ATOM 3155 N N   . HIS B 1 115 ? -37.908 15.592  -59.985 1.00 51.94  ? 123 HIS B N   1 
ATOM 3156 C CA  . HIS B 1 115 ? -36.801 16.191  -60.724 1.00 55.49  ? 123 HIS B CA  1 
ATOM 3157 C C   . HIS B 1 115 ? -36.507 15.295  -61.923 1.00 58.83  ? 123 HIS B C   1 
ATOM 3158 O O   . HIS B 1 115 ? -35.795 14.294  -61.799 1.00 60.41  ? 123 HIS B O   1 
ATOM 3159 C CB  . HIS B 1 115 ? -35.581 16.356  -59.827 1.00 53.29  ? 123 HIS B CB  1 
ATOM 3160 C CG  . HIS B 1 115 ? -35.800 17.291  -58.680 1.00 54.61  ? 123 HIS B CG  1 
ATOM 3161 N ND1 . HIS B 1 115 ? -36.376 18.533  -58.832 1.00 61.93  ? 123 HIS B ND1 1 
ATOM 3162 C CD2 . HIS B 1 115 ? -35.541 17.156  -57.357 1.00 54.51  ? 123 HIS B CD2 1 
ATOM 3163 C CE1 . HIS B 1 115 ? -36.449 19.130  -57.656 1.00 60.89  ? 123 HIS B CE1 1 
ATOM 3164 N NE2 . HIS B 1 115 ? -35.949 18.315  -56.744 1.00 60.78  ? 123 HIS B NE2 1 
ATOM 3165 N N   . ARG B 1 116 ? -37.057 15.656  -63.077 1.00 61.37  ? 124 ARG B N   1 
ATOM 3166 C CA  . ARG B 1 116 ? -36.873 14.875  -64.288 1.00 66.93  ? 124 ARG B CA  1 
ATOM 3167 C C   . ARG B 1 116 ? -35.511 15.169  -64.909 1.00 70.91  ? 124 ARG B C   1 
ATOM 3168 O O   . ARG B 1 116 ? -34.883 16.194  -64.634 1.00 67.42  ? 124 ARG B O   1 
ATOM 3169 C CB  . ARG B 1 116 ? -37.987 15.179  -65.289 1.00 65.95  ? 124 ARG B CB  1 
ATOM 3170 C CG  . ARG B 1 116 ? -39.373 14.804  -64.794 1.00 60.22  ? 124 ARG B CG  1 
ATOM 3171 C CD  . ARG B 1 116 ? -40.449 15.247  -65.769 1.00 70.68  ? 124 ARG B CD  1 
ATOM 3172 N NE  . ARG B 1 116 ? -41.691 14.505  -65.587 1.00 67.92  ? 124 ARG B NE  1 
ATOM 3173 C CZ  . ARG B 1 116 ? -41.917 13.289  -66.067 1.00 69.59  ? 124 ARG B CZ  1 
ATOM 3174 N NH1 . ARG B 1 116 ? -40.998 12.637  -66.760 1.00 67.97  ? 124 ARG B NH1 1 
ATOM 3175 N NH2 . ARG B 1 116 ? -43.093 12.710  -65.839 1.00 67.16  ? 124 ARG B NH2 1 
ATOM 3176 N N   . LEU B 1 117 ? -35.066 14.257  -65.771 1.00 67.11  ? 125 LEU B N   1 
ATOM 3177 C CA  . LEU B 1 117 ? -33.780 14.421  -66.431 1.00 64.24  ? 125 LEU B CA  1 
ATOM 3178 C C   . LEU B 1 117 ? -33.779 15.705  -67.260 1.00 71.75  ? 125 LEU B C   1 
ATOM 3179 O O   . LEU B 1 117 ? -34.821 16.118  -67.781 1.00 74.14  ? 125 LEU B O   1 
ATOM 3180 C CB  . LEU B 1 117 ? -33.482 13.215  -67.321 1.00 56.29  ? 125 LEU B CB  1 
ATOM 3181 C CG  . LEU B 1 117 ? -33.366 11.864  -66.611 1.00 48.66  ? 125 LEU B CG  1 
ATOM 3182 C CD1 . LEU B 1 117 ? -32.973 10.772  -67.592 1.00 52.75  ? 125 LEU B CD1 1 
ATOM 3183 C CD2 . LEU B 1 117 ? -32.367 11.946  -65.467 1.00 60.30  ? 125 LEU B CD2 1 
ATOM 3184 N N   . PRO B 1 118 ? -32.618 16.365  -67.404 1.00 67.03  ? 126 PRO B N   1 
ATOM 3185 C CA  . PRO B 1 118 ? -31.267 15.964  -66.988 1.00 60.50  ? 126 PRO B CA  1 
ATOM 3186 C C   . PRO B 1 118 ? -30.892 16.358  -65.562 1.00 67.97  ? 126 PRO B C   1 
ATOM 3187 O O   . PRO B 1 118 ? -29.710 16.570  -65.300 1.00 69.81  ? 126 PRO B O   1 
ATOM 3188 C CB  . PRO B 1 118 ? -30.386 16.698  -68.002 1.00 69.78  ? 126 PRO B CB  1 
ATOM 3189 C CG  . PRO B 1 118 ? -31.121 17.991  -68.238 1.00 69.53  ? 126 PRO B CG  1 
ATOM 3190 C CD  . PRO B 1 118 ? -32.599 17.670  -68.090 1.00 70.19  ? 126 PRO B CD  1 
ATOM 3191 N N   . ALA B 1 119 ? -31.859 16.509  -64.650 1.00 70.46  ? 127 ALA B N   1 
ATOM 3192 C CA  . ALA B 1 119 ? -31.562 16.840  -63.257 1.00 63.57  ? 127 ALA B CA  1 
ATOM 3193 C C   . ALA B 1 119 ? -30.422 16.007  -62.683 1.00 60.30  ? 127 ALA B C   1 
ATOM 3194 O O   . ALA B 1 119 ? -29.455 16.550  -62.138 1.00 61.94  ? 127 ALA B O   1 
ATOM 3195 C CB  . ALA B 1 119 ? -32.820 16.674  -62.401 1.00 65.37  ? 127 ALA B CB  1 
ATOM 3196 N N   . ALA B 1 120 ? -30.527 14.680  -62.788 1.00 58.60  ? 128 ALA B N   1 
ATOM 3197 C CA  . ALA B 1 120 ? -29.501 13.809  -62.219 1.00 65.79  ? 128 ALA B CA  1 
ATOM 3198 C C   . ALA B 1 120 ? -28.140 14.064  -62.856 1.00 70.68  ? 128 ALA B C   1 
ATOM 3199 O O   . ALA B 1 120 ? -27.110 14.046  -62.170 1.00 65.81  ? 128 ALA B O   1 
ATOM 3200 C CB  . ALA B 1 120 ? -29.902 12.343  -62.379 1.00 66.01  ? 128 ALA B CB  1 
ATOM 3201 N N   . PHE B 1 121 ? -28.114 14.298  -64.169 1.00 69.35  ? 129 PHE B N   1 
ATOM 3202 C CA  . PHE B 1 121 ? -26.847 14.541  -64.851 1.00 62.17  ? 129 PHE B CA  1 
ATOM 3203 C C   . PHE B 1 121 ? -26.226 15.860  -64.408 1.00 65.31  ? 129 PHE B C   1 
ATOM 3204 O O   . PHE B 1 121 ? -25.013 15.934  -64.174 1.00 67.33  ? 129 PHE B O   1 
ATOM 3205 C CB  . PHE B 1 121 ? -27.055 14.524  -66.363 1.00 60.61  ? 129 PHE B CB  1 
ATOM 3206 C CG  . PHE B 1 121 ? -27.675 13.257  -66.869 1.00 64.60  ? 129 PHE B CG  1 
ATOM 3207 C CD1 . PHE B 1 121 ? -27.114 12.026  -66.568 1.00 70.88  ? 129 PHE B CD1 1 
ATOM 3208 C CD2 . PHE B 1 121 ? -28.825 13.294  -67.637 1.00 62.97  ? 129 PHE B CD2 1 
ATOM 3209 C CE1 . PHE B 1 121 ? -27.689 10.857  -67.027 1.00 69.88  ? 129 PHE B CE1 1 
ATOM 3210 C CE2 . PHE B 1 121 ? -29.403 12.130  -68.100 1.00 66.68  ? 129 PHE B CE2 1 
ATOM 3211 C CZ  . PHE B 1 121 ? -28.835 10.910  -67.796 1.00 67.69  ? 129 PHE B CZ  1 
ATOM 3212 N N   . GLU B 1 122 ? -27.039 16.915  -64.305 1.00 64.94  ? 130 GLU B N   1 
ATOM 3213 C CA  . GLU B 1 122 ? -26.560 18.189  -63.779 1.00 65.25  ? 130 GLU B CA  1 
ATOM 3214 C C   . GLU B 1 122 ? -25.946 18.012  -62.396 1.00 71.07  ? 130 GLU B C   1 
ATOM 3215 O O   . GLU B 1 122 ? -24.873 18.552  -62.101 1.00 72.99  ? 130 GLU B O   1 
ATOM 3216 C CB  . GLU B 1 122 ? -27.711 19.194  -63.720 1.00 57.04  ? 130 GLU B CB  1 
ATOM 3217 C CG  . GLU B 1 122 ? -28.365 19.488  -65.055 1.00 56.74  ? 130 GLU B CG  1 
ATOM 3218 C CD  . GLU B 1 122 ? -29.550 20.419  -64.914 1.00 66.41  ? 130 GLU B CD  1 
ATOM 3219 O OE1 . GLU B 1 122 ? -29.833 20.851  -63.777 1.00 65.68  ? 130 GLU B OE1 1 
ATOM 3220 O OE2 . GLU B 1 122 ? -30.203 20.715  -65.937 1.00 75.05  ? 130 GLU B OE2 1 
ATOM 3221 N N   . ASP B 1 123 ? -26.626 17.258  -61.531 1.00 70.25  ? 131 ASP B N   1 
ATOM 3222 C CA  . ASP B 1 123 ? -26.111 17.012  -60.189 1.00 72.26  ? 131 ASP B CA  1 
ATOM 3223 C C   . ASP B 1 123 ? -24.807 16.230  -60.235 1.00 72.98  ? 131 ASP B C   1 
ATOM 3224 O O   . ASP B 1 123 ? -23.893 16.487  -59.444 1.00 76.95  ? 131 ASP B O   1 
ATOM 3225 C CB  . ASP B 1 123 ? -27.153 16.260  -59.366 1.00 70.65  ? 131 ASP B CB  1 
ATOM 3226 C CG  . ASP B 1 123 ? -28.487 16.967  -59.340 1.00 69.45  ? 131 ASP B CG  1 
ATOM 3227 O OD1 . ASP B 1 123 ? -28.546 18.151  -59.735 1.00 71.18  ? 131 ASP B OD1 1 
ATOM 3228 O OD2 . ASP B 1 123 ? -29.480 16.332  -58.935 1.00 74.17  ? 131 ASP B OD2 1 
ATOM 3229 N N   . ALA B 1 124 ? -24.709 15.264  -61.149 1.00 68.83  ? 132 ALA B N   1 
ATOM 3230 C CA  . ALA B 1 124 ? -23.471 14.510  -61.317 1.00 74.11  ? 132 ALA B CA  1 
ATOM 3231 C C   . ALA B 1 124 ? -22.299 15.432  -61.616 1.00 77.31  ? 132 ALA B C   1 
ATOM 3232 O O   . ALA B 1 124 ? -21.234 15.327  -60.996 1.00 78.90  ? 132 ALA B O   1 
ATOM 3233 C CB  . ALA B 1 124 ? -23.640 13.488  -62.433 1.00 76.15  ? 132 ALA B CB  1 
ATOM 3234 N N   . GLU B 1 125 ? -22.470 16.326  -62.591 1.00 73.92  ? 133 GLU B N   1 
ATOM 3235 C CA  . GLU B 1 125 ? -21.448 17.328  -62.873 1.00 71.88  ? 133 GLU B CA  1 
ATOM 3236 C C   . GLU B 1 125 ? -21.127 18.148  -61.629 1.00 74.67  ? 133 GLU B C   1 
ATOM 3237 O O   . GLU B 1 125 ? -19.972 18.533  -61.411 1.00 79.23  ? 133 GLU B O   1 
ATOM 3238 C CB  . GLU B 1 125 ? -21.905 18.226  -64.022 1.00 76.94  ? 133 GLU B CB  1 
ATOM 3239 C CG  . GLU B 1 125 ? -21.813 17.556  -65.391 1.00 90.59  ? 133 GLU B CG  1 
ATOM 3240 C CD  . GLU B 1 125 ? -22.231 18.471  -66.525 1.00 92.61  ? 133 GLU B CD  1 
ATOM 3241 O OE1 . GLU B 1 125 ? -21.702 19.598  -66.610 1.00 108.64 ? 133 GLU B OE1 1 
ATOM 3242 O OE2 . GLU B 1 125 ? -23.089 18.059  -67.334 1.00 76.31  ? 133 GLU B OE2 1 
ATOM 3243 N N   . ALA B 1 126 ? -22.140 18.431  -60.804 1.00 72.43  ? 134 ALA B N   1 
ATOM 3244 C CA  . ALA B 1 126 ? -21.906 19.152  -59.555 1.00 74.14  ? 134 ALA B CA  1 
ATOM 3245 C C   . ALA B 1 126 ? -21.013 18.358  -58.606 1.00 78.04  ? 134 ALA B C   1 
ATOM 3246 O O   . ALA B 1 126 ? -20.203 18.943  -57.877 1.00 77.61  ? 134 ALA B O   1 
ATOM 3247 C CB  . ALA B 1 126 ? -23.237 19.493  -58.885 1.00 77.36  ? 134 ALA B CB  1 
ATOM 3248 N N   . VAL B 1 127 ? -21.158 17.029  -58.582 1.00 78.30  ? 135 VAL B N   1 
ATOM 3249 C CA  . VAL B 1 127 ? -20.278 16.200  -57.755 1.00 78.24  ? 135 VAL B CA  1 
ATOM 3250 C C   . VAL B 1 127 ? -18.826 16.399  -58.167 1.00 80.36  ? 135 VAL B C   1 
ATOM 3251 O O   . VAL B 1 127 ? -17.949 16.634  -57.328 1.00 79.60  ? 135 VAL B O   1 
ATOM 3252 C CB  . VAL B 1 127 ? -20.684 14.717  -57.831 1.00 72.57  ? 135 VAL B CB  1 
ATOM 3253 C CG1 . VAL B 1 127 ? -20.035 13.938  -56.699 1.00 73.35  ? 135 VAL B CG1 1 
ATOM 3254 C CG2 . VAL B 1 127 ? -22.187 14.568  -57.753 1.00 73.18  ? 135 VAL B CG2 1 
ATOM 3255 N N   . LEU B 1 128 ? -18.552 16.279  -59.467 1.00 81.02  ? 136 LEU B N   1 
ATOM 3256 C CA  . LEU B 1 128 ? -17.204 16.488  -59.984 1.00 83.19  ? 136 LEU B CA  1 
ATOM 3257 C C   . LEU B 1 128 ? -16.669 17.859  -59.586 1.00 87.62  ? 136 LEU B C   1 
ATOM 3258 O O   . LEU B 1 128 ? -15.531 17.985  -59.120 1.00 90.68  ? 136 LEU B O   1 
ATOM 3259 C CB  . LEU B 1 128 ? -17.208 16.318  -61.501 1.00 77.44  ? 136 LEU B CB  1 
ATOM 3260 C CG  . LEU B 1 128 ? -17.546 14.896  -61.945 1.00 77.16  ? 136 LEU B CG  1 
ATOM 3261 C CD1 . LEU B 1 128 ? -17.692 14.838  -63.443 1.00 88.59  ? 136 LEU B CD1 1 
ATOM 3262 C CD2 . LEU B 1 128 ? -16.492 13.904  -61.473 1.00 77.02  ? 136 LEU B CD2 1 
ATOM 3263 N N   . THR B 1 129 ? -17.475 18.905  -59.792 1.00 83.87  ? 137 THR B N   1 
ATOM 3264 C CA  . THR B 1 129 ? -17.069 20.256  -59.413 1.00 83.69  ? 137 THR B CA  1 
ATOM 3265 C C   . THR B 1 129 ? -16.680 20.330  -57.941 1.00 88.23  ? 137 THR B C   1 
ATOM 3266 O O   . THR B 1 129 ? -15.693 20.984  -57.583 1.00 91.62  ? 137 THR B O   1 
ATOM 3267 C CB  . THR B 1 129 ? -18.192 21.250  -59.717 1.00 80.13  ? 137 THR B CB  1 
ATOM 3268 O OG1 . THR B 1 129 ? -18.623 21.089  -61.073 1.00 81.95  ? 137 THR B OG1 1 
ATOM 3269 C CG2 . THR B 1 129 ? -17.708 22.680  -59.516 1.00 81.43  ? 137 THR B CG2 1 
ATOM 3270 N N   . TRP B 1 130 ? -17.455 19.679  -57.069 1.00 89.68  ? 138 TRP B N   1 
ATOM 3271 C CA  . TRP B 1 130 ? -17.117 19.654  -55.648 1.00 90.38  ? 138 TRP B CA  1 
ATOM 3272 C C   . TRP B 1 130 ? -15.757 19.007  -55.413 1.00 94.08  ? 138 TRP B C   1 
ATOM 3273 O O   . TRP B 1 130 ? -14.957 19.503  -54.610 1.00 100.00 ? 138 TRP B O   1 
ATOM 3274 C CB  . TRP B 1 130 ? -18.201 18.924  -54.856 1.00 84.00  ? 138 TRP B CB  1 
ATOM 3275 C CG  . TRP B 1 130 ? -17.959 18.933  -53.374 1.00 79.65  ? 138 TRP B CG  1 
ATOM 3276 C CD1 . TRP B 1 130 ? -18.223 19.954  -52.509 1.00 79.60  ? 138 TRP B CD1 1 
ATOM 3277 C CD2 . TRP B 1 130 ? -17.396 17.876  -52.587 1.00 80.55  ? 138 TRP B CD2 1 
ATOM 3278 N NE1 . TRP B 1 130 ? -17.864 19.597  -51.232 1.00 79.57  ? 138 TRP B NE1 1 
ATOM 3279 C CE2 . TRP B 1 130 ? -17.353 18.326  -51.252 1.00 81.51  ? 138 TRP B CE2 1 
ATOM 3280 C CE3 . TRP B 1 130 ? -16.927 16.592  -52.880 1.00 86.52  ? 138 TRP B CE3 1 
ATOM 3281 C CZ2 . TRP B 1 130 ? -16.860 17.539  -50.214 1.00 91.26  ? 138 TRP B CZ2 1 
ATOM 3282 C CZ3 . TRP B 1 130 ? -16.438 15.812  -51.849 1.00 88.42  ? 138 TRP B CZ3 1 
ATOM 3283 C CH2 . TRP B 1 130 ? -16.408 16.288  -50.532 1.00 89.95  ? 138 TRP B CH2 1 
ATOM 3284 N N   . LEU B 1 131 ? -15.486 17.887  -56.090 1.00 90.82  ? 139 LEU B N   1 
ATOM 3285 C CA  . LEU B 1 131 ? -14.180 17.242  -55.974 1.00 93.39  ? 139 LEU B CA  1 
ATOM 3286 C C   . LEU B 1 131 ? -13.062 18.181  -56.414 1.00 94.14  ? 139 LEU B C   1 
ATOM 3287 O O   . LEU B 1 131 ? -12.030 18.295  -55.742 1.00 100.40 ? 139 LEU B O   1 
ATOM 3288 C CB  . LEU B 1 131 ? -14.150 15.952  -56.799 1.00 92.32  ? 139 LEU B CB  1 
ATOM 3289 C CG  . LEU B 1 131 ? -14.595 14.632  -56.159 1.00 88.25  ? 139 LEU B CG  1 
ATOM 3290 C CD1 . LEU B 1 131 ? -13.638 14.203  -55.051 1.00 83.63  ? 139 LEU B CD1 1 
ATOM 3291 C CD2 . LEU B 1 131 ? -16.020 14.714  -55.637 1.00 91.25  ? 139 LEU B CD2 1 
ATOM 3292 N N   . TRP B 1 132 ? -13.246 18.849  -57.556 1.00 88.10  ? 140 TRP B N   1 
ATOM 3293 C CA  . TRP B 1 132 ? -12.255 19.814  -58.022 1.00 95.79  ? 140 TRP B CA  1 
ATOM 3294 C C   . TRP B 1 132 ? -12.050 20.928  -57.006 1.00 101.30 ? 140 TRP B C   1 
ATOM 3295 O O   . TRP B 1 132 ? -10.911 21.317  -56.720 1.00 105.25 ? 140 TRP B O   1 
ATOM 3296 C CB  . TRP B 1 132 ? -12.679 20.386  -59.373 1.00 100.92 ? 140 TRP B CB  1 
ATOM 3297 C CG  . TRP B 1 132 ? -12.037 21.695  -59.721 1.00 104.32 ? 140 TRP B CG  1 
ATOM 3298 C CD1 . TRP B 1 132 ? -10.857 21.871  -60.383 1.00 106.55 ? 140 TRP B CD1 1 
ATOM 3299 C CD2 . TRP B 1 132 ? -12.555 23.008  -59.470 1.00 108.95 ? 140 TRP B CD2 1 
ATOM 3300 N NE1 . TRP B 1 132 ? -10.595 23.210  -60.538 1.00 112.78 ? 140 TRP B NE1 1 
ATOM 3301 C CE2 . TRP B 1 132 ? -11.622 23.930  -59.987 1.00 114.54 ? 140 TRP B CE2 1 
ATOM 3302 C CE3 . TRP B 1 132 ? -13.709 23.494  -58.848 1.00 105.84 ? 140 TRP B CE3 1 
ATOM 3303 C CZ2 . TRP B 1 132 ? -11.809 25.308  -59.903 1.00 117.92 ? 140 TRP B CZ2 1 
ATOM 3304 C CZ3 . TRP B 1 132 ? -13.892 24.863  -58.764 1.00 106.67 ? 140 TRP B CZ3 1 
ATOM 3305 C CH2 . TRP B 1 132 ? -12.947 25.753  -59.290 1.00 116.28 ? 140 TRP B CH2 1 
ATOM 3306 N N   . ASP B 1 133 ? -13.143 21.454  -56.448 1.00 98.80  ? 141 ASP B N   1 
ATOM 3307 C CA  . ASP B 1 133 ? -13.037 22.535  -55.477 1.00 97.08  ? 141 ASP B CA  1 
ATOM 3308 C C   . ASP B 1 133 ? -12.425 22.061  -54.168 1.00 95.85  ? 141 ASP B C   1 
ATOM 3309 O O   . ASP B 1 133 ? -11.856 22.874  -53.433 1.00 93.03  ? 141 ASP B O   1 
ATOM 3310 C CB  . ASP B 1 133 ? -14.411 23.155  -55.222 1.00 99.17  ? 141 ASP B CB  1 
ATOM 3311 C CG  . ASP B 1 133 ? -14.361 24.665  -55.138 1.00 106.13 ? 141 ASP B CG  1 
ATOM 3312 O OD1 . ASP B 1 133 ? -13.303 25.200  -54.747 1.00 102.42 ? 141 ASP B OD1 1 
ATOM 3313 O OD2 . ASP B 1 133 ? -15.371 25.318  -55.470 1.00 108.60 ? 141 ASP B OD2 1 
ATOM 3314 N N   . GLN B 1 134 ? -12.535 20.768  -53.864 1.00 100.98 ? 142 GLN B N   1 
ATOM 3315 C CA  . GLN B 1 134 ? -11.851 20.211  -52.705 1.00 107.00 ? 142 GLN B CA  1 
ATOM 3316 C C   . GLN B 1 134 ? -10.389 19.913  -53.014 1.00 114.58 ? 142 GLN B C   1 
ATOM 3317 O O   . GLN B 1 134 ? -9.556  19.888  -52.101 1.00 118.48 ? 142 GLN B O   1 
ATOM 3318 C CB  . GLN B 1 134 ? -12.561 18.937  -52.247 1.00 99.71  ? 142 GLN B CB  1 
ATOM 3319 C CG  . GLN B 1 134 ? -13.873 19.172  -51.512 1.00 95.62  ? 142 GLN B CG  1 
ATOM 3320 C CD  . GLN B 1 134 ? -13.738 20.121  -50.340 1.00 107.54 ? 142 GLN B CD  1 
ATOM 3321 O OE1 . GLN B 1 134 ? -14.160 21.276  -50.413 1.00 114.55 ? 142 GLN B OE1 1 
ATOM 3322 N NE2 . GLN B 1 134 ? -13.156 19.638  -49.249 1.00 106.09 ? 142 GLN B NE2 1 
ATOM 3323 N N   . ALA B 1 135 ? -10.069 19.679  -54.289 1.00 115.31 ? 143 ALA B N   1 
ATOM 3324 C CA  . ALA B 1 135 ? -8.701  19.396  -54.712 1.00 111.45 ? 143 ALA B CA  1 
ATOM 3325 C C   . ALA B 1 135 ? -7.858  20.665  -54.789 1.00 114.31 ? 143 ALA B C   1 
ATOM 3326 O O   . ALA B 1 135 ? -6.741  20.709  -54.261 1.00 116.22 ? 143 ALA B O   1 
ATOM 3327 C CB  . ALA B 1 135 ? -8.708  18.670  -56.058 1.00 103.11 ? 143 ALA B CB  1 
ATOM 3328 N N   . VAL B 1 136 ? -8.374  21.706  -55.449 1.00 110.81 ? 144 VAL B N   1 
ATOM 3329 C CA  . VAL B 1 136 ? -7.725  23.012  -55.461 1.00 108.64 ? 144 VAL B CA  1 
ATOM 3330 C C   . VAL B 1 136 ? -7.663  23.663  -54.088 1.00 117.81 ? 144 VAL B C   1 
ATOM 3331 O O   . VAL B 1 136 ? -7.040  24.718  -53.938 1.00 124.19 ? 144 VAL B O   1 
ATOM 3332 C CB  . VAL B 1 136 ? -8.441  23.957  -56.450 1.00 102.45 ? 144 VAL B CB  1 
ATOM 3333 C CG1 . VAL B 1 136 ? -8.517  23.323  -57.827 1.00 99.70  ? 144 VAL B CG1 1 
ATOM 3334 C CG2 . VAL B 1 136 ? -9.828  24.312  -55.936 1.00 104.72 ? 144 VAL B CG2 1 
ATOM 3335 N N   . SER B 1 137 ? -8.291  23.061  -53.081 1.00 118.75 ? 145 SER B N   1 
ATOM 3336 C CA  . SER B 1 137 ? -8.375  23.622  -51.739 1.00 126.60 ? 145 SER B CA  1 
ATOM 3337 C C   . SER B 1 137 ? -6.948  23.116  -51.918 1.00 143.88 ? 145 SER B C   1 
ATOM 3338 O O   . SER B 1 137 ? -6.710  22.222  -52.734 1.00 147.70 ? 145 SER B O   1 
ATOM 3339 C CB  . SER B 1 137 ? -9.513  22.972  -50.948 1.00 125.14 ? 145 SER B CB  1 
ATOM 3340 O OG  . SER B 1 137 ? -9.131  21.701  -50.453 1.00 125.81 ? 145 SER B OG  1 
ATOM 3341 N N   . ASP B 1 138 ? -6.004  23.689  -51.160 1.00 147.16 ? 146 ASP B N   1 
ATOM 3342 C CA  . ASP B 1 138 ? -4.559  23.495  -51.289 1.00 151.99 ? 146 ASP B CA  1 
ATOM 3343 C C   . ASP B 1 138 ? -4.462  22.188  -50.515 1.00 155.32 ? 146 ASP B C   1 
ATOM 3344 O O   . ASP B 1 138 ? -3.907  22.137  -49.414 1.00 164.95 ? 146 ASP B O   1 
ATOM 3345 C CB  . ASP B 1 138 ? -3.984  24.651  -50.457 1.00 154.96 ? 146 ASP B CB  1 
ATOM 3346 C CG  . ASP B 1 138 ? -4.784  24.942  -49.193 1.00 157.44 ? 146 ASP B CG  1 
ATOM 3347 O OD1 . ASP B 1 138 ? -5.909  25.470  -49.292 1.00 154.20 ? 146 ASP B OD1 1 
ATOM 3348 O OD2 . ASP B 1 138 ? -4.276  24.636  -48.094 1.00 155.63 ? 146 ASP B OD2 1 
ATOM 3349 N N   . GLY B 1 139 ? -4.976  21.125  -51.125 1.00 149.92 ? 147 GLY B N   1 
ATOM 3350 C CA  . GLY B 1 139 ? -5.006  19.788  -50.570 1.00 151.95 ? 147 GLY B CA  1 
ATOM 3351 C C   . GLY B 1 139 ? -5.317  19.702  -49.092 1.00 152.17 ? 147 GLY B C   1 
ATOM 3352 O O   . GLY B 1 139 ? -4.745  18.866  -48.383 1.00 153.06 ? 147 GLY B O   1 
ATOM 3353 N N   . VAL B 1 140 ? -6.221  20.575  -48.642 1.00 146.67 ? 148 VAL B N   1 
ATOM 3354 C CA  . VAL B 1 140 ? -6.676  20.465  -47.231 1.00 144.28 ? 148 VAL B CA  1 
ATOM 3355 C C   . VAL B 1 140 ? -7.535  19.198  -47.192 1.00 141.90 ? 148 VAL B C   1 
ATOM 3356 O O   . VAL B 1 140 ? -8.585  19.192  -47.867 1.00 134.15 ? 148 VAL B O   1 
ATOM 3357 C CB  . VAL B 1 140 ? -7.477  21.693  -46.768 1.00 138.93 ? 148 VAL B CB  1 
ATOM 3358 C CG1 . VAL B 1 140 ? -8.036  21.506  -45.363 1.00 131.52 ? 148 VAL B CG1 1 
ATOM 3359 C CG2 . VAL B 1 140 ? -6.654  22.971  -46.855 1.00 141.21 ? 148 VAL B CG2 1 
ATOM 3360 N N   . ASN B 1 141 ? -7.065  18.159  -46.495 1.00 143.37 ? 149 ASN B N   1 
ATOM 3361 C CA  . ASN B 1 141 ? -7.815  16.876  -46.450 1.00 135.78 ? 149 ASN B CA  1 
ATOM 3362 C C   . ASN B 1 141 ? -9.296  17.228  -46.401 1.00 128.43 ? 149 ASN B C   1 
ATOM 3363 O O   . ASN B 1 141 ? -10.045 16.721  -47.257 1.00 128.76 ? 149 ASN B O   1 
ATOM 3364 C CB  . ASN B 1 141 ? -7.410  16.012  -45.265 1.00 138.50 ? 149 ASN B CB  1 
ATOM 3365 C CG  . ASN B 1 141 ? -6.024  15.441  -45.441 1.00 135.69 ? 149 ASN B CG  1 
ATOM 3366 O OD1 . ASN B 1 141 ? -5.835  14.493  -46.210 1.00 129.10 ? 149 ASN B OD1 1 
ATOM 3367 N ND2 . ASN B 1 141 ? -5.049  15.997  -44.739 1.00 134.85 ? 149 ASN B ND2 1 
ATOM 3368 N N   . HIS B 1 142 ? -9.701  18.028  -45.412 1.00 129.25 ? 150 HIS B N   1 
ATOM 3369 C CA  . HIS B 1 142 ? -11.108 18.506  -45.337 1.00 132.69 ? 150 HIS B CA  1 
ATOM 3370 C C   . HIS B 1 142 ? -12.089 17.331  -45.355 1.00 130.05 ? 150 HIS B C   1 
ATOM 3371 O O   . HIS B 1 142 ? -13.298 17.580  -45.536 1.00 120.28 ? 150 HIS B O   1 
ATOM 3372 C CB  . HIS B 1 142 ? -11.405 19.472  -46.488 1.00 132.92 ? 150 HIS B CB  1 
ATOM 3373 C CG  . HIS B 1 142 ? -11.125 20.902  -46.176 1.00 136.41 ? 150 HIS B CG  1 
ATOM 3374 N ND1 . HIS B 1 142 ? -11.243 21.903  -47.116 1.00 138.44 ? 150 HIS B ND1 1 
ATOM 3375 C CD2 . HIS B 1 142 ? -10.739 21.501  -45.045 1.00 132.92 ? 150 HIS B CD2 1 
ATOM 3376 C CE1 . HIS B 1 142 ? -10.936 23.064  -46.557 1.00 136.49 ? 150 HIS B CE1 1 
ATOM 3377 N NE2 . HIS B 1 142 ? -10.627 22.843  -45.299 1.00 133.55 ? 150 HIS B NE2 1 
ATOM 3378 N N   . TRP B 1 143 ? -11.566 16.113  -45.234 1.00 127.59 ? 151 TRP B N   1 
ATOM 3379 C CA  . TRP B 1 143 ? -12.432 14.916  -45.154 1.00 120.34 ? 151 TRP B CA  1 
ATOM 3380 C C   . TRP B 1 143 ? -11.994 14.163  -43.912 1.00 116.32 ? 151 TRP B C   1 
ATOM 3381 O O   . TRP B 1 143 ? -12.707 14.197  -42.889 1.00 111.55 ? 151 TRP B O   1 
ATOM 3382 C CB  . TRP B 1 143 ? -12.249 14.063  -46.412 1.00 112.76 ? 151 TRP B CB  1 
ATOM 3383 C CG  . TRP B 1 143 ? -12.594 14.782  -47.688 1.00 113.92 ? 151 TRP B CG  1 
ATOM 3384 C CD1 . TRP B 1 143 ? -13.565 15.721  -47.868 1.00 113.47 ? 151 TRP B CD1 1 
ATOM 3385 C CD2 . TRP B 1 143 ? -11.962 14.608  -48.972 1.00 124.31 ? 151 TRP B CD2 1 
ATOM 3386 N NE1 . TRP B 1 143 ? -13.574 16.153  -49.165 1.00 118.04 ? 151 TRP B NE1 1 
ATOM 3387 C CE2 . TRP B 1 143 ? -12.608 15.486  -49.868 1.00 126.15 ? 151 TRP B CE2 1 
ATOM 3388 C CE3 . TRP B 1 143 ? -10.922 13.805  -49.447 1.00 126.06 ? 151 TRP B CE3 1 
ATOM 3389 C CZ2 . TRP B 1 143 ? -12.246 15.577  -51.209 1.00 118.82 ? 151 TRP B CZ2 1 
ATOM 3390 C CZ3 . TRP B 1 143 ? -10.566 13.897  -50.774 1.00 126.29 ? 151 TRP B CZ3 1 
ATOM 3391 C CH2 . TRP B 1 143 ? -11.220 14.771  -51.640 1.00 121.15 ? 151 TRP B CH2 1 
ATOM 3392 N N   . PHE B 1 144 ? -10.831 13.528  -43.994 1.00 115.71 ? 152 PHE B N   1 
ATOM 3393 C CA  . PHE B 1 144 ? -10.262 12.845  -42.810 1.00 113.33 ? 152 PHE B CA  1 
ATOM 3394 C C   . PHE B 1 144 ? -8.803  13.264  -42.755 1.00 123.90 ? 152 PHE B C   1 
ATOM 3395 O O   . PHE B 1 144 ? -7.949  12.570  -43.341 1.00 128.68 ? 152 PHE B O   1 
ATOM 3396 C CB  . PHE B 1 144 ? -10.475 11.338  -42.942 1.00 112.47 ? 152 PHE B CB  1 
ATOM 3397 C CG  . PHE B 1 144 ? -11.583 10.932  -43.902 1.00 111.85 ? 152 PHE B CG  1 
ATOM 3398 C CD1 . PHE B 1 144 ? -12.903 10.859  -43.476 1.00 111.36 ? 152 PHE B CD1 1 
ATOM 3399 C CD2 . PHE B 1 144 ? -11.302 10.633  -45.229 1.00 109.87 ? 152 PHE B CD2 1 
ATOM 3400 C CE1 . PHE B 1 144 ? -13.909 10.489  -44.353 1.00 105.50 ? 152 PHE B CE1 1 
ATOM 3401 C CE2 . PHE B 1 144 ? -12.313 10.269  -46.100 1.00 106.53 ? 152 PHE B CE2 1 
ATOM 3402 C CZ  . PHE B 1 144 ? -13.611 10.192  -45.659 1.00 105.45 ? 152 PHE B CZ  1 
ATOM 3403 N N   . GLU B 1 145 ? -8.521  14.390  -42.095 1.00 128.48 ? 153 GLU B N   1 
ATOM 3404 C CA  . GLU B 1 145 ? -7.137  14.927  -42.015 1.00 127.78 ? 153 GLU B CA  1 
ATOM 3405 C C   . GLU B 1 145 ? -6.115  13.801  -41.784 1.00 133.14 ? 153 GLU B C   1 
ATOM 3406 O O   . GLU B 1 145 ? -5.007  13.897  -42.352 1.00 131.37 ? 153 GLU B O   1 
ATOM 3407 C CB  . GLU B 1 145 ? -7.109  15.985  -40.914 1.00 120.87 ? 153 GLU B CB  1 
ATOM 3408 C CG  . GLU B 1 145 ? -8.334  16.893  -40.942 1.00 112.08 ? 153 GLU B CG  1 
ATOM 3409 C CD  . GLU B 1 145 ? -8.175  18.145  -40.102 1.00 119.67 ? 153 GLU B CD  1 
ATOM 3410 O OE1 . GLU B 1 145 ? -7.166  18.235  -39.374 1.00 143.39 ? 153 GLU B OE1 1 
ATOM 3411 O OE2 . GLU B 1 145 ? -9.055  19.027  -40.175 1.00 114.77 ? 153 GLU B OE2 1 
ATOM 3412 N N   . ASP B 1 146 ? -6.461  12.787  -40.986 1.00 137.55 ? 154 ASP B N   1 
ATOM 3413 C CA  . ASP B 1 146 ? -5.559  11.635  -40.716 1.00 131.34 ? 154 ASP B CA  1 
ATOM 3414 C C   . ASP B 1 146 ? -5.733  10.889  -42.037 1.00 130.80 ? 154 ASP B C   1 
ATOM 3415 O O   . ASP B 1 146 ? -6.637  10.032  -42.104 1.00 128.79 ? 154 ASP B O   1 
ATOM 3416 C CB  . ASP B 1 146 ? -6.133  10.779  -39.604 1.00 124.31 ? 154 ASP B CB  1 
ATOM 3417 C CG  . ASP B 1 146 ? -7.646  10.617  -39.650 1.00 129.55 ? 154 ASP B CG  1 
ATOM 3418 O OD1 . ASP B 1 146 ? -8.105  9.503   -39.975 1.00 136.65 ? 154 ASP B OD1 1 
ATOM 3419 O OD2 . ASP B 1 146 ? -8.352  11.611  -39.375 1.00 125.63 ? 154 ASP B OD2 1 
ATOM 3420 N N   . GLY B 1 147 ? -4.891  11.165  -43.036 1.00 130.87 ? 155 GLY B N   1 
ATOM 3421 C CA  . GLY B 1 147 ? -5.137  10.568  -44.361 1.00 119.69 ? 155 GLY B CA  1 
ATOM 3422 C C   . GLY B 1 147 ? -3.917  10.719  -45.236 1.00 118.05 ? 155 GLY B C   1 
ATOM 3423 O O   . GLY B 1 147 ? -3.042  11.547  -44.906 1.00 117.81 ? 155 GLY B O   1 
ATOM 3424 N N   . THR B 1 148 ? -3.874  9.946   -46.324 1.00 117.50 ? 156 THR B N   1 
ATOM 3425 C CA  . THR B 1 148 ? -2.740  9.980   -47.260 1.00 111.78 ? 156 THR B CA  1 
ATOM 3426 C C   . THR B 1 148 ? -3.161  10.809  -48.442 1.00 111.52 ? 156 THR B C   1 
ATOM 3427 O O   . THR B 1 148 ? -4.113  10.404  -49.142 1.00 107.89 ? 156 THR B O   1 
ATOM 3428 C CB  . THR B 1 148 ? -2.399  8.539   -47.623 1.00 111.07 ? 156 THR B CB  1 
ATOM 3429 O OG1 . THR B 1 148 ? -3.564  7.964   -48.206 1.00 106.97 ? 156 THR B OG1 1 
ATOM 3430 C CG2 . THR B 1 148 ? -1.958  7.761   -46.396 1.00 115.87 ? 156 THR B CG2 1 
ATOM 3431 N N   . ASP B 1 149 ? -2.510  11.956  -48.631 1.00 117.20 ? 157 ASP B N   1 
ATOM 3432 C CA  . ASP B 1 149 ? -2.919  12.871  -49.728 1.00 116.65 ? 157 ASP B CA  1 
ATOM 3433 C C   . ASP B 1 149 ? -3.218  12.046  -50.980 1.00 119.18 ? 157 ASP B C   1 
ATOM 3434 O O   . ASP B 1 149 ? -2.338  11.259  -51.386 1.00 118.78 ? 157 ASP B O   1 
ATOM 3435 C CB  . ASP B 1 149 ? -1.888  13.958  -49.976 1.00 113.87 ? 157 ASP B CB  1 
ATOM 3436 C CG  . ASP B 1 149 ? -2.172  14.845  -51.178 1.00 119.46 ? 157 ASP B CG  1 
ATOM 3437 O OD1 . ASP B 1 149 ? -3.342  15.251  -51.343 1.00 115.65 ? 157 ASP B OD1 1 
ATOM 3438 O OD2 . ASP B 1 149 ? -1.223  15.115  -51.943 1.00 125.87 ? 157 ASP B OD2 1 
ATOM 3439 N N   . VAL B 1 150 ? -4.396  12.241  -51.573 1.00 115.05 ? 158 VAL B N   1 
ATOM 3440 C CA  . VAL B 1 150 ? -4.831  11.494  -52.798 1.00 113.12 ? 158 VAL B CA  1 
ATOM 3441 C C   . VAL B 1 150 ? -4.569  9.990   -52.991 1.00 113.11 ? 158 VAL B C   1 
ATOM 3442 O O   . VAL B 1 150 ? -4.210  9.595   -54.118 1.00 112.89 ? 158 VAL B O   1 
ATOM 3443 C CB  . VAL B 1 150 ? -4.486  12.181  -54.138 1.00 105.61 ? 158 VAL B CB  1 
ATOM 3444 C CG1 . VAL B 1 150 ? -4.854  11.296  -55.320 1.00 105.33 ? 158 VAL B CG1 1 
ATOM 3445 C CG2 . VAL B 1 150 ? -5.116  13.560  -54.296 1.00 104.78 ? 158 VAL B CG2 1 
ATOM 3446 N N   . ASP B 1 151 ? -4.826  9.168   -51.959 1.00 114.25 ? 159 ASP B N   1 
ATOM 3447 C CA  . ASP B 1 151 ? -4.761  7.690   -52.129 1.00 114.66 ? 159 ASP B CA  1 
ATOM 3448 C C   . ASP B 1 151 ? -5.434  7.915   -53.479 1.00 112.65 ? 159 ASP B C   1 
ATOM 3449 O O   . ASP B 1 151 ? -6.528  8.520   -53.505 1.00 110.74 ? 159 ASP B O   1 
ATOM 3450 C CB  . ASP B 1 151 ? -5.839  6.859   -51.453 1.00 114.62 ? 159 ASP B CB  1 
ATOM 3451 C CG  . ASP B 1 151 ? -5.886  6.948   -49.935 1.00 116.01 ? 159 ASP B CG  1 
ATOM 3452 O OD1 . ASP B 1 151 ? -4.902  7.439   -49.343 1.00 115.38 ? 159 ASP B OD1 1 
ATOM 3453 O OD2 . ASP B 1 151 ? -6.914  6.535   -49.360 1.00 116.39 ? 159 ASP B OD2 1 
ATOM 3454 N N   . PHE B 1 152 ? -4.793  7.459   -54.556 1.00 111.49 ? 160 PHE B N   1 
ATOM 3455 C CA  . PHE B 1 152 ? -5.432  7.518   -55.893 1.00 112.28 ? 160 PHE B CA  1 
ATOM 3456 C C   . PHE B 1 152 ? -6.027  8.745   -56.538 1.00 111.82 ? 160 PHE B C   1 
ATOM 3457 O O   . PHE B 1 152 ? -7.230  8.755   -56.841 1.00 110.96 ? 160 PHE B O   1 
ATOM 3458 C CB  . PHE B 1 152 ? -6.141  6.259   -56.389 1.00 106.04 ? 160 PHE B CB  1 
ATOM 3459 C CG  . PHE B 1 152 ? -7.216  5.851   -55.405 1.00 100.44 ? 160 PHE B CG  1 
ATOM 3460 C CD1 . PHE B 1 152 ? -8.458  6.463   -55.438 1.00 98.45  ? 160 PHE B CD1 1 
ATOM 3461 C CD2 . PHE B 1 152 ? -6.959  4.905   -54.427 1.00 100.63 ? 160 PHE B CD2 1 
ATOM 3462 C CE1 . PHE B 1 152 ? -9.432  6.130   -54.529 1.00 99.83  ? 160 PHE B CE1 1 
ATOM 3463 C CE2 . PHE B 1 152 ? -7.939  4.577   -53.521 1.00 106.21 ? 160 PHE B CE2 1 
ATOM 3464 C CZ  . PHE B 1 152 ? -9.161  5.195   -53.579 1.00 104.09 ? 160 PHE B CZ  1 
ATOM 3465 N N   . ASP B 1 153 ? -5.217  9.781   -56.737 1.00 111.99 ? 161 ASP B N   1 
ATOM 3466 C CA  . ASP B 1 153 ? -5.726  10.955  -57.490 1.00 110.71 ? 161 ASP B CA  1 
ATOM 3467 C C   . ASP B 1 153 ? -6.509  10.409  -58.685 1.00 114.23 ? 161 ASP B C   1 
ATOM 3468 O O   . ASP B 1 153 ? -7.519  11.029  -59.053 1.00 109.30 ? 161 ASP B O   1 
ATOM 3469 C CB  . ASP B 1 153 ? -4.572  11.864  -57.863 1.00 112.96 ? 161 ASP B CB  1 
ATOM 3470 C CG  . ASP B 1 153 ? -4.988  13.152  -58.557 1.00 117.41 ? 161 ASP B CG  1 
ATOM 3471 O OD1 . ASP B 1 153 ? -6.206  13.355  -58.738 1.00 119.21 ? 161 ASP B OD1 1 
ATOM 3472 O OD2 . ASP B 1 153 ? -4.088  13.947  -58.896 1.00 112.84 ? 161 ASP B OD2 1 
ATOM 3473 N N   . ARG B 1 154 ? -6.050  9.306   -59.278 1.00 116.23 ? 162 ARG B N   1 
ATOM 3474 C CA  . ARG B 1 154 ? -6.771  8.628   -60.380 1.00 117.52 ? 162 ARG B CA  1 
ATOM 3475 C C   . ARG B 1 154 ? -8.251  8.379   -60.047 1.00 117.46 ? 162 ARG B C   1 
ATOM 3476 O O   . ARG B 1 154 ? -8.498  7.610   -59.096 1.00 114.17 ? 162 ARG B O   1 
ATOM 3477 C CB  . ARG B 1 154 ? -6.088  7.263   -60.420 1.00 114.32 ? 162 ARG B CB  1 
ATOM 3478 C CG  . ARG B 1 154 ? -4.674  7.270   -59.858 1.00 110.61 ? 162 ARG B CG  1 
ATOM 3479 C CD  . ARG B 1 154 ? -3.859  6.102   -60.381 1.00 117.67 ? 162 ARG B CD  1 
ATOM 3480 N NE  . ARG B 1 154 ? -4.707  4.943   -60.678 1.00 117.62 ? 162 ARG B NE  1 
ATOM 3481 C CZ  . ARG B 1 154 ? -4.766  3.851   -59.929 1.00 113.57 ? 162 ARG B CZ  1 
ATOM 3482 N NH1 . ARG B 1 154 ? -4.311  3.876   -58.690 1.00 111.54 ? 162 ARG B NH1 1 
ATOM 3483 N NH2 . ARG B 1 154 ? -5.277  2.738   -60.421 1.00 112.90 ? 162 ARG B NH2 1 
ATOM 3484 N N   . VAL B 1 155 ? -9.203  8.937   -60.814 1.00 114.70 ? 163 VAL B N   1 
ATOM 3485 C CA  . VAL B 1 155 ? -10.596 8.710   -60.453 1.00 104.73 ? 163 VAL B CA  1 
ATOM 3486 C C   . VAL B 1 155 ? -11.280 7.802   -61.454 1.00 102.02 ? 163 VAL B C   1 
ATOM 3487 O O   . VAL B 1 155 ? -10.990 7.802   -62.657 1.00 104.12 ? 163 VAL B O   1 
ATOM 3488 C CB  . VAL B 1 155 ? -11.361 10.034  -60.279 1.00 101.18 ? 163 VAL B CB  1 
ATOM 3489 C CG1 . VAL B 1 155 ? -10.619 10.845  -59.295 1.00 99.01  ? 163 VAL B CG1 1 
ATOM 3490 C CG2 . VAL B 1 155 ? -11.495 10.773  -61.592 1.00 103.96 ? 163 VAL B CG2 1 
ATOM 3491 N N   . PHE B 1 156 ? -12.214 7.017   -60.920 1.00 94.95  ? 164 PHE B N   1 
ATOM 3492 C CA  . PHE B 1 156 ? -12.899 5.964   -61.649 1.00 93.22  ? 164 PHE B CA  1 
ATOM 3493 C C   . PHE B 1 156 ? -14.368 6.031   -61.271 1.00 84.78  ? 164 PHE B C   1 
ATOM 3494 O O   . PHE B 1 156 ? -14.712 5.854   -60.099 1.00 86.66  ? 164 PHE B O   1 
ATOM 3495 C CB  . PHE B 1 156 ? -12.302 4.623   -61.242 1.00 95.74  ? 164 PHE B CB  1 
ATOM 3496 C CG  . PHE B 1 156 ? -10.854 4.498   -61.578 1.00 100.98 ? 164 PHE B CG  1 
ATOM 3497 C CD1 . PHE B 1 156 ? -10.441 4.221   -62.867 1.00 105.90 ? 164 PHE B CD1 1 
ATOM 3498 C CD2 . PHE B 1 156 ? -9.894  4.743   -60.607 1.00 98.93  ? 164 PHE B CD2 1 
ATOM 3499 C CE1 . PHE B 1 156 ? -9.097  4.125   -63.169 1.00 107.89 ? 164 PHE B CE1 1 
ATOM 3500 C CE2 . PHE B 1 156 ? -8.551  4.652   -60.906 1.00 106.79 ? 164 PHE B CE2 1 
ATOM 3501 C CZ  . PHE B 1 156 ? -8.152  4.347   -62.185 1.00 109.33 ? 164 PHE B CZ  1 
ATOM 3502 N N   . VAL B 1 157 ? -15.222 6.262   -62.242 1.00 84.45  ? 165 VAL B N   1 
ATOM 3503 C CA  . VAL B 1 157 ? -16.655 6.333   -61.997 1.00 82.38  ? 165 VAL B CA  1 
ATOM 3504 C C   . VAL B 1 157 ? -17.237 4.931   -62.085 1.00 81.40  ? 165 VAL B C   1 
ATOM 3505 O O   . VAL B 1 157 ? -16.840 4.131   -62.940 1.00 83.47  ? 165 VAL B O   1 
ATOM 3506 C CB  . VAL B 1 157 ? -17.324 7.295   -62.997 1.00 83.56  ? 165 VAL B CB  1 
ATOM 3507 C CG1 . VAL B 1 157 ? -18.840 7.233   -62.882 1.00 78.17  ? 165 VAL B CG1 1 
ATOM 3508 C CG2 . VAL B 1 157 ? -16.810 8.713   -62.790 1.00 75.60  ? 165 VAL B CG2 1 
ATOM 3509 N N   . VAL B 1 158 ? -18.193 4.632   -61.207 1.00 77.92  ? 166 VAL B N   1 
ATOM 3510 C CA  . VAL B 1 158 ? -18.859 3.334   -61.178 1.00 77.11  ? 166 VAL B CA  1 
ATOM 3511 C C   . VAL B 1 158 ? -20.356 3.580   -61.062 1.00 76.77  ? 166 VAL B C   1 
ATOM 3512 O O   . VAL B 1 158 ? -20.809 4.242   -60.122 1.00 77.53  ? 166 VAL B O   1 
ATOM 3513 C CB  . VAL B 1 158 ? -18.372 2.448   -60.016 1.00 74.24  ? 166 VAL B CB  1 
ATOM 3514 C CG1 . VAL B 1 158 ? -18.984 1.060   -60.113 1.00 76.79  ? 166 VAL B CG1 1 
ATOM 3515 C CG2 . VAL B 1 158 ? -16.851 2.358   -60.003 1.00 75.69  ? 166 VAL B CG2 1 
ATOM 3516 N N   . GLY B 1 159 ? -21.124 3.047   -62.008 1.00 76.32  ? 167 GLY B N   1 
ATOM 3517 C CA  . GLY B 1 159 ? -22.545 3.323   -62.061 1.00 75.65  ? 167 GLY B CA  1 
ATOM 3518 C C   . GLY B 1 159 ? -23.424 2.090   -62.058 1.00 78.85  ? 167 GLY B C   1 
ATOM 3519 O O   . GLY B 1 159 ? -23.324 1.238   -62.946 1.00 81.64  ? 167 GLY B O   1 
ATOM 3520 N N   . ASP B 1 160 ? -24.298 1.991   -61.062 1.00 78.71  ? 168 ASP B N   1 
ATOM 3521 C CA  . ASP B 1 160 ? -25.238 0.888   -60.936 1.00 78.00  ? 168 ASP B CA  1 
ATOM 3522 C C   . ASP B 1 160 ? -26.573 1.314   -61.534 1.00 74.76  ? 168 ASP B C   1 
ATOM 3523 O O   . ASP B 1 160 ? -27.051 2.422   -61.278 1.00 77.55  ? 168 ASP B O   1 
ATOM 3524 C CB  . ASP B 1 160 ? -25.404 0.499   -59.461 1.00 76.41  ? 168 ASP B CB  1 
ATOM 3525 C CG  . ASP B 1 160 ? -26.488 -0.555  -59.221 1.00 80.49  ? 168 ASP B CG  1 
ATOM 3526 O OD1 . ASP B 1 160 ? -27.263 -0.901  -60.135 1.00 82.86  ? 168 ASP B OD1 1 
ATOM 3527 O OD2 . ASP B 1 160 ? -26.571 -1.038  -58.072 1.00 75.53  ? 168 ASP B OD2 1 
ATOM 3528 N N   . SER B 1 161 ? -27.178 0.417   -62.317 1.00 71.48  ? 169 SER B N   1 
ATOM 3529 C CA  . SER B 1 161 ? -28.485 0.661   -62.923 1.00 73.51  ? 169 SER B CA  1 
ATOM 3530 C C   . SER B 1 161 ? -28.528 2.003   -63.639 1.00 73.26  ? 169 SER B C   1 
ATOM 3531 O O   . SER B 1 161 ? -27.792 2.221   -64.607 1.00 77.11  ? 169 SER B O   1 
ATOM 3532 C CB  . SER B 1 161 ? -29.593 0.602   -61.868 1.00 62.93  ? 169 SER B CB  1 
ATOM 3533 O OG  . SER B 1 161 ? -30.866 0.466   -62.480 1.00 46.66  ? 169 SER B OG  1 
ATOM 3534 N N   . SER B 1 162 ? -29.415 2.892   -63.183 1.00 71.98  ? 170 SER B N   1 
ATOM 3535 C CA  . SER B 1 162 ? -29.407 4.266   -63.670 1.00 69.74  ? 170 SER B CA  1 
ATOM 3536 C C   . SER B 1 162 ? -28.023 4.884   -63.548 1.00 69.54  ? 170 SER B C   1 
ATOM 3537 O O   . SER B 1 162 ? -27.556 5.553   -64.474 1.00 74.12  ? 170 SER B O   1 
ATOM 3538 C CB  . SER B 1 162 ? -30.438 5.098   -62.907 1.00 71.73  ? 170 SER B CB  1 
ATOM 3539 O OG  . SER B 1 162 ? -30.238 5.011   -61.506 1.00 72.32  ? 170 SER B OG  1 
ATOM 3540 N N   . GLY B 1 163 ? -27.332 4.614   -62.432 1.00 69.58  ? 171 GLY B N   1 
ATOM 3541 C CA  . GLY B 1 163 ? -25.992 5.151   -62.224 1.00 74.35  ? 171 GLY B CA  1 
ATOM 3542 C C   . GLY B 1 163 ? -25.071 4.969   -63.413 1.00 77.42  ? 171 GLY B C   1 
ATOM 3543 O O   . GLY B 1 163 ? -24.229 5.826   -63.695 1.00 75.91  ? 171 GLY B O   1 
ATOM 3544 N N   . GLY B 1 164 ? -25.200 3.842   -64.112 1.00 81.24  ? 172 GLY B N   1 
ATOM 3545 C CA  . GLY B 1 164 ? -24.418 3.648   -65.320 1.00 79.60  ? 172 GLY B CA  1 
ATOM 3546 C C   . GLY B 1 164 ? -24.688 4.723   -66.356 1.00 77.16  ? 172 GLY B C   1 
ATOM 3547 O O   . GLY B 1 164 ? -23.761 5.279   -66.950 1.00 79.99  ? 172 GLY B O   1 
ATOM 3548 N N   . ASN B 1 165 ? -25.968 5.037   -66.578 1.00 71.70  ? 173 ASN B N   1 
ATOM 3549 C CA  . ASN B 1 165 ? -26.329 6.095   -67.518 1.00 64.90  ? 173 ASN B CA  1 
ATOM 3550 C C   . ASN B 1 165 ? -25.583 7.393   -67.209 1.00 69.84  ? 173 ASN B C   1 
ATOM 3551 O O   . ASN B 1 165 ? -25.054 8.044   -68.117 1.00 72.40  ? 173 ASN B O   1 
ATOM 3552 C CB  . ASN B 1 165 ? -27.846 6.308   -67.507 1.00 67.62  ? 173 ASN B CB  1 
ATOM 3553 C CG  . ASN B 1 165 ? -28.333 7.132   -68.687 1.00 68.45  ? 173 ASN B CG  1 
ATOM 3554 O OD1 . ASN B 1 165 ? -27.807 8.204   -68.977 1.00 72.02  ? 173 ASN B OD1 1 
ATOM 3555 N ND2 . ASN B 1 165 ? -29.350 6.624   -69.378 1.00 67.66  ? 173 ASN B ND2 1 
ATOM 3556 N N   . ILE B 1 166 ? -25.544 7.799   -65.932 1.00 78.15  ? 174 ILE B N   1 
ATOM 3557 C CA  . ILE B 1 166 ? -24.753 8.972   -65.549 1.00 77.58  ? 174 ILE B CA  1 
ATOM 3558 C C   . ILE B 1 166 ? -23.301 8.836   -65.998 1.00 82.44  ? 174 ILE B C   1 
ATOM 3559 O O   . ILE B 1 166 ? -22.724 9.766   -66.573 1.00 86.87  ? 174 ILE B O   1 
ATOM 3560 C CB  . ILE B 1 166 ? -24.838 9.258   -64.034 1.00 77.46  ? 174 ILE B CB  1 
ATOM 3561 C CG1 . ILE B 1 166 ? -26.270 9.483   -63.510 1.00 73.04  ? 174 ILE B CG1 1 
ATOM 3562 C CG2 . ILE B 1 166 ? -23.890 10.370  -63.655 1.00 80.67  ? 174 ILE B CG2 1 
ATOM 3563 C CD1 . ILE B 1 166 ? -27.119 8.278   -63.314 1.00 66.81  ? 174 ILE B CD1 1 
ATOM 3564 N N   . ALA B 1 167 ? -22.684 7.677   -65.736 1.00 84.52  ? 175 ALA B N   1 
ATOM 3565 C CA  . ALA B 1 167 ? -21.277 7.497   -66.095 1.00 86.50  ? 175 ALA B CA  1 
ATOM 3566 C C   . ALA B 1 167 ? -21.046 7.720   -67.585 1.00 86.20  ? 175 ALA B C   1 
ATOM 3567 O O   . ALA B 1 167 ? -20.065 8.360   -67.981 1.00 87.15  ? 175 ALA B O   1 
ATOM 3568 C CB  . ALA B 1 167 ? -20.797 6.105   -65.682 1.00 84.97  ? 175 ALA B CB  1 
ATOM 3569 N N   . HIS B 1 168 ? -21.932 7.183   -68.424 1.00 82.12  ? 176 HIS B N   1 
ATOM 3570 C CA  . HIS B 1 168 ? -21.851 7.408   -69.863 1.00 81.05  ? 176 HIS B CA  1 
ATOM 3571 C C   . HIS B 1 168 ? -21.924 8.893   -70.194 1.00 74.97  ? 176 HIS B C   1 
ATOM 3572 O O   . HIS B 1 168 ? -21.023 9.450   -70.833 1.00 77.64  ? 176 HIS B O   1 
ATOM 3573 C CB  . HIS B 1 168 ? -22.963 6.640   -70.582 1.00 81.60  ? 176 HIS B CB  1 
ATOM 3574 C CG  . HIS B 1 168 ? -23.136 7.034   -72.018 1.00 79.99  ? 176 HIS B CG  1 
ATOM 3575 N ND1 . HIS B 1 168 ? -22.586 6.317   -73.060 1.00 76.37  ? 176 HIS B ND1 1 
ATOM 3576 C CD2 . HIS B 1 168 ? -23.809 8.063   -72.587 1.00 78.29  ? 176 HIS B CD2 1 
ATOM 3577 C CE1 . HIS B 1 168 ? -22.906 6.891   -74.206 1.00 81.25  ? 176 HIS B CE1 1 
ATOM 3578 N NE2 . HIS B 1 168 ? -23.648 7.953   -73.947 1.00 77.85  ? 176 HIS B NE2 1 
ATOM 3579 N N   . GLN B 1 169 ? -23.014 9.546   -69.778 1.00 70.42  ? 177 GLN B N   1 
ATOM 3580 C CA  . GLN B 1 169 ? -23.152 10.988  -69.951 1.00 76.35  ? 177 GLN B CA  1 
ATOM 3581 C C   . GLN B 1 169 ? -21.956 11.763  -69.410 1.00 78.07  ? 177 GLN B C   1 
ATOM 3582 O O   . GLN B 1 169 ? -21.664 12.861  -69.895 1.00 77.36  ? 177 GLN B O   1 
ATOM 3583 C CB  . GLN B 1 169 ? -24.437 11.465  -69.273 1.00 74.73  ? 177 GLN B CB  1 
ATOM 3584 C CG  . GLN B 1 169 ? -25.710 10.910  -69.901 1.00 73.32  ? 177 GLN B CG  1 
ATOM 3585 C CD  . GLN B 1 169 ? -25.933 11.380  -71.326 1.00 76.21  ? 177 GLN B CD  1 
ATOM 3586 O OE1 . GLN B 1 169 ? -25.393 12.402  -71.752 1.00 87.79  ? 177 GLN B OE1 1 
ATOM 3587 N NE2 . GLN B 1 169 ? -26.730 10.627  -72.074 1.00 75.97  ? 177 GLN B NE2 1 
ATOM 3588 N N   . LEU B 1 170 ? -21.252 11.222  -68.412 1.00 80.80  ? 178 LEU B N   1 
ATOM 3589 C CA  . LEU B 1 170 ? -20.101 11.943  -67.880 1.00 83.49  ? 178 LEU B CA  1 
ATOM 3590 C C   . LEU B 1 170 ? -18.842 11.695  -68.702 1.00 83.74  ? 178 LEU B C   1 
ATOM 3591 O O   . LEU B 1 170 ? -17.943 12.543  -68.721 1.00 85.30  ? 178 LEU B O   1 
ATOM 3592 C CB  . LEU B 1 170 ? -19.846 11.531  -66.426 1.00 83.34  ? 178 LEU B CB  1 
ATOM 3593 C CG  . LEU B 1 170 ? -20.722 12.101  -65.309 1.00 83.94  ? 178 LEU B CG  1 
ATOM 3594 C CD1 . LEU B 1 170 ? -19.924 12.123  -64.019 1.00 80.55  ? 178 LEU B CD1 1 
ATOM 3595 C CD2 . LEU B 1 170 ? -21.202 13.501  -65.659 1.00 74.94  ? 178 LEU B CD2 1 
ATOM 3596 N N   . ALA B 1 171 ? -18.757 10.549  -69.384 1.00 86.67  ? 179 ALA B N   1 
ATOM 3597 C CA  . ALA B 1 171 ? -17.715 10.356  -70.388 1.00 90.27  ? 179 ALA B CA  1 
ATOM 3598 C C   . ALA B 1 171 ? -17.968 11.254  -71.590 1.00 88.88  ? 179 ALA B C   1 
ATOM 3599 O O   . ALA B 1 171 ? -17.079 11.987  -72.035 1.00 91.15  ? 179 ALA B O   1 
ATOM 3600 C CB  . ALA B 1 171 ? -17.647 8.888   -70.808 1.00 88.55  ? 179 ALA B CB  1 
ATOM 3601 N N   . VAL B 1 172 ? -19.176 11.171  -72.150 1.00 85.98  ? 180 VAL B N   1 
ATOM 3602 C CA  . VAL B 1 172 ? -19.512 11.891  -73.373 1.00 84.34  ? 180 VAL B CA  1 
ATOM 3603 C C   . VAL B 1 172 ? -19.334 13.389  -73.171 1.00 89.62  ? 180 VAL B C   1 
ATOM 3604 O O   . VAL B 1 172 ? -18.828 14.096  -74.051 1.00 101.73 ? 180 VAL B O   1 
ATOM 3605 C CB  . VAL B 1 172 ? -20.946 11.538  -73.816 1.00 82.38  ? 180 VAL B CB  1 
ATOM 3606 C CG1 . VAL B 1 172 ? -21.497 12.584  -74.782 1.00 82.82  ? 180 VAL B CG1 1 
ATOM 3607 C CG2 . VAL B 1 172 ? -20.994 10.138  -74.422 1.00 80.84  ? 180 VAL B CG2 1 
ATOM 3608 N N   . ARG B 1 173 ? -19.758 13.895  -72.009 1.00 88.91  ? 181 ARG B N   1 
ATOM 3609 C CA  . ARG B 1 173 ? -19.618 15.316  -71.706 1.00 97.82  ? 181 ARG B CA  1 
ATOM 3610 C C   . ARG B 1 173 ? -18.148 15.734  -71.666 1.00 102.81 ? 181 ARG B C   1 
ATOM 3611 O O   . ARG B 1 173 ? -17.728 16.640  -72.394 1.00 106.64 ? 181 ARG B O   1 
ATOM 3612 C CB  . ARG B 1 173 ? -20.316 15.628  -70.375 1.00 96.95  ? 181 ARG B CB  1 
ATOM 3613 C CG  . ARG B 1 173 ? -20.167 17.057  -69.856 1.00 99.42  ? 181 ARG B CG  1 
ATOM 3614 C CD  . ARG B 1 173 ? -20.310 18.076  -70.979 1.00 103.18 ? 181 ARG B CD  1 
ATOM 3615 N NE  . ARG B 1 173 ? -19.716 19.361  -70.637 1.00 108.36 ? 181 ARG B NE  1 
ATOM 3616 C CZ  . ARG B 1 173 ? -18.525 19.759  -71.060 1.00 108.50 ? 181 ARG B CZ  1 
ATOM 3617 N NH1 . ARG B 1 173 ? -17.784 18.997  -71.849 1.00 101.05 ? 181 ARG B NH1 1 
ATOM 3618 N NH2 . ARG B 1 173 ? -18.064 20.945  -70.678 1.00 107.92 ? 181 ARG B NH2 1 
ATOM 3619 N N   . PHE B 1 174 ? -17.342 15.070  -70.833 1.00 98.97  ? 182 PHE B N   1 
ATOM 3620 C CA  . PHE B 1 174 ? -15.902 15.340  -70.787 1.00 98.11  ? 182 PHE B CA  1 
ATOM 3621 C C   . PHE B 1 174 ? -15.188 14.487  -71.832 1.00 102.42 ? 182 PHE B C   1 
ATOM 3622 O O   . PHE B 1 174 ? -14.571 13.460  -71.538 1.00 105.99 ? 182 PHE B O   1 
ATOM 3623 C CB  . PHE B 1 174 ? -15.352 15.105  -69.386 1.00 96.19  ? 182 PHE B CB  1 
ATOM 3624 C CG  . PHE B 1 174 ? -15.896 16.056  -68.357 1.00 96.85  ? 182 PHE B CG  1 
ATOM 3625 C CD1 . PHE B 1 174 ? -16.139 17.380  -68.674 1.00 96.04  ? 182 PHE B CD1 1 
ATOM 3626 C CD2 . PHE B 1 174 ? -16.135 15.635  -67.064 1.00 96.04  ? 182 PHE B CD2 1 
ATOM 3627 C CE1 . PHE B 1 174 ? -16.646 18.256  -67.727 1.00 98.86  ? 182 PHE B CE1 1 
ATOM 3628 C CE2 . PHE B 1 174 ? -16.629 16.513  -66.116 1.00 97.69  ? 182 PHE B CE2 1 
ATOM 3629 C CZ  . PHE B 1 174 ? -16.885 17.821  -66.447 1.00 96.39  ? 182 PHE B CZ  1 
ATOM 3630 N N   . GLY B 1 175 ? -15.277 14.933  -73.082 1.00 106.57 ? 183 GLY B N   1 
ATOM 3631 C CA  . GLY B 1 175 ? -14.616 14.258  -74.184 1.00 104.57 ? 183 GLY B CA  1 
ATOM 3632 C C   . GLY B 1 175 ? -13.112 14.448  -74.173 1.00 116.82 ? 183 GLY B C   1 
ATOM 3633 O O   . GLY B 1 175 ? -12.617 15.524  -73.836 1.00 122.51 ? 183 GLY B O   1 
ATOM 3634 N N   . ILE B 1 179 ? -8.794  21.569  -70.816 1.00 113.95 ? 187 ILE B N   1 
ATOM 3635 C CA  . ILE B 1 179 ? -8.975  20.517  -69.827 1.00 121.39 ? 187 ILE B CA  1 
ATOM 3636 C C   . ILE B 1 179 ? -9.855  21.024  -68.719 1.00 124.88 ? 187 ILE B C   1 
ATOM 3637 O O   . ILE B 1 179 ? -9.427  21.777  -67.839 1.00 121.79 ? 187 ILE B O   1 
ATOM 3638 C CB  . ILE B 1 179 ? -7.634  20.049  -69.303 1.00 118.36 ? 187 ILE B CB  1 
ATOM 3639 C CG1 . ILE B 1 179 ? -6.755  19.731  -70.503 1.00 111.15 ? 187 ILE B CG1 1 
ATOM 3640 C CG2 . ILE B 1 179 ? -7.811  18.844  -68.373 1.00 116.03 ? 187 ILE B CG2 1 
ATOM 3641 C CD1 . ILE B 1 179 ? -5.530  20.558  -70.576 1.00 107.05 ? 187 ILE B CD1 1 
ATOM 3642 N N   . GLU B 1 180 ? -11.081 20.486  -68.652 1.00 122.04 ? 188 GLU B N   1 
ATOM 3643 C CA  . GLU B 1 180 ? -12.025 20.856  -67.562 1.00 109.07 ? 188 GLU B CA  1 
ATOM 3644 C C   . GLU B 1 180 ? -11.554 20.276  -66.221 1.00 104.66 ? 188 GLU B C   1 
ATOM 3645 O O   . GLU B 1 180 ? -10.916 19.206  -66.241 1.00 103.31 ? 188 GLU B O   1 
ATOM 3646 C CB  . GLU B 1 180 ? -13.410 20.295  -67.870 1.00 100.85 ? 188 GLU B CB  1 
ATOM 3647 C CG  . GLU B 1 180 ? -14.069 20.940  -69.085 1.00 106.58 ? 188 GLU B CG  1 
ATOM 3648 C CD  . GLU B 1 180 ? -15.416 20.343  -69.447 1.00 105.23 ? 188 GLU B CD  1 
ATOM 3649 O OE1 . GLU B 1 180 ? -15.782 19.294  -68.880 1.00 97.28  ? 188 GLU B OE1 1 
ATOM 3650 O OE2 . GLU B 1 180 ? -16.105 20.935  -70.301 1.00 109.54 ? 188 GLU B OE2 1 
ATOM 3651 N N   . LEU B 1 181 ? -11.875 20.944  -65.109 1.00 100.40 ? 189 LEU B N   1 
ATOM 3652 C CA  . LEU B 1 181 ? -11.486 20.466  -63.754 1.00 103.07 ? 189 LEU B CA  1 
ATOM 3653 C C   . LEU B 1 181 ? -10.149 19.726  -63.792 1.00 106.67 ? 189 LEU B C   1 
ATOM 3654 O O   . LEU B 1 181 ? -10.093 18.606  -63.264 1.00 106.74 ? 189 LEU B O   1 
ATOM 3655 C CB  . LEU B 1 181 ? -12.580 19.574  -63.174 1.00 100.02 ? 189 LEU B CB  1 
ATOM 3656 C CG  . LEU B 1 181 ? -14.018 19.988  -63.497 1.00 102.87 ? 189 LEU B CG  1 
ATOM 3657 C CD1 . LEU B 1 181 ? -14.970 18.831  -63.261 1.00 105.77 ? 189 LEU B CD1 1 
ATOM 3658 C CD2 . LEU B 1 181 ? -14.434 21.201  -62.682 1.00 100.29 ? 189 LEU B CD2 1 
ATOM 3659 N N   . THR B 1 182 ? -9.113  20.349  -64.344 1.00 104.04 ? 190 THR B N   1 
ATOM 3660 C CA  . THR B 1 182 ? -7.826  19.645  -64.520 1.00 106.54 ? 190 THR B CA  1 
ATOM 3661 C C   . THR B 1 182 ? -7.284  18.914  -63.301 1.00 104.39 ? 190 THR B C   1 
ATOM 3662 O O   . THR B 1 182 ? -6.883  17.748  -63.473 1.00 107.04 ? 190 THR B O   1 
ATOM 3663 C CB  . THR B 1 182 ? -6.795  20.649  -65.034 1.00 109.26 ? 190 THR B CB  1 
ATOM 3664 O OG1 . THR B 1 182 ? -7.473  21.397  -66.038 1.00 104.05 ? 190 THR B OG1 1 
ATOM 3665 C CG2 . THR B 1 182 ? -5.567  19.973  -65.615 1.00 111.14 ? 190 THR B CG2 1 
ATOM 3666 N N   . PRO B 1 183 ? -7.225  19.481  -62.070 1.00 102.25 ? 191 PRO B N   1 
ATOM 3667 C CA  . PRO B 1 183 ? -6.566  18.782  -60.928 1.00 105.51 ? 191 PRO B CA  1 
ATOM 3668 C C   . PRO B 1 183 ? -7.093  17.357  -60.855 1.00 104.04 ? 191 PRO B C   1 
ATOM 3669 O O   . PRO B 1 183 ? -6.383  16.468  -60.338 1.00 101.43 ? 191 PRO B O   1 
ATOM 3670 C CB  . PRO B 1 183 ? -6.951  19.625  -59.724 1.00 102.47 ? 191 PRO B CB  1 
ATOM 3671 C CG  . PRO B 1 183 ? -6.897  21.024  -60.300 1.00 108.71 ? 191 PRO B CG  1 
ATOM 3672 C CD  . PRO B 1 183 ? -7.529  20.907  -61.645 1.00 105.10 ? 191 PRO B CD  1 
ATOM 3673 N N   . VAL B 1 184 ? -8.308  17.138  -61.357 1.00 108.72 ? 192 VAL B N   1 
ATOM 3674 C CA  . VAL B 1 184 ? -8.928  15.782  -61.262 1.00 111.48 ? 192 VAL B CA  1 
ATOM 3675 C C   . VAL B 1 184 ? -9.051  15.198  -62.678 1.00 112.18 ? 192 VAL B C   1 
ATOM 3676 O O   . VAL B 1 184 ? -9.630  15.870  -63.555 1.00 104.65 ? 192 VAL B O   1 
ATOM 3677 C CB  . VAL B 1 184 ? -10.285 15.827  -60.533 1.00 110.00 ? 192 VAL B CB  1 
ATOM 3678 C CG1 . VAL B 1 184 ? -10.987 14.476  -60.534 1.00 105.79 ? 192 VAL B CG1 1 
ATOM 3679 C CG2 . VAL B 1 184 ? -10.171 16.389  -59.120 1.00 107.88 ? 192 VAL B CG2 1 
ATOM 3680 N N   . ARG B 1 185 ? -8.507  14.000  -62.895 1.00 111.52 ? 193 ARG B N   1 
ATOM 3681 C CA  . ARG B 1 185 ? -8.523  13.433  -64.265 1.00 103.18 ? 193 ARG B CA  1 
ATOM 3682 C C   . ARG B 1 185 ? -9.263  12.094  -64.262 1.00 103.32 ? 193 ARG B C   1 
ATOM 3683 O O   . ARG B 1 185 ? -8.744  11.118  -63.683 1.00 104.11 ? 193 ARG B O   1 
ATOM 3684 C CB  . ARG B 1 185 ? -7.100  13.287  -64.818 1.00 100.16 ? 193 ARG B CB  1 
ATOM 3685 C CG  . ARG B 1 185 ? -6.185  12.285  -64.129 1.00 101.96 ? 193 ARG B CG  1 
ATOM 3686 C CD  . ARG B 1 185 ? -4.774  12.291  -64.694 1.00 98.68  ? 193 ARG B CD  1 
ATOM 3687 N NE  . ARG B 1 185 ? -3.925  11.285  -64.046 1.00 99.70  ? 193 ARG B NE  1 
ATOM 3688 C CZ  . ARG B 1 185 ? -3.298  11.467  -62.892 1.00 97.62  ? 193 ARG B CZ  1 
ATOM 3689 N NH1 . ARG B 1 185 ? -2.000  11.241  -62.803 1.00 98.65  ? 193 ARG B NH1 1 
ATOM 3690 N NH2 . ARG B 1 185 ? -3.975  11.872  -61.832 1.00 95.54  ? 193 ARG B NH2 1 
ATOM 3691 N N   . VAL B 1 186 ? -10.451 12.057  -64.861 1.00 99.63  ? 194 VAL B N   1 
ATOM 3692 C CA  . VAL B 1 186 ? -11.121 10.770  -64.982 1.00 102.53 ? 194 VAL B CA  1 
ATOM 3693 C C   . VAL B 1 186 ? -10.269 9.830   -65.821 1.00 103.11 ? 194 VAL B C   1 
ATOM 3694 O O   . VAL B 1 186 ? -9.755  10.205  -66.885 1.00 105.55 ? 194 VAL B O   1 
ATOM 3695 C CB  . VAL B 1 186 ? -12.527 10.942  -65.576 1.00 100.18 ? 194 VAL B CB  1 
ATOM 3696 C CG1 . VAL B 1 186 ? -12.471 11.605  -66.953 1.00 94.34  ? 194 VAL B CG1 1 
ATOM 3697 C CG2 . VAL B 1 186 ? -13.228 9.595   -65.646 1.00 92.27  ? 194 VAL B CG2 1 
ATOM 3698 N N   . ARG B 1 187 ? -10.094 8.605   -65.330 1.00 97.87  ? 195 ARG B N   1 
ATOM 3699 C CA  . ARG B 1 187 ? -9.309  7.600   -66.032 1.00 98.57  ? 195 ARG B CA  1 
ATOM 3700 C C   . ARG B 1 187 ? -10.170 6.511   -66.650 1.00 106.15 ? 195 ARG B C   1 
ATOM 3701 O O   . ARG B 1 187 ? -10.007 6.180   -67.830 1.00 113.11 ? 195 ARG B O   1 
ATOM 3702 C CB  . ARG B 1 187 ? -8.290  6.975   -65.077 1.00 99.99  ? 195 ARG B CB  1 
ATOM 3703 C CG  . ARG B 1 187 ? -7.230  7.961   -64.611 1.00 104.39 ? 195 ARG B CG  1 
ATOM 3704 C CD  . ARG B 1 187 ? -6.193  7.317   -63.731 1.00 111.34 ? 195 ARG B CD  1 
ATOM 3705 N NE  . ARG B 1 187 ? -5.186  8.257   -63.260 1.00 116.54 ? 195 ARG B NE  1 
ATOM 3706 C CZ  . ARG B 1 187 ? -4.121  8.625   -63.957 1.00 118.52 ? 195 ARG B CZ  1 
ATOM 3707 N NH1 . ARG B 1 187 ? -4.029  8.387   -65.254 1.00 113.67 ? 195 ARG B NH1 1 
ATOM 3708 N NH2 . ARG B 1 187 ? -3.155  9.304   -63.350 1.00 117.10 ? 195 ARG B NH2 1 
ATOM 3709 N N   . GLY B 1 188 ? -11.088 5.937   -65.868 1.00 104.30 ? 196 GLY B N   1 
ATOM 3710 C CA  . GLY B 1 188 ? -11.906 4.841   -66.331 1.00 103.61 ? 196 GLY B CA  1 
ATOM 3711 C C   . GLY B 1 188 ? -13.363 5.059   -65.967 1.00 100.39 ? 196 GLY B C   1 
ATOM 3712 O O   . GLY B 1 188 ? -13.706 5.922   -65.156 1.00 97.60  ? 196 GLY B O   1 
ATOM 3713 N N   . TYR B 1 189 ? -14.216 4.254   -66.592 1.00 98.76  ? 197 TYR B N   1 
ATOM 3714 C CA  . TYR B 1 189 ? -15.656 4.331   -66.388 1.00 97.20  ? 197 TYR B CA  1 
ATOM 3715 C C   . TYR B 1 189 ? -16.182 2.913   -66.239 1.00 95.62  ? 197 TYR B C   1 
ATOM 3716 O O   . TYR B 1 189 ? -16.065 2.111   -67.168 1.00 98.19  ? 197 TYR B O   1 
ATOM 3717 C CB  . TYR B 1 189 ? -16.336 5.032   -67.567 1.00 96.28  ? 197 TYR B CB  1 
ATOM 3718 C CG  . TYR B 1 189 ? -16.270 6.541   -67.512 1.00 92.29  ? 197 TYR B CG  1 
ATOM 3719 C CD1 . TYR B 1 189 ? -17.146 7.272   -66.722 1.00 90.68  ? 197 TYR B CD1 1 
ATOM 3720 C CD2 . TYR B 1 189 ? -15.326 7.235   -68.259 1.00 93.19  ? 197 TYR B CD2 1 
ATOM 3721 C CE1 . TYR B 1 189 ? -17.081 8.654   -66.676 1.00 86.61  ? 197 TYR B CE1 1 
ATOM 3722 C CE2 . TYR B 1 189 ? -15.255 8.612   -68.221 1.00 93.44  ? 197 TYR B CE2 1 
ATOM 3723 C CZ  . TYR B 1 189 ? -16.134 9.318   -67.428 1.00 88.43  ? 197 TYR B CZ  1 
ATOM 3724 O OH  . TYR B 1 189 ? -16.060 10.691  -67.389 1.00 88.92  ? 197 TYR B OH  1 
ATOM 3725 N N   . VAL B 1 190 ? -16.750 2.598   -65.081 1.00 88.58  ? 198 VAL B N   1 
ATOM 3726 C CA  . VAL B 1 190 ? -17.343 1.287   -64.842 1.00 81.97  ? 198 VAL B CA  1 
ATOM 3727 C C   . VAL B 1 190 ? -18.850 1.416   -64.993 1.00 79.85  ? 198 VAL B C   1 
ATOM 3728 O O   . VAL B 1 190 ? -19.475 2.284   -64.370 1.00 85.40  ? 198 VAL B O   1 
ATOM 3729 C CB  . VAL B 1 190 ? -16.964 0.741   -63.455 1.00 85.68  ? 198 VAL B CB  1 
ATOM 3730 C CG1 . VAL B 1 190 ? -17.680 -0.573  -63.196 1.00 86.64  ? 198 VAL B CG1 1 
ATOM 3731 C CG2 . VAL B 1 190 ? -15.459 0.553   -63.353 1.00 86.94  ? 198 VAL B CG2 1 
ATOM 3732 N N   . LEU B 1 191 ? -19.434 0.547   -65.814 1.00 79.51  ? 199 LEU B N   1 
ATOM 3733 C CA  . LEU B 1 191 ? -20.829 0.658   -66.236 1.00 84.44  ? 199 LEU B CA  1 
ATOM 3734 C C   . LEU B 1 191 ? -21.523 -0.651  -65.873 1.00 82.71  ? 199 LEU B C   1 
ATOM 3735 O O   . LEU B 1 191 ? -21.384 -1.652  -66.581 1.00 88.60  ? 199 LEU B O   1 
ATOM 3736 C CB  . LEU B 1 191 ? -20.934 0.938   -67.735 1.00 93.68  ? 199 LEU B CB  1 
ATOM 3737 C CG  . LEU B 1 191 ? -20.619 2.316   -68.335 1.00 92.55  ? 199 LEU B CG  1 
ATOM 3738 C CD1 . LEU B 1 191 ? -21.663 3.312   -67.892 1.00 84.07  ? 199 LEU B CD1 1 
ATOM 3739 C CD2 . LEU B 1 191 ? -19.212 2.827   -68.031 1.00 92.55  ? 199 LEU B CD2 1 
ATOM 3740 N N   . MET B 1 192 ? -22.277 -0.640  -64.777 1.00 79.47  ? 200 MET B N   1 
ATOM 3741 C CA  . MET B 1 192 ? -22.788 -1.860  -64.162 1.00 80.14  ? 200 MET B CA  1 
ATOM 3742 C C   . MET B 1 192 ? -24.291 -1.945  -64.390 1.00 79.30  ? 200 MET B C   1 
ATOM 3743 O O   . MET B 1 192 ? -25.063 -1.236  -63.736 1.00 76.99  ? 200 MET B O   1 
ATOM 3744 C CB  . MET B 1 192 ? -22.450 -1.884  -62.676 1.00 82.17  ? 200 MET B CB  1 
ATOM 3745 C CG  . MET B 1 192 ? -20.967 -1.769  -62.404 1.00 81.91  ? 200 MET B CG  1 
ATOM 3746 S SD  . MET B 1 192 ? -20.564 -2.110  -60.691 1.00 98.08  ? 200 MET B SD  1 
ATOM 3747 C CE  . MET B 1 192 ? -20.592 -3.890  -60.752 1.00 88.07  ? 200 MET B CE  1 
ATOM 3748 N N   . GLY B 1 193 ? -24.701 -2.836  -65.293 1.00 75.15  ? 201 GLY B N   1 
ATOM 3749 C CA  . GLY B 1 193 ? -26.074 -2.916  -65.734 1.00 77.02  ? 201 GLY B CA  1 
ATOM 3750 C C   . GLY B 1 193 ? -26.661 -1.559  -66.071 1.00 79.05  ? 201 GLY B C   1 
ATOM 3751 O O   . GLY B 1 193 ? -27.662 -1.133  -65.487 1.00 88.54  ? 201 GLY B O   1 
ATOM 3752 N N   . PRO B 1 194 ? -26.045 -0.850  -67.019 1.00 71.37  ? 202 PRO B N   1 
ATOM 3753 C CA  . PRO B 1 194 ? -26.451 0.536   -67.281 1.00 71.04  ? 202 PRO B CA  1 
ATOM 3754 C C   . PRO B 1 194 ? -27.880 0.616   -67.795 1.00 64.34  ? 202 PRO B C   1 
ATOM 3755 O O   . PRO B 1 194 ? -28.309 -0.182  -68.631 1.00 66.15  ? 202 PRO B O   1 
ATOM 3756 C CB  . PRO B 1 194 ? -25.448 1.007   -68.340 1.00 80.04  ? 202 PRO B CB  1 
ATOM 3757 C CG  . PRO B 1 194 ? -24.317 0.033   -68.272 1.00 80.24  ? 202 PRO B CG  1 
ATOM 3758 C CD  . PRO B 1 194 ? -24.945 -1.268  -67.903 1.00 75.06  ? 202 PRO B CD  1 
ATOM 3759 N N   . PHE B 1 195 ? -28.616 1.598   -67.282 1.00 66.02  ? 203 PHE B N   1 
ATOM 3760 C CA  . PHE B 1 195 ? -30.028 1.788   -67.607 1.00 73.22  ? 203 PHE B CA  1 
ATOM 3761 C C   . PHE B 1 195 ? -30.130 2.587   -68.902 1.00 72.39  ? 203 PHE B C   1 
ATOM 3762 O O   . PHE B 1 195 ? -30.151 3.819   -68.899 1.00 64.62  ? 203 PHE B O   1 
ATOM 3763 C CB  . PHE B 1 195 ? -30.737 2.479   -66.449 1.00 67.46  ? 203 PHE B CB  1 
ATOM 3764 C CG  . PHE B 1 195 ? -32.209 2.656   -66.650 1.00 70.33  ? 203 PHE B CG  1 
ATOM 3765 C CD1 . PHE B 1 195 ? -32.995 1.599   -67.075 1.00 74.63  ? 203 PHE B CD1 1 
ATOM 3766 C CD2 . PHE B 1 195 ? -32.815 3.872   -66.381 1.00 71.97  ? 203 PHE B CD2 1 
ATOM 3767 C CE1 . PHE B 1 195 ? -34.354 1.757   -67.250 1.00 70.63  ? 203 PHE B CE1 1 
ATOM 3768 C CE2 . PHE B 1 195 ? -34.173 4.035   -66.551 1.00 74.37  ? 203 PHE B CE2 1 
ATOM 3769 C CZ  . PHE B 1 195 ? -34.943 2.974   -66.984 1.00 72.94  ? 203 PHE B CZ  1 
ATOM 3770 N N   . PHE B 1 196 ? -30.189 1.878   -70.026 1.00 73.97  ? 204 PHE B N   1 
ATOM 3771 C CA  . PHE B 1 196 ? -30.319 2.490   -71.339 1.00 66.43  ? 204 PHE B CA  1 
ATOM 3772 C C   . PHE B 1 196 ? -31.709 2.219   -71.904 1.00 69.87  ? 204 PHE B C   1 
ATOM 3773 O O   . PHE B 1 196 ? -32.409 1.300   -71.471 1.00 68.88  ? 204 PHE B O   1 
ATOM 3774 C CB  . PHE B 1 196 ? -29.243 1.967   -72.297 1.00 57.13  ? 204 PHE B CB  1 
ATOM 3775 C CG  . PHE B 1 196 ? -27.877 2.545   -72.046 1.00 58.19  ? 204 PHE B CG  1 
ATOM 3776 C CD1 . PHE B 1 196 ? -27.671 3.914   -72.087 1.00 59.76  ? 204 PHE B CD1 1 
ATOM 3777 C CD2 . PHE B 1 196 ? -26.799 1.719   -71.775 1.00 61.97  ? 204 PHE B CD2 1 
ATOM 3778 C CE1 . PHE B 1 196 ? -26.417 4.450   -71.857 1.00 63.55  ? 204 PHE B CE1 1 
ATOM 3779 C CE2 . PHE B 1 196 ? -25.542 2.249   -71.547 1.00 69.54  ? 204 PHE B CE2 1 
ATOM 3780 C CZ  . PHE B 1 196 ? -25.351 3.615   -71.586 1.00 69.43  ? 204 PHE B CZ  1 
ATOM 3781 N N   . GLY B 1 197 ? -32.106 3.033   -72.890 1.00 72.25  ? 205 GLY B N   1 
ATOM 3782 C CA  . GLY B 1 197 ? -33.474 3.045   -73.360 1.00 78.27  ? 205 GLY B CA  1 
ATOM 3783 C C   . GLY B 1 197 ? -33.561 2.982   -74.875 1.00 71.91  ? 205 GLY B C   1 
ATOM 3784 O O   . GLY B 1 197 ? -32.554 3.030   -75.585 1.00 75.48  ? 205 GLY B O   1 
ATOM 3785 N N   . GLY B 1 198 ? -34.799 2.860   -75.355 1.00 68.03  ? 206 GLY B N   1 
ATOM 3786 C CA  . GLY B 1 198 ? -35.092 2.787   -76.775 1.00 77.38  ? 206 GLY B CA  1 
ATOM 3787 C C   . GLY B 1 198 ? -36.461 2.190   -77.038 1.00 83.34  ? 206 GLY B C   1 
ATOM 3788 O O   . GLY B 1 198 ? -36.918 1.333   -76.276 1.00 80.48  ? 206 GLY B O   1 
ATOM 3789 N N   . GLU B 1 199 ? -37.133 2.636   -78.105 1.00 87.59  ? 207 GLU B N   1 
ATOM 3790 C CA  . GLU B 1 199 ? -38.497 2.177   -78.363 1.00 92.80  ? 207 GLU B CA  1 
ATOM 3791 C C   . GLU B 1 199 ? -38.526 0.722   -78.801 1.00 92.14  ? 207 GLU B C   1 
ATOM 3792 O O   . GLU B 1 199 ? -39.324 -0.074  -78.293 1.00 92.01  ? 207 GLU B O   1 
ATOM 3793 C CB  . GLU B 1 199 ? -39.160 3.042   -79.431 1.00 90.92  ? 207 GLU B CB  1 
ATOM 3794 C CG  . GLU B 1 199 ? -39.717 4.326   -78.916 1.00 86.35  ? 207 GLU B CG  1 
ATOM 3795 C CD  . GLU B 1 199 ? -41.014 4.141   -78.156 1.00 92.31  ? 207 GLU B CD  1 
ATOM 3796 O OE1 . GLU B 1 199 ? -41.890 3.396   -78.644 1.00 93.11  ? 207 GLU B OE1 1 
ATOM 3797 O OE2 . GLU B 1 199 ? -41.156 4.742   -77.070 1.00 92.53  ? 207 GLU B OE2 1 
ATOM 3798 N N   . GLU B 1 200 ? -37.512 0.342   -79.569 1.00 93.08  ? 208 GLU B N   1 
ATOM 3799 C CA  . GLU B 1 200 ? -37.400 -1.068  -79.999 1.00 96.47  ? 208 GLU B CA  1 
ATOM 3800 C C   . GLU B 1 200 ? -36.823 -1.920  -78.867 1.00 88.13  ? 208 GLU B C   1 
ATOM 3801 O O   . GLU B 1 200 ? -35.680 -1.648  -78.446 1.00 78.46  ? 208 GLU B O   1 
ATOM 3802 C CB  . GLU B 1 200 ? -36.450 -1.147  -81.191 1.00 104.52 ? 208 GLU B CB  1 
ATOM 3803 C CG  . GLU B 1 200 ? -36.897 -0.298  -82.377 1.00 103.99 ? 208 GLU B CG  1 
ATOM 3804 C CD  . GLU B 1 200 ? -36.673 -0.969  -83.720 1.00 105.54 ? 208 GLU B CD  1 
ATOM 3805 O OE1 . GLU B 1 200 ? -35.743 -1.795  -83.817 1.00 109.06 ? 208 GLU B OE1 1 
ATOM 3806 O OE2 . GLU B 1 200 ? -37.427 -0.667  -84.666 1.00 107.39 ? 208 GLU B OE2 1 
ATOM 3807 N N   . ARG B 1 201 ? -37.578 -2.914  -78.399 1.00 91.89  ? 209 ARG B N   1 
ATOM 3808 C CA  . ARG B 1 201 ? -37.029 -3.860  -77.395 1.00 90.70  ? 209 ARG B CA  1 
ATOM 3809 C C   . ARG B 1 201 ? -36.041 -4.748  -78.153 1.00 87.98  ? 209 ARG B C   1 
ATOM 3810 O O   . ARG B 1 201 ? -36.030 -4.671  -79.398 1.00 101.53 ? 209 ARG B O   1 
ATOM 3811 C CB  . ARG B 1 201 ? -38.169 -4.656  -76.761 1.00 90.54  ? 209 ARG B CB  1 
ATOM 3812 C CG  . ARG B 1 201 ? -38.925 -3.920  -75.667 1.00 84.37  ? 209 ARG B CG  1 
ATOM 3813 C CD  . ARG B 1 201 ? -40.258 -3.391  -76.165 1.00 86.37  ? 209 ARG B CD  1 
ATOM 3814 N NE  . ARG B 1 201 ? -40.247 -1.931  -76.299 1.00 90.17  ? 209 ARG B NE  1 
ATOM 3815 C CZ  . ARG B 1 201 ? -39.893 -1.098  -75.332 1.00 92.44  ? 209 ARG B CZ  1 
ATOM 3816 N NH1 . ARG B 1 201 ? -40.743 -0.814  -74.363 1.00 106.35 ? 209 ARG B NH1 1 
ATOM 3817 N NH2 . ARG B 1 201 ? -38.691 -0.550  -75.342 1.00 85.38  ? 209 ARG B NH2 1 
ATOM 3818 N N   . THR B 1 202 ? -35.196 -5.495  -77.474 1.00 75.96  ? 210 THR B N   1 
ATOM 3819 C CA  . THR B 1 202 ? -34.315 -6.286  -78.343 1.00 90.31  ? 210 THR B CA  1 
ATOM 3820 C C   . THR B 1 202 ? -34.576 -7.750  -78.092 1.00 86.51  ? 210 THR B C   1 
ATOM 3821 O O   . THR B 1 202 ? -35.466 -8.292  -78.778 1.00 84.96  ? 210 THR B O   1 
ATOM 3822 C CB  . THR B 1 202 ? -32.871 -5.798  -78.248 1.00 92.96  ? 210 THR B CB  1 
ATOM 3823 O OG1 . THR B 1 202 ? -32.492 -5.926  -76.880 1.00 97.94  ? 210 THR B OG1 1 
ATOM 3824 C CG2 . THR B 1 202 ? -32.728 -4.412  -78.845 1.00 75.88  ? 210 THR B CG2 1 
ATOM 3825 N N   . ASN B 1 203 ? -33.879 -8.394  -77.172 1.00 95.10  ? 211 ASN B N   1 
ATOM 3826 C CA  . ASN B 1 203 ? -34.210 -9.828  -76.992 1.00 92.55  ? 211 ASN B CA  1 
ATOM 3827 C C   . ASN B 1 203 ? -34.316 -10.056 -75.493 1.00 92.62  ? 211 ASN B C   1 
ATOM 3828 O O   . ASN B 1 203 ? -35.193 -10.820 -75.052 1.00 92.98  ? 211 ASN B O   1 
ATOM 3829 C CB  . ASN B 1 203 ? -33.181 -10.732 -77.657 1.00 92.65  ? 211 ASN B CB  1 
ATOM 3830 C CG  . ASN B 1 203 ? -32.858 -10.299 -79.067 1.00 88.52  ? 211 ASN B CG  1 
ATOM 3831 O OD1 . ASN B 1 203 ? -33.660 -10.513 -79.982 1.00 77.28  ? 211 ASN B OD1 1 
ATOM 3832 N ND2 . ASN B 1 203 ? -31.700 -9.684  -79.261 1.00 83.29  ? 211 ASN B ND2 1 
ATOM 3833 N N   . SER B 1 204 ? -33.439 -9.389  -74.756 1.00 93.16  ? 212 SER B N   1 
ATOM 3834 C CA  . SER B 1 204 ? -33.463 -9.526  -73.288 1.00 88.99  ? 212 SER B CA  1 
ATOM 3835 C C   . SER B 1 204 ? -34.748 -8.878  -72.772 1.00 90.97  ? 212 SER B C   1 
ATOM 3836 O O   . SER B 1 204 ? -35.397 -9.491  -71.902 1.00 94.98  ? 212 SER B O   1 
ATOM 3837 C CB  . SER B 1 204 ? -32.249 -8.899  -72.703 1.00 83.34  ? 212 SER B CB  1 
ATOM 3838 O OG  . SER B 1 204 ? -32.076 -7.592  -73.224 1.00 81.87  ? 212 SER B OG  1 
ATOM 3839 N N   . GLU B 1 205 ? -35.122 -7.709  -73.302 1.00 88.99  ? 213 GLU B N   1 
ATOM 3840 C CA  . GLU B 1 205 ? -36.307 -7.041  -72.716 1.00 89.26  ? 213 GLU B CA  1 
ATOM 3841 C C   . GLU B 1 205 ? -37.539 -7.927  -72.922 1.00 90.85  ? 213 GLU B C   1 
ATOM 3842 O O   . GLU B 1 205 ? -38.318 -8.097  -71.965 1.00 92.42  ? 213 GLU B O   1 
ATOM 3843 C CB  . GLU B 1 205 ? -36.494 -5.701  -73.416 1.00 87.15  ? 213 GLU B CB  1 
ATOM 3844 C CG  . GLU B 1 205 ? -35.651 -4.586  -72.811 1.00 80.95  ? 213 GLU B CG  1 
ATOM 3845 C CD  . GLU B 1 205 ? -34.518 -4.182  -73.728 1.00 75.42  ? 213 GLU B CD  1 
ATOM 3846 O OE1 . GLU B 1 205 ? -33.537 -4.944  -73.801 1.00 73.52  ? 213 GLU B OE1 1 
ATOM 3847 O OE2 . GLU B 1 205 ? -34.628 -3.120  -74.373 1.00 73.30  ? 213 GLU B OE2 1 
ATOM 3848 N N   . ASN B 1 206 ? -37.703 -8.473  -74.124 1.00 89.50  ? 214 ASN B N   1 
ATOM 3849 C CA  . ASN B 1 206 ? -38.853 -9.313  -74.398 1.00 92.14  ? 214 ASN B CA  1 
ATOM 3850 C C   . ASN B 1 206 ? -38.662 -10.639 -73.678 1.00 99.23  ? 214 ASN B C   1 
ATOM 3851 O O   . ASN B 1 206 ? -37.538 -11.118 -73.514 1.00 100.20 ? 214 ASN B O   1 
ATOM 3852 C CB  . ASN B 1 206 ? -39.003 -9.540  -75.902 1.00 94.59  ? 214 ASN B CB  1 
ATOM 3853 C CG  . ASN B 1 206 ? -38.846 -8.258  -76.701 1.00 95.68  ? 214 ASN B CG  1 
ATOM 3854 O OD1 . ASN B 1 206 ? -37.733 -7.773  -76.901 1.00 93.15  ? 214 ASN B OD1 1 
ATOM 3855 N ND2 . ASN B 1 206 ? -39.962 -7.705  -77.163 1.00 92.05  ? 214 ASN B ND2 1 
ATOM 3856 N N   . GLY B 1 207 ? -39.758 -11.225 -73.217 1.00 98.52  ? 215 GLY B N   1 
ATOM 3857 C CA  . GLY B 1 207 ? -39.630 -12.489 -72.541 1.00 97.98  ? 215 GLY B CA  1 
ATOM 3858 C C   . GLY B 1 207 ? -39.586 -12.376 -71.032 1.00 100.17 ? 215 GLY B C   1 
ATOM 3859 O O   . GLY B 1 207 ? -40.411 -11.706 -70.403 1.00 97.21  ? 215 GLY B O   1 
ATOM 3860 N N   . PRO B 1 208 ? -38.603 -13.042 -70.422 1.00 103.57 ? 216 PRO B N   1 
ATOM 3861 C CA  . PRO B 1 208 ? -38.645 -13.282 -68.974 1.00 96.63  ? 216 PRO B CA  1 
ATOM 3862 C C   . PRO B 1 208 ? -38.357 -12.063 -68.112 1.00 93.01  ? 216 PRO B C   1 
ATOM 3863 O O   . PRO B 1 208 ? -37.251 -11.514 -68.125 1.00 91.59  ? 216 PRO B O   1 
ATOM 3864 C CB  . PRO B 1 208 ? -37.562 -14.349 -68.780 1.00 92.56  ? 216 PRO B CB  1 
ATOM 3865 C CG  . PRO B 1 208 ? -36.559 -14.050 -69.864 1.00 94.71  ? 216 PRO B CG  1 
ATOM 3866 C CD  . PRO B 1 208 ? -37.331 -13.475 -71.029 1.00 101.54 ? 216 PRO B CD  1 
ATOM 3867 N N   . SER B 1 209 ? -39.373 -11.623 -67.376 1.00 90.83  ? 217 SER B N   1 
ATOM 3868 C CA  . SER B 1 209 ? -39.181 -10.600 -66.360 1.00 86.55  ? 217 SER B CA  1 
ATOM 3869 C C   . SER B 1 209 ? -38.308 -11.139 -65.234 1.00 88.89  ? 217 SER B C   1 
ATOM 3870 O O   . SER B 1 209 ? -38.426 -12.303 -64.841 1.00 91.59  ? 217 SER B O   1 
ATOM 3871 C CB  . SER B 1 209 ? -40.530 -10.145 -65.804 1.00 77.11  ? 217 SER B CB  1 
ATOM 3872 O OG  . SER B 1 209 ? -41.330 -9.554  -66.813 1.00 82.05  ? 217 SER B OG  1 
ATOM 3873 N N   . GLU B 1 210 ? -37.424 -10.293 -64.715 1.00 88.36  ? 218 GLU B N   1 
ATOM 3874 C CA  . GLU B 1 210 ? -36.562 -10.722 -63.628 1.00 86.43  ? 218 GLU B CA  1 
ATOM 3875 C C   . GLU B 1 210 ? -37.333 -10.709 -62.313 1.00 89.89  ? 218 GLU B C   1 
ATOM 3876 O O   . GLU B 1 210 ? -38.464 -10.223 -62.229 1.00 92.03  ? 218 GLU B O   1 
ATOM 3877 C CB  . GLU B 1 210 ? -35.352 -9.799  -63.483 1.00 82.35  ? 218 GLU B CB  1 
ATOM 3878 C CG  . GLU B 1 210 ? -34.241 -9.961  -64.492 1.00 85.43  ? 218 GLU B CG  1 
ATOM 3879 C CD  . GLU B 1 210 ? -33.193 -8.870  -64.340 1.00 88.98  ? 218 GLU B CD  1 
ATOM 3880 O OE1 . GLU B 1 210 ? -32.582 -8.782  -63.256 1.00 83.90  ? 218 GLU B OE1 1 
ATOM 3881 O OE2 . GLU B 1 210 ? -32.982 -8.095  -65.294 1.00 94.71  ? 218 GLU B OE2 1 
ATOM 3882 N N   . ALA B 1 211 ? -36.717 -11.269 -61.277 1.00 89.14  ? 219 ALA B N   1 
ATOM 3883 C CA  . ALA B 1 211 ? -37.117 -10.893 -59.932 1.00 93.00  ? 219 ALA B CA  1 
ATOM 3884 C C   . ALA B 1 211 ? -36.889 -9.395  -59.814 1.00 88.10  ? 219 ALA B C   1 
ATOM 3885 O O   . ALA B 1 211 ? -35.785 -8.919  -60.094 1.00 81.86  ? 219 ALA B O   1 
ATOM 3886 C CB  . ALA B 1 211 ? -36.317 -11.662 -58.881 1.00 90.76  ? 219 ALA B CB  1 
ATOM 3887 N N   . LEU B 1 212 ? -37.946 -8.661  -59.451 1.00 87.98  ? 220 LEU B N   1 
ATOM 3888 C CA  . LEU B 1 212 ? -37.965 -7.199  -59.367 1.00 84.70  ? 220 LEU B CA  1 
ATOM 3889 C C   . LEU B 1 212 ? -37.969 -6.315  -60.612 1.00 83.90  ? 220 LEU B C   1 
ATOM 3890 O O   . LEU B 1 212 ? -38.280 -5.123  -60.522 1.00 87.07  ? 220 LEU B O   1 
ATOM 3891 C CB  . LEU B 1 212 ? -36.672 -6.633  -58.764 1.00 84.84  ? 220 LEU B CB  1 
ATOM 3892 C CG  . LEU B 1 212 ? -36.684 -5.240  -58.133 1.00 80.69  ? 220 LEU B CG  1 
ATOM 3893 C CD1 . LEU B 1 212 ? -38.038 -4.915  -57.529 1.00 84.80  ? 220 LEU B CD1 1 
ATOM 3894 C CD2 . LEU B 1 212 ? -35.577 -5.123  -57.094 1.00 85.45  ? 220 LEU B CD2 1 
ATOM 3895 N N   . LEU B 1 213 ? -37.632 -6.873  -61.774 1.00 83.33  ? 221 LEU B N   1 
ATOM 3896 C CA  . LEU B 1 213 ? -37.361 -6.061  -62.957 1.00 78.04  ? 221 LEU B CA  1 
ATOM 3897 C C   . LEU B 1 213 ? -38.308 -6.683  -63.977 1.00 73.97  ? 221 LEU B C   1 
ATOM 3898 O O   . LEU B 1 213 ? -38.215 -7.877  -64.281 1.00 78.71  ? 221 LEU B O   1 
ATOM 3899 C CB  . LEU B 1 213 ? -35.965 -5.948  -63.573 1.00 73.38  ? 221 LEU B CB  1 
ATOM 3900 C CG  . LEU B 1 213 ? -34.781 -5.378  -62.790 1.00 77.42  ? 221 LEU B CG  1 
ATOM 3901 C CD1 . LEU B 1 213 ? -34.212 -6.339  -61.741 1.00 79.18  ? 221 LEU B CD1 1 
ATOM 3902 C CD2 . LEU B 1 213 ? -33.731 -4.925  -63.783 1.00 77.28  ? 221 LEU B CD2 1 
ATOM 3903 N N   . SER B 1 214 ? -39.209 -5.859  -64.507 1.00 65.71  ? 222 SER B N   1 
ATOM 3904 C CA  . SER B 1 214 ? -40.099 -6.231  -65.595 1.00 70.25  ? 222 SER B CA  1 
ATOM 3905 C C   . SER B 1 214 ? -40.066 -5.143  -66.659 1.00 70.03  ? 222 SER B C   1 
ATOM 3906 O O   . SER B 1 214 ? -39.818 -3.972  -66.358 1.00 66.39  ? 222 SER B O   1 
ATOM 3907 C CB  . SER B 1 214 ? -41.533 -6.446  -65.100 1.00 74.43  ? 222 SER B CB  1 
ATOM 3908 O OG  . SER B 1 214 ? -41.588 -7.496  -64.149 1.00 82.22  ? 222 SER B OG  1 
ATOM 3909 N N   . LEU B 1 215 ? -40.322 -5.543  -67.908 1.00 76.62  ? 223 LEU B N   1 
ATOM 3910 C CA  . LEU B 1 215 ? -40.289 -4.605  -69.029 1.00 76.21  ? 223 LEU B CA  1 
ATOM 3911 C C   . LEU B 1 215 ? -41.137 -3.373  -68.746 1.00 72.08  ? 223 LEU B C   1 
ATOM 3912 O O   . LEU B 1 215 ? -40.691 -2.237  -68.949 1.00 70.81  ? 223 LEU B O   1 
ATOM 3913 C CB  . LEU B 1 215 ? -40.750 -5.312  -70.310 1.00 77.87  ? 223 LEU B CB  1 
ATOM 3914 C CG  . LEU B 1 215 ? -40.589 -4.673  -71.699 1.00 78.90  ? 223 LEU B CG  1 
ATOM 3915 C CD1 . LEU B 1 215 ? -41.494 -3.473  -71.938 1.00 68.94  ? 223 LEU B CD1 1 
ATOM 3916 C CD2 . LEU B 1 215 ? -39.160 -4.220  -71.844 1.00 71.03  ? 223 LEU B CD2 1 
ATOM 3917 N N   . ASP B 1 216 ? -42.375 -3.579  -68.297 1.00 71.39  ? 224 ASP B N   1 
ATOM 3918 C CA  . ASP B 1 216 ? -43.235 -2.443  -67.993 1.00 67.51  ? 224 ASP B CA  1 
ATOM 3919 C C   . ASP B 1 216 ? -42.619 -1.556  -66.918 1.00 67.25  ? 224 ASP B C   1 
ATOM 3920 O O   . ASP B 1 216 ? -42.760 -0.330  -66.972 1.00 69.54  ? 224 ASP B O   1 
ATOM 3921 C CB  . ASP B 1 216 ? -44.617 -2.937  -67.563 1.00 66.18  ? 224 ASP B CB  1 
ATOM 3922 C CG  . ASP B 1 216 ? -45.615 -1.809  -67.391 1.00 70.91  ? 224 ASP B CG  1 
ATOM 3923 O OD1 . ASP B 1 216 ? -45.345 -0.692  -67.876 1.00 66.12  ? 224 ASP B OD1 1 
ATOM 3924 O OD2 . ASP B 1 216 ? -46.675 -2.045  -66.775 1.00 82.08  ? 224 ASP B OD2 1 
ATOM 3925 N N   . LEU B 1 217 ? -41.906 -2.149  -65.956 1.00 70.19  ? 225 LEU B N   1 
ATOM 3926 C CA  . LEU B 1 217 ? -41.241 -1.357  -64.923 1.00 73.27  ? 225 LEU B CA  1 
ATOM 3927 C C   . LEU B 1 217 ? -40.121 -0.502  -65.509 1.00 71.30  ? 225 LEU B C   1 
ATOM 3928 O O   . LEU B 1 217 ? -40.007 0.688   -65.190 1.00 69.56  ? 225 LEU B O   1 
ATOM 3929 C CB  . LEU B 1 217 ? -40.701 -2.269  -63.822 1.00 76.43  ? 225 LEU B CB  1 
ATOM 3930 C CG  . LEU B 1 217 ? -39.804 -1.569  -62.799 1.00 68.51  ? 225 LEU B CG  1 
ATOM 3931 C CD1 . LEU B 1 217 ? -40.639 -0.745  -61.830 1.00 71.93  ? 225 LEU B CD1 1 
ATOM 3932 C CD2 . LEU B 1 217 ? -38.946 -2.578  -62.056 1.00 71.08  ? 225 LEU B CD2 1 
ATOM 3933 N N   . LEU B 1 218 ? -39.269 -1.096  -66.352 1.00 66.55  ? 226 LEU B N   1 
ATOM 3934 C CA  . LEU B 1 218 ? -38.239 -0.305  -67.019 1.00 59.23  ? 226 LEU B CA  1 
ATOM 3935 C C   . LEU B 1 218 ? -38.857 0.820   -67.836 1.00 62.31  ? 226 LEU B C   1 
ATOM 3936 O O   . LEU B 1 218 ? -38.331 1.939   -67.862 1.00 63.57  ? 226 LEU B O   1 
ATOM 3937 C CB  . LEU B 1 218 ? -37.356 -1.186  -67.907 1.00 62.66  ? 226 LEU B CB  1 
ATOM 3938 C CG  . LEU B 1 218 ? -36.251 -2.037  -67.268 1.00 62.45  ? 226 LEU B CG  1 
ATOM 3939 C CD1 . LEU B 1 218 ? -35.156 -1.153  -66.679 1.00 62.13  ? 226 LEU B CD1 1 
ATOM 3940 C CD2 . LEU B 1 218 ? -36.779 -3.013  -66.230 1.00 70.19  ? 226 LEU B CD2 1 
ATOM 3941 N N   . ASP B 1 219 ? -39.969 0.541   -68.520 1.00 67.60  ? 227 ASP B N   1 
ATOM 3942 C CA  . ASP B 1 219 ? -40.689 1.608   -69.205 1.00 69.71  ? 227 ASP B CA  1 
ATOM 3943 C C   . ASP B 1 219 ? -41.122 2.689   -68.222 1.00 73.18  ? 227 ASP B C   1 
ATOM 3944 O O   . ASP B 1 219 ? -40.851 3.875   -68.436 1.00 74.74  ? 227 ASP B O   1 
ATOM 3945 C CB  . ASP B 1 219 ? -41.895 1.040   -69.953 1.00 74.67  ? 227 ASP B CB  1 
ATOM 3946 C CG  . ASP B 1 219 ? -41.501 0.060   -71.038 1.00 77.98  ? 227 ASP B CG  1 
ATOM 3947 O OD1 . ASP B 1 219 ? -40.291 -0.208  -71.188 1.00 79.71  ? 227 ASP B OD1 1 
ATOM 3948 O OD2 . ASP B 1 219 ? -42.402 -0.435  -71.747 1.00 79.86  ? 227 ASP B OD2 1 
ATOM 3949 N N   . LYS B 1 220 ? -41.746 2.285   -67.107 1.00 72.77  ? 228 LYS B N   1 
ATOM 3950 C CA  . LYS B 1 220 ? -42.171 3.229   -66.074 1.00 71.90  ? 228 LYS B CA  1 
ATOM 3951 C C   . LYS B 1 220 ? -41.042 4.174   -65.688 1.00 64.96  ? 228 LYS B C   1 
ATOM 3952 O O   . LYS B 1 220 ? -41.186 5.399   -65.771 1.00 65.79  ? 228 LYS B O   1 
ATOM 3953 C CB  . LYS B 1 220 ? -42.681 2.485   -64.837 1.00 68.66  ? 228 LYS B CB  1 
ATOM 3954 C CG  . LYS B 1 220 ? -43.973 1.721   -65.039 1.00 71.95  ? 228 LYS B CG  1 
ATOM 3955 C CD  . LYS B 1 220 ? -44.564 1.284   -63.709 1.00 74.93  ? 228 LYS B CD  1 
ATOM 3956 C CE  . LYS B 1 220 ? -46.003 0.824   -63.873 1.00 73.41  ? 228 LYS B CE  1 
ATOM 3957 N NZ  . LYS B 1 220 ? -46.622 0.447   -62.571 1.00 66.86  ? 228 LYS B NZ  1 
ATOM 3958 N N   . PHE B 1 221 ? -39.925 3.610   -65.220 1.00 57.75  ? 229 PHE B N   1 
ATOM 3959 C CA  . PHE B 1 221 ? -38.725 4.390   -64.937 1.00 60.09  ? 229 PHE B CA  1 
ATOM 3960 C C   . PHE B 1 221 ? -38.495 5.466   -65.990 1.00 64.20  ? 229 PHE B C   1 
ATOM 3961 O O   . PHE B 1 221 ? -38.290 6.639   -65.663 1.00 70.50  ? 229 PHE B O   1 
ATOM 3962 C CB  . PHE B 1 221 ? -37.510 3.464   -64.860 1.00 62.75  ? 229 PHE B CB  1 
ATOM 3963 C CG  . PHE B 1 221 ? -37.406 2.687   -63.579 1.00 63.21  ? 229 PHE B CG  1 
ATOM 3964 C CD1 . PHE B 1 221 ? -38.301 2.896   -62.543 1.00 65.22  ? 229 PHE B CD1 1 
ATOM 3965 C CD2 . PHE B 1 221 ? -36.413 1.734   -63.418 1.00 60.44  ? 229 PHE B CD2 1 
ATOM 3966 C CE1 . PHE B 1 221 ? -38.198 2.177   -61.367 1.00 61.37  ? 229 PHE B CE1 1 
ATOM 3967 C CE2 . PHE B 1 221 ? -36.307 1.012   -62.248 1.00 62.22  ? 229 PHE B CE2 1 
ATOM 3968 C CZ  . PHE B 1 221 ? -37.200 1.232   -61.221 1.00 59.17  ? 229 PHE B CZ  1 
ATOM 3969 N N   . TRP B 1 222 ? -38.527 5.077   -67.268 1.00 67.85  ? 230 TRP B N   1 
ATOM 3970 C CA  . TRP B 1 222 ? -38.327 6.042   -68.344 1.00 69.44  ? 230 TRP B CA  1 
ATOM 3971 C C   . TRP B 1 222 ? -39.432 7.096   -68.373 1.00 67.30  ? 230 TRP B C   1 
ATOM 3972 O O   . TRP B 1 222 ? -39.149 8.297   -68.448 1.00 70.70  ? 230 TRP B O   1 
ATOM 3973 C CB  . TRP B 1 222 ? -38.218 5.329   -69.694 1.00 60.48  ? 230 TRP B CB  1 
ATOM 3974 C CG  . TRP B 1 222 ? -36.942 4.541   -69.877 1.00 64.32  ? 230 TRP B CG  1 
ATOM 3975 C CD1 . TRP B 1 222 ? -36.834 3.217   -70.191 1.00 72.61  ? 230 TRP B CD1 1 
ATOM 3976 C CD2 . TRP B 1 222 ? -35.599 5.025   -69.721 1.00 60.21  ? 230 TRP B CD2 1 
ATOM 3977 N NE1 . TRP B 1 222 ? -35.510 2.853   -70.263 1.00 69.18  ? 230 TRP B NE1 1 
ATOM 3978 C CE2 . TRP B 1 222 ? -34.733 3.946   -69.979 1.00 63.50  ? 230 TRP B CE2 1 
ATOM 3979 C CE3 . TRP B 1 222 ? -35.047 6.269   -69.397 1.00 62.08  ? 230 TRP B CE3 1 
ATOM 3980 C CZ2 . TRP B 1 222 ? -33.347 4.070   -69.912 1.00 62.88  ? 230 TRP B CZ2 1 
ATOM 3981 C CZ3 . TRP B 1 222 ? -33.670 6.390   -69.337 1.00 65.47  ? 230 TRP B CZ3 1 
ATOM 3982 C CH2 . TRP B 1 222 ? -32.837 5.298   -69.596 1.00 63.44  ? 230 TRP B CH2 1 
ATOM 3983 N N   . ARG B 1 223 ? -40.700 6.668   -68.325 1.00 64.51  ? 231 ARG B N   1 
ATOM 3984 C CA  . ARG B 1 223 ? -41.806 7.627   -68.360 1.00 66.22  ? 231 ARG B CA  1 
ATOM 3985 C C   . ARG B 1 223 ? -41.648 8.696   -67.286 1.00 69.98  ? 231 ARG B C   1 
ATOM 3986 O O   . ARG B 1 223 ? -41.806 9.893   -67.555 1.00 68.10  ? 231 ARG B O   1 
ATOM 3987 C CB  . ARG B 1 223 ? -43.157 6.918   -68.208 1.00 69.05  ? 231 ARG B CB  1 
ATOM 3988 C CG  . ARG B 1 223 ? -43.255 5.536   -68.840 1.00 76.92  ? 231 ARG B CG  1 
ATOM 3989 C CD  . ARG B 1 223 ? -44.677 5.217   -69.273 1.00 80.34  ? 231 ARG B CD  1 
ATOM 3990 N NE  . ARG B 1 223 ? -45.427 4.495   -68.251 1.00 80.44  ? 231 ARG B NE  1 
ATOM 3991 C CZ  . ARG B 1 223 ? -45.380 3.181   -68.069 1.00 78.40  ? 231 ARG B CZ  1 
ATOM 3992 N NH1 . ARG B 1 223 ? -44.518 2.423   -68.723 1.00 76.33  ? 231 ARG B NH1 1 
ATOM 3993 N NH2 . ARG B 1 223 ? -46.192 2.620   -67.176 1.00 80.85  ? 231 ARG B NH2 1 
ATOM 3994 N N   . LEU B 1 224 ? -41.335 8.279   -66.058 1.00 70.98  ? 232 LEU B N   1 
ATOM 3995 C CA  . LEU B 1 224 ? -41.145 9.239   -64.977 1.00 68.44  ? 232 LEU B CA  1 
ATOM 3996 C C   . LEU B 1 224 ? -39.866 10.056  -65.151 1.00 70.09  ? 232 LEU B C   1 
ATOM 3997 O O   . LEU B 1 224 ? -39.811 11.212  -64.715 1.00 71.93  ? 232 LEU B O   1 
ATOM 3998 C CB  . LEU B 1 224 ? -41.138 8.516   -63.628 1.00 63.78  ? 232 LEU B CB  1 
ATOM 3999 C CG  . LEU B 1 224 ? -42.395 7.706   -63.289 1.00 62.34  ? 232 LEU B CG  1 
ATOM 4000 C CD1 . LEU B 1 224 ? -42.030 6.285   -62.878 1.00 69.21  ? 232 LEU B CD1 1 
ATOM 4001 C CD2 . LEU B 1 224 ? -43.216 8.387   -62.207 1.00 63.50  ? 232 LEU B CD2 1 
ATOM 4002 N N   . SER B 1 225 ? -38.833 9.481   -65.773 1.00 66.57  ? 233 SER B N   1 
ATOM 4003 C CA  . SER B 1 225 ? -37.525 10.133  -65.811 1.00 62.41  ? 233 SER B CA  1 
ATOM 4004 C C   . SER B 1 225 ? -37.428 11.181  -66.917 1.00 69.73  ? 233 SER B C   1 
ATOM 4005 O O   . SER B 1 225 ? -37.125 12.350  -66.652 1.00 71.24  ? 233 SER B O   1 
ATOM 4006 C CB  . SER B 1 225 ? -36.420 9.088   -65.977 1.00 56.34  ? 233 SER B CB  1 
ATOM 4007 O OG  . SER B 1 225 ? -36.404 8.194   -64.880 1.00 60.03  ? 233 SER B OG  1 
ATOM 4008 N N   . LEU B 1 226 ? -37.684 10.784  -68.164 1.00 70.39  ? 234 LEU B N   1 
ATOM 4009 C CA  . LEU B 1 226 ? -37.393 11.668  -69.283 1.00 63.88  ? 234 LEU B CA  1 
ATOM 4010 C C   . LEU B 1 226 ? -38.387 12.825  -69.347 1.00 61.67  ? 234 LEU B C   1 
ATOM 4011 O O   . LEU B 1 226 ? -39.493 12.743  -68.805 1.00 63.40  ? 234 LEU B O   1 
ATOM 4012 C CB  . LEU B 1 226 ? -37.403 10.906  -70.608 1.00 57.01  ? 234 LEU B CB  1 
ATOM 4013 C CG  . LEU B 1 226 ? -36.469 9.713   -70.796 1.00 61.23  ? 234 LEU B CG  1 
ATOM 4014 C CD1 . LEU B 1 226 ? -37.256 8.437   -70.913 1.00 67.05  ? 234 LEU B CD1 1 
ATOM 4015 C CD2 . LEU B 1 226 ? -35.586 9.931   -72.009 1.00 69.56  ? 234 LEU B CD2 1 
ATOM 4016 N N   . PRO B 1 227 ? -37.997 13.928  -69.988 1.00 62.68  ? 235 PRO B N   1 
ATOM 4017 C CA  . PRO B 1 227 ? -38.904 15.074  -70.126 1.00 71.61  ? 235 PRO B CA  1 
ATOM 4018 C C   . PRO B 1 227 ? -40.239 14.683  -70.747 1.00 66.46  ? 235 PRO B C   1 
ATOM 4019 O O   . PRO B 1 227 ? -40.323 13.771  -71.570 1.00 59.15  ? 235 PRO B O   1 
ATOM 4020 C CB  . PRO B 1 227 ? -38.118 16.038  -71.025 1.00 72.38  ? 235 PRO B CB  1 
ATOM 4021 C CG  . PRO B 1 227 ? -36.695 15.660  -70.838 1.00 70.08  ? 235 PRO B CG  1 
ATOM 4022 C CD  . PRO B 1 227 ? -36.686 14.187  -70.608 1.00 64.43  ? 235 PRO B CD  1 
ATOM 4023 N N   . ASN B 1 228 ? -41.296 15.364  -70.305 1.00 69.57  ? 236 ASN B N   1 
ATOM 4024 C CA  . ASN B 1 228 ? -42.647 15.090  -70.779 1.00 68.83  ? 236 ASN B CA  1 
ATOM 4025 C C   . ASN B 1 228 ? -42.719 15.143  -72.299 1.00 71.00  ? 236 ASN B C   1 
ATOM 4026 O O   . ASN B 1 228 ? -42.191 16.064  -72.929 1.00 73.50  ? 236 ASN B O   1 
ATOM 4027 C CB  . ASN B 1 228 ? -43.621 16.096  -70.167 1.00 77.27  ? 236 ASN B CB  1 
ATOM 4028 C CG  . ASN B 1 228 ? -43.669 16.010  -68.658 1.00 84.63  ? 236 ASN B CG  1 
ATOM 4029 O OD1 . ASN B 1 228 ? -44.200 15.053  -68.097 1.00 84.45  ? 236 ASN B OD1 1 
ATOM 4030 N ND2 . ASN B 1 228 ? -43.110 17.014  -67.990 1.00 84.70  ? 236 ASN B ND2 1 
ATOM 4031 N N   . GLY B 1 229 ? -43.371 14.140  -72.885 1.00 74.37  ? 237 GLY B N   1 
ATOM 4032 C CA  . GLY B 1 229 ? -43.489 14.034  -74.318 1.00 69.70  ? 237 GLY B CA  1 
ATOM 4033 C C   . GLY B 1 229 ? -42.347 13.306  -74.993 1.00 76.70  ? 237 GLY B C   1 
ATOM 4034 O O   . GLY B 1 229 ? -42.481 12.917  -76.160 1.00 85.36  ? 237 GLY B O   1 
ATOM 4035 N N   . ALA B 1 230 ? -41.231 13.112  -74.296 1.00 69.80  ? 238 ALA B N   1 
ATOM 4036 C CA  . ALA B 1 230 ? -40.073 12.468  -74.891 1.00 66.33  ? 238 ALA B CA  1 
ATOM 4037 C C   . ALA B 1 230 ? -40.354 10.991  -75.155 1.00 64.10  ? 238 ALA B C   1 
ATOM 4038 O O   . ALA B 1 230 ? -41.373 10.428  -74.743 1.00 66.00  ? 238 ALA B O   1 
ATOM 4039 C CB  . ALA B 1 230 ? -38.847 12.618  -73.994 1.00 62.78  ? 238 ALA B CB  1 
ATOM 4040 N N   . THR B 1 231 ? -39.418 10.365  -75.857 1.00 67.19  ? 239 THR B N   1 
ATOM 4041 C CA  . THR B 1 231 ? -39.531 8.984   -76.285 1.00 70.65  ? 239 THR B CA  1 
ATOM 4042 C C   . THR B 1 231 ? -38.370 8.198   -75.684 1.00 72.01  ? 239 THR B C   1 
ATOM 4043 O O   . THR B 1 231 ? -37.399 8.779   -75.197 1.00 69.03  ? 239 THR B O   1 
ATOM 4044 C CB  . THR B 1 231 ? -39.531 8.925   -77.820 1.00 80.58  ? 239 THR B CB  1 
ATOM 4045 O OG1 . THR B 1 231 ? -40.512 9.843   -78.316 1.00 96.34  ? 239 THR B OG1 1 
ATOM 4046 C CG2 . THR B 1 231 ? -39.931 7.573   -78.303 1.00 70.65  ? 239 THR B CG2 1 
ATOM 4047 N N   . ARG B 1 232 ? -38.476 6.866   -75.685 1.00 71.43  ? 240 ARG B N   1 
ATOM 4048 C CA  . ARG B 1 232 ? -37.381 6.059   -75.153 1.00 71.13  ? 240 ARG B CA  1 
ATOM 4049 C C   . ARG B 1 232 ? -36.092 6.225   -75.950 1.00 75.06  ? 240 ARG B C   1 
ATOM 4050 O O   . ARG B 1 232 ? -35.009 5.970   -75.411 1.00 69.01  ? 240 ARG B O   1 
ATOM 4051 C CB  . ARG B 1 232 ? -37.776 4.582   -75.089 1.00 73.29  ? 240 ARG B CB  1 
ATOM 4052 C CG  . ARG B 1 232 ? -38.661 4.222   -73.897 1.00 74.57  ? 240 ARG B CG  1 
ATOM 4053 C CD  . ARG B 1 232 ? -38.954 2.727   -73.867 1.00 72.86  ? 240 ARG B CD  1 
ATOM 4054 N NE  . ARG B 1 232 ? -39.968 2.332   -74.838 1.00 79.78  ? 240 ARG B NE  1 
ATOM 4055 C CZ  . ARG B 1 232 ? -41.251 2.662   -74.772 1.00 85.39  ? 240 ARG B CZ  1 
ATOM 4056 N NH1 . ARG B 1 232 ? -41.722 3.428   -73.800 1.00 86.01  ? 240 ARG B NH1 1 
ATOM 4057 N NH2 . ARG B 1 232 ? -42.081 2.232   -75.718 1.00 87.07  ? 240 ARG B NH2 1 
ATOM 4058 N N   . ASP B 1 233 ? -36.176 6.647   -77.212 1.00 84.63  ? 241 ASP B N   1 
ATOM 4059 C CA  . ASP B 1 233 ? -34.988 6.910   -78.014 1.00 85.81  ? 241 ASP B CA  1 
ATOM 4060 C C   . ASP B 1 233 ? -34.463 8.330   -77.839 1.00 80.78  ? 241 ASP B C   1 
ATOM 4061 O O   . ASP B 1 233 ? -33.510 8.713   -78.526 1.00 84.53  ? 241 ASP B O   1 
ATOM 4062 C CB  . ASP B 1 233 ? -35.274 6.640   -79.494 1.00 87.05  ? 241 ASP B CB  1 
ATOM 4063 C CG  . ASP B 1 233 ? -35.398 5.161   -79.804 1.00 92.02  ? 241 ASP B CG  1 
ATOM 4064 O OD1 . ASP B 1 233 ? -34.363 4.461   -79.801 1.00 86.89  ? 241 ASP B OD1 1 
ATOM 4065 O OD2 . ASP B 1 233 ? -36.530 4.699   -80.051 1.00 106.06 ? 241 ASP B OD2 1 
ATOM 4066 N N   . HIS B 1 234 ? -35.066 9.111   -76.943 1.00 73.61  ? 242 HIS B N   1 
ATOM 4067 C CA  . HIS B 1 234 ? -34.492 10.385  -76.530 1.00 69.83  ? 242 HIS B CA  1 
ATOM 4068 C C   . HIS B 1 234 ? -33.072 10.197  -76.022 1.00 70.00  ? 242 HIS B C   1 
ATOM 4069 O O   . HIS B 1 234 ? -32.754 9.189   -75.384 1.00 72.26  ? 242 HIS B O   1 
ATOM 4070 C CB  . HIS B 1 234 ? -35.353 11.003  -75.421 1.00 65.08  ? 242 HIS B CB  1 
ATOM 4071 C CG  . HIS B 1 234 ? -35.172 12.480  -75.243 1.00 65.81  ? 242 HIS B CG  1 
ATOM 4072 N ND1 . HIS B 1 234 ? -34.043 13.019  -74.666 1.00 58.92  ? 242 HIS B ND1 1 
ATOM 4073 C CD2 . HIS B 1 234 ? -35.974 13.527  -75.550 1.00 74.55  ? 242 HIS B CD2 1 
ATOM 4074 C CE1 . HIS B 1 234 ? -34.157 14.334  -74.624 1.00 62.44  ? 242 HIS B CE1 1 
ATOM 4075 N NE2 . HIS B 1 234 ? -35.318 14.669  -75.157 1.00 70.51  ? 242 HIS B NE2 1 
ATOM 4076 N N   . HIS B 1 235 ? -32.205 11.157  -76.336 1.00 68.04  ? 243 HIS B N   1 
ATOM 4077 C CA  . HIS B 1 235 ? -30.892 11.132  -75.723 1.00 63.15  ? 243 HIS B CA  1 
ATOM 4078 C C   . HIS B 1 235 ? -31.082 11.245  -74.215 1.00 72.80  ? 243 HIS B C   1 
ATOM 4079 O O   . HIS B 1 235 ? -32.125 11.704  -73.739 1.00 73.17  ? 243 HIS B O   1 
ATOM 4080 C CB  . HIS B 1 235 ? -30.003 12.252  -76.267 1.00 62.71  ? 243 HIS B CB  1 
ATOM 4081 C CG  . HIS B 1 235 ? -30.270 13.594  -75.662 1.00 59.87  ? 243 HIS B CG  1 
ATOM 4082 N ND1 . HIS B 1 235 ? -29.509 14.110  -74.636 1.00 64.77  ? 243 HIS B ND1 1 
ATOM 4083 C CD2 . HIS B 1 235 ? -31.200 14.534  -75.951 1.00 54.40  ? 243 HIS B CD2 1 
ATOM 4084 C CE1 . HIS B 1 235 ? -29.967 15.305  -74.309 1.00 61.12  ? 243 HIS B CE1 1 
ATOM 4085 N NE2 . HIS B 1 235 ? -30.993 15.586  -75.092 1.00 53.24  ? 243 HIS B NE2 1 
ATOM 4086 N N   . MET B 1 236 ? -30.069 10.791  -73.470 1.00 76.83  ? 244 MET B N   1 
ATOM 4087 C CA  . MET B 1 236 ? -30.067 10.676  -72.010 1.00 72.62  ? 244 MET B CA  1 
ATOM 4088 C C   . MET B 1 236 ? -30.779 9.380   -71.644 1.00 73.27  ? 244 MET B C   1 
ATOM 4089 O O   . MET B 1 236 ? -30.939 9.056   -70.463 1.00 78.31  ? 244 MET B O   1 
ATOM 4090 C CB  . MET B 1 236 ? -30.863 11.794  -71.328 1.00 66.74  ? 244 MET B CB  1 
ATOM 4091 C CG  . MET B 1 236 ? -30.200 13.154  -71.322 1.00 72.28  ? 244 MET B CG  1 
ATOM 4092 S SD  . MET B 1 236 ? -31.195 14.352  -70.413 1.00 75.01  ? 244 MET B SD  1 
ATOM 4093 C CE  . MET B 1 236 ? -32.828 14.025  -71.079 1.00 63.25  ? 244 MET B CE  1 
ATOM 4094 N N   . ALA B 1 237 ? -31.219 8.639   -72.663 1.00 76.26  ? 245 ALA B N   1 
ATOM 4095 C CA  . ALA B 1 237 ? -31.779 7.303   -72.492 1.00 74.01  ? 245 ALA B CA  1 
ATOM 4096 C C   . ALA B 1 237 ? -31.119 6.383   -73.507 1.00 72.45  ? 245 ALA B C   1 
ATOM 4097 O O   . ALA B 1 237 ? -30.510 5.379   -73.125 1.00 70.99  ? 245 ALA B O   1 
ATOM 4098 C CB  . ALA B 1 237 ? -33.305 7.261   -72.648 1.00 73.60  ? 245 ALA B CB  1 
ATOM 4099 N N   . ASN B 1 238 ? -31.226 6.700   -74.797 1.00 74.65  ? 246 ASN B N   1 
ATOM 4100 C CA  . ASN B 1 238 ? -30.556 5.940   -75.836 1.00 76.84  ? 246 ASN B CA  1 
ATOM 4101 C C   . ASN B 1 238 ? -29.328 6.707   -76.292 1.00 75.66  ? 246 ASN B C   1 
ATOM 4102 O O   . ASN B 1 238 ? -29.468 7.848   -76.763 1.00 76.98  ? 246 ASN B O   1 
ATOM 4103 C CB  . ASN B 1 238 ? -31.493 5.694   -77.012 1.00 80.52  ? 246 ASN B CB  1 
ATOM 4104 C CG  . ASN B 1 238 ? -30.959 4.651   -77.978 1.00 86.76  ? 246 ASN B CG  1 
ATOM 4105 O OD1 . ASN B 1 238 ? -29.798 4.247   -77.899 1.00 78.72  ? 246 ASN B OD1 1 
ATOM 4106 N ND2 . ASN B 1 238 ? -31.810 4.206   -78.895 1.00 91.13  ? 246 ASN B ND2 1 
ATOM 4107 N N   . PRO B 1 239 ? -28.121 6.147   -76.179 1.00 75.50  ? 247 PRO B N   1 
ATOM 4108 C CA  . PRO B 1 239 ? -26.947 6.813   -76.764 1.00 79.06  ? 247 PRO B CA  1 
ATOM 4109 C C   . PRO B 1 239 ? -26.902 6.727   -78.279 1.00 80.99  ? 247 PRO B C   1 
ATOM 4110 O O   . PRO B 1 239 ? -26.077 7.415   -78.895 1.00 82.25  ? 247 PRO B O   1 
ATOM 4111 C CB  . PRO B 1 239 ? -25.767 6.065   -76.132 1.00 73.80  ? 247 PRO B CB  1 
ATOM 4112 C CG  . PRO B 1 239 ? -26.316 4.718   -75.795 1.00 76.10  ? 247 PRO B CG  1 
ATOM 4113 C CD  . PRO B 1 239 ? -27.760 4.929   -75.433 1.00 73.81  ? 247 PRO B CD  1 
ATOM 4114 N N   . PHE B 1 240 ? -27.759 5.910   -78.894 1.00 76.40  ? 248 PHE B N   1 
ATOM 4115 C CA  . PHE B 1 240 ? -27.786 5.724   -80.340 1.00 78.24  ? 248 PHE B CA  1 
ATOM 4116 C C   . PHE B 1 240 ? -29.138 6.107   -80.931 1.00 82.53  ? 248 PHE B C   1 
ATOM 4117 O O   . PHE B 1 240 ? -29.461 5.706   -82.055 1.00 78.92  ? 248 PHE B O   1 
ATOM 4118 C CB  . PHE B 1 240 ? -27.435 4.279   -80.698 1.00 76.51  ? 248 PHE B CB  1 
ATOM 4119 C CG  . PHE B 1 240 ? -26.261 3.737   -79.934 1.00 75.07  ? 248 PHE B CG  1 
ATOM 4120 C CD1 . PHE B 1 240 ? -25.034 4.379   -79.976 1.00 73.27  ? 248 PHE B CD1 1 
ATOM 4121 C CD2 . PHE B 1 240 ? -26.385 2.586   -79.174 1.00 80.20  ? 248 PHE B CD2 1 
ATOM 4122 C CE1 . PHE B 1 240 ? -23.953 3.882   -79.274 1.00 70.37  ? 248 PHE B CE1 1 
ATOM 4123 C CE2 . PHE B 1 240 ? -25.307 2.085   -78.470 1.00 82.10  ? 248 PHE B CE2 1 
ATOM 4124 C CZ  . PHE B 1 240 ? -24.089 2.734   -78.520 1.00 77.28  ? 248 PHE B CZ  1 
ATOM 4125 N N   . GLY B 1 241 ? -29.937 6.868   -80.186 1.00 79.49  ? 249 GLY B N   1 
ATOM 4126 C CA  . GLY B 1 241 ? -31.138 7.479   -80.704 1.00 82.51  ? 249 GLY B CA  1 
ATOM 4127 C C   . GLY B 1 241 ? -30.841 8.491   -81.792 1.00 81.20  ? 249 GLY B C   1 
ATOM 4128 O O   . GLY B 1 241 ? -29.692 8.893   -82.002 1.00 79.30  ? 249 GLY B O   1 
ATOM 4129 N N   . PRO B 1 242 ? -31.878 8.914   -82.522 1.00 81.22  ? 250 PRO B N   1 
ATOM 4130 C CA  . PRO B 1 242 ? -31.651 9.897   -83.595 1.00 78.91  ? 250 PRO B CA  1 
ATOM 4131 C C   . PRO B 1 242 ? -31.140 11.228  -83.074 1.00 79.91  ? 250 PRO B C   1 
ATOM 4132 O O   . PRO B 1 242 ? -30.263 11.839  -83.699 1.00 85.07  ? 250 PRO B O   1 
ATOM 4133 C CB  . PRO B 1 242 ? -33.037 10.032  -84.245 1.00 74.01  ? 250 PRO B CB  1 
ATOM 4134 C CG  . PRO B 1 242 ? -33.782 8.796   -83.845 1.00 65.57  ? 250 PRO B CG  1 
ATOM 4135 C CD  . PRO B 1 242 ? -33.270 8.437   -82.485 1.00 76.95  ? 250 PRO B CD  1 
ATOM 4136 N N   . THR B 1 243 ? -31.669 11.701  -81.945 1.00 79.16  ? 251 THR B N   1 
ATOM 4137 C CA  . THR B 1 243 ? -31.261 12.994  -81.413 1.00 84.08  ? 251 THR B CA  1 
ATOM 4138 C C   . THR B 1 243 ? -29.928 12.913  -80.676 1.00 80.20  ? 251 THR B C   1 
ATOM 4139 O O   . THR B 1 243 ? -29.271 13.944  -80.488 1.00 76.20  ? 251 THR B O   1 
ATOM 4140 C CB  . THR B 1 243 ? -32.344 13.544  -80.477 1.00 82.98  ? 251 THR B CB  1 
ATOM 4141 O OG1 . THR B 1 243 ? -33.636 13.282  -81.035 1.00 83.62  ? 251 THR B OG1 1 
ATOM 4142 C CG2 . THR B 1 243 ? -32.186 15.049  -80.297 1.00 70.56  ? 251 THR B CG2 1 
ATOM 4143 N N   . SER B 1 244 ? -29.513 11.714  -80.266 1.00 77.73  ? 252 SER B N   1 
ATOM 4144 C CA  . SER B 1 244 ? -28.280 11.569  -79.508 1.00 80.05  ? 252 SER B CA  1 
ATOM 4145 C C   . SER B 1 244 ? -27.073 11.858  -80.401 1.00 83.91  ? 252 SER B C   1 
ATOM 4146 O O   . SER B 1 244 ? -27.142 11.697  -81.623 1.00 84.59  ? 252 SER B O   1 
ATOM 4147 C CB  . SER B 1 244 ? -28.176 10.160  -78.930 1.00 77.23  ? 252 SER B CB  1 
ATOM 4148 O OG  . SER B 1 244 ? -27.973 9.206   -79.958 1.00 76.87  ? 252 SER B OG  1 
ATOM 4149 N N   . PRO B 1 245 ? -25.955 12.284  -79.819 1.00 82.05  ? 253 PRO B N   1 
ATOM 4150 C CA  . PRO B 1 245 ? -24.798 12.671  -80.634 1.00 89.78  ? 253 PRO B CA  1 
ATOM 4151 C C   . PRO B 1 245 ? -24.071 11.469  -81.222 1.00 97.13  ? 253 PRO B C   1 
ATOM 4152 O O   . PRO B 1 245 ? -24.321 10.309  -80.888 1.00 92.66  ? 253 PRO B O   1 
ATOM 4153 C CB  . PRO B 1 245 ? -23.907 13.426  -79.636 1.00 84.18  ? 253 PRO B CB  1 
ATOM 4154 C CG  . PRO B 1 245 ? -24.806 13.684  -78.432 1.00 76.92  ? 253 PRO B CG  1 
ATOM 4155 C CD  . PRO B 1 245 ? -25.664 12.472  -78.392 1.00 77.13  ? 253 PRO B CD  1 
ATOM 4156 N N   . THR B 1 246 ? -23.148 11.780  -82.130 1.00 104.49 ? 254 THR B N   1 
ATOM 4157 C CA  . THR B 1 246 ? -22.268 10.781  -82.720 1.00 106.28 ? 254 THR B CA  1 
ATOM 4158 C C   . THR B 1 246 ? -21.090 10.525  -81.786 1.00 105.99 ? 254 THR B C   1 
ATOM 4159 O O   . THR B 1 246 ? -20.498 11.466  -81.248 1.00 109.31 ? 254 THR B O   1 
ATOM 4160 C CB  . THR B 1 246 ? -21.783 11.239  -84.095 1.00 105.82 ? 254 THR B CB  1 
ATOM 4161 O OG1 . THR B 1 246 ? -20.747 12.217  -83.946 1.00 104.47 ? 254 THR B OG1 1 
ATOM 4162 C CG2 . THR B 1 246 ? -22.936 11.838  -84.893 1.00 105.47 ? 254 THR B CG2 1 
ATOM 4163 N N   . LEU B 1 247 ? -20.735 9.253   -81.617 1.00 104.41 ? 255 LEU B N   1 
ATOM 4164 C CA  . LEU B 1 247 ? -19.697 8.851   -80.669 1.00 110.30 ? 255 LEU B CA  1 
ATOM 4165 C C   . LEU B 1 247 ? -18.308 8.699   -81.297 1.00 109.78 ? 255 LEU B C   1 
ATOM 4166 O O   . LEU B 1 247 ? -17.302 8.896   -80.601 1.00 106.84 ? 255 LEU B O   1 
ATOM 4167 C CB  . LEU B 1 247 ? -20.086 7.542   -79.962 1.00 107.82 ? 255 LEU B CB  1 
ATOM 4168 C CG  . LEU B 1 247 ? -20.899 7.646   -78.662 1.00 99.04  ? 255 LEU B CG  1 
ATOM 4169 C CD1 . LEU B 1 247 ? -19.980 8.046   -77.509 1.00 96.01  ? 255 LEU B CD1 1 
ATOM 4170 C CD2 . LEU B 1 247 ? -22.078 8.606   -78.783 1.00 99.73  ? 255 LEU B CD2 1 
ATOM 4171 N N   . GLU B 1 248 ? -18.227 8.275   -82.566 1.00 111.33 ? 256 GLU B N   1 
ATOM 4172 C CA  . GLU B 1 248 ? -16.954 8.059   -83.258 1.00 112.37 ? 256 GLU B CA  1 
ATOM 4173 C C   . GLU B 1 248 ? -15.999 9.246   -83.164 1.00 109.28 ? 256 GLU B C   1 
ATOM 4174 O O   . GLU B 1 248 ? -14.827 9.071   -82.820 1.00 109.70 ? 256 GLU B O   1 
ATOM 4175 C CB  . GLU B 1 248 ? -17.216 7.701   -84.727 1.00 108.69 ? 256 GLU B CB  1 
ATOM 4176 C CG  . GLU B 1 248 ? -15.990 7.681   -85.677 1.00 110.50 ? 256 GLU B CG  1 
ATOM 4177 C CD  . GLU B 1 248 ? -14.680 7.190   -85.050 1.00 115.86 ? 256 GLU B CD  1 
ATOM 4178 O OE1 . GLU B 1 248 ? -14.695 6.225   -84.256 1.00 113.47 ? 256 GLU B OE1 1 
ATOM 4179 O OE2 . GLU B 1 248 ? -13.613 7.762   -85.372 1.00 113.29 ? 256 GLU B OE2 1 
ATOM 4180 N N   . SER B 1 249 ? -16.471 10.447  -83.493 1.00 104.03 ? 257 SER B N   1 
ATOM 4181 C CA  . SER B 1 249 ? -15.631 11.636  -83.378 1.00 103.89 ? 257 SER B CA  1 
ATOM 4182 C C   . SER B 1 249 ? -15.114 11.808  -81.950 1.00 111.74 ? 257 SER B C   1 
ATOM 4183 O O   . SER B 1 249 ? -13.901 11.877  -81.719 1.00 114.23 ? 257 SER B O   1 
ATOM 4184 C CB  . SER B 1 249 ? -16.411 12.863  -83.847 1.00 102.54 ? 257 SER B CB  1 
ATOM 4185 O OG  . SER B 1 249 ? -17.764 12.786  -83.432 1.00 103.86 ? 257 SER B OG  1 
ATOM 4186 N N   . ILE B 1 250 ? -16.031 11.883  -80.977 1.00 112.72 ? 258 ILE B N   1 
ATOM 4187 C CA  . ILE B 1 250 ? -15.657 12.091  -79.580 1.00 110.30 ? 258 ILE B CA  1 
ATOM 4188 C C   . ILE B 1 250 ? -14.723 10.989  -79.098 1.00 112.02 ? 258 ILE B C   1 
ATOM 4189 O O   . ILE B 1 250 ? -14.984 9.796   -79.293 1.00 111.82 ? 258 ILE B O   1 
ATOM 4190 C CB  . ILE B 1 250 ? -16.918 12.160  -78.706 1.00 106.68 ? 258 ILE B CB  1 
ATOM 4191 C CG1 . ILE B 1 250 ? -17.996 12.990  -79.397 1.00 102.29 ? 258 ILE B CG1 1 
ATOM 4192 C CG2 . ILE B 1 250 ? -16.586 12.754  -77.349 1.00 108.61 ? 258 ILE B CG2 1 
ATOM 4193 C CD1 . ILE B 1 250 ? -19.248 13.191  -78.564 1.00 93.15  ? 258 ILE B CD1 1 
ATOM 4194 N N   . SER B 1 251 ? -13.632 11.390  -78.447 1.00 114.56 ? 259 SER B N   1 
ATOM 4195 C CA  . SER B 1 251 ? -12.710 10.447  -77.823 1.00 118.08 ? 259 SER B CA  1 
ATOM 4196 C C   . SER B 1 251 ? -13.192 10.074  -76.426 1.00 117.18 ? 259 SER B C   1 
ATOM 4197 O O   . SER B 1 251 ? -13.488 10.951  -75.608 1.00 113.05 ? 259 SER B O   1 
ATOM 4198 C CB  . SER B 1 251 ? -11.301 11.040  -77.754 1.00 123.32 ? 259 SER B CB  1 
ATOM 4199 O OG  . SER B 1 251 ? -11.286 12.244  -77.006 1.00 125.08 ? 259 SER B OG  1 
ATOM 4200 N N   . LEU B 1 252 ? -13.263 8.775   -76.151 1.00 120.78 ? 260 LEU B N   1 
ATOM 4201 C CA  . LEU B 1 252 ? -13.720 8.271   -74.866 1.00 119.11 ? 260 LEU B CA  1 
ATOM 4202 C C   . LEU B 1 252 ? -12.560 7.724   -74.046 1.00 115.29 ? 260 LEU B C   1 
ATOM 4203 O O   . LEU B 1 252 ? -11.529 7.310   -74.586 1.00 114.50 ? 260 LEU B O   1 
ATOM 4204 C CB  . LEU B 1 252 ? -14.764 7.164   -75.045 1.00 114.51 ? 260 LEU B CB  1 
ATOM 4205 C CG  . LEU B 1 252 ? -16.119 7.499   -75.664 1.00 108.93 ? 260 LEU B CG  1 
ATOM 4206 C CD1 . LEU B 1 252 ? -17.150 6.477   -75.216 1.00 101.97 ? 260 LEU B CD1 1 
ATOM 4207 C CD2 . LEU B 1 252 ? -16.562 8.904   -75.293 1.00 105.71 ? 260 LEU B CD2 1 
ATOM 4208 N N   . GLU B 1 253 ? -12.743 7.733   -72.731 1.00 117.30 ? 261 GLU B N   1 
ATOM 4209 C CA  . GLU B 1 253 ? -11.817 7.083   -71.823 1.00 112.53 ? 261 GLU B CA  1 
ATOM 4210 C C   . GLU B 1 253 ? -12.146 5.594   -71.744 1.00 107.77 ? 261 GLU B C   1 
ATOM 4211 O O   . GLU B 1 253 ? -13.268 5.182   -72.050 1.00 103.87 ? 261 GLU B O   1 
ATOM 4212 C CB  . GLU B 1 253 ? -11.886 7.735   -70.443 1.00 103.11 ? 261 GLU B CB  1 
ATOM 4213 C CG  . GLU B 1 253 ? -11.359 9.166   -70.398 1.00 104.16 ? 261 GLU B CG  1 
ATOM 4214 C CD  . GLU B 1 253 ? -9.961  9.301   -70.984 1.00 109.29 ? 261 GLU B CD  1 
ATOM 4215 O OE1 . GLU B 1 253 ? -9.120  8.409   -70.736 1.00 112.73 ? 261 GLU B OE1 1 
ATOM 4216 O OE2 . GLU B 1 253 ? -9.701  10.298  -71.690 1.00 105.41 ? 261 GLU B OE2 1 
ATOM 4217 N N   . PRO B 1 254 ? -11.179 4.762   -71.356 1.00 107.49 ? 262 PRO B N   1 
ATOM 4218 C CA  . PRO B 1 254 ? -11.449 3.321   -71.260 1.00 104.33 ? 262 PRO B CA  1 
ATOM 4219 C C   . PRO B 1 254 ? -12.571 3.012   -70.276 1.00 101.33 ? 262 PRO B C   1 
ATOM 4220 O O   . PRO B 1 254 ? -12.653 3.590   -69.191 1.00 103.41 ? 262 PRO B O   1 
ATOM 4221 C CB  . PRO B 1 254 ? -10.109 2.734   -70.799 1.00 104.83 ? 262 PRO B CB  1 
ATOM 4222 C CG  . PRO B 1 254 ? -9.315  3.896   -70.305 1.00 103.98 ? 262 PRO B CG  1 
ATOM 4223 C CD  . PRO B 1 254 ? -9.777  5.089   -71.055 1.00 109.13 ? 262 PRO B CD  1 
ATOM 4224 N N   . MET B 1 255 ? -13.442 2.085   -70.675 1.00 102.37 ? 263 MET B N   1 
ATOM 4225 C CA  . MET B 1 255 ? -14.653 1.756   -69.936 1.00 97.79  ? 263 MET B CA  1 
ATOM 4226 C C   . MET B 1 255 ? -14.715 0.257   -69.664 1.00 99.01  ? 263 MET B C   1 
ATOM 4227 O O   . MET B 1 255 ? -13.978 -0.537  -70.253 1.00 105.22 ? 263 MET B O   1 
ATOM 4228 C CB  . MET B 1 255 ? -15.907 2.206   -70.695 1.00 92.64  ? 263 MET B CB  1 
ATOM 4229 C CG  . MET B 1 255 ? -15.960 3.697   -70.987 1.00 100.45 ? 263 MET B CG  1 
ATOM 4230 S SD  . MET B 1 255 ? -17.650 4.321   -71.075 1.00 123.84 ? 263 MET B SD  1 
ATOM 4231 C CE  . MET B 1 255 ? -18.518 2.851   -71.616 1.00 99.62  ? 263 MET B CE  1 
ATOM 4232 N N   . LEU B 1 256 ? -15.613 -0.124  -68.754 1.00 91.97  ? 264 LEU B N   1 
ATOM 4233 C CA  . LEU B 1 256 ? -15.851 -1.524  -68.413 1.00 92.26  ? 264 LEU B CA  1 
ATOM 4234 C C   . LEU B 1 256 ? -17.342 -1.719  -68.186 1.00 89.49  ? 264 LEU B C   1 
ATOM 4235 O O   . LEU B 1 256 ? -17.925 -1.074  -67.308 1.00 96.04  ? 264 LEU B O   1 
ATOM 4236 C CB  . LEU B 1 256 ? -15.062 -1.934  -67.164 1.00 96.20  ? 264 LEU B CB  1 
ATOM 4237 C CG  . LEU B 1 256 ? -15.209 -3.370  -66.647 1.00 101.20 ? 264 LEU B CG  1 
ATOM 4238 C CD1 . LEU B 1 256 ? -15.324 -4.377  -67.791 1.00 101.32 ? 264 LEU B CD1 1 
ATOM 4239 C CD2 . LEU B 1 256 ? -14.061 -3.737  -65.712 1.00 98.90  ? 264 LEU B CD2 1 
ATOM 4240 N N   . VAL B 1 257 ? -17.958 -2.595  -68.977 1.00 89.53  ? 265 VAL B N   1 
ATOM 4241 C CA  . VAL B 1 257 ? -19.380 -2.901  -68.862 1.00 97.94  ? 265 VAL B CA  1 
ATOM 4242 C C   . VAL B 1 257 ? -19.535 -4.282  -68.234 1.00 99.84  ? 265 VAL B C   1 
ATOM 4243 O O   . VAL B 1 257 ? -18.955 -5.263  -68.717 1.00 100.96 ? 265 VAL B O   1 
ATOM 4244 C CB  . VAL B 1 257 ? -20.074 -2.831  -70.234 1.00 96.68  ? 265 VAL B CB  1 
ATOM 4245 C CG1 . VAL B 1 257 ? -21.572 -3.060  -70.090 1.00 93.34  ? 265 VAL B CG1 1 
ATOM 4246 C CG2 . VAL B 1 257 ? -19.788 -1.493  -70.905 1.00 94.98  ? 265 VAL B CG2 1 
ATOM 4247 N N   . ILE B 1 258 ? -20.316 -4.357  -67.156 1.00 98.44  ? 266 ILE B N   1 
ATOM 4248 C CA  . ILE B 1 258 ? -20.599 -5.604  -66.450 1.00 87.66  ? 266 ILE B CA  1 
ATOM 4249 C C   . ILE B 1 258 ? -22.105 -5.820  -66.442 1.00 84.21  ? 266 ILE B C   1 
ATOM 4250 O O   . ILE B 1 258 ? -22.864 -4.915  -66.076 1.00 83.33  ? 266 ILE B O   1 
ATOM 4251 C CB  . ILE B 1 258 ? -20.045 -5.587  -65.015 1.00 83.92  ? 266 ILE B CB  1 
ATOM 4252 C CG1 . ILE B 1 258 ? -18.625 -5.026  -65.003 1.00 83.81  ? 266 ILE B CG1 1 
ATOM 4253 C CG2 . ILE B 1 258 ? -20.079 -6.988  -64.418 1.00 89.34  ? 266 ILE B CG2 1 
ATOM 4254 C CD1 . ILE B 1 258 ? -18.126 -4.660  -63.631 1.00 80.08  ? 266 ILE B CD1 1 
ATOM 4255 N N   . VAL B 1 259 ? -22.537 -7.013  -66.854 1.00 87.55  ? 267 VAL B N   1 
ATOM 4256 C CA  . VAL B 1 259 ? -23.955 -7.325  -66.976 1.00 89.36  ? 267 VAL B CA  1 
ATOM 4257 C C   . VAL B 1 259 ? -24.217 -8.748  -66.491 1.00 91.56  ? 267 VAL B C   1 
ATOM 4258 O O   . VAL B 1 259 ? -23.361 -9.631  -66.599 1.00 94.55  ? 267 VAL B O   1 
ATOM 4259 C CB  . VAL B 1 259 ? -24.431 -7.152  -68.440 1.00 86.49  ? 267 VAL B CB  1 
ATOM 4260 C CG1 . VAL B 1 259 ? -25.925 -7.353  -68.559 1.00 90.13  ? 267 VAL B CG1 1 
ATOM 4261 C CG2 . VAL B 1 259 ? -24.032 -5.789  -68.990 1.00 83.37  ? 267 VAL B CG2 1 
ATOM 4262 N N   . GLY B 1 260 ? -25.416 -8.961  -65.951 1.00 86.10  ? 268 GLY B N   1 
ATOM 4263 C CA  . GLY B 1 260 ? -25.864 -10.294 -65.583 1.00 93.57  ? 268 GLY B CA  1 
ATOM 4264 C C   . GLY B 1 260 ? -26.501 -10.986 -66.778 1.00 87.76  ? 268 GLY B C   1 
ATOM 4265 O O   . GLY B 1 260 ? -27.172 -10.355 -67.592 1.00 80.25  ? 268 GLY B O   1 
ATOM 4266 N N   . GLY B 1 261 ? -26.252 -12.293 -66.884 1.00 89.50  ? 269 GLY B N   1 
ATOM 4267 C CA  . GLY B 1 261 ? -26.770 -13.061 -68.009 1.00 90.51  ? 269 GLY B CA  1 
ATOM 4268 C C   . GLY B 1 261 ? -28.269 -12.931 -68.207 1.00 92.85  ? 269 GLY B C   1 
ATOM 4269 O O   . GLY B 1 261 ? -28.746 -12.799 -69.337 1.00 101.10 ? 269 GLY B O   1 
ATOM 4270 N N   . SER B 1 262 ? -29.033 -12.978 -67.118 1.00 86.38  ? 270 SER B N   1 
ATOM 4271 C CA  . SER B 1 262 ? -30.490 -12.953 -67.191 1.00 86.55  ? 270 SER B CA  1 
ATOM 4272 C C   . SER B 1 262 ? -31.074 -11.546 -67.254 1.00 85.26  ? 270 SER B C   1 
ATOM 4273 O O   . SER B 1 262 ? -32.301 -11.407 -67.298 1.00 78.88  ? 270 SER B O   1 
ATOM 4274 C CB  . SER B 1 262 ? -31.094 -13.701 -65.998 1.00 92.63  ? 270 SER B CB  1 
ATOM 4275 O OG  . SER B 1 262 ? -30.592 -15.025 -65.924 1.00 88.88  ? 270 SER B OG  1 
ATOM 4276 N N   . GLU B 1 263 ? -30.238 -10.510 -67.246 1.00 87.98  ? 271 GLU B N   1 
ATOM 4277 C CA  . GLU B 1 263 ? -30.734 -9.139  -67.232 1.00 89.84  ? 271 GLU B CA  1 
ATOM 4278 C C   . GLU B 1 263 ? -31.554 -8.830  -68.481 1.00 86.06  ? 271 GLU B C   1 
ATOM 4279 O O   . GLU B 1 263 ? -31.298 -9.357  -69.567 1.00 92.80  ? 271 GLU B O   1 
ATOM 4280 C CB  . GLU B 1 263 ? -29.569 -8.155  -67.131 1.00 87.60  ? 271 GLU B CB  1 
ATOM 4281 C CG  . GLU B 1 263 ? -28.957 -8.042  -65.749 1.00 84.00  ? 271 GLU B CG  1 
ATOM 4282 C CD  . GLU B 1 263 ? -28.257 -6.715  -65.535 1.00 85.36  ? 271 GLU B CD  1 
ATOM 4283 O OE1 . GLU B 1 263 ? -28.950 -5.677  -65.492 1.00 79.55  ? 271 GLU B OE1 1 
ATOM 4284 O OE2 . GLU B 1 263 ? -27.015 -6.709  -65.408 1.00 89.04  ? 271 GLU B OE2 1 
ATOM 4285 N N   . LEU B 1 264 ? -32.555 -7.956  -68.317 1.00 82.96  ? 272 LEU B N   1 
ATOM 4286 C CA  . LEU B 1 264 ? -33.290 -7.453  -69.473 1.00 87.52  ? 272 LEU B CA  1 
ATOM 4287 C C   . LEU B 1 264 ? -32.470 -6.444  -70.260 1.00 88.38  ? 272 LEU B C   1 
ATOM 4288 O O   . LEU B 1 264 ? -32.772 -6.191  -71.432 1.00 88.25  ? 272 LEU B O   1 
ATOM 4289 C CB  . LEU B 1 264 ? -34.621 -6.811  -69.061 1.00 87.58  ? 272 LEU B CB  1 
ATOM 4290 C CG  . LEU B 1 264 ? -35.768 -7.641  -68.480 1.00 83.83  ? 272 LEU B CG  1 
ATOM 4291 C CD1 . LEU B 1 264 ? -35.583 -7.907  -67.006 1.00 88.60  ? 272 LEU B CD1 1 
ATOM 4292 C CD2 . LEU B 1 264 ? -37.100 -6.945  -68.731 1.00 77.71  ? 272 LEU B CD2 1 
ATOM 4293 N N   . LEU B 1 265 ? -31.447 -5.858  -69.641 1.00 84.82  ? 273 LEU B N   1 
ATOM 4294 C CA  . LEU B 1 265 ? -30.537 -4.943  -70.312 1.00 85.74  ? 273 LEU B CA  1 
ATOM 4295 C C   . LEU B 1 265 ? -29.242 -5.629  -70.727 1.00 89.61  ? 273 LEU B C   1 
ATOM 4296 O O   . LEU B 1 265 ? -28.218 -4.959  -70.891 1.00 90.57  ? 273 LEU B O   1 
ATOM 4297 C CB  . LEU B 1 265 ? -30.234 -3.750  -69.404 1.00 87.94  ? 273 LEU B CB  1 
ATOM 4298 C CG  . LEU B 1 265 ? -31.447 -3.007  -68.842 1.00 86.13  ? 273 LEU B CG  1 
ATOM 4299 C CD1 . LEU B 1 265 ? -31.019 -1.758  -68.090 1.00 70.58  ? 273 LEU B CD1 1 
ATOM 4300 C CD2 . LEU B 1 265 ? -32.427 -2.657  -69.950 1.00 78.71  ? 273 LEU B CD2 1 
ATOM 4301 N N   . ARG B 1 266 ? -29.265 -6.954  -70.895 1.00 92.18  ? 274 ARG B N   1 
ATOM 4302 C CA  . ARG B 1 266 ? -28.074 -7.666  -71.347 1.00 91.36  ? 274 ARG B CA  1 
ATOM 4303 C C   . ARG B 1 266 ? -27.667 -7.226  -72.753 1.00 88.72  ? 274 ARG B C   1 
ATOM 4304 O O   . ARG B 1 266 ? -26.561 -6.713  -72.957 1.00 90.94  ? 274 ARG B O   1 
ATOM 4305 C CB  . ARG B 1 266 ? -28.289 -9.187  -71.227 1.00 93.62  ? 274 ARG B CB  1 
ATOM 4306 C CG  . ARG B 1 266 ? -28.889 -9.940  -72.410 1.00 96.35  ? 274 ARG B CG  1 
ATOM 4307 C CD  . ARG B 1 266 ? -29.169 -11.392 -72.087 1.00 98.98  ? 274 ARG B CD  1 
ATOM 4308 N NE  . ARG B 1 266 ? -28.687 -12.270 -73.146 1.00 102.52 ? 274 ARG B NE  1 
ATOM 4309 C CZ  . ARG B 1 266 ? -29.448 -12.777 -74.106 1.00 101.81 ? 274 ARG B CZ  1 
ATOM 4310 N NH1 . ARG B 1 266 ? -30.731 -12.470 -74.208 1.00 97.65  ? 274 ARG B NH1 1 
ATOM 4311 N NH2 . ARG B 1 266 ? -28.900 -13.591 -75.003 1.00 99.94  ? 274 ARG B NH2 1 
ATOM 4312 N N   . ASP B 1 267 ? -28.556 -7.394  -73.735 1.00 83.21  ? 275 ASP B N   1 
ATOM 4313 C CA  . ASP B 1 267 ? -28.213 -7.036  -75.106 1.00 88.00  ? 275 ASP B CA  1 
ATOM 4314 C C   . ASP B 1 267 ? -28.039 -5.531  -75.275 1.00 85.43  ? 275 ASP B C   1 
ATOM 4315 O O   . ASP B 1 267 ? -27.224 -5.099  -76.097 1.00 86.87  ? 275 ASP B O   1 
ATOM 4316 C CB  . ASP B 1 267 ? -29.250 -7.602  -76.076 1.00 87.51  ? 275 ASP B CB  1 
ATOM 4317 C CG  . ASP B 1 267 ? -30.655 -7.180  -75.742 1.00 85.22  ? 275 ASP B CG  1 
ATOM 4318 O OD1 . ASP B 1 267 ? -30.836 -6.223  -74.959 1.00 85.91  ? 275 ASP B OD1 1 
ATOM 4319 O OD2 . ASP B 1 267 ? -31.592 -7.827  -76.247 1.00 79.57  ? 275 ASP B OD2 1 
ATOM 4320 N N   . ARG B 1 268 ? -28.808 -4.724  -74.535 1.00 81.62  ? 276 ARG B N   1 
ATOM 4321 C CA  . ARG B 1 268 ? -28.614 -3.277  -74.572 1.00 78.44  ? 276 ARG B CA  1 
ATOM 4322 C C   . ARG B 1 268 ? -27.162 -2.927  -74.292 1.00 77.81  ? 276 ARG B C   1 
ATOM 4323 O O   . ARG B 1 268 ? -26.535 -2.162  -75.033 1.00 77.69  ? 276 ARG B O   1 
ATOM 4324 C CB  . ARG B 1 268 ? -29.524 -2.583  -73.560 1.00 81.66  ? 276 ARG B CB  1 
ATOM 4325 C CG  . ARG B 1 268 ? -30.972 -2.961  -73.687 1.00 79.63  ? 276 ARG B CG  1 
ATOM 4326 C CD  . ARG B 1 268 ? -31.477 -2.612  -75.060 1.00 69.24  ? 276 ARG B CD  1 
ATOM 4327 N NE  . ARG B 1 268 ? -31.869 -1.218  -75.218 1.00 59.80  ? 276 ARG B NE  1 
ATOM 4328 C CZ  . ARG B 1 268 ? -32.558 -0.765  -76.255 1.00 68.15  ? 276 ARG B CZ  1 
ATOM 4329 N NH1 . ARG B 1 268 ? -32.999 -1.579  -77.198 1.00 70.68  ? 276 ARG B NH1 1 
ATOM 4330 N NH2 . ARG B 1 268 ? -32.820 0.534   -76.343 1.00 69.44  ? 276 ARG B NH2 1 
ATOM 4331 N N   . ALA B 1 269 ? -26.613 -3.485  -73.214 1.00 82.00  ? 277 ALA B N   1 
ATOM 4332 C CA  . ALA B 1 269 ? -25.215 -3.246  -72.891 1.00 81.36  ? 277 ALA B CA  1 
ATOM 4333 C C   . ALA B 1 269 ? -24.278 -3.984  -73.843 1.00 82.07  ? 277 ALA B C   1 
ATOM 4334 O O   . ALA B 1 269 ? -23.151 -3.525  -74.068 1.00 81.99  ? 277 ALA B O   1 
ATOM 4335 C CB  . ALA B 1 269 ? -24.942 -3.628  -71.441 1.00 82.46  ? 277 ALA B CB  1 
ATOM 4336 N N   . LYS B 1 270 ? -24.695 -5.133  -74.393 1.00 87.23  ? 278 LYS B N   1 
ATOM 4337 C CA  . LYS B 1 270 ? -23.881 -5.750  -75.440 1.00 89.39  ? 278 LYS B CA  1 
ATOM 4338 C C   . LYS B 1 270 ? -23.878 -4.895  -76.694 1.00 86.02  ? 278 LYS B C   1 
ATOM 4339 O O   . LYS B 1 270 ? -22.813 -4.529  -77.202 1.00 87.96  ? 278 LYS B O   1 
ATOM 4340 C CB  . LYS B 1 270 ? -24.368 -7.157  -75.802 1.00 93.43  ? 278 LYS B CB  1 
ATOM 4341 C CG  . LYS B 1 270 ? -23.819 -8.291  -74.965 1.00 98.41  ? 278 LYS B CG  1 
ATOM 4342 C CD  . LYS B 1 270 ? -24.627 -9.570  -75.104 1.00 103.46 ? 278 LYS B CD  1 
ATOM 4343 C CE  . LYS B 1 270 ? -25.750 -9.643  -74.103 1.00 103.62 ? 278 LYS B CE  1 
ATOM 4344 N NZ  . LYS B 1 270 ? -26.018 -11.043 -73.680 1.00 101.25 ? 278 LYS B NZ  1 
ATOM 4345 N N   . GLU B 1 271 ? -25.069 -4.555  -77.196 1.00 83.97  ? 279 GLU B N   1 
ATOM 4346 C CA  . GLU B 1 271 ? -25.179 -3.681  -78.358 1.00 85.39  ? 279 GLU B CA  1 
ATOM 4347 C C   . GLU B 1 271 ? -24.395 -2.396  -78.147 1.00 84.58  ? 279 GLU B C   1 
ATOM 4348 O O   . GLU B 1 271 ? -23.699 -1.927  -79.054 1.00 88.24  ? 279 GLU B O   1 
ATOM 4349 C CB  . GLU B 1 271 ? -26.651 -3.386  -78.637 1.00 77.32  ? 279 GLU B CB  1 
ATOM 4350 C CG  . GLU B 1 271 ? -27.375 -4.517  -79.339 1.00 76.54  ? 279 GLU B CG  1 
ATOM 4351 C CD  . GLU B 1 271 ? -28.720 -4.095  -79.883 1.00 81.34  ? 279 GLU B CD  1 
ATOM 4352 O OE1 . GLU B 1 271 ? -29.011 -2.882  -79.862 1.00 71.03  ? 279 GLU B OE1 1 
ATOM 4353 O OE2 . GLU B 1 271 ? -29.491 -4.976  -80.319 1.00 84.55  ? 279 GLU B OE2 1 
ATOM 4354 N N   . TYR B 1 272 ? -24.499 -1.813  -76.953 1.00 86.14  ? 280 TYR B N   1 
ATOM 4355 C CA  . TYR B 1 272 ? -23.674 -0.661  -76.611 1.00 88.66  ? 280 TYR B CA  1 
ATOM 4356 C C   . TYR B 1 272 ? -22.194 -0.998  -76.761 1.00 88.88  ? 280 TYR B C   1 
ATOM 4357 O O   . TYR B 1 272 ? -21.508 -0.461  -77.637 1.00 92.13  ? 280 TYR B O   1 
ATOM 4358 C CB  . TYR B 1 272 ? -24.007 -0.195  -75.190 1.00 84.48  ? 280 TYR B CB  1 
ATOM 4359 C CG  . TYR B 1 272 ? -23.197 0.980   -74.685 1.00 81.70  ? 280 TYR B CG  1 
ATOM 4360 C CD1 . TYR B 1 272 ? -21.951 0.800   -74.095 1.00 86.34  ? 280 TYR B CD1 1 
ATOM 4361 C CD2 . TYR B 1 272 ? -23.685 2.275   -74.801 1.00 75.33  ? 280 TYR B CD2 1 
ATOM 4362 C CE1 . TYR B 1 272 ? -21.219 1.878   -73.634 1.00 82.63  ? 280 TYR B CE1 1 
ATOM 4363 C CE2 . TYR B 1 272 ? -22.960 3.356   -74.346 1.00 76.03  ? 280 TYR B CE2 1 
ATOM 4364 C CZ  . TYR B 1 272 ? -21.728 3.154   -73.764 1.00 79.21  ? 280 TYR B CZ  1 
ATOM 4365 O OH  . TYR B 1 272 ? -21.004 4.232   -73.309 1.00 78.55  ? 280 TYR B OH  1 
ATOM 4366 N N   . ALA B 1 273 ? -21.695 -1.921  -75.931 1.00 87.71  ? 281 ALA B N   1 
ATOM 4367 C CA  . ALA B 1 273 ? -20.284 -2.303  -75.971 1.00 86.79  ? 281 ALA B CA  1 
ATOM 4368 C C   . ALA B 1 273 ? -19.844 -2.677  -77.383 1.00 97.54  ? 281 ALA B C   1 
ATOM 4369 O O   . ALA B 1 273 ? -18.831 -2.174  -77.881 1.00 97.01  ? 281 ALA B O   1 
ATOM 4370 C CB  . ALA B 1 273 ? -20.025 -3.458  -75.002 1.00 92.71  ? 281 ALA B CB  1 
ATOM 4371 N N   . TYR B 1 274 ? -20.590 -3.580  -78.029 1.00 102.85 ? 282 TYR B N   1 
ATOM 4372 C CA  . TYR B 1 274 ? -20.367 -3.929  -79.433 1.00 103.22 ? 282 TYR B CA  1 
ATOM 4373 C C   . TYR B 1 274 ? -20.110 -2.707  -80.309 1.00 95.82  ? 282 TYR B C   1 
ATOM 4374 O O   . TYR B 1 274 ? -19.151 -2.676  -81.086 1.00 92.90  ? 282 TYR B O   1 
ATOM 4375 C CB  . TYR B 1 274 ? -21.567 -4.717  -79.967 1.00 103.94 ? 282 TYR B CB  1 
ATOM 4376 C CG  . TYR B 1 274 ? -21.243 -5.682  -81.085 1.00 104.81 ? 282 TYR B CG  1 
ATOM 4377 C CD1 . TYR B 1 274 ? -20.477 -6.817  -80.852 1.00 103.76 ? 282 TYR B CD1 1 
ATOM 4378 C CD2 . TYR B 1 274 ? -21.712 -5.462  -82.374 1.00 104.49 ? 282 TYR B CD2 1 
ATOM 4379 C CE1 . TYR B 1 274 ? -20.182 -7.702  -81.876 1.00 111.66 ? 282 TYR B CE1 1 
ATOM 4380 C CE2 . TYR B 1 274 ? -21.424 -6.339  -83.402 1.00 108.83 ? 282 TYR B CE2 1 
ATOM 4381 C CZ  . TYR B 1 274 ? -20.658 -7.458  -83.148 1.00 117.30 ? 282 TYR B CZ  1 
ATOM 4382 O OH  . TYR B 1 274 ? -20.370 -8.334  -84.171 1.00 118.49 ? 282 TYR B OH  1 
ATOM 4383 N N   . LYS B 1 275 ? -20.977 -1.698  -80.215 1.00 91.31  ? 283 LYS B N   1 
ATOM 4384 C CA  . LYS B 1 275 ? -20.853 -0.535  -81.087 1.00 93.10  ? 283 LYS B CA  1 
ATOM 4385 C C   . LYS B 1 275 ? -19.612 0.285   -80.751 1.00 99.08  ? 283 LYS B C   1 
ATOM 4386 O O   . LYS B 1 275 ? -18.862 0.684   -81.649 1.00 107.11 ? 283 LYS B O   1 
ATOM 4387 C CB  . LYS B 1 275 ? -22.122 0.314   -81.012 1.00 85.85  ? 283 LYS B CB  1 
ATOM 4388 C CG  . LYS B 1 275 ? -23.312 -0.340  -81.703 1.00 79.06  ? 283 LYS B CG  1 
ATOM 4389 C CD  . LYS B 1 275 ? -24.539 0.553   -81.715 1.00 79.46  ? 283 LYS B CD  1 
ATOM 4390 C CE  . LYS B 1 275 ? -25.715 -0.152  -82.376 1.00 64.67  ? 283 LYS B CE  1 
ATOM 4391 N NZ  . LYS B 1 275 ? -26.884 0.752   -82.551 1.00 57.03  ? 283 LYS B NZ  1 
ATOM 4392 N N   . LEU B 1 276 ? -19.384 0.559   -79.463 1.00 94.81  ? 284 LEU B N   1 
ATOM 4393 C CA  . LEU B 1 276 ? -18.189 1.299   -79.058 1.00 93.53  ? 284 LEU B CA  1 
ATOM 4394 C C   . LEU B 1 276 ? -16.903 0.605   -79.509 1.00 95.39  ? 284 LEU B C   1 
ATOM 4395 O O   . LEU B 1 276 ? -16.020 1.242   -80.096 1.00 95.10  ? 284 LEU B O   1 
ATOM 4396 C CB  . LEU B 1 276 ? -18.183 1.524   -77.540 1.00 93.87  ? 284 LEU B CB  1 
ATOM 4397 C CG  . LEU B 1 276 ? -19.068 2.595   -76.879 1.00 86.28  ? 284 LEU B CG  1 
ATOM 4398 C CD1 . LEU B 1 276 ? -18.664 3.975   -77.381 1.00 87.44  ? 284 LEU B CD1 1 
ATOM 4399 C CD2 . LEU B 1 276 ? -20.557 2.391   -77.096 1.00 89.14  ? 284 LEU B CD2 1 
ATOM 4400 N N   . LYS B 1 277 ? -16.765 -0.697  -79.229 1.00 100.37 ? 285 LYS B N   1 
ATOM 4401 C CA  . LYS B 1 277 ? -15.530 -1.398  -79.590 1.00 108.18 ? 285 LYS B CA  1 
ATOM 4402 C C   . LYS B 1 277 ? -15.322 -1.431  -81.102 1.00 107.44 ? 285 LYS B C   1 
ATOM 4403 O O   . LYS B 1 277 ? -14.195 -1.268  -81.585 1.00 99.90  ? 285 LYS B O   1 
ATOM 4404 C CB  . LYS B 1 277 ? -15.538 -2.822  -79.026 1.00 108.65 ? 285 LYS B CB  1 
ATOM 4405 C CG  . LYS B 1 277 ? -16.693 -3.680  -79.508 1.00 106.10 ? 285 LYS B CG  1 
ATOM 4406 C CD  . LYS B 1 277 ? -16.648 -5.103  -78.983 1.00 103.68 ? 285 LYS B CD  1 
ATOM 4407 C CE  . LYS B 1 277 ? -17.237 -5.176  -77.587 1.00 91.08  ? 285 LYS B CE  1 
ATOM 4408 N NZ  . LYS B 1 277 ? -18.004 -6.435  -77.386 1.00 81.12  ? 285 LYS B NZ  1 
ATOM 4409 N N   . LYS B 1 278 ? -16.398 -1.626  -81.863 1.00 105.21 ? 286 LYS B N   1 
ATOM 4410 C CA  . LYS B 1 278 ? -16.344 -1.669  -83.318 1.00 104.33 ? 286 LYS B CA  1 
ATOM 4411 C C   . LYS B 1 278 ? -16.213 -0.281  -83.936 1.00 102.88 ? 286 LYS B C   1 
ATOM 4412 O O   . LYS B 1 278 ? -15.969 -0.167  -85.143 1.00 109.11 ? 286 LYS B O   1 
ATOM 4413 C CB  . LYS B 1 278 ? -17.601 -2.398  -83.833 1.00 97.86  ? 286 LYS B CB  1 
ATOM 4414 C CG  . LYS B 1 278 ? -17.936 -2.277  -85.314 1.00 91.77  ? 286 LYS B CG  1 
ATOM 4415 C CD  . LYS B 1 278 ? -18.785 -3.456  -85.767 1.00 90.00  ? 286 LYS B CD  1 
ATOM 4416 C CE  . LYS B 1 278 ? -17.923 -4.675  -86.045 1.00 97.17  ? 286 LYS B CE  1 
ATOM 4417 N NZ  . LYS B 1 278 ? -18.704 -5.800  -86.630 1.00 103.85 ? 286 LYS B NZ  1 
ATOM 4418 N N   . MET B 1 279 ? -16.268 0.770   -83.125 1.00 98.16  ? 287 MET B N   1 
ATOM 4419 C CA  . MET B 1 279 ? -16.247 2.123   -83.653 1.00 103.05 ? 287 MET B CA  1 
ATOM 4420 C C   . MET B 1 279 ? -14.841 2.694   -83.783 1.00 104.95 ? 287 MET B C   1 
ATOM 4421 O O   . MET B 1 279 ? -14.626 3.577   -84.619 1.00 107.57 ? 287 MET B O   1 
ATOM 4422 C CB  . MET B 1 279 ? -17.146 3.000   -82.774 1.00 102.42 ? 287 MET B CB  1 
ATOM 4423 C CG  . MET B 1 279 ? -17.117 4.484   -83.013 1.00 102.93 ? 287 MET B CG  1 
ATOM 4424 S SD  . MET B 1 279 ? -18.432 5.237   -82.035 1.00 110.43 ? 287 MET B SD  1 
ATOM 4425 C CE  . MET B 1 279 ? -19.849 4.920   -83.083 1.00 105.80 ? 287 MET B CE  1 
ATOM 4426 N N   . GLY B 1 280 ? -13.871 2.183   -83.028 1.00 97.67  ? 288 GLY B N   1 
ATOM 4427 C CA  . GLY B 1 280 ? -12.506 2.634   -83.208 1.00 102.39 ? 288 GLY B CA  1 
ATOM 4428 C C   . GLY B 1 280 ? -11.966 3.582   -82.160 1.00 100.24 ? 288 GLY B C   1 
ATOM 4429 O O   . GLY B 1 280 ? -12.555 4.634   -81.895 1.00 97.41  ? 288 GLY B O   1 
ATOM 4430 N N   . GLY B 1 281 ? -10.837 3.217   -81.563 1.00 101.23 ? 289 GLY B N   1 
ATOM 4431 C CA  . GLY B 1 281 ? -10.112 4.060   -80.624 1.00 101.78 ? 289 GLY B CA  1 
ATOM 4432 C C   . GLY B 1 281 ? -10.552 3.886   -79.189 1.00 108.25 ? 289 GLY B C   1 
ATOM 4433 O O   . GLY B 1 281 ? -9.718  3.851   -78.282 1.00 109.72 ? 289 GLY B O   1 
ATOM 4434 N N   . LYS B 1 282 ? -11.860 3.800   -78.963 1.00 104.61 ? 290 LYS B N   1 
ATOM 4435 C CA  . LYS B 1 282 ? -12.376 3.644   -77.613 1.00 101.04 ? 290 LYS B CA  1 
ATOM 4436 C C   . LYS B 1 282 ? -11.967 2.293   -77.042 1.00 105.28 ? 290 LYS B C   1 
ATOM 4437 O O   . LYS B 1 282 ? -12.044 1.265   -77.721 1.00 109.02 ? 290 LYS B O   1 
ATOM 4438 C CB  . LYS B 1 282 ? -13.900 3.774   -77.588 1.00 105.92 ? 290 LYS B CB  1 
ATOM 4439 C CG  . LYS B 1 282 ? -14.449 5.112   -78.059 1.00 104.55 ? 290 LYS B CG  1 
ATOM 4440 C CD  . LYS B 1 282 ? -14.672 5.148   -79.560 1.00 95.77  ? 290 LYS B CD  1 
ATOM 4441 C CE  . LYS B 1 282 ? -15.846 6.043   -79.906 1.00 94.61  ? 290 LYS B CE  1 
ATOM 4442 N NZ  . LYS B 1 282 ? -15.500 7.487   -79.828 1.00 105.24 ? 290 LYS B NZ  1 
ATOM 4443 N N   . ARG B 1 283 ? -11.524 2.296   -75.789 1.00 103.40 ? 291 ARG B N   1 
ATOM 4444 C CA  . ARG B 1 283 ? -11.199 1.069   -75.074 1.00 101.06 ? 291 ARG B CA  1 
ATOM 4445 C C   . ARG B 1 283 ? -12.414 0.691   -74.236 1.00 102.03 ? 291 ARG B C   1 
ATOM 4446 O O   . ARG B 1 283 ? -12.726 1.360   -73.248 1.00 99.39  ? 291 ARG B O   1 
ATOM 4447 C CB  . ARG B 1 283 ? -9.967  1.247   -74.191 1.00 100.16 ? 291 ARG B CB  1 
ATOM 4448 C CG  . ARG B 1 283 ? -8.662  1.476   -74.930 1.00 100.72 ? 291 ARG B CG  1 
ATOM 4449 C CD  . ARG B 1 283 ? -7.502  1.422   -73.949 1.00 101.80 ? 291 ARG B CD  1 
ATOM 4450 N NE  . ARG B 1 283 ? -7.378  0.099   -73.347 1.00 108.54 ? 291 ARG B NE  1 
ATOM 4451 C CZ  . ARG B 1 283 ? -6.587  -0.192  -72.323 1.00 107.52 ? 291 ARG B CZ  1 
ATOM 4452 N NH1 . ARG B 1 283 ? -5.843  0.733   -71.740 1.00 102.78 ? 291 ARG B NH1 1 
ATOM 4453 N NH2 . ARG B 1 283 ? -6.550  -1.441  -71.867 1.00 109.17 ? 291 ARG B NH2 1 
ATOM 4454 N N   . VAL B 1 284 ? -13.109 -0.369  -74.636 1.00 105.28 ? 292 VAL B N   1 
ATOM 4455 C CA  . VAL B 1 284 ? -14.291 -0.840  -73.922 1.00 106.62 ? 292 VAL B CA  1 
ATOM 4456 C C   . VAL B 1 284 ? -14.172 -2.348  -73.733 1.00 105.98 ? 292 VAL B C   1 
ATOM 4457 O O   . VAL B 1 284 ? -13.991 -3.095  -74.704 1.00 106.79 ? 292 VAL B O   1 
ATOM 4458 C CB  . VAL B 1 284 ? -15.609 -0.451  -74.624 1.00 103.20 ? 292 VAL B CB  1 
ATOM 4459 C CG1 . VAL B 1 284 ? -15.688 1.057   -74.805 1.00 98.12  ? 292 VAL B CG1 1 
ATOM 4460 C CG2 . VAL B 1 284 ? -15.744 -1.117  -75.976 1.00 101.60 ? 292 VAL B CG2 1 
ATOM 4461 N N   . ASP B 1 285 ? -14.194 -2.783  -72.480 1.00 102.39 ? 293 ASP B N   1 
ATOM 4462 C CA  . ASP B 1 285 ? -14.237 -4.191  -72.128 1.00 101.60 ? 293 ASP B CA  1 
ATOM 4463 C C   . ASP B 1 285 ? -15.650 -4.565  -71.702 1.00 102.61 ? 293 ASP B C   1 
ATOM 4464 O O   . ASP B 1 285 ? -16.381 -3.747  -71.138 1.00 108.93 ? 293 ASP B O   1 
ATOM 4465 C CB  . ASP B 1 285 ? -13.251 -4.496  -71.001 1.00 104.43 ? 293 ASP B CB  1 
ATOM 4466 C CG  . ASP B 1 285 ? -11.814 -4.225  -71.397 1.00 103.62 ? 293 ASP B CG  1 
ATOM 4467 O OD1 . ASP B 1 285 ? -11.562 -3.977  -72.594 1.00 106.27 ? 293 ASP B OD1 1 
ATOM 4468 O OD2 . ASP B 1 285 ? -10.938 -4.247  -70.507 1.00 92.22  ? 293 ASP B OD2 1 
ATOM 4469 N N   . TYR B 1 286 ? -16.033 -5.811  -71.970 1.00 98.72  ? 294 TYR B N   1 
ATOM 4470 C CA  . TYR B 1 286 ? -17.371 -6.278  -71.639 1.00 99.24  ? 294 TYR B CA  1 
ATOM 4471 C C   . TYR B 1 286 ? -17.251 -7.636  -70.961 1.00 101.21 ? 294 TYR B C   1 
ATOM 4472 O O   . TYR B 1 286 ? -16.533 -8.515  -71.451 1.00 105.81 ? 294 TYR B O   1 
ATOM 4473 C CB  . TYR B 1 286 ? -18.264 -6.350  -72.892 1.00 92.05  ? 294 TYR B CB  1 
ATOM 4474 C CG  . TYR B 1 286 ? -19.621 -6.984  -72.659 1.00 85.23  ? 294 TYR B CG  1 
ATOM 4475 C CD1 . TYR B 1 286 ? -19.765 -8.354  -72.453 1.00 85.77  ? 294 TYR B CD1 1 
ATOM 4476 C CD2 . TYR B 1 286 ? -20.759 -6.194  -72.602 1.00 89.27  ? 294 TYR B CD2 1 
ATOM 4477 C CE1 . TYR B 1 286 ? -21.003 -8.911  -72.221 1.00 90.90  ? 294 TYR B CE1 1 
ATOM 4478 C CE2 . TYR B 1 286 ? -21.995 -6.741  -72.371 1.00 92.77  ? 294 TYR B CE2 1 
ATOM 4479 C CZ  . TYR B 1 286 ? -22.113 -8.096  -72.178 1.00 93.70  ? 294 TYR B CZ  1 
ATOM 4480 O OH  . TYR B 1 286 ? -23.359 -8.625  -71.953 1.00 93.42  ? 294 TYR B OH  1 
ATOM 4481 N N   . ILE B 1 287 ? -17.950 -7.800  -69.834 1.00 100.21 ? 295 ILE B N   1 
ATOM 4482 C CA  . ILE B 1 287 ? -17.973 -9.055  -69.083 1.00 96.57  ? 295 ILE B CA  1 
ATOM 4483 C C   . ILE B 1 287 ? -19.415 -9.400  -68.728 1.00 91.33  ? 295 ILE B C   1 
ATOM 4484 O O   . ILE B 1 287 ? -20.153 -8.550  -68.221 1.00 89.95  ? 295 ILE B O   1 
ATOM 4485 C CB  . ILE B 1 287 ? -17.132 -8.986  -67.792 1.00 93.74  ? 295 ILE B CB  1 
ATOM 4486 C CG1 . ILE B 1 287 ? -15.777 -8.323  -68.043 1.00 95.51  ? 295 ILE B CG1 1 
ATOM 4487 C CG2 . ILE B 1 287 ? -16.928 -10.382 -67.222 1.00 93.51  ? 295 ILE B CG2 1 
ATOM 4488 C CD1 . ILE B 1 287 ? -14.777 -8.575  -66.942 1.00 95.70  ? 295 ILE B CD1 1 
ATOM 4489 N N   . GLU B 1 288 ? -19.809 -10.649 -68.981 1.00 91.41  ? 296 GLU B N   1 
ATOM 4490 C CA  . GLU B 1 288 ? -21.108 -11.190 -68.595 1.00 90.70  ? 296 GLU B CA  1 
ATOM 4491 C C   . GLU B 1 288 ? -20.951 -12.244 -67.509 1.00 95.56  ? 296 GLU B C   1 
ATOM 4492 O O   . GLU B 1 288 ? -19.985 -13.015 -67.509 1.00 95.26  ? 296 GLU B O   1 
ATOM 4493 C CB  . GLU B 1 288 ? -21.844 -11.830 -69.777 1.00 93.19  ? 296 GLU B CB  1 
ATOM 4494 C CG  . GLU B 1 288 ? -23.051 -11.063 -70.274 1.00 93.33  ? 296 GLU B CG  1 
ATOM 4495 C CD  . GLU B 1 288 ? -23.816 -11.812 -71.356 1.00 98.15  ? 296 GLU B CD  1 
ATOM 4496 O OE1 . GLU B 1 288 ? -23.180 -12.294 -72.318 1.00 102.54 ? 296 GLU B OE1 1 
ATOM 4497 O OE2 . GLU B 1 288 ? -25.056 -11.929 -71.238 1.00 98.42  ? 296 GLU B OE2 1 
ATOM 4498 N N   . PHE B 1 289 ? -21.906 -12.271 -66.585 1.00 94.14  ? 297 PHE B N   1 
ATOM 4499 C CA  . PHE B 1 289 ? -21.976 -13.289 -65.547 1.00 94.82  ? 297 PHE B CA  1 
ATOM 4500 C C   . PHE B 1 289 ? -23.228 -14.124 -65.802 1.00 89.63  ? 297 PHE B C   1 
ATOM 4501 O O   . PHE B 1 289 ? -24.347 -13.601 -65.756 1.00 86.53  ? 297 PHE B O   1 
ATOM 4502 C CB  . PHE B 1 289 ? -21.993 -12.651 -64.156 1.00 97.65  ? 297 PHE B CB  1 
ATOM 4503 C CG  . PHE B 1 289 ? -20.676 -12.030 -63.748 1.00 102.30 ? 297 PHE B CG  1 
ATOM 4504 C CD1 . PHE B 1 289 ? -20.155 -10.948 -64.444 1.00 100.36 ? 297 PHE B CD1 1 
ATOM 4505 C CD2 . PHE B 1 289 ? -19.957 -12.534 -62.676 1.00 100.73 ? 297 PHE B CD2 1 
ATOM 4506 C CE1 . PHE B 1 289 ? -18.949 -10.378 -64.075 1.00 95.80  ? 297 PHE B CE1 1 
ATOM 4507 C CE2 . PHE B 1 289 ? -18.749 -11.969 -62.304 1.00 97.98  ? 297 PHE B CE2 1 
ATOM 4508 C CZ  . PHE B 1 289 ? -18.245 -10.890 -63.004 1.00 92.69  ? 297 PHE B CZ  1 
ATOM 4509 N N   . GLU B 1 290 ? -23.034 -15.416 -66.073 1.00 91.48  ? 298 GLU B N   1 
ATOM 4510 C CA  . GLU B 1 290 ? -24.096 -16.255 -66.621 1.00 94.42  ? 298 GLU B CA  1 
ATOM 4511 C C   . GLU B 1 290 ? -25.244 -16.452 -65.639 1.00 89.48  ? 298 GLU B C   1 
ATOM 4512 O O   . GLU B 1 290 ? -25.031 -16.880 -64.502 1.00 84.23  ? 298 GLU B O   1 
ATOM 4513 C CB  . GLU B 1 290 ? -23.530 -17.620 -67.005 1.00 95.12  ? 298 GLU B CB  1 
ATOM 4514 C CG  . GLU B 1 290 ? -24.567 -18.579 -67.563 1.00 91.89  ? 298 GLU B CG  1 
ATOM 4515 C CD  . GLU B 1 290 ? -24.051 -19.999 -67.661 1.00 98.69  ? 298 GLU B CD  1 
ATOM 4516 O OE1 . GLU B 1 290 ? -22.992 -20.211 -68.285 1.00 104.65 ? 298 GLU B OE1 1 
ATOM 4517 O OE2 . GLU B 1 290 ? -24.710 -20.904 -67.104 1.00 95.05  ? 298 GLU B OE2 1 
ATOM 4518 N N   . ASN B 1 291 ? -26.469 -16.261 -66.129 1.00 84.08  ? 299 ASN B N   1 
ATOM 4519 C CA  . ASN B 1 291 ? -27.733 -16.473 -65.425 1.00 83.17  ? 299 ASN B CA  1 
ATOM 4520 C C   . ASN B 1 291 ? -27.994 -15.497 -64.281 1.00 85.72  ? 299 ASN B C   1 
ATOM 4521 O O   . ASN B 1 291 ? -28.981 -15.674 -63.556 1.00 89.18  ? 299 ASN B O   1 
ATOM 4522 C CB  . ASN B 1 291 ? -27.847 -17.904 -64.882 1.00 87.59  ? 299 ASN B CB  1 
ATOM 4523 C CG  . ASN B 1 291 ? -28.910 -18.716 -65.591 1.00 90.54  ? 299 ASN B CG  1 
ATOM 4524 O OD1 . ASN B 1 291 ? -30.073 -18.317 -65.660 1.00 89.95  ? 299 ASN B OD1 1 
ATOM 4525 N ND2 . ASN B 1 291 ? -28.517 -19.871 -66.118 1.00 89.87  ? 299 ASN B ND2 1 
ATOM 4526 N N   . LYS B 1 292 ? -27.162 -14.474 -64.085 1.00 88.00  ? 300 LYS B N   1 
ATOM 4527 C CA  . LYS B 1 292 ? -27.402 -13.548 -62.985 1.00 89.88  ? 300 LYS B CA  1 
ATOM 4528 C C   . LYS B 1 292 ? -28.362 -12.444 -63.410 1.00 93.96  ? 300 LYS B C   1 
ATOM 4529 O O   . LYS B 1 292 ? -28.428 -12.054 -64.579 1.00 97.03  ? 300 LYS B O   1 
ATOM 4530 C CB  . LYS B 1 292 ? -26.121 -12.902 -62.438 1.00 86.34  ? 300 LYS B CB  1 
ATOM 4531 C CG  . LYS B 1 292 ? -24.784 -13.642 -62.463 1.00 91.20  ? 300 LYS B CG  1 
ATOM 4532 C CD  . LYS B 1 292 ? -24.802 -15.137 -62.166 1.00 94.56  ? 300 LYS B CD  1 
ATOM 4533 C CE  . LYS B 1 292 ? -25.575 -15.511 -60.907 1.00 85.58  ? 300 LYS B CE  1 
ATOM 4534 N NZ  . LYS B 1 292 ? -25.890 -16.967 -60.921 1.00 85.42  ? 300 LYS B NZ  1 
ATOM 4535 N N   . GLU B 1 293 ? -29.120 -11.957 -62.436 1.00 88.66  ? 301 GLU B N   1 
ATOM 4536 C CA  . GLU B 1 293 ? -30.082 -10.887 -62.623 1.00 80.57  ? 301 GLU B CA  1 
ATOM 4537 C C   . GLU B 1 293 ? -29.452 -9.548  -62.251 1.00 86.92  ? 301 GLU B C   1 
ATOM 4538 O O   . GLU B 1 293 ? -28.338 -9.480  -61.727 1.00 91.62  ? 301 GLU B O   1 
ATOM 4539 C CB  . GLU B 1 293 ? -31.334 -11.170 -61.792 1.00 80.66  ? 301 GLU B CB  1 
ATOM 4540 C CG  . GLU B 1 293 ? -32.061 -12.420 -62.267 1.00 83.44  ? 301 GLU B CG  1 
ATOM 4541 C CD  . GLU B 1 293 ? -33.527 -12.432 -61.914 1.00 86.70  ? 301 GLU B CD  1 
ATOM 4542 O OE1 . GLU B 1 293 ? -33.865 -12.098 -60.762 1.00 91.61  ? 301 GLU B OE1 1 
ATOM 4543 O OE2 . GLU B 1 293 ? -34.340 -12.805 -62.785 1.00 78.26  ? 301 GLU B OE2 1 
ATOM 4544 N N   . HIS B 1 294 ? -30.184 -8.473  -62.538 1.00 86.20  ? 302 HIS B N   1 
ATOM 4545 C CA  . HIS B 1 294 ? -29.658 -7.129  -62.332 1.00 86.10  ? 302 HIS B CA  1 
ATOM 4546 C C   . HIS B 1 294 ? -29.321 -6.899  -60.866 1.00 85.39  ? 302 HIS B C   1 
ATOM 4547 O O   . HIS B 1 294 ? -30.068 -7.293  -59.966 1.00 90.10  ? 302 HIS B O   1 
ATOM 4548 C CB  . HIS B 1 294 ? -30.674 -6.086  -62.793 1.00 86.64  ? 302 HIS B CB  1 
ATOM 4549 C CG  . HIS B 1 294 ? -30.185 -4.672  -62.700 1.00 85.63  ? 302 HIS B CG  1 
ATOM 4550 N ND1 . HIS B 1 294 ? -28.856 -4.349  -62.530 1.00 88.05  ? 302 HIS B ND1 1 
ATOM 4551 C CD2 . HIS B 1 294 ? -30.855 -3.496  -62.732 1.00 77.32  ? 302 HIS B CD2 1 
ATOM 4552 C CE1 . HIS B 1 294 ? -28.727 -3.035  -62.474 1.00 82.88  ? 302 HIS B CE1 1 
ATOM 4553 N NE2 . HIS B 1 294 ? -29.926 -2.495  -62.594 1.00 75.09  ? 302 HIS B NE2 1 
ATOM 4554 N N   . GLY B 1 295 ? -28.188 -6.246  -60.633 1.00 83.41  ? 303 GLY B N   1 
ATOM 4555 C CA  . GLY B 1 295 ? -27.770 -5.962  -59.280 1.00 92.12  ? 303 GLY B CA  1 
ATOM 4556 C C   . GLY B 1 295 ? -27.413 -7.184  -58.472 1.00 98.59  ? 303 GLY B C   1 
ATOM 4557 O O   . GLY B 1 295 ? -27.706 -7.227  -57.277 1.00 104.17 ? 303 GLY B O   1 
ATOM 4558 N N   . PHE B 1 296 ? -26.832 -8.209  -59.100 1.00 98.23  ? 304 PHE B N   1 
ATOM 4559 C CA  . PHE B 1 296 ? -26.296 -9.316  -58.315 1.00 100.18 ? 304 PHE B CA  1 
ATOM 4560 C C   . PHE B 1 296 ? -25.148 -8.824  -57.443 1.00 106.22 ? 304 PHE B C   1 
ATOM 4561 O O   . PHE B 1 296 ? -24.932 -9.335  -56.339 1.00 111.01 ? 304 PHE B O   1 
ATOM 4562 C CB  . PHE B 1 296 ? -25.884 -10.472 -59.231 1.00 98.36  ? 304 PHE B CB  1 
ATOM 4563 C CG  . PHE B 1 296 ? -24.823 -10.123 -60.236 1.00 102.14 ? 304 PHE B CG  1 
ATOM 4564 C CD1 . PHE B 1 296 ? -23.487 -10.089 -59.876 1.00 103.01 ? 304 PHE B CD1 1 
ATOM 4565 C CD2 . PHE B 1 296 ? -25.170 -9.793  -61.534 1.00 96.35  ? 304 PHE B CD2 1 
ATOM 4566 C CE1 . PHE B 1 296 ? -22.515 -9.764  -60.800 1.00 104.31 ? 304 PHE B CE1 1 
ATOM 4567 C CE2 . PHE B 1 296 ? -24.206 -9.464  -62.461 1.00 104.53 ? 304 PHE B CE2 1 
ATOM 4568 C CZ  . PHE B 1 296 ? -22.875 -9.447  -62.093 1.00 107.75 ? 304 PHE B CZ  1 
ATOM 4569 N N   . TYR B 1 297 ? -24.359 -7.884  -57.960 1.00 101.88 ? 305 TYR B N   1 
ATOM 4570 C CA  . TYR B 1 297 ? -23.508 -7.050  -57.126 1.00 97.40  ? 305 TYR B CA  1 
ATOM 4571 C C   . TYR B 1 297 ? -24.381 -6.140  -56.264 1.00 100.24 ? 305 TYR B C   1 
ATOM 4572 O O   . TYR B 1 297 ? -25.544 -5.889  -56.581 1.00 105.33 ? 305 TYR B O   1 
ATOM 4573 C CB  . TYR B 1 297 ? -22.550 -6.232  -57.991 1.00 94.58  ? 305 TYR B CB  1 
ATOM 4574 C CG  . TYR B 1 297 ? -23.248 -5.222  -58.867 1.00 95.03  ? 305 TYR B CG  1 
ATOM 4575 C CD1 . TYR B 1 297 ? -24.002 -5.633  -59.959 1.00 93.87  ? 305 TYR B CD1 1 
ATOM 4576 C CD2 . TYR B 1 297 ? -23.196 -3.866  -58.580 1.00 95.24  ? 305 TYR B CD2 1 
ATOM 4577 C CE1 . TYR B 1 297 ? -24.656 -4.725  -60.759 1.00 87.46  ? 305 TYR B CE1 1 
ATOM 4578 C CE2 . TYR B 1 297 ? -23.849 -2.946  -59.378 1.00 91.18  ? 305 TYR B CE2 1 
ATOM 4579 C CZ  . TYR B 1 297 ? -24.579 -3.384  -60.464 1.00 87.06  ? 305 TYR B CZ  1 
ATOM 4580 O OH  . TYR B 1 297 ? -25.233 -2.477  -61.260 1.00 90.92  ? 305 TYR B OH  1 
ATOM 4581 N N   . SER B 1 298 ? -23.798 -5.622  -55.182 1.00 97.63  ? 306 SER B N   1 
ATOM 4582 C CA  . SER B 1 298 ? -24.497 -4.780  -54.209 1.00 101.72 ? 306 SER B CA  1 
ATOM 4583 C C   . SER B 1 298 ? -25.904 -5.331  -54.016 1.00 113.61 ? 306 SER B C   1 
ATOM 4584 O O   . SER B 1 298 ? -26.854 -4.559  -53.856 1.00 117.35 ? 306 SER B O   1 
ATOM 4585 C CB  . SER B 1 298 ? -25.145 -3.556  -54.869 1.00 96.02  ? 306 SER B CB  1 
ATOM 4586 O OG  . SER B 1 298 ? -26.371 -3.894  -55.494 1.00 99.67  ? 306 SER B OG  1 
ATOM 4587 N N   . ASN B 1 299 ? -26.067 -6.651  -54.046 1.00 108.61 ? 307 ASN B N   1 
ATOM 4588 C CA  . ASN B 1 299 ? -27.322 -7.197  -53.562 1.00 104.45 ? 307 ASN B CA  1 
ATOM 4589 C C   . ASN B 1 299 ? -26.444 -8.439  -53.410 1.00 105.56 ? 307 ASN B C   1 
ATOM 4590 O O   . ASN B 1 299 ? -25.324 -8.492  -53.924 1.00 109.91 ? 307 ASN B O   1 
ATOM 4591 C CB  . ASN B 1 299 ? -28.574 -7.496  -54.385 1.00 99.61  ? 307 ASN B CB  1 
ATOM 4592 C CG  . ASN B 1 299 ? -29.336 -6.245  -54.761 1.00 97.96  ? 307 ASN B CG  1 
ATOM 4593 O OD1 . ASN B 1 299 ? -28.742 -5.214  -55.070 1.00 95.18  ? 307 ASN B OD1 1 
ATOM 4594 N ND2 . ASN B 1 299 ? -30.662 -6.330  -54.739 1.00 97.09  ? 307 ASN B ND2 1 
ATOM 4595 N N   . TYR B 1 300 ? -26.968 -9.444  -52.698 1.00 99.04  ? 308 TYR B N   1 
ATOM 4596 C CA  . TYR B 1 300 ? -26.296 -10.702 -52.363 1.00 98.40  ? 308 TYR B CA  1 
ATOM 4597 C C   . TYR B 1 300 ? -24.775 -10.606 -52.452 1.00 97.15  ? 308 TYR B C   1 
ATOM 4598 O O   . TYR B 1 300 ? -24.162 -11.289 -53.284 1.00 90.17  ? 308 TYR B O   1 
ATOM 4599 C CB  . TYR B 1 300 ? -26.769 -11.842 -53.276 1.00 94.03  ? 308 TYR B CB  1 
ATOM 4600 C CG  . TYR B 1 300 ? -28.258 -11.897 -53.563 1.00 90.00  ? 308 TYR B CG  1 
ATOM 4601 C CD1 . TYR B 1 300 ? -28.877 -10.948 -54.371 1.00 92.36  ? 308 TYR B CD1 1 
ATOM 4602 C CD2 . TYR B 1 300 ? -29.046 -12.904 -53.023 1.00 94.52  ? 308 TYR B CD2 1 
ATOM 4603 C CE1 . TYR B 1 300 ? -30.234 -11.001 -54.629 1.00 91.19  ? 308 TYR B CE1 1 
ATOM 4604 C CE2 . TYR B 1 300 ? -30.403 -12.966 -53.275 1.00 99.39  ? 308 TYR B CE2 1 
ATOM 4605 C CZ  . TYR B 1 300 ? -30.992 -12.012 -54.079 1.00 89.83  ? 308 TYR B CZ  1 
ATOM 4606 O OH  . TYR B 1 300 ? -32.343 -12.072 -54.331 1.00 72.59  ? 308 TYR B OH  1 
ATOM 4607 N N   . PRO B 1 301 ? -24.126 -9.765  -51.633 1.00 104.34 ? 309 PRO B N   1 
ATOM 4608 C CA  . PRO B 1 301 ? -22.666 -9.636  -51.723 1.00 104.72 ? 309 PRO B CA  1 
ATOM 4609 C C   . PRO B 1 301 ? -21.958 -10.868 -51.192 1.00 108.87 ? 309 PRO B C   1 
ATOM 4610 O O   . PRO B 1 301 ? -22.608 -11.814 -50.735 1.00 109.97 ? 309 PRO B O   1 
ATOM 4611 C CB  . PRO B 1 301 ? -22.359 -8.397  -50.868 1.00 105.43 ? 309 PRO B CB  1 
ATOM 4612 C CG  . PRO B 1 301 ? -23.689 -7.784  -50.541 1.00 109.24 ? 309 PRO B CG  1 
ATOM 4613 C CD  . PRO B 1 301 ? -24.677 -8.898  -50.583 1.00 112.16 ? 309 PRO B CD  1 
ATOM 4614 N N   . SER B 1 302 ? -20.627 -10.871 -51.273 1.00 109.36 ? 310 SER B N   1 
ATOM 4615 C CA  . SER B 1 302 ? -19.798 -11.980 -50.811 1.00 106.74 ? 310 SER B CA  1 
ATOM 4616 C C   . SER B 1 302 ? -20.210 -13.288 -51.481 1.00 108.46 ? 310 SER B C   1 
ATOM 4617 O O   . SER B 1 302 ? -19.812 -14.367 -51.030 1.00 109.73 ? 310 SER B O   1 
ATOM 4618 C CB  . SER B 1 302 ? -19.996 -12.211 -49.309 1.00 104.42 ? 310 SER B CB  1 
ATOM 4619 O OG  . SER B 1 302 ? -19.020 -13.101 -48.795 1.00 102.70 ? 310 SER B OG  1 
ATOM 4620 N N   . SER B 1 303 ? -21.022 -13.219 -52.535 1.00 110.20 ? 311 SER B N   1 
ATOM 4621 C CA  . SER B 1 303 ? -21.250 -14.397 -53.357 1.00 108.00 ? 311 SER B CA  1 
ATOM 4622 C C   . SER B 1 303 ? -20.085 -14.382 -54.337 1.00 102.30 ? 311 SER B C   1 
ATOM 4623 O O   . SER B 1 303 ? -19.568 -13.319 -54.692 1.00 101.73 ? 311 SER B O   1 
ATOM 4624 C CB  . SER B 1 303 ? -22.579 -14.287 -54.104 1.00 104.31 ? 311 SER B CB  1 
ATOM 4625 O OG  . SER B 1 303 ? -22.803 -15.425 -54.917 1.00 94.52  ? 311 SER B OG  1 
ATOM 4626 N N   . GLU B 1 304 ? -19.683 -15.577 -54.785 1.00 102.67 ? 312 GLU B N   1 
ATOM 4627 C CA  . GLU B 1 304 ? -18.573 -15.707 -55.727 1.00 107.93 ? 312 GLU B CA  1 
ATOM 4628 C C   . GLU B 1 304 ? -18.620 -14.659 -56.829 1.00 105.38 ? 312 GLU B C   1 
ATOM 4629 O O   . GLU B 1 304 ? -17.631 -13.962 -57.074 1.00 100.61 ? 312 GLU B O   1 
ATOM 4630 C CB  . GLU B 1 304 ? -18.545 -17.112 -56.330 1.00 106.91 ? 312 GLU B CB  1 
ATOM 4631 C CG  . GLU B 1 304 ? -18.111 -18.189 -55.353 1.00 106.66 ? 312 GLU B CG  1 
ATOM 4632 C CD  . GLU B 1 304 ? -17.998 -19.551 -56.004 1.00 103.46 ? 312 GLU B CD  1 
ATOM 4633 O OE1 . GLU B 1 304 ? -17.445 -19.629 -57.121 1.00 104.19 ? 312 GLU B OE1 1 
ATOM 4634 O OE2 . GLU B 1 304 ? -18.455 -20.542 -55.399 1.00 99.22  ? 312 GLU B OE2 1 
ATOM 4635 N N   . ALA B 1 305 ? -19.777 -14.516 -57.480 1.00 102.96 ? 313 ALA B N   1 
ATOM 4636 C CA  . ALA B 1 305 ? -19.932 -13.508 -58.525 1.00 100.04 ? 313 ALA B CA  1 
ATOM 4637 C C   . ALA B 1 305 ? -19.475 -12.136 -58.041 1.00 97.64  ? 313 ALA B C   1 
ATOM 4638 O O   . ALA B 1 305 ? -18.698 -11.456 -58.719 1.00 94.33  ? 313 ALA B O   1 
ATOM 4639 C CB  . ALA B 1 305 ? -21.387 -13.457 -58.995 1.00 92.09  ? 313 ALA B CB  1 
ATOM 4640 N N   . ALA B 1 306 ? -19.916 -11.736 -56.845 1.00 97.81  ? 314 ALA B N   1 
ATOM 4641 C CA  . ALA B 1 306 ? -19.575 -10.418 -56.313 1.00 99.90  ? 314 ALA B CA  1 
ATOM 4642 C C   . ALA B 1 306 ? -18.063 -10.231 -56.207 1.00 101.10 ? 314 ALA B C   1 
ATOM 4643 O O   . ALA B 1 306 ? -17.511 -9.259  -56.736 1.00 97.62  ? 314 ALA B O   1 
ATOM 4644 C CB  . ALA B 1 306 ? -20.248 -10.210 -54.955 1.00 104.12 ? 314 ALA B CB  1 
ATOM 4645 N N   . GLU B 1 307 ? -17.377 -11.134 -55.494 1.00 102.35 ? 315 GLU B N   1 
ATOM 4646 C CA  . GLU B 1 307 ? -15.924 -11.014 -55.383 1.00 101.05 ? 315 GLU B CA  1 
ATOM 4647 C C   . GLU B 1 307 ? -15.247 -11.001 -56.749 1.00 102.03 ? 315 GLU B C   1 
ATOM 4648 O O   . GLU B 1 307 ? -14.220 -10.334 -56.919 1.00 97.95  ? 315 GLU B O   1 
ATOM 4649 C CB  . GLU B 1 307 ? -15.321 -12.133 -54.527 1.00 99.31  ? 315 GLU B CB  1 
ATOM 4650 C CG  . GLU B 1 307 ? -15.543 -12.009 -53.016 1.00 99.60  ? 315 GLU B CG  1 
ATOM 4651 C CD  . GLU B 1 307 ? -16.640 -12.906 -52.493 1.00 107.07 ? 315 GLU B CD  1 
ATOM 4652 O OE1 . GLU B 1 307 ? -17.331 -13.540 -53.312 1.00 101.77 ? 315 GLU B OE1 1 
ATOM 4653 O OE2 . GLU B 1 307 ? -16.801 -12.990 -51.257 1.00 117.08 ? 315 GLU B OE2 1 
ATOM 4654 N N   . GLN B 1 308 ? -15.792 -11.730 -57.729 1.00 99.96  ? 316 GLN B N   1 
ATOM 4655 C CA  . GLN B 1 308 ? -15.253 -11.648 -59.084 1.00 104.75 ? 316 GLN B CA  1 
ATOM 4656 C C   . GLN B 1 308 ? -15.373 -10.234 -59.638 1.00 101.83 ? 316 GLN B C   1 
ATOM 4657 O O   . GLN B 1 308 ? -14.417 -9.697  -60.208 1.00 99.01  ? 316 GLN B O   1 
ATOM 4658 C CB  . GLN B 1 308 ? -15.949 -12.648 -60.009 1.00 104.38 ? 316 GLN B CB  1 
ATOM 4659 C CG  . GLN B 1 308 ? -15.955 -14.091 -59.527 1.00 106.91 ? 316 GLN B CG  1 
ATOM 4660 C CD  . GLN B 1 308 ? -14.592 -14.579 -59.079 1.00 113.13 ? 316 GLN B CD  1 
ATOM 4661 O OE1 . GLN B 1 308 ? -13.597 -14.423 -59.785 1.00 114.74 ? 316 GLN B OE1 1 
ATOM 4662 N NE2 . GLN B 1 308 ? -14.543 -15.181 -57.895 1.00 109.15 ? 316 GLN B NE2 1 
ATOM 4663 N N   . VAL B 1 309 ? -16.532 -9.604  -59.434 1.00 100.43 ? 317 VAL B N   1 
ATOM 4664 C CA  . VAL B 1 309 ? -16.676 -8.184  -59.877 1.00 97.07  ? 317 VAL B CA  1 
ATOM 4665 C C   . VAL B 1 309 ? -15.555 -7.384  -59.203 1.00 94.11  ? 317 VAL B C   1 
ATOM 4666 O O   . VAL B 1 309 ? -14.836 -6.647  -59.903 1.00 88.54  ? 317 VAL B O   1 
ATOM 4667 C CB  . VAL B 1 309 ? -18.057 -7.589  -59.554 1.00 90.15  ? 317 VAL B CB  1 
ATOM 4668 C CG1 . VAL B 1 309 ? -18.053 -6.071  -59.655 1.00 82.68  ? 317 VAL B CG1 1 
ATOM 4669 C CG2 . VAL B 1 309 ? -19.149 -8.185  -60.432 1.00 92.29  ? 317 VAL B CG2 1 
ATOM 4670 N N   . LEU B 1 310 ? -15.400 -7.561  -57.893 1.00 96.34  ? 318 LEU B N   1 
ATOM 4671 C CA  . LEU B 1 310 ? -14.302 -6.876  -57.172 1.00 101.00 ? 318 LEU B CA  1 
ATOM 4672 C C   . LEU B 1 310 ? -12.994 -7.132  -57.920 1.00 102.34 ? 318 LEU B C   1 
ATOM 4673 O O   . LEU B 1 310 ? -12.263 -6.164  -58.200 1.00 104.11 ? 318 LEU B O   1 
ATOM 4674 C CB  . LEU B 1 310 ? -14.234 -7.444  -55.761 1.00 101.13 ? 318 LEU B CB  1 
ATOM 4675 C CG  . LEU B 1 310 ? -15.445 -7.182  -54.861 1.00 102.04 ? 318 LEU B CG  1 
ATOM 4676 C CD1 . LEU B 1 310 ? -15.334 -7.912  -53.535 1.00 93.25  ? 318 LEU B CD1 1 
ATOM 4677 C CD2 . LEU B 1 310 ? -15.579 -5.687  -54.638 1.00 101.46 ? 318 LEU B CD2 1 
ATOM 4678 N N   . ARG B 1 311 ? -12.720 -8.398  -58.221 1.00 99.92  ? 319 ARG B N   1 
ATOM 4679 C CA  . ARG B 1 311 ? -11.441 -8.746  -58.879 1.00 102.69 ? 319 ARG B CA  1 
ATOM 4680 C C   . ARG B 1 311 ? -11.254 -7.907  -60.143 1.00 105.40 ? 319 ARG B C   1 
ATOM 4681 O O   . ARG B 1 311 ? -10.203 -7.245  -60.269 1.00 108.82 ? 319 ARG B O   1 
ATOM 4682 C CB  . ARG B 1 311 ? -11.482 -10.223 -59.270 1.00 103.40 ? 319 ARG B CB  1 
ATOM 4683 C CG  . ARG B 1 311 ? -10.245 -11.036 -58.920 1.00 104.73 ? 319 ARG B CG  1 
ATOM 4684 C CD  . ARG B 1 311 ? -10.596 -12.508 -58.773 1.00 103.91 ? 319 ARG B CD  1 
ATOM 4685 N NE  . ARG B 1 311 ? -11.881 -12.703 -58.094 1.00 103.25 ? 319 ARG B NE  1 
ATOM 4686 C CZ  . ARG B 1 311 ? -12.024 -12.785 -56.778 1.00 107.54 ? 319 ARG B CZ  1 
ATOM 4687 N NH1 . ARG B 1 311 ? -12.130 -13.965 -56.199 1.00 108.41 ? 319 ARG B NH1 1 
ATOM 4688 N NH2 . ARG B 1 311 ? -12.056 -11.686 -56.046 1.00 109.05 ? 319 ARG B NH2 1 
ATOM 4689 N N   . ILE B 1 312 ? -12.252 -7.899  -61.024 1.00 102.32 ? 320 ILE B N   1 
ATOM 4690 C CA  . ILE B 1 312 ? -12.067 -7.220  -62.342 1.00 105.42 ? 320 ILE B CA  1 
ATOM 4691 C C   . ILE B 1 312 ? -11.895 -5.700  -62.174 1.00 107.02 ? 320 ILE B C   1 
ATOM 4692 O O   . ILE B 1 312 ? -10.986 -5.150  -62.822 1.00 110.89 ? 320 ILE B O   1 
ATOM 4693 C CB  . ILE B 1 312 ? -13.207 -7.604  -63.308 1.00 103.12 ? 320 ILE B CB  1 
ATOM 4694 C CG1 . ILE B 1 312 ? -14.515 -6.869  -63.026 1.00 96.06  ? 320 ILE B CG1 1 
ATOM 4695 C CG2 . ILE B 1 312 ? -13.414 -9.118  -63.313 1.00 108.12 ? 320 ILE B CG2 1 
ATOM 4696 C CD1 . ILE B 1 312 ? -15.755 -7.652  -63.414 1.00 94.75  ? 320 ILE B CD1 1 
ATOM 4697 N N   . ILE B 1 313 ? -12.708 -5.046  -61.343 1.00 104.44 ? 321 ILE B N   1 
ATOM 4698 C CA  . ILE B 1 313 ? -12.623 -3.556  -61.275 1.00 103.78 ? 321 ILE B CA  1 
ATOM 4699 C C   . ILE B 1 313 ? -11.221 -3.175  -60.784 1.00 105.15 ? 321 ILE B C   1 
ATOM 4700 O O   . ILE B 1 313 ? -10.651 -2.207  -61.317 1.00 110.93 ? 321 ILE B O   1 
ATOM 4701 C CB  . ILE B 1 313 ? -13.742 -2.954  -60.406 1.00 100.08 ? 321 ILE B CB  1 
ATOM 4702 C CG1 . ILE B 1 313 ? -13.805 -3.576  -59.020 1.00 91.72  ? 321 ILE B CG1 1 
ATOM 4703 C CG2 . ILE B 1 313 ? -15.087 -3.056  -61.123 1.00 101.84 ? 321 ILE B CG2 1 
ATOM 4704 C CD1 . ILE B 1 313 ? -15.186 -3.530  -58.397 1.00 99.06  ? 321 ILE B CD1 1 
ATOM 4705 N N   . GLY B 1 314 ? -10.685 -3.920  -59.823 1.00 102.20 ? 322 GLY B N   1 
ATOM 4706 C CA  . GLY B 1 314 ? -9.314  -3.640  -59.371 1.00 109.32 ? 322 GLY B CA  1 
ATOM 4707 C C   . GLY B 1 314 ? -8.389  -3.575  -60.562 1.00 113.33 ? 322 GLY B C   1 
ATOM 4708 O O   . GLY B 1 314 ? -7.728  -2.537  -60.752 1.00 114.81 ? 322 GLY B O   1 
ATOM 4709 N N   . ASP B 1 315 ? -8.342  -4.657  -61.334 1.00 114.04 ? 323 ASP B N   1 
ATOM 4710 C CA  . ASP B 1 315 ? -7.487  -4.673  -62.546 1.00 119.16 ? 323 ASP B CA  1 
ATOM 4711 C C   . ASP B 1 315 ? -7.834  -3.445  -63.386 1.00 118.79 ? 323 ASP B C   1 
ATOM 4712 O O   . ASP B 1 315 ? -6.921  -2.648  -63.665 1.00 119.06 ? 323 ASP B O   1 
ATOM 4713 C CB  . ASP B 1 315 ? -7.636  -5.975  -63.313 1.00 123.43 ? 323 ASP B CB  1 
ATOM 4714 C CG  . ASP B 1 315 ? -9.039  -6.265  -63.826 1.00 124.34 ? 323 ASP B CG  1 
ATOM 4715 O OD1 . ASP B 1 315 ? -9.949  -5.468  -63.517 1.00 121.33 ? 323 ASP B OD1 1 
ATOM 4716 O OD2 . ASP B 1 315 ? -9.206  -7.281  -64.531 1.00 124.79 ? 323 ASP B OD2 1 
ATOM 4717 N N   . PHE B 1 316 ? -9.113  -3.280  -63.733 1.00 117.73 ? 324 PHE B N   1 
ATOM 4718 C CA  . PHE B 1 316 ? -9.535  -2.151  -64.602 1.00 110.91 ? 324 PHE B CA  1 
ATOM 4719 C C   . PHE B 1 316 ? -8.844  -0.884  -64.155 1.00 108.83 ? 324 PHE B C   1 
ATOM 4720 O O   . PHE B 1 316 ? -8.536  -0.044  -65.009 1.00 108.37 ? 324 PHE B O   1 
ATOM 4721 C CB  . PHE B 1 316 ? -11.048 -1.951  -64.534 1.00 100.32 ? 324 PHE B CB  1 
ATOM 4722 C CG  . PHE B 1 316 ? -11.575 -0.881  -65.476 1.00 101.57 ? 324 PHE B CG  1 
ATOM 4723 C CD1 . PHE B 1 316 ? -12.288 0.206   -64.990 1.00 100.18 ? 324 PHE B CD1 1 
ATOM 4724 C CD2 . PHE B 1 316 ? -11.350 -0.963  -66.844 1.00 106.77 ? 324 PHE B CD2 1 
ATOM 4725 C CE1 . PHE B 1 316 ? -12.770 1.178   -65.851 1.00 103.32 ? 324 PHE B CE1 1 
ATOM 4726 C CE2 . PHE B 1 316 ? -11.831 0.014   -67.699 1.00 100.25 ? 324 PHE B CE2 1 
ATOM 4727 C CZ  . PHE B 1 316 ? -12.539 1.080   -67.199 1.00 101.13 ? 324 PHE B CZ  1 
ATOM 4728 N N   . MET B 1 317 ? -8.611  -0.740  -62.853 1.00 104.57 ? 325 MET B N   1 
ATOM 4729 C CA  . MET B 1 317 ? -8.018  0.516   -62.338 1.00 105.47 ? 325 MET B CA  1 
ATOM 4730 C C   . MET B 1 317 ? -6.489  0.418   -62.343 1.00 111.92 ? 325 MET B C   1 
ATOM 4731 O O   . MET B 1 317 ? -5.844  1.421   -62.703 1.00 109.64 ? 325 MET B O   1 
ATOM 4732 C CB  . MET B 1 317 ? -8.528  0.802   -60.925 1.00 107.66 ? 325 MET B CB  1 
ATOM 4733 C CG  . MET B 1 317 ? -10.020 1.056   -60.888 1.00 109.61 ? 325 MET B CG  1 
ATOM 4734 S SD  . MET B 1 317 ? -10.732 1.011   -59.233 1.00 125.35 ? 325 MET B SD  1 
ATOM 4735 C CE  . MET B 1 317 ? -12.418 0.545   -59.646 1.00 105.64 ? 325 MET B CE  1 
ATOM 4736 N N   . ASN B 1 318 ? -5.930  -0.728  -61.953 1.00 116.43 ? 326 ASN B N   1 
ATOM 4737 C CA  . ASN B 1 318 ? -4.444  -0.796  -61.856 1.00 119.20 ? 326 ASN B CA  1 
ATOM 4738 C C   . ASN B 1 318 ? -3.852  -0.818  -63.266 1.00 116.06 ? 326 ASN B C   1 
ATOM 4739 O O   . ASN B 1 318 ? -2.721  -0.329  -63.439 1.00 114.35 ? 326 ASN B O   1 
ATOM 4740 C CB  . ASN B 1 318 ? -3.951  -1.949  -60.988 1.00 121.87 ? 326 ASN B CB  1 
ATOM 4741 C CG  . ASN B 1 318 ? -4.520  -3.289  -61.384 1.00 126.46 ? 326 ASN B CG  1 
ATOM 4742 O OD1 . ASN B 1 318 ? -4.385  -3.714  -62.536 1.00 123.63 ? 326 ASN B OD1 1 
ATOM 4743 N ND2 . ASN B 1 318 ? -5.128  -3.981  -60.432 1.00 125.24 ? 326 ASN B ND2 1 
ATOM 4744 N N   . ASN B 1 319 ? -4.584  -1.371  -64.232 1.00 118.13 ? 327 ASN B N   1 
ATOM 4745 C CA  . ASN B 1 319 ? -4.091  -1.315  -65.633 1.00 122.12 ? 327 ASN B CA  1 
ATOM 4746 C C   . ASN B 1 319 ? -4.370  0.091   -66.170 1.00 119.12 ? 327 ASN B C   1 
ATOM 4747 O O   . ASN B 1 319 ? -3.717  0.489   -67.154 1.00 119.67 ? 327 ASN B O   1 
ATOM 4748 C CB  . ASN B 1 319 ? -4.655  -2.435  -66.505 1.00 118.78 ? 327 ASN B CB  1 
ATOM 4749 C CG  . ASN B 1 319 ? -6.163  -2.450  -66.588 1.00 118.74 ? 327 ASN B CG  1 
ATOM 4750 O OD1 . ASN B 1 319 ? -6.788  -1.436  -66.913 1.00 119.28 ? 327 ASN B OD1 1 
ATOM 4751 N ND2 . ASN B 1 319 ? -6.764  -3.601  -66.327 1.00 116.45 ? 327 ASN B ND2 1 
ATOM 4752 N N   . LEU B 1 320 ? -5.302  0.808   -65.539 1.00 113.97 ? 328 LEU B N   1 
ATOM 4753 C CA  . LEU B 1 320 ? -5.593  2.199   -65.968 1.00 115.16 ? 328 LEU B CA  1 
ATOM 4754 C C   . LEU B 1 320 ? -4.737  3.167   -65.141 1.00 117.74 ? 328 LEU B C   1 
ATOM 4755 O O   . LEU B 1 320 ? -4.830  4.389   -65.385 1.00 117.59 ? 328 LEU B O   1 
ATOM 4756 C CB  . LEU B 1 320 ? -7.076  2.520   -65.829 1.00 108.15 ? 328 LEU B CB  1 
ATOM 4757 C CG  . LEU B 1 320 ? -7.834  2.715   -67.142 1.00 104.49 ? 328 LEU B CG  1 
ATOM 4758 C CD1 . LEU B 1 320 ? -7.373  1.687   -68.159 1.00 102.32 ? 328 LEU B CD1 1 
ATOM 4759 C CD2 . LEU B 1 320 ? -9.315  2.576   -66.880 1.00 99.86  ? 328 LEU B CD2 1 
ATOM 4760 N N   . SER B 1 321 ? -3.953  2.645   -64.197 1.00 118.27 ? 329 SER B N   1 
ATOM 4761 C CA  . SER B 1 321 ? -3.037  3.524   -63.428 1.00 119.21 ? 329 SER B CA  1 
ATOM 4762 C C   . SER B 1 321 ? -2.061  4.208   -64.397 1.00 118.18 ? 329 SER B C   1 
ATOM 4763 O O   . SER B 1 321 ? -1.142  3.553   -64.879 1.00 116.88 ? 329 SER B O   1 
ATOM 4764 C CB  . SER B 1 321 ? -2.312  2.758   -62.350 1.00 116.33 ? 329 SER B CB  1 
ATOM 4765 O OG  . SER B 1 321 ? -1.356  1.865   -62.904 1.00 115.33 ? 329 SER B OG  1 
ATOM 4766 O OXT . SER B 1 321 ? -2.253  5.405   -64.652 1.00 116.40 ? 329 SER B OXT 1 
# 
